NDLI: Two arginine residues in the substrate pocket predominantly control the substrate selectivity of thiocyanate hydrolase.

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Two arginine residues in the substrate pocket predominantly control the substrate selectivity of thiocyanate hydrolase.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Yamanaka, Yasuaki Arakawa, Takatoshi Watanabe, Toshinori Namima, Satoshi Sato, Masa Hori, Shota Ohtaki, Akashi Noguchi, Keiichi Katayama, Yoko Yohda, Masafumi Odaka, Masafumi
Description	Country affiliation: Japan Author Affiliation: Yamanaka Y ( Department of Biotechnology and Life Science, Graduate School of Technology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan.)
Abstract	Thiocyanate hydrolase (SCNase) of Thiobacillus thioparus THI115 is a cobalt (Co)-containing enzyme that catalyzes the hydrolysis of thiocyanate (SCNâ»), a major component of wastewater from coke oven factories, to carbonyl sulfide and ammonia. Although SCNase exhibits high structural similarities to Co-type nitrile hydratase (NHase), including a unique Co³âº catalytic center with two oxidized Cys ligands, both SCNase and NHase exclusively catalyze only their own substrates. Based on the differences in the substrate-binding pockets of these enzymes, ßArg90 and Î³Arg136 of SCNase, with side chains extending toward the pocket, were separately substituted with Phe and Trp, the corresponding residues, respectively, in Co-type NHase. Both SCNase ßArg90 and SCNase Î³Arg136 mutants showed no SCNâ» hydrolysis activity but did catalyze the hydration of nitriles. The estimated kcat values (â¼2 sâ»¹) corresponded to approximately 0.2% of that of Co-type NHase for nitrile hydration and approximately 3% of that of wild-type SCNase for SCNâ» hydrolysis. The crystal structure of SCNase Î³R136W is essentially identical to that of the wild-type, including the Co³âº center having Cys oxidations; the size of the substrate pocket was enlarged because of conformational changes on the side chains of the mutated residue. Discussion of the difference in the environments around the substrate-binding pockets among the wild-type and mutant SCNases and Co-type NHase strongly suggests that ßArg90 and Î³Arg136, positioned at the top of the Co³âº center, predominantly control the substrate selectivity of SCNase.
File Format	HTM / HTML
ISSN	13891723
Issue Number	1
Volume Number	116
e-ISSN	13474421
Journal	Journal of Bioscience and Bioengineering
Language	English
Publisher	Elsevier
Publisher Date	2013-07-01
Publisher Place	Japan
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biomedical Engineering Discipline Microbiology Arginine Chemistry Hydrolases Amino Acid Substitution Biocatalysis Cobalt Cysteine Hydro-lyases Genetics Models, Molecular Oxidation-reduction Substrate Specificity Thiobacillus Enzymology Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Bioengineering Applied Microbiology and Biotechnology Biotechnology

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