An enzyme that catalyzes the conversion of L-aspartate 4-semialdehyde, orthophosphate, and NADP+ to yield L-4-aspartyl phosphate and NADPH. EC 1.2.1.11.
An enzyme that catalyzes the formation of beta-aspartyl phosphate from aspartic acid and ATP. Threonine serves as an allosteric regulator of this enzyme to control the biosynthetic pathway from aspartic acid to threonine. EC 2.7.2.4.
An enzyme that catalyzes the reduction of aspartic beta-semialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. EC 1.1.1.3.
An enzyme that plays a role in the GLUTAMATE and butanoate metabolism pathways by catalyzing the oxidation of succinate semialdehyde to SUCCINATE using NAD+ as a coenzyme. Deficiency of this enzyme, causes 4-hydroxybutyricaciduria, a rare inborn error in the metabolism of the neurotransmitter 4-aminobutyric acid (GABA).
An enzyme that plays a role in the VALINE; LEUCINE; and ISOLEUCINE catabolic pathways by catalyzing the oxidation of 2-methyl-3-oxopropanate to propanoyl-CoA using NAD+ as a coenzyme. Methylmalonate semialdehyde dehydrogenase deficiency is characterized by elevated BETA-ALANINE and 3-hydropropionic acid.
Oxidoreductases that are specific for ALDEHYDES.
Brain disorders resulting from inborn metabolic errors, primarily from enzymatic defects which lead to substrate accumulation, product reduction, or increase in toxic metabolites through alternate pathways. The majority of these conditions are familial, however spontaneous mutation may also occur in utero.
An enzyme that converts brain gamma-aminobutyric acid (GAMMA-AMINOBUTYRIC ACID) into succinate semialdehyde, which can be converted to succinic acid and enter the citric acid cycle. It also acts on beta-alanine. EC 2.6.1.19.
An NAD+ dependent enzyme that catalyzes the oxidation of 2-aminomuconate 6-semialdehyde to 2-aminomuconate.
The sodium salt of 4-hydroxybutyric acid. It is used for both induction and maintenance of ANESTHESIA.
Disorders affecting amino acid metabolism. The majority of these disorders are inherited and present in the neonatal period with metabolic disturbances (e.g., ACIDOSIS) and neurologic manifestations. They are present at birth, although they may not become symptomatic until later in life.
An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70.
Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC 2.6.1.1.
Salts and esters of hydroxybutyric acid.
An NADP+ dependent enzyme that catalyzes the oxidation of L-glutamate 5-semialdehyde to L-glutamyl 5-phosphate. It plays a role in the urea cycle and metabolism of amino groups.
Derivatives of SUCCINIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,4-carboxy terminated aliphatic structure.
Derivatives of adipic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,6-carboxy terminated aliphatic structure.
A gram-positive organism found in the upper respiratory tract, inflammatory exudates, and various body fluids of normal and/or diseased humans and, rarely, domestic animals.
A genus of gram-positive, coccoid bacteria whose organisms occur in pairs or chains. No endospores are produced. Many species exist as commensals or parasites on man or animals with some being highly pathogenic. A few species are saprophytes and occur in the natural environment.
An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The degree of 3-dimensional shape similarity between proteins. It can be an indication of distant AMINO ACID SEQUENCE HOMOLOGY and used for rational DRUG DESIGN.
Macromolecular molds for the synthesis of complementary macromolecules, as in DNA REPLICATION; GENETIC TRANSCRIPTION of DNA to RNA, and GENETIC TRANSLATION of RNA into POLYPEPTIDES.
The process of pictorial communication, between human and computers, in which the computer input and output have the form of charts, drawings, or other appropriate pictorial representation.
The portion of an interactive computer program that issues messages to and receives commands from a user.
A large collection of DNA fragments cloned (CLONING, MOLECULAR) from a given organism, tissue, organ, or cell type. It may contain complete genomic sequences (GENOMIC LIBRARY) or complementary DNA sequences, the latter being formed from messenger RNA and lacking intron sequences.
Strains of Neisseria meningitidis found mostly in Africa.
A shiny gray element with atomic symbol As, atomic number 33, and atomic weight 75. It occurs throughout the universe, mostly in the form of metallic arsenides. Most forms are toxic. According to the Fourth Annual Report on Carcinogens (NTP 85-002, 1985), arsenic and certain arsenic compounds have been listed as known carcinogens. (From Merck Index, 11th ed)
Enzymes that catalyze the joining of glutamine-derived ammonia and another molecule. The linkage is in the form of a carbon-nitrogen bond. EC 6.3.5.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A plant genus of the family ROSACEAE known for the edible fruit.
Organic compounds containing a carbonyl group in the form -CHO.
A plant genus in the family ROSACEAE and order Rosales. This should not be confused with the genus RHODIOLA which is sometimes called roseroot.
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
A metalloflavoprotein enzyme involved the metabolism of VITAMIN A, this enzyme catalyzes the oxidation of RETINAL to RETINOIC ACID, using both NAD+ and FAD coenzymes. It also acts on both the 11-trans- and 13-cis-forms of RETINAL.
A species of bacteria that causes ANTHRAX in humans and animals.
The outermost layer of a cell in most PLANTS; BACTERIA; FUNGI; and ALGAE. The cell wall is usually a rigid structure that lies external to the CELL MEMBRANE, and provides a protective barrier against physical or chemical agents.
An acute infection caused by the spore-forming bacteria BACILLUS ANTHRACIS. It commonly affects hoofed animals such as sheep and goats. Infection in humans often involves the skin (cutaneous anthrax), the lungs (inhalation anthrax), or the gastrointestinal tract. Anthrax is not contagious and can be treated with antibiotics.
Heat and stain resistant, metabolically inactive bodies formed within the vegetative cells of bacteria of the genera Bacillus and Clostridium.
A methylpentose whose L- isomer is found naturally in many plant glycosides and some gram-negative bacterial lipopolysaccharides.
Phosphate esters of THYMIDINE in N-glycosidic linkage with ribose or deoxyribose, as occurs in nucleic acids. (From Dorland, 28th ed, p1154)

An integrated study of threonine-pathway enzyme kinetics in Escherichia coli. (1/46)

We have determined the kinetic parameters of the individual steps of the threonine pathway from aspartate in Escherichia coli under a single set of experimental conditions chosen to be physiologically relevant. Our aim was to summarize the kinetic behaviour of each enzyme in a single tractable equation that takes into account the effect of the products as competitive inhibitors of the substrates in the forward reaction and also, when appropriate (e.g. near-equilibrium reactions), as substrates of the reverse reactions. Co-operative feedback inhibition by threonine and lysine was also included as necessary. We derived the simplest rate equations that describe the salient features of the enzymes in the physiological range of metabolite concentrations in order to incorporate them ultimately into a complete model of the threonine pathway, able to predict quantitatively the behaviour of the pathway under natural or engineered conditions.  (+info)

Threonine synthesis from aspartate in Escherichia coli cell-free extracts: pathway dynamics. (2/46)

We have developed an experimental model of the whole threonine pathway that allows us to study the production of threonine from aspartate under different conditions. The model consisted of a desalted crude extract of Escherichia coli to which we added the substrates and necessary cofactors of the pathway: aspartate, ATP and NADPH. In this experimental model we measured not only the production of threonine, but also the time dependence of all the intermediate metabolites and of the initial substrates, aspartate, ATP and NADPH. A stoichiometric conversion of precursors into threonine was observed. We have derived conditions in which a quasi steady state can be transiently observed and used to simulate physiological conditions of functioning of the pathway in the cell. The dependence of threonine synthesis and of the aspartate and NADPH consumption on the initial aspartate and threonine concentrations exhibits greater sensitivity to the aspartate concentration than to the threonine concentration in these non-steady-state conditions. A response to threonine is only observed in a narrow concentration range from 0.23 to 2 mM.  (+info)

Control of the threonine-synthesis pathway in Escherichia coli: a theoretical and experimental approach. (3/46)

A computer simulation of the threonine-synthesis pathway in Escherichia coli Tir-8 has been developed based on our previous measurements of the kinetics of the pathway enzymes under near-physiological conditions. The model successfully simulates the main features of the time courses of threonine synthesis previously observed in a cell-free extract without alteration of the experimentally determined parameters, although improved quantitative fits can be obtained with small parameter adjustments. At the concentrations of enzymes, precursors and products present in cells, the model predicts a threonine-synthesis flux close to that required to support cell growth. Furthermore, the first two enzymes operate close to equilibrium, providing an example of a near-equilibrium feedback-inhibited enzyme. The predicted flux control coefficients of the pathway enzymes under physiological conditions show that the control of flux is shared between the first three enzymes: aspartate kinase, aspartate semialdehyde dehydrogenase and homoserine dehydrogenase, with no single activity dominating the control. The response of the model to the external metabolites shows that the sharing of control between the three enzymes holds across a wide range of conditions, but that the pathway flux is sensitive to the aspartate concentration. When the model was embedded in a larger model to simulate the variable demands for threonine at different growth rates, it showed the accumulation of free threonine that is typical of the Tir-8 strain at low growth rates. At low growth rates, the control of threonine flux remains largely with the pathway enzymes. As an example of the predictive power of the model, we studied the consequences of over-expressing different enzymes in the pathway.  (+info)

Structure of the ask-asd operon and formation of aspartokinase subunits in the cephamycin producer 'Amycolatopsis lactamdurans'. (4/46)

The first two genes of the lysine pathway are closely linked forming a transcriptional operon in the cephamycin producer 'Amycolatopsis lactamdurans'. The asd gene, encoding the enzyme aspartic semialdehyde dehydrogenase, has been cloned by complementation of Escherichia coli asd mutants. It encodes a protein of 355 aa with a deduced M(r) of 37109. The ask gene encoding the aspartokinase (Ask) is located upstream of the asd gene as shown by determination of Ask activity conferred to E. coli transformants. asd and ask are separated by 2 nt and are transcribed in a bicistronic 2.6 kb mRNA. As occurs in corynebacteria, the presence of a ribosome-binding site within the ask sequence suggests that this ORF encodes two overlapping proteins, Askalpha of 421 aa and M(r) 44108, and Askbeta of 172 aa and M(r) 18145. The formation of both subunits of Ask from a single gene (ask) was confirmed by using antibodies against the C-terminal end of Ask which is identical in both subunits. Ask activity of 'A. lactamdurans' is regulated by the concerted action of lysine plus threonine and this inhibition is abolished in E. coli transformants containing Ser(301) to Tyr, or Gly(345) to Asp mutations of the 'A. lactamdurans' ask gene.  (+info)

A structural basis for the mechanism of aspartate-beta-semialdehyde dehydrogenase from Vibrio cholerae. (5/46)

L-Aspartate-beta-semialdehyde dehydrogenase (ASADH) catalyzes the reductive dephosphorylation of beta-aspartyl phosphate to L-aspartate-beta-semialdehyde in the aspartate biosynthetic pathway of plants and micro-organisms. The aspartate pathway produces fully one-quarter of the naturally occurring amino acids, but is not found in humans or other eukaryotic organisms, making ASADH an attractive target for the development of new antibacterial, fungicidal, or herbicidal compounds. We have determined the structure of ASADH from Vibrio cholerae in two states; the apoenzyme and a complex with NADP, and a covalently bound active site inhibitor, S-methyl-L-cysteine sulfoxide. Upon binding the inhibitor undergoes an enzyme-catalyzed reductive demethylation leading to a covalently bound cysteine that is observed in the complex structure. The enzyme is a functional homodimer, with extensive intersubunit contacts and a symmetrical 4-amino acid bridge linking the active site residues in adjacent subunits that could serve as a communication channel. The active site is essentially preformed, with minimal differences in active site conformation in the apoenzyme relative to the ternary inhibitor complex. The conformational changes that do occur result primarily from NADP binding, and are localized to the repositioning of two surface loops located on the rim at opposite sides of the NADP cleft.  (+info)

Cloning of dapD, aroD and asd of Leptospira interrogans serovar icterohaemorrhagiae, and nucleotide sequence of the asd gene. (6/46)

Metabolites such as diaminopimelate and some aromatic derivatives, not synthesized in mammalian cells, are essential for growth of bacteria. As a first step towards the design of a new human live vaccine that uses attenuated strains of Leptospira interrogans, the asd, aroD and dapD genes, encoding aspartate beta-semialdehyde dehydrogenase, 3-dehydroquinase and tetrahydrodipicolinate N-succinyltransferase, respectively, were cloned by complementation of Escherichia coli mutants. The complete nucleotide sequence of the asd gene was determined and found to contain an open reading frame capable of encoding a protein of 349 amino acids with a calculated Mr of 38,007. Comparison of this deduced L. interrogans aspartate beta-semialdehyde dehydrogenase amino acid sequence with those of the same enzyme from Saccharomyces cerevisiae and Corynebacterium glutamicum revealed 46% and 36% identity, respectively. By contrast, the identity between the L. interrogans enzyme and the Streptococcus mutans or E. coli enzymes was less than 31%. Highly conserved sequences within aspartate semialdehyde dehydrogenase from the five organisms were observed at the amino and carboxyl termini, and around the cysteine of the active site.  (+info)

Mechanism of action of an antifungal antibiotic, RI-331, (S) 2-amino-4-oxo-5-hydroxypentanoic acid; kinetics of inactivation of homoserine dehydrogenase from Saccharomyces cerevisiae. (7/46)

An antifungal antibiotic (S) 2-amino-4-oxo-5-hydroxypentanoic acid, inhibited the biosynthesis of the aspartate family of amino acids (methionine, isoleucine and threonine) followed by the inhibition of protein biosynthesis in Saccharomyces cerevisiae. This inhibition was effected by impeding the biosynthesis of their common intermediate precursor, homoserine. The inhibition of biosynthesis of homoserine by the antibiotic was attributable to inactivation of homoserine dehydrogenase [EC 1.1.1.3], which is involved in the conversion of aspartate semialdehyde to homoserine in the metabolic pathway leading to threonine, methionine and isoleucine. Since such enzymic activity is not present in animal cells, the selective antifungal activity of the antibiotic is thus explained.  (+info)

Capture of an intermediate in the catalytic cycle of L-aspartate-beta-semialdehyde dehydrogenase. (8/46)

The structural analysis of an enzymatic reaction intermediate affords a unique opportunity to study a catalytic mechanism in extraordinary detail. Here we present the structure of a tetrahedral intermediate in the catalytic cycle of aspartate-beta-semialdehyde dehydrogenase (ASADH) from Haemophilus influenzae at 2.0-A resolution. ASADH is not found in humans, yet its catalytic activity is required for the biosynthesis of essential amino acids in plants and microorganisms. Diaminopimelic acid, also formed by this enzymatic pathway, is an integral component of bacterial cell walls, thus making ASADH an attractive target for the development of new antibiotics. This enzyme is able to capture the substrates aspartate-beta-semialdehyde and phosphate as an active complex that does not complete the catalytic cycle in the absence of NADP. A distinctive binding pocket in which the hemithioacetal oxygen of the bound substrate is stabilized by interaction with a backbone amide group dictates the R stereochemistry of the tetrahedral intermediate. This pocket, reminiscent of the oxyanion hole found in serine proteases, is completed through hydrogen bonding to the bound phosphate substrate.  (+info)

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Protein target information for Chain A, Aspartate beta-semialdehyde dehydrogenase (Streptococcus pneumoniae). Find diseases associated with this biological target and compounds tested against it in bioassay experiments.
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Arsenic atom in PDB 1pqu: Crystal Structure Of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound With Nadp, S-Methyl Cysteine Sulfoxide and Cacodylate
SWISS-MODEL Template Library (SMTL) entry for 1t4b.1. 1.6 Angstrom structure of Esherichia coli aspartate-semialdehyde dehydrogenase.
The lysine, threonine, and methionine biosynthetic pathways share the three initial enzymatic steps, which are referred to as the Common Pathway (CP). In Escherichia coli three different aspartokinases (AKI, AKII, AKIII, the products of thrA, metL and lysC, respectively) can perform the first step of the CP. Moreover, two of them (AKI and AKII) are bifunctional, carrying also homoserine dehydrogenasic activity (hom product). The second step of the CP is catalyzed by a single aspartate semialdehyde dehydrogenase (ASDH, the product of asd). Thus, in the CP of E. coli while a single copy of ASDH performs the same reaction for three different metabolic routes, three different AKs perfom a unique step. Why and how such a situation did emerge and maintain? How is it correlated to the different regulatory mechanisms acting on these genes? The aim of this work was to trace the evolutionary pathway leading to the extant scenario in proteobacteria. The analysis of the structure, organization, phylogeny, and
Staphylococcus aureus; strain: Newman; locus tag: NWMN_1305 (NWMN_RS07350); symbol: asd; product: aspartate semialdehyde dehydrogenase
Acupuncture is the practice of placing very thin needles through the skin in specific locations of the body for the purpose of healing and relief of symptoms.
The antileukemic activity of l-asparaginase (ASNase), an important component of therapy for acute lymphoblastic leukemia, is thought to result from depletion of serum l-asparagine (Asn). In studies of the pharmacological effects of ASNase, investigators have reported prolonged reduction in the serum concentration of Asn after the administration of ASNase. Such measurements may not be valid because ASNase present in the blood sample may hydrolyze Asn before its determination. We examined recovery of [U-14C]Asn from blood samples with and without various concentrations of added ASNase. In the presence of ≥0.01 IU/ml of ASNase, the amount of [U-14C]Asn recovered was ,15% of that without ASNase. Utilizing this assay, we studied the effect of 2 known inhibitors of ASNase in an attempt to improve Asn recovery. In the presence of aspartic β semialdehyde (ASA), or 5-diazo-4-oxo-l-norvaline (DONV), and up to 1.0 IU/ml ASNase, Asn levels remained at ,90% of control. ASA prevented the hydrolysis of ...
A novel N-acetyltranferase (NAT) with high specificity for L-dopa was partially purified and characterized during this study. Streptomyces akiyoshiensis NAT was isolated from liquid cultures and the cell free extract was ...
Lysine biosynthesis is one of the unique metabolic capabilities of cyst forming Coccidia such as Toxoplasma gondii and Neospora caninum. Toxoplasma and Neospora genome analysis shows that they have the unique metabolic capability to synthesise lysine, an essential amino acid in humans. This capability is absent in other Apicomplexa. It has been suggested that Toxoplasma can convert aspartate into lysine via diaminopimelate pathway [1]. This pathway takes place via four different routes in different organisms (KEGG Lysine biosynthesis pathway). Of these, three variants belong to different groups of prokaryotes and the plant variant of the pathway was identified recently in Arabidopsis thaliana [2]. The first four enzymes (aspartate kinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase) and the last enzyme (diaminopimelate decarboxylase) is the same in all variants of the pathway and these five enzymes are present in T. gondii and N. caninum ...
Small differences in as many as a thousand genes contribute to risk for autism, according to a study led by Mount Sinai researchers and the Autism Sequencing Consortium (ASC), and published today in the journal Nature.. The new study examined data on several types of rare, genetic differences in more than 14,000 DNA samples from parents, affected children, and unrelated individuals - by far the largest number to date - to dramatically expand the list of genes identified with autism spectrum disorder (ASD).. Most of the genes that contribute to autism remain unknown, but the current study increases the number of definitive autism genes almost fourfold to 33, compared to the 9 genes most closely tied to risk in recent years by similar studies in several labs. It also identified more than 70 additional, likely ASD genes. Each of these genes is mutated in more than 5 percent of individuals with autism, signifying a large, relative contribution to risk for a complex genetic disease.. By casting a ...
Curtiss, R. III, Jagusztyn-Krynicka, E.K., Hansen, J.B., Smorawinska, M., Abiko, Y., and Cardineau, G.A. 1982. Expression of Streptococcus mutans plasmid and chromosomal gene in Escherichia coli K-12. In: Microbial. Drug resistance, S. Mitsuhashi (ed.), Japan Scientific Societies Press, Tokyo and University Park press, Baltimore, Vol. 3, pp. 15-27.. Murchison, H.H., Barrett, J.F., Cardineau, G.A., and Curtiss III, R. 1986. Transformation of Streptococcus mutans with chromosomal and shuttle plasmid (pYA629) DNAs. Infection and Immunity 54: 273-282.. Cardineau, G.A. and Curtiss III, R. 1987. Nucleotide sequence of the asd gene of Streptococcus mutans: identification of the promoter region and evidence for attenuator like sequences preceding the structural gene. J. Biol. Chem.262: 3344-3353.. Adang, M.J., Brody, M., Cardineau, G.A., Eagan, N., Roush, R.T., Shewmaker, C.K., Jones, A., Oakes, J.V., and McBride, K.E. 1993. The construction and expression of a Bacillus thuringiensis cryIIIA gene in ...
The aspartate biosynthetic pathway, essential in plants and in most bacteria and fungi, can produce the amino acids threonine, lysine, methionine, and isoleucine. The first commitment step of this pathway is catalyzed by aspartokinase (AK). The archeal thermophilic Methanococcus jannaschii has only a single, monofunctional form of AK. X-ray crystallographic studies indicate that mjAK is a tetramer in the crystalline state, which coincides with the oligomeric structure in solution. The substrate L-aspartate binds to this recombinant enzyme in two different orientations, providing the first structural evidence supporting the relaxed regiospecificity previously observed with several alternative substrates of E. coli AK.5 Binding of the nucleotide substrate triggers significant domain movements that result in a more compact quaternary structure. The allosteric inhibitor, L-threonine, cooperatively binds to two sites in each monomer of this dimer of dimers, one site in the regulatory domain interface ...
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K00928 lysC; aspartate kinase [EC:2.7.2.4] K00928 lysC; aspartate kinase [EC:2.7.2.4] K00928 lysC; aspartate kinase [EC:2.7.2.4] K12524 thrA; bifunctional aspartokinase / homoserine dehydrogenase 1 [EC:2.7.2.4 1.1.1.3] K12525 metL; bifunctional aspartokinase / homoserine dehydrogenase 2 [EC:2.7.2.4 1.1.1.3 ...
Residues 1 to 131 (E-value = 9.7e-37) place NG1997 in the Semialdhyde_dh family which is described as Semialdehyde dehydrogenase, NAD binding domain (PF01118 ...
6-Phosphogluconate dehydrogenase is a potential target for new drugs against African trypanosomiasis. Phosphorylated aldonic acids are strong inhibitors of 6-phosphogluconate dehydrogenase, and 4-phospho-d-erythronate (4PE) and 4-phospho-d-erythronohydroxamate are two of the strongest inhibitors of the Trypanosoma brucei enzyme. Binding of the substrate 6-phospho-d-gluconate (6PG), the inhibitors 5-phospho-d-ribonate (5PR) and 4PE, and the coenzymes NADP, NADPH and NADP analogue 3-amino-pyridine adenine dinucleotide phosphate to 6-phospho-d-gluconate dehydrogenase from T. brucei was studied using isothermal titration calorimetry. Binding of the substrate (K(d) = 5 microm) and its analogues (K(d) =1.3 microm and K(d) = 2.8 microm for 5PR and 4PE, respectively) is entropy driven, whereas binding of the coenzymes is enthalpy driven. Oxidized coenzyme and its analogue, but not reduced coenzyme, display a half-site reactivity in the ternary complex with the substrate or inhibitors. Binding of 6PG and ...
Background The identification of genetic target genes is a key step for rational engineering of production strains towards bio-based chemicals, fuels or therapeutics. This is often a difficult task,...
SWISS-MODEL Template Library (SMTL) entry for 3hij.1. Crystal structure of dihydrodipicolinate synthase from Bacillus anthracis in complex with its substrate, pyruvate
Glutamate-5-semialdehyde is a non-proteinogenic amino acid involved in the biosynthesis of proline and arginine (via ornithine), as well as in the biosynthesis of antibiotics, such as carbapenems. It is synthesized by the reduction of glutamyl-5-phosphate by glutamate-5-semialdehyde dehydrogenase. Glutamate-1-semialdehyde Baich A (1971). The biosynthesis of proline in Escherichia coli: phosphate-dependent glutamate -semialdehyde dehydrogenase (NADP), the second enzyme in the pathway. Biochim. Biophys. Acta. 244 (1): 129-34. doi:10.1016/0304-4165(71)90129-2. PMID 4399189 ...
Complete information for LYZ gene (Protein Coding), Lysozyme, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
2 For my friends. Aware of how they worry about me and of how terrible I am when it comes to staying in touch, I want them to know that I still feel them lifting me up ...
Eternal Pump is the peak in performance pump formulas available in the market today.It increases nitric oxide levels as weil as, muscular volume and muscular hydration. It improves nutrient uptake, oxygenation of the muscles ad durability of the pump. It stimulates the developement and recoveryof tissues in addition to improving blood circulationthis is the ultimate formula for all who seek an Eternal Pump
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Clinical trial for Obesity | Polycystic Ovary Syndrome , DAPA EQW DAPA/MET ER and PHEN/TPM ER in Obese Women With PolycysticOvary Syndrome (PCOS)
Introduction: Aspartokinase (A1, A2, A3) Homoserine dehydrogenase (B1, B2) Threonine dehydratase (C1, C2) Allosteric regulation of selective isozymes some unregulated Sequential feedback inhibition Same product inhibits its biosynthetic path at multiple sites Inhibits first enzyme in pathway
Peptidoglycan Pimelic acid Aspartate-semialdehyde dehydrogenase, an enzyme involved in DAP synthesis Brooks, George H.; Geo F. ...
... aspartokinase β-aspartate semialdehyde dehydrogenase homoserine dehydrogenase homoserine kinase threonine synthase. Threonine ... Threonine is synthesized from aspartate in bacteria such as E. coli. It is encoded by all the codons starting AC (ACU, ACC, ACA ... In humans the gene for threonine dehydrogenase is an inactive pseudogene, so threonine is converted to α-ketobutyrate. The ... In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. ...
Aspartate-β-semialdehyde dehydrogenase (asd) gene deletion mutants are auxotrophic for diaminopimelate (DAP) in rich media and ...
Finally, although the asd gene encodes an enzyme, aspartate-semialdehyde dehydrogenase, that participates in the synthesis of ...
... may refer to: Allosteric Database, ASD (database), a protein database Asd RNA motif Aspartate-semialdehyde dehydrogenase ...
Aspartokinase Aspartate-semialdehyde dehydrogenase Homoserine dehydrogenase Homoserine O-transsuccinylase Cystathionine-γ- ... The intermediate aspartate-semialdehyde is the branching point with the lysine biosynthetic pathway, where it is instead ... 7) The enzyme α-ketoacid dehydrogenase converts α-ketobutyrate to propionyl-CoA, which is metabolized to succinyl-CoA in a ... First, aspartic acid is converted via β-aspartyl-semialdehyde into homoserine by two reduction steps of the terminal carboxyl ...
The major ionotropic glutamine receptors include the N-methyl-D-aspartate (NMDA) and alpha-amino-3-hydroxy-5-methylisoxazole-4- ... Succinic semialdehyde dehydrogenase deficiency (SSADHD), also known as 4-hydroxybutyric aciduria or gamma-hydroxybutyric ... Finally, succinic semialdehyde dehydrogenase levels can be measured in cultured leukocytes of the patient. This occurs due to ... Succinic semialdehyde dehydrogenase deficiency. From Wikipedia, the free encyclopedia. (Redirected from Gamma-hydroxybutyric ...
The major ionotropic glutamine receptors include the N-methyl-D-aspartate (NMDA) and alpha-amino-3-hydroxy-5-methylisoxazole-4- ... Finally, succinic semialdehyde dehydrogenase levels can be measured in cultured leukocytes of the patient. This occurs due to ... Succinic semialdehyde dehydrogenase deficiency (SSADHD), also known as 4-hydroxybutyric aciduria or gamma-hydroxybutyric ... Pearl, P. L.; Novotny, E. J.; Acosta, M. T.; Jakobs, C.; Gibson, K. M. (2003). "Succinic semialdehyde dehydrogenase deficiency ...
... catalyzes the reaction of aspartate-semialdehyde (ASA) to homoserine. The overall reaction reduces the ... Homoserine dehydrogenase catalyses the third step in the aspartate pathway; the NAD(P)-dependent reduction of aspartate beta- ... At night, aspartate is converted to asparagine for storage. Additionally, the aspartate kinase-homoserine dehydrogenase gene is ... Homoserine dehydrogenase and aspartate kinase are both subject to significant regulation (refer to figure 3). HSD is inhibited ...
Relevant enzymes include aspartokinase, aspartate-semialdehyde dehydrogenase, homoserine dehydrogenase, homoserine O- ... β-aspartate semialdehyde dehydrogenase, homoserine dehydrogenase, homoserine kinase, threonine synthase. The biosynthesis of ... The initial two stages of the DAP pathway are catalyzed by aspartokinase and aspartate semialdehyde dehydrogenase. These ... Aspartate kinase becomes downregulated by the presence of threonine or lysine. Lysine is synthesized from aspartate via the ...
Other names in common use include aspartate semialdehyde dehydrogenase, aspartic semialdehyde dehydrogenase, L-aspartate-beta- ... and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. It also ... "Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino ... Aspartate-semialdehyde dehydrogenase may be cis-regulated by an Asd RNA motif found in the 5' UTR of some Asd genes. This ...
L-Aspartate-4-semialdehyde is synthesized by the enzyme aspartate semialdehyde dehydrogenase, which catalyzes the following ... L-Aspartic-4-semialdehyde (also L-Aspartate-4-semialdehyde) is an α-amino acid derivative of aspartate. It is an important ... This reaction, which turns L-aspartate-4-semialdehyde into homoserine is shown below: L-Aspartate-4-semialdehyde + NAD(P)H + H+ ... L-aspartate-4-semialdehyde + NADP+ + phosphate Once L-aspartate-4-semialdehyde is synthesized, the molecule can then progress ...
This enzyme participates in 4 metabolic pathways: inositol metabolism, alanine and aspartate metabolism, beta-alanine ... In enzymology, a malonate-semialdehyde dehydrogenase (acetylating) (EC 1.2.1.18) is an enzyme that catalyzes the chemical ... Jakoby WB (1963). "Aldehyde dehydrogenase". In Boyer PD, Lardy H, Myrback K (eds.). The Enzymes. 7 (2nd ed.). New York: ... V. Direct conversion of malonic semialdehyde to acetyl-coenzyme A". The Journal of Biological Chemistry. 235: 589-94. PMID ...
Aspartate carbamoyltransferase. *Aspartate-semialdehyde dehydrogenase. *Asprosin. *Ataxin 7. *ATCase/OTCase family. *Atg1 ...
Aspartate semialdehyde dehydrogenase catalyzes the NADPH-dependent reduction of aspartyl phosphate to yield aspartate ... "Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino ... Aspartate-semialdehyde dehydrogenase catalyzes the reduction reaction by dephosphorylation of aspartyl-β-phosphate to yield ... aspartate-β-semialdehyde. Dihydrodipicolinate synthase catalyzes the condensation reaction of aspartate-β-semialdehyde with ...
... aminomuconate-semialdehyde dehydrogenase MeSH D08.811.682.657.163.374 - aspartate-semialdehyde dehydrogenase MeSH D08.811. ... succinate-semialdehyde dehydrogenase MeSH D08.811.682.657.163.875 - succinate-semialdehyde dehydrogenase (NAD(P)+) MeSH D08.811 ... l-aminoadipate-semialdehyde dehydrogenase MeSH D08.811.682.657.163.812 - malonate-semialdehyde dehydrogenase (acetylating) MeSH ... betaine-aldehyde dehydrogenase MeSH D08.811.682.657.163.562 - glutamate-5-semialdehyde dehydrogenase MeSH D08.811.682.657. ...
L-aspartate 4-semialdehyde + putrescine + NADPH + H+ The reaction takes place in the opposite direction. Nakao H, Shinoda S, ... Carboxynorspermidine synthase (EC 1.5.1.43, carboxynorspermidine dehydrogenase, carboxyspermidine dehydrogenase, CASDH, CANSDH ... L-aspartate 4-semialdehyde + propane-1,3-diamine + NADPH + H+ (2) carboxyspermidine + H2O + NADP+ ⇌ {\displaystyle \ ...
The production of dihydropicolinate from aspartate-semialdehyde controls flux into the lysine/diaminopimelic acid pathway. ... In the third variant, found in some Gram-positive bacteria, a dehydrogenase converts tetrahydropicolinate directly to meso-DAP ... Viola RE (2001). "The central enzymes of the aspartate family of amino acid biosynthesis". Acc. Chem. Res. 34 (5): 339-49. doi: ... The lysine/diaminopimelic acid branch of the aspartate pathway produces the essential amino acid lysine via the intermediate ...
... catalysed condensation reaction between the aspartate derived, L-aspartate semialdehyde, and pyruvate to form (4S)-4-hydroxy-2, ... AAS dehydrogenase (AASD) (E.C 1.2.1.31) then further dehydrates the molecule into AAA. Subsequently, PLP-AT catalyses the ... In fungi, AAA is reduced to α‑aminoadipate-semialdehyde via AAA reductase (E.C 1.2.1.95) in a unique process involving both ... The DAP pathway is regulated at multiple levels, including upstream at the enzymes involved in aspartate processing as well as ...
... acetaldehyde dehydrogenase (acetylating) EC 1.2.1.11: aspartate-semialdehyde dehydrogenase EC 1.2.1.12: glyceraldehyde-3- ... lysine 6-dehydrogenase EC 1.4.1.19: tryptophan dehydrogenase EC 1.4.1.20: phenylalanine dehydrogenase EC 1.4.1.21: aspartate ... glutarate-semialdehyde dehydrogenase EC 1.2.1.21: glycolaldehyde dehydrogenase EC 1.2.1.22: lactaldehyde dehydrogenase EC 1.2. ... succinate-semialdehyde dehydrogenase (acylating) EC 1.2.1.77: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+) EC 1.2. ...
Finally, succinic semialdehyde is oxidized by succinic semialdehyde dehydrogenase (SSADH) to form succinate, re-entering the ... Under pathological and physiological conditions, the malate-aspartate shuttle or the purine nucleotide shuttle can increase ... Loss-of-function mutations in the genes encoding succinate dehydrogenase, frequently found in hereditary paraganglioma and ... King, A.; Selak, M. A.; Gottlieb, E. (2006-01-01). "Succinate dehydrogenase and fumarate hydratase: linking mitochondrial ...
... the semialdehyde produced by GABA-T will be oxidized to succinic acid by succinate-semialdehyde dehydrogenase, resulting in ... This enzyme participates in 5 metabolic pathways: alanine and aspartate metabolism, glutamate metabolism, beta-alanine ... This produces succinate semialdehyde and L-glutamate. In plants, pyruvate and glyoxylate can be used in the place of 2- ... The two products are succinate semialdehyde and L-glutamate. This enzyme belongs to the family of transferases, specifically ...
This motif was identified clustering genes of tartrate dehydrogenase, succinate semialdehyde dehydrogenase, 3- ... Aspartate amino transferase and LysR/unknown transcriptional regulator) with partial synteny to the first group. A very ... hydroxyisobutyrate dehydrogenase and hydroxypyruvate isomerase in S. meliloti, and several Rhizobiums and it is marked in the ...
Succinic semialdehyde dehydrogenase deficiency is a disease that causes GHB to accumulate in the blood. GHB is used for medical ... Sircar R, Basak A (December 2004). "Adolescent gamma-hydroxybutyric acid exposure decreases cortical N-methyl-D-aspartate ... Succinic Semialdehyde Dehydrogenase Deficiency. Retrieved 6 March 2010. Andriamampandry C, Taleb O, Viry S, Muller C, Humbert ... People with the disorder known as succinic semialdehyde dehydrogenase deficiency, also known as γ-hydroxybutyric aciduria, have ...
Aspartate → β-aspartate-semialdehyde → Homoserine + lysine Aspartic Acid -OOC-CH2- Oxaloacetate → Aspartic Acid ( ... 3-phosphoglycerate → 3-phosphohydroxypyruvate (3-phosphoglycerate dehydrogenase) → 3-phosphoserine (aminotransferase) → Serine ... Aspartate → β-aspartate-semialdehyde → Homoserine → Threonine Cysteine HS-CH2- Serine → Cystathionine → α-ketobutyrate → ... Glutamate → Glutamate-5-semialdehyde (γ-glutamyl kinase) → Arginine Histidine§. NH-CH=N-CH=C-CH2- Glucose → Glucose-6-phosphate ...
synthese van glutamaat-5-semialdehyde glutamate-5-semialdehyde dehydrogenase Ja 1.2.1.47 4-trimethylammoniobutyraldehyde ... glutamate dehydrogenase NAD(P)+ Ja 1.4.1.21 aspartate dehydrogenase Ja 1.4.3.1 D-aspartate oxidase Ja ... oxoglutarate dehydrogenase (succinyl-transferring) Ja 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl- ... L-iditol 2-dehydrogenase Ja 1.1.1.15 D-iditol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. D-sorbose + NADH + H+ D-iditol 2- ...
2cg5: STRUCTURE OF AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE IN COMPLEX WITH CYTOSOLIC ACYL ... Aspartate carbamoyltransferase. *Dihydroorotase. *Cholesterol side-chain cleavage enzyme. *Cytochrome b6f complex. *Electron ... "The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chem Biol Interact. 178 (1-3): 94- ...
... succinate-semialdehyde dehydrogenase. In cancer, there are substantial metabolic derangements that occur to ensure the ... Of these amino acids, aspartate and glutamine are used, together with carbon and nitrogen atoms from other sources, to form the ... inhibits pyruvate dehydrogenase, isocitrate dehydrogenase, α-ketoglutarate dehydrogenase, and also citrate synthase. Acetyl-coA ... It activates pyruvate dehydrogenase phosphatase which in turn activates the pyruvate dehydrogenase complex. Calcium also ...
It is formed by the oxidation of succinate by the enzyme succinate dehydrogenase. Fumarate is then converted by the enzyme ... 2-Amino-3-carboxymuconic semialdehyde. *2-Aminomuconic semialdehyde. *2-Aminomuconic acid. *Glutaryl-CoA ... in eukaryotic organisms from succinate in complex 2 of the electron transport chain via the enzyme succinate dehydrogenase. It ...
3-hydroxyisobutyrate dehydrogenase. *Methylmalonate semialdehyde dehydrogenase. ISOLEUCINE→. *Branched-chain amino acid ... Aspartic acid (aspartate). *DIDS. *Direct blue 71. *Erythro-4-methyl-L-glutamic acid ...
Glyoxylate is then oxidized by hepatic lactate dehydrogenase to oxalate in an NAD+-dependent reaction.[26] ... 2-Amino-3-carboxymuconic semialdehyde. *2-Aminomuconic semialdehyde. *2-Aminomuconic acid. *Glutaryl-CoA ...
3-hydroxyisobutyrate dehydrogenase. *Methylmalonate semialdehyde dehydrogenase. ISOLEUCINE→. *Branched-chain amino acid ... Kynureninase belongs to the class V group of aspartate aminotransferase superfamily of structurally homologous pyridoxal 5'- ...
3-hydroxyisobutyrate dehydrogenase. *Methylmalonate semialdehyde dehydrogenase. ISOLEUCINE→. *Branched-chain amino acid ... glycine dehydrogenase (decarboxylating) or just glycine dehydrogenase. L-protein (GCSL or DLD) EC 1.8.1.4 known by many names, ... but most commonly dihydrolipoyl dehydrogenase H-protein (GCSH) is modified with lipoic acid and interacts with all other ...
Glutamate undergoes deamination, an oxidative reaction catalysed by glutamate dehydrogenase,[15] as follows: glutamate + H2O + ... Aspartate + α-ketoglutarate ⇌ oxaloacetate + glutamate. Both pyruvate and oxaloacetate are key components of cellular ... 2-Amino-3-carboxymuconic semialdehyde. *2-Aminomuconic semialdehyde. *2-Aminomuconic acid. *Glutaryl-CoA ... Grabowska, A.; Nowicki, M.; Kwinta, J. (2011). "Glutamate dehydrogenase of the germinating triticale seeds: Gene expression, ...
inborn errors of metabolism, such as Succinic semialdehyde dehydrogenase deficiency, porphyria and metachromatic leukodystrophy ... "Psychosis associated with anti-N-methyl-D-aspartate receptor antibodies". CNS Spectr. 13 (8): 699-703. ...
3-hydroxyisobutyrate dehydrogenase. *Methylmalonate semialdehyde dehydrogenase. ISOLEUCINE→. *Branched-chain amino acid ... Glutamate aspartate transporter. *Glycerol-3-phosphate dehydrogenase. *ATP synthase. *Carnitine palmitoyltransferase II ...
... succinate-semialdehyde dehydrogenase.[31] ... Of these amino acids, aspartate and glutamine are used, ... inhibits pyruvate dehydrogenase, isocitrate dehydrogenase, α-ketoglutarate dehydrogenase, and also citrate synthase. Acetyl-coA ... Calcium also activates isocitrate dehydrogenase and α-ketoglutarate dehydrogenase.[33] This increases the reaction rate of many ... NADH, a product of all dehydrogenases in the citric acid cycle with the exception of succinate dehydrogenase, ...
Finally, succinic semialdehyde is oxidized by succinic semialdehyde dehydrogenase (SSADH) to form succinate, re-entering the ... Under pathological and physiological conditions, the malate-aspartate shuttle or the purine nucleotide shuttle can increase ... Catalyzed by the enzyme succinate dehydrogenase (SDH), succinate is subsequently oxidized to fumarate:[22]:Section 17.1 ... See also: Tricarboxylic acid cycle and Succinate dehydrogenase. Succinate is a key intermediate in the tricarboxylic acid cycle ...
Succinic semialdehyde is then oxidized into succinic acid by succinic semialdehyde dehydrogenase and as such enters the citric ...
3-hydroxyisobutyrate dehydrogenase. *Methylmalonate semialdehyde dehydrogenase. ISOLEUCINE→. *Branched-chain amino acid ...
3-hydroxyisobutyrate dehydrogenase. *Methylmalonate semialdehyde dehydrogenase. ISOLEUCINE→. *Branched-chain amino acid ...
Other names in common use include aspartate semialdehyde dehydrogenase, aspartic semialdehyde dehydrogenase, L-aspartate-beta- ... and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. It also ... "Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino ... Aspartate-semialdehyde dehydrogenase may be cis-regulated by an Asd RNA motif found in the 5 UTR of some Asd genes. This ...
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH. UniProt ... Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4- ...
Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4- ... Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase ( ... Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase ( ... Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase ( ...
Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4- ... Aspartate-semialdehyde dehydrogenase (asd). *Bifunctional aspartokinase/homoserine dehydrogenase (thrA), Bifunctional ... Aspartate-semialdehyde dehydrogenase (asd). *Bifunctional aspartokinase/homoserine dehydrogenase (thrA), Bifunctional ... Aspartate-semialdehyde dehydrogenase (asd). *Dihydrodipicolinate synthase (dapA-1), 4-hydroxy-tetrahydrodipicolinate synthase ( ...
Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase from Streptococcus pneumoniae with cysteamine bound covalently ... Aspartate beta-semialdehyde dehydrogenase. A, B, C, D. 366. Streptococcus pneumoniae (strain ATCC BAA-255 / R6). Mutation(s): 0 ... Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase from Streptococcus pneumoniae with cysteamine bound covalently ... An early pathway enzyme, l-aspartate-β-semialdehyde dehydrogenase, produces a key intermediate at the first branch point of ...
Aspartate beta-semialdehyde dehydrogenase (Streptococcus pneumoniae). Find diseases associated with this biological target and ...
Recombinant Protein and Aspartate-semialdehyde dehydrogenase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and ... Aspartate-semialdehyde dehydrogenase 1. Aspartate-semialdehyde dehydrogenase 1 ELISA Kit. Aspartate-semialdehyde dehydrogenase ... Aspartate-semialdehyde dehydrogenase 2. Aspartate-semialdehyde dehydrogenase 2 ELISA Kit. Aspartate-semialdehyde dehydrogenase ... Aspartate-semialdehyde dehydrogenase. Aspartate-semialdehyde dehydrogenase ELISA Kit. Aspartate-semialdehyde dehydrogenase ...
Recombinant Protein and Aspartate-semialdehyde dehydrogenase leader peptide Antibody at MyBioSource. Custom ELISA Kit, ... Shop Aspartate-semialdehyde dehydrogenase leader peptide ELISA Kit, ... Aspartate-semialdehyde dehydrogenase leader peptide. Aspartate-semialdehyde dehydrogenase leader peptide ELISA Kit. Aspartate- ... semialdehyde dehydrogenase leader peptide Recombinant. Aspartate-semialdehyde dehydrogenase leader peptide Antibody. SMU_988.1 ...
... was identified as the aspartate semialdehyde dehydrogenase gene (asd), encoding a polypeptide of 346 amino acids. Subclones ... Sequence analysis and expression of the aspartokinase and aspartate semialdehyde dehydrogenase operon from rifamycin SV- ... Expression in Escherichia coli, purification and kinetic analysis of the aspartokinase and aspartate semialdehyde dehydrogenase ... Sequence analysis and expression of the aspartokinase and aspartate semialdehyde dehydrogenase operon from rifamycin SV- ...
Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase complex with NADP and 2-aminoterephthalate ... Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase complex with NADP and 2-aminoterephthalate. Coordinates. PDB ...
Complex Crystal structure of 4-nitro-2-phosphono-benzoic acid with sp-Aspartate-Semialdehyde Dehydrogenase and Nicotinamide- ... Complex Crystal structure of 4-nitro-2-phosphono-benzoic acid with sp-Aspartate-Semialdehyde Dehydrogenase and Nicotinamide- ... A cautionary tale of structure-guided inhibitor development against an essential enzyme in the aspartate-biosynthetic pathway. ...
Cinnamomum zeylanicum (Cinnamon) Derived Phytochemicals against Aspartate Semialdehyde Dehydrogenase of Aspergillus fumigatus ... Cinnamomum zeylanicum (Cinnamon) Derived Phytochemicals against Aspartate Semialdehyde Dehydrogenase of Aspergillus fumigatus ...
Crystal Structure Of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus Influenzae Bound With Nadp, S- ... Arsenic in the structure of Crystal Structure Of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase From Haemophilus ... binding sites of Arsenic atom in the structure of Crystal Structure Of the H277N Mutant of Aspartate Semialdehyde Dehydrogenase ...
Aspartokinase genes lysC alpha and lysC beta overlap and are adjacent to the aspartate beta-semialdehyde dehydrogenase gene asd ... Aspartokinase genes lysC alpha and lysC beta overlap and are adjacent to the aspartate beta-semialdehyde dehydrogenase gene asd ... "Aspartokinase genes lysC alpha and lysC beta overlap and are adjacent to the aspartate beta-semialdehyde dehydrogenase gene asd ... Aspartate-semialdehyde dehydrogenase (UNIPROT: P0C1D8). Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / ...
The structure of aspartate semialdehyde dehydrogenase (ASADH) from the fungal pathogen C. neoformans has been determined. The ... Cover illustration: Structure of a fungal form of aspartate semi-aldehyde de-hydrogenase from Cryptococcus neoformans (Dahal & ... Structure of a fungal form of aspartate semi-aldehyde de-hydrogenase from Cryptococcus neoformans. ...
Crystal structures of aspartate semialdehyde dehydrogenase from Mycobacterium tuberculosis in complex with glycerol and with ... PDB references: aspartate-semialdehyde dehydrogenase, complex with SMCS and sulfate, 3tz6; complex with glycerol and sulfate, ... Structures of ternary complexes of aspartate-semi-aldehyde de-hydrogenase (Rv3708c) from Mycobacterium tuberculosis H37Rv. ...
β-aspartate semialdehyde dehydrogenase. *homoserine dehydrogenase. *homoserine acyltransferase. *cystathionine-γ-synthase. * ... 7) α-ketoacid dehydrogenase converts α-ketobutyrate to propionyl-CoA, which is metabolized to succinyl-CoA in a three-step ... First, aspartic acid is converted via β-aspartyl-semialdehyde into homoserine, introducing the pair of contiguous methylene ...
α-aspartate semialdehyde dehydrogenase. *homoserine dehydrogenase. *homoserine kinase. *threonine synthase. Threonine ... In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. ...
1.2.1.10 acetaldehyde dehydrogenase (acetylating) 1.2.1.11 aspartate-semialdehyde dehydrogenase 1.2.1.12 glyceraldehyde-3- ... 1.2.1.3 aldehyde dehydrogenase (NAD+) 101298221 aldehyde dehydrogenase family 2 member B4 101311183 aldehyde dehydrogenase ... 101298824 aldehyde dehydrogenase family 7 member A1 K00128 ALDH; aldehyde dehydrogenase (NAD+) [EC:1.2.1.3] K00128 ALDH; ... 101311533 aldehyde dehydrogenase family 3 member H1-like 101313059 aldehyde dehydrogenase family 3 member H1-like 101310892 ...
Critical catalytic functional groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase. Blanco, J.; Moore, R.A.; ... L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+ ... soaking of crystals before harvest in 100 mM phosphate and 2 mM aspartate-beta-semialdehyde, crystallization of mutant H277N in ... soaking of crystals before harvest in 100 mM phosphate and 2 mM aspartate-beta-semialdehyde, crystallization of mutant H277N in ...
Compound: aspartate-semialdehyde dehydrogenase. Species: Streptococcus pneumoniae [TaxId:406563]. Gene: CGSSp23BS72_03388. ... Compound: aspartate-semialdehyde dehydrogenase. Species: Streptococcus pneumoniae [TaxId:406563]. Gene: CGSSp23BS72_03388. ... Description: Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase complex with NADP and 2-aminoterephthalate. Class ...
Details6. Aspartate-semialdehyde dehydrogenase. Kind. Protein. Organism. Haemophilus influenzae (strain ATCC 51907 / DSM 11121 ... UAspartate-semialdehyde dehydrogenase. Not Available. Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). ... UShikimate dehydrogenase. Not Available. Escherichia coli (strain K12). UNADP-dependent isopropanol dehydrogenase. Not ... Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4- ...
Compound: aspartate-semialdehyde dehydrogenase. Species: Vibrio cholerae [TaxId:666]. Gene: VC_2036. Database cross-references ... Compound: aspartate-semialdehyde dehydrogenase. Species: Vibrio cholerae [TaxId:666]. Gene: VC_2036. Database cross-references ... Description: Crystals Structure of Aspartate beta-Semialdehyde Dehydrogenase from Vibrio Cholerae with product of S-allyl-L- ...
α-aspartate semialdehyde dehydrogenase * homoserine dehydrogenase * homoserine kinase * threonine synthase. Metabolism. ... It is converted to pyruvate via Threonine Dehydrogenase. An intermediate in this pathway can undergo thiolysis with CoA to ... In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. ...
Next-day shipping cDNA ORF clones derived from HOM2 aspartate-semialdehyde dehydrogenase available at GenScript, starting from ... aspartate-semialdehyde dehydrogenase. Comment. Comment: REVIEWED REFSEQ: This record has been curated by SGD. This record is ... Saccharomyces cerevisiae S288C aspartate-semialdehyde dehydrogenase (HOM2), partial mRNA.. Target ORF information:. Epitope ... Saccharomyces cerevisiae S288C aspartate-semialdehyde dehydrogenase (HOM2), partial mRNA.. pcDNA3.1+/C-(K)DYK or customized ...
Aspartate-semialdehyde dehydrogenase. 760/1. 0.17. DNAK_ECOLI (0.48). 384/1. 0.81 ...
Aspartate-semialdehyde dehydrogenase (EC 1.2.1.11). lysC† Aspartate kinase (EC 2.7.2.4). ... Enzymes involved in these conversions include citrate lyase (1), aspartate aminotransferase (2), phosphoenolpyruvate ...
... aspartate-β-semialdehyde dehydrogenase gene; PA1-O4/O3, modified promoter for the lac operon;gef, killing gene from E. coli. ... The asd gene product is involved in the biosynthesis of aspartate-β-semialdehyde, a key intermediate in the biosynthesis of ... analysis of the region containing the essential Pseudomonas aeruginosa asd gene encoding aspartate-β-semialdehyde dehydrogenase ... mutants appear no killing can take place because of the continuous synthesis of LacI and aspartate β-semialdehide dehydrogenase ...
Structure of aspartate β -semialdehyde dehydrogenase from Francisella tularensis. Aspartate β -semialdehyde dehydrogenase ( ... amino-acid biosynthesis lysine biosynthesis aspartate β -semialdehyde dehydrogenase oxidoreductases Francisella tularensis ... Aspartate racemase (AspR) is a pyridoxal 5 ′ -phosphate (PLP)-dependent enzyme that is responsible for d-aspartate biosynthesis ... Crystal structure of a pyridoxal 5 ′ -phosphate-dependent aspartate racemase derived from the bivalve mollusc Scapharca ...
... and succinic semialdehyde dehydrogenase (SSADH). The GABA shunt plays a major role in primary carbon and nitrogen metabolism ... and succinic semialdehyde dehydrogenase. The GABA shunt plays a major role in primary carbon and nitrogen metabolism and is an ... succinic semialdehyde dehydrogenase; GDH, glutamate dehydrogenase; SSR, succinic semialdehyde reductase; Asp-AT, aspartate ... succinic semialdehyde dehydrogenase; Asp-AT, aspartate aminotransferase; Glu, glutamate; Asp, aspartate. ...
  • Other names in common use include aspartate semialdehyde dehydrogenase, aspartic semialdehyde dehydrogenase, L-aspartate-beta-semialdehyde:NADP+ oxidoreductase, (phosphorylating), aspartic beta-semialdehyde dehydrogenase, and ASA dehydrogenase. (wikipedia.org)
  • Also known as Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (Aspartate-beta-semialdehyde dehydrogenase). (mybiosource.com)
  • The amino acid sequence deduced from ORF3, termed asd, is highly homologous to that of the Streptococcus mutans aspartate beta-semialdehyde dehydrogenase (ASD). (uni-bielefeld.de)
  • The asd gene encodes aspartate beta-semialdehyde dehydrogenase, an enzyme essential in amino acid and cell wall biosyntheses. (asm.org)
  • S. typhimurium delta cya delta crp strains with a delta asd mutation (abolishing production of aspartate beta-semialdehyde dehydrogenase), have an obligate requirement for diaminopimelic acid (DAP). (nih.gov)
  • Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichiacoli, a key enzyme in the aspartate family of amino acid biosynthesis. (embl.de)
  • Aspartate beta-semialdehyde dehydrogenase (ASADH) lies at the first branchpoint in an essential aspartic biosynthetic pathway found in bacteria,fungi and the higher plants. (embl.de)
  • In enzymology, an aspartate-semialdehyde dehydrogenase (EC 1.2.1.11) is an enzyme that is very important in the biosynthesis of amino acids in prokaryotes, fungi, and some higher plants. (wikipedia.org)
  • citation needed] The enzyme catalyzes the reversible chemical reaction L-aspartate 4-semialdehyde + phosphate + NADP+ ⇌ {\displaystyle \rightleftharpoons } L-4-aspartyl phosphate + NADPH + H+ The 3 substrates of this enzyme are L-aspartate 4-semialdehyde, phosphate, and NADP+, whereas its 3 products are L-4-aspartyl phosphate, NADPH, and H+. (wikipedia.org)
  • The systematic name of this enzyme class is L-aspartate-4-semialdehyde:NADP+ oxidoreductase (phosphorylating). (wikipedia.org)
  • This domain contains both N-acetyl-glutamine semialdehyde dehydrogenase (AgrC), which is involved in arginine biosynthesis, and aspartate-semialdehyde dehydrogenase, an enzyme involved in the biosynthesis of various amino acids from aspartate. (wikipedia.org)
  • An early pathway enzyme, l-aspartate-β-semialdehyde dehydrogenase, produces a key intermediate at the first branch point of this pathway. (rcsb.org)
  • Kinetic studies of two small molecule fragment libraries have identified inhibitors that show good selectivity against l-aspartate-β-semialdehyde dehydrogenases from two different bacterial species, Streptococcus pneumoniae and Vibrio cholerae, despite the presence of an identical constellation of active site amino acids in this homologous enzyme family. (rcsb.org)
  • A cautionary tale of structure-guided inhibitor development against an essential enzyme in the aspartate-biosynthetic pathway. (expasy.org)
  • In enzymology, a homoserine dehydrogenase (EC 1.1.1.3) is an enzyme that catalyzes the chemical reaction L-homoserine + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } L-aspartate 4-semialdehyde + NAD(P)H + H+ The 2 substrates of this enzyme are L-homoserine and NAD+ (or NADP+), whereas its 3 products are L-aspartate 4-semialdehyde, NADH (or NADPH), and H+. (wikipedia.org)
  • The enzyme can also be found in a bifunctional form consisting of an N-terminal aspartokinase domain and a C-terminal homoserine dehydrogenase domain, as found in bacteria such as Escherichia coli and in plants. (wikipedia.org)
  • The bifunctional aspartokinase-homoserine dehydrogenase (AK-HSD) enzyme has a regulatory domain that consists of two subdomains with a common loop-alpha helix-loop-beta strand loop-beta strand motif. (wikipedia.org)
  • The homoserine dehydrogenase-catalyzed reaction has been postulated to proceed through a bi-bi kinetic mechanism, where the NAD(P)H cofactor binds the enzyme first and is the last to dissociate from the enzyme once the reaction is complete. (wikipedia.org)
  • Additionally, the variable kinetics for homoserine dehydrogenase is an artifact of the faster dissociation of the amino acid substrate from the enzyme complex as compared to cofactor dissociation. (wikipedia.org)
  • In this pathway, GABA is synthesized from glutamate in a reaction catalyzed by the enzyme glutamate decarboxylase (GAD) and subsequently catabolized to succinate through two consecutive reactions catalyzed by GABA transaminase (GABA-T) and succinic semialdehyde dehydrogenase (SSADH). (frontiersin.org)
  • The substrate L-aspartate binds to this recombinant enzyme in two different orientations, providing the first structural evidence supporting the relaxed regiospecificity previously observed with several alternative substrates of E. coli AK.5 Binding of the nucleotide substrate triggers significant domain movements that result in a more compact quaternary structure. (openthesis.org)
  • semialdehyde dehydrogenase allows further inhibitor development to target this essential enzyme from infectious microorganisms. (openthesis.org)
  • The implementation of a mutant aspartokinase enzyme ensured efficient supply of L-aspartate-beta-semialdehyde, the precursor for ectoine biosynthesis. (biomedcentral.com)
  • The first key reaction is catalyzed by aspartate kinase (AK, EC 2.7.2.4), which phosphorylates aspartate to produce β-aspartyl phosphate, which is then converted into β-aspartyl semialdehyde by the enzyme aspartate semialdehyde dehydrogenase (ASADH, EC 1.2.1.11). (scielo.br)
  • The asd gene, encoding the enzyme aspartic semialdehyde dehydrogenase, has been cloned by complementation of Escherichia coli asd mutants. (microbiologyresearch.org)
  • L-aspartate 4-semialdehyde + phosphate + NADP + = L-4-aspartyl phosphate + NADPH. (rcsb.org)
  • The structure of aspartate semialdehyde dehydrogenase (ASADH) from the fungal pathogen C. neoformans has been determined. (iucr.org)
  • semialdehyde dehydrogenase (ASADH). (openthesis.org)
  • It forms an early branch point in the metabolic pathway forming lysine, methionine, leucine and isoleucine from aspartate. (wikipedia.org)
  • The aspartate biosynthetic pathway provides essential metabolites for many important biological functions, including the production of four essential amino acids. (rcsb.org)
  • The aspartate metabolic pathway is involved in both storage of asparagine and in synthesis of aspartate-family amino acids. (wikipedia.org)
  • Homoserine dehydrogenase catalyzes an intermediate step in this nitrogen and carbon storage and utilization pathway. (wikipedia.org)
  • Mammals lack the enzymes involved in the aspartate metabolic pathway, including homoserine dehydrogenase. (wikipedia.org)
  • HSD is inhibited by downstream products of the aspartate metabolic pathway, mainly threonine. (wikipedia.org)
  • The biosynthetic pathway proceeds from aspartate via homoserine and cystathionine to L -homocysteine (Hcy), whose thiol group is then methylated to give Met [ 7 ]. (portlandpress.com)
  • The aspartate biosynthetic pathway, essential in plants and in most bacteria and fungi, can produce the amino acids threonine, lysine, methionine, and isoleucine. (openthesis.org)
  • In summary, structural studies of threonine-sensitive AK have provided new insights into the regulation mechanism of the aspartate pathway. (openthesis.org)
  • The ectoine biosynthetic pathway starts with the phosphorylation of L-aspartate and consumes oxaloacetate (OAA) and acetyl-CoA, the latter of which is produced by oxidative decarboxylation of pyruvate by pyruvate dehydrogenase. (biomedcentral.com)
  • In plants and microorganisms , threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. (newworldencyclopedia.org)
  • It is converted to pyruvate via Threonine Dehydrogenase. (bionity.com)
  • Biosynthesis of aspartate (Asp)-derived amino acids lysine (Lys), methionine (Met), threonine (Thr), and isoleucine involves monofunctional Asp kinases (AKs) and dual-functional Asp kinase-homoserine dehydrogenases (AK-HSDHs). (plantphysiol.org)
  • The allosteric inhibitor, L-threonine, cooperatively binds to two sites in each monomer of this dimer of dimers, one site in the regulatory domain interface and the other in the kinase domain close to the proposed L-aspartate binding site. (openthesis.org)
  • Alanine and aspartate are synthesized by the transamination of pyruvate and oxaloacetate , respectively. (wikipedia.org)
  • Here we subject previously published kinetic models of pyruvate metabolism in Lactococcus lactis and aspartate-derived amino acid synthesis in Arabidopsis thaliana to generalised supply-demand analysis. (biomedcentral.com)
  • Dihydrodipicolinate synthase adds a pyruvate group to the β-aspartyl-4-semialdehyde, and two water molecules are removed. (worldheritage.org)
  • It is now clear that the involvement of enzymes is a key aspect for Lys accumulation in grains, such as lysine α-ketoglutarate reductase (LKR, EC 1.5.1.8) and saccharopine dehydrogenase (SDH, EC 1.5.1.9), which regulate Lys catabolism ( Azevedo and Arruda, 2010 ). (scielo.br)
  • Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. (rcsb.org)
  • The GABA shunt bypasses two steps (the oxidation of α-ketoglutarate to succinate) of the tricarboxylic acid (TCA) cycle via reactions catalyzed by three enzymes: glutamate decarboxylase, GABA transaminase, and succinic semialdehyde dehydrogenase. (frontiersin.org)
  • In addition to a preliminary description of a protein kinase C-like activity ( 12 ), this organism possesses two well characterized Ser/Thr kinases: the isocitrate dehydrogenase kinase/phosphorylase ( 13 ) and the recently described YihE kinase ( 14 ). (mcponline.org)
  • Additionally, the aspartate kinase-homoserine dehydrogenase gene is primarily expressed in actively growing, young plant tissues, particularly in the apical and lateral meristems. (wikipedia.org)
  • L -aspartate is first converted to L-aspartyl-4-phosphate by aspartokinase (or Aspartate kinase). (worldheritage.org)
  • glutathione-dependent formaldehyde dehydrogenase. (qmul.ac.uk)
  • The AK-HSD gene codes for aspartate kinase, an intermediate domain (coding for the linker region between the two enzymes in the bifunctional form), and finally the coding sequence for homoserine dehydrogenase. (wikipedia.org)
  • bifunctional aspartokinase I/homoserine dehydrogenase I (STM0002) [Salmonella enterica subsp. (godziklab.org)
  • First, aspartic acid is converted via β-aspartyl-semialdehyde into homoserine, introducing the pair of contiguous methylene groups. (newworldencyclopedia.org)
  • In plants and microorganisms, it is synthesized from aspartic acid , which is first converted to β-aspartyl-semialdehyde. (wikidoc.org)
  • However, Lys metabolism in immature grains was modified, showing increases in the specific activities of aspartate kinase (AK) and dihydrodipicolinate synthase (DHDPS) after Cd exposure. (scielo.br)
  • All proteins in this entry contain a dimerisation domain of semialdehyde dehydrogenase. (wikipedia.org)
  • Sequence analysis and expression of the aspartokinase and aspartate semialdehyde dehydrogenase operon from rifamycin SV-producing amycolatopsis mediterranei. (semanticscholar.org)
  • The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. (hmdb.ca)
  • Aspartate-semialdehyde dehydrogenase may be cis-regulated by an Asd RNA motif found in the 5' UTR of some Asd genes. (wikipedia.org)
  • Structure of a fungal form of aspartate semi-aldehyde de-hydrogenase from Cryptococcus neoformans (Dahal & Viola, p. 1365) . (iucr.org)
  • Transcriptome-based analysis of gene expression combined with physiological verification suggested that the 5 mg L−1 AZ treatment did not inhibit ATP generation in C. pyrenoidosa, but did significantly alter amino acid metabolism, especially in aspartate- and glutamine-related reactions. (deepdyve.com)