1gq2

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[[Category: pigeon liver]]
[[Category: pigeon liver]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:30:53 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:17:01 2007''

Revision as of 13:12, 30 October 2007


1gq2, resolution 2.5Å

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MALIC ENZYME FROM PIGEON LIVER

Overview

Malic enzymes are widely distributed in nature, and have important, biological functions. They catalyze the oxidative decarboxylation of, malate to produce pyruvate and CO(2) in the presence of divalent cations, (Mg(2+), Mn(2+)). Most malic enzymes have a clear selectivity for the, dinucleotide cofactor, being able to use either NAD(+) or NADP(+), but not, both. Structural studies of the human mitochondrial NAD(+)-dependent malic, enzyme established that malic enzymes belong to a new class of oxidative, decarboxylases. Here we report the crystal structure of the pigeon, cytosolic NADP(+)-dependent malic enzyme, in a closed form, in a, quaternary complex with NADP(+), Mn(2+), and oxalate. This represents the, first structural information on an NADP(+)-dependent malic enzyme. Despite, the ... [(full description)]

About this Structure

1GQ2 is a [Single protein] structure of sequence from [Columba livia] with OXL, MN, CL, NA and NAP as [ligands]. Active as [Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP(+))], with EC number [1.1.1.40]. Structure known Active Site: 1. Full crystallographic information is available from [OCA].

Reference

Structural studies of the pigeon cytosolic NADP(+)-dependent malic enzyme., Yang Z, Zhang H, Hung HC, Kuo CC, Tsai LC, Yuan HS, Chou WY, Chang GG, Tong L, Protein Sci. 2002 Feb;11(2):332-41. PMID:11790843

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