MUTATIONS IN THE ACTIVE-SITE OF ESCHERICHIA-COLI PHOSPHOFRUCTOKINASE

[1] REFINED MODEL OF SUGAR BINDING-SITE OF YEAST HEXOKINASE-B [J]. JOURNAL OF MOLECULAR BIOLOGY, 1978, 123 (02) : 207 - 219

[2] Benkovic S. J, 1973, ENZYMES, P201

[3] KINETICS OF ALLOSTERIC INTERACTIONS OF PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI [J]. JOURNAL OF MOLECULAR BIOLOGY, 1968, 31 (01) : 13 - &

[4] INTRAMOLECULAR GENERAL ACID CATALYSIS OF PHOSPHATE MONOESTER HYDROLYSIS - HYDROLYSIS OF SALICYL PHOSPHATE [J]. JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 2, 1972, (02): : 149 - &

[5] BUCHWALD SL, 1982, METHOD ENZYMOL, V87, P279

[6] IMPROVED OLIGONUCLEOTIDE SITE-DIRECTED MUTAGENESIS USING M13 VECTORS [J]. NUCLEIC ACIDS RESEARCH, 1985, 13 (12) : 4431 - 4443

[7] ROLE OF ARGININE RESIDUES AT ENZYME ACTIVE-SITES - INTERACTION BETWEEN GUANIDINIUM IONS AND PARA-NITROPHENYL PHOSPHATE AND ITS EFFECT ON RATE OF HYDROLYSIS OF ESTER [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1977, 481 (01) : 1 - 5

[8] STAPHYLOCOCCAL NUCLEASE - PROPOSED MECHANISM OF ACTION BASED ON STRUCTURE OF ENZYME-THYMIDINE 3',5'-BISPHOSPHATE-CALCIUM ION COMPLEX AT 1.5-A RESOLUTION [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1979, 76 (06) : 2551 - 2555

[9] STRUCTURE AND CONTROL OF PHOSPHOFRUCTOKINASE FROM BACILLUS-STEAROTHERMOPHILUS [J]. NATURE, 1979, 279 (5713) : 500 - 504

[10] PHOSPHOFRUCTOKINASE - STRUCTURE AND CONTROL [J]. PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES B-BIOLOGICAL SCIENCES, 1981, 293 (1063) : 53 - 62

[1] REFINED MODEL OF SUGAR BINDING-SITE OF YEAST HEXOKINASE-B [J]. JOURNAL OF MOLECULAR BIOLOGY, 1978, 123 (02) : 207 - 219

[2] Benkovic S. J, 1973, ENZYMES, P201

[3] KINETICS OF ALLOSTERIC INTERACTIONS OF PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI [J]. JOURNAL OF MOLECULAR BIOLOGY, 1968, 31 (01) : 13 - &

[4] INTRAMOLECULAR GENERAL ACID CATALYSIS OF PHOSPHATE MONOESTER HYDROLYSIS - HYDROLYSIS OF SALICYL PHOSPHATE [J]. JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 2, 1972, (02): : 149 - &

[5] BUCHWALD SL, 1982, METHOD ENZYMOL, V87, P279

[6] IMPROVED OLIGONUCLEOTIDE SITE-DIRECTED MUTAGENESIS USING M13 VECTORS [J]. NUCLEIC ACIDS RESEARCH, 1985, 13 (12) : 4431 - 4443

[7] ROLE OF ARGININE RESIDUES AT ENZYME ACTIVE-SITES - INTERACTION BETWEEN GUANIDINIUM IONS AND PARA-NITROPHENYL PHOSPHATE AND ITS EFFECT ON RATE OF HYDROLYSIS OF ESTER [J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1977, 481 (01) : 1 - 5

[8] STAPHYLOCOCCAL NUCLEASE - PROPOSED MECHANISM OF ACTION BASED ON STRUCTURE OF ENZYME-THYMIDINE 3',5'-BISPHOSPHATE-CALCIUM ION COMPLEX AT 1.5-A RESOLUTION [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1979, 76 (06) : 2551 - 2555

[9] STRUCTURE AND CONTROL OF PHOSPHOFRUCTOKINASE FROM BACILLUS-STEAROTHERMOPHILUS [J]. NATURE, 1979, 279 (5713) : 500 - 504

[10] PHOSPHOFRUCTOKINASE - STRUCTURE AND CONTROL [J]. PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES B-BIOLOGICAL SCIENCES, 1981, 293 (1063) : 53 - 62