Cloning and characterization of the gene encoding phosphoketolase in Leuconostoc mesenteroides isolated from kimchi

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...

Full description

Saved in:
Bibliographic Details
Published in:Biotechnology letters 2005-06, Vol.27 (12), p.853-858
Main Authors: JUNG MIN LEE, JEONG, Do-Won, OK KYUNG MIN JUNG KIM, LEE, Jong-Hoon, HAE CHOON CHANG, JEONG HWAN KIM, HYONG JOO LEE
Format: Article
Language:English
Subjects:
Acetic acid
Aldehyde-Lyases - genetics
Aldehyde-Lyases - metabolism
Amino Acid Sequence
Amino acids
Bacteria
Biological and medical sciences
Biotechnology
Cloning
Cloning, Molecular
DNA, Bacterial - chemistry
DNA, Bacterial - genetics
E coli
Enzymes
Escherichia coli
Fructosephosphates - metabolism
Fundamental and applied biological sciences. Psychology
Leuconostoc - enzymology
Leuconostoc - genetics
Leuconostoc - isolation & purification
Leuconostoc mesenteroides
Microbiology
Molecular Sequence Data
Pentosephosphates - metabolism
Sequence Alignment
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Substrate Specificity
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0141-5492
1573-6776
DOI:10.1007/s10529-005-6718-2