Correction- The "Phosphoryl-Enzyme" from Phosphoglycerate Kinase

Johnson, Patricia E.; Abbott, Steven; Orr, George A.; Knowles, Jeremy R.

doi:10.1021/bi00662a605

Cited by 4 publications

(4 citation statements)

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“…Yet for many of these studies relatively crude commercial enzyme was used, and efforts to ensure the absence of substrate (or substrate analogue) contaminants were often not reported. The phosphokinase field is bedeviled by problems arising from the presence of small amounts of contaminating kinases (it is rare, for instance, to find a commercial kinase preparation that will not support ATP-ADP exchange) or from the presence of small amounts of contaminating substrate [see, e.g., Johnson et al (1976) and Switzer St Simcox (1974)]. The effective consequence of most such contamination is to yield results that suggest the kinetic importance of a phosphoryl-enzyme intermediate.…”

Section: Discussionmentioning

confidence: 99%

Stereochemical course of phosphokinases. The use of adenosine [.gamma.-(S)-16O,17O,18O]triphosphate and the mechanistic consequences for the reactions catalyzed by glycerol kinase, hexokinase, pyruvate kinase, and acetate kinase

Blättler¹,

Knowles²

1979

Biochemistry

106

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We report the synthesis of adenosine [gamma-(S)-16O,17O,18O]triphosphate, an isotopically labeled species of ATP that is chiral at the gamma-phosphoryl group, the configuration of which has been confirmed by independent stereochemical analysis. This molecule has been used as a substrate in the reactions catalyzed by glycerol kinase and by acetate kinase. The resulting samples of isotopically labeled sn-glycerol 3-phosphate and of acetyl phosphate have been used as substrates in the alkaline phosphatase mediated transfer of the chiral phosphoryl groups to (S)-propane-1,2-diol, whence the configuration at phosphorus has been determined [Abbott, S. J., Jones, S. R., Weinman, S. A., & Knowles, J. R. (1978) J. Am. Chem. Soc. 100, 2558]. It is shown that glycerol kinase and acetate kinase (and, by virtue of an earlier correlation, pyruvate kinase and hexokinase) proceed by pathways that result in inversion of the configuration at phosphorus. The sterochemical approach provides an access to the otherwise cryptic events that are involved in phosphoryl-group transfer within the ternary complexes of these kinases and their substrates.

show abstract

Section: Discussionmentioning

confidence: 99%

Stereochemical course of phosphokinases. The use of adenosine [.gamma.-(S)-16O,17O,18O]triphosphate and the mechanistic consequences for the reactions catalyzed by glycerol kinase, hexokinase, pyruvate kinase, and acetate kinase

Blättler¹,

Knowles²

1979

Biochemistry

106

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“…Among them, nm23-H1 and nm23-H2, the predominant isoforms residing in the cytoplasm (18), have been characterized in detail with regard to their kinetic properties and catalytic mechanisms (29). Other enzymes that are able to phosphorylate nucleoside diphosphates include creatine kinase (CK), pyruvate kinase (PK), and 3-phosphoglycerate kinase (PGK) (14)(15)(16)(17). Our previous studies demonstrated that TK1 is the enzyme responsible for the phosphorylation of 4Ј-ethynyl D4T to 4Ј-ethynyl D4TMP (6).…”

mentioning

confidence: 99%

Comparison of the Phosphorylation of 4′-Ethynyl 2′,3′-Dihydro-3′-Deoxythymidine with That of Other Anti-Human Immunodeficiency Virus Thymidine Analogs

Hsu

Dutschman

et al. 2007

Antimicrob Agents Chemother

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Thymidine analogs, including 3-azido-3-deoxythymidine (AZT) and 2,3-dideoxy-3-deoxythymidine (D4T), are important antiretroviral agents. To exert antiretroviral activity, these analogs undergo a stepwise phosphorylation intracellularly to the active triphosphate metabolites. We previously reported that 4-substituted D4T with an ethynyl group (i.e., 4-ethynyl D4T) increased the anti-human immunodeficiency virus (HIV) activity and was active against multidrug-resistant HIV strains. 4-Ethynyl D4T is a better substrate for phosphorylation by human thymidine kinase 1 than D4T is. In this report, we first studied the enzymes involved in the phosphorylation of 4-ethynyl D4T from monophosphate to triphosphate metabolites.

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“…In optimal cases the existence of a catalytically significant phosphoryl enzyme can be demonstrated by an apparent association of 32P label with a purifiable protein and the demonstration of the catalytic competence of such a species, although an apparent phosphoryl enzyme could be simply a tightly bound ligand (Walsh & Spector, 1971;Johnson et al, 1976). The demonstration of ping-pong kinetics (for twosubstrate reactions) or of an exchange half-reaction becomes the only feasible probe with increasing instability of the phosphoryl enzyme.…”

Section: Discussionmentioning

confidence: 99%

Fructose 1,6-bisphosphatase from rabbit liver. [18O]Phosphate-water exchange as a probe of the catalytic mechanism

Sharp¹,

Benkovic²

1979

Biochemistry

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Correction- The "Phosphoryl-Enzyme" from Phosphoglycerate Kinase

Cited by 4 publications

References 0 publications

Stereochemical course of phosphokinases. The use of adenosine [.gamma.-(S)-16O,17O,18O]triphosphate and the mechanistic consequences for the reactions catalyzed by glycerol kinase, hexokinase, pyruvate kinase, and acetate kinase

Stereochemical course of phosphokinases. The use of adenosine [.gamma.-(S)-16O,17O,18O]triphosphate and the mechanistic consequences for the reactions catalyzed by glycerol kinase, hexokinase, pyruvate kinase, and acetate kinase

Comparison of the Phosphorylation of 4′-Ethynyl 2′,3′-Dihydro-3′-Deoxythymidine with That of Other Anti-Human Immunodeficiency Virus Thymidine Analogs

Fructose 1,6-bisphosphatase from rabbit liver. [18O]Phosphate-water exchange as a probe of the catalytic mechanism

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