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Information on EC 1.4.9.2 - aralkylamine dehydrogenase (azurin) and Organism(s) Alcaligenes faecalis and UniProt Accession P84887
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1.4.9.2 aralkylamine dehydrogenase (azurin)IUBMB Comments
Phenazine methosulfate can act as acceptor. Acts on aromatic amines and, more slowly, on some long-chain aliphatic amines, but not on methylamine or ethylamine
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Word Map
- 1.4.9.2
- methylamine
- ttq
- tryptophylquinone
-
quinoproteins
-
tunnel
-
deamination
- tryptamine
-
half-reaction
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ttq-dependent
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alcaligenes
- benzylamines
- faecalis
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breakage
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h-transfer
- phenylethylamines
-
deflated
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structure-reactivity
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iminoquinone
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enzyme-catalysed
- amicyanin
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semi-classical
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interprotein
The taxonomic range for the selected organisms is: Alcaligenes faecalis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
aromatic amine dehydrogenase, tyramine dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AADH
aromatic amine dehydrogenase
dehydrogenase, arylamine
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tyramine dehydrogenase
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AADH
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aromatic amine dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
aralkylamaralkylamine:azurin oxidoreductase (deaminating)
Phenazine methosulfate can act as acceptor. Acts on aromatic amines and, more slowly, on some long-chain aliphatic amines, but not on methylamine or ethylamine
CAS REGISTRY NUMBER
COMMENTARY
85030-73-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzylamine + acceptor + H2O
benzaldehyde + NH3 + reduced acceptor
-
-
-
-
?
beta-phenylethylamine + acceptor + H2O
? + NH3 + reduced acceptor
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-
-
?
beta-phenylethylamine + H2O + 2,6-dichlorophenolindophenol
phenylacetaldehyde + NH3 + reduced 2,6-dichlorophenolindophenol
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-
-
-
?
dopamine + acceptor + H2O
4-(2-oxoethyl)-1,2-benzenediol + NH3 + reduced acceptor
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-
-
-
?
methylamine + acceptor + H2O
formaldehyde + NH3 + reduced acceptor
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-
-
-
?
phenazine ethosulfate + H2O + 2,6-dichlorophenol indophenol
? + NH3 + reduced 2,6-dichlorophenol indophenol
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-
-
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?
phenazine methosulfate + H2O + 2,6-dichlorophenol indophenol
? + NH3 + reduced 2,6-dichlorophenol indophenol
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-
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?
phenylethylamine + acceptor + H2O
phenylacetaldehyde + NH3 + reduced acceptor
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-
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?
serotonin + acceptor + H2O
3-(2-oxoethyl)-1H-indol-5-ol + NH3 + reduced acceptor
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-
-
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?
tryptamine + acceptor + H2O
1H-indole-3-acetaldehyde + NH3 + reduced acceptor
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-
-
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?
tyramine + H2O + 2,6-dichlorophenol indophenol
4-hydroxyphenylacetaldehyde + NH3 + reduced 2,6-dichlorophenol indophenol
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-
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-
?
ArCH2NH2 + H2O + 2 azurin
ArCHO + NH3 + 2 reduced azurin
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azurin markedly facilitates electron transfer from the enzyme to each cytochrome tested. AADH and azurin may form an electron transfer complex with a c-type cytochrome
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?
aromatic amines + acceptor + H2O
? + reduced acceptor + NH3
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physiological acceptor: azurin, not amicyanin
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?
aromatic amines + acceptor + H2O
? + reduced acceptor + NH3
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specific for phenylethylamines, but also reacts to a lesser extent with primary aliphatic amines
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?
benzylamine + H2O + 2,6-dichlorophenol
? + NH3 + reduced 2,6-dichlorophenol indophenol
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?
benzylamine + H2O + 2,6-dichlorophenol
? + NH3 + reduced 2,6-dichlorophenol indophenol
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analysis of limiting rate constants
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?
tyramine + acceptor + H2O
4-hydroxyphenylacetaldehyde + NH3 + reduced acceptor
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?
tyramine + acceptor + H2O
4-hydroxyphenylacetaldehyde + NH3 + reduced acceptor
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electron acceptor: azurin
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?
tyramine + acceptor + H2O
4-hydroxyphenylacetaldehyde + NH3 + reduced acceptor
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electron acceptor: phenazine methosulfate or phenazine ethosulfate
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?
additional information
?
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para-substituted benzylamines like 4-methylbenzylamine, 4-nitrobenzylamine, 4-methoxybenzylamine, 4-fluorobenzylamine, 4-chlorobenzylamine, and 4-bromobenzylamine are poor reactivity probes for AADH
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
aromatic amines + acceptor + H2O
? + reduced acceptor + NH3
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physiological acceptor: azurin, not amicyanin
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tryptophan tryptophylquinone
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two molecules per enzyme, tryptophan tryptophylquinone reduction is about 80 times more rapid with tryptamine compared to beta-phenylethylamine
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
analysis of limiting rate constants of reaction with benzylamine and deuterated benzylamine at different pH values
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
during phenylethylamine-dependent growth, aromatic amine dehydrogenase, azurin, and a single cytochrome c are localized in the periplasm
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19652
alpha2beta2, 2 * 38222 + 2 * 19652, calculated from DNA sequence
38222
alpha2beta2, 2 * 38222 + 2 * 19652, calculated from DNA sequence
46000
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alpha2beta2, 2 * 46000 + 2 * 8000, high speed gel filtration in 6 M guanidine hydrochloride
8000
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alpha2beta2, 2 * 46000 + 2 * 8000, high speed gel filtration in 6 M guanidine hydrochloride
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
tetramer
tetramer
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alpha2beta2, 2 * 46000 + 2 * 8000, high speed gel filtration in 6 M guanidine hydrochloride
tetramer
alpha2beta2, 2 * 38222 + 2 * 19652, calculated from DNA sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
electron transfer complex between aromatic amine dehydrogenase and azurin. The interface of the proteins is largely hydrophobic, covering 500 squareAngstrom, with one direct hydrogen bond linking them
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structure of the O-quinol, N-quinol, and N-semiquinone forms of enzyme
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nozaki, M.
Aromatic amine dehydrogenase from Alcaligenes faecalis
Methods Enzymol.
142
650-655
1987
Alcaligenes faecalis, Alcaligenes faecalis IFO 14479
Govindaraj, S.; Eisenstein, E.; Jones, L.H.; Sanders-Loehr, J.; Chistoserdov, A.Y.; Davidson, V.L.; Edwards, S.L.
Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme
J. Bacteriol.
176
2922-2929
1994
Alcaligenes faecalis, Alcaligenes faecalis IFO 14479
Hyun, Y.L.; Davidson, V.L.
Electron transfer reactions between aromatic amine dehydrogenase and azurin
Biochemistry
34
12249-12254
1995
Alcaligenes faecalis, Alcaligenes faecalis IFO 14479
Hyun, Y.L.; Davidson, V.L.
Unusually large isotope effect for the reaction of aromatic amine dehydrogenase. A common feature of quinoproteins?
Biochim. Biophys. Acta
1251
198-200
1995
Alcaligenes faecalis, Alcaligenes faecalis IFO 14479
Hyun, Y.L.; Zhu, Z.; Davidson, V.L.
Gated and ungated electron transfer reactions from aromatic amine dehydrogenase to azurin
J. Biol. Chem.
274
29081-29086
1999
Alcaligenes faecalis, Alcaligenes faecalis IFO 14479
Chistoserdov, A.Y.
Cloning, sequencing and mutagenesis of the genes for aromatic amine dehydrogenase from Alcaligenes faecalis and evolution of amine dehydrogenases
Microbiology
147
2195-2202
2001
Achromobacter xylosoxidans, Alcaligenes faecalis (P84887 and P84888), Alcaligenes faecalis
Sukumar, N.; Chen, Z.W.; Ferrari, D.; Merli, A.; Rossi, G.L.; Bellamy, H.D.; Chistoserdov, A.; Davidson, V.L.; Mathews, F.S.
Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis
Biochemistry
45
13500-13510
2006
Alcaligenes faecalis
Hothi, P.; Abu Khadra, K.; Combe, J.P.; Leys, D.; Scrutton, N.S.
Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans. [Erratum to document cited in CA144:14530]
FEBS J.
273
430
2006
Alcaligenes faecalis
Roujeinikova, A.; Scrutton, N.S.; Leys, D.
Atomic level insight into the oxidative half-reaction of aromatic amine dehydrogenase
J. Biol. Chem.
281
40264-40272
2006
Alcaligenes faecalis
Massgrau, L.; Roujeinikova, A.; Johannissen, L.O.; Hothi, P.; Basran, J.; Ranaghan, K.E.; Mulholland, A.J.; Sutcliffe, M.J.; Scrutton, N.S.; Leys, D.
Atomic description of an enzyme reaction dominated by proton tunneling.
Science
312
237-241
2006
Alcaligenes faecalis
Hothi, P.; Roujeinikova, A.; Khadra, K.A.; Lee, M.; Cullis, P.; Leys, D.; Scrutton, N.S.
Isotope effects reveal that para-substituted benzylamines are poor reactivity probes of the quinoprotein mechanism for aromatic amine dehydrogenase
Biochemistry
46
9250-9259
2007
Alcaligenes faecalis, Alcaligenes faecalis IFO 14479
Hothi, P.; Lee, M.; Cullis, P.M.; Leys, D.; Scrutton, N.S.
Catalysis by the isolated tryptophan tryptophylquinone-containing subunit of aromatic amine dehydrogenase is distinct from native enzyme and synthetic model compounds and allows further probing of TTQ mechanism
Biochemistry
47
183-194
2008
Alcaligenes faecalis, Alcaligenes faecalis IFO 14479
Roujeinikova, A.; Hothi, P.; Masgrau, L.; Sutcliffe, M.J.; Scrutton, N.S.; Leys, D.
New insights into the reductive half-reaction mechanism of aromatic amine dehydrogenase revealed by reaction with carbinolamine substrates
J. Biol. Chem.
282
23766-23777
2007
Alcaligenes faecalis, Alcaligenes faecalis IFO 14479
Zhu, Z.; Sun, D.; Davidson, V.L.
Localization of periplasmic redox proteins of Alcaligenes faecalis by a modified general method for fractionating gram-negative bacteria
J. Bacteriol.
181
6540-6542
1999
Alcaligenes faecalis
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