Sheraz Gul

Molecular recognition and electrostatic effects in papain and actinidin cysteine proteinases exhibiting extremes of kinetic behaviour. (1997)

Gul, Sheraz.

Thesis (Ph. D.)--University of London, 1997.

Staphylococcus aureus DNA ligase: characterization of its kinetics of catalysis and development of a high-throughput screening compatible chemiluminescent hybridization protection assay

Gul, Sheraz, Brown, Richard, May, Earl, Mazzulla, Marie, Smyth, Martin G., Berry, Colin, ...

DNA ligases are key enzymes involved in the repair and replication of DNA. Prokaryotic DNA ligases uniquely use NAD+ as the adenylate donor during catalysis, whereas eukaryotic enzymes use ATP. This...

Evidence for ‘lock and key’ character in an anti-phosphonate hydrolytic antibody catalytic site augmented by non-reaction centre recognition: variation in substrate selectivity between an anti-phosphonate antibody, an anti-phosphate antibody and two hydrolytic enzymes

Sonkaria, Sanjiv, Boucher, Guillaume, FLóREZ-ÁLVAREZ, José, Said, Bilal, Hussain, Syeed, Ostler, Elizabeth L., ...

The substrate selectivities of an anti-phosphonate and an anti-phosphate kinetically homogeneous polyclonal catalytic antibody preparation and two hydrolytic enzymes were compared by using...

Improvement in hydrolytic antibody activity by change in haptenic structure from phosphate to phosphonate with retention of a common leaving-group determinant: evidence for the 'flexibility' hypothesis.

Gul, Sheraz, Sonkaria, Sanjiv, Pinitglang, Surapong, Florez-Alvarez, José, Hussain, Syeed, Thomas, Emrys W, ...

To investigate the hypothesis that decreased hapten flexibility may lead to increased catalytic antibody activity, we used two closely related immunogens differing only in the flexibility of the...

Temperature-dependences of the kinetics of reactions of papain and actinidin with a series of reactivity probes differing in key molecular recognition features

Gul, Sheraz, Mellor, Geoffrey W., Thomas, Emrys W., Brocklehurst, Keith

The temperature-dependences of the second-order rate constants (k) of the reactions of the catalytic site thiol groups of two cysteine peptidases papain (EC 3.4.22.2) and actinidin (EC 3.4.22.14)...

Staphylococcus aureus DNA ligase: characterization of its kinetics of catalysis and development of a high-throughput screening compatible chemiluminescent hybridization protection assay

Gul, Sheraz, Brown, Richard, May, Earl, Mazzulla, Marie, Smyth, Martin G., Berry, Colin, ...

DNA ligases are key enzymes involved in the repair and replication of DNA. Prokaryotic DNA ligases uniquely use NAD+ as the adenylate donor during catalysis, whereas eukaryotic enzymes use ATP. This...

Evidence for ‘lock and key’ character in an anti-phosphonate hydrolytic antibody catalytic site augmented by non-reaction centre recognition: variation in substrate selectivity between an anti-phosphonate antibody, an anti-phosphate antibody and two hydrolytic enzymes

Sonkaria, Sanjiv, Boucher, Guillaume, FLóREZ-ÁLVAREZ, José, Said, Bilal, Hussain, Syeed, Ostler, Elizabeth L., ...

The substrate selectivities of an anti-phosphonate and an anti-phosphate kinetically homogeneous polyclonal catalytic antibody preparation and two hydrolytic enzymes were compared by using...

Improvement in hydrolytic antibody activity by change in haptenic structure from phosphate to phosphonate with retention of a common leaving-group determinant: evidence for the 'flexibility' hypothesis.

Gul, Sheraz, Sonkaria, Sanjiv, Pinitglang, Surapong, Florez-Alvarez, José, Hussain, Syeed, Thomas, Emrys W, ...

To investigate the hypothesis that decreased hapten flexibility may lead to increased catalytic antibody activity, we used two closely related immunogens differing only in the flexibility of the...

Temperature-dependences of the kinetics of reactions of papain and actinidin with a series of reactivity probes differing in key molecular recognition features

Gul, Sheraz, Mellor, Geoffrey W., Thomas, Emrys W., Brocklehurst, Keith

The temperature-dependences of the second-order rate constants (k) of the reactions of the catalytic site thiol groups of two cysteine peptidases papain (EC 3.4.22.2) and actinidin (EC 3.4.22.14)...