Universität zu Köln

Hoeppner, Astrid ORCID: 0000-0002-7076-5936, Schomburg, Dietmar ORCID: 0000-0002-3354-822X and Niefind, Karsten ORCID: 0000-0002-0183-6315 (2013). Enzyme-substrate complexes of the quinate/shikimate dehydrogenase from Corynebacterium glutamicum enable new insights in substrate and cofactor binding, specificity, and discrimination. Biol. Chem., 394 (11). S. 1505 - 1517. BERLIN: WALTER DE GRUYTER GMBH. ISSN 1437-4315

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Abstract

Quinate dehydrogenase (QDH) catalyzes the reversible oxidation of quinate to 3-dehydroquinate by nicotineamide adenine dinucleotide (NADH) and is involved in the catabolic quinate metabolism required for the degradation of lignin. The enzyme is a member of the family of shikimate/quinate dehydrogenases (SDH/QDH) occurring in bacteria and plants. We characterized the dual-substrate quinate/shikimate dehydrogenase (QSDH) from Corynebacterium glutamicum (CglQSDH) kinetically and revealed a clear substrate pre-ference of CglQSDH for quinate compared with shikimate both at the pH optimum and in a physiological pH range, which is a remarkable contrast to closely related SDH/QDH enzymes. With respect to the cosubstrate, CglQSDH is strictly NAD(H) dependent. These substrate and cosubstrate profiles correlate well with the details of three atomic resolution crystal structures of CglQSDH in different functional states we report here: with bound NAD+ (binary complex) and as ternary complexes with NADH plus either shikimate or quinate. The CglQSDH-NADH-quinate structure is the first complex structure of any member of the SDH/QDH family with quinate. Based on this novel structural information and systematic sequence and structure comparisons with closely related enzymes, we can explain the strict NAD(H) dependency of CglQSDH as well as its discrimination between shikimate and quinate.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Hoeppner, Astrid UNSPECIFIED orcid.org/0000-0002-7076-5936 UNSPECIFIED Schomburg, Dietmar UNSPECIFIED orcid.org/0000-0002-3354-822X UNSPECIFIED Niefind, Karsten UNSPECIFIED orcid.org/0000-0002-0183-6315 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-473301
DOI:	10.1515/hsz-2013-0170
Journal or Publication Title:	Biol. Chem.
Volume:	394
Number:	11
Page Range:	S. 1505 - 1517
Date:	2013
Publisher:	WALTER DE GRUYTER GMBH
Place of Publication:	BERLIN
ISSN:	1437-4315
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language SHIKIMATE DEHYDROGENASE; CRYSTAL-STRUCTURE; AROMATIC BIOSYNTHESIS; SYNTHASE REVEALS; QUINATE; PURIFICATION; PATHWAY; ACID; AROE; EXPRESSION Multiple languages Biochemistry & Molecular Biology Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/47330