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Information on EC 5.1.1.1 - alanine racemase and Organism(s) Streptomyces lavendulae and UniProt Accession Q65YW7

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EC Tree
     5 Isomerases
         5.1 Racemases and epimerases
             5.1.1 Acting on amino acids and derivatives
                5.1.1.1 alanine racemase
IUBMB Comments
A pyridoxal-phosphate protein.
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This record set is specific for:
Streptomyces lavendulae
UNIPROT: Q65YW7
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Word Map
The taxonomic range for the selected organisms is: Streptomyces lavendulae
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
alanine racemase, alr-2, d-alanine racemase, alrbax, mbalr2, alrtt, alraba, cdalr, l-alanine racemase, ecalr, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-Alanine racemase
-
-
-
-
L-Alanine:D-alanine racemase
-
-
-
-
Racemase, alanine
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
racemization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
alanine racemase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-06-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-alanine
L-alanine
show the reaction diagram
-
-
-
r
L-alanine
D-alanine
show the reaction diagram
-
-
-
r
D-alanine
L-alanine
show the reaction diagram
-
-
-
-
r
D-serine
L-serine
show the reaction diagram
-
-
-
-
r
L-alanine
D-alanine
show the reaction diagram
-
-
-
-
r
L-serine
D-serine
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-cycloserine
time-dependent inactivation rate of enzyme from Streptomyces lavendulae is slower than for enzyme from Escherichia coli. Enzyme from Streptomyces lavendulae is one of its self-resistance determinants
D-cycloserine
-
mechanism of inactivation and comparison with inactivation of Bacillus stearothermophilus enzyme
L-Cycloserine
-
mechanism of inactivation and comparison with inactivation of Bacillus stearothermophilus enzyme
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7
D-alanine
pH 8.2, 25°C
0.7
L-alanine
pH 8.2, 25°C
0.4
D-alanine
-
pH 8.2, 37°C
10
D-serine
-
pH 8.2, 37°C
0.4
L-alanine
-
pH 8.2, 37°C
27
L-serine
-
pH 8.2, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
70
D-alanine
pH 8.2, 25°C
55
L-alanine
pH 8.2, 25°C
63.3
D-alanine
-
pH 8.2, 37°C
5.5
D-serine
-
pH 8.2, 37°C
55
L-alanine
-
pH 8.2, 37°C
13.3
L-serine
-
pH 8.2, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.87
D-cycloserine
pH 8.2, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
assay method based on circular dichroism spectra of D- and L-alanine
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39900
2 * 39900, calculated, 2 * 42000, SDs-PAGE
42000
2 * 39900, calculated, 2 * 42000, SDs-PAGE
80000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 39900, calculated, 2 * 42000, SDs-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
free enzyme and in complex with D- or L-cycloserine
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Noda, M.; Matoba, Y.; Kumagai, T.; Sugiyama, M.
A novel assay method for an amino acid racemase reaction based on circular dichroism
Biochem. J.
389
491-496
2005
Streptomyces lavendulae, Escherichia coli
Manually annotated by BRENDA team
Noda, M.; Kawahara, Y.; Ichikawa, A.; Matoba, Y.; Matsuo, H.; Lee, D.G.; Kumagai, T.; Sugiyama, M.
Self-protection mechanism in D-cycloserine-producing Streptomyces lavendulae. Gene cloning, characterization, and kinetics of its alanine racemase and D-alanyl-D-alanine ligase, which are target enzymes of D-cycloserine
J. Biol. Chem.
279
46143-46152
2004
Escherichia coli, Streptomyces lavendulae (Q65YW7), Streptomyces lavendulae
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team