Ontology highlight
ABSTRACT:
SUBMITTER: Stetefeld J
PROVIDER: S-EPMC1564225 | biostudies-literature | 2006 Sep
REPOSITORIES: biostudies-literature
Stetefeld J J Jenny M M Burkhard P P
Proceedings of the National Academy of Sciences of the United States of America 20060905 37
Enzymes are highly dynamic and tightly controlled systems. However, allosteric communication linked to catalytic turnover is poorly understood. We have performed an integrated approach to trap several catalytic intermediates in the alpha2-dimeric key enzyme of chlorophyll biosynthesis, glutamate-1-semialdehyde aminomutase. Our data reveal an active-site "gating loop," which undergoes a dramatic conformational change during catalysis, that is simultaneously open in one subunit and closed in the o ...[more]