1.4.9.1: methylamine dehydrogenase (amicyanin)
This is an abbreviated version!
For detailed information about methylamine dehydrogenase (amicyanin), go to the full flat file.
Word Map on EC 1.4.9.1
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1.4.9.1
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tryptophylquinone
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ttq
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paracoccus
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denitrificans
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maug
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quinoproteins
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diheme
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versutus
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bis-feiv
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protein-derived
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methylobacterium
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premadh
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thiobacillus
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davidson
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interprotein
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extorquens
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azurins
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quinol
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six-electron
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substrate-derived
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reorganizational
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n-methylglutamate
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n-butylamine
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diferrous
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aminoquinols
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high-valence
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methylomonas
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mathews
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analysis
- 1.4.9.1
- tryptophylquinone
- ttq
- paracoccus
- denitrificans
- maug
-
quinoproteins
-
diheme
- versutus
-
bis-feiv
-
protein-derived
- methylobacterium
-
premadh
-
thiobacillus
-
davidson
-
interprotein
- extorquens
- azurins
- quinol
-
six-electron
-
substrate-derived
-
reorganizational
- n-methylglutamate
- n-butylamine
-
diferrous
-
aminoquinols
-
high-valence
- methylomonas
-
mathews
- analysis
Reaction
+ + 2 amicyanin = + + 2 reduced amicyanin
Synonyms
amine dehydrogenase, amine: oxidoreductase (acceptor deaminating), dehydrogenase, amine, EC 1.4.98.1, EC 1.4.99.3, Heme 2, MADH, mauA, methylamine dehydrogenase, primary-amine dehydrogenase, QH-AmDH, QHNDH, quinohaemoprotein amine dehydrogenase, quinohemoprotein amine dehydrogenase, quinohemoprotein amine dehydrogenases, sQH-AmDH
ECTree
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Subunits
Subunits on EC 1.4.9.1 - methylamine dehydrogenase (amicyanin)
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dimer
heterotetramer
heterotrimer
monomer
tetramer
additional information
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anion-exchange chromatography and SDS-PAGE, 12000 Da and 42000 Da subunits
dimer
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anion-exchange chromatography and SDS-PAGE, 12000 Da and 42000 Da subunits
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heterotetramer
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alpha2beta2 protein, with each beta subunit possessing a tryptophan tryptophylquinone, TTQ, protein-derived cofactor
heterotetramer
alpha2beta2, 2 * 42500, alpha-subunit, + 2 * 14200, beta-subunit, SDS-PAGE
heterotetramer
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crystal structure, enzyme shows a alpha2beta2 structure, consisting of two heavy chains and two light chains, alpha subunit: 43300 Da, beta subunit: 14200 Da
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gel filtration, mass spectroscopy and UV-VIS spectroscopy: the gamma subunit of sQH-AmDH shows a sharp peak at 390 nm in UV-VIS spectrum clearly distinguishable from that of QH-AmDH. Electrospray ionization mass spectrometric analysis shows that the molecular mass of the gamma subunit of sQH-AmDH is larger than that of QH-AmDH by 15.6. The data suggest that the cysteine tryptophylquinone-like moiety (catalytic center) of the gamma subunit of sQH-AmDH is an oxime
heterotrimer
1 * 60000, alpha-subunit, + 1 * 37000, beta-subunit, + 1 * 9000, gamma-subunit, SDS-PAGE
heterotrimer
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1 * 53917 + 1 * 39234 + 1 * 8597, calculated from amino acid sequence
heterotrimer
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consists of a four-domain alpha-subunit (about 60000 Da) that harbors a di-heme cytochrome c, a seven-bladed beta-propeller beta-subunit(about 40000 Da) that provides part of the active site, and a small gamma-subunit (about 9000 Da) that contains the cofactor cysteine tryptophylquinone
heterotrimer
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determinated by in silico-experiments, beta-subunit with 349 aa, gamma-subunit with 79 aa and an alpha-subunit with 494 aa
tetramer
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
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2 * 14000 + 2 * 41000, X-ray crystallography
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MADH is a 114 kDa alpha2beta2 heterotetramer with two independent active sites, each containing a TTQ cofactor biosynthesized from betaTrp57 and betaTrp108 of the beta-subunit
additional information
MADH is a heterotetramer consisting of two alpha subunits and two beta subunits which are encoded by mauB and mauA, respectively
additional information
QHNDH is composed of three nonidentical subunits, designated alpha, beta, and gamma. The alpha subunit, the largest, has a four-domain structure with two heme c groups contained in the N-terminal diheme cytochrome c-like domain. The beta subunit has a seven-bladed beta propeller structure that is well-conserved across quinoproteins. The gamma subunit, the smallest of the three, is buried inside the alpha subunit. It has a particularly unusual structure consisting mostly of featureless coils with a covalently bound quinone cofactor, cysteine tryptophylquinone (CTQ), derived from Trp and Cys residues, and three intrapeptidyl thioether cross-links formed between Cys and Glu or Asp residues. The gamma subunit clearly indicate that it must undergo multiple posttranslational modifications before it can form an active QHNDH complex with the alpha and beta subunits
additional information
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QHNDH is composed of three nonidentical subunits, designated alpha, beta, and gamma. The alpha subunit, the largest, has a four-domain structure with two heme c groups contained in the N-terminal diheme cytochrome c-like domain. The beta subunit has a seven-bladed beta propeller structure that is well-conserved across quinoproteins. The gamma subunit, the smallest of the three, is buried inside the alpha subunit. It has a particularly unusual structure consisting mostly of featureless coils with a covalently bound quinone cofactor, cysteine tryptophylquinone (CTQ), derived from Trp and Cys residues, and three intrapeptidyl thioether cross-links formed between Cys and Glu or Asp residues. The gamma subunit clearly indicate that it must undergo multiple posttranslational modifications before it can form an active QHNDH complex with the alpha and beta subunits
additional information
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protein PeaB, although not interacting with the active QHNDH along the catalytic reaction, is needed for the correct functionality of this enzyme and for the post-translational modification of the gamma-subunit before its translocation to the periplasmic space.