Backbone assignments of the 34 kDa ketopantoate reductase from E. coli

Stephen J Headey; Amelia Vom; Jamie S Simpson; Martin J Scanlon

doi:10.1007/s12104-008-9093-9

Backbone assignments of the 34 kDa ketopantoate reductase from E. coli

Biomol NMR Assign. 2008 Jun;2(1):93-6. doi: 10.1007/s12104-008-9093-9. Epub 2008 Apr 26.

Authors

Stephen J Headey¹, Amelia Vom, Jamie S Simpson, Martin J Scanlon

Affiliation

¹ Medicinal Chemistry and Drug Action, Monash Institute of Pharmaceutical Sciences, Monash University (Parkville Campus), 381 Royal Parade, Parkville, VIC 3052, Australia.

PMID: 19636932
DOI: 10.1007/s12104-008-9093-9

Abstract

Ketopantoate reductase is an essential enzyme for pantothenate (vitamin B5) synthesis and a potential antibiotic target. Here we report the 15N and 1HN, 13C', 13C(alpha) and 13C(beta) chemical shift assignments of the 34 kDa ketopantoate reductase in its apo state.

MeSH terms

Alcohol Oxidoreductases / chemistry*
Amino Acid Sequence
Carbon Isotopes / chemistry
Escherichia coli / enzymology*
Escherichia coli Proteins / chemistry*
Magnetic Resonance Spectroscopy / methods*
Molecular Sequence Data
Molecular Weight
Nitrogen Isotopes / chemistry
Protons

Substances

Carbon Isotopes
Escherichia coli Proteins
Nitrogen Isotopes
Protons
Alcohol Oxidoreductases
2-dehydropantoate 2-reductase