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PMID: 3001029 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Purification and properties of shikimate kinase II from Escherichia coli K-12.

Journal of bacteriology ·Vol. 165 ·No. 1 ·1986-01-00 ·Pages 331-3

DeFeyter RC, Pittard J

Abstract

Shikimate kinase II was purified to near homogeneity from an Escherichia coli strain which overproduced the enzyme. The apparent Km of this isoenzyme for shikimate was 200 microM, and for ATP it was 160 microM. The Km for shikimate is approximately 100-fold lower than the Km of shikimate kinase I, suggesting that shikimate kinase II is the isoenzyme normally functioning in aromatic biosynthesis. Shikimate kinase II is dependent on metal ions for activity.

MeSH Terms
Amino Acid Sequence Escherichia coli/enzymology Isoenzymes/isolation & purification Kinetics Phosphotransferases/analysis,antagonists & inhibitors,isolation & purification Phosphotransferases (Alcohol Group Acceptor)
Chemicals
Isoenzymes Phosphotransferases Phosphotransferases (Alcohol Group Acceptor) shikimate kinase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
DeFeyter R C
Pittard J
References (7)
7 references, click to expand
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    J Bacteriol. 1986 Jan;165(1):226-32 PMID: 3001024
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  6. [The biosynthesis of beta-galactosidase (lactase) in Escherichia coli; the specificity of induction].
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  7. Protein measurement with the Folin phenol reagent.
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1986-01-00
Pages
331-3
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC214414
Subset
IM
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