Aralkylamine dehydrogenase heavy chain

Details

Name
Aralkylamine dehydrogenase heavy chain
Synonyms
  • 1.4.9.2
  • AADH
  • Aromatic amine dehydrogenase
Gene Name
aauB
Organism
Alcaligenes faecalis
Amino acid sequence
>lcl|BSEQ0022108|Aralkylamine dehydrogenase heavy chain
MKSKFKLTTAAAMLGLMVLAGGAQAQDKPREVLTGGHSVSAPQENRIYVMDSVFMHLTES
RVHVYDYTNGKFLGMVPTAFNGHVQVSNDGKKIYTMTTYHERITRGKRSDVVEVWDADKL
TFEKEISLPPKRVQGLNYDGLFRQTTDGKFIVLQNASPATSIGIVDVAKGDYVEDVTAAA
GCWSVIPQPNRPRSFMTICGDGGLLTINLGEDGKVASQSRSKQMFSVKDDPIFIAPALDK
DKAHFVSYYGNVYSADFSGDEVKVDGPWSLLNDEDKAKNWVPGGYNLVGLHRASGRMYVF
MHPDGKEGTHKFPAAEIWVMDTKTKQRVARIPGRDALSMTIDQQRNLMLTLDGGNVNVYD
ISQPEPKLLRTIEGAAEASLQVQFHPVGGV
Number of residues
390
Molecular Weight
42924.595
Theoretical pI
7.36
GO Classification
Functions
amine dehydrogenase activity / aralkylamine dehydrogenase (azurin) activity
Components
periplasmic space
General Function
Aralkylamine dehydrogenase (azurin) activity
Specific Function
Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP84888
UniProtKB Entry NameAAUB_ALCFA
GenBank Gene IDAF302652
General References
  1. Chistoserdov AY: Cloning, sequencing and mutagenesis of the genes for aromatic amine dehydrogenase from Alcaligenes faecalis and evolution of amine dehydrogenases. Microbiology. 2001 Aug;147(Pt 8):2195-202. [Article]
  2. Hothi P, Khadra KA, Combe JP, Leys D, Scrutton NS: Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans. FEBS J. 2005 Nov;272(22):5894-909. [Article]
  3. Govindaraj S, Eisenstein E, Jones LH, Sanders-Loehr J, Chistoserdov AY, Davidson VL, Edwards SL: Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme. J Bacteriol. 1994 May;176(10):2922-9. [Article]
  4. Edwards SL, Davidson VL, Hyun YL, Wingfield PT: Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes. J Biol Chem. 1995 Mar 3;270(9):4293-8. [Article]
  5. Bishop GR, Zhu Z, Whitehead TL, Hicks RP, Davidson VL: Identification of reaction products and intermediates of aromatic-amine dehydrogenase by 15N and 13C NMR. Biochem J. 1998 Mar 15;330 ( Pt 3):1159-63. [Article]
  6. Zhu Z, Sun D, Davidson VL: Localization of periplasmic redox proteins of Alcaligenes faecalis by a modified general method for fractionating gram-negative bacteria. J Bacteriol. 1999 Oct;181(20):6540-2. [Article]
  7. Sukumar N, Chen ZW, Ferrari D, Merli A, Rossi GL, Bellamy HD, Chistoserdov A, Davidson VL, Mathews FS: Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis. Biochemistry. 2006 Nov 14;45(45):13500-10. [Article]
  8. Roujeinikova A, Scrutton NS, Leys D: Atomic level insight into the oxidative half-reaction of aromatic amine dehydrogenase. J Biol Chem. 2006 Dec 29;281(52):40264-72. Epub 2006 Sep 27. [Article]
  9. Masgrau L, Roujeinikova A, Johannissen LO, Hothi P, Basran J, Ranaghan KE, Mulholland AJ, Sutcliffe MJ, Scrutton NS, Leys D: Atomic description of an enzyme reaction dominated by proton tunneling. Science. 2006 Apr 14;312(5771):237-41. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB08649(1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOLexperimentalunknownDetails
DB08652IndoleacetamideexperimentalunknownDetails
DB08653TryptamineexperimentalunknownDetails
DB087672-(4-METHOXYPHENYL)ACETAMIDEexperimentalunknownDetails