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Information on EC 5.1.1.1 - alanine racemase and Organism(s) Bacillus subtilis and UniProt Accession P10725
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5.1.1.1 alanine racemaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 5.1.1.1
- pyridoxal
- 5'-phosphate
- peptidoglycan
-
racemization
- d-cycloserine
- stearothermophilus
-
plp-dependent
-
d-amino
-
aldimine
- d-alanyl-d-alanine
- exosporium
-
pyridoxal-5'-phosphate-dependent
- drug development
-
5'-phosphate-dependent
-
d-alanine:d-alanine
- medicine
- biotechnology
- pharmacology
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
alanine racemase, alr-2, d-alanine racemase, alrbax, mbalr2, alrtt, alraba, cdalr, l-alanine racemase, alr2 racemase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-Alanine racemase
-
-
-
-
L-Alanine:D-alanine racemase
-
-
-
-
Racemase, alanine
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-alanine = D-alanine
the active site of the alanine racemase reacts asymmetrically with the enantiomers of the substrate and has a conformation which greatly favors the D-enantiomer
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
racemization
racemization
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
alanine racemase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
9024-06-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
exchange of the alpha-hydrogen of D-Ala and L-Ala with D2O
-
-
?
L-alanine
D-alanine
-
alanine racemase can discriminate effectively between L-alanine and L-2-aminobutyric acid, and selectively and reversibly catalyzes L-alanine to D-alanine transformation Therefore, the enzyme shows ability of eliminating L-Ala from the reaction mixtures of L-2-aminobutyric acid biosynthesis, method optimization and evaluation in a coupled reaction with D-amino acid oxidase converting D-alanine to pyruvate stereoselectively, overview
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate binds to Lys of the enzyme protein and forms an aldimine Schiff base. The alpha-proton of the substrate is then abstracted, and the pyridoxal 5'-phosphate carbanion is generated
pyridoxal 5'-phosphate
-
stabilizes anionic intermediate after abstraction of alpha-hydrogen of the substrate amino acid by forming a quinoid intermediate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
beta-Chloro-D-alanine
BCDA, its primary target is glutamate racemase, poor activity oagainst alanine racemase activity, potent antituberculosis activity. BCDA does not inhibit the D-alanine pathway in intact cells, consistent with its poor in vitro activity, it is instead an irreversible mechanism-based inactivator of glutamate racemase (MurI), an upstream enzyme in the same early stage of peptidoglycan biosynthesis. Inhibition kinetics, overview. Glutamate racemase (MurI) is a pyridoxal 5'-phosphate-independent racemase and is therefore unable to undergo the same mechanism of inhibition as Alr with BCDA
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.5
dal, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
10 - 10.5
yncD, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5 - 11
pH 8.5: 35% of max. activity, pH 11: 8% of max. activity, dal, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
8.5 - 11
pH 8.5: 42% of max. activity, pH 11: 58% of max. activity, yncD, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
dal, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
37
55
yncD, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
30°C and 60°C: approx. 20% of max. activity, dal, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
30 - 70
30°C: approx. 25% of max. activity, 70°C: approx. 8% of max. activity, yncD, extracts are assayed (in triplicate) by monitoring NADH production in spectrophotometric assay with L-alanine dehydrogenase
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43650
precided weight from primary sequence of 394 amino acids, yncD
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression in D-Alanine auxotrophic Escherichia coli strains MB2159 and DN1686, a D-Ala auxotrophic mutant
gene alr, recombinant His-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression in D-Alanine auxotrophic Escherichia coli strain MB2159 and DN1686, a D-Ala auxotrophic mutant
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Babu, U.M.; Johnston, R.B.
D2O-alanine exchange reactions catalyzed by alanine racemase and glutamic pyruvic transaminase
Biochem. Biophys. Res. Commun.
58
460-466
1974
Bacillus subtilis
Henderson, L.L.; Johnson, R.B.
Inhibition studies of the enantiomers of beta-chloroalanine on purified alanine racemase from Bacillus subtilis
Biochem. Biophys. Res. Commun.
68
793-798
1976
Bacillus subtilis
Tanizawa, K.; Ohshima, A.; Scheidegger, A.; Inagaki, K.; Tanaka, H.; Soda, K.
Thermostable alanine racemase from Bacillus stearothermophilus: DNA and protein sequence determination and secondary structure prediction
Biochemistry
27
1311-1316
1988
Geobacillus stearothermophilus, Bacillus subtilis, Salmonella enterica subsp. enterica serovar Typhimurium
Yoshimura, T.; Esaki, N.; Soda, K.
Structure and function of alanine racemase
Bull. Inst. Chem. Res. Kyoto Univ.
70
378-384
1992
Geobacillus stearothermophilus, Bacillus subtilis, Enterococcus faecalis, Pseudomonas putida, Salmonella enterica subsp. enterica serovar Typhimurium
-
Yoshimura, T.; Goto, M.
D-amino acids in the brain: structure and function of pyridoxal phosphate-dependent amino acid racemases
FEBS J.
275
3527-3537
2008
Bacillus subtilis, Bipolaris zeicola, Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Tolypocladium inflatum, Geobacillus stearothermophilus (P10724)
Pierce, K.J.; Salifu, S.P.; Tangney, M.
Gene cloning and characterization of a second alanine racemase from Bacillus subtilis encoded by yncD
FEMS Microbiol. Lett.
283
69-74
2009
no activity in Bacillus subtilis, Bacillus subtilis (P10725), Bacillus subtilis (P94494), Bacillus subtilis, Bacillus subtilis 168 (P10725), Bacillus subtilis 168 (P94494), no activity in Bacillus subtilis DN1686
Zhu, L.; Tao, R.; Wang, Y.; Jiang, Y.; Lin, X.; Yang, Y.; Zheng, H.; Jiang, W.; Yang, S.
Removal of L-alanine from the production of L-2-aminobutyric acid by introduction of alanine racemase and D-amino acid oxidase
Appl. Microbiol. Biotechnol.
90
903-910
2011
Bacillus subtilis
Prosser, G.A.; Rodenburg, A.; Khoury, H.; de Chiara, C.; Howell, S.; Snijders, A.P.; de Carvalho, L.P.
Glutamate racemase is the primary target of beta-chloro-D-alanine in Mycobacterium tuberculosis
Antimicrob. Agents Chemother.
60
6091-6099
2016
Bacillus subtilis (P94556), Mycobacterium tuberculosis (P9WPW9), Mycobacterium tuberculosis, Bacillus subtilis 168 (P94556), Mycobacterium tuberculosis ATCC 25618 / H37Rv (P9WPW9)
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