Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Miguel St-Jean"'
Publikováno v:
Biochemistry. 48:4528-4537
Fructose-1,6-bisphosphate muscle aldolase is an essential glycolytic enzyme that catalyzes reversible carbon-carbon bond formation by cleaving fructose 1,6-bisphosphate to yield dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde phosphate. To elu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6edeb8a08ea723acb7382e5d08849761
https://doi.org/10.1021/bi8021558
https://doi.org/10.1021/bi8021558
Autor:
Miguel St-Jean, Jurgen Sygusch
Publikováno v:
Journal of Biological Chemistry. 282:31028-31037
Class I fructose-1,6-bisphosphate aldolases catalyze the interconversion between the enamine and iminium covalent enzymatic intermediates by stereospecific exchange of the pro(S) proton of the dihydroxyacetone-phosphate C3 carbon, an obligatory react
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd62be57cc5f4abac156cf49d0d6f40c
https://doi.org/10.1074/jbc.m704968200
https://doi.org/10.1074/jbc.m704968200
Publikováno v:
Journal of Biological Chemistry. 280:27262-27270
Crystal structures were determined to 1.8 A resolution of the glycolytic enzyme fructose-1,6-bis(phosphate) aldolase trapped in complex with its substrate and a competitive inhibitor, mannitol-1,6-bis(phosphate). The enzyme substrate complex correspo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::478bf2f6828fc366f40971ef647979f0
https://doi.org/10.1074/jbc.m502413200
https://doi.org/10.1074/jbc.m502413200
Publikováno v:
The Journal of biological chemistry. 282(19)
Aldolase plays essential catalytic roles in glycolysis and gluconeogenesis. However, aldolase is a highly abundant protein that is remarkably promiscuous in its interactions with other cellular proteins. In particular, aldolase binds to highly acidic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b04692781eebd7f0fcfb4344d8e2b99
https://pubmed.ncbi.nlm.nih.gov/17329259
https://pubmed.ncbi.nlm.nih.gov/17329259
Publikováno v:
The Journal of biological chemistry. 280(29)
Crystal structures were determined to 1.8 A resolution of the glycolytic enzyme fructose-1,6-bis(phosphate) aldolase trapped in complex with its substrate and a competitive inhibitor, mannitol-1,6-bis(phosphate). The enzyme substrate complex correspo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3581be202244f4e01d90562e4c3be631
https://pubmed.ncbi.nlm.nih.gov/15870069
https://pubmed.ncbi.nlm.nih.gov/15870069