SEQUENCE AND CRYSTALLIZATION OF ESCHERICHIA-COLI DETHIOBIOTIN SYNTHETASE, THE PENULTIMATE ENZYME OF BIOTIN BIOSYNTHESIS

被引：16

作者：

ALEXEEV, D

BURY, SM

BOYS, CWG

TURNER, MA

SAWYER, L

RAMSEY, AJ

BAXTER, HC

BAXTER, RL

机构：

[1] UNIV EDINBURGH,DEPT BIOCHEM,EDINBURGH CTR MOLEC RECOGNIT,HUGH ROBSON BLDG,GEORGE SQ,EDINBURGH EH8 9XD,SCOTLAND

[2] UNIV EDINBURGH,EDINBURGH CTR MOLEC RECOGNIT,DEPT CHEM,EDINBURGH EH9 3JX,SCOTLAND

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1994年 / 235卷 / 02期

关键词：

DETHIOBIOTIN SYNTHETASE; CRYSTALLIZATION; SEQUENCE;

D O I：

10.1006/jmbi.1994.1030

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 enzyme dethiobiotin synthetase (EC 6.3.3.3) has been cloned and over- expressed in Escherichia coli in such a way that milligram quantities are available. The purified enzyme has been subjected to a number of physical and chemical studies, sequenced and most notably it has been crystallized in a form that is suitable for X-ray structure determination. The cell dimensions are a = 72·8 å, b = 49·2 å, c = 61·4 å, β = 106·2°. The systematic absences are consistent with the monoclinic space group C2 with one polypeptide chain in the asymmetric unit. © 1994 Academic Press Limited.

引用

页码：774 / 776

页数：3

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