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Literature summary for 5.1.1.1 extracted from

  • Davis, E.; Scaletti-Hutchinson, E.; Opel-Reading, H.; Nakatani, Y.; Krause, K.L.
    The structure of alanine racemase from Acinetobacter baumannii (2014), Acta Crystallogr. Sect. F, 70, 1199-1205 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
drug development the enzyme is a target for antibiotic drug development, especially the dimer interface a potential target for structure-aided drug design Acinetobacter baumannii

Cloned(Commentary)

Cloned (Comment) Organism
gene alr, recombinant expression in Escherichia coli strain BL21(DE3) Acinetobacter baumannii

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme, sitting drop vapour diffusion, 6 mg/ml protein solution is mixed with crystallization solution containing 100 mM MES, pH 6.0, 200 mM CaCl2, and 20% PEG 6000, 4 days, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement using the ligand- and water-free monomer structure of Pseudomonas aeruginosa as the search model Acinetobacter baumannii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.56
-
D-alanine pH not specified in the publication, 30°C Acinetobacter baumannii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-alanine Acinetobacter baumannii
-
D-alanine
-
r

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii D0C5Y6
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) by hydrophobic interaction and anion-exchange chromatography, gel filtration, and ultrafiltration Acinetobacter baumannii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-alanine
-
Acinetobacter baumannii L-alanine
-
r
L-alanine
-
Acinetobacter baumannii D-alanine
-
r

Subunits

Subunits Comment Organism
dimer enzyme structure comparisons, overview Acinetobacter baumannii

Synonyms

Synonyms Comment Organism
ALR
-
Acinetobacter baumannii
AlrAba
-
Acinetobacter baumannii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Acinetobacter baumannii

Cofactor

Cofactor Comment Organism Structure
additional information there is no additional density in the AlrAba structure consistent with the presence of any additional ligands besides pyridoxal 5'-phosphate Acinetobacter baumannii
pyridoxal 5'-phosphate PLP, dependent on. The PLP-binding motif containing the catalytic Lys34 (sequence SMVKANAYGHG) is largely conserved between the various enzymes. The essential PLP cofactor is covalently bound to Lys34 via an internal aldimine linkage and extends towards the centre of the alpha/beta-barrel. The pyridine N1 of the PLP ring is stabilized by hydrogen bonding to Arg209, which is further stabilized by interactions with His159. The phosphate tail of PLP is stabilized by several residues from one monomer. The OP1 of the phosphate group hydrogen bonds to Ile212 and Tyr38, OP2 hydrogen bonds to Try341 and OP3 hydrogen bonds to Ile212 and Ser190. Arg132 is not within hydrogen-bonding distance of PLP in the AlrAba structure Acinetobacter baumannii

General Information

General Information Comment Organism
malfunction inhibition of the enzyme is lethal to prokaryotes Acinetobacter baumannii
additional information enzyme structure comparisons, active site structure, overview Acinetobacter baumannii
physiological function the enzyme is responsible for racemization between enantiomers of alanine, D-alanine is an essential component of the bacterial cell wall Acinetobacter baumannii