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TitleStructural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power.
Journal, issue, pagesProtein Eng., Vol. 12, Page 243-250, Year 1999
Publish dateJun 17, 1997 (structure data deposition date)
AuthorsWilliams, J.C. / Zeelen, J.P. / Neubauer, G. / Vriend, G. / Backmann, J. / Michels, P.A. / Lambeir, A.M. / Wierenga, R.K.
External linksProtein Eng. / PubMed:10235625
MethodsX-ray diffraction
Resolution1.83 Å
Structure data

PDB-1amk:
LEISHMANIA MEXICANA TRIOSE PHOSPHATE ISOMERASE
Method: X-RAY DIFFRACTION / Resolution: 1.83 Å

Chemicals

ChemComp-PGA:
2-PHOSPHOGLYCOLIC ACID

ChemComp-HOH:
WATER

Source
  • leishmania mexicana (eukaryote)
KeywordsGLUCONEOGENESIS / TIM / 2-PG / PGA / FATTY ACID BIOSYNTHESIS

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