A pyridoxal-phosphate protein that reversibly catalyzes the conversion of L-alanine to D-alanine. EC 5.1.1.1.
Enzymes that catalyze inversion of the configuration around an asymmetric carbon in a substrate having one (racemase) or more (epimerase) center(s) of asymmetry. (Dorland, 28th ed) EC 5.1.
A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.
Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. EC 5.1.1.
Antibiotic substance produced by Streptomyces garyphalus.
An NAD-dependent enzyme that catalyzes the reversible DEAMINATION of L-ALANINE to PYRUVATE and AMMONIA. The enzyme is needed for growth when ALANINE is the sole CARBON or NITROGEN source. It may also play a role in CELL WALL synthesis because L-ALANINE is an important constituent of the PEPTIDOGLYCAN layer.
An organophosphorus compound isolated from human and animal tissues.
A species of GRAM-POSITIVE ENDOSPORE-FORMING BACTERIA in the family BACILLACEAE, found in soil, hot springs, Arctic waters, ocean sediments, and spoiled food products.
A species of gram-negative bacteria parasitic on HORSES and DONKEYS causing GLANDERS, which can be transmitted to humans.
The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
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 class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.
A species of bacteria that causes ANTHRAX in humans and animals.
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.
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 strong oxidizing agent.

Aromatic L-amino acid decarboxylase: conformational change in the flexible region around Arg334 is required during the transaldimination process. (1/84)

Aromatic L-amino acid decarboxylase (AADC) catalytic mechanism has been proposed to proceed through two consecutive intermediates (i.e., Michaelis complex and the external aldimine). Limited proteolysis of AADC that preferentially digested at the C-terminal side of Arg334 was slightly retarded in the presence of dihydroxyphenyl acetate that formed a stable Michaelis complex. On the contrary, AADC was scarcely digested in the presence of L-dopa methyl ester that formed a stable external aldimine. Similar protection by the substrate analogs was observed in the chemical modification experiment. From these results, we concluded that the region around Arg334 must be exposed and flexible in the unliganded state, and forming the Michaelis complex generated a subtle conformational change, then underwent marked conformational change during the subsequent transaldimination process prerequisite to forming the external aldimine. For further analyses, we constructed a mutant gene encoding in tandem the two peptides of AADC cleaved at the Asn327-Met328 bond inside the putative flexible region. The gene product, fragmentary AADC, was still active with L-dopa as substrate, but its k(cat) value was decreased 57-fold, and the Km value was increased 9-fold compared with those of the wild-type AADC. The absorption spectra of the fragmentary AADC in the presence of L-dopa methyl ester showed shift in the equilibrium of the transaldimination from the external aldimine to the Michaelis complex. Tryptic digestion of the fragmentary AADC removed seven amino acid residues, Met328-Arg334, and resulted in complete inactivation. Susceptibility of the fragmentary enzyme to trypsin was not changed by L-dopa methyl ester revealing the loss of appropriate conformational change in the flexible region induced by substrate binding. From these results we propose that the conformational change in the flexible region is required during the transaldimination process.  (+info)

Role of tyrosine 265 of alanine racemase from Bacillus stearothermophilus. (2/84)

Tyrosine 265 (Y265) of Bacillus stearothermophilus is believed to serve as a catalytic base specific to the L-enantiomer of a substrate amino acid by removing (or returning) an alpha-hydrogen from (or to) the isomer on the basis of the X-ray structure of the enzyme [Stamper, C.G., Morollo, A.A., and Ringe, D. (1998) Biochemistry 37, 10438-10443]. We found that the Y265-->Ala mutant (Y265A) enzyme is virtually inactive as a catalyst for alanine racemization. We examined the role of Y265 further with beta-chloroalanine as a substrate with the expectation that the Y265A mutant only catalyzes the alpha,beta-elimination of the D-enantiomer of beta-chloroalanine. However, L-beta-chloroalanine also served as a substrate; this enantiomer was rather better as a substrate than its antipode. Moreover, the mutant enzyme was as equally active as the wild-type enzyme in the elimination reaction. These findings indicate that Y265 is essential for alanine racemization but not for beta-chloroalanine elimination.  (+info)

Transcriptional control of peptidoglycan precursor synthesis during sporulation in Bacillus sphaericus. (3/84)

Synthesis of enzymes functional in the synthesis of nucleotide precursors of peptidoglycan ceases upon initiation of sporulation in Bacillus sphaericus. During sporulation, two periods of synthesis of these enzymes occur. The first starts at spore septum formation and is conincident with forespore engulfment; it involves the synthesis of those enzymes required for making the precursor of vegetative-type peptidoglycan, including L-lysyl ligase but no mesodiaminopimelyl ligase. The second period occurs shortly before the appearance of cortex. It involves the synthesis of diaminopimelyl ligase and the other enzymes needed for making the precursor of cortical peptidoglycan, but not lysyl ligase. Both events are a consequence of derepression at the level of transcription. Neither period of synthesis occurs in asporogenous mutants whose morphological block is at the point of spore septum formation.  (+info)

Tyrosine 265 of alanine racemase serves as a base abstracting alpha-hydrogen from L-alanine: the counterpart residue to lysine 39 specific to D-alanine. (4/84)

Alanine racemase of Bacillus stearothermophilus has been proposed to catalyze alanine racemization by means of two catalytic bases: lysine 39 (K39) abstracting specifically the alpha-hydrogen of D-alanine and tyrosine 265 (Y265) playing the corresponding role for the antipode L-alanine. The role of K39 as indicated has already been verified [Watanabe, A., Kurokawa, Y., Yoshimura, T., Kurihara, T., Soda, K., and Esaki, N. (1999) J. Biol. Chem. 274, 4189-4194]. We here present evidence for the functioning of Y265 as the base catalyst specific to L-alanine. The Y265-->Ala mutant enzyme (Y265A), like Y265S and Y265F, was a poor catalyst for alanine racemization. However, Y265A and Y265S catalyzed transamination with D-alanine much more rapidly than the wild-type enzyme, and the bound coenzyme, pyridoxal 5'-phosphate (PLP), was converted to pyridoxamine 5'-phosphate (PMP). The rate of transamination catalyzed by Y265F was about 9% of that by the wild-type enzyme. However, Y265A, Y265S, and Y265F were similar in that L-alanine was inert as a substrate in transamination. The apo-form of the wild-type enzyme catalyzes the abstraction of tritium non-specifically from both (4'S)- and (4'R)-[4'-(3)H]PMP in the presence of pyruvate. In contrast, apo-Y265A abstracts tritium virtually from only the R-isomer. This indicates that the side-chain of Y265 abstracts the alpha-hydrogen of L-alanine and transfers it supra-facially to the pro-S position at C-4' of PMP. Y265 is the counterpart residue to K39 that transfers the alpha-hydrogen of D-alanine to the pro-R position of PMP.  (+info)

A eukaryotic alanine racemase gene involved in cyclic peptide biosynthesis. (5/84)

The cyclic tetrapeptide HC-toxin is an essential virulence determinant for the plant pathogenic fungus Cochliobolus carbonum and an inhibitor of histone deacetylase. The major form of HC-toxin contains the D-isomers of Ala and Pro. The non-ribosomal peptide synthetase that synthesizes HC-toxin has only one epimerizing domain for conversion of L-Pro to D-Pro; the source of D-Ala has remained unknown. Here we present the cloning and characterization of a new gene involved in HC-toxin biosynthesis, TOXG. TOXG is present only in HC-toxin-producing (Tox2(+)) isolates of C. carbonum. TOXG is able to support D-Ala-independent growth of a strain of Escherichia coli defective in D-Ala synthesis. A C. carbonum strain with both of its copies of TOXG mutated grows normally in culture, and although it no longer makes the three forms of HC-toxin that contain D-Ala, it still makes a minor form of HC-toxin that contains Gly in place of D-Ala. The addition of D-Ala to the culture medium restores production of the D-Ala-containing forms of HC-toxin by the toxG mutant. The toxG mutant has only partially reduced virulence. It is concluded that TOXG encodes an alanine racemase whose function is to synthesize D-Ala for incorporation into HC-toxin.  (+info)

The manifold of vitamin B6 dependent enzymes. (6/84)

Pyridoxal-5'-phosphate (vitamin B6) binding enzymes form a large superfamily that contains at least five different folds. The availability of an increasing number of known three-dimensional structures for members of this superfamily has allowed a detailed structural classification. Most progress has been made with the fold type I or aspartate aminotransferase family.  (+info)

Serine and alanine racemase activities of VanT: a protein necessary for vancomycin resistance in Enterococcus gallinarum BM4174. (7/84)

Vancomycin resistance in Enterococcus gallinarum results from the production of UDP-MurNAc-pentapeptide[D-Ser]. VanT, a membrane-bound serine racemase, is one of three proteins essential for this resistance. To investigate the selectivity of racemization of L-Ser or L-Ala by VanT, a strain of Escherichia coli TKL-10 that requires D-Ala for growth at 42 degrees C was used as host for transformation experiments using plasmids containing the full-length vanT from Ent. gallinarum or the alanine racemase gene (alr) of Bacillus stearothermophilus: both plasmids were able to complement E. coli TKL-10 at 42 degrees C. No alanine or serine racemase activities were detected in the host strain E. coli TKL-10 grown at 30, 34 or 37 degrees C. Serine and alanine racemase activities were found almost exclusively (96%) in the membrane fraction of E. coli TKL-10/pCA4(vanT): the alanine racemase activity of VanT was 14% of the serine racemase activity in both E. coli TKL-10/pCA4(vanT) and E. coli XL-1 Blue/pCA4(vanT). Alanine racemase activity was present mainly (95%) in the cytoplasmic fraction of E. coli TKL-10/pJW40(alr), with a trace (1.6%) of serine racemase activity. Additionally, DNA encoding the soluble domain of VanT was cloned and expressed in E. coli M15 as a His-tagged polypeptide and purified: this polypeptide also exhibited both serine and alanine racemase activities; the latter was approximately 18% of the serine racemase activity, similar to that of the full-length, membrane-bound enzyme. N-terminal sequencing of the purified His-tagged polypeptide revealed a single amino acid sequence, indicating that the formation of heterodimers between subunits of His-tagged C-VanT and endogenous alanine racemases from E. coli was unlikely. The authors conclude that the membrane-bound serine racemase VanT also has alanine racemase activity but is able to racemize serine more efficiently than alanine, and that the cytoplasmic domain is responsible for the racemase activity.  (+info)

Functional characterization of alanine racemase from Schizosaccharomyces pombe: a eucaryotic counterpart to bacterial alanine racemase. (8/84)

Schizosaccharomyces pombe has an open reading frame, which we named alr1(+), encoding a putative protein similar to bacterial alanine racemase. We cloned the alr1(+) gene in Escherichia coli and purified the gene product (Alr1p), with an M(r) of 41,590, to homogeneity. Alr1p contains pyridoxal 5'-phosphate as a coenzyme and catalyzes the racemization of alanine with apparent K(m) and V(max) values as follows: for L-alanine, 5.0 mM and 670 micromol/min/mg, respectively, and for D-alanine, 2.4 mM and 350 micromol/min/mg, respectively. The enzyme is almost specific to alanine, but L-serine and L-2-aminobutyrate are racemized slowly at rates 3.7 and 0.37% of that of L-alanine, respectively. S. pombe uses D-alanine as a sole nitrogen source, but deletion of the alr1(+) gene resulted in retarded growth on the same medium. This indicates that S. pombe has catabolic pathways for both enantiomers of alanine and that the pathway for L-alanine coupled with racemization plays a major role in the catabolism of D-alanine. Saccharomyces cerevisiae differs markedly from S. pombe: S. cerevisiae uses L-alanine but not D-alanine as a sole nitrogen source. Moreover, D-alanine is toxic to S. cerevisiae. However, heterologous expression of the alr1(+) gene enabled S. cerevisiae to grow efficiently on D-alanine as a sole nitrogen source. The recombinant yeast was relieved from the toxicity of D-alanine.  (+info)

Alanine racemase is an enzyme that catalyzes the conversion of the amino acid alanine between its two stereoisomeric forms, D-alanine and L-alanine. This enzyme plays a crucial role in the biosynthesis of peptidoglycan, a major component of bacterial cell walls. In humans, alanine racemase is found in the cytosol of many tissues, including the liver, kidneys, and brain. It is also an important enzyme in the metabolism of amino acids and has been implicated in various disease processes, including neurodegenerative disorders and cancer.

Racemases and epimerases are two types of enzymes that are involved in the modification of the stereochemistry of molecules, particularly amino acids and sugars. Here is a brief definition for each:

1. Racemases: These are enzymes that catalyze the interconversion of D- and L-stereoisomers of amino acids or other chiral compounds. They do this by promoting the conversion of one stereoisomer to its mirror image, resulting in a racemic mixture (a 1:1 mixture of two enantiomers). Racemases are important in various biological processes, such as the biosynthesis of some amino acids and the degradation of certain carbohydrates.

Example: Alanine racemase is an enzyme that catalyzes the conversion of L-alanine to D-alanine, which is essential for bacterial cell wall biosynthesis.

2. Epimerases: These are enzymes that convert one stereoisomer (epimer) of a chiral compound into another stereoisomer by changing the configuration at a single asymmetric carbon atom while keeping the rest of the molecule unchanged. Unlike racemases, epimerases do not produce racemic mixtures but rather create specific stereoisomers.

Example: Glucose-1-phosphate epimerase is an enzyme that converts glucose-1-phosphate to galactose-1-phosphate during the Leloir pathway, which is the primary metabolic route for lactose digestion in mammals.

Both racemases and epimerases play crucial roles in various biochemical processes, including the synthesis and degradation of essential molecules like amino acids and carbohydrates.

Alanine is an alpha-amino acid that is used in the biosynthesis of proteins. The molecular formula for alanine is C3H7NO2. It is a non-essential amino acid, which means that it can be produced by the human body through the conversion of other nutrients, such as pyruvate, and does not need to be obtained directly from the diet.

Alanine is classified as an aliphatic amino acid because it contains a simple carbon side chain. It is also a non-polar amino acid, which means that it is hydrophobic and tends to repel water. Alanine plays a role in the metabolism of glucose and helps to regulate blood sugar levels. It is also involved in the transfer of nitrogen between tissues and helps to maintain the balance of nitrogen in the body.

In addition to its role as a building block of proteins, alanine is also used as a neurotransmitter in the brain and has been shown to have a calming effect on the nervous system. It is found in many foods, including meats, poultry, fish, eggs, dairy products, and legumes.

Amino acid isomerases are a class of enzymes that catalyze the conversion of one amino acid stereoisomer to another. These enzymes play a crucial role in the metabolism and biosynthesis of amino acids, which are the building blocks of proteins.

Amino acids can exist in two forms, called L- and D-stereoisomers, based on the spatial arrangement of their constituent atoms around a central carbon atom. While most naturally occurring amino acids are of the L-configuration, some D-amino acids are also found in certain proteins and peptides, particularly in bacteria and lower organisms.

Amino acid isomerases can convert one stereoisomer to another by breaking and reforming chemical bonds in a process that requires energy. This conversion can be important for the proper functioning of various biological processes, such as protein synthesis, neurotransmitter metabolism, and immune response.

Examples of amino acid isomerases include proline racemase, which catalyzes the interconversion of L-proline and D-proline, and serine hydroxymethyltransferase, which converts L-serine to D-serine. These enzymes are essential for maintaining the balance of amino acids in living organisms and have potential therapeutic applications in various diseases, including neurodegenerative disorders and cancer.

Cycloserine is an antibiotic medication used to treat tuberculosis (TB) that is resistant to other antibiotics. It works by killing or inhibiting the growth of the bacteria that cause TB. Cycloserine is a second-line drug, which means it is used when first-line treatments have failed or are not effective.

The medical definition of Cycloserine is:

A bacteriostatic antibiotic derived from Streptomyces orchidaceus that inhibits gram-positive and gram-negative bacteria by interfering with peptidoglycan synthesis in the bacterial cell wall. It has been used to treat tuberculosis, but its use is limited due to its adverse effects, including neurotoxicity, which can manifest as seizures, dizziness, and confusion. Cycloserine is also used in the treatment of urinary tract infections and other bacterial infections that are resistant to other antibiotics. It is available in oral form and is typically taken two to four times a day.

Alanine Dehydrogenase (ADH) is an enzyme that catalyzes the reversible conversion between alanine and pyruvate with the reduction of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide hydride (NADH). This reaction plays a role in the metabolism of amino acids, particularly in the catabolism of alanine.

In humans, there are multiple isoforms of ADH that are expressed in different tissues and have different functions. The isoform known as ALDH4A1 is primarily responsible for the conversion of alanine to pyruvate in the liver. Deficiencies or mutations in this enzyme can lead to a rare genetic disorder called 4-hydroxybutyric aciduria, which is characterized by elevated levels of 4-hydroxybutyric acid in the urine and neurological symptoms.

Aminoethylphosphonic acid is a chemical compound with the formula (HO)₂P(O)CH₂CH₂NH₂. It is an organophosphorus compound that contains both phosphonic and amino groups. This compound is a colorless solid that is soluble in water and has various applications in industry, including as a corrosion inhibitor and a scale inhibitor in water treatment systems. It may also have potential uses in medicine, such as in the treatment of kidney stones, although its use in this context is still being studied.

"Geobacillus stearothermophilus" is a species of gram-positive, rod-shaped bacteria that is thermophilic, meaning it thrives at relatively high temperatures. It is commonly found in soil and hot springs, and can also be found in other environments such as compost piles, oil fields, and even in some food products.

The bacterium is known for its ability to form endospores that are highly resistant to heat, radiation, and chemicals, making it a useful organism for sterility testing and bioprotection applications. It has an optimum growth temperature of around 60-70°C (140-158°F) and can survive at temperatures up to 80°C (176°F).

In the medical field, "Geobacillus stearothermophilus" is not typically associated with human disease or infection. However, there have been rare cases of infections reported in immunocompromised individuals who have come into contact with contaminated medical devices or materials.

Burkholderia mallei is a gram-negative, non-motile, rod-shaped bacterium that causes the disease glanders in horses, donkeys, and other solipeds. It can also cause severe and often fatal illness in humans who come into contact with infected animals or contaminated materials. Glanders is rare in developed countries but still occurs in parts of Asia, Africa, and Central and South America.

Human infection with Burkholderia mallei typically occurs through inhalation of infectious aerosols, direct contact with broken skin or mucous membranes, or ingestion of contaminated food or water. The bacterium can cause a range of symptoms, including fever, chills, headache, muscle and joint pain, cough, chest pain, and pneumonia. In severe cases, it can spread to other organs, such as the skin, bones, brain, and spleen, leading to sepsis and death if left untreated.

Burkholderia mallei is highly infectious and resistant to environmental degradation, making it a potential agent of bioterrorism. It is classified as a Tier 1 select agent by the Centers for Disease Control and Prevention (CDC) in the United States, meaning that it poses a high risk to national security and public health.

Prevention and control measures include avoiding contact with infected animals or contaminated materials, using personal protective equipment when handling suspect specimens, and implementing strict biosecurity measures in laboratories and animal facilities. Treatment typically involves a combination of antibiotics, such as ceftazidime, meropenem, or trimethoprim-sulfamethoxazole, for at least 3 weeks to ensure complete eradication of the bacterium.

Stereoisomerism is a type of isomerism (structural arrangement of atoms) in which molecules have the same molecular formula and sequence of bonded atoms, but differ in the three-dimensional orientation of their atoms in space. This occurs when the molecule contains asymmetric carbon atoms or other rigid structures that prevent free rotation, leading to distinct spatial arrangements of groups of atoms around a central point. Stereoisomers can have different chemical and physical properties, such as optical activity, boiling points, and reactivities, due to differences in their shape and the way they interact with other molecules.

There are two main types of stereoisomerism: enantiomers (mirror-image isomers) and diastereomers (non-mirror-image isomers). Enantiomers are pairs of stereoisomers that are mirror images of each other, but cannot be superimposed on one another. Diastereomers, on the other hand, are non-mirror-image stereoisomers that have different physical and chemical properties.

Stereoisomerism is an important concept in chemistry and biology, as it can affect the biological activity of molecules, such as drugs and natural products. For example, some enantiomers of a drug may be active, while others are inactive or even toxic. Therefore, understanding stereoisomerism is crucial for designing and synthesizing effective and safe drugs.

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.

Isomerases are a class of enzymes that catalyze the interconversion of isomers of a single molecule. They do this by rearranging atoms within a molecule to form a new structural arrangement or isomer. Isomerases can act on various types of chemical bonds, including carbon-carbon and carbon-oxygen bonds.

There are several subclasses of isomerases, including:

1. Racemases and epimerases: These enzymes interconvert stereoisomers, which are molecules that have the same molecular formula but different spatial arrangements of their atoms in three-dimensional space.
2. Cis-trans isomerases: These enzymes interconvert cis and trans isomers, which differ in the arrangement of groups on opposite sides of a double bond.
3. Intramolecular oxidoreductases: These enzymes catalyze the transfer of electrons within a single molecule, resulting in the formation of different isomers.
4. Mutases: These enzymes catalyze the transfer of functional groups within a molecule, resulting in the formation of different isomers.
5. Tautomeres: These enzymes catalyze the interconversion of tautomers, which are isomeric forms of a molecule that differ in the location of a movable hydrogen atom and a double bond.

Isomerases play important roles in various biological processes, including metabolism, signaling, and regulation.

'Bacillus anthracis' is the scientific name for the bacterium that causes anthrax, a serious and potentially fatal infectious disease. This gram-positive, spore-forming rod-shaped bacterium can be found in soil and commonly affects animals such as sheep, goats, and cattle. Anthrax can manifest in several forms, including cutaneous (skin), gastrointestinal, and inhalation anthrax, depending on the route of infection.

The spores of Bacillus anthracis are highly resistant to environmental conditions and can survive for years, making them a potential agent for bioterrorism or biowarfare. When inhaled, ingested, or introduced through breaks in the skin, these spores can germinate into vegetative bacteria that produce potent exotoxins responsible for anthrax symptoms and complications.

It is essential to distinguish Bacillus anthracis from other Bacillus species due to its public health significance and potential use as a biological weapon. Proper identification, prevention strategies, and medical countermeasures are crucial in mitigating the risks associated with this bacterium.

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.

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.

Periodic acid is not a medical term per se, but it is a chemical reagent that is used in some laboratory tests and staining procedures in the field of pathology, which is a medical specialty.

Periodic acid is an oxidizing agent with the chemical formula HIO4 or H5IO6. It is often used in histology (the study of the microscopic structure of tissues) to perform a special staining technique called the periodic acid-Schiff (PAS) reaction. This reaction is used to identify certain types of carbohydrates, such as glycogen and some types of mucins, in tissues.

The periodic acid first oxidizes the carbohydrate molecules, creating aldehydes. These aldehydes then react with a Schiff reagent, which results in a pink or magenta color. This reaction can help pathologists identify and diagnose various medical conditions, such as cancer, infection, and inflammation.

... can be found in some invertebrates. Bacteria can have one (alr gene) or two alanine racemase genes. Bacterial ... The systematic name of this enzyme class is alanine racemase. This enzyme is also called L-alanine racemase. This enzyme ... The D-alanine produced by alanine racemase is used for peptidoglycan biosynthesis. Peptidoglycan is found in the cell walls of ... In enzymology, an alanine racemase (EC 5.1.1.1) is an enzyme that catalyzes the chemical reaction L-alanine ⇌ {\displaystyle \ ...
Fermentation routes to L-alanine are complicated by alanine racemase. Racemic alanine can be prepared by the condensation of ... is so-called alanine scanning, where every position in turn is mutated to alanine. Hydrogenation of alanine gives the amino ... forming alanine and α-ketoglutarate. The alanine enters the bloodstream, and is transported to the liver. The alanine ... Alanine (symbol Ala or A), or α-alanine, is an α-amino acid that is used in the biosynthesis of proteins. It contains an amine ...
DAPDC is a PLP-dependent enzyme belonging to the alanine racemase family. This enzyme is generally dimeric with each monomer ... "Functional classification of amino acid decarboxylases from the alanine racemase structural family by phylogenetic studies". ...
The racemization of L-Ala to D-Ala by alanine racemase is pyridoxal phosphate-dependent. The formation of butenyl-methyl-L- ... Of these 12 genes, SimA (Q09164) is the cyclosporin synthetase, SimB (CAA02484.1) is the alanine racemase, and SimG (similar to ... di Salvo ML, Florio R, Paiardini A, Vivoli M, D'Aguanno S, Contestabile R (January 2013). "Alanine racemase from Tolypocladium ... Cyclosporin synthetase substrates include L-valine, L-leucine, L-alanine, glycine, 2-aminobutyric acid, 4-methylthreonine, and ...
The expression levels of alanine racemase affects the level of cyclosporine production by T. inflatum. Ciclosporin A was first ... "Alanine racemase from Tolypocladium inflatum: A key PLP-dependent enzyme in cyclosporin biosynthesis and a model of catalytic ...
... and one of them is alanine racemase (alr). This enzyme is significant because it is found in D-alanine-D-alanine ligase and ... alanine/Aspartate metabolism. Other essential enzymes include putative dTDP4deydrorhamnose 3, 5epimerase (rm1C) which plays an ...
AlaP (alanine phosphonate) inhibits alanine racemases, but its lack of specificity has prompted further designs of ALR ... D-alanine aminotransferase family and the alanine racemase family. An example of the evolutionary similarity in the Beta family ... Fold Type I - aspartate aminotransferase family Fold Type II - tryptophan synthase family Fold Type III - alanine racemase ... 2011). Ahmed N (ed.). "New classes of alanine racemase inhibitors identified by high-throughput screening show antimicrobial ...
"Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent ...
"A Combined Quantum Mechanical and Molecular Mechanical Study of the Reaction Mechanism and α-Amino Acidity in Alanine Racemase ...
Seven proteins have been identified in washed exosporium: alanine racemase, inosine hydrolase, ExsF, CotY, ExsY, CotB, and a ...
... alr encodes an enzyme L-alanine racemase, which converts L-alanine to D-alanine in the first step of peptidoglycan synthesis ...
... alanine racemase (Alr) and D-alanine:D-alanine ligase (Ddl). The first enzyme is a pyridoxal 5'-phosphate-dependent enzyme ... Lambert MP, Neuhaus FC (June 1972). "Mechanism of D-cycloserine action: alanine racemase from Escherichia coli W". Journal of ... If both of these enzymes are inhibited, then D-alanine residues cannot form and previously formed D-alanine molecules cannot be ... Prosser GA, de Carvalho LP (February 2013). "Kinetic mechanism and inhibition of Mycobacterium tuberculosis D-alanine:D-alanine ...
... alanine racemase MeSH D08.811.399.894.500 - carbohydrate epimerases MeSH D08.811.399.894.500.700 - UDP-glucose 4-epimerase MeSH ... beta-alanine-pyruvate transaminase MeSH D08.811.913.477.700.347 - d-alanine transaminase MeSH D08.811.913.477.700.470 - ... alanine-tRNA ligase MeSH D08.811.464.263.200.100 - arginine-tRNA ligase MeSH D08.811.464.263.200.150 - aspartate-tRNA ligase ... alanine dehydrogenase MeSH D08.811.682.664.500.125 - d-amino-acid oxidase MeSH D08.811.682.664.500.261 - d-aspartate oxidase ...
EC 5.1.1.1: alanine racemase EC 5.1.1.2: methionine racemase EC 5.1.1.3: glutamate racemase EC 5.1.1.4: proline racemase EC 5.1 ... allantoin racemase EC 5.1.99.4: α-methylacyl-CoA racemase EC 5.1.99.5: hydantoin racemase EC 5.1.99.6: NAD(P)H-hydrate ... lactate racemase EC 5.1.2.2: mandelate racemase EC 5.1.2.3: 3-hydroxybutyryl-CoA epimerase EC 5.1.2.4: acetoin racemase EC 5.1. ... arginine racemase EC 5.1.1.10: amino-acid racemase EC 5.1.1.11: phenylalanine racemase (ATP-hydrolysing) EC 5.1.1.12: ornithine ...
D-alanine-D-serine ligase, alanine racemase, phosphate acetyltransferase, NADH peroxidase,Phosphopantetheine ... Glutamate racemase, hydroxymethylglutaryl-CoA synthase, diphosphomevalonate decarboxylase, topoisomerase DNA gyrase B, ...
... iron-sulphur cluster-binding protein and alanine racemase, which in most cases are exclusively shared by either all or most ...
It was then determined that aspartate racemase also racemizes L-alanine around half as quickly as it does L-aspartate, but does ... proline racemase, and hydroxyproline-2-epimerase. Mammalian aspartate racemase, in contrast with bacterial aspartate racemase, ... First, D-aspartate is isomerized to L-aspartate by aspartate racemase, followed by decarboxylation to form L-alanine. D-amino ... Notably, aspartate racemase in E. coli is also able to catalyze the racemization of glutamate. In 2004, an aspartate racemase ...
Human epimerases include methylmalonyl-CoA epimerase, involved in the metabolic breakdown of the amino acids alanine, ... Racemases catalyze the stereochemical inversion around the asymmetric carbon atom in a substrate having only one center of ... Epimerases and racemases are isomerase enzymes that catalyze the inversion of stereochemistry in biological molecules. ... "Isomerase , enzyme , Britannica". http://medical-dictionary.thefreedictionary.com/racemase http://medical-dictionary. ...
D-alanine. L-alanine. L- and D-amino acids are usually enantiomers. The exceptions are two amino acids with two stereogenic ... D-Amino-acid racemase, a PLP-dependent enzyme, racemizes amino acids via the formation of the alpha-iminoacids, where the ... The D-alanine in peptidoglycans that comprise bacterial cell walls helps its host resist attack by proteolytic enzymes. Several ... They have been known to synthesize more than 10 kinds of D-amino acids, most frequently D-alanine and D-glutamate for ...
Other names in common use include D-aspartate transaminase, D-alanine aminotransferase, D-aspartic aminotransferase, D-alanine- ... "Characterization of the genes encoding D-amino acid transaminase and glutamate racemase, two D-glutamate biosynthetic enzymes ... In enzymology, a D-amino-acid transaminase (EC 2.6.1.21) is an enzyme that catalyzes the chemical reaction: D-alanine + 2- ... Martinez-Carrion M, Jenkins WT (1965). "D-Alanine-D-glutamate transaminase. I. Purification and characterization". J. Biol. ...
... endogenous glycine site agonist Alanine (D-alanine, L-alanine) - endogenous glycine site agonist Milacemide - synthetic glycine ... It is produced by serine racemase, and is enriched in the same areas as NMDA receptors. Removal of D-serine can block NMDA- ... 1 takes part to the Ca2+-related prosurvival pathway of SOD1 in primary motor neurons exposed to beta-methylamino-L-alanine". ...
The DXP-dependent pathway: The starting material is either the amino acid alanine, or propionic acid converted into alanine via ... Serine racemase which synthesizes the neuromodulator D-serine from its enantiomer is a PLP-dependent enzyme. PLP is a coenzyme ...
EC 5.1.1 Amino-acid racemase: Phenylalanine racemase (ATP-hydrolysing) Serine racemase Category:EC 5.1.2 Mandelate racemase ... EC 2.6.1 Alanine transaminase EC 2.6.1.2 Aspartate transaminase EC 2.6.1.1 Category:EC 2.7.2 Butyrate kinase (EC 2.7.2.7) EC ... D-alanine-D-alanyl-carrier protein ligase EC 6.2.1.55: E1 SAMP-activating enzyme Glutamine synthetase (EC 6.3.1.2) ... EC 3.4.11 Alanine aminopeptidase Category:EC 3.4.15 Angiotensin converting enzyme Category:EC 3.4.21 Serine protease ...
Examples are as follows: Alanine + α-ketoglutarate ⇌ pyruvate + glutamate Aspartate + α-ketoglutarate ⇌ oxaloacetate + ... which produce it from the l form with the enzyme glutamate racemase) and the liver of mammals. Although they occur naturally in ...
Examples include β-alanine, GABA, and δ-aminolevulinic acid. β-alanine: an amino acid produced by aspartate 1-decarboxylase and ... serine racemase from vancomycin-resistant Enterococcus gallinarum BM4174". Molecular Microbiology. 31 (6): 1653-1664. doi: ... alanine aminoisobutyric acid dehydroalanine A subset of L-α-amino acids are ambiguous as to which of two ends is the α-carbon. ... This compound is similar to alanine, but possesses an additional methyl group on the α-carbon instead of a hydrogen. It is ...
Ashiuchi, M.; Kuwana, E; Yamamoto, T; Komatsu, K; Soda, K; Misono, H (2002). "Glutamate Racemase is an Endogenous DNA Gyrase ... Schulz, Ju¨Rgen; Sparmann, Gisela; Hofmann, Eberhard (1975). "Alanine-mediated reversible inactivation of tumour pyruvate ... Ashiuchi, M.; Tani, K.; Soda, K.; Misono, H. (1998). "Properties of Glutamate Racemase from Bacillus subtilis IFO 3336 ... 2007). "Structural and Functional Analysis of Two Glutamate Racemase Isozymes from Bacillus anthracis and Implications for ...
Alanine racemase can be found in some invertebrates. Bacteria can have one (alr gene) or two alanine racemase genes. Bacterial ... The systematic name of this enzyme class is alanine racemase. This enzyme is also called L-alanine racemase. This enzyme ... The D-alanine produced by alanine racemase is used for peptidoglycan biosynthesis. Peptidoglycan is found in the cell walls of ... In enzymology, an alanine racemase (EC 5.1.1.1) is an enzyme that catalyzes the chemical reaction L-alanine ⇌ {\displaystyle \ ...
Family c.1.6.1: Alanine racemase-like, N-terminal domain [51420] (4 proteins). ...
alanine racemase. 4. A1E_00475 (rpmB). 109015..109308 [+], 294. 157803281. 50S ribosomal protein L28. ...
alanine racemase (EC 5.1.1.1). 48%. 348.2. Confidence: high confidence medium confidence low confidence. ? - known gap: despite ...
Purification, properties, and partial amino acid sequences of alanine racemase from the muscle of the black tiger prawn Penaeus ... Purification and some properties of alanine racemase from a bivalve mollusc Corbicula japonica. J. Exp. Zool. ... Cloning and expression of a cDNA encoding the transporter of taurine and beta-alanine in mouse brain. Proc. Natl. Acad. Sci. ... 4). A much smaller competitive effect from α-alanine and proline has been reported for the taurine transporter of human ...
Alanine racemase and neutral protease were uniquely immunogenic to B. anthracis. Comparative analysis of the spore immunome ...
Racemase, Alanine use Alanine Racemase Racemases use Racemases and Epimerases Racemases and Epimerases ...
Racemase, Alanine use Alanine Racemase Racemases use Racemases and Epimerases Racemases and Epimerases ...
AGXT: alanine--glyoxylate aminotransferase. *AHCY: adenosylhomocysteinase. *AHDC1: AT-hook DNA binding motif containing 1 ... AMACR: alpha-methylacyl-CoA racemase. *AMELX: amelogenin X-linked. *AMER1: APC membrane recruitment protein 1 ...
TDP-43 was mutated to alanine or aspartic acid at Ser379, Ser403/404, or Ser409/410 to block or mimic phosphorylation. Site- ... Recombinant Human Serine racemase (SRR). 2249 mg. Ask for price Recombinant Human Serine racemase (SRR). ...
... alpha-methylacyl-CoA racemase) AMACR. RCC with haemangioblastoma-like features did not display any VHL alterations, including ... 16 years of age with alanine or aspartate aminotransferase levels of >500 IU. Data were analyzed for the periods of October 1, ...
HUMAN Myristoylated alanine-rich C-kinase substrate OS=Homo sapiens GN=MARCKS PE=1 SV=4 ... HUMAN Alpha-methylacyl-CoA racemase OS=Homo sapiens GN=AMACR PE=1 SV=2 ... HUMAN N-acetylmuramoyl-L-alanine amidase OS=Homo sapiens GN=PGLYRP2 PE=1 SV=1 ...
We report the crystal structure of alanine racemase from Mycobacterium tuberculosis (Alr(Mtb)) at 1.9 A resolution. In our ... D-Cycloserine destruction by alanine racemase and the limit of irreversible inhibition. de Chiara C, Homšak M, Prosser GA, ... The domain makeup of each monomer is similar to that of Bacillus and Pseudomonas alanine racemases and includes both an alpha/ ... Analysis of the active site pocket, in the context of other known alanine racemases, allows us to propose the inclusion of ...
D-alanine racemase and ligase. Data taken from [36,38].. Tables. Table 2. Recommended anti-TB drug regimens; including details ...
The 1.9 A crystal structure of alanine racemase from Mycobacterium tuberculosis contains a conserved entryway into the active ...
... the initial step of peptidoglycan synthesis involves conversion of L-alanine to D-alanine by alanine racemase. Two D-alanine ... Both alanine racemase and D-ala-D-ala ligase are competitively inhibited by D-cycloserine, an analog of D-alanine. ... Role of Alanine Racemase Mutations in Mycobacterium tuberculosis d-Cycloserine Resistance. Nakatani Y, Opel-Reading HK, Merker ... Overexpression of the D-alanine racemase gene confers resistance to D-cycloserine in Mycobacterium smegmatis. Cáceres NE, ...
Alanine racemase (substance). Code System Preferred Concept Name. Alanine racemase (substance). Concept Status. Published. ...
Racemases and Epimerases [D08.811.399.894] * Amino Acid Isomerases [D08.811.399.894.200] * Alanine Racemase [D08.811.399.894. ... Alanine racemase. Previous Indexing. Alanine (1974-1975). Amino Acid Isomerases (1970-1975). Public MeSH Note. 91; was see ... A pyridoxal-phosphate protein that reversibly catalyzes the conversion of L-alanine to D-alanine. EC 5.1.1.1.. Terms. Alanine ... Alanine Racemase Preferred Concept UI. M0000622. Registry Number. EC 5.1.1.1. Related Numbers. 9024-06-0. Scope Note. ...
Racemases and Epimerases [D08.811.399.894] * Amino Acid Isomerases [D08.811.399.894.200] * Alanine Racemase [D08.811.399.894. ... Alanine racemase. Previous Indexing. Alanine (1974-1975). Amino Acid Isomerases (1970-1975). Public MeSH Note. 91; was see ... A pyridoxal-phosphate protein that reversibly catalyzes the conversion of L-alanine to D-alanine. EC 5.1.1.1.. Terms. Alanine ... Alanine Racemase Preferred Concept UI. M0000622. Registry Number. EC 5.1.1.1. Related Numbers. 9024-06-0. Scope Note. ...
"Alanine racemase, N-terminal; D-serine dehydratase-like domain [Interproscan].","protein_coding" "XM_003060978.1","MicpuC2_ ... membrane alanine aminopeptidase [Interproscan].","protein_coding" "Dusal.0069s00012.1","33202982","Dunaliella sp.","Peptidase ... ","Pantoate-beta-alanine ligase [Interproscan].","protein_coding" "PTI_20G02010.1","No alias","Phaeodactylum tricornutum","Ion ... ","Putative ribosomal-protein-alanine acetyltransferase","protein_coding" "lcl,VRMN01000001.1_cds_KAA8497942.1_6895"," ...
Dive into the research topics of Cloning and characterization of a novel aspartate/glutamate racemase from the acorn worm ... Cloning and characterization of a novel aspartate/glutamate racemase from the acorn worm Saccoglossus kowalevskii. ...
Alanine N0000167835 Alanine Dehydrogenase N0000168101 Alanine Racemase N0000168389 Alanine Transaminase N0000167784 Alanine- ... 27 N0000170401 D-Ala(2),MePhe(4),Met(0)-ol-enkephalin N0000168380 D-Alanine Transaminase N0000167841 D-Amino-Acid Oxidase ... N0000169677 beta Karyopherins N0000170599 beta-Adrenergic Receptor Kinases N0000170224 beta-Alanine N0000168381 beta-Alanine- ... Leucine-2-Alanine N0000170400 Enkephalin, Methionine N0000170395 Enkephalins N0000006256 Enoxacin N0000006809 Enoxaparin ...
Inhibition of Mycobacterial Alanine Racemase Activity and Growth by Thiadiazolidinones. Lee, Y., S. Mootien, C. Shoen, M. ...
This threshold effect correlated with D-alanine production, was prevented by an alanine racemase inhibitor, and required L- ... Racemase-mediated production of endogenous D-alanine by B. anthracis altered the kinetics for initiation of germination over a ... Racemase-dependent production of D-alanine enhanced survival of B. anthracis during interaction with murine macrophages, ... Not only D-isomers but also L-isomers of many alanine analogues showed inhibitory action on L-alanine-initiated germination. ...
C14.240.400.44 Alanine Racemase D8.586.399.894.200.200 D8.811.399.894.200.200 Alanine Transaminase D8.586.913.477.700.100 ... D8.811.913.477.700.100 Alanine-tRNA Ligase D8.586.464.263.200.50 D8.811.464.263.200.50 Alcaligenes B3.440.400.425.125 B3.440. ... B1.150.900.649.147.802 Racemases and Epimerases D8.586.399.894 D8.811.399.894 Radiation Chimera B1.30.530.750.760 B1.50.530.750 ... D8.811.913.400.450.400.500.100 N-Acetylmuramoyl-L-alanine Amidase D8.586.277.87.30 D8.811.277.87.30 N-Acylneuraminate ...
Racemase, Alanine use Alanine Racemase Racemases use Racemases and Epimerases Racemases and Epimerases ...
Alanine Alanine Dehydrogenase Alanine Racemase Alanine Transaminase Alanine-tRNA Ligase Alarmins Alaska Alaska Natives Albania ... beta-Alanine beta-Alanine-Pyruvate Transaminase beta-Aminoethyl Isothiourea beta-Amylase beta-Arrestin 1 beta-Arrestin 2 beta- ... D-Alanine Transaminase D-Amino-Acid Oxidase D-Aspartate Oxidase D-Aspartic Acid D-Xylulose Reductase Dabigatran Dacarbazine ... Leucine-2-Alanine Enkephalin, Methionine Enkephalins Enophthalmos Enoplida Enoplida Infections Enoxacin Enoxaparin Enoximone ...
... gngm serine racemase,serine racemase,C1422619,ilv1,gngm spam1 wt allele,spam1 wt allele,C1709994,sperm adhesion molecule 1 wt ... gngm alanine--glyoxylate aminotransferase 2,alanine -- glyoxylate aminotransferase 2,C1422631,beta-alaat ii,gngm dhrs7c,dhrs7c, ...
... x RACEMASES x RHODANESE x SATURASE x THIAMINASE x TRANSMETHYLASE x TRIACETASE x TRIACETIC ENZYME x TYRAMINE OXIDASE x URIC ASE ... ALANINE ALASTRIM see SMALLPOX ALBINISM see also VITDLIGO xx PIGMENTATION ALBRIGHTS DISEASE see OSTEITIS FIBROSA ALBUMIN see ... x LACTIC ACID RACEMASE x LEVANSUCRASE X LUCIFERASE x NITRILASE X OXYNITRILASE x PICTOCINASE x PROINVASINS x PYOCYANASE ... RACEMASES see ENZYMES RACHITIS see RICKETS RADIATION COUNTERS x GEIGER-MUELLER COUNTER X SCINTILLATION COUNTER RADIATION ...
... gngm serine racemase,serine racemase,C1422619,ilv1,gngm spam1 wt allele,spam1 wt allele,C1709994,sperm adhesion molecule 1 wt ... gngm alanine--glyoxylate aminotransferase 2,alanine -- glyoxylate aminotransferase 2,C1422631,beta-alaat ii,gngm dhrs7c,dhrs7c, ...
Transports both taurine and beta-alanine which requires sodium ions. Chloride ions are necessary for optimal uptake (By ... 036948 13.43 alpha-methylacyl-CoA racemase Amacr Rattus norvegicus " Racemization of 2-methyl-branched fatty acid CoA esters. ... Can also convert delta-aminovalerate and beta-alanine. " P50554.3 ... Converts N-carbamyl-beta-aminoisobutyric acid and N-carbamyl-beta-alanine to, respectively, beta-aminoisobutyric acid and beta- ...
  • Bacterial species with two genes for alanine racemase have one that is continually expressed and one that is inducible, which makes it difficult to target both genes for drug studies. (wikipedia.org)
  • Mutants with in-frame deletion mutations in the genes for alanine dehydrogenase and alanine permease lost the ability to grow on either isomer of alanine, while a mutant with an in-frame deletion mutation in the gene for alanine racemase lost only the ability to grow on D-alanine. (rhea-db.org)
  • The RCCs with haemangioblastoma-like features exhibited a unique immunohistochemical profile, with positive staining for inhibin-α, S100, carbonic-anhydrase-9, keratin7, and high molecular weight keratin and negative staining for (alpha-methylacyl-CoA racemase) AMACR. (bvsalud.org)
  • audit_author.name 'Goto, M.' _audit_author.pdbx_ordinal 1 # _citation.id primary _citation.title 'Crystal structure of a homolog of mammalian serine racemase from Schizosaccharomyces pombe' _citation.journal_abbrev J.Biol.Chem. (rcsb.org)
  • The N-terminal domain is also found in the PROSC (proline synthetase co-transcribed bacterial homolog) family of proteins, which are not known to have alanine racemase activity. (wikipedia.org)
  • It interferes with an early step in bacterial cell wall synthesis in the cytoplasm by competitive inhibition of two enzymes, L-alanine racemase, which forms D-alanine from L-alanine, and D-alanylalanine synthetase, which incorporates D-alanine into the pentapeptide necessary for peptidoglycan formation and bacterial cell wall synthesis. (pediatriconcall.com)
  • N-acetylmuramoyl-L-alanine amidase [Interproscan]. (ntu.edu.sg)
  • Alanine racemase, N-terminal [Interproscan]. (ntu.edu.sg)
  • We queried electronic medical records of children ≤16 years of age with alanine or aspartate aminotransferase levels of >500 IU. (bvsalud.org)
  • This enzyme participates in alanine and aspartate metabolism and D-alanine metabolism. (wikipedia.org)
  • Bacteria can have one (alr gene) or two alanine racemase genes. (wikipedia.org)
  • However, knockout studies have shown that without the alr gene being expressed, the bacteria would need an external source of D-alanine in order to survive. (wikipedia.org)
  • The wild-type gene for alanine dehydrogenase, incorporated into the upt site, complemented the alanine dehydrogenase mutation. (rhea-db.org)
  • The D-alanine produced by alanine racemase is used for peptidoglycan biosynthesis. (wikipedia.org)
  • The traditional mechanism attributed to an alanine racemase reaction is that of a two-base mechanism with a PLP-stabilized carbanion intermediate. (wikipedia.org)
  • Markerless mutagenesis in Methanococcus maripaludis demonstrates roles for alanine dehydrogenase, alanine racemase, and alanine permease. (rhea-db.org)
  • To understand how this occurs, we tested the roles of three adjacent genes encoding homologs of alanine dehydrogenase, alanine racemase, and alanine permease. (rhea-db.org)
  • Alanine racemase, for example, catalyzes the conversion of L -alanine into its isomeric (mirror-image) form, D -alanine. (britannica.com)
  • The structure of alanine racemase from Bacillus stearothermophilus (Geobacillus stearothermophilus) was determined by X-ray crystallography to a resolution of 1.9 A. The alanine racemase monomer is composed of two domains, an eight-stranded alpha/beta barrel at the N terminus, and a C-terminal domain essentially composed of beta-strand. (wikipedia.org)
  • Another problem identified was the need for another basic residue to return Lys39 and Tyr265 back to their protonated and unprotonated forms for L-alanine and vice versa for D-alanine. (wikipedia.org)
  • Ni/Co-cyclam modified materials were tested for their ability to immobilise His6-alanine racemase (HT-AlaR). (ul.ie)
  • Among the archaea, Methanococcus maripaludis has the unusual ability to use L- or D-alanine as a nitrogen source. (rhea-db.org)
  • This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. (wikipedia.org)
  • d-boroAla was previously characterized as an inhibitor of bacterial alanine racemase and d-Ala-d-Ala ligase enzymes (Biochemistry, 28, 1989, 3541). (nau.edu)
  • Alanine racemase (Alr), a pyridoxal 5-phosphate (PLP)-dependent enzyme, is an important target for developing fresh antibiotics as it is a key enzyme in bacterial cell wall synthesis [4]. (edrc2013.org)
  • Description: Treponema Pallidum (strain Nichols) D-alanine--D-alanine ligase (ddl), recombinant protein. (develogen.com)
  • Also, as observed in other alanine racemase structures, PLP adopts a conformation that significantly distorts the planarity of the extended conjugated system between the PLP ring and the internal aldimine bond. (nih.gov)
  • A pyridoxal-phosphate protein that reversibly catalyzes the conversion of L-alanine to D-alanine. (nih.gov)
  • Description: Treponema Pallidum (strain Nichols) alanine racemase (alr), recombinant protein. (develogen.com)
  • Analysis of the active site pocket, in the context of other known alanine racemases, allows us to propose the inclusion of conserved residues found at the entrance to the binding pocket as additional targets in ongoing structure-aided drug design efforts. (nih.gov)