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pro vyhledávání: '"Brigitte, Liotard"'
Publikováno v:
Journal of Biological Chemistry. 285:21143-21152
Tagatose-1,6-bisphosphate aldolase from Streptococcus pyogenes is a class I aldolase that exhibits a remarkable lack of chiral discrimination with respect to the configuration of hydroxyl groups at both C3 and C4 positions. The enzyme catalyzes the r
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
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
Autor:
Brigitte Liotard, Jurgen Sygusch
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 60(Pt 3)
Tagatose-1,6-bisphosphate aldolase (EC 4.1.2.40) is situated at the branching of the tagatose-6-phosphate and Embden-Meyerhof-Parnas (glycolysis) metabolic pathways, where it catalyzes the reversible cleavage of tagatose-1,6-bisphosphate to dihydroxy
Autor:
Liotard, Brigitte1 brigitte.liotard@umontreal.ca, Sygusch, Jurgen1
Publikováno v:
Acta Crystallographica: Section D (Wiley-Blackwell). Mar2004, Vol. 60 Issue 3, p528-530. 3p.