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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

Reaction

methylamine
+
H2O
+ 2 amicyanin =
formaldehyde
+
NH3
+ 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

     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)

Crystallization

Crystallization on EC 1.4.9.1 - methylamine dehydrogenase (amicyanin)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
one week in 19% PEG4000, 70 mM acetate buffer, pH 4.1
-
as MADH/amicyanin binary complex
-
crystals are grown in presence of 100 mM sodium citrate, pH 5.6, 18% PEG 4000 and 21% t-butyl alcohol. Complex of enzyme with the inhibitor phenylhydrazine determined at 1.7 A resolution
-
in complex with electron transfer protein amicyanin and with amicyanin mutant P52G. Model of electron transfer reaction between enzyme and amicyanin
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macroseeding using a 9-to-1 mixture of monobasic sodium (3 M) and dibasic potassium (3 M) phosphate solutions as precipitant
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MauG in complex with pre-methylamine dehydrogenase, hanging drop vapor diffusion method, using 23-25% (w/v) PEG 8000, 0.1 M sodium acetate, 0.1 M MES pH 6.4, at 20°C
MauG in complex with preMADH, X-ray diffraction structure determination and analysis at 2.1 resolution
MauG-pre-enzyme complex, hanging drop vapor diffusion method, using 0.1 M sodium acetate, 0.1 M MES pH 6.4, 22-26% PEG 8000
molecular dynamics simulations of the complex of redox proteins methylamine dehydrogenase and amicyanin to generate configurations over a duration of 40 ns in conjunction with an electron trnasfer pathway analysis. In the wild-type complex, the most frequently occurring molecular configurations afford superior electronic coupling due to the consistent presence of a water molecule hydrogen-bonded between the donor and acceptor sites. The water bridge function of nearby solvent-organizing residues by limiting the exchange of water molecules between the sterically constrained electron transfer region and the more turbulent surrounding bulk. When the water bridge is affected by a mutation, bulk solvent molecules disrupt it, resulting in reduced electronic coupling
-
preMADH complexed with MauG, X-ray diffraction structure determination and analysis at 2.1 A resolution
-
purified preenzyme pre-MADH in complex with activator mutant Q103N MauG, X-ray diffraction structure determination and analysis
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
-
MADH-amicyanin binary complex, hanging drop vapour diffusion method, in 28-29.5% PEG8000, 0.2 M Li2SO4, and 0.1 M phosphate (pH 6.5)
-
the crystal structure of the complex of MADH and amicyanin is determined to 2.5 A using the hanging-drop method. Enzyme is a heterotetramer consisting of two heavy chains and two light chains. The heavy chain of MADH folds into a characteristic, seven-blade beta-propeller domain and contains an N-terminal extension (residues 1-80) that wraps around the neighboring light chain, fixing it to the tetrameric enzyme. The light subunit consists mainly of loop regions with only four beta-strands, stabilized by a total of six disulfide bridges, containing the active site of the enzyme, a tryptophan tryptophylquinone moiety formed by Trp57 covalently linked to Trp108
-
hanging drop vapour diffusion method with 18% (w/v) polyethylene glycol 2000 monomethylether and 50 mM NiCl2
-