Crystal Structure of d-Aminoacylase from Alcaligenes faecalis DA1
نویسندگان
چکیده
منابع مشابه
Role of conserved histidine residues in D-aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6.
D-Aminoacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 (Alcaligenes A-6) was strongly inactivated by diethylpyrocarbonate (DEPC). An H67N mutant was barely active, with a kcat/Km 6.3 x 10(4) times lower than that of the recombinant wild-type enzyme, while the H67I mutant lost detectable activity. The H67N mutant had almost constant Km, but greatly decreased kcat. These results sug...
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A d-aminoacylase-producing microorganism, strain DA181, isolated from soil was identified as Alcaligenes denitrificans subsp. denitrificans. This strain produced about 29,300 units (micromoles of product formed per hour) of d-aminoacylase and 2,300 units of l-aminoacylase per gram of cells (wet weight) when cultivated in a medium containing 1% N-acetyl-dl-leucine as the carbon source. The d-ami...
متن کاملD-erythrose metabolism in a strain of Alcaligenes faecalis.
Except for the oxidation of erythritol to L-erythrulose by Acetobacter (Bertrand, 1900) little is known of the metabolism of tetroses in microorganisms. Barker and Lipmann (1949) found erythritol to be esterified and oxidized by Propionibacterium pentosaceum, although a tetrose intermediate was not identified. The utilization of D-erythrose by mammalian liver slices has been reported by Abraham...
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The crystal structure of the redox protein pseudoazurin (123 amino acid residues; molecular weight 13,000 daltons) from Alcaligenes faecalis has been refined by fast Fourier restrained least-squares minimization. Cycles of rebuilding were carried out to escape from local minima. Individual isotropic temperature factor values were refined separately for all atoms. The R factor was reduced from 0...
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Poly(3-hydroxybutyrate) (PHB) depolymerase from Alcaligenes faecalis T1 is composed of three domains: the catalytic (C) domain, the fibronectin type III-like (F) domain, and the substrate-binding (S) domain. We constructed domain deletion, inversion, chimera, and extra-F-domain mutants and examined their enzyme activity and PHB-binding ability. In addition, we performed substitution of 214Asp a...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2003
ISSN: 0021-9258
DOI: 10.1074/jbc.m210795200