“Malate dehydrogenase (NADP+)”的意思、由来-开放百科全书

词条

Malate dehydrogenase (NADP+)

释义

Structural studies
References

{{DISPLAYTITLE:Malate dehydrogenase (NADP⁺)}}{{enzyme
| Name = malate dehydrogenase (NADP⁺)
| EC_number = 1.1.1.82
| CAS_number = 37250-19-4
| IUBMB_EC_number = 1/1/1/82
| GO_code = 0046554
| image =
| width =
| caption =
}}

In enzymology, a malate dehydrogenase (NADP⁺) ({{EC number|1.1.1.82}}) is an enzyme that catalyzes the chemical reaction

(S)-malate + NADP⁺ oxaloacetate + NADPH + H⁺

Thus, the two substrates of this enzyme are (S)-malate and NADP⁺, whereas its 3 products are oxaloacetate, NADPH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD⁺ or NADP⁺ as acceptor. The systematic name of this enzyme class is (S)-malate:NADP⁺ oxidoreductase. Other names in common use include NADP⁺-malic enzyme, NADP⁺-malate dehydrogenase, malic dehydrogenase (nicotinamide adenine dinucleotide phosphate), malate NADP⁺ dehydrogenase, NADP⁺ malate dehydrogenase, NADP⁺-linked malate dehydrogenase, and malate dehydrogenase (NADP⁺). This enzyme participates in pyruvate metabolism and carbon fixation. This enzyme has at least one effector, hn.

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1CIV}} and {{PDB link|7MDH}}.

References

{{cite journal | vauthors = Connelly JL, Danner DJ, Bowden JA | date = 1968 | title = Branched chain alpha-keto acid metabolism. I. Isolation, purification, and partial characterization of bovine liver alpha-ketoisocaproic:alpha-keto-beta-methylvaleric acid dehydrogenase | journal = J. Biol. Chem. | volume = 243 | pages = 1198–203 | pmid = 5689906 | issue = 6 }}
{{cite journal | author = Johnson HS | date = 1971 | title = NADP-malate dehydrogenase: photoactivation in leaves of plants with Calvin cycle photosynthesis | journal = Biochem. Biophys. Res. Commun. | volume = 43 | pages = 703–9 | pmid = 4397919 | doi = 10.1016/0006-291X(71)90672-3 | issue = 4 }}
{{cite journal | vauthors = Johnson HS, Hatch MD | date = 1970 | title = Properties and regulation of leaf nicotinamide–adenine dinucleotide phosphate–malate dehydrogenase and 'malic' enzyme in plants with the C4-dicarboxylic acid pathway of photosynthesis | journal = Biochem. J. | volume = 119 | pages = 273–80 | pmid = 4395182 | issue = 2 | pmc = 1179348 }}

3 : EC 1.1.1|NADPH-dependent enzymes|Enzymes of known structure

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