Escherichia coli β-galactosidase recognizes a high-energy conformation of C-lactose, a nonhydrolizable substrate analogue, NMR and modeling studies of the molecular complex

Journal of the American Chemical Society

Volumn 120, Issue 6, 1998, Pages 1309-1318

  Espinosa, J F ^a  

^a INSTITUTO DE QUÍMICA ORGÁNICA GENERAL   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDASE;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CATALYSIS; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; ESCHERICHIA COLI; MOLECULAR INTERACTION; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

EID: 0032542581     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja972291q     Document Type: Article

References (3)

1. Sinnott, M. L. Chem. Rev. 1990 90, 1171-1202.
2. Huber, R. E.; Gupta, M. N.; Khare, S. K. Int. J. Biochem. 1994 26, 309-318.
3. Jacobson, R. H.; Zhang, X.-J.; DuBose, R. F.; Matthews, B. W Nature 1994, 369, 761-766.