Bacillus subtilis YxaG is a novel Fe-containing quercetin 2,3-dioxygenase

被引：68

作者：

Bowater, L ^{[1
]}

Fairhurst, SA ^{[1
]}

Just, VJ ^{[1
]}

Bornemann, S ^{[1
]}

机构：

[1] John Innes Ctr, Dept Biol Chem, Norwich NR4 7UH, Norfolk, England

来源：

FEBS LETTERS | 2004年 / 557卷 / 1-3期

基金：

英国生物技术与生命科学研究理事会;

关键词：

quercetin 2,3-dioxygenase; prokaryote; flavonol; carbon monoxide production; iron; Bacillus subtilis;

D O I：

10.1016/S0014-5793(03)01439-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The Bacillus subtilis genome contains genes for three hypothetical proteins belonging to the bicupin family, two of which we have previously shown to be Mn(II)-dependent oxalate decarboxylases. We have now shown that the third, YxaG, exhibits quercetin 2,3-dioxygenase activity and that it contains Fe ions. This contrasts with the eukaryotic enzyme which contains a Cu ion. YxaG is the first prokaryotic carbon monoxide-forming enzyme that utilises a flavonol to be characterised and is only the second example of a prokaryotic dioxygenolytic carbon monoxide-forming enzyme known to contain a cofactor. It is proposed to rename the B. subtilis gene qdol (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：45 / 48

页数：4

共 32 条

[1] Structure of oxalate decarboxylase from Bacillus subtilis at 1.75 Å resolution [J].

Anand, R ;

Dorrestein, PC ;

Kinsland, C ;

Begley, TP ;

Ealick, SE .

BIOCHEMISTRY, 2002, 41 (24) :7659-7669

[2]

Ausubel FM., 1994, Curr. Protoc. Mol. Biol

[3] ELECTRONIC ABSORPTION-SPECTROSCOPY OF NONHEME IRON PROTEINS [J].

AVERILL, BA ;

VINCENT, JB .

METALLOBIOCHEMISTRY, PART C: SPECTROSCOPIC AND PHYSICAL METHODS FOR PROBING METAL ION ENVIRONMENTS IN METALLOENZYMES AND METALLOPROTEINS, 1993, 226 :33-51

[4] 2,4-Dioxyenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide - Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp Ru61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1 [J].

Bauer, I ;

Max, N ;

Fetzner, S ;

Lingens, F .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1996, 240 (03) :576-583

[5] MICROBIAL-METABOLISM OF QUINOLINE AND RELATED-COMPOUNDS .5. DEGRADATION OF 1H-4-OXOQUINOLINE BY PSEUDOMONAS-PUTIDA 33/1 [J].

BOTT, G ;

SCHMIDT, M ;

ROMMEL, TO ;

LINGENS, F .

BIOLOGICAL CHEMISTRY HOPPE-SEYLER, 1990, 371 (10) :999-1003

[6] Oxygenases:: mechanisms and structural motifs for O2 activation [J].

Bugg, TDH .

CURRENT OPINION IN CHEMICAL BIOLOGY, 2001, 5 (05) :550-555

[7] One protein, two enzymes [J].

Dai, Y ;

Wensink, PC ;

Abeles, RH .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (03) :1193-1195

[8] Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae [J].

Dai, Y ;

Pochapsky, TC ;

Abeles, RH .

BIOCHEMISTRY, 2001, 40 (21) :6379-6387

[9] Microbial relatives of the seed storage proteins of higher plants: Conservation of structure and diversification of function during evolution of the cupin superfamily [J].

Dunwell, JM ;

Khuri, S ;

Gane, PJ .

MICROBIOLOGY AND MOLECULAR BIOLOGY REVIEWS, 2000, 64 (01) :153-+

[10] Oxygenases without requirement for cofactors or metal ions [J].

Fetzner, S .

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 2002, 60 (03) :243-257

← 1 2 3 4 →