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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Engineering
Engineering on EC 1.4.9.1 - methylamine dehydrogenase (amicyanin)
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alphaF55A
alphaF55I
betaD32N
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preparation contains a major species with six disulfides but no oxygen incorporated into betaTrp57 and a minor species with both oxygens incorporated, which is active. 1000fold increase in KM-value for methylamine
betaI107N
betaI107V
T122A
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the presence of Thr122 has a deleterious effect on the proton transfer step that is proposed to determine the rate of the reaction, the substitution of Thr122 by Ala does not significantly modify the preference of the proton by atom OD2 of Asp76
additional information
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1656fold increase in Km-value for methylamine compared to wild-type enzyme, 484fold increase in Km-value for ethylamine compared to wild-type enzyme, 36fold increase in Km-value for propylamine compared to wild-type enzyme, 3.6fold decrease in Km-value for butylamine compared to wild-type enzyme, 53.2fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 34.3fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 54.3fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme
alphaF55A
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inactivation by the mechanism-based inhibitor cyclopropylamine is accompanied by the formation of a covalent cross-link between the alpha and beta subunits of the enzyme. No cross-linking is seen with mutant enzymes alphaF55A or alphaF55I mutant enzymes
alphaF55A
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mutation decreases the affinity for binding of monovalent cations, Na+ or K+. 1656fold increase in Km-value for methylamine compared to wild-type enzyme, 484fold increase in Km-value for ethylamine compared to wild-type enzyme, 36fold increase in Km-value for propylamine compared to wild-type enzyme, 3.6fold decrease in Km-value for butylamine compared to wild-type enzyme, 53.2fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 34.3fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 54.3fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme
alphaF55A
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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
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1.2fold decrease in Km-value for methylamine compared to wild-type enzyme, 18.9fold increase in Km-value for ethylamine compared to wild-type enzyme, 5.6fold increase in Km-value for propylamine compared to wild-type enzyme, 4.2fold decrease in Km-value for butylamine compared to wild-type enzyme, 10fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 7.3fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 6.7fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzym. Ability to discriminate between amines of different chain length is abolished
alphaF55I
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inactivation by the mechanism-based inhibitor cyclopropylamine is accompanied by the formation of a covalent cross-link between the alpha and beta subunits of the enzyme. No cross-linking is seen with mutant enzymes alphaF55A or alphaF55I mutant enzymes
alphaF55I
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mutation has no effect on binding of monovalent cation. 1.2fold decrease in Km-value for methylamine compared to wild-type enzyme, 18.9fold increase in Km-value for ethylamine compared to wild-type enzyme, 5.6fold increase in Km-value for propylamine compared to wild-type enzyme, 4.2fold decrease in Km-value for butylamine compared to wild-type enzyme, 10fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 7.3fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 6.7fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme
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27.8fold increase in Km-value for methylamine compared to wild-type enzyme, 44.2fold increase in Km-value for ethylamine compared to wild-type enzyme, 8.5fold decrease in Km-value for propylamine compared to wild-type enzyme, 124fold decrease in Km-value for butylamine compared to wild-type enzyme, 62.5fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 23.2fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 5.6fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme
betaI107N
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27.8fold increase in Km-value for methylamine compared to wild-type enzyme, 44.2fold increase in Km-value for ethylamine compared to wild-type enzyme, 8.5fold decrease in Km-value for propylamine compared to wild-type enzyme, 124fold decrease in Km-value for butylamine compared to wild-type enzyme, 62.5fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 23.2fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 5.6fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme. Mutant enzyme exhibity a strong preference for 1-aminopentane compared to strong preference for methylamine of the wild-type enzyme
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7.7fold increase in Km-value for methylamine compared to wild-type enzyme, 17.9fold increase in Km-value for ethylamine compared to wild-type enzyme, 6fold decrease in Km-value for propylamine compared to wild-type enzyme, 9.9fold decrease in Km-value for butylamine compared to wild-type enzyme, 19.2fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 4.2fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 1.3fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme
betaI107V
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mutant enzyme exhibits a strong preference for propylamine compared to strong preference for methylamine of the wild-type enzyme. 7.7fold increase in Km-value for methylamine compared to wild-type enzyme, 17.9fold increase in Km-value for ethylamine compared to wild-type enzyme, 6fold decrease in Km-value for propylamine compared to wild-type enzyme, 9.9fold decrease in Km-value for butylamine compared to wild-type enzyme, 19.2fold decrease in Km-value for 1-aminopentane compared to wild-type enzyme, 4.2fold decrease in Km-value for 1-6-diaminohexane compared to wild-type enzyme, 1.3fold decrease in Km-value for 1,7-diaminoheptane compared to wild-type enzyme
generation of of the gene disrupted mutant strains PdDELTAqhpF, PdDELTAqhpG, and PdDELTAqhpR
additional information
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generation of of the gene disrupted mutant strains PdDELTAqhpF, PdDELTAqhpG, and PdDELTAqhpR