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
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1.4.9.2
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methylamine
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ttq
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tryptophylquinone
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quinoproteins
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tunnel
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deamination
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tryptamine
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half-reaction
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ttq-dependent
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alcaligenes
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benzylamines
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faecalis
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breakage
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h-transfer
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phenylethylamines
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deflated
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structure-reactivity
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iminoquinone
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enzyme-catalysed
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amicyanin
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semi-classical
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interprotein
- 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
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Reaction
Reaction on EC 1.4.9.2 - aralkylamine dehydrogenase (azurin)
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ArCH2NH2 + H2O + 2 azurin = ArCHO + NH3 + 2 reduced azurin
ping-pong mechanism
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ArCH2NH2 + H2O + 2 azurin = ArCHO + NH3 + 2 reduced azurin
breakage of the substrate C-H bond occurs via quantum mechanical tunneling. In steady-state reactions with benzylamine, breakage of C-H bond is only partially rate-limiting
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ArCH2NH2 + H2O + 2 azurin = ArCHO + NH3 + 2 reduced azurin
mechanism. In presence of substrate a covalent N-semiquinone substrate adduct is observed. Tryptophan tryptophylquinone redox state influences interprotein electron transfer
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ArCH2NH2 + H2O + 2 azurin = ArCHO + NH3 + 2 reduced azurin
proton transfer occurs predominantly to oxygen O2 of D128 in beta subunit in a reaction dominated by tunneling over 0.6 Angstroms. Tunneling is promoted by a short-range motion modulating proton-acceptor distance and no long-range coupled motion is required
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ArCH2NH2 + H2O + 2 azurin = ArCHO + NH3 + 2 reduced azurin
ping-pong mechanism
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