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

Crystallization and preliminary X-ray characterization of the 2,4'-dihydroxyacetophenone dioxygenase from Alcaligenes sp. 4HAP.
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产碱杆菌 2,4-二羟基苯乙酮双加氧酶的结晶和初步 X 射线表征。

DOI:
10.1107/s2053230x14009649
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发表时间:
2014
期刊:
Acta crystallographica. Section F, Structural biology communications
影响因子:
--
通讯作者:
Beaven G
Beaven G
中科院分区:
--
文献类型:
--
作者:
Beaven G

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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 Å.
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