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Information on EC 5.1.1.1 - alanine racemase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9HTQ2
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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
-
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: Pseudomonas aeruginosa
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, alr2 racemase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ALR
L-Alanine racemase
-
-
-
-
L-Alanine:D-alanine racemase
-
-
-
-
Racemase, alanine
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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-Ala
D-Ala
-
enzyme is required for production of D-Ala, a necessary component of the bacterial cell wall
-
?
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-Ala
D-Ala
-
enzyme is required for production of D-Ala, a necessary component of the bacterial cell wall
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
each monomer is comprised of two domains, an eight-stranded alpha/beta barrel containing the pyridoxal 5'-phosphate cofactor and a second domain primarily composed of beta-strands. The cofactor adopts two partially occupied conformational states that resemble previously reported and external aldimine complexes
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
((6R)-2-carboxy-8-oxo-7-[2-(thiophen-2-yl)acetamido]-5-thia-1-azabicyclo[4.2.0]oct-2-en-3-yl)methyl 3-chloro-D-alanyl-D-alaninate
-
(2S)-1-oxo-1-([(1R)-1-phosphonoethyl]amino)propan-2-yl L-methioninate
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alafosfalin
selective inhibitor of peptidoglycan biosynthesis in both Grampositive and Gram-negative bacteria
D-cycloserine
competitive inhibition, importance of N2-structural site in cyloserine for bioactivity
L-Cycloserine
competitive inhibition, importance of N2-structural site in cyloserine for bioactivity
additional information
N2-substitution of carboxybenzyl-protected derivatives of DL-cycloserine proceed smoothly with the requisite alkyl halide in the presence of potassium tert-butoxide in dimethylformamide. The synthesised compounds are evaluated for their inhibitory activity against purified Alrs (Alr gene product). Structural modification at the N2 position result in reduced activity in the enzyme assay and underscore the importance of structural modification at N2-position of cycloserine. A compound with CH2CONHOCH3 substituent at (N)-2 position exhibits modest inhibitory activity against purified Alr enzyme from Escherichia coli, Ki is 0.47 mM. No inhibition by ((6R)-2-carboxy-8-oxo-7-[2-(thiophen-2-yl)acetamido]-5-thia-1-azabicyclo[4.2.0]oct-2-en-3-yl)methyl 3-chloro-D-alanyl-3-chloro-D-alaninate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0138
D-cycloserine
pH and temperature not specified in the publication
0.0138
L-Cycloserine
pH and temperature not specified in the publication
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
alanine racemase is a fold type III pyridoxal 5'-phosphate-dependent amino acid racemase enzyme. Pseudomonas aeruginosa has two isozymes, encoded by the Alr and the DadB genes
metabolism
DadB expression is induced by L-alanine to a level much greater than that of Alr and is probably responsible for the catabolism of D-Ala. Alr is constitutively expressed and seems to provide the D-alanine necessary to maintain cell growth
physiological function
D-alanine, produced by the action of alanine racemase on L-alanine, is important to both Gram-positive and Gram-negative bacteria, since it is required for the synthesis of the peptidoglycan in the cell wall
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
each monomer is comprised of two domains, an eight-stranded alpha/beta barrel containing the pyridoxal 5'-phosphate cofactor and a second domain primarily composed of beta-strands
homodimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drops equilibrated versus 1.5 M (NH4)2SO4, 2% polyethylene glycol 400 and 0.1 M HEPES, pH 7.5, crystal strcuture at 1.45 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of two independent alanine racemases in Escherichia coli: Alr and DadX
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
Alr is a target for the development of antibacterial drugs
medicine
-
the requirement for D-Ala as a necessary component of the bacterial cell wall makes the enzyme a logical target for the development of novel antibiotics
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lacoste, A.M.; Darriet, M.; Neuzil, E.; Le Goffic, F.
Inhibition of alanine racemase by vinylglycine and its phosphonic analogue: a 1H nuclear magnetic resonance spectroscopy study
Biochem. Soc. Trans.
16
606-608
1988
Pseudomonas aeruginosa, Pseudomonas aeruginosa A237
-
LeMagueres, P.; Im, H.; Dvorak, A.; Strych, U.; Benedik, M.; Krause, K.L.
Crystal structure at 1.45 A resolution of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms
Biochemistry
42
14752-14761
2003
Pseudomonas aeruginosa (Q9HTQ2), Pseudomonas aeruginosa
Strych, U.; Huang, H.C.; Krause, K.L.; Benedik, M.J.
Characterization of the alanine racemases from Pseudomonas aeruginosa PAO1
Curr. Microbiol.
41
290-294
2000
Pseudomonas aeruginosa
Priyadarshi, A.; Lee, E.H.; Sung, M.W.; Nam, K.H.; Lee, W.H.; Kim, E.E.; Hwang, K.Y.
Structural insights into the alanine racemase from Enterococcus faecalis
Biochim. Biophys. Acta
1794
1030-1040
2009
Escherichia coli (P0A6B4), Geobacillus stearothermophilus (P10724), Haemophilus influenzae (P45257), Mycobacterium tuberculosis (P9WQA9), Helicobacter pylori (Q1XG01), Enterococcus faecalis v583 (Q837J0), Enterococcus faecalis v583, Pseudomonas aeruginosa (Q9HTQ2), Mycobacterium tuberculosis H37Rv (P9WQA9)
Ju, J.; Xu, S.; Furukawa, Y.; Zhang, Y.; Misono, H.; Minamino, T.; Namba, K.; Zhao, B.; Ohnishi, K.
Correlation between catalytic activity and monomer-dimer equilibrium of bacterial alanine racemases
J. Biochem.
149
83-89
2011
Escherichia coli, Pseudomonas aeruginosa, Pseudomonas fluorescens, Pseudomonas fluorescens LRB3W1, Pseudomonas fluorescens TM5-2, Pseudomonas putida, Pseudomonas putida KT 2240, Salmonella enterica subsp. enterica serovar Typhimurium
Azam, M.A.; Jayaram, U.
Inhibitors of alanine racemase enzyme a review
J. Enzyme Inhib. Med. Chem.
31
517-526
2016
Geobacillus stearothermophilus, Bacillus cereus, Chlamydia pneumoniae, Enterobacter sp., Enterococcus faecalis, Lactiplantibacillus plantarum, Lactococcus lactis, Listeria monocytogenes, Methanococcus maripaludis, Staphylococcus aureus, Mycobacterium tuberculosis, Mycolicibacterium smegmatis, no activity in Homo sapiens, Proteus mirabilis, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens, Erysipelothrix rhusiopathiae, Escherichia coli (P0A6B4), Pseudomonas aeruginosa (Q9HUN4), Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 (Q9HUN4)
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