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・ Malat
・ MALAT1
・ MALAT1-associated small cytoplasmic RNA
・ Malatang
・ Malataverne
・ Malate Catholic School
・ Malate Church
・ Malate dehydrogenase
・ Malate dehydrogenase (decarboxylating)
・ Malate dehydrogenase (disambiguation)
・ Malate dehydrogenase (NAD(P)+)
・ Malate dehydrogenase (NADP+)
・ Malate dehydrogenase (oxaloacetate-decarboxylating)
・ Malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)
・ Malate dehydrogenase (quinone)
Malate dehydrogenase 2
・ Malate oxidase
・ Malate synthase
・ Malate, Manila
・ Malate-aspartate shuttle
・ Malateh
・ Malatesta
・ Malatesta (film)
・ Malatesta (Rome Metro)
・ Malatesta da Verucchio
・ Malatesta II Baglioni
・ Malatesta II Malatesta
・ Malatesta IV Malatesta
・ Malatesta Malatesta
・ Malatesta Novello


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Malate dehydrogenase 2 : ウィキペディア英語版
Malate dehydrogenase 2

Malate dehydrogenase, mitochondrial also known as malate dehydrogenase 2 is an enzyme that in humans is encoded by the ''MDH2'' gene.
Malate dehydrogenase catalyzes the reversible oxidation of malate to oxaloacetate, utilizing the NAD/NADH cofactor system in the citric acid cycle. The protein encoded by this gene is localized to the mitochondria and may play pivotal roles in the malate-aspartate shuttle that operates in the metabolic coordination between cytosol and mitochondria.〔(【引用サイトリンク】 url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4191 )
==Structure==
The protein encoded by MDH2 exists as a dimer, which indicate the important connection between protein stability and enzymatic activity. Each subunit contains two structurally and functionally distinct domains. The first is the NAD-binding domain, which exists in the amino-terminal half of each molecule, and contains a parallel-sheet structure, otherwise known as a Rosman fold motif. The core dinucleotide binding structure is composed of four beta-sheets and one
alpha-helix. The other domain is a carboxy-terminal domain that contains the substrate binding site and amino acids that are necessary for catalysis. The active site of these enzymes is in a cleft between two domains. Crystallography reveals the dimer interface, which consists mainly of interacting alpha-helices that form a compact interaction. The active sites in these dimeric proteins are well separated from each other.

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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