1vll

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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

1vll is a 2 chain structure with sequence from Archaeoglobus fulgidus DSM 4304. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

ALADH_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

  1. Schroder I, Vadas A, Johnson E, Lim S, Monbouquette HG. A novel archaeal alanine dehydrogenase homologous to ornithine cyclodeaminase and mu-crystallin. J Bacteriol. 2004 Nov;186(22):7680-9. PMID:15516582 doi:http://dx.doi.org/10.1128/JB.186.22.7680-7689.2004

1vll, resolution 2.80Å

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OCA