DIENELACTONE HYDROLASE FROM RHODOCOCCUS-ERYTHROPOLIS-1-CP - PURIFICATION AND PROPERTIES

被引：9

作者：

MALTSEVA, OV

SOLYANIKOVA, IP

GOLOVLEVA, LA

SCHLOMANN, M

KNACKMUSS, HJ

机构：

[1] RUSSIAN ACAD SCI, INST BIOCHEM & PHYSIOL MICROORGANISMS, PUSHCHINO 142292, RUSSIA

[2] UNIV STUTTGART, INST MIKROBIOL, D-70569 STUTTGART, GERMANY

来源：

ARCHIVES OF MICROBIOLOGY | 1994年 / 162卷 / 05期

关键词：

DIENELACTONE HYDROLASE; RHODOCOCCUS ERYTHROPOLIS; ORTHO-CLEAVAGE PATHWAY (MODIFIED); CHLOROCATECHOL DEGRADATION;

D O I：

10.1007/s002030050152

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Dienelactone hydrolases (EC 3.1.1.45) have been shown to play an indispensable role in the degradation of chloroaromatic compounds via ortho-cleavage of chlorocatechols. We report on the purification of dienelactone hydrolase of the chlorophenol-utilizing strain Rhodococcus erythropolis 1CP to apparent homogeneity. Dienelactone hydrolase differed from the corresponding enzymes of other chloroaromatic compound-catabolizing strains in being restricted to substrates with a cis-dienelactone structure. From the cis-dienelactone-hydrolyzing enzyme of a 4-fluorobenzoate-utilizing Burkholderia (Pseudomonas) cepacia strain, it differed considerably in properties such as pH optimum of activity, inhibition by p-chloromercuribenzoate, and amino acid composition. Thus, there is not necessarily a close relationship between substrate specificity and other properties of dienelactone hydrolases.

引用

页码：368 / 374

页数：7

共 42 条

[1] PURIFICATION OF 3,5-DICHLOROCATECHOL 1,2-DIOXYGENASE, A NONHEME IRON DIOXYGENASE AND A KEY ENZYME IN THE BIODEGRADATION OF A HERBICIDE, 2,4-DICHLOROPHENOXYACETIC ACID (2,4-D), FROM PSEUDOMONAS-CEPACIA CSV90 [J].