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Desensitized Phosphofructokinase from Ascaris suum: A Study in Noncooperative Allostery

The studies described in this dissertation examine the effects of F-2,6-P2 and AMP or phosphorylation on the kinetic mechanism of d-PFK. The effect of varied pH on the activation by F-2,6-P2 is also described.

Date: May 1993

Creator: Payne, Marvin A.

Item Type: Thesis or Dissertation

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Kinetic and Chemical Mechanism of 6-phosphogluconate Dehydrogenase from Candida Utilis

A complete initial velocity study of the 6-phosphogluconate dehydrogenase from Candida utilis in both reaction directions suggests a rapid equilibrium random kinetic mechanism with dead-end E:NADP:(ribulose 5-phosphate) and E:NADPH:(6- phosphogluconate) complexes. Initial velocity studies obtained as a function of pH and using NAD as the dinucleotide substrate for the reaction suggest that the 2'-phosphate is critical for productive binding of the dinucleotide substrate. Primary deuterium isoto… more

Date: May 1993

Creator: Berdis, Anthony J. (Anthony Joseph)

Item Type: Thesis or Dissertation

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A Study of the Intrinsic Fluorescence of O-Acetyl-L-Serine Sulfhydrylase-A from Salmonella typhimurium

O-Acetyl-L-serine sulfhydrylase-A (OASS-A) forms acetate and L-cysteine from O-acetyl-L-serine (OAS) and sulfide. One molecule of the cofactor pyridoxal 5'- phosphate (PLP) is bound in each holoenzyme protomer.

Date: May 1993

Creator: McClure, G. David (George David)

Item Type: Thesis or Dissertation

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Desensitized Phosphofructokinase from Ascaris suum: A Study in Noncooperative Allostery

Kinetic and Chemical Mechanism of 6-phosphogluconate Dehydrogenase from Candida Utilis

A Study of the Intrinsic Fluorescence of O-Acetyl-L-Serine Sulfhydrylase-A from Salmonella typhimurium