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Information on EC 5.1.1.1 - alanine racemase and Organism(s) Peribacillus psychrosaccharolyticus and UniProt Accession Q9S5V6

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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:
Peribacillus psychrosaccharolyticus
UNIPROT: Q9S5V6
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Word Map
The taxonomic range for the selected organisms is: Peribacillus psychrosaccharolyticus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
alanine racemase, alr-2, d-alanine racemase, alrbax, mbalr2, alrtt, l-alanine racemase, alraba, cdalr, alr2 racemase, 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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
Km: 0.005 mM, at 30°C
pyridoxal 5'-phosphate
-
Km at 30°C is 0.005 mM. Maximal activity is obtained in presence of more than 0.125 mM pyridoxal 5'-phosphate. The decrease in activity at incubation temperatures over 40°C is consistent with the decrease in the amount of bound pyridoxal 5'-phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
in absence of pyridoxal 5'-phosphate
60
in presence of an excess amount of pyridoxal 5'-phosphate, 0.4 mM
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 60
about 30% of maximal activity at 0°C and at 60°C, in absence of pyridoxal 5'-phosphate
30 - 50
30°C, 45% of maximal activity, 50°C: about 50% of maximal activity, in presence of an excess amount of pyridoxal 5'-phosphate, 0.4 mM
40 - 70
-
40°C: about 60% of maximal activity, 70°C: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALR_PERPY
383
0
42519
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
pH 8.3, 1 h, the purified is extremely labile over 35°C
50
pH 8.3, 1 h, stabilized up to 50°C in presence of excess amounts of pyridoxal 5'-phosphate, 0.4 mM, complete inactivation in absence of pyridoxal 5'-phosphate
40
-
the decrease in the enzyme activity at incubation temperatures over 40°C is consistent with the decrease in the amount of bound pyridoxal 5'-phosphate, no effect on stability at lower temperatures, 0-30°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
pyridoxal 5'-phosphate present in the solvent suppresses the enzyme's unfolding
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli SOLR with a plasmid yYOK3
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okubo, Y.; Yokoigawa, K.; Esaki, N.; Soda, K.; Kawai, H.
Characterization of psychrophilic alanine racemase from Bacillus psychrosaccharolyticus
Biochem. Biophys. Res. Commun.
256
333-340
1999
Peribacillus psychrosaccharolyticus (Q9S5V6), Peribacillus psychrosaccharolyticus
Manually annotated by BRENDA team
Okubo, Y.; Yokoigawa, K.; Esaki, N.; Soda, K.; Misono, H.
High catalytic activity of alanine racemase from psychrophilic Bacillus psychrosaccharolyticus at high temperatures in the presence of pyridoxal 5'-phosphate
FEMS Microbiol. Lett.
192
169-173
2000
Peribacillus psychrosaccharolyticus
Manually annotated by BRENDA team