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Literature summary for 1.1.1.71 extracted from

  • Korkhin, Y.; Kalb(Giloa), A.J.; Peretz, M.; Bogin, O.; Burstein, Y.; Frolow, F.
    NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii (1998), J. Mol. Biol., 278, 967-981.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
2.05 A resolution, tetramer of 222 symmetry, the monomer is composed of a cofactor-binding domain and a catalytic domain, it contains a single zinc atom in the putative active side, the tetramer is composed of two dimers Thermoanaerobacter brockii
2.15 A resolution, tetramer of 222 symmetry, the monomer is composed of a cofactor-binding domain and a catalytic domain, it contains a single zinc atom in the putative active side, the tetramer is composed of two dimers Clostridium beijerinckii

Organism

Organism UniProt Comment Textmining
Clostridium beijerinckii
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Thermoanaerobacter brockii
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Cofactor

Cofactor Comment Organism Structure
NADPH the specificity towards NADP(H) is determined by residues Gly198, Ser199, Arg200 and Tyr218 Clostridium beijerinckii
NADPH the specificity towards NADP(H) is determined by residues Gly198, Ser199, Arg200 and Tyr218 Thermoanaerobacter brockii