1.4.9.2: aralkylamine dehydrogenase (azurin)

This is an abbreviated version!
For detailed information about aralkylamine dehydrogenase (azurin), go to the full flat file.

Word Map on EC 1.4.9.2

1.4.9.2

methylamine

ttq

tryptophylquinone

quinoproteins

tunnel

deamination

tryptamine

half-reaction

ttq-dependent

alcaligenes

benzylamines

faecalis

breakage

h-transfer

phenylethylamines

deflated

structure-reactivity

iminoquinone

enzyme-catalysed

amicyanin

semi-classical

interprotein

Reaction

+ 2 azurin =

+ 2 reduced azurin

Synonyms

AADH, AauA, AauB, AMDH, aromatic amine dehydrogenase, dehydrogenase, arylamine, EC 1.4.99.4, quinohemoprotein amine dehydrogenase, tyramine dehydrogenase

ECTree

1 Oxidoreductases

1.4 Acting on the CH-NH₂ group of donors

1.4.9 With a copper protein as acceptor

1.4.9.2 aralkylamine dehydrogenase (azurin)

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Results	in table
129	AA Sequence
1	CAS Registry Number
1	Cloned(Commentary)
10	Cofactor
8	Crystallization (Commentary)
1	General Stability
37	Inhibitors
3	Ki Value [mM]
18	KM Value [mM]
3	Localization
2	Metals/Ions
21	Molecular Weight [Da]
7	Natural Substrates/ Products (Substrates)
86	Organism
5	Pathway
3	pH Optimum
1	pH Range
1	pH Stability
8	Purification (Commentary)
6	Reaction
4	Reaction Type
30	Reference
5	Source Tissue
9	Specific Activity [micromol/min/mg]
1	Storage Stability
95	Substrates and Products (Substrate)
14	Subunits
24	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
1	Temperature Range [°C]
4	Temperature Stability [°C]
6	Turnover Number [1/s]

Cofactor

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Cofactor on EC 1.4.9.2 - aralkylamine dehydrogenase (azurin)

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heme c

Pseudomonas putida

P0A182

two mol of heme per mole of AMDH, 60 kDa subunit carries heme c. Typical absorption stectrum shows maxima at 554, 522, 420, and 320 nm in the reduced state and one peak at 410 nm, a shoulder at 350 nm, and a braod hill at 530 nm in the oxidized form

714515

tryptophan tryptophylquinone

4 entries

additional information

Alcaligenes faecalis

probably chromophore with quinone structure

396589