1m7j
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Crystal structure of D-aminoacylase defines a novel subset of amidohydrolases
OverviewOverview
D-Aminoacylase is an attractive candidate for commercial production of, D-amino acids through its catalysis in the hydrolysis of N-acyl-D-amino, acids. We report here the first D-aminoacylase crystal structure from A., faecalis at 1.5-A resolution. The protein comprises a small beta-barrel, and a catalytic (betaalpha)(8)-barrel with a 63-residue insertion. The, enzyme structure shares significant similarity to the alpha/beta-barrel, amidohydrolase superfamily, in which the beta-strands in both barrels, superimpose well. Unexpectedly, the enzyme binds two zinc ions with widely, different affinities, although only the tightly bound zinc ion is required, for activity. One zinc ion is coordinated by Cys(96), His(220), and, His(250), while the other is loosely chelated by His(67), His(69), and, Cys(96). This is the first example of the metal ion coordination by a, cysteine residue in the superfamily. Therefore, D-aminoacylase defines a, novel subset and is a mononuclear zinc metalloenzyme but containing a, binuclear active site. The preferred substrate was modeled into a, hydrophobic pocket, revealing the substrate specificity and enzyme, catalysis. The 63-residue insertion containing substrate-interacting, residues may act as a gate controlling access to the active site, revealing that the substrate binding would induce a closed conformation to, sequester the catalysis from solvent.
About this StructureAbout this Structure
1M7J is a Single protein structure of sequence from Alcaligenes faecalis with ZN and ACT as ligands. Active as N-acyl-D-amino-acid deacylase, with EC number 3.5.1.81 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of D-aminoacylase from Alcaligenes faecalis DA1. A novel subset of amidohydrolases and insights into the enzyme mechanism., Liaw SH, Chen SJ, Ko TP, Hsu CS, Chen CJ, Wang AH, Tsai YC, J Biol Chem. 2003 Feb 14;278(7):4957-62. Epub 2002 Nov 25. PMID:12454005
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