Log in to save to my catalogue

Coenzymes; Researchers from University of Tokai Describe Findings in Coenzymes

Coenzymes; Researchers from University of Tokai Describe Findings in Coenzymes

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_wirefeeds_858385984

Coenzymes; Researchers from University of Tokai Describe Findings in Coenzymes

About this item

Full title

Coenzymes; Researchers from University of Tokai Describe Findings in Coenzymes

Publisher

Atlanta: NewsRx

Journal title

Science Letter, 2011, p.178

Language

English

Publication information

Publisher

Atlanta: NewsRx

Subjects

Subjects and topics

More information

Scope and Contents

Contents

The expressed enzyme is the most thermostable L-lysine dehydrogenase yet described, with a half-life of 180 min at 100 degrees C. The product of the enzyme's catalytic activity is Delta(1)-piperideine-6-carboxylate, which makes this enzyme an L-lysine 6-dehydrogenase (EC 1.4.1.18) that catalyzes the reductive deamination of the epsilon-amino group...

Alternative Titles

Full title

Coenzymes; Researchers from University of Tokai Describe Findings in Coenzymes

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_wirefeeds_858385984

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_wirefeeds_858385984

Other Identifiers

ISSN

1538-9111

E-ISSN

1538-9162

How to access this item