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Literature summary for 1.1.2.7 extracted from

  • Zheng, Y.J.; Bruice, T.C.
    Conformation of coenzyme pyrroloquinoline quinone and role of Ca2+ in the catalytic mechanism of quinoprotein methanol dehydrogenase (1997), Proc. Natl. Acad. Sci. USA, 94, 11881-11886.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required for activity, overview Methylophilus methylotrophus

Organism

Organism UniProt Comment Textmining
Methylophilus methylotrophus P38539 and P38540 P38539 (large subunit, alpha) and P38540 (small subunit, beta)
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Methylophilus methylotrophus W3A1 P38539 and P38540 P38539 (large subunit, alpha) and P38540 (small subunit, beta)
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Synonyms

Synonyms Comment Organism
quinoprotein methanol dehydrogenase
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Methylophilus methylotrophus

Cofactor

Cofactor Comment Organism Structure
pyrroloquinoline quinone PQQ, tetrahedral configuration of the C-5 atom of PQQ, configuration and binding structure at the active site, ab initio structures of 2,7,9-tricarboxypyrroloquinoline quinone, semiquinone, and dihydroquinone, free and in complex with Ca2+, overview Methylophilus methylotrophus