Alanine Racemase
Racemases and Epimerases
Alanine
Amino Acid Isomerases
Alanine Dehydrogenase
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.
Geobacillus stearothermophilus
Burkholderia mallei
Stereoisomerism
Pyridoxal Phosphate
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).
Isomerases
Molecular Sequence Data
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.
Amino Acid Sequence
Enterococcus faecalis
Enterococcus
Enterococcus faecium
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)New Classes of Alanine Racemase Inhibitors Identified by High-Throughput Screening Show Antimicrobial Activity against...
Structural insights into the alanine racemase from Enterococcus faecalis<...
Alanine racemase elisa and antibody
Silica-immobilized His(6)-tagged enzyme : Alanine racemase in hydrophobic solvent
Active site of A. baumannii alanine racemase. (a) 2Fo | Open-i
Alanine racemase C-terminal domain-like superfamily
EC 5.1.1.1
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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 \ ...
Alanine
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 ...
Diaminopimelate decarboxylase
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". ...
Ciclosporin
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 ...
Tolypocladium inflatum
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 ...
Mycobacterium leprae
... 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 ...
Pyridoxal phosphate
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 ...
D-threonine aldolase
"Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent ...
Dan T. Major
"A Combined Quantum Mechanical and Molecular Mechanical Study of the Reaction Mechanism and α-Amino Acidity in Alanine Racemase ...
Exosporium
Seven proteins have been identified in washed exosporium: alanine racemase, inosine hydrolase, ExsF, CotY, ExsY, CotB, and a ...
Orientia tsutsugamushi
... alr encodes an enzyme L-alanine racemase, which converts L-alanine to D-alanine in the first step of peptidoglycan synthesis ...
Cycloserine
... 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 ...
List of MeSH codes (D08)
... 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 ...
List of EC numbers (EC 5)
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 ...
Enterococcus faecalis
D-alanine-D-serine ligase, alanine racemase, phosphate acetyltransferase, NADH peroxidase,Phosphopantetheine ... Glutamate racemase, hydroxymethylglutaryl-CoA synthase, diphosphomevalonate decarboxylase, topoisomerase DNA gyrase B, ...
Siminovitchia
... iron-sulphur cluster-binding protein and alanine racemase, which in most cases are exclusively shared by either all or most ...
Aspartate racemase
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 ...
Epimerase and 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-Amino acid
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 ...
D-amino-acid transaminase
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. ...
NMDA receptor
... 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". ...
Vitamin B6
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 ...
List of enzymes
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 ...
Glutamic acid
Examples are as follows: Alanine + α-ketoglutarate ⇌ pyruvate + glutamate Aspartate + α-ketoglutarate ⇌ oxaloacetate + ... which can manufacture it from the l form with the enzyme glutamate racemase) and the liver of mammals. Although they occur ...
Non-proteinogenic amino acids
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 ...
Morpheein
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造句 用"alanine racemase"造句
... or two alanine racemase genes. 2. The traditional mechanism attributed to an alanine racemase reaction is that of a two-base ... alanine racemase的造句和例句: 1. Bacteria can have one ( alr gene ) ... mechanism with a PLP-stabilized carbanion intermediate.点击查看更多alanine racemase的造句... ... Bacteria can have one ( alr gene ) or two alanine racemase genes.. *The traditional mechanism attributed to an alanine racemase
Structural insights into the alanine racemase from Enterococcus faecalis<...
title = "Structural insights into the alanine racemase from Enterococcus faecalis",. abstract = "Alanine racemase (AlaR) is a ... N2 - Alanine racemase (AlaR) is a bacterial enzyme that belongs to the fold-type III group of pyridoxal 5′-phosphate (PLP)- ... AB - Alanine racemase (AlaR) is a bacterial enzyme that belongs to the fold-type III group of pyridoxal 5′-phosphate (PLP)- ... Alanine racemase (AlaR) is a bacterial enzyme that belongs to the fold-type III group of pyridoxal 5′-phosphate (PLP)-dependent ...
A Novel PLP-Dependent Alanine/Serine Racemase From the Hyperthermophilic Archaeon Pyrococcus horikoshii OT-3 - Bioscience and...
A Novel PLP-Dependent Alanine/Serine Racemase From the Hyperthermophilic Archaeon Pyrococcus horikoshii OT-3 ... A Novel PLP-Dependent Alanine/Serine Racemase From the Hyperthermophilic Archaeon Pyrococcus horikoshii OT-3 ... The enzyme was therefore designated Ala/Ser racemase (ASR). Like BAR, ASR was highly stable at high temperatures and over a ... In this study, we detected pyridoxal 5-phosphate (PLP)-dependent amino acid racemase activity in the protein encoded by PH0782 ...
Thermostable Alanine Racemase from Bacillus Stearothermophilus: DNA and Protein Sequence Determination and Secondary Structure...
The alanine racemase gene consists of 1158 base pairs encoding a protein of 386 amino acid residues; the molecular weight of ... The alanine racemase gene consists of 1158 base pairs encoding a protein of 386 amino acid residues; the molecular weight of ... The alanine racemase gene consists of 1158 base pairs encoding a protein of 386 amino acid residues; the molecular weight of ... The alanine racemase gene consists of 1158 base pairs encoding a protein of 386 amino acid residues; the molecular weight of ...
Pyridoxal phosphate - Wikipedia
AlaP (alanine phosphonate) inhibits alanine racemases, but its lack of specificity has prompted further designs of ALR ... alanine aminotransferase family and the alanine racemase family. An example of the evolutionary similarity in the Beta family ... "New classes of alanine racemase inhibitors identified by high-throughput screening show antimicrobial activity against ... liver cysteine desulfhydrase activity disappears and serine and threonine dehydrase and alanine glutamate transaminase ...
Impairment of d-alanine biosynthesis in Mycobacterium smegmatis determines decreased intracellular survival in human...
... a reaction catalysed by d-alanine racemase (Alr). Mycobacterium smegmatis alr insertion mutants are not dependent on d-alanine ... The primary route of d-alanine biosynthesis in eubacteria is the enantiomeric conversion from l-alanine, ... In this study, we demonstrate that the M. smegmatis alr insertion mutant TAM23 can synthesize d-alanine at lower levels than ... d-Alanine supplementation considerably increased TAM23 viability in nutritionally deficient media and within macrophages. These ...
HOMD :: SEQF2617
Display 100 results per page
"sequence id","alias","species","description",...
... "alanine racemase 2 [Ensembl]. Alanine racemase [Interproscan].","protein_coding" "AAL20718","STM1803","Salmonella enterica","D- ... "alanine racemase [Ensembl]. N-terminal domain, C-terminal domain [InterProScan].","protein_coding" "AGT23716","N559_1989"," ... D-alanyl-D-alanine carboxypeptidase [Interproscan].","protein_coding" "AAC73941","potF","Escherichia coli","putrescine ABC ... ","D-alanine/D-serine/glycine transport protein [Ensembl]. Amino acid permease/ SLC12A domain [InterProScan].","protein_coding ...
Difference between revisions of "Methanococcus maripaludis" - microbewiki
New TB Drugs Possible With Understanding of an Old Antibiotic
The drug attacks bacteria by inhibiting two separate enzymes (D-alanine racemase and D-alanine--D-alanine ligase) each required ... With the D-alanine racemase enzyme, it is known that the drug forms a molecular bond with a chemical group required for the ... The researchers have observed, for the first time, how D-cycloserine inhibits the D-alanine-D-alanine ligase enzyme. ... we see that D-cycloserine binds to the D-alanine-D-alanine ligase enzyme and becomes chemically modified on the enzyme. The ...
15+ Isomerase Enzyme Example: Detailed Facts - Lambda Geeks
7. Alanine racemase. An alanine racemase is a catalyzing enzyme for a chemical process. This enzyme is a member of the ... Methionine racemase. An isomerase enzyme called methionine racemase stimulates the chemical change. Pyridoxal phosphate is the ... Maleate isomerase, also known as maleate cis-trans isomerase, is a bacterial member of the Glu racemase superfamily. It is a ... isomerase family, particularly racemases and epimerases that operate on amino acids and other derivatives. ...
New tuberculosis drugs possible with understanding of old antibiotic
The drug attacks bacteria by inhibiting two separate enzymes (D-alanine racemase and D-alanine-D-alanine ligase) each required ... With the D-alanine racemase enzyme, it is known that the drug forms a molecular bond with a chemical group required for the ... "In this new discovery, we see that D-cycloserine binds to the D-alanine-D-alanine ligase enzyme and becomes chemically modified ... The researchers have observed, for the first time, how D-cycloserine inhibits the D-alanine-D-alanine ligase enzyme. ...
Team:Bielefeld-Germany/Datapage - 2013.igem.org
Alanine racemase (alr) under the control of the Ptac promoter: Testing part for the complementation of the alanine racemase ( ... Alanine racemase from E. coli: Catalyzes the reversible isomerization from L-alanine into the enatiomer D-alanine. In an D- ... bbpart,BBa_K1172903,/bbpart, - Alanine racemase (alr) with double terminator: Cloning intermediate of the construction of the ... bbpart,BBa_K1172909,/bbpart, - Biosafety System araCtive: Biosafety System taking advantage of the alanine racemase and the ...
DeCS
Code System Concept
Andres S
HOMD :: SEQF1173
B6db sequences : edt66487
Thermus thermophilus HB8 Whole Cell Project Database -Target List
English-Armenian Medical - Terms starting with 'L' - MEDINDEX.AM
"sequence id","alias","species","description",...
Alanine racemase [Interproscan].","protein_coding" "AAC76001","nupG","Escherichia coli","nucleoside transporter [Ensembl]. ... ","1,6-anhydro-N-acetylmuramyl-L-alanine amidase, Zn-dependent; murein amidase [Ensembl]. N-acetylmuramoyl-L-alanine amidase [ ... ","D-alanyl-D-alanine endopeptidase [Ensembl]. D-alanyl-D-alanine carboxypeptidase [Interproscan].","protein_coding" "AAC75204 ... D-alanyl-D-alanine carboxypeptidase [Interproscan].","protein_coding" "CCL18922","argH","Clostridioides difficile"," ...
Nucleoid (470)
Network Portal - Gene BC2583
NWMN RS07380 - AureoWiki
Pesquisa | Portal Regional da BVS
... maritima has neither alanine racemase nor glutamate racemase enzymes; hence, the precise biosynthetic pathways of d-alanine and ... We previously identified a lysine racemase involved in d-lysine biosynthesis, and this enzyme also possesses alanine racemase ... Alanina Racemase , Aminoácidos , Alanina/genética , Alanina/metabolismo , Alanina Racemase/metabolismo , Aminoácidos/ ... TM0831 is a novel d-amino acid aminotransferase with racemase activity that is involved in the production of d-amino acids in T ...
DeCS 2017 - December 21, 2017 version
Cycloserine: Uses, Interactions, Mechanism of Action | DrugBank Online
L-alanine racemase, which forms D-alanine from L-alanine, and D-alanylalanine synthetase, which incorporates D-alanine into the ... Catalyzes the interconversion of L-alanine and D-alanine.. Gene Name. alr. Uniprot ID. Q9L888. Uniprot Name. Alanine racemase. ... Feng Z, Barletta RG: Roles of Mycobacterium smegmatis D-alanine:D-alanine ligase and D-alanine racemase in the mechanisms of ... Gene cloning, characterization, and kinetics of its alanine racemase and D-alanyl-D-alanine ligase, which are target enzymes of ...
Serine racemaseLigaseEnzymesMycobacteriumCarboxypeptidaseEnzymeAmino acidGlutamateProteinReactionBiosynthesisAmidaseInhibitsGenePeptidoglycanStructuralCatalyzesGenesStrainSimilarFindProline racemaseHistidine racemaseBacillusPseudomonasCompoundsArgininePathwayOenococcusNitrogen sourceCharacterizationBacteriaBurkholderiaSubstrateStructuresResiduesSpeciesEssentialActivityFoldStructureSignificant
Serine racemase4
- RESULTS The vanGCar locus contained four genes encoding a carboxypeptidase, a d-alanine:d-serine ligase, a serine transporter and a serine racemase, and was present in the seven C. argentinense studied. (archives-ouvertes.fr)
- A similar enzyme is serine racemase (EC 2.6.1.3). (matteoferla.com)
- There are two types of serine racemase, the eukaryotic and archaeal one, srr encoded, and a bacterial one, vanT encoded. (matteoferla.com)
- This study investigated N-methyl-D-aspartate receptor (NMDAR) antagonist interactions with serine racemase (SR) to obtain potential chronic pain target therapy. (d-aminoacids.com)
Ligase5
- D-cylcoserine phosphate in complex with ADP and magnesium bound at the active site of E. coli D-ala-D-alanine ligase. (infectioncontroltoday.com)
- The drug attacks bacteria by inhibiting two separate enzymes (D-alanine racemase and D-alanine--D-alanine ligase) each required to build and maintain the structural integrity of bacterial cell walls. (infectioncontroltoday.com)
- The researchers have observed, for the first time, how D-cycloserine inhibits the D-alanine-D-alanine ligase enzyme. (infectioncontroltoday.com)
- David Roper, who is professor of biochemistry and structural biology at the University Warwick, commented, 'In this new discovery, we see that D-cycloserine binds to the D-alanine-D-alanine ligase enzyme and becomes chemically modified on the enzyme. (infectioncontroltoday.com)
- In this new discovery, we see that D-cycloserine binds to the D-alanine-D-alanine ligase enzyme and becomes chemically modified on the enzyme . (medicalxpress.com)
Enzymes4
- Alanine racemase (AlaR) is a bacterial enzyme that belongs to the fold-type III group of pyridoxal 5′-phosphate (PLP)-dependent enzymes. (elsevier.com)
- 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. (drugbank.com)
- These proteins are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases, eukaryotic ornithine decarboxylases and diaminopimelate decarboxylases. (umbc.edu)
- These enzymes catalyze the transfer of a particular group from one substrate to another e.g., aspartate amino transferase (AST), alanine aminotransferase (ALT), hexokinase, phosphoglucomutase, hexose- 1-phosphate uridyltransferase, ornithine carbamoyl transferase etc. (amano-enzyme.com)
Mycobacterium2
- Mycobacterium smegmatis alr insertion mutants are not dependent on d -alanine for growth and display a metabolic pattern consistent with an alternative pathway for d -alanine biosynthesis. (microbiologyresearch.org)
- A screening of more than 1,500 drug-resistant strains of Mycobacterium tuberculosis revealed evolutionary patterns characteristic of positive selection for three alanine racemase (Alr) mutations. (unl.pt)
Carboxypeptidase1
- Penicillin-binding protein 5, D-alanyl-D-alanine carboxypeptidase [Interproscan]. (ntu.edu.sg)
Enzyme9
- The enzyme was therefore designated Ala/Ser racemase (ASR). (tokushima-u.ac.jp)
- With the D-alanine racemase enzyme, it is known that the drug forms a molecular bond with a chemical group required for the enzyme activity, stopping it from working. (infectioncontroltoday.com)
- An alanine racemase is a catalyzing enzyme for a chemical process. (lambdageeks.com)
- This enzyme is a member of the isomerase family, particularly racemases and epimerases that operate on amino acids and other derivatives. (lambdageeks.com)
- Cysteine racemase: an impossible enzyme? (matteoferla.com)
- Cysteine racemase is an enzyme (EC 5.1.1.10) that was characterised in lysates long ago, but have never been found since. (matteoferla.com)
- The alanine racemase inhibitor β-chloroalanine works thanks to the fact that the enzyme tries to racemise it, but instead quickly eliminates it and the PLP π-stacking tyrosine (eventually) gets alkylated (=electrophilic aromatic substitution). (matteoferla.com)
- Broad spectrum racemases, such as the one encoded by bsrV in Vibrio , also can racemise cysteine and this is the strongest proof that the enzyme activity is actually possible. (matteoferla.com)
- In fact, the origins of the word "Enzyme" derive from Greek: "en" (in) and "zyme" (ferment). (amano-enzyme.com)
Amino acid4
- We recently identified and characterized a novel broad substrate specificity amino acid racemase (BAR) from the hyperthermophilic archaeon Pyrococcus horikoshii OT-3. (tokushima-u.ac.jp)
- In this study, we detected pyridoxal 5'-phosphate (PLP)-dependent amino acid racemase activity in the protein encoded by PH0782. (tokushima-u.ac.jp)
- Cycloserine is an analog of the amino acid D-alanine. (drugbank.com)
- It is an analogue of D-alanine amino acid. (pharmasyntez.com)
Glutamate2
- X-ray diffraction data for the Crystal structure of glutamate racemase from Francisella tularensis subsp. (proteindiffraction.org)
- In this reaction the amino group from alanine is transferred to α -ketoglutarate to form glutamate. (brainkart.com)
Protein2
- Biosafety System taking advantage of the alanine racemase and the tight repression of the arabinose promoter P araBAD by the AraC protein. (igem.org)
- A pyridoxal-phosphate protein that reversibly catalyzes the conversion of L-alanine to D-alanine. (bvsalud.org)
Reaction3
- The traditional mechanism attributed to an alanine racemase reaction is that of a two-base mechanism with a PLP-stabilized carbanion intermediate. (ichacha.net)
- The primary route of d -alanine biosynthesis in eubacteria is the enantiomeric conversion from l -alanine, a reaction catalysed by d -alanine racemase (Alr). (microbiologyresearch.org)
- No enzymatic steps are represented because L-alanine is a single transamination reaction away from pyruvate, which is a central metabolic intermediate. (lbl.gov)
Biosynthesis1
- AlaR catalyzes the interconversion between l- and d-alanine, which is important for peptidoglycan biosynthesis. (elsevier.com)
Amidase2
- N-acetylmuramoyl-L-alanine amidase [Interproscan]. (ntu.edu.sg)
- X-ray diffraction data for the 2.15 Angstrom Crystal Structure of N-acetylmuramoyl-L-alanine Amidase from Staphylococcus aureus. (proteindiffraction.org)
Inhibits1
- It competitively inhibits activity of alanine racemase converting L-alanine into D-alanine and D-alanine syntase which incorporates D-alanine into the pentapeptide necessary for peptidoglycan formation and bacterial cell wall synthesis. (pharmasyntez.com)
Gene2
- Bacteria can have one ( alr gene ) or two alanine racemase genes. (ichacha.net)
- The nucleotide sequence of the alanine racemase (EC 5.1.1.1) gene from a thermophile, Bacillus stearothermophilus, was determined by the dideoxy chain termination method with universal and synthetic site-specific primers. (elsevier.com)
Peptidoglycan2
- d -Alanine is a structural component of mycobacterial peptidoglycan. (microbiologyresearch.org)
- Peptidoglycan precursors may contain D-lactate as the C-terminal D-alanine residue of the muramyl pentapeptide is replaced by D-lactate, known as a pentadepsipeptide. (biomedcentral.com)
Structural1
- Our results provide structural insights into AlaR that may be used for the development of new antibiotics targeting the alanine racemase in pathogenic bacteria. (elsevier.com)
Catalyzes1
- Catalyzes the reversible isomerization from L-alanine into the enatiomer D-alanine. (igem.org)
Genes1
- 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. (ichacha.net)
Strain2
- In this study, we demonstrate that the M. smegmatis alr insertion mutant TAM23 can synthesize d -alanine at lower levels than the parental strain. (microbiologyresearch.org)
- In an D-alanine auxotrophic strain it can be used as a antibiotic free selection marker. (igem.org)
Similar1
- Although the residues common inthe four racemases are not continuously arrayed, these constitute distinct domains and theirhydropathy profiles are very similar. (elsevier.com)
Find1
- It's difficult to find alanine racemase in a sentence. (ichacha.net)
Proline racemase1
- In pathway II, proline racemase (prdF) forms D-proline, and a reductase forms 5-aminovalerate. (lbl.gov)
Histidine racemase2
Bacillus1
- The domain makeup of each monomer is similar to that of Bacillus and Pseudomonas alanine racemases and includes both an alpha/beta-barrel at the N-terminus and a C-terminus primarily made of beta-strands. (nih.gov)
Pseudomonas1
- Arginine racemase of Pseudomonas graveolens. (unipr.it)
Compounds1
- Chemical derivatization of the lead resulted in compounds NR-1213 AND NR-1124 as the potent M. tuberculosis glutamate racemase inhibitors with IC50 of 4-5µM which are remarkable and were found to be non-cytotoxic. (waset.org)
Arginine1
- Can also use arginine and ornithine, but not alanine. (uniprot.org)
Pathway1
- 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. (omicsdi.org)
Oenococcus1
- When comparing the 3D structure of Lm-HisR with those of racemases from Geobacillus stearothermophilus and Oenococcus oeni, Met315 was completely conserved, but Val357 was not. (unipr.it)
Nitrogen source1
- Saccharomyces cerevisiae differs markedly from S. pombe: S. cerevisiae uses L-alanine but not D-alanine as a sole nitrogen source. (omicsdi.org)
Characterization1
- Functional characterization of alanine racemase from Schizosaccharomyces pombe: a eucaryotic counterpart to bacterial alanine racemase. (omicsdi.org)
Bacteria2
- Comparison of AlrAba with alanine racemases from closely related bacteria demonstrates a conserved overall fold. (omicsdi.org)
- Phylogenetic analysis of Lm-HisR showed that Lm-HisR was located far from the cluster of alanine racemases reported thus far and only in lactic acid bacteria of the genus Leuconostoc. (unipr.it)
Burkholderia1
- Alanine racemase mutants of Burkholderia pseudomallei and Burkholderia mallei and use of alanine racemase as a non-antibiotic-based selectable marker. (ucdenver.edu)
Substrate1
- Based on the structural analysis, comparison with alanine racemase, and docking simulation, three significant residues, Phe44, His286, and Val357, were identified that may control the substrate specificity of Lm-HisR. (unipr.it)
Structures1
- 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)
Residues1
- 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)
Species1
- Binding of both alanine enantiomers leads to the appearance of an external aldimine absorbing at 429 nm and of a band absorbing at 498 nm, indicative of a quinonoid species. (omicsdi.org)
Essential1
- As D-alanine is an essential component of the bacterial cell wall, its inhibition is lethal to prokaryotes, making it an excellent antibiotic drug target. (omicsdi.org)
Activity3
- Treponema denticola cystalysin exhibits significant alanine racemase activity accompanied by transamination: mechanistic implications. (omicsdi.org)
- During the reaction of cystalysin with L- or D-alanine, a time-dependent loss of beta-elimination activity occurs concomitantly with the conversion of the pyridoxal 5'-phosphate (PLP) coenzyme into pyridoxamine 5'-phosphate (PMP). (omicsdi.org)
- Lm-HisR showed amino acid racemase activity on histidine specifically. (unipr.it)
Fold1
- The catalytic efficiency of the half-transamination of L-alanine is found to be 5.3x10(-5) mM(-1) x s(-1), 5-fold higher when compared with that of D-alanine. (omicsdi.org)
Structure1
- The structure of alanine racemase from Acinetobacter baumannii. (omicsdi.org)
Significant1
- In addition, two significant differences were observed between Lm-HisR and G. stearothermophilus alanine racemase. (unipr.it)