1h5q
From Proteopedia
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(New page: 200px<br /> <applet load="1h5q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h5q, resolution 1.50Å" /> '''MANNITOL DEHYDROGEN...)
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Revision as of 16:03, 29 October 2007
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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
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