PROPERTIES AND SEQUENCE OF THE COENZYME B-12-DEPENDENT GLYCEROL DEHYDRATASE OF CLOSTRIDIUM-PASTEURIANUM

Citation
L. Macis et al., PROPERTIES AND SEQUENCE OF THE COENZYME B-12-DEPENDENT GLYCEROL DEHYDRATASE OF CLOSTRIDIUM-PASTEURIANUM, FEMS microbiology letters, 164(1), 1998, pp. 21-28
Citations number
25
Categorie Soggetti
Microbiology
Journal title
ISSN journal
03781097
Volume
164
Issue
1
Year of publication
1998
Pages
21 - 28
Database
ISI
SICI code
0378-1097(1998)164:1<21:PASOTC>2.0.ZU;2-5
Abstract
The genes encoding coenzyme B-12-dependent glycerol dehydratase of Clo s:Clostridium pasteurianum were subcloned and expressed in Escherichia coli. The native molecular mass of the enzyme is 190 000 Da. The enzy me converts glycerol, 1,2-propanediol and 1.2-ethanediol to 3-hydroxyp ropionaldehyde, propionaldehyde and acetaldehyde, respectively, but gl ycerol is the preferred substrate. The nucleotide sequences of the dha BCE genes encoding the three subunits of glycerol dehydratase and of o rfZ whose function is unknown were determined. The deduced products of the dhaBCE genes with calculated molecular masses of 60 813. 19 549 a nd 16 722 Da, respectively, revealed high similarity to amino acid seq uences of subunits of coenzyme B-12-dependent glycerol and diol dehydr atases from other organisms. (C) 1998 Federation of European Microbiol ogical Societies. Published by Elsevier Science B.V. All rights reserv ed.