Any feedback?
Information on EC 5.1.1.1 - alanine racemase and Organism(s) Bacillus anthracis and UniProt Accession Q81VF6
for references in articles please use BRENDA:EC5.1.1.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
5.1.1.1 alanine racemaseIUBMB Comments
A pyridoxal-phosphate protein.
Specify your search results
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 anthracis
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, l-alanine racemase, alraba, cdalr, cbl/alr, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-Alanine racemase
-
-
-
-
L-Alanine:D-alanine racemase
-
-
-
-
Racemase, alanine
-
-
-
-
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
L-leucine
D-leucine
-
activity is 20% compared with L-alanine, other amino acids are not racemized
-
-
r
L-alanine
D-alanine
Q81VF6
-
enzyme provides D-Ala as a required compound for the synthesis of the peptidoglycan layer of the bacterial cell wall, Tolypocladium niveum requires alanine racemase for cyclosporin biosynthesis
-
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
L-alanine
D-alanine
Q81VF6
-
enzyme provides D-Ala as a required compound for the synthesis of the peptidoglycan layer of the bacterial cell wall, Tolypocladium niveum requires alanine racemase for cyclosporin biosynthesis
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
PLP is inherently bound to the enzyme, removal of PLP inactivates the enzyme, adding PLP restores the activity, addition of 10 microM PLP to native enzyme slightly enhances activity
pyridoxal 5'-phosphate
Q81VF6
C-terminal region of 1 subdomain: Arg138 donates a hydrogen bond to the phenolic O atom of PLP, Arg224 donates a hydrogen bond to the pyridinyl N atom of PLP, Lys41 forms an aldimine linkage with the PLP, eliminating water to form the Schiff base, C-terminal atoms of second subunit Ser209, Gly226 and Ile227 stabilize the PLP phosphate with the help of Ser209 O(gamma), Tyr45 O(eta) and Tyr359 O(eta)
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(R)-1-aminoethylphosphonic acid
Q81VF6
in combination with pyridoxal 5'-phosphate
propionate
-
propionate influences both Km (affinity for substrate) and Vmax (enzyme catalysis)
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Q81VF6
Vmax of racemization of L- to D-alanine is 101 micromol/min/mg
additional information
-
Vmax of racemization of L- to D-alanine is 101 micromol/min/mg
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
deltaalr
Q81VF6
mutant with knocked out alanine racemase gene alr (2 alanine racemase-genes have been found in Bacillus anthracis jet)
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 85
-
between 60 and 70°C 50% of the enzyme activity is lost, at 85°C 50% of the protein molecules are denatured, the residual activity is 4%
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
amplified by PCR, cloned and overexpressed with pOPINB in Escherichia coli Rosetta pLysS cells, His-tagged product
Q81VF6
analyzation of alanine racemase-transcripts (RT-PCR) during growth and sporulation of wild-type shows low transcription level during early and higher during late sporulation states, analyzed expression level (immunoblotting) shows only alanine racemase during late sporulating states, growth rate of alr-gene knockout mutant and wild-type are identical, mutant only produces half as many spores as wild-type, mutant and wild-type show same resistance against heat, lysozyme and organic solvents, germination takes place in mutant at lower levels of L-alanine (a suggested germination activator) than in wild-type (D-alanine ist suggested to inhibit germination when unfavourable growth conditions), conversion of phase-bright spores to phase-dark germinating cells takes already place within mother cells of the alr mutant (phase dark to phase light), not in wild-type cells resulting in non-resistant mutant-germinants and resistant wild-type-spores respectively
Q81VF6
subcloned in a D-alanine auxotrophic Escherichia coli strain MB2795 and in Escherichia coli BL21(DE3)
Q81VF6
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
-
potential candidate for the development of a recombinant vaccine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Au, K.; Ren, J.; Walter, T.S.; Harlos, K.; Nettleship, J.E.; Owens, R.J.; Stuart, D.I.; Esnouf, R.M.
Structures of an alanine racemase from Bacillus anthracis (BA0252) in the presence and absence of (R)-1-aminoethylphosphonic acid (L-Ala-P)
Acta Crystallogr. Sect. F
F64
327-333
2008
Bacillus anthracis (Q81VF6), Bacillus anthracis
Chesnokova, O.N.; McPherson, S.A.; Steichen, C.T.; Turnbough, C.L.
The spore-specific alanine racemase of Bacillus anthracis and its role in suppressing germination during spore development
J. Bacteriol.
191
1303-1310
2009
Bacillus anthracis (Q81VF6), Bacillus anthracis
Kanodia, S.; Agarwal, S.; Singh, P.; Agarwal, S.; Singh, P.; Bhatnagar, R.
Biochemical characterization of alanine racemase -a spore protein produced by Bacillus anthracis
BMB Rep.
42
47-52
2009
Bacillus anthracis
EXTERNAL LINKS (specific for EC-Number 5.1.1.1)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
