The thermostable allosteric nature of fructose 1,6-diphosphatase from an extreme thermophile.

Biochemical and biophysical research communications ·Vol. 45 ·No. 2 ·1971-10-15 ·Pages 495-500

Yoshida M, Oshima T

Abstract

暂无摘要

MeSH Terms

Adenosine Monophosphate Allosteric Regulation Drug Stability Enzyme Activation Flavobacterium/enzymology Fructose-Bisphosphatase/antagonists & inhibitors Fructosephosphates Hot Temperature Hydrogen-Ion Concentration Kinetics Magnesium Manganese Nitrophenols Phosphoenolpyruvate Phosphoric Acids Phosphoric Monoester Hydrolases/isolation & purification

Chemicals

Fructosephosphates Nitrophenols Phosphoric Acids Adenosine Monophosphate Manganese Phosphoenolpyruvate Fructose-Bisphosphatase Phosphoric Monoester Hydrolases Magnesium

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Yoshida M

Oshima T

Article Info

Journal

Biochemical and biophysical research communications

Abbr.

Biochem Biophys Res Commun

ISSN

0006-291X

DOI

10.1016/0006-291x(71)90846-1

Published

1971-10-15

Pages

495-500

Language

English

Region

United States

NLM ID

0372516

Subset

External Links

PubMed source DOI: 10.1016/0006-291x(71)90846-1 View journal details

Analysis Services

The thermostable allosteric nature of fructose 1,6-diphosphatase from an extreme thermophile.

Contact

WeChat Official Account