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.

Reaction

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

     1 Oxidoreductases

         1.4 Acting on the CH-NH₂ group of donors

             1.4.9 With a copper protein as acceptor

                1.4.9.1 methylamine dehydrogenase (amicyanin)

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Results	in table
14	Activating Compound
573	AA Sequence
1	Application
2	CAS Registry Number
12	Cloned(Commentary)
38	Cofactor
16	Crystallization (Commentary)
1	Expression
9	General Information
4	General Stability
35	Inhibitors
88	KM Value [mM]
4	Localization
14	Metals/Ions
38	Molecular Weight [Da]
11	Natural Substrates/ Products (Substrates)
104	Organism
4	Pathway
20	PDB ID
9	pH Optimum
1	pH Range
2	pH Stability
7	Posttranslational Modification
20	Protein Variants
20	Purification (Commentary)
5	Reaction
5	Reaction Type
67	Reference
1	Source Tissue
8	Specific Activity [micromol/min/mg]
1	Storage Stability
104	Substrates and Products (Substrate)
26	Subunits
64	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
4	Temperature Stability [°C]
64	Turnover Number [1/s]

Engineering

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Engineering on EC 1.4.9.1 - methylamine dehydrogenase (amicyanin)

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

alphaF55A

4 entries

alphaF55I

3 entries

betaD32N

Paracoccus denitrificans

-

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

656282

betaD76N

Paracoccus denitrificans

-

mutant enzyme is completely inactive

656282

betaI107N

2 entries

betaI107V

2 entries

F55A

Paracoccus denitrificans

-

mutation of the alpha subunit

396586, 396587

F55E

Paracoccus denitrificans

-

mutation of the alpha subunit

396586

T122A

Paracoccus denitrificans

-

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

686067

K14E

Paracoccus versutus

-

mutation of cytochrome c-550

396583

K14Q

Paracoccus versutus

-

mutation of cytochrome c-550

396583

additional information

2 entries

alphaF55A

Paracoccus denitrificans

-

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

656086

alphaF55A

Paracoccus denitrificans

-

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

655553

alphaF55A

Paracoccus denitrificans

-

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

654866

alphaF55A

Paracoccus denitrificans

-

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

654628

alphaF55I

Paracoccus denitrificans

-

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

656086

alphaF55I

Paracoccus denitrificans

-

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

655553

alphaF55I

Paracoccus denitrificans

-

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

654866

betaI107N

Paracoccus denitrificans

-

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

654866

betaI107N

Paracoccus denitrificans

-

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

656086

betaI107V

Paracoccus denitrificans

-

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

654866

betaI107V

Paracoccus denitrificans

-

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

656086

additional information

Paracoccus denitrificans

P22619; P29894

generation of of the gene disrupted mutant strains PdDELTAqhpF, PdDELTAqhpG, and PdDELTAqhpR

741905

additional information

Paracoccus denitrificans

-

generation of of the gene disrupted mutant strains PdDELTAqhpF, PdDELTAqhpG, and PdDELTAqhpR

741905