An enzyme of the transferase class that catalyzes condensation of the succinyl group from succinyl coenzyme A with glycine to form delta-aminolevulinate. It is a pyridoxyal phosphate protein and the reaction occurs in mitochondria as the first step of the heme biosynthetic pathway. The enzyme is a key regulatory enzyme in heme biosynthesis. In liver feedback is inhibited by heme. EC 2.3.1.37.
A compound produced from succinyl-CoA and GLYCINE as an intermediate in heme synthesis. It is used as a PHOTOCHEMOTHERAPY for actinic KERATOSIS.
An enzyme that catalyzes the formation of porphobilinogen from two molecules of 5-aminolevulinic acid. EC 4.2.1.24.
Anemia characterized by the presence of erythroblasts containing excessive deposits of iron in the marrow.
An enzyme that catalyzes the conversion of ATP, L-glutamate, and NH3 to ADP, orthophosphate, and L-glutamine. It also acts more slowly on 4-methylene-L-glutamate. (From Enzyme Nomenclature, 1992) EC 6.3.1.2.
A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.
An enzyme that catalyzes the conversion of ATP into a series of (2'-5') linked oligoadenylates and pyrophosphate in the presence of double-stranded RNA. These oligonucleotides activate an endoribonuclease (RNase L) which cleaves single-stranded RNA. Interferons can act as inducers of these reactions. EC 2.7.7.-.
An enzyme that catalyzes the tetrapolymerization of the monopyrrole PORPHOBILINOGEN into the hydroxymethylbilane preuroporphyrinogen (UROPORPHYRINOGENS) in several discrete steps. It is the third enzyme in the 8-enzyme biosynthetic pathway of HEME. In humans, deficiency in this enzyme encoded by HMBS (or PBGD) gene results in a form of neurological porphyria (PORPHYRIA, ACUTE INTERMITTENT). This enzyme was formerly listed as EC 4.3.1.8
Salts and esters of the 7-carbon saturated monocarboxylic acid heptanoic acid.
The collective name for the boron hydrides, which are analogous to the alkanes and silanes. Numerous boranes are known. Some have high calorific values and are used in high-energy fuels. (From Grant & Hackh's Chemical Dictionary, 5th ed)
Chloro(7,12-diethenyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-dipropanoato(4-)-N(21),N(22),N(23),N(24)) ferrate(2-) dihydrogen.
An allylic compound that acts as a suicide inactivator of CYTOCHROME P450 by covalently binding to its heme moiety or surrounding protein.
1,4-Dihydro-2,4,6-trimethyl-3,5-pyridinedicarboxylic acid diethyl ester.
Amino acids with uncharged R groups or side chains.
Non-pathogenic ovoid to rod-shaped bacteria that are widely distributed and found in fresh water as well as marine and hypersaline habitats.
The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Genetic diseases that are linked to gene mutations on the X CHROMOSOME in humans (X CHROMOSOME, HUMAN) or the X CHROMOSOME in other species. Included here are animal models of human X-linked diseases.
Porphobilinogen is a porphyrin precursor, specifically the organic compound intermediate in the biosynthesis of heme and chlorophyll, formed by the condensation of two pyrrole molecules in the liver and other tissues.
Ligases that catalyze the joining of adjacent AMINO ACIDS by the formation of carbon-nitrogen bonds between their carboxylic acid groups and amine groups.
Any horny growth such as a wart or callus.
The rate dynamics in chemical or physical systems.
Enzymes that catalyze the formation of acyl-CoA derivatives. EC 6.2.1.
This is the active form of VITAMIN B 6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (PYRIDOXAMINE).
A group of compounds containing the porphin structure, four pyrrole rings connected by methine bridges in a cyclic configuration to which a variety of side chains are attached. The nature of the side chain is indicated by a prefix, as uroporphyrin, hematoporphyrin, etc. The porphyrins, in combination with iron, form the heme component in biologically significant compounds such as hemoglobin and myoglobin.
Condensation products of aromatic amines and aldehydes forming azomethines substituted on the N atom, containing the general formula R-N:CHR. (From Grant & Hackh's Chemical Dictionary, 5th ed)
A mitochondrial enzyme found in a wide variety of cells and tissues. It is the final enzyme in the 8-enzyme biosynthetic pathway of HEME. Ferrochelatase catalyzes ferrous insertion into protoporphyrin IX to form protoheme or heme. Deficiency in this enzyme results in ERYTHROPOIETIC PROTOPORPHYRIA.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Enzymes of the isomerase class that catalyze the transfer of acyl-, phospho-, amino- or other groups from one position within a molecule to another. EC 5.4.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
The 4-carboxyaldehyde form of VITAMIN B 6 which is converted to PYRIDOXAL PHOSPHATE which is a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid.
A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.
Immature, nucleated ERYTHROCYTES occupying the stage of ERYTHROPOIESIS that follows formation of ERYTHROID PRECURSOR CELLS and precedes formation of RETICULOCYTES. The normal series is called normoblasts. Cells called MEGALOBLASTS are a pathologic series of erythroblasts.
Immunologic techniques involved in diagnosis.
An enzyme that activates aspartic acid with its specific transfer RNA. EC 6.1.1.12.
An enzyme that activates methionine with its specific transfer RNA. EC 6.1.1.10.
An enzyme that activates tryptophan with its specific transfer RNA. EC 6.1.1.2.
Proteins that regulate cellular and organismal iron homeostasis. They play an important biological role by maintaining iron levels that are adequate for metabolic need, but below the toxicity threshold.
Enzymes that catalyze the joining of two molecules by the formation of a carbon-nitrogen bond. EC 6.3.
Porphyrins with four methyl, two vinyl, and two propionic acid side chains attached to the pyrrole rings. Protoporphyrin IX occurs in hemoglobin, myoglobin, and most of the cytochromes.
An enzyme that activates isoleucine with its specific transfer RNA. EC 6.1.1.5.
An enzyme that catalyzes the formation of asparagine from ammonia and aspartic acid, in the presence of ATP. EC 6.3.1.1.
A non-essential amino acid. It is found primarily in gelatin and silk fibroin and used therapeutically as a nutrient. It is also a fast inhibitory neurotransmitter.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
The 4-methanol form of VITAMIN B 6 which is converted to PYRIDOXAL PHOSPHATE which is a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. Although pyridoxine and Vitamin B 6 are still frequently used as synonyms, especially by medical researchers, this practice is erroneous and sometimes misleading (EE Snell; Ann NY Acad Sci, vol 585 pg 1, 1990).
An enzyme that activates phenylalanine with its specific transfer RNA. EC 6.1.1.20.
An enzyme that activates tyrosine with its specific transfer RNA. EC 6.1.1.1.
Therapy using oral or topical photosensitizing agents with subsequent exposure to light.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
An enzyme that catalyzes the formation of carbamoyl phosphate from ATP, carbon dioxide, and ammonia. This enzyme is specific for arginine biosynthesis or the urea cycle. Absence or lack of this enzyme may cause CARBAMOYL-PHOSPHATE SYNTHASE I DEFICIENCY DISEASE. EC 6.3.4.16.
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
An enzyme that activates leucine with its specific transfer RNA. EC 6.1.1.4.
An enzyme that activates serine with its specific transfer RNA. EC 6.1.1.11.
An enzyme that activates valine with its specific transfer RNA. EC 6.1.1.9
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
An enzyme of the urea cycle that catalyzes the formation of argininosuccinic acid from citrulline and aspartic acid in the presence of ATP. Absence or deficiency of this enzyme causes the metabolic disease CITRULLINEMIA in humans. EC 6.3.4.5.
An enzyme that catalyzes the formation of CoA derivatives from ATP, acetate, and CoA to form AMP, pyrophosphate, and acetyl CoA. It acts also on propionates and acrylates. EC 6.2.1.1.
An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.
An enzyme that activates glutamic acid with its specific transfer RNA. EC 6.1.1.17.

delta-Aminolevulinate synthetases in the liver cytosol fraction and mitochondria of mice treated with allylisopropylacetamide and 3,5-dicarbethoxyl-1,4-dihydrocollidine. (1/369)

Hepatic delta-aminolevulinate (ALA) synthetase was induced in mice by the administration of allylisopropylacetamide (AIA) and 3,5-dicarbethoxy-1,4-dihydrocollidine (DDC). In both cases, a significant amount of ALA synthetase accumulated in the liver cytosol fraction as well as in the mitochondria. The apparent molecular weight of the cytosol ALA synthetase was estimated to be 320,000 by gel filtration, but when the cytosol ALA synthetase was subjected to sucrose density gradient centrifugation, it showed a molecular weight of 110,000. In the mitochondria, there were two different sizes of ALA synthetase with molecular weights of 150,000 and 110,000, respectively; the larger enzyme was predominant in DDC-treated mice, whereas in AIA-treated mice and normal mice the enzyme existed mostly in the smaller form. When hemin was injected into mice pretreated with DDC, the molecular size of the mitochondrial ALA synthetase changed from 150,000 to 110,000. The half-life of ALA synthetase in the liver cytosol fraction was about 30 min in both the AIA-treated and DDC-treated mice. The half-life of the mitochondrial ALA synthetase in AIA-treated mice and normal mice was about 60 min, but in DDC-treated mice the half-life was as long as 150 min. The data suggest that the cytosol ALA synthetase of mouse liver is a protein complex with properties very similar to those of the cytosol ALA synthetase of rat liver, which has been shown to be composed of the enzyme active protein and two catalytically inactive binding proteins, and that ALA synthetase may be transferred from the liver cytosol fraction to the mitochondria with a size of about 150,000 daltons, followed by its conversion to enzyme with a molecular weight of 110,000 within the mitochondria. The process of intramitochondrial enzyme degradation seems to be affected in DDC-treated animals.  (+info)

Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis. (2/369)

X-linked sideroblastic anemia (XLSA) in four unrelated male probands was caused by missense mutations in the erythroid-specific 5-aminolevulinate synthase gene (ALAS2). All were new mutations: T647C, C1283T, G1395A, and C1406T predicting amino acid substitutions Y199H, R411C, R448Q, and R452C. All probands were clinically pyridoxine-responsive. The mutation Y199H was shown to be the first de novo XLSA mutation and occurred in a gamete of the proband's maternal grandfather. There was a significantly higher frequency of coinheritance of the hereditary hemochromatosis (HH) HFE mutant allele C282Y in 18 unrelated XLSA hemizygotes than found in the normal population, indicating a role for coinheritance of HFE alleles in the expression of this disorder. One proband (Y199H) with severe and early iron loading coinherited HH as a C282Y homozygote. The clinical and hematologic histories of two XLSA probands suggest that iron overload suppresses pyridoxine responsiveness. Notably, reversal of the iron overload in the Y199H proband by phlebotomy resulted in higher hemoglobin concentrations during pyridoxine supplementation. The proband with the R452C mutation was symptom-free on occasional phlebotomy and daily pyridoxine. These studies indicate the value of combined phlebotomy and pyridoxine supplementation in the management of XLSA probands in order to prevent a downward spiral of iron toxicity and refractory anemia.  (+info)

Properties of 5-aminolaevulinate synthetase and its relationship to microsomal mixed-function oxidation in the southern armyworm (Spodoptera eridania). (3/369)

1. Activity of 5-aminolaevulinate synthetase was measured in the midgut and other tissues of the last larval instar of the southern armyworm (Spodoptera eridania Cramer, formerly Prodenia eridania Cramer). 2. Optimum conditions for measuring the activity were established with respect to all variables involved and considerable differences from those reported for mammalian enzyme preparations were found. 3. Maximum activity (20 nmol/h per mg of protein) occurs 18-24 h after the fifth moult and thereafter decreases to trace amounts as the larvae age and approach pupation. 4. Synthetase activity was rapidly induced by oral administration (in the diet) of pentamethylbenzene, phenobarbital, diethyl 1,4-dihydro-2,4,6-trimethylpyridine-3, 5-dicarboxylate, and 2-allyl-2-isopropylacetamide. 5. Puromycin inhibited the induction of synthetase by pentamethylbenzene. 6. Induction of 5-aminolaevulinate synthetase correlated well with the induction of microsomal N-demethylation of p-chloro-N-methylaniline, except for phenobarbital, which induced the microsomal oxidase relatively more than the synthetase.  (+info)

Pre-steady-state reaction of 5-aminolevulinate synthase. Evidence for a rate-determining product release. (4/369)

5-Aminolevulinate synthase (ALAS) is the first enzyme of the heme biosynthetic pathway in non-plant eukaryotes and the alpha-subclass of purple bacteria. The pyridoxal 5'-phosphate cofactor at the active site undergoes changes in absorptive properties during substrate binding and catalysis that have allowed us to study the kinetics of these reactions spectroscopically. Rapid scanning stopped-flow experiments of murine erythroid 5-aminolevulinate synthase demonstrate that reaction with glycine plus succinyl-CoA results in a pre-steady-state burst of quinonoid intermediate formation. Thus, a step following binding of substrates and initial quinonoid intermediate formation is rate-determining. The steady-state spectrum of the enzyme is similar to that formed in the presence of 5-aminolevulinate, suggesting that release of this product limits the overall rate. Reaction of either glycine or 5-aminolevulinate with ALAS is slow (kf = 0.15 s-1) and approximates kcat. The rate constant for reaction with glycine is increased at least 90-fold in the presence of succinyl-CoA and most likely represents a slow conformational change of the enzyme that is accelerated by succinyl-CoA. The slow rate of reaction of 5-aminolevulinate with ALAS is 5-aminolevulinate-independent, suggesting that it also represents a slow isomerization of the enzyme. Reaction of succinyl-CoA with the enzyme-glycine complex to form a quinonoid intermediate is a biphasic process and may be irreversible. Taken together, the data suggest that turnover is limited by release of 5-aminolevulinate or a conformational change associated with 5-aminolevulinate release.  (+info)

Phylogenetic analysis of the 5-aminolevulinate synthase gene. (5/369)

The evolution of 5-aminolevulinate synthase (ALS) was studied by acquiring sequence data and generating phylogenetic trees. Gene sequences were already available for a variety of vertebrates (which have both a housekeeping and an erythroid form of the gene), fungi, alpha-proteobacteria, and one protist and one protostome. In order to generate representative trees, ALS sequence data were acquired from various deuterostomes and protostomes. The species and tissues selected for study were beluga whale liver, hagfish blood, sea urchin gonadal tissue, cuttlefish hepatopancreas, horseshoe crab hepatopancreas, and bloodworm blood. The new sequences and those previously published were examined for the presence of heme-regulatory motifs (HRMs) and iron-responsive elements (IREs). The HRMs are present in almost all eukaryotic species, which suggests their fundamental role in the regulation of ALS. The IREs are present in all vertebrate erythroid forms of ALS, which indicates that in those animals, expression of the erythroid form of the enzyme and, hence, hemoglobin production can be influenced by the intracellular content of iron. The new sequences were aligned with previously reported ALS sequences, and phylogenetic analyses were performed. The resulting trees provided evidence regarding the timing of the gene duplication event that led to the two forms of the ALS gene in vertebrates. It appears that the housekeeping and erythroid forms of ALS probably arose before the divergence of hagfish from the deuterostome line leading to the vertebrates. The data also add to the evidence indicating that alpha-proteobacteria are the nearest contemporary relatives of mitochondria.  (+info)

Respiratory uncoupling induces delta-aminolevulinate synthase expression through a nuclear respiratory factor-1-dependent mechanism in HeLa cells. (6/369)

Nuclear respiratory factor (NRF)-1 appears to be important for the expression of several respiratory genes, but there is no direct evidence that NRF-1 transduces a physiological signal into the production of an enzyme critical for mitochondrial biogenesis. We generated HeLa cells containing plasmids allowing doxycycline-inducible expression of uncoupling protein (UCP)-1. In the absence of doxycycline, UCP-1 mRNA and protein were undetectable. In the presence of doxycycline, UCP-1 was expressed and oxygen consumption doubled. This rise in oxygen consumption was associated with an increase in NRF-1 mRNA. It was also associated with an increase in NRF-1 protein binding activity as determined by electrophoretic mobility shift assay using a functional NRF-1 binding site from the delta-aminolevulinate (ALA) synthase promoter. Respiratory uncoupling also caused a time-dependent increase in protein levels of ALA synthase, an early marker for mitochondrial biogenesis. ALA synthase induction by respiratory uncoupling was prevented by transfecting cells with an oligonucleotide antisense to the region of the NRF-1 initiation codon; a scrambled oligonucleotide with the same base composition had no effect. Respiratory uncoupling increases oxygen consumption and lowers energy reserves. In HeLa cells, uncoupling also increases ALA synthase, an enzyme critical for mitochondrial respiration, but only if translatable mRNA for NRF-1 is available. These data suggest that the transcription factor NRF-1 plays a key role in cellular adaptation to energy demands by translating physiological signals into an increased capacity for generating energy.  (+info)

Characterization of the rhodobacter sphaeroides 5-aminolaevulinic acid synthase isoenzymes, HemA and HemT, isolated from recombinant Escherichia coli. (7/369)

The hemA and hemT genes encoding 5-aminolaevulinic acid synthase (ALAS) from the photosynthetic bacterium Rhodobacter sphaeroides, were cloned to allow high expression in Escherichia coli. Both HemA and HemT appeared to be active in vivo as plasmids carrying the respective genes complemented an E. coli hemA strain (glutamyl-tRNA reductase deficient). The over-expressed isoenzymes were isolated and purified to homogeneity. Isolated HemA was soluble and catalytically active whereas HemT was largely insoluble and failed to show any activity ex vivo. Pure HemA was recovered in yields of 5-7 mg x L-1 of starting bacterial culture and pure HemT at 10 mg x L-1 x HemA has a final specific activity of 13 U x mg-1 with 1 unit defined as 1 micromol of 5-aminolaevulinic acid formed per hour at 37 degrees C. The Km values for HemA are 1.9 mM for glycine and 17 microM for succinyl-CoA, with the enzyme showing a turnover number of 430 h-1. In common with other ALASs the recombinant R. sphaeroides HemA requires pyridoxal 5'-phosphate (PLP) as a cofactor for catalysis. Removal of this cofactor resulted in inactive apo-ALAS. Similarly, reduction of the HemA-PLP complex using sodium borohydride led to > 90% inactivation of the enzyme. Ultraviolet-visible spectroscopy with HemA suggested the presence of an aldimine linkage between the enzyme and pyridoxal 5'-phosphate that was not observed when HemT was incubated with the cofactor. HemA was found to be sensitive to reagents that modify histidine, arginine and cysteine amino acid residues and the enzyme was also highly sensitive to tryptic cleavage between Arg151 and Ser152 in the presence or absence of PLP and substrates. Antibodies were raised to both HemA and HemT but the respective antisera were not only found to bind both enzymes but also to cross-react with mouse ALAS, indicating that all of the proteins have conserved epitopes.  (+info)

A photosensitising adenovirus for photodynamic therapy. (8/369)

We have developed a new approach to photodynamic therapy based on adenoviral transduction of the rate-limiting enzyme in heme synthesis. Conventional phototherapy uses porphyrin-based chemical photosensitisers, including delta-aminolaevulinic acid (ALA) which is converted to protoporphyrin IX (PpIX) by the enzymes of the heme biosynthetic pathway. The lack of a specific mechanism for targeting chemical photosensitisers and PpIX to tumour cells means that therapeutic irradiation can damage normal tissue and exposure to sunlight following treatment can cause severe burns. The rate limiting enzyme in PpIX synthesis is ALA-synthase (ALA-S). We have developed a new yeast vector system for manipulation of the adeno- virus genome and used it to construct a virus expressing a mutant form of ALA-S lacking the iron response elements which regulate ALA-S translation and the heme regulatory motifs which regulate import of ALA-S into mitochondria. The virus induces a large increase in PpIX expression and confers photosensitivity on cultured cells. Unlike conventional photodynamic therapy, a viral approach makes it possible to restrict photosensitivity by biological rather than purely physical or chemical means. As with HSV thymidine kinase, ALA-S expression is a general mechanism for sensitisation to a therapeutic agent which can easily be adapted to whatever means of gene delivery is most effective.  (+info)

5-Aminolevulinate synthase (ALAS) is an enzyme that catalyzes the first step in heme biosynthesis, a metabolic pathway that produces heme, a porphyrin ring with an iron atom at its center. Heme is a crucial component of hemoglobin, cytochromes, and other important molecules in the body.

ALAS exists in two forms: ALAS1 and ALAS2. ALAS1 is expressed in all tissues, while ALAS2 is primarily expressed in erythroid cells (precursors to red blood cells). The reaction catalyzed by ALAS involves the condensation of glycine and succinyl-CoA to form 5-aminolevulinate.

Deficiencies or mutations in the ALAS2 gene can lead to a rare genetic disorder called X-linked sideroblastic anemia, which is characterized by abnormal red blood cell maturation and iron overload in mitochondria.

Aminolevulinic acid (ALA) is a naturally occurring compound in the human body and is a key precursor in the biosynthesis of heme, which is a component of hemoglobin in red blood cells. It is also used as a photosensitizer in dermatology for the treatment of certain types of skin conditions such as actinic keratosis and basal cell carcinoma.

In medical terms, ALA is classified as an α-keto acid and a porphyrin precursor. It is synthesized in the mitochondria from glycine and succinyl-CoA in a reaction catalyzed by the enzyme aminolevulinic acid synthase. After its synthesis, ALA is transported to the cytosol where it undergoes further metabolism to form porphyrins, which are then used for heme biosynthesis in the mitochondria.

In dermatology, topical application of ALA followed by exposure to a specific wavelength of light can lead to the production of reactive oxygen species that destroy abnormal cells in the skin while leaving healthy cells unharmed. This makes it an effective treatment for precancerous and cancerous lesions on the skin.

It is important to note that ALA can cause photosensitivity, which means that patients who have undergone ALA-based treatments should avoid exposure to sunlight or other sources of bright light for a period of time after the treatment to prevent adverse reactions.

Porphobilinogen Synthase (also known as PBGD or hydroxymethylbilane synthase) is an enzyme that catalyzes the second step in the heme biosynthesis pathway. This enzyme is responsible for converting two molecules of porphobilinogen into a linear tetrapyrrole called hydroxymethylbilane, which is then converted into uroporphyrinogen III by uroporphyrinogen III synthase.

Deficiency in Porphobilinogen Synthase can lead to a rare genetic disorder known as acute intermittent porphyria (AIP), which is characterized by the accumulation of porphobilinogen and other precursors in the heme biosynthesis pathway, resulting in neurovisceral symptoms such as abdominal pain, vomiting, neuropathy, and psychiatric disturbances.

Sideroblastic anemia is a type of anemia characterized by the presence of ringed sideroblasts in the bone marrow. Ringed sideroblasts are red blood cell precursors that have an abnormal amount of iron accumulated in their mitochondria, which forms a ring around the nucleus. This results in the production of abnormal hemoglobin and impaired oxygen transport.

Sideroblastic anemia can be classified as congenital or acquired. Congenital sideroblastic anemias are caused by genetic defects that affect heme synthesis or mitochondrial function, while acquired sideroblastic anemias are associated with various conditions such as myelodysplastic syndromes, chronic alcoholism, lead toxicity, and certain medications.

Symptoms of sideroblastic anemia may include fatigue, weakness, shortness of breath, and pallor. Diagnosis is typically made through a bone marrow aspiration and biopsy, which can identify the presence of ringed sideroblasts. Treatment depends on the underlying cause but may include iron chelation therapy, vitamin B6 supplementation, or blood transfusions.

Glutamate-ammonia ligase, also known as glutamine synthetase, is an enzyme that plays a crucial role in nitrogen metabolism. It catalyzes the formation of glutamine from glutamate and ammonia in the presence of ATP, resulting in the conversion of ammonia to a less toxic form. This reaction is essential for maintaining nitrogen balance in the body and for the synthesis of various amino acids, nucleotides, and other biomolecules. The enzyme is widely distributed in various tissues, including the brain, liver, and muscle, and its activity is tightly regulated through feedback inhibition by glutamine and other metabolites.

Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) are a group of enzymes that play a crucial role in protein synthesis. They are responsible for attaching specific amino acids to their corresponding transfer RNAs (tRNAs), creating aminoacyl-tRNA complexes. These complexes are then used in the translation process to construct proteins according to the genetic code.

Each aminoacyl-tRNA synthetase is specific to a particular amino acid, and there are 20 different synthetases in total, one for each of the standard amino acids. The enzymes catalyze the reaction between an amino acid and ATP to form an aminoacyl-AMP intermediate, which then reacts with the appropriate tRNA to create the aminoacyl-tRNA complex. This two-step process ensures the fidelity of the translation process by preventing mismatching of amino acids with their corresponding tRNAs.

Defects in aminoacyl-tRNA synthetases can lead to various genetic disorders and diseases, such as Charcot-Marie-Tooth disease type 2D, distal spinal muscular atrophy, and leukoencephalopathy with brainstem and spinal cord involvement and lactate acidosis (LBSL).

2',5'-Oligoadenylate synthetase (2'-5' OAS) is an enzyme that plays a crucial role in the innate immune response to viral infections. It is activated by double-stranded RNA, a molecular pattern often associated with viral replication. Once activated, 2'-5' OAS catalyzes the synthesis of 2'-5'-linked oligoadenylates, which then activate another enzyme called RNase L. RNase L degrades single-stranded RNA, thereby inhibiting viral replication and translation. This defense mechanism helps to limit the spread of viruses within the body. Additionally, 2'-5' OAS has been implicated in regulating cell death pathways and inflammatory responses.

Hydroxymethylbilane Synthase (HMBS) is an enzyme that plays a crucial role in the metabolic pathway known as heme biosynthesis. Heme is an essential component of various proteins, including hemoglobin, which is responsible for oxygen transport in the blood.

The HMBS enzyme catalyzes the conversion of aminolevulinic acid (ALA) and glycine into a linear tetrapyrrole intermediate called hydroxymethylbilane. This reaction is the third step in the heme biosynthesis pathway, and it takes place in the mitochondria of cells.

Deficiencies in HMBS can lead to a rare genetic disorder called acute intermittent porphyria (AIP), which is characterized by neurovisceral attacks and neurological symptoms such as abdominal pain, vomiting, hypertension, tachycardia, and mental disturbances.

Heptanoates are chemical compounds that contain the functional group of heptanoic acid. Heptanoic acid, also known as n-caproic acid, is a type of carboxylic acid with a 7-carbon chain and the molecular formula C7H15COOH.

Heptanoates are commonly used in the production of various chemicals, including flavors, fragrances, and pharmaceuticals. In medicine, heptanoates may be used as esters in the formulation of drugs to improve their solubility, absorption, and stability. For example, some injectable forms of medications may use heptanoate salts or esters to enhance their delivery into the body.

It's important to note that specific medical definitions for "heptanoates" may vary depending on the context and application.

Boranes are a group of chemical compounds that contain only boron and hydrogen. The most well-known borane is BH3, also known as diborane. These compounds are highly reactive and have unusual structures, with the boron atoms bonded to each other in three-center, two-electron bonds. Boranes are used in research and industrial applications, including as reducing agents and catalysts. They are highly flammable and toxic, so they must be handled with care.

Hemin is defined as the iron(III) complex of protoporphyrin IX, which is a porphyrin derivative. It is a naturally occurring substance that is involved in various biological processes, most notably in the form of heme, which is a component of hemoglobin and other hemoproteins. Hemin is also used in medical research and therapy, such as in the treatment of methemoglobinemia and lead poisoning.

Allylisopropylacetamide is not a term that has a widely accepted or established medical definition. It is a chemical compound with the formula (CH₂CHCH₂)N(C=O)CH(CH₃)₂, and it may have various chemical or industrial uses, but it is not a term that is commonly used in medical contexts.

If you have any specific questions about this compound or its potential uses or effects, I would recommend consulting with a relevant expert, such as a chemist or toxicologist, who can provide more detailed and accurate information based on their expertise and knowledge of the subject.

I apologize, but I am unable to find a medical definition for "dicarbethoxydihydrocollidine." It is possible that this term does not have a specific meaning within the field of medicine. A more general search indicates that dicarbethoxydihydrocollidine may be a chemical compound used in research or industry, but it does not appear to have direct relevance to medical diagnosis, treatment, or health. If you have further questions or need information on a related medical topic, I would be happy to help you with those.

Neutral amino acids are a type of amino acids that are characterized by the presence of a neutral side chain in their chemical structure. In other words, the side chain of these amino acids does not contain any ionizable groups, such as carboxyl or amino groups, which can give rise to positive or negative charges.

There are nine neutral amino acids in total, and they include:

1. Alanine (Ala) - has a methyl group (-CH3) as its side chain
2. Glycine (Gly) - has a hydrogen atom (-H) as its side chain
3. Valine (Val) - has an isopropyl group (-CH(CH3)2) as its side chain
4. Leucine (Leu) - has a branched alkyl group (-CH2CH(CH3)2) as its side chain
5. Isoleucine (Ile) - has a sec-butyl group (-CH(CH3)(CH2CH3)) as its side chain
6. Proline (Pro) - has a cyclic structure containing a secondary amino group (-NH-) as its side chain
7. Phenylalanine (Phe) - has an aromatic ring with a methyl group (-CH3) attached to it as its side chain
8. Tryptophan (Trp) - has an indole ring as its side chain
9. Methionine (Met) - has a sulfur-containing alkyl group (-CH2CH2SH) as its side chain

Neutral amino acids play important roles in various biological processes, such as protein synthesis, metabolism, and signaling pathways. They are also essential components of many dietary proteins and are required for the growth, development, and maintenance of tissues and organs in the body.

Rhodobacter capsulatus is not a medical term, but a species name in the field of microbiology. It refers to a type of purple nonsulfur bacteria that is capable of photosynthesis and can be found in freshwater and soil environments. These bacteria are known for their ability to switch between using light and organic compounds as sources of energy, depending on the availability of each. They have been studied for their potential applications in biotechnology and renewable energy production.

While not directly related to medical definitions, some research has explored the potential use of Rhodobacter capsulatus in bioremediation and wastewater treatment due to its ability to break down various organic compounds. However, it is not a pathogenic organism and does not have any direct relevance to human health or disease.

Heme is not a medical term per se, but it is a term used in the field of medicine and biology. Heme is a prosthetic group found in hemoproteins, which are proteins that contain a heme iron complex. This complex plays a crucial role in various biological processes, including oxygen transport (in hemoglobin), electron transfer (in cytochromes), and chemical catalysis (in peroxidases and catalases).

The heme group consists of an organic component called a porphyrin ring, which binds to a central iron atom. The iron atom can bind or release electrons, making it essential for redox reactions in the body. Heme is also vital for the formation of hemoglobin and myoglobin, proteins responsible for oxygen transport and storage in the blood and muscles, respectively.

In summary, heme is a complex organic-inorganic structure that plays a critical role in several biological processes, particularly in electron transfer and oxygen transport.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

X-linked genetic diseases refer to a group of disorders caused by mutations in genes located on the X chromosome. These conditions primarily affect males since they have only one X chromosome and therefore don't have a second normal copy of the gene to compensate for the mutated one. Females, who have two X chromosomes, are typically less affected because they usually have one normal copy of the gene on their other X chromosome.

Examples of X-linked genetic diseases include Duchenne and Becker muscular dystrophy, hemophilia A and B, color blindness, and fragile X syndrome. Symptoms and severity can vary widely depending on the specific condition and the nature of the genetic mutation involved. Treatment options depend on the particular disease but may include physical therapy, medication, or in some cases, gene therapy.

Porphobilinogen (PBG) is a bioactive compound that plays a crucial role in the biosynthesis pathway of heme, which is an essential component of hemoglobin and other hemoproteins. It is a porphyrin precursor and is synthesized from aminolevulinic acid (ALA) by the enzyme ALA dehydratase in the second step of heme biosynthesis.

In medical terms, abnormal accumulation or increased levels of PBG in the body can indicate an underlying disorder in heme biosynthesis, such as acute intermittent porphyria (AIP), variegate porphyria (VP), or hereditary coproporphyria (HCP). These disorders are known as porphyrias and are characterized by the buildup of porphyrin precursors in various tissues, leading to neurological and gastrointestinal symptoms.

Therefore, measuring PBG levels in urine or blood can help diagnose and monitor these conditions.

Peptide synthases are a group of enzymes that catalyze the formation of peptide bonds between specific amino acids to produce peptides or proteins. They are responsible for the biosynthesis of many natural products, including antibiotics, bacterial toxins, and immunomodulatory peptides.

Peptide synthases are large, complex enzymes that consist of multiple domains and modules, each of which is responsible for activating and condensing specific amino acids. The activation of amino acids involves the formation of an aminoacyl-adenylate intermediate, followed by transfer of the activated amino acid to a thiol group on the enzyme. The condensation of two activated amino acids results in the formation of a peptide bond and release of adenosine monophosphate (AMP) and pyrophosphate.

Peptide synthases are found in all three domains of life, but are most commonly associated with bacteria and fungi. They play important roles in the biosynthesis of many natural products that have therapeutic potential, making them targets for drug discovery and development.

Keratosis, in general, refers to a skin condition characterized by the abnormal growth or development of keratin, a protein that forms part of the outer layer of the skin (epidermis). There are several types of keratosis, including:

1. Seborrheic Keratosis: benign, often pigmented, rough, and scaly growths that can appear anywhere on the body. They tend to increase in number with age.
2. Actinic Keratosis: rough, scaly patches or spots on the skin that are caused by long-term exposure to sunlight or artificial UV light. These have the potential to develop into squamous cell carcinoma, a type of skin cancer.
3. Solar Keratosis: another term for actinic keratosis, as it is primarily caused by sun damage.
4. Keratosis Pilaris: a common condition where small, rough bumps appear on the skin, often on the arms, thighs, or cheeks. These are caused by excess keratin blocking hair follicles.
5. Follicular Keratosis: a disorder characterized by the formation of horny plugs within the hair follicles, leading to rough, sandpaper-like bumps on the skin.
6. Intraepidermal Keratosis: a term used to describe the abnormal accumulation of keratin in the epidermis, which can lead to various skin conditions.

It's important to consult with a healthcare professional or dermatologist for proper diagnosis and treatment if you suspect having any form of keratosis.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Coenzyme A (CoA) ligases, also known as CoA synthetases, are a class of enzymes that activate acyl groups, such as fatty acids and amino acids, by forming a thioester bond with coenzyme A. This activation is an essential step in various metabolic pathways, including fatty acid oxidation, amino acid catabolism, and the synthesis of several important compounds like steroids and acetylcholine.

CoA ligases catalyze the following reaction:

acyl group + ATP + CoA ↔ acyl-CoA + AMP + PP~i~

In this reaction, an acyl group (R-) from a carboxylic acid is linked to the thiol (-SH) group of coenzyme A through a high-energy thioester bond. The energy required for this activation is provided by the hydrolysis of ATP to AMP and inorganic pyrophosphate (PP~i~).

CoA ligases are classified into three main types based on the nature of the acyl group they activate:

1. Acyl-CoA synthetases (or long-chain fatty acid CoA ligases) activate long-chain fatty acids, typically containing 12 or more carbon atoms.
2. Aminoacyl-CoA synthetases activate amino acids to form aminoacyl-CoAs, which are essential intermediates in the catabolism of certain amino acids.
3. Short-chain specific CoA ligases activate short-chain fatty acids (up to 6 carbon atoms) and other acyl groups like acetate or propionate.

These enzymes play a crucial role in maintaining cellular energy homeostasis, metabolism, and the synthesis of various essential biomolecules.

Pyridoxal phosphate (PLP) is the active form of vitamin B6 and functions as a cofactor in various enzymatic reactions in the human body. It plays a crucial role in the metabolism of amino acids, carbohydrates, lipids, and neurotransmitters. Pyridoxal phosphate is involved in more than 140 different enzyme-catalyzed reactions, making it one of the most versatile cofactors in human biochemistry.

As a cofactor, pyridoxal phosphate helps enzymes carry out their functions by facilitating chemical transformations in substrates (the molecules on which enzymes act). In particular, PLP is essential for transamination, decarboxylation, racemization, and elimination reactions involving amino acids. These processes are vital for the synthesis and degradation of amino acids, neurotransmitters, hemoglobin, and other crucial molecules in the body.

Pyridoxal phosphate is formed from the conversion of pyridoxal (a form of vitamin B6) by the enzyme pyridoxal kinase, using ATP as a phosphate donor. The human body obtains vitamin B6 through dietary sources such as whole grains, legumes, vegetables, nuts, and animal products like poultry, fish, and pork. It is essential to maintain adequate levels of pyridoxal phosphate for optimal enzymatic function and overall health.

Porphyrins are complex organic compounds that contain four pyrrole rings joined together by methine bridges (=CH-). They play a crucial role in the biochemistry of many organisms, as they form the core structure of various heme proteins and other metalloproteins. Some examples of these proteins include hemoglobin, myoglobin, cytochromes, and catalases, which are involved in essential processes such as oxygen transport, electron transfer, and oxidative metabolism.

In the human body, porphyrins are synthesized through a series of enzymatic reactions known as the heme biosynthesis pathway. Disruptions in this pathway can lead to an accumulation of porphyrins or their precursors, resulting in various medical conditions called porphyrias. These disorders can manifest as neurological symptoms, skin lesions, and gastrointestinal issues, depending on the specific type of porphyria and the site of enzyme deficiency.

It is important to note that while porphyrins are essential for life, their accumulation in excessive amounts or at inappropriate locations can result in pathological conditions. Therefore, understanding the regulation and function of porphyrin metabolism is crucial for diagnosing and managing porphyrias and other related disorders.

A Schiff base is not a medical term per se, but rather a chemical concept that can be relevant in various scientific and medical fields. A Schiff base is a chemical compound that contains a carbon-nitrogen double bond with the nitrogen atom connected to an aryl or alkyl group, excluding hydrogen. This structure is also known as an azomethine.

The general formula for a Schiff base is R1R2C=NR3, where R1 and R2 are organic groups (aryl or alkyl), and R3 is a hydrogen atom or an organic group. These compounds can be synthesized by the condensation of a primary amine with a carbonyl compound, such as an aldehyde or ketone.

Schiff bases have been studied in various medical and biological contexts due to their potential bioactivities. Some Schiff bases exhibit antimicrobial, antifungal, anti-inflammatory, and anticancer properties. They can also serve as ligands for metal ions, forming complexes with potential applications in medicinal chemistry, such as in the development of new drugs or diagnostic agents.

Ferrochelatase is a medical/biochemical term that refers to an enzyme called Fe-chelatase or heme synthase. This enzyme plays a crucial role in the biosynthesis of heme, which is a vital component of hemoglobin, cytochromes, and other important biological molecules.

Ferrochelatase functions by catalyzing the insertion of ferrous iron (Fe2+) into protoporphyrin IX, the final step in heme biosynthesis. This enzyme is located within the inner mitochondrial membrane of cells and is widely expressed in various tissues, with particularly high levels found in erythroid precursor cells, liver, and brain.

Defects or mutations in the ferrochelatase gene can lead to a rare genetic disorder called erythropoietic protoporphyria (EPP), which is characterized by an accumulation of protoporphyrin IX in red blood cells, plasma, and other tissues. This accumulation results in photosensitivity, skin lesions, and potential complications such as liver dysfunction and gallstones.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Intramolecular transferases are a specific class of enzymes that catalyze the transfer of a functional group from one part of a molecule to another within the same molecule. These enzymes play a crucial role in various biochemical reactions, including the modification of complex carbohydrates, lipids, and nucleic acids. By facilitating intramolecular transfers, these enzymes help regulate cellular processes, signaling pathways, and metabolic functions.

The systematic name for this class of enzymes is: [donor group]-transferring intramolecular transferases. The classification system developed by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB) categorizes them under EC 2.5. This category includes enzymes that transfer alkyl or aryl groups, other than methyl groups; methyl groups; hydroxylyl groups, including glycosyl groups; and various other specific functional groups.

Examples of intramolecular transferases include:

1. Protein kinases (EC 2.7.11): Enzymes that catalyze the transfer of a phosphate group from ATP to a specific amino acid residue within a protein, thereby regulating protein function and cellular signaling pathways.
2. Glycosyltransferases (EC 2.4): Enzymes that facilitate the transfer of glycosyl groups between donor and acceptor molecules; some of these enzymes can catalyze intramolecular transfers, playing a role in the biosynthesis and modification of complex carbohydrates.
3. Methyltransferases (EC 2.1): Enzymes that transfer methyl groups between donor and acceptor molecules; some of these enzymes can catalyze intramolecular transfers, contributing to the regulation of gene expression and other cellular processes.

Understanding the function and regulation of intramolecular transferases is essential for elucidating their roles in various biological processes and developing targeted therapeutic strategies for diseases associated with dysregulation of these enzymes.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Pyridoxal is a form of vitamin B6, specifically the alcohol form of pyridoxine. It is a cofactor for many enzymes involved in protein metabolism and synthesis of neurotransmitters. Pyridoxal can be converted to its active form, pyridoxal 5'-phosphate (PLP), which serves as a coenzyme in various biochemical reactions, including transamination, decarboxylation, and racemization/elimination reactions. Deficiency in vitamin B6 can lead to neurological disorders and impaired synthesis of amino acids and neurotransmitters.

Ligases are a group of enzymes that catalyze the formation of a covalent bond between two molecules, usually involving the joining of two nucleotides in a DNA or RNA strand. They play a crucial role in various biological processes such as DNA replication, repair, and recombination. In DNA ligases, the enzyme seals nicks or breaks in the phosphodiester backbone of the DNA molecule by catalyzing the formation of an ester bond between the 3'-hydroxyl group and the 5'-phosphate group of adjacent nucleotides. This process is essential for maintaining genomic integrity and stability.

Erythroblasts are immature red blood cells that are produced in the bone marrow. They are also known as normoblasts and are a stage in the development of red blood cells, or erythrocytes. Erythroblasts are larger than mature red blood cells and have a nucleus, which is lost during the maturation process. These cells are responsible for producing hemoglobin, the protein that carries oxygen in the blood. Abnormal increases or decreases in the number of erythroblasts can be indicative of certain medical conditions, such as anemia or leukemia.

Immunologic tests are a type of diagnostic assay that detect and measure the presence or absence of specific immune responses in a sample, such as blood or tissue. These tests can be used to identify antibodies, antigens, immune complexes, or complement components in a sample, which can provide information about the health status of an individual, including the presence of infection, autoimmune disease, or immunodeficiency.

Immunologic tests use various methods to detect these immune components, such as enzyme-linked immunosorbent assays (ELISAs), Western blots, immunofluorescence assays, and radioimmunoassays. The results of these tests can help healthcare providers diagnose and manage medical conditions, monitor treatment effectiveness, and assess immune function.

It's important to note that the interpretation of immunologic test results should be done by a qualified healthcare professional, as false positives or negatives can occur, and the results must be considered in conjunction with other clinical findings and patient history.

Aspartate-tRNA ligase is an enzyme that plays a crucial role in protein synthesis. Its specific function is to join the amino acid aspartic acid to its corresponding transfer RNA (tRNA) molecule, forming an aspartyl-tRNA complex. This complex is essential for the accurate translation of genetic information encoded in messenger RNA (mRNA) into a polypeptide chain during protein synthesis.

The systematic name for this enzyme is L-aspartate:tRNA(Asn) ligase (AMP-forming), which reflects its role in catalyzing the reaction between aspartic acid and tRNA(Asn). The enzyme can also activate aspartic acid by forming an aspartyl-AMP intermediate before transferring the activated aspartate to the appropriate tRNA molecule.

Deficiencies or mutations in aspartate-tRNA ligase can lead to various genetic disorders and impairments in protein synthesis, which may have severe consequences for cellular function and overall health.

Methionine-tRNA Ligase is an enzyme involved in the process of protein synthesis. Its specific role is to catalyze the attachment of methionine, which is the first amino acid in a newly forming polypeptide chain, to its corresponding transfer RNA (tRNA) molecule. This enzyme binds methionine with a tRNAMet, creating a secure bond that allows for the accurate translation of genetic information from messenger RNA (mRNA) into a protein sequence during translation.

There are two types of Methionine-tRNA Ligases: one for cytoplasmic proteins and another for mitochondrial proteins. These enzymes play crucial roles in initiating protein synthesis within their respective cellular compartments, ensuring proper protein production and maintenance of cellular function.

Tryptophan-tRNA ligase is an enzyme that plays a crucial role in protein synthesis. Its primary function is to join tryptophan, one of the twenty standard amino acids, to its corresponding transfer RNA (tRNA) molecule. This enzyme catalyzes the formation of a peptide bond between tryptophan and the tRNA during the translation process, where genetic information from messenger RNA (mRNA) is translated into a specific protein sequence. The correct pairing of amino acids with their respective tRNAs is essential for maintaining the fidelity of protein synthesis and ensuring the production of functional proteins.

Iron-regulatory proteins (IRPs) are specialized RNA-binding proteins that play a crucial role in the post-transcriptional regulation of iron homeostasis in mammalian cells. They are named as such because they regulate the expression of genes involved in iron metabolism, primarily by binding to specific cis-acting elements known as iron-responsive elements (IREs) located within the untranslated regions (UTRs) of target mRNAs.

There are two main IRPs: IRP1 and IRP2. Both proteins contain an N-terminal RNA-binding domain that recognizes and binds to IREs, as well as a C-terminal region involved in protein-protein interactions and other regulatory functions. Under conditions of iron deficiency or oxidative stress, IRPs become activated and bind to IREs, leading to changes in mRNA stability, translation, or both.

IRP1 can exist in two distinct conformational states: an active RNA-binding form (when iron levels are low) and an inactive aconitase form (when iron levels are sufficient). In contrast, IRP2 is primarily regulated by protein degradation, with its stability being modulated by the presence or absence of iron.

By binding to IREs within mRNAs encoding proteins involved in iron uptake, storage, and utilization, IRPs help maintain cellular iron homeostasis through a variety of mechanisms, including:

1. Promoting translation of transferrin receptor 1 (TfR1) mRNA to increase iron import when iron levels are low.
2. Inhibiting translation of ferritin heavy chain and light chain mRNAs to reduce iron storage when iron levels are low.
3. Stabilizing the mRNA encoding divalent metal transporter 1 (DMT1) to enhance iron uptake under conditions of iron deficiency.
4. Promoting degradation of transferrin receptor 2 (TfR2) and ferroportin mRNAs to limit iron import and export, respectively, when iron levels are high.

Overall, the regulation of iron metabolism by IRPs is crucial for maintaining proper cellular function and preventing the accumulation of toxic free radicals generated by iron-catalyzed reactions.

Carbon-Nitrogen (C-N) ligases are a class of enzymes that catalyze the joining of a carbon atom from a donor molecule to a nitrogen atom in an acceptor molecule through a process called ligase reaction. This type of enzyme plays a crucial role in various biological processes, including the biosynthesis of amino acids, nucleotides, and other biomolecules that contain both carbon and nitrogen atoms.

C-N ligases typically require ATP or another energy source to drive the reaction forward, as well as cofactors such as metal ions or vitamins to facilitate the chemical bond formation between the carbon and nitrogen atoms. The specificity of C-N ligases varies depending on the enzyme, with some acting only on specific donor and acceptor molecules while others have broader substrate ranges.

Examples of C-N ligases include glutamine synthetase, which catalyzes the formation of glutamine from glutamate and ammonia, and asparagine synthetase, which catalyzes the formation of asparagine from aspartate and ammonia. Understanding the function and regulation of C-N ligases is important for understanding various biological processes and developing strategies to modulate them in disease states.

Protoporphyrins are organic compounds that are the immediate precursors to heme in the porphyrin synthesis pathway. They are composed of a porphyrin ring, which is a large, complex ring made up of four pyrrole rings joined together, with an acetate and a propionate side chain at each pyrrole. Protoporphyrins are commonly found in nature and are important components of many biological systems, including hemoglobin, the protein in red blood cells that carries oxygen throughout the body.

There are several different types of protoporphyrins, including protoporphyrin IX, which is the most common form found in humans and other animals. Protoporphyrins can be measured in the blood or other tissues as a way to diagnose or monitor certain medical conditions, such as lead poisoning or porphyrias, which are rare genetic disorders that affect the production of heme. Elevated levels of protoporphyrins in the blood or tissues can indicate the presence of these conditions and may require further evaluation and treatment.

Isoleucine-tRNA ligase is an enzyme involved in the process of protein synthesis in cells. Its specific role is to catalyze the attachment of the amino acid isoleucine to its corresponding transfer RNA (tRNA) molecule, which then participates in the translation of genetic information from messenger RNA (mRNA) into a polypeptide chain during protein synthesis. This enzyme helps ensure that the correct amino acids are incorporated into proteins according to the genetic code.

Aspartate-ammonia ligase, also known as aspartate transcarbamylase or ATC, is an enzyme that catalyzes the first reaction in the synthesis of pyrimidines, which are essential components of nucleotides and nucleic acids. The reaction catalyzed by aspartate-ammonia ligase is the condensation of aspartate and ammonia to form N-carbamoyl-L-aspartate and releases ADP and Pi. This enzyme plays a crucial role in the regulation of pyrimidine biosynthesis, and its activity is tightly regulated in response to changes in cellular demand for nucleotides. Defects in aspartate-ammonia ligase have been implicated in several genetic disorders, including ornithine transcarbamylase deficiency and citrullinemia.

Glycine is a simple amino acid that plays a crucial role in the body. According to the medical definition, glycine is an essential component for the synthesis of proteins, peptides, and other biologically important compounds. It is also involved in various metabolic processes, such as the production of creatine, which supports muscle function, and the regulation of neurotransmitters, affecting nerve impulse transmission and brain function. Glycine can be found as a free form in the body and is also present in many dietary proteins.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Pyridoxine is the chemical name for Vitamin B6. According to the medical definition, Pyridoxine is a water-soluble vitamin that is part of the B-vitamin complex and is essential for the metabolism of proteins, carbohydrates, and fats. It plays a vital role in the regulation of homocysteine levels in the body, the formation of neurotransmitters such as serotonin and dopamine, and the synthesis of hemoglobin.

Pyridoxine can be found naturally in various foods, including whole grains, legumes, vegetables, nuts, seeds, meat, poultry, and fish. It is also available as a dietary supplement and may be prescribed by healthcare providers to treat or prevent certain medical conditions, such as vitamin B6 deficiency, anemia, seizures, and carpal tunnel syndrome.

Like other water-soluble vitamins, Pyridoxine cannot be stored in the body and must be replenished regularly through diet or supplementation. Excessive intake of Pyridoxine can lead to toxicity symptoms such as nerve damage, skin lesions, and light sensitivity.

Phenylalanine-tRNA ligase, also known as Phe-tRNA synthetase, is an enzyme that plays a crucial role in protein synthesis. Its primary function is to catalyze the attachment of the amino acid phenylalanine to its corresponding transfer RNA (tRNA) molecule. This reaction forms a phenylalanine-tRNA complex, which is then used in the translation process to create proteins according to the genetic code. The systematic name for this enzyme is phenylalanyl-tRNA synthetase (EC 6.1.1.20). Any defects or mutations in the Phe-tRNA ligase can lead to various medical conditions, including neurological disorders and impaired growth.

Tyrosine-tRNA ligase is an enzyme that plays a crucial role in protein synthesis, specifically in the process of translating the genetic code from messenger RNA (mRNA) into proteins. More formally known as tyrosyl-tRNA synthetase, this enzyme is responsible for charging tRNA molecules with their specific amino acids. In this case, it catalyzes the attachment of the amino acid tyrosine to its corresponding transfer RNA (tRNA) molecule. This enzymatic reaction involves the activation of tyrosine with ATP to form an aminoacyl-AMP intermediate, followed by the transfer of the tyrosyl group from the intermediate to the 3' end of its appropriate tRNA. The resulting tyrosine-tRNA complex is then used in the translation process to incorporate tyrosine into the growing polypeptide chain during protein synthesis.

Photochemotherapy is a medical treatment that combines the use of drugs and light to treat various skin conditions. The most common type of photochemotherapy is PUVA (Psoralen + UVA), where the patient takes a photosensitizing medication called psoralen, followed by exposure to ultraviolet A (UVA) light.

The psoralen makes the skin more sensitive to the UVA light, which helps to reduce inflammation and suppress the overactive immune response that contributes to many skin conditions. This therapy is often used to treat severe cases of psoriasis, eczema, and mycosis fungoides (a type of cutaneous T-cell lymphoma). It's important to note that photochemotherapy can increase the risk of skin cancer and cataracts, so it should only be administered under the close supervision of a healthcare professional.

Spectrophotometry is a technical analytical method used in the field of medicine and science to measure the amount of light absorbed or transmitted by a substance at specific wavelengths. This technique involves the use of a spectrophotometer, an instrument that measures the intensity of light as it passes through a sample.

In medical applications, spectrophotometry is often used in laboratory settings to analyze various biological samples such as blood, urine, and tissues. For example, it can be used to measure the concentration of specific chemicals or compounds in a sample by measuring the amount of light that is absorbed or transmitted at specific wavelengths.

In addition, spectrophotometry can also be used to assess the properties of biological tissues, such as their optical density and thickness. This information can be useful in the diagnosis and treatment of various medical conditions, including skin disorders, eye diseases, and cancer.

Overall, spectrophotometry is a valuable tool for medical professionals and researchers seeking to understand the composition and properties of various biological samples and tissues.

Circular dichroism (CD) is a technique used in physics and chemistry to study the structure of molecules, particularly large biological molecules such as proteins and nucleic acids. It measures the difference in absorption of left-handed and right-handed circularly polarized light by a sample. This difference in absorption can provide information about the three-dimensional structure of the molecule, including its chirality or "handedness."

In more technical terms, CD is a form of spectroscopy that measures the differential absorption of left and right circularly polarized light as a function of wavelength. The CD signal is measured in units of millidegrees (mdeg) and can be positive or negative, depending on the type of chromophore and its orientation within the molecule.

CD spectra can provide valuable information about the secondary and tertiary structure of proteins, as well as the conformation of nucleic acids. For example, alpha-helical proteins typically exhibit a strong positive band near 190 nm and two negative bands at around 208 nm and 222 nm, while beta-sheet proteins show a strong positive band near 195 nm and two negative bands at around 217 nm and 175 nm.

CD spectroscopy is a powerful tool for studying the structural changes that occur in biological molecules under different conditions, such as temperature, pH, or the presence of ligands or other molecules. It can also be used to monitor the folding and unfolding of proteins, as well as the binding of drugs or other small molecules to their targets.

Leucine-tRNA Ligase, also known as Leucyl-tRNA Synthetase, is an enzyme (EC 6.1.1.4) that plays a crucial role in protein synthesis. This enzyme is responsible for catalyzing the esterification of the amino acid leucine to its corresponding transfer RNA (tRNA) molecule. The resulting leucine-tRNA complex is then used in the translation process, where genetic information encoded in mRNA is translated into a specific protein sequence.

The reaction catalyzed by Leucine-tRNA Ligase can be represented as follows:

Leucine + tRNA(Leu) + ATP → Leucyl-tRNA(Leu) + AMP + PP\_i

In this reaction, leucine is activated by attachment to an adenosine monophosphate (AMP) molecule with the help of ATP. The activated leucine is then transferred to the appropriate tRNA molecule, releasing AMP and inorganic pyrophosphate (PP\_i). This enzyme's function is essential for maintaining the accuracy of protein synthesis, as it ensures that only the correct amino acids are incorporated into proteins according to the genetic code.

Serine-tRNA ligase is an enzyme that plays a crucial role in protein synthesis, specifically in the attachment of the amino acid serine to its corresponding transfer RNA (tRNA) molecule. This enzyme catalyzes the formation of a ester bond between the carboxyl group of L-serine and the 3'-hydroxyl group of the tRNASerine, creating a charged tRNASerine molecule that can participate in protein synthesis on the ribosome.

The systematic name for this enzyme is L-serine:tRNA(Ser) ligase (AMP-forming), and it belongs to the family of ligases, specifically the transfer RNA ligases, which form aminoacyl-tRNA and related compounds. This enzyme is essential for maintaining the accuracy and fidelity of protein synthesis, as it ensures that the correct amino acid is attached to its corresponding tRNA molecule before being translated into a polypeptide chain on the ribosome.

Valine-tRNA Ligase is an enzyme that plays a crucial role in protein synthesis in the body. Its specific function is to catalyze the attachment of the amino acid valine to its corresponding transfer RNA (tRNA) molecule during translation, the process by which genetic information encoded in messenger RNA (mRNA) is used to synthesize proteins.

The reaction catalyzed by Valine-tRNA Ligase involves the activation of valine through the formation of an adenylate intermediate with ATP, followed by the transfer of valine to the appropriate tRNA molecule. This enzyme is essential for maintaining the fidelity and efficiency of protein synthesis, as it ensures that the correct amino acid is incorporated into the growing polypeptide chain during translation.

Valine-tRNA Ligase is a member of the class II aminoacyl-tRNA synthetases and contains several functional domains, including an anticodon-binding domain that recognizes and binds to specific tRNA molecules, and a catalytic domain that carries out the reaction with valine. Mutations in the gene encoding Valine-tRNA Ligase have been associated with various genetic disorders, highlighting its importance in maintaining normal cellular function.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Argininosuccinate synthase (ASS) is a urea cycle enzyme that plays a crucial role in the detoxification of ammonia in the body. This enzyme catalyzes the reaction that combines citrulline and aspartate to form argininosuccinate, which is subsequently converted to arginine and fumarate in the urea cycle.

The reaction catalyzed by argininosuccinate synthase is as follows:

Citrulline + Aspartate + ATP → Argininosuccinate + AMP + PPi

Deficiency in argininosuccinate synthase leads to a genetic disorder known as citrullinemia, which is characterized by an accumulation of ammonia in the blood and neurodevelopmental abnormalities. There are two forms of citrullinemia, type I and type II, with type I being more severe and caused by mutations in the ASS1 gene located on chromosome 9q34.

Acetate-CoA ligase is an enzyme that plays a role in the metabolism of acetate in cells. The enzyme catalyzes the conversion of acetate and coenzyme A (CoA) to acetyl-CoA, which is a key molecule in various metabolic pathways, including the citric acid cycle (also known as the Krebs cycle).

The reaction catalyzed by Acetate-CoA ligase can be summarized as follows:

acetate + ATP + CoA → acetyl-CoA + AMP + PPi

In this reaction, acetate is activated by combining it with ATP to form acetyl-AMP, which then reacts with CoA to produce acetyl-CoA. The reaction also produces AMP and pyrophosphate (PPi) as byproducts.

There are two main types of Acetate-CoA ligases: the short-chain fatty acid-CoA ligase, which is responsible for activating acetate and other short-chain fatty acids, and the acyl-CoA synthetase, which activates long-chain fatty acids. Both types of enzymes play important roles in energy metabolism and the synthesis of various biological molecules.

Enzyme induction is a process by which the activity or expression of an enzyme is increased in response to some stimulus, such as a drug, hormone, or other environmental factor. This can occur through several mechanisms, including increasing the transcription of the enzyme's gene, stabilizing the mRNA that encodes the enzyme, or increasing the translation of the mRNA into protein.

In some cases, enzyme induction can be a beneficial process, such as when it helps the body to metabolize and clear drugs more quickly. However, in other cases, enzyme induction can have negative consequences, such as when it leads to the increased metabolism of important endogenous compounds or the activation of harmful procarcinogens.

Enzyme induction is an important concept in pharmacology and toxicology, as it can affect the efficacy and safety of drugs and other xenobiotics. It is also relevant to the study of drug interactions, as the induction of one enzyme by a drug can lead to altered metabolism and effects of another drug that is metabolized by the same enzyme.

Glutamate-tRNA ligase is an enzyme involved in the process of protein synthesis, specifically during the charging or aminoacylation of transfer RNA (tRNA). This enzyme is responsible for catalyzing the reaction between glutamic acid (Glu) and its corresponding tRNA molecule (tRNAGlu), forming a covalent bond between them. The resulting product, Glu-tRNAGlu, then participates in the translation of messenger RNA (mRNA) into a specific protein sequence at the ribosome.

The reaction catalyzed by glutamate-tRNA ligase is as follows:

Glutamic acid + ATP + tRNAGlu ↔ Glu-tRNAGlu + AMP + PP~i~ (pyrophosphate)

This enzyme plays a crucial role in maintaining the accuracy and efficiency of protein synthesis, ensuring that the correct amino acids are incorporated into proteins according to the genetic code. Defects or mutations in glutamate-tRNA ligase can lead to various genetic disorders and impairments in cellular function.

... succinyl-CoA synthetase, and mitoferrin-1. Multiple studies have suggested the existence of an oligomeric complex that enables ... 269 (1): 390-5. doi:10.1016/S0021-9258(17)42362-3. PMID 8276824. Wang X, Poh-Fitzpatrick M, Carriero D, Ostasiewicz L, Chen T, ... 89 (1): 281-5. Bibcode:1992PNAS...89..281N. doi:10.1073/pnas.89.1.281. PMC 48220. PMID 1729699. Lamoril J, Boulechfar S, de ... 378 (5): 1074-1083. doi:10.1016/j.jmb.2008.03.040. PMC 2852141. PMID 18423489. Bencze, Krisztina Z.; Yoon, Taejin; Mill?n- ...
... amino acyl-trna synthetases MeSH D08.811.464.263.200.050 - alanine-tRNA ligase MeSH D08.811.464.263.200.100 - arginine-tRNA ... atp synthetase complexes MeSH D08.811.913.696.650.150.500 - proton-translocating atpases MeSH D08.811.913.696.650.150.500.249 ... fatty acid synthetase complex MeSH D08.811.600.391 - glycine decarboxylase complex MeSH D08.811.600.391.100 - ... uroporphyrinogen iii synthetase MeSH D08.811.520.241.700 - polysaccharide-lyases MeSH D08.811.520.241.700.350 - chondroitinases ...
Succinyl-CoA synthetase (SCS) is a mitochondrial matrix enzyme that acts as a heterodimer, being composed of an invariant alpha ... Succinyl-CoA synthetase SUCLG1 SUCLG2 GRCh38: Ensembl release 89: ENSG00000136143 - Ensembl, May 2017 GRCm38: Ensembl release ... Furuyama K, Sassa S (March 2000). "Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is ... Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial (SUCLA2), also known as ADP-forming succinyl-CoA synthetase (SCS- ...
The gene ann1 encodes an ATP-dependent amide synthetase and is predicted to condense the amine of the C5N group with the ... Moreover, module 5 contains a dehydratase (DH) domain that is not functional. Kalan, Lindsay; Gessner, Arne; Thaker, Maulik N ... The ann5 gene product is organized in modules 4 and 5, the latter terminating with a thioesterase domain. One of the most ... The ann2 gene encodes a 5-aminolevulinate synthase which condenses glycine and succinyl-CoA in a Claisen-like reaction to form ...
... argininosuccinate synthetase BANCR: encoding protein BRAF-activated non-protein coding RNA BNC2: zinc finger protein basonuclin ... aminolevulinate, delta-, dehydratase ALS4: amyotrophic lateral sclerosis 4 ANGPTL2: angiopoietin-related protein 2 ASS: ... 5 (2): 157-74. doi:10.1089/109065701753145664. PMID 11551106. Humphray SJ, Oliver K, Hunt AR, et al. (2004). "DNA sequence and ... 11 (5): 206. doi:10.1186/gb-2010-11-5-206. PMC 2898077. PMID 20441615. "Statistics & Downloads for chromosome 9". HUGO Gene ...
"Entrez Gene: Delta-aminolevulinate synthase 2". Han L, Zhong Y, Huang B, Han L, Pan L, Xu X, Wang X, Huang B, Lu J (2008). " ... Furuyama K, Sassa S (Mar 2000). "Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is ... Delta-aminolevulinate synthase 2 also known as ALAS2 is a protein that in humans is encoded by the ALAS2 gene. ALAS2 is an ... Bishop DF, Henderson AS, Astrin KH (Jun 1990). "Human delta-aminolevulinate synthase: assignment of the housekeeping gene to ...
Partial list of the genes located on p-arm (short arm) of human chromosome 3: ALAS1: aminolevulinate, delta-, synthase 1 APEH: ... leucyl-tRNA synthetase, mitochondrial LIMD1: LIM domain-containing protein 1 LOC105377021: encoding protein LOC105377021 ... 11 (5): 206. doi:10.1186/gb-2010-11-5-206. PMC 2898077. PMID 20441615. "Statistics & Downloads for chromosome 3". HUGO Gene ... ETS variant 5 FAM3D: family with sequence similarity 3, member D FAM43A: family with sequence similarity 43 member A FAM162A: ...
Additionally, alcohol has been shown to increase the activity of the delta-aminolevulinic acid synthetase (ALA synthetase), the ... 14 (38): 5913-5. doi:10.3748/wjg.14.5913. PMC 2751904. PMID 18855993. Sökmen, M; Demirsoy, H; Ersoy, O; Gökdemir, G; Akbayir, N ... 18 (3): 200-5. PMID 17891697. Frank, J; Poblete-Gutiérrez, P; Weiskirchen, R; Gressner, O; Merk, H. F.; Lammert, F (2006). " ... 58 (5): 1089-97. doi:10.1172/JCI108560. PMC 333275. PMID 993332. Di Padova, C.; Marchesi, L.; Cainelli, T.; Gori, G.; Podenzani ...
AKs are one of the most common dermatologic lesions for which photodynamic therapy, including topical methyl aminolevulinate ( ... destroys AKs by blocking methylation of thymidylate synthetase, thereby interrupting DNA and RNA synthesis. This in turn ... Topical 5-FU is the most utilized treatment for AK, and often results in effective removal of the lesion. Overall, there is a ... 5-FU may be up to 90% effective in treating non-hyperkeratotic lesions. While topical 5-FU is a widely used and cost-effective ...
... aminolevulinate transaminase EC 2.6.1.44: alanine-glyoxylate transaminase EC 2.6.1.45: serine-glyoxylate transaminase EC 2.6. ... glutamine synthetase]-adenylyl-L-tyrosine phosphorylase EC 2.7.7.90: 8-amino-3,8-dideoxy-manno-octulosonate ... glutamine synthetase] adenylyltransferase EC 2.7.7.43: N-acylneuraminate cytidylyltransferase EC 2.7.7.44: glucuronate-1- ... 5-hydroxyanthranilate N-hydroxycinnamoyltransferase (*) EC 2.3.1.303: α-L-Rha-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-α-D-Gal-PP-Und ...
... succinyl-CoA synthetase, and mitoferrin-1. Multiple studies have suggested the existence of an oligomeric complex that enables ... 269 (1): 390-5. doi:10.1016/S0021-9258(17)42362-3. PMID 8276824. Wang X, Poh-Fitzpatrick M, Carriero D, Ostasiewicz L, Chen T, ... 89 (1): 281-5. Bibcode:1992PNAS...89..281N. doi:10.1073/pnas.89.1.281. PMC 48220. PMID 1729699. Lamoril J, Boulechfar S, de ... 378 (5): 1074-1083. doi:10.1016/j.jmb.2008.03.040. PMC 2852141. PMID 18423489. Bencze, Krisztina Z.; Yoon, Taejin; Mill?n- ...
Aminolevulinate synthase: lysine 313 is not essential for binding the pyridoxal phosphate cofactor but is essential for ... Towards this goal, our on-going research focuses on establishing 1) whether succinyl-CoA synthetase b-subunit allosterically ... Transient kinetic studies support refinements to the chemical and kinetic mechanisms of aminolevulinate synthase. The Journal ... Aspartate-279 in aminolevulinate synthase affects enzyme catalysis through enhancing the function of the pyridoxal 5- ...
Early-onset biotin-responsive multiple carboxylase deficiency, see Holocarboxylase synthetase deficiency. *Early-onset combined ... Epiphyseal dysplasia, multiple, 5, see Multiple epiphyseal dysplasia. *Epiphyseal dysplasia, Ribbing type, see Multiple ... Erythroid 5-aminolevulinate synthase deficiency, see X-linked sideroblastic anemia. *Erythrokeratodermia variabilis, see ... carboxylase deficiency, see Holocarboxylase synthetase deficiency. *Early-onset generalized torsion dystonia, see Early-onset ...
Ceramide Synthetase Term UI T164314. LexicalTag NON. ThesaurusID NLM (2006). Fatty Acyl-CoA - Sphingosine Acyltransferase Term ... Ceramide Synthetase Fatty Acyl-CoA - Sphingosine Acyltransferase Sphingosine Acyltransferase Registry Number. EC 2.3.1.24. ...
... achlorobenzene on the activities of hepatic delta-amino levulinate synthetase, delta-amino levulinate dehydratase and ... 5: 277-282 (1985). 54. Duverger-vanBogaert, M., Stecca, C., and Leonard, A. Detection of mutagenic activity in urine samples ... 121) phenyl ring; negative in < 2 or >3 halogens each ring, in CEL cellsb t Uro 3,4,5,3 ,4 ,5 - Hexachlorobiphenyl, lindane, ... The National Research Council study prinarily dealt with effect markers (5). Although both exposure and outcome measures are ...
Methyl aminolevulinate cream is a porphyrin precursor used in combination with narrow-band, red-light illumination for ... It interferes with DNA synthesis by blocking methylation of deoxyuridylic acid and inhibiting thymidylate synthetase and, ... Photodynamic therapy using methyl aminolevulinate acid in eyelid basal cell carcinoma: a 5-year follow-up study. Ophthal Plast ... Five-year follow-up of a randomized, prospective trial of topical methyl aminolevulinate photodynamic therapy vs surgery for ...
3-Deoxyarabinoheptulosonate-7-Phosphate Synthetase use 3-Deoxy-7-Phosphoheptulonate Synthase 3 End Processing, RNA use RNA 3 ... 2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 5,10-Methylenetetrahydrofolate-Reductase (NADH) use Methylenetetrahydrofolate Dehydrogenase (NAD+) 5,12-DiHETE use Leukotriene ... 3,5-Cyclic-Nucleotide Phosphodiesterase use 3,5-Cyclic-AMP Phosphodiesterases 3-alpha-Hydroxysteroid Dehydrogenase (B- ...
3-Deoxyarabinoheptulosonate-7-Phosphate Synthetase use 3-Deoxy-7-Phosphoheptulonate Synthase 3-Hydroxy-3-methylglutaric Acid ... 2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 5,10-Methylenetetrahydrofolate-Reductase (NADH) use Methylenetetrahydrofolate Dehydrogenase (NAD+) 5,12-diHETE use Leukotriene ... 3-Keto-5-alpha-Steroid delta-4-Dehydrogenase use 3-Oxo-5-alpha-Steroid 4-Dehydrogenase ...
ALA synthetase activity is also closely associated with cytochrome P-450 activity. Induction of the P-450 system by exogenous ... delta-Aminolevulinate dehydratase (ALAD) porphyria: the first case in North America with two novel ALAD mutations. Mol Genet ... Highly heterogeneous nature of delta-aminolevulinate dehydratase (ALAD) deficiencies in ALAD porphyria. Blood. 2001 May 15. 97( ... Decreased heme production de-represses ALA synthetase and further increases ALA levels. Urine coproporphyrin III and ...
It involves topical application of a photosensitizer (eg, aminolevulinate, methyl aminolevulinate) followed by light of a ... 5-FU 5% cream is applied 2 times a day for 3 to 4 weeks. A recent study has shown 5-FU to be the most effective treatment for ... Early data suggest that combining 5% FU cream with 0.005% calcipotriol may enhance efficacy of 5-FU (2 Довідкові матеріали щодо ... Topical fluorouracil (5-FU) cream and imiquimod cream are the usual first-line drug treatments. Alternatives include diclofenac ...
3-Deoxyarabinoheptulosonate-7-Phosphate Synthetase use 3-Deoxy-7-Phosphoheptulonate Synthase 3-Hydroxy-3-methylglutaric Acid ... 2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 5,10-Methylenetetrahydrofolate-Reductase (NADH) use Methylenetetrahydrofolate Dehydrogenase (NAD+) 5,12-diHETE use Leukotriene ... 3-Keto-5-alpha-Steroid delta-4-Dehydrogenase use 3-Oxo-5-alpha-Steroid 4-Dehydrogenase ...
ALA synthetase activity is also closely associated with cytochrome P-450 activity. Induction of the P-450 system by exogenous ... delta-Aminolevulinate dehydratase (ALAD) porphyria: the first case in North America with two novel ALAD mutations. Mol Genet ... Highly heterogeneous nature of delta-aminolevulinate dehydratase (ALAD) deficiencies in ALAD porphyria. Blood. 2001 May 15. 97( ... Decreased heme production de-represses ALA synthetase and further increases ALA levels. Urine coproporphyrin III and ...
ALA synthetase activity is also closely associated with cytochrome P-450 activity. Induction of the P-450 system by exogenous ... delta-Aminolevulinate dehydratase (ALAD) porphyria: the first case in North America with two novel ALAD mutations. Mol Genet ... Inoue R, Akagi R. Co-synthesis of human delta-aminolevulinate dehydratase (ALAD) mutants with the wild-type enzyme in cell-free ... de Verneuil H, Doss M, Brusco N, Beaumont C, Nordmann Y. Hereditary hepatic porphyria with delta aminolevulinate dehydrase ...
histidyl-tRNA synthetase 1 [Sourc.... HDAC1. 3065. HDAC1. histone deacetylase 1 [Source:HGN.... ... aminolevulinate synthase 2 [So.... ARHGAP20. 57569. ARHGAP20. Rho GTPase activating protein 20 .... ...
Rat ALAS1(Aminolevulinate Delta Synthase 1) ELISA Kit. *Mouse TNNT2(Troponin T Type 2, Cardiac) ELISA Kit ... Rat GS(Glutamine synthetase) ELISA Kit. *Rat LIPE(Lipase, Hormone Sensitive) ELISA Kit ... Rat IGFBP5(Insulin Like Growth Factor Binding Protein 5) ELISA Kit. *Cattle TGFb2(Transforming Growth Factor Beta 2) ELISA Kit ... Human FAM5C(Family With Sequence Similarity 5, Member C) ELISA Kit. *Rat ARNTL(Aryl Hydrocarbon Receptor Nuclear Translocator ...
Moreover, molecular docking was used to evaluate the binding affinity with the S. aureus tyrosyl-tRNA synthetase as the ... Field cancerization treatment using topical photodynamic therapy: A comparison between two aminolevulinate derivatives. ... aureus tyrosyl-tRNA synthetase. Finally, residues Tyr36, Asp40, and Asp177 contact curcumin and may contribute to orienting the ... in field cancerization using two aminolevulinate derivatives. Forty patients with multiple actinic keratosis (AK) on forearms ...
Human ALAD(Aminolevulinate Delta Dehydratase) ELISA Kit. *Human ALDM(Aldehyde Dehydrogenase, Mitochondrial) ELISA Kit ... Oligoadenylate Synthetase 1) ELISA Kit. *Human OCLN(Occludin) ELISA Kit ... Human IGFBP5(Insulin Like Growth Factor Binding Protein 5) ELISA Kit. *Human IGFBP7(Insulin Like Growth Factor Binding Protein ... Human IGFBP5(Insulin Like Growth Factor Binding Protein 5) ELISA Kit. *Human IGFBP7(Insulin Like Growth Factor Binding Protein ...
... in four unrelated male probands was caused by missense mutations in the erythroid-specific 5-aminolevulinate synthase gene ( ... Missense mutations in the erythroid delta-aminolevulinate synthase (ALAS2) gene in two pyridoxine-responsive patients initially ... 5-Aminolevulinate synthase catalysis: The catcher in heme biosynthesis. Stojanovski BM, Hunter GA, Na I, Uversky VN, Jiang RHY ... 2018 May 14;39(5):414-419. doi: 10.3760/cma.j.issn.0253-2727.2018.05.014. Zhonghua Xue Ye Xue Za Zhi. 2018. PMID: 29779353 Free ...
... δ-aminolevulinate synthetase; δ-aminolevulinic acid synthase; δ-aminolevulinic acid synthetase; δ-aminolevulinic synthetase; 5- ... aminolevulinate synthetase; aminolevulinic acid synthase; aminolevulinic acid synthetase; aminolevulinic synthetase. Systematic ... aminolevulinate synthetase; 5-aminolevulinic acid synthetase; ALA synthetase; aminolevulinate synthase; ... Scholnick, P.L., Hammaker, L.E. and Marver, H.S. Soluble δ-aminolevulinic acid synthetase of rat liver. I. Some properties of ...
1980;12(5-6):941-6. doi: 10.1016/0020-711x(80)90189-5. Int J Biochem. 1980. PMID: 7450153 No abstract available. ... 1987 Sep-Oct;2(5):324-37. doi: 10.1007/BF03259952. Med Toxicol Adverse Drug Exp. 1987. PMID: 3312929 Review. ... 1984;26(5):587-90. doi: 10.1007/BF00543490. Eur J Clin Pharmacol. 1984. PMID: 6468473 ... 1980 Sep-Oct;10(5):395-401. Ann Clin Lab Sci. 1980. PMID: 6999973 Review. ...
Aminolevulinic Acid Synthetase delta-Aminolevulinate Synthase delta-Aminolevulinic Acid Synthetase Registry Number. EC 2.3.1.37 ... delta-Aminolevulinic Acid Synthetase Term UI T001868. Date06/25/1981. LexicalTag NON. ThesaurusID UNK (19XX). ... delta-Aminolevulinate Synthase Term UI T001867. Date05/01/1997. LexicalTag NON. ThesaurusID NLM (1998). ... Aminolevulinic Acid Synthetase Term UI T001866. Date12/03/1996. LexicalTag NON. ThesaurusID NLM (1998). ...
Aminolevulinic Acid Synthetase delta-Aminolevulinate Synthase delta-Aminolevulinic Acid Synthetase Registry Number. EC 2.3.1.37 ... delta-Aminolevulinic Acid Synthetase Term UI T001868. Date06/25/1981. LexicalTag NON. ThesaurusID UNK (19XX). ... delta-Aminolevulinate Synthase Term UI T001867. Date05/01/1997. LexicalTag NON. ThesaurusID NLM (1998). ... Aminolevulinic Acid Synthetase Term UI T001866. Date12/03/1996. LexicalTag NON. ThesaurusID NLM (1998). ...
Synthetase, delta-Aminolevulinic Acid delta Aminolevulinate Synthase delta Aminolevulinic Acid Synthetase delta-Aminolevulinate ... delta Aminolevulinic Acid Synthetase. delta-Aminolevulinate Synthase. delta-Aminolevulinic Acid Synthetase. Tree number(s):. ... Synthetase, Aminolevulinic Acid. Synthetase, delta-Aminolevulinic Acid. delta Aminolevulinate Synthase. ... Acid Synthetase, Aminolevulinic Acid Synthetase, delta-Aminolevulinic Aminolevulinic Acid Synthetase Synthase, 5- ...
Unsaturated N0000167864 Fatty Acid Desaturases N0000167741 Fatty Acid Synthetase Complex N0000178814 Fatty Acid Synthetase ... Oligoadenylate Synthetase N0000167243 2,2-Dipyridyl N0000166927 2,3,4,5-Tetrahydro-7,8-dihydroxy-1-phenyl-1H-3-benzazepine ... Sulfur N0000167776 Amino Acyl-tRNA Synthetases N0000007838 Amino Alcohols N0000008208 Amino Sugars N0000168141 Amino-Acid N- ... Lyase N0000168360 ATP Phosphoribosyltransferase N0000168256 ATP Synthetase Complexes N0000011431 ATP-Binding Cassette ...
Oligoadenylate Synthetase D8.586.913.696.445.625 D8.811.913.696.445.625 2-Acetolactate Mutase D8.586.399.520.100 D8.811.399.520 ... D10.212.507 Fatty Acid Synthetase Complex D8.586.600.317 D8.811.600.317 Fatty Acids D10.516.251 D10.251 Fatty Acids, Essential ... B1.500.841.800.800.800 Squalene Synthetase D8.586.682.820 D8.811.682.675.700 Squid B1.644.857 B1.500.644.857 src-Family Kinases ... D8.811.913.400.725.200 ATP Synthetase Complexes D8.586.913.696.650.150 D8.811.913.696.650.150 Atracurium D3.438.531.70 D3.438. ...
Methyl aminolevulinate cream is a porphyrin precursor used in combination with narrow-band, red-light illumination for ... It interferes with DNA synthesis by blocking methylation of deoxyuridylic acid and inhibiting thymidylate synthetase and, ... Photodynamic therapy using methyl aminolevulinate acid in eyelid basal cell carcinoma: a 5-year follow-up study. Ophthal Plast ... Five-year follow-up of a randomized, prospective trial of topical methyl aminolevulinate photodynamic therapy vs surgery for ...
An enzyme that, in the presence of ATP and COENZYME A, catalyzes the cleavage of citrate to yield acetyl CoA, oxaloacetate, ADP, and ORTHOPHOSPHATE. This reaction represents an important step in fatty acid biosynthesis. This enzyme was formerly listed as EC 4.1.3.8 ...
3-Oxoacyl Synthetase Acyl-Malonyl-ACP Condensing Enzyme beta Keto Acyl Synthetase beta Keto-Acyl Carrier Protein Synthase I ... beta Keto Acyl Synthetase Term UI T044080. Date06/03/1982. LexicalTag NON. ThesaurusID UNK (19XX). ... 3-Oxoacyl Synthetase Term UI T044079. Date06/29/1983. LexicalTag NON. ThesaurusID UNK (19XX). ... 9077-10-5. Scope Note. An enzyme of long-chain fatty acid synthesis, that adds a two-carbon unit from malonyl-(acyl carrier ...
Malate Synthetase Term UI T024735. Date04/14/1976. LexicalTag NON. ThesaurusID UNK (19XX). ... Malate Synthetase Registry Number. EC 2.3.3.9. Related Numbers. 9013-48-3. CAS Type 1 Name. L-Malate glyoxylate-lyase (CoA- ...
Induction of glutamate-cysteine ligase (gamma-glutamylcysteine synthetase) in the brains of adult female mice subchronically ... and cadmium-induced inhibition of δ-aminolevulinate dehydratase. Toxicology 184:85-9512499112. Crossref, Medline, Google ... Environ Health Perspect 110(suppl 5):689-69412426113. Link, Google Scholar. *Ballatori N, Lieberman MW, Wang W. 1998. N- ...
3-Deoxyarabinoheptulosonate-7-Phosphate Synthetase use 3-Deoxy-7-Phosphoheptulonate Synthase 3-Hydroxy-3-methylglutaric Acid ... 2-Amino-5-phosphonovaleric Acid use 2-Amino-5-phosphonovalerate 2-Amino-6-(1,2,3-trihydroxypropyl)-4(3H)-pteridinone use ... 5,10-Methylenetetrahydrofolate-Reductase (NADH) use Methylenetetrahydrofolate Dehydrogenase (NAD+) 5,12-diHETE use Leukotriene ... 3-Keto-5-alpha-Steroid delta-4-Dehydrogenase use 3-Oxo-5-alpha-Steroid 4-Dehydrogenase ...
It involves topical application of a photosensitizer (eg, aminolevulinate, methyl aminolevulinate) followed by light of a ... 5-FU 5% cream is applied 2 times a day for 3 to 4 weeks. A recent study has shown 5-FU to be the most effective treatment for ... Topical fluorouracil (5-FU) cream and imiquimod cream are the usual first-line drug treatments. Alternatives include diclofenac ... Early data suggest that combining 5% FU cream with 0.005% calcipotriol may enhance efficacy of 5-FU (2 Treatment references ...
... fatty acyl CoA synthetase F.A.C.S.,fatty acyl coenzyme A synthetase F.A.C.S.,fatty acyl-CoA synthetase F.A.C.S.,fatty acyl- ... aminolevulinate Ala,aminolevulinic acid Ala,amoebic liver abscess alpha-1-at,alpha 1 anti-trypsin alpha-1-at,alpha 1 anti- ... adenosyl methionine synthetase A.M.S.,adenosylmethionine synthetase A.M.S.,aerosol mass spectrometer A.M.S.,ageing male symptom ... coenzyme A synthetase F.A.C.S.,Fellow of the American College of Surgeons F.A.C.S.,Fellow of the American College of Surgeons F ...
Increased heme oxygenase-1 and decreased delta-aminolevulinate synthase expression in the liver of patients with acute liver ... biliverdin IXalpha reductase and delta-aminolevulinic acid synthetase 1 in rats with wild-type or variant AH receptor. ... 5. Enhancement of Cancer-Specific Protoporphyrin IX Fluorescence by Targeting Oncogenic Ras/MEK Pathway.. Yoshioka E; Chelakkot ... Expression levels of PEPT1 and ABCG2 play key roles in 5-aminolevulinic acid (ALA)-induced tumor-specific protoporphyrin IX ( ...
Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This ... Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta- ... 058769 12.57 glutamine synthetase Glul Rattus norvegicus " Essential for proliferation of fetal skin fibroblasts. This enzyme ... 075592 2.69 acetoacetyl-CoA synthetase Aacs Rattus norvegicus Activates acetoacetate to acetoacetyl-CoA. May be involved in ...
... fatty acyl CoA synthetase F.A.C.S.,fatty acyl coenzyme A synthetase F.A.C.S.,fatty acyl-CoA synthetase F.A.C.S.,fatty acyl- ... aminolevulinate Ala,aminolevulinic acid Ala,amoebic liver abscess alpha-1-at,alpha 1 anti-trypsin alpha-1-at,alpha 1 anti- ... adenosyl methionine synthetase A.M.S.,adenosylmethionine synthetase A.M.S.,aerosol mass spectrometer A.M.S.,ageing male symptom ... coenzyme A synthetase F.A.C.S.,Fellow of the American College of Surgeons F.A.C.S.,Fellow of the American College of Surgeons F ...
In support of this hypothesis, red blood cells in sir zebrafish mutants lack aminolevulinate synthase 2 (ALAS2), the first ... glutamine synthetase, and arginase. Mn is transported through the body by transferrin, macroglobulins, and albumin (Fraga, 2005 ... 5:33. doi: 10.3389/fphar.2014.00033. Received: 24 January 2014; Paper pending published: 12 February 2014;. Accepted: 17 ... The copper metabolism-related proteins in fish and mammals are summarized in Table 5, and the currently available fish and ...
ALA synthetase activity is also closely associated with cytochrome P-450 activity. Induction of the P-450 system by exogenous ... delta-Aminolevulinate dehydratase (ALAD) porphyria: the first case in North America with two novel ALAD mutations. Mol Genet ... Highly heterogeneous nature of delta-aminolevulinate dehydratase (ALAD) deficiencies in ALAD porphyria. Blood. 2001 May 15. 97( ... Decreased heme production de-represses ALA synthetase and further increases ALA levels. Urine coproporphyrin III and ...
ALA synthetase activity is also closely associated with cytochrome P-450 activity. Induction of the P-450 system by exogenous ... delta-Aminolevulinate dehydratase (ALAD) porphyria: the first case in North America with two novel ALAD mutations. Mol Genet ... Highly heterogeneous nature of delta-aminolevulinate dehydratase (ALAD) deficiencies in ALAD porphyria. Blood. 2001 May 15. 97( ... Decreased heme production de-represses ALA synthetase and further increases ALA levels. Urine coproporphyrin III and ...
The synthesis of ALA is normally tightly controlled by feedback inhibition of the enzyme, ALA synthetase, presumably by ... aminolevulinate 200 MG/ML Topical Solution. SCD. 3. 762672. aminolevulinate 20 % Topical Solution. SY. ... TABLE 5 Post-PDT Cutaneous Adverse Events - ALA-018/ALA-019 FACE. SCALP. ... Table 5 depicts the incidence and severity of cutaneous adverse events, stratified by anatomic site treated. ...
... and L-malic acids involved in the glyoxylate cycle significantly accumulated and the malate synthetase gene was up-regulated in ... L-Glutamic acid and 5-Aminolevulinate involved in chlorophyll synthesis decreased under salt stress and alkali stress. The ... involved in pyruvate-citrate metabolism increased distinctly and genes encoding pyruvate decarboxylase and citrate synthetase ...
Localization and nucleotide specificity of Blastocystis succinyl-CoA synthetase. Mol. Microbiol. 68: 1395-1405 ... 17(16): 1420-5. *Andersson, J. O., Sjogren, A. M., Horner, D. S., Murphy, C. A., Dyal, P. L., Svard, S. G., Logsdon, J. M. Jr ... Biology Direct 7: 5.. *Torruella, G., Derelle, R., Paps, J., Lang, B.F., Roger, A.J., Shalchian-Tabrizi, K. and Ruiz-Trillo, I ... Open Sci., 5: 171707. *Leger, M.M., Eme, L., Stairs, C.W. and Roger, A.J. (2018) Demystifying eukaryote lateral gene transfer ( ...
Rat ALAS1(Aminolevulinate Delta Synthase 1) ELISA Kit. *Mouse TNNT2(Troponin T Type 2, Cardiac) ELISA Kit ... Rat GS(Glutamine synthetase) ELISA Kit. *Rat LIPE(Lipase, Hormone Sensitive) ELISA Kit ... Rat IGFBP5(Insulin Like Growth Factor Binding Protein 5) ELISA Kit. *Cattle TGFb2(Transforming Growth Factor Beta 2) ELISA Kit ... Human FAM5C(Family With Sequence Similarity 5, Member C) ELISA Kit. *Rat ARNTL(Aryl Hydrocarbon Receptor Nuclear Translocator ...
  • Our main research interest is defining the reaction and regulatory mechanisms of the first and terminal heme biosynthetic pathway enzymes, 5-aminolevulinate synthase (ALAS) and ferrochelatase (FC). (usf.edu)
  • Isoniazid inhibits human erythroid 5-aminolevulinate synthase: Molecular mechanism and tolerance study with four X-linked protoporphyria patients. (usf.edu)
  • Molecular dynamics analysis of the structural and dynamic properties of the functionally enhanced hepta-variant of mouse 5-aminolevulinate synthase. (usf.edu)
  • The unfolding pathways of the native and molten globule states of 5-aminolevulinate synthase. (usf.edu)
  • Murine erythroid 5-aminolevulinate synthase: Truncation of a disordered N-terminal extension is not detrimental for catalysis. (usf.edu)
  • Macromolecular Crowders and Osmolytes Modulate the Structural and Catalytic Properties of Alkaline Molten Globular 5-Aminolevulinate Synthase. (usf.edu)
  • Asn-150 of Murine Erythroid 5-Aminolevulinate Synthase Modulates the Catalytic Balance between the Rates of the Reversible Reaction. (usf.edu)
  • Murine erythroid 5-aminolevulinate synthase: Adenosyl-binding site Lys221 modulates substrate binding and catalysis. (usf.edu)
  • Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release. (usf.edu)
  • Catalytically active alkaline molten globular enzyme: Effect of pH and temperature on the structural integrity of 5-aminolevulinate synthase. (usf.edu)
  • A review of the disease progression among the eight reported cases found an elevation in circulating levels of the rate-limiting hepatic enzyme 5-aminolevulinic acid synthase-1 (ALAS1) and response to treatment with hemin. (medscape.com)
  • 5'-aminolevulinate synthase 2 [So. (gsea-msigdb.org)
  • Towards this goal, our on-going research focuses on establishing 1) whether succinyl-CoA synthetase b-subunit allosterically fine-tunes the activity of erythroid ALAS and 2) the mechanism of Fe2+ delivery to FC. (usf.edu)
  • Decreased heme production de-represses ALA synthetase and further increases ALA levels. (medscape.com)
  • 5-Aminolevulinic acid dehydratase deficiency porphyria: a twenty-year clinical and biochemical follow-up. (medscape.com)
  • delta-Aminolevulinate dehydratase (ALAD) porphyria: the first case in North America with two novel ALAD mutations. (medscape.com)
  • Phosphoribosyl synthetase-associated domain, N-terminal domain of ribose phosphate pyrophosphokinase [Interproscan]. (ntu.edu.sg)
  • tRNA synthetases class I (R), DALR anticodon binding domain, Arginyl tRNA synthetase N terminal domain [Interproscan]. (ntu.edu.sg)
  • ALA synthetase activity is also closely associated with cytochrome P-450 activity. (medscape.com)
  • Ramaswamy, N.K. and Nair, P.M. δ-Aminolevulinic acid synthetase from cold-stored potatoes. (enzyme-database.org)
  • Scholnick, P.L., Hammaker, L.E. and Marver, H.S. Soluble δ-aminolevulinic acid synthetase of rat liver. (enzyme-database.org)
  • 2. Expression of peptide transporter 1 has a positive correlation in protoporphyrin IX accumulation induced by 5-aminolevulinic acid with photodynamic detection of non-small cell lung cancer and metastatic brain tumor specimens originating from non-small cell lung cancer. (nih.gov)
  • 3. Improvement of the efficacy of 5-aminolevulinic acid-mediated photodynamic treatment in human oral squamous cell carcinoma HSC-4. (nih.gov)
  • 11. Expression levels of PEPT1 and ABCG2 play key roles in 5-aminolevulinic acid (ALA)-induced tumor-specific protoporphyrin IX (PpIX) accumulation in bladder cancer. (nih.gov)
  • 14. Effect of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) on heme oxygenase-1, biliverdin IXalpha reductase and delta-aminolevulinic acid synthetase 1 in rats with wild-type or variant AH receptor. (nih.gov)
  • LEVULAN® KERASTICK® (aminolevulinic acid HCl) for Topical Solution, 20%, contains the hydrochloride salt of aminolevulinic acid (ALA), an endogenous 5-carbon aminoketone. (nih.gov)
  • An enzyme of the transferase class that catalyzes condensation of the succinyl group from succinyl coenzyme A with glycine to form delta-aminolevulinate. (nih.gov)
  • The synthesis of ALA is normally tightly controlled by feedback inhibition of the enzyme, ALA synthetase, presumably by intracellular heme levels. (nih.gov)
  • Topical fluorouracil (5-FU) cream and imiquimod cream are the usual first-line drug treatments. (msdmanuals.com)
  • The most common chemotherapeutic agent used in superficial basal cell carcinoma is topical 5-fluorouracil. (medscape.com)
  • 5-Fluorouracil topical 5% cream or solution is used topically for the management of superficial BCC. (medscape.com)
  • Methyl aminolevulinate cream is a porphyrin precursor used in combination with narrow-band, red-light illumination for nonhyperkeratotic, nonpigmented actinic keratoses. (medscape.com)