Steady state kinetics of mannitol phosphorylation catalyzed by enzyme IImtl of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system.-Reference-Cited by-同舟云学术

Steady state kinetics of mannitol phosphorylation catalyzed by enzyme IImtl of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system.

Published:1993-08 Issue:24 Volume:268 Page:17844-17849
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Lolkema J.S.,ten Hoeve-Duurkens R.H.,Robillard G.T.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference20 articles.

1. Phosphoenolpyruvate:carbohydrate phosphotransferase system of bacteria

2. Chapter 5 The Enzymes II of the phosphoenol-pyruvate-dependent carbohydrate transport systems

3. Mannitol-specific enzyme II of the bacterial phosphotransferase system. I. Properties of the purified permease.

4. Kinetics and subunit interaction of the mannitol-specific enzyme II of the Escherichia coli phosphotransferase system

5. Enzyme II of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: protein-protein and protein-phospholipid interactions

Cited by 11 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. The Bacterial Phosphoenolpyruvate:Carbohydrate Phosphotransferase System: Regulation by Protein Phosphorylation and Phosphorylation-Dependent Protein-Protein Interactions;Microbiology and Molecular Biology Reviews;2014-06

2. Transient State Kinetics of Enzyme IICBGlc, a Glucose Transporter of the Phosphoenolpyruvate Phosphotransferase System of Escherichia coli;Journal of Biological Chemistry;2005-12

3. Stoichiometry and Substrate Affinity of the Mannitol Transporter, EnzymeIImtl, from Escherichia coli;Biophysical Journal;2005-07

4. Characterization of Soluble Enzyme II Complexes of the Escherichia coli Phosphotransferase System;Journal of Bacteriology;2004-12-15

5. Kinetic Modelling as a Modern Technology to Explore and Modify Living Cells;Natural Computing Series;2004