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
- Functionsamine dehydrogenase activity / aralkylamine dehydrogenase (azurin) activityComponentsperiplasmic 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
- Me-amine-dh_H (PF06433)
- Transmembrane Regions
- Not Available
- Cellular Location
- Periplasm
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P84888 UniProtKB Entry Name AAUB_ALCFA GenBank Gene ID AF302652 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]