1h5q

From Proteopedia

Revision as of 16:03, 29 October 2007 by OCA (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search

1h5q, resolution 1.50Å

Drag the structure with the mouse to rotate

MANNITOL DEHYDROGENASE FROM AGARICUS BISPORUS

Overview

Mannitol, an acyclic six-carbon polyol, is one of the most abundant sugar, alcohols occurring in nature. In the button mushroom, Agaricus bisporus, it is synthesized from fructose by the enzyme mannitol 2-dehydrogenase, (MtDH; EC ) using NADPH as a cofactor. Mannitol serves as the main storage, carbon (up to 50% of the fruit body dry weight) and plays a critical role, in growth, fruit body development, osmoregulation, and salt tolerance., Furthermore, mannitol dehydrogenases are being evaluated for commercial, mannitol production as alternatives to the less efficient chemical, reduction of fructose. Given the importance of mannitol metabolism and, mannitol dehydrogenases, MtDH was cloned into the pET28 expression system, and overexpressed in Escherichia coli. Kinetic and physicochemical, ... [(full description)]

About this Structure

1H5Q is a [Single protein] structure of sequence from [Agaricus bisporus] with NI and NAP as [ligands]. Active as [[1]], with EC number [1.1.1.138]. Full crystallographic information is available from [OCA].

Reference

The crystallographic structure of the mannitol 2-dehydrogenase NADP+ binary complex from Agaricus bisporus., Horer S, Stoop J, Mooibroek H, Baumann U, Sassoon J, J Biol Chem. 2001 Jul 20;276(29):27555-61. Epub 2001 May 2. PMID:11335726

Page seeded by OCA on Mon Oct 29 18:08:29 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools