1h5q

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==Overview==
==Overview==
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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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11335726 (full description)]]
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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, properties of the recombinant enzyme are indistinguishable from the, natural enzyme. The crystal structure of its binary complex with NADP was, solved at 1.5-A resolution and refined to an R value of 19.3%. It shows, MtDH to be a tetramer and a member of the short chain, dehydrogenase/reductase family of enzymes. The catalytic residues forming, the so-called catalytic triad can be assigned to Ser(149), Tyr(169), and, Lys(173).
==About this Structure==
==About this Structure==
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1H5Q is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Agaricus_bisporus Agaricus bisporus]] with NI and NAP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Mannitol_2-dehydrogenase_(NADP(+)) Mannitol 2-dehydrogenase (NADP(+))]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.138 1.1.1.138]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H5Q OCA]].
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1H5Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agaricus_bisporus Agaricus bisporus] with NI and NAP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Mannitol_2-dehydrogenase_(NADP(+)) Mannitol 2-dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.138 1.1.1.138] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H5Q OCA].
==Reference==
==Reference==
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:29:44 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:22:19 2007''

Revision as of 11:17, 5 November 2007


1h5q, resolution 1.50Å

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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, properties of the recombinant enzyme are indistinguishable from the, natural enzyme. The crystal structure of its binary complex with NADP was, solved at 1.5-A resolution and refined to an R value of 19.3%. It shows, MtDH to be a tetramer and a member of the short chain, dehydrogenase/reductase family of enzymes. The catalytic residues forming, the so-called catalytic triad can be assigned to Ser(149), Tyr(169), and, Lys(173).

About this Structure

1H5Q is a Single protein structure of sequence from Agaricus bisporus with NI and NAP as ligands. Active as Mannitol 2-dehydrogenase (NADP(+)), with EC number 1.1.1.138 Structure known Active Site: AC1. 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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