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Information on EC 5.1.1.1 - alanine racemase and Organism(s) Shigella sonnei and UniProt Accession Q93HP9

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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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Select one or more organisms in this record: ?
This record set is specific for:
Shigella sonnei
UNIPROT: Q93HP9
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Word Map
The taxonomic range for the selected organisms is: Shigella sonnei
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
alanine racemase, alr-2, d-alanine racemase, alrbax, mbalr2, alrtt, cdalr, l-alanine racemase, alraba, cbl/alr, 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
L-Ala
D-Ala
show the reaction diagram
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
cofactor
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Sodium borohydride
reduction of the enzyme by dialysis with sodium borohydride, the reduced enzyme is catalytically inactive and addition of pyridoxal 5'-phosphate does not reverse the inactivation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALR1_SHISO
359
0
39165
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
1 * 43000, SDS-PAGE
46000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 43000, SDS-PAGE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
1 h, quick loss of activity in absence of pyridoxal 5'-phosphate
50
the enzyme is stabilized up to 50°C in presence of 0.4 mM pyridoxal 5'-phosphate
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, over 60 days
4°C, 3 weeks
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli JM109
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yokoigawa, K.; Hirasawa, R.; Ueno, H.; Okubo, Y.; Umesako, S.; Soda, K.
Gene cloning and characterization of alanine racemases from Shigella dysenteriae, Shigella boydii, Shigella flexneri, and Shigella sonnei
Biochem. Biophys. Res. Commun.
288
676-684
2001
Shigella flexneri (P0A6B5), Shigella flexneri, Shigella boydii (P0A6B6), Shigella boydii, Shigella dysenteriae (Q932V0), Shigella dysenteriae, Shigella sonnei (Q93HP9), Shigella sonnei
Manually annotated by BRENDA team