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Crystal structure of alanine dehydrogenase (AF1665) from Archaeoglobus fulgidus at 2.80 A resolutionCrystal structure of alanine dehydrogenase (AF1665) from Archaeoglobus fulgidus at 2.80 A resolution
Structural highlights
FunctionALADH_ARCFU Catalyzes the NAD(+)-dependent oxidative deamination of L-alanine to pyruvate, and the reverse reaction, the reductive amination of pyruvate. Its physiological role is not known. Can not use NADP(+) instead of NAD(+) as a cosubstrate. In the deamination direction, can also efficiently use L-2-aminobutyrate as substrate. In the reductive amination direction, also exhibits high activity with 2-oxobutyrate and oxaloacetate as substrate. In contrast to bacterial homologs, does not exhibit any ornithine cyclodeaminase activity.[HAMAP-Rule:MF_00935][1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
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