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Proceedings of the National Academy of Sciences of the United States of America

Volumn 103, Issue 19, 2006, Pages 7246-7251

Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized

(3) Tcherkez, Guillaume G B a,b Farquhar, Graham D a Andrews, T John a

a AUSTRALIAN NATIONAL UNIVERSITY (Australia)

b UNIVERSITÉ PARIS SACLAY (France)

Author keywords

Enzyme mechanisms; Isotope fractionation; Transition states

Indexed keywords

CARBON; CARBON 13; CARBON DIOXIDE; CARBOXYLIC ACID; KETONE; OXYGEN; RIBULOSEBISPHOSPHATE CARBOXYLASE;

ARTICLE; ATMOSPHERE; AUTOTROPHY; CARBON DIOXIDE FIXATION; CARBOXYLATION; CATALYSIS; CONCENTRATION (PARAMETERS); CONFORMATIONAL TRANSITION; ENTROPY; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE COMPLEX; FRACTIONATION; HYDROLYSIS; NONHUMAN; OXYGENATION; PRIORITY JOURNAL; TEMPERATURE;

CARBON DIOXIDE; CATALYSIS; KETONES; KINETICS; MOLECULAR STRUCTURE; OXYGEN; RIBULOSE-BISPHOSPHATE CARBOXYLASE; SUBSTRATE SPECIFICITY; WATER;

EID: 33646583168 PISSN: 00278424 EISSN: None Source Type: Journal
DOI: 10.1073/pnas.0600605103 Document Type: Article

Times cited : (597)

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