Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 288, Issue 5, Pages 1169-1174Publisher
ACADEMIC PRESS INC
DOI: 10.1006/bbrc.2001.5897
Keywords
cysteine-sulfinic acid; cysteine-sulfenic acid; posttranslational modification; noncorrin cobalt; nitrile; hydration
Categories
Ask authors/readers for more resources
The crystal structure of cobalt-containing nitrile hydratase from Pseudonocardia thermophila JCM 3095 at 1.8 Angstrom resolution revealed the structure of the non-corrin cobalt at the catalytic center. Two cysteine residues (alpha Cys(111) and alpha Cys(113)) coordinated to the cobalt were posttranslationally modified to cysteine-sulfinic acid and to cysteine-sulfenic acid, respectively, like in iron-containing nitrile hydratase. A tryptophan residue (beta Trp(72)), which may be involved in substrate binding, replaced the tyrosine residue of iron-containing nitrile hydratase. The difference seems to be responsible for the preference for aromatic nitriles rather than aliphatic ones of cobalt-containing nitrile hydratase. (C) 2001 Academic Press.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available