1ped

From Proteopedia

BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM)

Structural highlights

1ped is a 4 chain structure with sequence from Clostridium beijerinckii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.15Å
Ligands:	ZN
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ADH_CLOBE Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is active with acetaldehyde and propionaldehyde.^[1] ^[2]

Evolutionary Conservation

Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Ismaiel AA, Zhu CX, Colby GD, Chen JS. Purification and characterization of a primary-secondary alcohol dehydrogenase from two strains of Clostridium beijerinckii. J Bacteriol. 1993 Aug;175(16):5097-105. PMID:8349550
↑ Goihberg E, Peretz M, Tel-Or S, Dym O, Shimon L, Frolow F, Burstein Y. Biochemical and Structural Properties of Chimeras Constructed by Exchange of Cofactor-Binding Domains in Alcohol Dehydrogenases from Thermophilic and Mesophilic Microorganisms. Biochemistry. 2010 Feb 9. PMID:20102159 doi:10.1021/bi901730x

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 See Also
5 References

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PDB ID 1ped

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Categories: Clostridium beijerinckii | Large Structures | Frolow F | Korkhin Y

1ped

From Proteopedia

BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM)

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

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