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Archives of Biochemistry and Biophysics

Volumn 539, Issue 1, 2013, Pages 70-80

Redesign of MST enzymes to target lyase activity instead promotes mutase and dehydratase activities

(3) Meneely, Kathleen M a Luo, Qianyi a Lamb, Audrey L a

a UNIVERSITY OF KANSAS (United States)

Author keywords

Enzyme engineering; Isochorismate synthase; Salicylate synthase; Siderophore biosynthesis

Indexed keywords

HYDROLYASE; LYASE; MORPHINE SULFATE; MUTASE; PHENYLPYRUVIC ACID; SALICYLIC ACID;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ENGINEERING; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; NONHUMAN; PRIORITY JOURNAL; STEADY STATE;

ENZYME ENGINEERING; ISOCHORISMATE SYNTHASE; SALICYLATE SYNTHASE; SIDEROPHORE BIOSYNTHESIS;

BACTERIAL PROTEINS; CATALYTIC DOMAIN; HYDROGEN BONDING; INTRAMOLECULAR TRANSFERASES; KINETICS; LYASES; MUTATION; PROTEIN ENGINEERING; SALICYLATES; SIDEROPHORES; TRYPTOPHAN; VITAMIN K 2;

EID: 84884937629 PISSN: 00039861 EISSN: 10960384 Source Type: Journal
DOI: 10.1016/j.abb.2013.09.007 Document Type: Article

Times cited : (5)

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