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Literature summary for 1.4.9.1 extracted from

  • Sun, D.; Chen, Z.W.; Mathews, F.S.; Davidson, V.L.
    Mutation of alphaPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyanin (2002), Biochemistry, 41, 13926-13933.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop method, crystal structure of alphaF55A in complex with its electron acceptors, amicyanin and cytochrome c-551i. Little difference in the overal structure is seen, relative to the native complex. There are significant changes in the solvent content of the active site and substrate channel. Crystal structure of alphaF55A with phenylhydrazine covalently bound to tryptophan tryptophylquinone in the active site Paracoccus denitrificans

Protein Variants

Protein Variants Comment Organism
alphaF55A mutation increases the rate of the electron transfer reaction from the fully reduced tryptophan tryptophylquinone tryptophan tryptophylquinone methylamine dehydrogenase to amicyanin. Little difference in the overal structure of alphaF55A in complex with its electron acceptors, amicyanin and cytochrome c-551i, relative to the native complex. There are significant changes in the solvent content of the active site and substrate channel Paracoccus denitrificans

Organism

Organism UniProt Comment Textmining
Paracoccus denitrificans
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methylamine + acceptor + H2O acceptor: amicyanin Paracoccus denitrificans formaldehyde + NH3 + reduced acceptor
-
?

Synonyms

Synonyms Comment Organism
MADH
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Paracoccus denitrificans

Cofactor

Cofactor Comment Organism Structure
tryptophan tryptophylquinone
-
Paracoccus denitrificans