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methylamine dehydrogenase

Known as: primary-amine dehydrogenase 
National Institutes of Health

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2 relations

Broader (1)

Oxidoreductases Acting on CH-NH Group Donors
amine dehydrogenase activity

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2012
2012
Characterization of electron tunneling and hole hopping reactions between different forms of MauG and methylamine dehydrogenase within a natural protein complex.
Respiration, photosynthesis, and metabolism require the transfer of electrons through and between proteins over relatively long… 
2011
2011
Crystal structures of CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: implications for the mechanism of dioxygen activation.
MauG is a diheme enzyme responsible for the post-translational formation of the catalytic tryptophan tryptophylquinone (TTQ… 
2003
2003
Understanding quinone cofactor biogenesis in methylamine dehydrogenase through novel cofactor generation.
Cofactors made from constitutive amino acids in proteins are now known to be relatively common. A number of these involve the… 
2002
2002
Improved sensitivity of a histamine sensor using an engineered methylamine dehydrogenase.
Methylamine dehydrogenase (MADH) may be immobilized in a polypyrrole (PPy) film on an electrode surface and used as an… 
2002
2002
Mutation of alphaPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyanin.
Methylamine dehydrogenase (MADH) possesses an alpha(2)beta(2) structure with each smaller beta subunit possessing a tryptophan… 
2000
2000
Conversion of methylamine dehydrogenase to a long-chain amine dehydrogenase by mutagenesis of a single residue.
Methylamine dehydrogenase (MADH) is a tryptophan tryptophylquinone (TTQ) dependent enzyme that catalyzes the oxidative… 
Highly Cited
1998
Highly Cited
1998
Molecular basis for interprotein complex-dependent effects on the redox properties of amicyanin.
The quinoprotein methylamine dehydrogenase (MADH), type I copper protein amicyanin, and cytochrome c-551i form a complex within… 
1998
1998
Electron transfer from the aminosemiquinone reaction intermediate of methylamine dehydrogenase to amicyanin.
The tryptophan tryptophylquinone (TTQ) cofactor of methylamine dehydrogenase (MADH) is covalently modified by substrate-derived… 
1994
1994
Kinetic and thermodynamic analysis of a physiologic intermolecular electron-transfer reaction between methylamine dehydrogenase and amicyanin.
The quinoprotein methylamine dehydrogenase (MADH) and a type I copper protein, amicyanin, form a physiologic complex in which… 
1994
1994
The effects of pH and cations on the spectral and kinetic properties of methylamine dehydrogenase from Thiobacillus versutus.
The catalytic parameters of Thiobacillus versutus methylamine dehydrogenase (MADH) with the physiological substrates methylamine… 
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