Crystallization and preliminary X-ray characterization of the 2,4′-dihydroxyacetophenone dioxygenase from Alcaligenes sp 4HAP

被引：4

作者：

Beaven, G. ^{[1
]}

Bowyer, A. ^{[1
]}

Erskine, P. ^{[2
]}

Wood, S. P. ^{[2
]}

McCoy, A. ^{[3
]}

Coates, L. ^{[4
]}

Keegan, R. ^{[5
]}

Lebedev, A. ^{[5
]}

Hopper, D. J. ^{[6
]}

Kaderbhai, M. A. ^{[6
]}

Cooper, J. B. ^{[2
]}

机构：

[1] Univ Southampton, Sch Biol Sci, Southampton, Hants, England

[2] UCL Div Med, Ctr Amyloidosis & Acute Phase Prot, Lab Prot Crystallog, London NW3 2PF, England

[3] Univ Cambridge, Cambridge Inst Med Res, Cambridge, England

[4] Oak Ridge Natl Lab, Oak Ridge, TN USA

[5] STFC Rutherford Appleton Lab, RAL, Didcot OX11 0FA, Oxon, England

[6] Aberystwyth Univ, Inst Biol Environm & Rural Sci, Aberystwyth SY23 3DA, Dyfed, Wales

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2014年 / 70卷

基金：

英国生物技术与生命科学研究理事会;

关键词：

ENZYME;

D O I：

10.1107/S2053230X14009649

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The enzyme 2,4'-dihydroxyacetophenone dioxygenase (or DAD) catalyses the conversion of 2,4'-dihydroxyacetophenone to 4-hydroxybenzoic acid and formic acid with the incorporation of molecular oxygen. Whilst the vast majority of dioxygenases cleave within the aromatic ring of the substrate, DAD is very unusual in that it is involved in C-C bond cleavage in a substituent of the aromatic ring. There is evidence that the enzyme is a homotetramer of 20.3 kDa subunits each containing nonhaem iron and its sequence suggests that it belongs to the cupin family of dioxygenases. By the use of limited chymotrypsinolysis, the DAD enzyme from Alcaligenes sp. 4HAP has been crystallized in a form that diffracts synchrotron radiation to a resolution of 2.2 angstrom.

引用

页码：823 / 826

页数：4

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