Cloning and characterization of phosphomannose isomerase from Sphingomonas chungbukensis DJ77.

Abstract:

:Phosphomannose isomerase (PMI) catalyzes the interconversion of fructose-6-phosphate and mannose-6-phosphate in the extracellular polysaccharide (EPS) synthesis pathway. The gene encoding PMI in Sphingomonas chungbukensis DJ77 was cloned and expressed in E. coli. The pmi gene is 1,410 nucleotides long and the deduced amino acid sequence shares high homology with other bifunctional proteins that possess both PMI and GDP-mannose pyrophosphorylase (GMP) activities. The sequence analysis of PMI revealed two domains with three conserved motifs: a GMP domain at the N-terminus and a PMI domain at the C-terminus. Enzyme assays using the PMI protein confirmed its bifunctional activity. Both activities required divalent metal ions such as Co(2+), Ca(2+), Mg(2+), Ni(2+) or Zn(2+). Of these ions, Co(2+) was found to be the most effective activator of PMI. GDP-D-mannose was found to inhibit the PMI activity, suggesting feedback regulation of this pathway.

journal_name

BMB Rep

journal_title

BMB reports

authors

Tran ST,Le DT,Kim YC,Shin M,Choi JD

doi

10.5483/bmbrep.2009.42.8.523

subject

Has Abstract

pub_date

2009-08-31 00:00:00

pages

523-8

issue

8

eissn

1976-6696

issn

1976-670X

journal_volume

42

pub_type

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