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pro vyhledávání: '"Shamina Hakda"'
Publikováno v:
Biochemistry. 42:13505-13511
The open-closed conformational switch in the active site of Escherichia coli beta-galactosidase was studied by X-ray crystallography and enzyme kinetics. Replacement of Gly794 by alanine causes the apoenzyme to adopt the closed rather than the open c
Publikováno v:
Biochemistry. 42:1796-1803
Trp-999 is a key residue for the action of beta-galactosidases (Escherichia coli). Several site specific substitutions (Phe, Gly, Tyr, Leu) for Trp-999 were made. Each substitution caused greatly decreased affinities for substrates and inhibitors tha
Publikováno v:
Cryobiology. 53:378-379