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Information on EC 5.1.1.1 - alanine racemase and Organism(s) Streptomyces coelicolor and UniProt Accession O86786
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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
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racemization
- d-cycloserine
- stearothermophilus
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plp-dependent
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d-amino
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aldimine
- d-alanyl-d-alanine
- exosporium
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pyridoxal-5'-phosphate-dependent
- drug development
-
5'-phosphate-dependent
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d-alanine:d-alanine
- medicine
- biotechnology
- pharmacology
The taxonomic range for the selected organisms is: Streptomyces coelicolor
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, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-Alanine racemase
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L-Alanine:D-alanine racemase
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Racemase, alanine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
racemization
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SYSTEMATIC NAME
IUBMB Comments
alanine racemase
A pyridoxal-phosphate protein.
CAS REGISTRY NUMBER
COMMENTARY
9024-06-0
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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
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
PLP, dependent on, binding structure analysis: the phosphate group of the pyridoxal 5'-phosphate is stabilized by hydrogen bonds with the side chains of Tyr50, Ser222 and Tyr374, and with the backbone of Gly239, Ser222, and Ile240. The pyridine ring of the PLP is stabilized by a hydrogen bond between the N-1 of the cofactor and Nepsilon of Arg237. The C2A of the PLP also interacts with oxygen Q1 of the carboxylated Lys141. All residues stabilizing the PLP cofactor (Tyr50, Ser222, Gly239, Ile240, Arg237, Tyr374) are conserved among Alr proteins. But the AlrSco lacks one important hydrogen bond between Arg148 and the phenolic oxygen of the PLP molecule
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-cycloserine
structural features such as the hinge angle or the surface area between the monomers do not contribute to D-cycloserine resistance, binding structure analysis, overview
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
104
racemization of D- to L-Ala, purified enzyme, pH 7.0, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the Fold Type III of pyridoxal 5'-phosphate-dependent enzymes
physiological function
the conversion of L-alanine (L-Ala) into D-alanine (D-Ala) in bacteria is performed by pyridoxal 5'-phosphate-dependent enzymes, alanine racemases. D-Ala is an essential component of the bacterial peptidoglycan and hence required for survival
additional information
additional information
structure-function realtionship analysis, overview
additional information
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structure-function realtionship analysis, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme Alr is a homodimer with residues from both monomers contributing to the active site. There are two active sites per dimer, which are located at the interface between each alpha/beta-barrel of one subunit and the C-terminal domain of the other. The catalytic core consists of the pyridoxal 5'-phosphate cofactor, a Lys, and a Tyr, which is contributed by the other subunit. The cofactor is bound through an internal aldimine bond to the amino group of Lys46, located at the C-terminal side of the first beta-strand of the alpha/beta-barrel. The side chain of the catalytic Lys46 points out of the alpha/beta-barrel, towards the C-terminal domain of the interacting subunit, and in particular, towards Tyr283'. The phosphate group of the pyridoxal-5'-phosphate is stabilized by hydrogen bonds with the side chains of Tyr50, Ser222 and Tyr374, and with the backbone of Gly239, Ser222, and Ile240
additional information
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enzyme Alr is a homodimer with residues from both monomers contributing to the active site. There are two active sites per dimer, which are located at the interface between each alpha/beta-barrel of one subunit and the C-terminal domain of the other. The catalytic core consists of the pyridoxal 5'-phosphate cofactor, a Lys, and a Tyr, which is contributed by the other subunit. The cofactor is bound through an internal aldimine bond to the amino group of Lys46, located at the C-terminal side of the first beta-strand of the alpha/beta-barrel. The side chain of the catalytic Lys46 points out of the alpha/beta-barrel, towards the C-terminal domain of the interacting subunit, and in particular, towards Tyr283'. The phosphate group of the pyridoxal-5'-phosphate is stabilized by hydrogen bonds with the side chains of Tyr50, Ser222 and Tyr374, and with the backbone of Gly239, Ser222, and Ile240
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant N-terminally His-tagged enzyme free, or in complex with inhibitors D-cycloserine and propionate, sitting drop vapor diffusion, mixing of 0.001 ml of 20 mg/ml protein solution with 0.001 ml of crystallization solution containing 0.1 M Bis-Tris propane, pH 8.5, 0.2 M NaBr, 20% w/v PEG 3350, 38 days, X-ray diffraction structure determination and analysis at 2.8 A for the free enzyme, and at 1.51-1.64 A resolution for the enzyme complexes, model building
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21 Star (DE3)pLysS by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene alr, sequence comparisons, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21 Star (DE3)pLysS
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tassoni, R.; van der Aart, L.T.; Ubbink, M.; van Wezel, G.P.; Pannu, N.S.
Structural and functional characterization of the alanine racemase from Streptomyces coelicolor A3(2)
Biochem. Biophys. Res. Commun.
483
122-128
2017
Streptomyces coelicolor (O86786), Streptomyces coelicolor, Streptomyces coelicolor ATCC BAA-471 / A3(2) / M145 (O86786)
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Release 2023.1 (January 2023)
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