1H5Q

Mannitol dehydrogenase from Agaricus bisporus

1H5Q の概要

• エントリーDOI: 10.2210/pdb1h5q/pdb
• 分子名称: NADP-DEPENDENT MANNITOL DEHYDROGENASE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, NICKEL (II) ION, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, mannitol metabolism
• 由来する生物種: AGARICUS BISPORUS (COMMON MUSHROOM)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 348128.38

構造登録者

Horer, S.,Stoop, J.,Mooibroek, H.,Baumann, U.,Sassoon, J. (登録日: 2001-05-24, 公開日: 2001-06-21, 最終更新日: 2023-12-13)

主引用文献

Horer, S.,Stoop, J.,Mooibroek, H.,Baumann, U.,Sassoon, J.
The Crystallographic Structure of the Mannitol 2-Dehydrogenase Nadp+ Binary Complex from Agaricus Bisporus
J.Biol.Chem., 276:27555-, 2001

PubMed Abstract: 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).

PubMed: 11335726
DOI: 10.1074/JBC.M102850200

実験手法

X-RAY DIFFRACTION (1.5 Å)