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- Title
Cloning and characterization of the gene encoding phosphoketolase in Leuconostoc mesenteroides isolated from kimchi.
- Authors
Jung Min Lee; Do-Won Jeong; Ok Kyung Min Jung Kim; Jong-Hoon Lee; Hae Choon Chang; Jeong Hwan Kim; Hyong Joo Lee
- Abstract
The gene encoding phosphoketolase, which is 2749 bp long and contains 814 amino acid polypeptides with a total molecular mass of 91.9 kDa, was cloned from Leuconostoc mesenteroides C7 (LMC7) and expressed in Escherichia coli. It exhibited a homology of >58% with phosphoketolases from other lactic acid bacteria. The phosphoketolase of LMC7 belongs to the xylulose 5-phosphate (X5P)/fructose 6-phosphate (F6P) phosphoketolase (Xfp) family, which is an enzyme with dual specificity for X5P and F6P. The members of this family contain typical thiamin pyrophosphate (TPP) binding sites as reported for other TPP-dependent enzymes, and several highly conserved regions as signature patterns for phosphoketolases. The plasmid pGPK containing the Xfp gene ( xfp) exhibits phosphoketolase activity in E. coli. The specific activities of the enzyme from E. coli BL21 and E. coli EC101 harboring xfp were 0.28 and 0.14 units/mg, respectively. They both exhibited a 1.5-fold increase in the production of acetic acid from acetyl phosphate compared with their corresponding original strain.
- Subjects
LEUCONOSTOC; KIMCHI; AMINO acids; ESCHERICHIA coli; THIAMIN pyrophosphate
- Publication
Biotechnology Letters, 2005, Vol 27, Issue 12, p853
- ISSN
0141-5492
- Publication type
Article
- DOI
10.1007/s10529-005-6718-2