5.1.1.1: alanine racemase
This is an abbreviated version!
For detailed information about alanine racemase, go to the full flat file.
Word Map on EC 5.1.1.1
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5.1.1.1
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pyridoxal
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5'-phosphate
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peptidoglycan
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racemization
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d-cycloserine
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stearothermophilus
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plp-dependent
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d-amino
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aldimine
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d-alanyl-d-alanine
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exosporium
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pyridoxal-5'-phosphate-dependent
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drug development
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5'-phosphate-dependent
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d-alanine:d-alanine
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medicine
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biotechnology
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pharmacology
- 5.1.1.1
- pyridoxal
- 5'-phosphate
- peptidoglycan
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racemization
- d-cycloserine
- stearothermophilus
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plp-dependent
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d-amino
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aldimine
- d-alanyl-d-alanine
- exosporium
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pyridoxal-5'-phosphate-dependent
- drug development
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5'-phosphate-dependent
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d-alanine:d-alanine
- medicine
- biotechnology
- pharmacology
Reaction
Synonyms
1SFT, AAR, alanine racemase, AlaR, ALR, alr-2, ALR1, ALR2, Alr2 racemase, AlrA, AlrAba, AlrBax, AlrMtb, alrTt, ARL, BA0252, BAS0238, CBL/ALR, CdAlr, cystathionine beta-lyase, D-alanine racemase, DadB, DadX, dadXOF4, dal1, EcAlr, EcCBL, EfAlaR, L-Alanine racemase, L-Alanine:D-alanine racemase, MBalr1, MBAlr2, MetC, More, MurI, OEOE_1641, PDB, Racemase, alanine, tAlaRac, TmCBL, wMelCBL
ECTree
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General Information
General Information on EC 5.1.1.1 - alanine racemase
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evolution
malfunction
metabolism
physiological function
additional information
alanine racemase belongs to the fold-type III group of pyridoxal 5'-phosphate-dependent enzymes
evolution
alanine racemase belongs to the fold-type III group of pyridoxal 5'-phosphate-dependent enzymes
evolution
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the enzyme shows evolutionary and structural similarity to the promiscuous enzymes serine hydroxymethyltransferase, EC 2.1.2.1, and threonine aldolase, EC 4.1.2.48. The three enzymes represent a model of divergent evolution from an ancestral enzyme that was able to catalyse all the reactions of the modern enzymes. Similarly to serine hydroxymethyltransferase and threonine aldolase, Tolypocladium inflatum alanine racemase is able to catalyse retroaldol cleavage and transamination reactions
evolution
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alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
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alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
-
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme
evolution
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme. Pseudomonas aeruginosa has two isozymes, encoded by the Alr and the DadB genes
evolution
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alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme. The genome sequences of methanogenic archaeon, Methanococcus maripaludis reveals the presence of alanine dehydrogenase gene adjacent to genes for alanine racemase and alanine permease, apparently acquired from bacteria
evolution
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alanine racemase is a fold type III pyridoxal-5'-phosphate-dependent amino acid racemase enzyme
evolution
in bacteria, two types of alanine racemase are encoded independently by two genes named dadX and alr. The dadX gene encodes a catabolic alanine racemase DadX, which catalyzes direct conversion of L-Ala to D-Ala. Its expression is induced by L- or D-Ala. The alr gene encodes an anabolic alanine racemase Alr, it is expressed constitutively at low level and essential for providing abundant D-Ala for peptidoglycan biosynthesis. Some bacteria only contain one type alanine racemase gene, whereas others have two of them. Thermoanaerobacter tengcongensis strain MB4 contains two annotated alanine racemase genes MBalr1 and MBalr2. Both genes encode 388 amino acids long alanine racemase, sharing a 58.3% amino acid sequence identity. Compared with MBAlr2, MBAlr1 shows very low catalytic efficiency and limited substrate spectrum. It is probable that MBAlr1 serves as an anabolic and MBAlr2 as the catabolic alanine racemase in Thermoanaerobacter tengcongensis strain MB4
evolution
the enzyme belongs to the Fold Type III of pyridoxal 5'-phosphate-dependent enzymes
evolution
two kinds of Alr have been identified in bacteria: the alr-encoded racemase, which is constitutive and used for D-Ala biosynthesis, and the dadX-encoded racemase, which is inducible and used for the catabolism of D-Ala
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
evolution
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
-
evolution
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
-
evolution
Streptococcus mutans serotype c ATCC 700610 / UA159
-
two kinds of Alr have been identified in bacteria: the alr-encoded racemase, which is constitutive and used for D-Ala biosynthesis, and the dadX-encoded racemase, which is inducible and used for the catabolism of D-Ala
-
evolution
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
-
evolution
Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145
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the enzyme belongs to the Fold Type III of pyridoxal 5'-phosphate-dependent enzymes
-
evolution
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
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alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme. Pseudomonas aeruginosa has two isozymes, encoded by the Alr and the DadB genes
-
evolution
-
alanine racemase belongs to the fold-type III group of pyridoxal 5'-phosphate-dependent enzymes
-
evolution
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
-
evolution
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
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during log phase growth without D-alanine, the viable counts of alanine racemase-deficient mutants of Burkholderia pseudomallei decrease within 2 h by about 1000fold, and no viable bacteria are present at 24 h. The alanine racemase-deficient mutant of Burkholderia pseudomallei K96243 exhibits attenuation versus its isogenic parental strain with respect to growth and survival in murine peritoneal macrophages
malfunction
during log phase growth without D-alanine, the viable counts of alanine racemase-deficient mutants of Burkholderia pseudomallei decrease within 2 h by about 10fold, and no viable bacteria are present at 24 h
malfunction
because D-alanine is an essential component of the bacterial cell-wall peptidoglycan, inhibition of alanine racemase is lethal to prokaryotes
malfunction
depletion of D-alanine results in rapid loss of viability. The alr mutant is defective for growth in macrophages
malfunction
depletion of alr in Streptococcus mutans significantly compromises its competitiveness with other co-residents, e.g. Streptococcus sanguinis, in the oral biofilm. D-Ala starvation causes cell morphology alterations of the alr mutant
malfunction
Alkalihalophilus pseudofirmus
enzyme Alr inhibition is lethal to prokaryotes
malfunction
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growth of the Alr mutant on a mixture of D- and L-alanine is compromised
malfunction
lack of expression of the alr gene is lethal when there is no addition of exogenous D-Ala. Upregulated expression of extracellular polysaccharide synthesis-associated genes in the alr-mutant group (genes gtfB, gtfC, and gtfD) according to quantitative RT-PCR expression analysis, and loosened biofilm with fewer cells but more extracellular matrix within the biofilms in the alr mutant. The mutant shows increased extracellular polysaccharide synthesis and decreased acid tolerance. Decreased cariogenicity of alr-mutant strain in rats
malfunction
Mycobacterium smegmatis strains with a deletion of the alr gene require D-Ala for growth, indicating the essential role of Alr in D-Ala production. Gln360 and conformational changes of active site residues disrupt the hydrogen bonding interactions necessary for proper pyridoxal 5'-phosphate immobilization, and decrease both the substrate affinity and turnover number of AlrTt. Introduction of hydrophobic amino acids at Gln360 increase the racemase activity of AlrTt
malfunction
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role of alanine racemase mutations in Mycobacterium tuberculosis D-cycloserine resistance, overview
malfunction
Streptococcus mutans serotype c ATCC 700610 / UA159
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depletion of alr in Streptococcus mutans significantly compromises its competitiveness with other co-residents, e.g. Streptococcus sanguinis, in the oral biofilm. D-Ala starvation causes cell morphology alterations of the alr mutant
-
malfunction
Streptococcus mutans serotype c ATCC 700610 / UA159
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lack of expression of the alr gene is lethal when there is no addition of exogenous D-Ala. Upregulated expression of extracellular polysaccharide synthesis-associated genes in the alr-mutant group (genes gtfB, gtfC, and gtfD) according to quantitative RT-PCR expression analysis, and loosened biofilm with fewer cells but more extracellular matrix within the biofilms in the alr mutant. The mutant shows increased extracellular polysaccharide synthesis and decreased acid tolerance. Decreased cariogenicity of alr-mutant strain in rats
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malfunction
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during log phase growth without D-alanine, the viable counts of alanine racemase-deficient mutants of Burkholderia pseudomallei decrease within 2 h by about 10fold, and no viable bacteria are present at 24 h
-
malfunction
Alkalihalophilus pseudofirmus OF4
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enzyme Alr inhibition is lethal to prokaryotes
-
malfunction
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depletion of D-alanine results in rapid loss of viability. The alr mutant is defective for growth in macrophages
-
malfunction
-
during log phase growth without D-alanine, the viable counts of alanine racemase-deficient mutants of Burkholderia pseudomallei decrease within 2 h by about 1000fold, and no viable bacteria are present at 24 h. The alanine racemase-deficient mutant of Burkholderia pseudomallei K96243 exhibits attenuation versus its isogenic parental strain with respect to growth and survival in murine peritoneal macrophages
-
malfunction
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because D-alanine is an essential component of the bacterial cell-wall peptidoglycan, inhibition of alanine racemase is lethal to prokaryotes
-
biosynthesis of D-alanine as building blocks in the peptidoglycan layers of bacterial cell walls
metabolism
DadB expression is induced by L-alanine to a level much greater than that of Alr and is probably responsible for the catabolism of D-Ala. Alr is constitutively expressed and seems to provide the D-alanine necessary to maintain cell growth
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13) which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13) which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
-
DadB expression is induced by L-alanine to a level much greater than that of Alr and is probably responsible for the catabolism of D-Ala. Alr is constitutively expressed and seems to provide the D-alanine necessary to maintain cell growth
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
-
alanine racemase plays an essential role in cell wall synthesis as it racemizes L-alanine into D-alanine, a key building block in the biosynthesis of peptidoglycan
physiological function
-
alanine racemase catalyzes the racemization of L-alanine to D-alanine, which is a key component of the peptidoglycan layer, especially in cross-linking the bacterial cell walls
physiological function
-
involvement of alanine racemase in germination of Bacillus cereus spores lacking an intact exosporium. L-Alanine-mediated germination of food isolated Bacillus cereus DSA 1 spores, which lack an intact exosporium, is increased in the presence of D-cycloserine, an alanine racemase inhibitor, reflecting the activity of the Alr enzyme, capable of converting L-alanine to the germination inhibitor D-alanine, contribution of alanine racemase to the autoinhibition of Bacillus cereus spore germination
physiological function
the enzyme is essential for the organism, it is not possible to generate an alr knockout mutant in the absence of a complementing gene copy or D-alanine in the growth medium
physiological function
-
the pyridoxal 5'-phosphate-dependent enzyme alanine racemase produces the D-alanine incorporated in the cyclic peptide cyclosporine A synthesized by the fungus
physiological function
alanine racemase (Alr) is a bacterial enzyme that catalyses the conversion of L-Ala to D-Ala. This function is critical for the growth of bacteria due to their need for D-alanine, an essential component in the biosynthesis of cell wall peptidoglycan in both gram-positive and gram-negative bacteria2. Two kinds of Alr have been identified in bacteria: the alr-encoded racemase, which is constitutive and used for D-Ala biosynthesis, and the dadX-encoded racemase, which is inducible and used for the catabolism of D-Ala. Enzyme Alr is essential for the growth and interspecies competitiveness of Streptococcus mutans, the major causative organism of dental caries
physiological function
alanine racemase (Alr) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the reversible racemization of L- and D-alanine. D-alanine is an essential component of the bacterial cell-wall peptidoglycan
physiological function
Alkalihalophilus pseudofirmus
alanine racemase (Alr) is a pyridoxal 5'-phosphate-dependent (PLP) enzyme that catalyzes a reversible racemization between the enantiomers of alanine. D-Alanine is an indispensable constituent in the biosynthesis of bacterial cell-wall peptidoglycan
physiological function
alanine racemase (ALR) is responsible for the high D-alanine production in Lactobacillus salivarius
physiological function
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D-alanine, produced by the action of alanine racemase on L-alanine, is important to both Gram-positive and Gram-negative bacteria, since it is required for the synthesis of the peptidoglycan in the cell wall
physiological function
D-alanine, produced by the action of alanine racemase on L-alanine, is important to both Gram-positive and Gram-negative bacteria, since it is required for the synthesis of the peptidoglycan in the cell wall
physiological function
D-alanine, produced by the action of alanine racemase on L-alanine, is important to both Gram-positive and Gram-negative bacteria, since it is required for the synthesis of the peptidoglycan in the cell wall
physiological function
-
in addition to its function in the utilisation of D-alanine, Alr exhibits a role in protecting the system from inhibition by D-alanine
physiological function
in bacteria, two types of alanine racemase are encoded independently by two genes named dadX and alr. The dadX gene encodes a catabolic alanine racemase DadX, which catalyzes direct conversion of L-Ala to D-Ala. Its expression is induced by L- or D-Ala. The alr gene encodes an anabolic alanine racemase Alr, it is expressed constitutively at low level and essential for providing abundant D-Ala for peptidoglycan biosynthesis. The catabolic alanine racemase DadX usually shows much higher catalytic efficiency than the anabolic enzyme Alr. Essential role of Alr in D-Ala production
physiological function
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in the absence of genes coding for alanine racemase Alr and DadX homologues in Chlamydia pneumonia a serine hydroxymethyl transferase GlyA serves as a source of D-Ala. D-alanine, produced by the action of alanine racemase on L-alanine, is important to both Gram-positive and Gram-negative bacteria, since it is required for the synthesis of the peptidoglycan in the cell wall
physiological function
many endospore-forming bacteria embed alanine racemases into their spore coats, and these enzymes are thought to convert the L-alanine germinant into D-alanine, a spore germination inhibitor. Clostridium difficile spores can respond to a diverse set of amino acid co-germinants and Alr2 can accommodate serine as a substrate. L-alanine is a co-germinant, and D-alanine also functions as a co-germinant. L- and D-serine are also co-germinants for Clostridium difficile spores. Only the L-form of alanine can trigger spore germination when added with taurocholic acid. Gene alr2 is dispensable for germination in response to L-alanine but essential for germination in response to D-alanine
physiological function
the conversion of L-alanine (L-Ala) into D-alanine (D-Ala) in bacteria is performed by pyridoxal 5'-phosphate-dependent enzymes, alanine racemases. D-Ala is an essential component of the bacterial peptidoglycan and hence required for survival
physiological function
the enzyme catalyzes the interconversion of L-alanine to D-alanine. D-Alanine is an essential building block of the cell wall of both gram-positive and gram-negative bacteria
physiological function
the enzyme is an essential factor to maintain the growth and cell wall integrity of Streptococcus mutans
physiological function
the enzyme is responsible for racemization between enantiomers of alanine, D-alanine is an essential component of the bacterial cell wall
physiological function
Streptococcus mutans serotype c ATCC 700610 / UA159
-
the enzyme is an essential factor to maintain the growth and cell wall integrity of Streptococcus mutans
-
physiological function
Streptococcus mutans serotype c ATCC 700610 / UA159
-
alanine racemase (Alr) is a bacterial enzyme that catalyses the conversion of L-Ala to D-Ala. This function is critical for the growth of bacteria due to their need for D-alanine, an essential component in the biosynthesis of cell wall peptidoglycan in both gram-positive and gram-negative bacteria2. Two kinds of Alr have been identified in bacteria: the alr-encoded racemase, which is constitutive and used for D-Ala biosynthesis, and the dadX-encoded racemase, which is inducible and used for the catabolism of D-Ala. Enzyme Alr is essential for the growth and interspecies competitiveness of Streptococcus mutans, the major causative organism of dental caries
-
physiological function
-
alanine racemase (ALR) is responsible for the high D-alanine production in Lactobacillus salivarius
-
physiological function
Alkalihalophilus pseudofirmus OF4
-
alanine racemase (Alr) is a pyridoxal 5'-phosphate-dependent (PLP) enzyme that catalyzes a reversible racemization between the enantiomers of alanine. D-Alanine is an indispensable constituent in the biosynthesis of bacterial cell-wall peptidoglycan
-
physiological function
-
many endospore-forming bacteria embed alanine racemases into their spore coats, and these enzymes are thought to convert the L-alanine germinant into D-alanine, a spore germination inhibitor. Clostridium difficile spores can respond to a diverse set of amino acid co-germinants and Alr2 can accommodate serine as a substrate. L-alanine is a co-germinant, and D-alanine also functions as a co-germinant. L- and D-serine are also co-germinants for Clostridium difficile spores. Only the L-form of alanine can trigger spore germination when added with taurocholic acid. Gene alr2 is dispensable for germination in response to L-alanine but essential for germination in response to D-alanine
-
physiological function
-
alanine racemase (Alr) is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the reversible racemization of L- and D-alanine. D-alanine is an essential component of the bacterial cell-wall peptidoglycan
-
physiological function
Aeromonas hydrophila subsp. hydrophila HBNUAh01 / ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
-
the enzyme catalyzes the interconversion of L-alanine to D-alanine. D-Alanine is an essential building block of the cell wall of both gram-positive and gram-negative bacteria
-
physiological function
-
alanine racemase catalyzes the racemization of L-alanine to D-alanine, which is a key component of the peptidoglycan layer, especially in cross-linking the bacterial cell walls
-
physiological function
-
involvement of alanine racemase in germination of Bacillus cereus spores lacking an intact exosporium. L-Alanine-mediated germination of food isolated Bacillus cereus DSA 1 spores, which lack an intact exosporium, is increased in the presence of D-cycloserine, an alanine racemase inhibitor, reflecting the activity of the Alr enzyme, capable of converting L-alanine to the germination inhibitor D-alanine, contribution of alanine racemase to the autoinhibition of Bacillus cereus spore germination
-
physiological function
Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145
-
the conversion of L-alanine (L-Ala) into D-alanine (D-Ala) in bacteria is performed by pyridoxal 5'-phosphate-dependent enzymes, alanine racemases. D-Ala is an essential component of the bacterial peptidoglycan and hence required for survival
-
physiological function
-
the enzyme is essential for the organism, it is not possible to generate an alr knockout mutant in the absence of a complementing gene copy or D-alanine in the growth medium
-
physiological function
Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1
-
D-alanine, produced by the action of alanine racemase on L-alanine, is important to both Gram-positive and Gram-negative bacteria, since it is required for the synthesis of the peptidoglycan in the cell wall
-
Alr2 racemase is the sixth most highly expressed gene during Clostridium difficile spore formation
additional information
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Alr2 racemase is the sixth most highly expressed gene during Clostridium difficile spore formation
additional information
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amino acid residues 319 and 364 are located directly in the active site. Y364 is involved in the positioning of the phosphate moiety of PLP and thus represents a prominent active site residue in the conserved inner layer of the substrate entrance corridor of Alr
additional information
analysis of the enzyme structure, active site structure, and intermolecular interactions, structure comparisons, overview. The N-terminal and C-terminal domains of all reported Alr structures are connected by a short hinge region, but the hinge angles between the N- and C-terminal of Alrs vary
additional information
-
analysis of the enzyme structure, active site structure, and intermolecular interactions, structure comparisons, overview. The N-terminal and C-terminal domains of all reported Alr structures are connected by a short hinge region, but the hinge angles between the N- and C-terminal of Alrs vary
additional information
Alkalihalophilus pseudofirmus
enzyme molecular structure analysis. The conserved residues at the substrate entryway and the salt bridge at the dimer interface are critical for enzyme activity
additional information
enzyme structure comparisons, active site structure, overview
additional information
-
enzyme structure comparisons, active site structure, overview
additional information
enzyme structure homology modeling using the crystal structure of Escherichia coli AlaR with PDB ID 2rjh
additional information
Residue Gln360 plays an essential role in substrate selection and has a preference for hydrophobic amino acids, especially Tyr, in bacterial alanine racemization. Enzyme structure determination and analysis, active site structure, detailed overview
additional information
structure-function realtionship analysis, overview
additional information
-
structure-function realtionship analysis, overview
additional information
comparisons of structure and function of CBL and ALR, overview
additional information
-
comparisons of structure and function of CBL and ALR, overview
additional information
Alkalihalophilus pseudofirmus OF4
-
enzyme molecular structure analysis. The conserved residues at the substrate entryway and the salt bridge at the dimer interface are critical for enzyme activity
-
additional information
-
Alr2 racemase is the sixth most highly expressed gene during Clostridium difficile spore formation
-
additional information
-
analysis of the enzyme structure, active site structure, and intermolecular interactions, structure comparisons, overview. The N-terminal and C-terminal domains of all reported Alr structures are connected by a short hinge region, but the hinge angles between the N- and C-terminal of Alrs vary
-
additional information
Aeromonas hydrophila subsp. hydrophila HBNUAh01 / ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
-
enzyme structure homology modeling using the crystal structure of Escherichia coli AlaR with PDB ID 2rjh
-
additional information
Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145
-
structure-function realtionship analysis, overview
-