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 (Comment) | Organism |
---|---|
gene alr, recombinant expression in Escherichia coli strain BL21(DE3) | Acinetobacter baumannii |
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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.56 | - |
D-alanine | pH not specified in the publication, 30°C | Acinetobacter baumannii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-alanine | Acinetobacter baumannii | - |
D-alanine | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acinetobacter baumannii | D0C5Y6 | - |
- |
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-alanine | - |
Acinetobacter baumannii | L-alanine | - |
r | |
L-alanine | - |
Acinetobacter baumannii | D-alanine | - |
r |
Subunits | Comment | Organism |
---|---|---|
dimer | enzyme structure comparisons, overview | Acinetobacter baumannii |
Synonyms | Comment | Organism |
---|---|---|
ALR | - |
Acinetobacter baumannii |
AlrAba | - |
Acinetobacter baumannii |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Acinetobacter baumannii |
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 | 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 |