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Titolo:
Glycerol dehydrogenase: Structure, specificity, and mechanism of a family III polyol dehydrogenase
Autore:
Ruzheinikov, SN; Burke, J; Sedelnikova, S; Baker, PJ; Taylor, R; Bullough, PA; Muir, NM; Gore, MG; Rice, DW;
Indirizzi:
Univ Sheffield, Dept Mol Biol & Biotechnol, Krebs Inst Biomol Res, Sheffield S10 2TN, S Yorkshire, England Univ Sheffield Sheffield S Yorkshire England S10 2TN S Yorkshire, England Univ Southampton, Dept Biochem & Mol Biol, Southampton SO16 7PX, Hants, England Univ Southampton Southampton Hants England SO16 7PX 6 7PX, Hants, England
Titolo Testata:
STRUCTURE
fascicolo: 9, volume: 9, anno: 2001,
pagine: 789 - 802
SICI:
0969-2126(200109)9:9<789:GDSSAM>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACTIVATED ALCOHOL-DEHYDROGENASE; X-RAY-DIFFRACTION; ESCHERICHIA-COLI; 3-DIMENSIONAL RECONSTRUCTION; BACILLUS-STEAROTHERMOPHILUS; PROTEIN-STRUCTURE; SEQUENCE; PURIFICATION; CLONING; SYSTEM;
Keywords:
crystal structure; metallo-enzyme; glycerol dehydrogenase; EC 1.1.1.6; glycerol oxidation; Bacillus stearothermophilus;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Rice, DW Univ Sheffield, Dept Mol Biol & Biotechnol, Krebs Inst Biomol Res, 5th Court,Western Bank, Sheffield S10 2TN, S Yorkshire, England Univ Sheffield 5th Court,Western Bank Sheffield S Yorkshire England S10 2TN
Citazione:
S.N. Ruzheinikov et al., "Glycerol dehydrogenase: Structure, specificity, and mechanism of a family III polyol dehydrogenase", STRUCTURE, 9(9), 2001, pp. 789-802

Abstract

Background: Bacillus stearothermophilus glycerol dehydrogenase (GlyDH) (glycerol:NAD(+) 2-oxidoreductase, EC 1.1.1.6) catalyzes the oxidation of glycerol to dihydroxyacetone (1,3-dihydroxypropanone) with concomitant reduction of NAD(+) to NADH. Analysis of the sequence of this enzyme indicates thatit is a member of the so-called iron-containing alcohol dehydrogenase family. Despite this sequence similarity, GlyDH shows a strict dependence on zinc for activity. On the basis of this, we propose to rename this group the family III metaldependent polyol dehydrogenases. To date, no structural data have been reported for any enzyme in this group. Results: The crystal structure of B. stearothermophilus glycerol dehydrogenase has been determined at 1.7 Angstrom resolution to provide structural insights into the mechanistic features of this family. The enzyme has 370 amino acid residues, has a molecular mass of 39.5 kDa, and is a homooctamer in solution. Conclusions: Analysis of the crystal structures of the free enzyme and of the binary complexes with NAD(+) and glycerol show that the active site of GlyDH lies in the cleft between the enzyme's two domains, with the catalytic zinc ion playing a role in stabilizing an alkoxide intermediate. In addition, the specificity of this enzyme for a range of diols can be understood,as both hydroxyls of the glycerol form ligands to the enzyme-bound Zn2+ ion at the active site. The structure further reveals a previously unsuspected similarity to dehydroquinate synthase, an enzyme whose more complex chemistry shares a common chemical step with that catalyzed by glycerol dehydrogenase, providing a striking example of divergent evolution. Finally, the structure suggests that the NAD(+) binding domain of GlyDH may be related to that of the classical Rossmann fold by switching the sequence order of the two mononucleotide binding folds that make up this domain.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 13:57:58