Solution Structural Studies And Substrate Binding Properties Of The Amino-Terminal Domain Of E.coli Pantothenate Synthetase

Solution Structural Studies And Substrate Binding Properties Of The Amino-Terminal Domain Of E.coli Pantothenate Synthetase

Pantothenate synthetase (PS), which catalyzes the last step in the pantothenate (vitamin B5) biosynthesis, is a dimeric enzyme present in bacteria, fungi and plants. The enzymatic properties of PS from Escherichia Coli, Mycobacterium tuberculosi, Fusarium Oxysporum, Lotus japonicus, Oryza sativum, B...

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Bibliographic Details
Main Author: Chakrabarti, Kalyan Sundar
Other Authors: Sarma, Siddhartha P
Language:en_US
Published: 2011
Subjects:
Biosynthesis
Proteins - Biosynthesis
Pantothenate Synthetase (PS)
Nuclear Magnetic Resonance (NMR) Spectroscopy
Pantothenate Synthetase - NMR Spectroscopy
Protein Stability
E.Coli Pantothenate Synthetase
Allosteric Proteins
Protein Binding
Residual Dipolar Couplings
Apo-pantothenate Synthetase
Molecular Biology
Online Access:http://hdl.handle.net/2005/1103

Internet

http://hdl.handle.net/2005/1103

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