A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2009-12

AUTHORS

Bo Liu, Lei Wu, Tianming Liu, Ye Hong, Yulong Shen, Jinfeng Ni

ABSTRACT

A glycerate kinase gene (ST2037) from the hyperthermophilic crenarchaeon Sulfolobus tokodaii was cloned and expressed in Escherichia coli. The purified homodimeric protein (45 kDa) specifically catalyzed the formation of 2-phosphoglycerate with D-glycerate as substrate. The thermostable enzyme displayed maximum activity (over 20 min) at 90 degrees C and pH 4.5. The maximal activity was in the presence of Co(2+). The MOFRL family glycerate kinase used AMP as phosphate donor with maximal activity towards GTP. These characteristics of the enzyme suggested its potential in the catalytic production of 2-phosphoglycerate. More... »

PAGES

1937

Journal

TITLE

Biotechnology Letters

ISSUE

12

VOLUME

31

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10529-009-0089-z

DOI

http://dx.doi.org/10.1007/s10529-009-0089-z

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1013808905

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/19690808


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