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Information on EC 5.1.1.1 - alanine racemase and Organism(s) Geobacillus stearothermophilus and UniProt Accession P10724
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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: Geobacillus stearothermophilus
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, ecalr, 
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
consensus water sites at the interface between the two enzyme monomers maintain and stabilize dimer and supply the active site continuously with water molecules to allow rapid equilibration of active site protons
L-alanine = D-alanine
the alanine racemase builds two different bases in the active site. The base for D-Ala may be closer to the enzyme surface, and that for L-Ala inside
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
racemization
racemization
-
-
-
-
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
D-lysine
L-lysine
enzyme mutant I222T/Y354W, no activity with the wild-type enzyme
-
-
?
L-Ala
D-Ala
the enzyme catalyzes the first committed step in bacterial cell wall biosynthesis
-
?
L-lysine
D-lysine
enzyme mutant I222T/Y354W, no activity with the wild-type enzyme
-
-
?
L-Ala
?
-
enzyme provides D-Ala as an essential building block for biosynthesis of the peptidoglycan layer of the cell wall
-
-
?
L-Arg
D-Arg
-
stepwise mechanism for alanine racemase at both 25°C and at 65°C. The carbanionic intermediate is obligatory, and Arg219 may serve to destabilize it to avoid side reactions such as transamination, a detailed reaction mechanism is proposed that includes enzyme and substrate protonation states
-
r
L-alanine
D-alanine
first step in the biosynthesis of the peptidoglycan
-
-
?
L-Ala
D-Ala
-
the enzyme catalyzes transamination as a side function.The pyridoxal form of the enzyme is converted to the pyridoxamine form by incubation with its natural substrate, D-alanine or L-alanine, under acidic conditions: the enzyme loses its racemase activity concomitantly. The pyridoxamine form of the enzyme returns to the pyridoxal form by incubation with pyruvate at alkaline pH
-
r
L-Ala
D-Ala
-
Tyr265 and Lys39 are the catalytic bases removing alpha-hydrogen from L- and D-alanine
-
r
L-alanine
D-alanine
-
The bacterium utilizes D-alanine (DAla) for synthesis of the peptidoglycan cell wall.
-
-
r
additional information
?
-
residues Ile222 and Tyr354 are important for the enzyme substrate specificity
-
-
?
additional information
?
-
-
residues Ile222 and Tyr354 are important for the enzyme substrate specificity
-
-
?
additional information
?
-
-
the enzyme catalyzes transamination as side reaction, R-isomer preference in the hydrogen abstraction from pyridoxamine 5'-phosphate
-
?
additional information
?
-
-
the epsilon-amino group of Lys39 participates in both racemization and transamination when catalyzed by the wild-type enzyme
-
?
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
L-Ala
D-Ala
the enzyme catalyzes the first committed step in bacterial cell wall biosynthesis
-
?
L-Ala
?
-
enzyme provides D-Ala as an essential building block for biosynthesis of the peptidoglycan layer of the cell wall
-
-
?
L-alanine
D-alanine
first step in the biosynthesis of the peptidoglycan
-
-
?
L-alanine
D-alanine
-
The bacterium utilizes D-alanine (DAla) for synthesis of the peptidoglycan cell wall.
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
both active sites of the dimer contain a pyridoxal 5'-phosphate molecule in aldimine linkage to Lys39 as a protonated Schiff base. The protonated pyridoxal 5'-phosphate-Lys39 Schiff base is the reactive form of the enzyme
pyridoxal 5'-phosphate
once per 1 million turnovers of racemization a H-atom is added to C4-atom of the substrate moiety of the anionic intermediate instead of the reprotonation of the abstracted hydrogen at C(alpha) resulting in pyridoxamine 5'-phosphate
pyridoxal 5'-phosphate
-
the monomeric inactive enzyme appears to bind the cofactor pyridoxal 5'-phosphate by a non-covalent linkage, although the native dimeric enzyme binds the cofactor through an aldimine Schiff base linkage
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
-
pyridoxal 5'-phosphate dependent enzyme
pyridoxal 5'-phosphate
-
2 mol of pyridoxal 5'-phosphate bound per mol of enzyme dimer
pyridoxal 5'-phosphate
-
Arg219 forms a hydrogen bond with the pyridine nitrogen of the cofactor, Arg136 donates a hydrogen bond to the phenolic oxygen of pyridoxal 5'-phosphate and may be involved in the binding of substrate as well as stabilization of intermediates
pyridoxal 5'-phosphate
-
the pyridoxal form of the enzyme is converted to the pyridoxamine form by incubation with its natural substrate, D-alanine or L-alanine, under acidic conditions: the enzyme loses its racemase activity concomitantly. The pyridoxamine form of the enzyme returns to the pyridoxal form by incubation with pyruvate at alkaline pH
pyridoxal 5'-phosphate
-
PLP, dependent on, enzyme-cofactor complex structure, with inhibitor acetate, PDB ID 1SFT
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(R)-1-aminoethylphosphonic acid
upon formation of the external aldimine the phosphonate group interacts with putative catalytic residues, thereby rendering them unavailable for catalysis
L-Cycloserine
model for inactivation mechanism via geminal diamine and ketimine to isoxazole
acetate
-
enzyme-inhibitor complex structure, with pyridoxyl 5'-phosphate, PDB ID 1SFT
beta,beta,beta-trifluoroalanine
-
nucleophilic attack of Lys38 on the electrophilic beta-difluoro-alpha,beta-unsaturated imine
beta-chloroalanine
-
enantiomers of beta-chloroalanine as Alr inhibitors
D-cycloserine
model for inactivation mechanism via geminal diamine and ketimine to isoxazole
D-cycloserine
-
mechanism of inactivation and comparison with inactivation of Streptomyces lavendulae enzyme
D-cycloserine
-
importance of N2-structural site in cyloserine for bioactivity
L-Cycloserine
-
mechanism of inactivation and comparison with inactivation of Streptomyces lavendulae enzyme
L-Cycloserine
-
importance of N2-structural site in cyloserine for bioactivity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
18
D-Lysine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
32
L-lysine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
additional information
additional information
-
Km values of L-Ala in the presence of urea at various concentrations
-
2.8
D-alanine
pH 8.0, 30°C, recombinant wild-type enzyme
4
D-alanine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
5.1
L-alanine
pH 8.0, 30°C, recombinant wild-type enzyme
8.3
L-alanine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.5
D-Lysine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
4.17
L-lysine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
633
D-alanine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
1017
D-alanine
pH 8.0, 30°C, recombinant wild-type enzyme
1133
L-alanine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
1533
L-alanine
pH 8.0, 30°C, recombinant wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
D-Lysine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
0.13
L-lysine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
158.3
D-alanine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
366.7
D-alanine
pH 8.0, 30°C, recombinant wild-type enzyme
136.7
L-alanine
pH 8.0, 30°C, recombinant mutant I222T/Y354W
300
L-alanine
pH 8.0, 30°C, recombinant wild-type enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5 - 11
-
pH 8.5: about 55% of maximal activity, pH 11.0: about 65% of maximal activity, racemization from L-Ala to D-Ala
9 - 11
-
pH 9: about 50% of maximal activity, pH 11.0: about 35% of maximal activity, racemization from D-Ala to L-Ala
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
evolution
-
alanine racemase is a fold type III pyridoxal-5'-phosphate-dependent amino acid racemase enzyme
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
metabolism
biosynthesis of D-alanine as building blocks in the peptidoglycan layers of bacterial cell walls
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
dimer
homodimer
homodimer
-
the homodimeric enzyme of 388 residues formed by a head-to-tail association of two monomers. Each monomer is composed of two folded domains: (i) an N-terminal domain formed by the portion 1-240 and (ii) a C-terminal domain with the remaining portion of the monomer (241-388). The N-terminal domain consists of an eight-stranded alpha/beta-barrel, while the C-terminal domain is made up of beta-strands. Molecular dynamics study
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop method using purified enzyme concentrated to 22 mg/ml. The hanging drop contains 0.01 ml of the protein solution, 0.01 ml of 23% polyethylene glycol 4K, 200 mM sodium acetate and 100 mM Tris, pH 8.5. Drops are equilibrated against 0.7 ml of polyethylene glycol 4K solution
hanging drop method, determination of the crystal structure of the (R)-1-aminoethylphosphonic acid-pyridoxal 5'-phosphate aldimine in complex with alanine racemase at 1.6 A resolution
hanging drop method, the structure of the enzyme with the inhibitor propionate bound in the active site is determined by X-ray crystallography to a resolution of 1.9 A
study of water molecules by cluster analysis of several crystal structures
enzyme in complex with pyridoxyl 5'-phosphate and inhibitor acetate, PDB ID 1SFT
-
hanging-drop vapor diffusion method. Crystal structure of the enzyme bound with reaction intermediate analogs, N-(5'-phosphopyridoxyl)-L-alanine and N-(5'-phosphopyridoxyl)-D-alanine, determined at 2.0 A resolution with the crystallographic R factor of 17.2 for PLP-L-Ala and 16.9 for PLP-D-Ala complexes
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I222T
site-directed mutagenesis, the mutant is an alanine racemase with lysine racemization activity
I222T/Y354W
site-directed mutagenesis, the double mutant is an alanine racemase with lysine racemization activity
K39A
Lys39 is the catalytic residue required for the abstraction and addition of the alpha-hydrogen of D-alanine, As shown by site-directed mutagenesis (K39A mutant) and chemical rescue studies. Tyr265 is catalytic residue for L-alanine, shown by site-directed mutagenesis (Y265A mutant)
R219E
catalytical active mutant, the catalytic effect in the Arg219Glu mutant enzyme is due to a combined solvent and inherent stabilizing effect of the protonated cofactor, in contrast to the wild-type enzyme where the catalytic effect may be ascribed to solvent effects alone
Y265A
Lys39 is the catalytic residue required for the abstraction and addition of the alpha-hydrogen of D-alanine, As shown by site-directed mutagenesis (K39A mutant) and chemical rescue studies. Tyr265 is catalytic residue for L-alanine, shown by site-directed mutagenesis (Y265A mutant)
Y354W
site-directed mutagenesis, the mutant is an alanine racemase with lysine racemization activity
K39A
-
mutant enzyme is inactive as a catalyst for racemization as well as transamination
additional information
additional information
-
mutant gene which tandemly encodes the two polypeptides of the enzyme subunit, fragment 1 and fragment 2, cleaved at the position corresponding to the predicted hinge region. The mutant fragmentary alanine racemase is active at about 40% of the activity of the wild type enzyme
additional information
-
mutant gene which tandemly encodes the two polypeptides of the enzyme subunit, fragment 1 and fragment 2, cleaved at the position corresponding to the predicted hinge region. The mutant fragmentary alanine racemase is active at about 40% of the activity of the wild type enzyme
additional information
-
mutant gene which tandemly encodes the two polypeptides of the enzyme subunit, fragment 1 and fragment 2, cleaved at the position corresponding to the predicted hinge region. The mutant fragmentary alanine racemase is active at about 40% of the activity of the wild type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
5 min, resistant to incubation with 0.08% SDS, 1 M guanidine hydrochloride, 4 M urea, 45% ethanol or 50% dimethyl sulfoxide
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
5 min, resistant to incubation with 0.08% SDS, 1 M guanidine hydrochloride, 4 M urea, 45% ethanol or 50% dimethyl sulfoxide
-
in 0.6 M to 1.5 M guanidine hydrochloride the dimeric enzyme is dissociated into a monomeric form, which is catalytically inactive
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
ethyl acetate destroyes the enzyme activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene alr, expression of the enzyme in Escherichia coli strain BL21
31-54% sequence homologies with Bacillus subtilis and Salmonella typhimurium dadB and alr enzymes
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
enzyme denatured in 6 M guanidine hydrochloride is renatured either by dialysis or dilution to reduce the guanidine hydrochloride concentration
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
Alr is a target for the development of antibacterial drugs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Walsh, C.T.
Enzymes in the D-alanine branch of bacterial cell wall peptidoglycan assembly
J. Biol. Chem.
264
2393-2396
1989
Geobacillus stearothermophilus, Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium, Staphylococcus sp.
Inagaki, K.; Tanizawa, K.; Badet, B.; Walsh, C.T.; Tanaka, H.; Soda, K.
Thermostable alanine racemase from Bacillus stearothermophilus: molecular cloning of the gene, enzyme purification, and characterization
Biochemistry
25
3268-3274
1986
Geobacillus stearothermophilus
Neidhart, D.J.; Distefano, M.D.; Tanizawa, K.; Soda, K.; Walsh, C.T.; Petsko, G.A.
X-ray crystallographic studies of the alanine-specific racemase from Bacillus stearothermophilus
J. Biol. Chem.
262
15323-15326
1987
Geobacillus stearothermophilus
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
Faraci, W.S.; Walsh, C.T.
Racemization of alanine by the alanine racemase from Salmonella typhimurium and Bacillus stearothermophilus: energetic reaction profiles
Biochemistry
27
3267-3276
1988
Geobacillus stearothermophilus, Salmonella enterica subsp. enterica serovar Typhimurium
Copie, V.; Faraci, W.S.; Walsh, C.T.; Griffin, R.G.
Inhibition of alanine racemase by alanine phosphonate: detection of an imine linkage to pyridoxal 5'-phosphate in the enzyme-inhibitor complex by solid-state 15N nuclear magnetic resonance
Biochemistry
27
4966-4970
1988
Geobacillus stearothermophilus
Faraci, W.S.; Walsh, C.T.
Mechanism of inactivation of alanine racemase by beta,beta,beta-trifluoroalanine
Biochemistry
28
431-437
1989
Geobacillus stearothermophilus, Salmonella enterica subsp. enterica serovar Typhimurium
Duncan, K.; Faraci, W.S.; Matteson, D.S.; Walsh, C.T.
(1-Aminoethyl)boronic acid: a novel inhibitor for Bacillus stearothermophilus alanine racemase and Salmonella typhimurium D-alanine:D-alanine ligase (ADP-forming)
Biochemistry
28
3541-3549
1989
Geobacillus stearothermophilus
Toyama, H.; Esaki, N.; Yoshimura, T.; Tanizawa, K.; Soda, K.
Thermostable alanine racemase of Bacillus stearothermophilus: subunit dissociation and unfolding
J. Biochem.
110
279-283
1991
Geobacillus stearothermophilus
Sawada, S.; Tanaka, Y.; Hayashi,S.; Ryu, M.; Hasegawa, T.; Yamamoto, Y.; Esaki, N.; Soda, K.; Takahashi, S.
Kinetics of thermostable alanine racemase of Bacillus stearothermophilus
Biosci. Biotechnol. Biochem.
58
807-811
1994
Geobacillus stearothermophilus
-
Soda, K.; Tanizawa, K.
Thermostable alanine racemase. Its structural stability
Ann. N. Y. Acad. Sci.
585
386-393
1990
Geobacillus stearothermophilus
Soda, K.; Esaki, N.
Pyridoxal enzymes acting on D-amino acids
Pure Appl. Chem.
66
709-714
1994
Geobacillus stearothermophilus, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) YM-1
-
Toyama, H.; Tanizawa, K.; Wakayama, M.; Lee, Q.L.; Yoshimura, T.; Esaki, N.; Soda, K.
Limited proteolysis of thermostable alanine racemase of Bacillus stearothermophilus
Agric. Biol. Chem.
55
2881-2882
1991
Geobacillus stearothermophilus
-
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
-
Okubo, Y.; Tomioka, R.; Yokoigawa, K.; Kawai, H.
Lability of alanine racemase from a psychrotroph
J. Home Econ. Jpn.
46
1135-1140
1995
Geobacillus stearothermophilus, Pseudomonas fluorescens
-
Shaw, J.P.; Petsko, G.A.; Ringe, D.
Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution
Biochemistry
36
1329-1342
1997
Geobacillus stearothermophilus
Stamper, G.F.; Morollo, A.A.; Ringe, D.; Stamper, C.G.
Reaction of alanine racemase with 1-aminoethylphosphonic acid forms a stable external aldimine
Biochemistry
37
10438-10445
1998
Geobacillus stearothermophilus (P10724)
Morollo, A.A.; Petsko, G.A.; Ringe, D.
Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase
Biochemistry
38
3293-3301
1999
Geobacillus stearothermophilus (P10724), Geobacillus stearothermophilus
Spies, M.A.; Toney, M.D.
Multiple hydrogen kinetic isotope effects for enzymes catalyzing exchange with solvent: application to alanine racemase
Biochemistry
42
5099-5107
2003
Geobacillus stearothermophilus
Fenn, T.D.; Stamper, G.F.; Morollo, A.A.; Ringe, D.
A side reaction of alanine racemase: transamination of cycloserine
Biochemistry
42
5775-5783
2003
Geobacillus stearothermophilus (P10724), Geobacillus stearothermophilus
Kurokawa, Y.; Watanabe, A.; Yoshimura, T.; Esaki, N.; Soda, K.
Transamination as a side-reaction catalyzed by alanine racemase of Bacillus stearothermophilus
J. Biochem.
124
1163-1169
1998
Geobacillus stearothermophilus
Watanabe, A.; Yoshimura, T.; Mikami, B.; Hayashi, H.; Kagamiyama, H.; Esaki, N.
Reaction mechanism of alanine racemase from Bacillus stearothermophilus: X-ray crystallographic studies of the enzyme bound with N-(5'-phosphopyridoxyl)alanine
J. Biol. Chem.
277
19166-19172
2002
Geobacillus stearothermophilus
Watanabe, A.; Yoshimura, T.; Hee Lim, Y.; Kurokawa, Y.; Soda, K.; Esaki, N.
Stereochemistry of the hydrogen abstraction from pyridoxamine phosphate catalyzed by alanine racemase of Bacillus stearothermophilus
J. Mol. Catal. B
12
145-150
2001
Geobacillus stearothermophilus
-
Fenn, T.D.; Holyoak, T.; Stamper, G.F.; Ringe, D.
Effect of a Y265F mutant on the transamination-based cycloserine inactivation of alanine racemase
Biochemistry
44
5317-5327
2005
Geobacillus stearothermophilus (P10724), Geobacillus stearothermophilus
Noda, M.; Matoba, Y.; Kumagai, T.; Sugiyama, M.
Structural evidence that alanine racemase from a D-cycloserine-producing microorganism exhibits resistance to its own product
J. Biol. Chem.
279
46153-46161
2004
Streptomyces lavendulae, Geobacillus stearothermophilus
Mustata, G.; Briggs, J.M.
Cluster analysis of water molecules in alanine racemase and their putative structural role
Protein Eng. Des. Sel.
17
223-234
2004
Geobacillus stearothermophilus (P10724), Geobacillus stearothermophilus
Huang, H.C.; Jupiter, D.; Qiu, M.; Briggs, J.M.; Vanburen, V.
Cluster analysis of hydration waters around the active sites of bacterial alanine racemase using a 2-ns MD simulation
Biopolymers
89 (3)
210-219
2007
Geobacillus stearothermophilus (P10724)
Cassimjee, K.E.; Trummer, M.; Branneby, C.; Berglund, P.
Silica-immobilized His(6)-tagged enzyme: Alanine racemase in hydrophobic solvent
Biotechnol. Bioeng.
99 (3)
712-716
2007
Geobacillus stearothermophilus
Major, D.T.; Gao, J.
A combined quantum mechanical and molecular mechanical study of the reaction mechanism and alpha-amino acidity in alanine racemase
J. Am. Chem. Soc.
128
16345-16357
2006
Geobacillus stearothermophilus (P10724)
Spies, M.A.; Toney, M.D.
Intrinsic primary and secondary hydrogen kinetic isotope effects for alanine racemase from global analysis of progress curves
J. Am. Chem. Soc.
129
10678-10685
2007
Geobacillus stearothermophilus
Huang, H.; Jupiter, D.; Qiu, M.; Briggs, J.M.; VanBuren, V.
Cluster analysis of hydration waters around the active sites of bacterial alanine racemase using a 2-ns MD simulation
Biopolymers
89
210-219
2008
Geobacillus stearothermophilus (P10724)
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)
Rubinstein, A.; Major, D.T.
Understanding catalytic specificity in alanine racemase from quantum mechanical and molecular mechanical simulations of the arginine 219 mutant
Biochemistry
49
3957-3964
2010
Geobacillus stearothermophilus (P10724)
Priyadarshi, A.; Lee, E.H.; Sung, M.W.; Nam, K.H.; Lee, W.H.; Kim, E.E.; Hwang, K.Y.
Structural insights into the alanine racemase from Enterococcus faecalis
Biochim. Biophys. Acta
1794
1030-1040
2009
Escherichia coli (P0A6B4), Geobacillus stearothermophilus (P10724), Haemophilus influenzae (P45257), Mycobacterium tuberculosis (P9WQA9), Helicobacter pylori (Q1XG01), Enterococcus faecalis v583 (Q837J0), Enterococcus faecalis v583, Pseudomonas aeruginosa (Q9HTQ2), Mycobacterium tuberculosis H37Rv (P9WQA9)
Kato, S.; Hemmi, H.; Yoshimura, T.
Lysine racemase from a lactic acid bacterium, Oenococcus oeni: structural basis of substrate specificity
J. Biochem.
152
505-508
2012
Geobacillus stearothermophilus (P10724), Geobacillus stearothermophilus
Azam, M.A.; Jayaram, U.
Inhibitors of alanine racemase enzyme a review
J. Enzyme Inhib. Med. Chem.
31
517-526
2016
Geobacillus stearothermophilus, Bacillus cereus, Chlamydia pneumoniae, Enterobacter sp., Enterococcus faecalis, Lactiplantibacillus plantarum, Lactococcus lactis, Listeria monocytogenes, Methanococcus maripaludis, Staphylococcus aureus, Mycobacterium tuberculosis, Mycolicibacterium smegmatis, no activity in Homo sapiens, Proteus mirabilis, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens, Erysipelothrix rhusiopathiae, Escherichia coli (P0A6B4), Pseudomonas aeruginosa (Q9HUN4), Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 (Q9HUN4)
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