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1
The Role of Binding Energy in Catalysis: the Work of William P. Jencks
The Role of Binding Energy in Catalysis: the Work of William P. Jencks
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The Role of Binding Energy in Catalysis: the Work of William P. Jencks

Kresge, Nicole ; Simoni, Robert D. ; Hill, Robert L.

The Journal of biological chemistry, 2010-11, Vol.285 (45), p.e16-e17 [Periódico revisado por pares]

9650 Rockville Pike, Bethesda, MD 20814, U.S.A: Elsevier Inc

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2
Two functional domains of coenzyme A activate catalysis by coenzyme A transferase. Pantetheine and adenosine 3‘-phosphate 5‘-diphosphate
Two functional domains of coenzyme A activate catalysis by coenzyme A transferase. Pantetheine and adenosine 3‘-phosphate 5‘-diphosphate
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Two functional domains of coenzyme A activate catalysis by coenzyme A transferase. Pantetheine and adenosine 3‘-phosphate 5‘-diphosphate

Fierke, C A ; Jencks, W P

The Journal of biological chemistry, 1986-06, Vol.261 (17), p.7603-7606 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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3
Energetics of the calcium-transporting ATPase
Energetics of the calcium-transporting ATPase
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Energetics of the calcium-transporting ATPase

Pickart, C M ; Jencks, W P

The Journal of biological chemistry, 1984-02, Vol.259 (3), p.1629-1643 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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4
Slow dissociation of ATP from the calcium ATPase
Slow dissociation of ATP from the calcium ATPase
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Slow dissociation of ATP from the calcium ATPase

Pickart, C M ; Jencks, W P

The Journal of biological chemistry, 1982-05, Vol.257 (10), p.5319-5322 [Periódico revisado por pares]

United States: Elsevier Inc

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5
Formation of stable anhydrides from CoA transferase and hydroxamic acids
Formation of stable anhydrides from CoA transferase and hydroxamic acids
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Formation of stable anhydrides from CoA transferase and hydroxamic acids

Pickart, C M ; Jencks, W P

The Journal of biological chemistry, 1979-09, Vol.254 (18), p.9120-9129 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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6
Acetyl coenzyme A: arylamine acetyltransferase. Measurement of the steady state concentration of the acetyl-enzyme intermediate
Acetyl coenzyme A: arylamine acetyltransferase. Measurement of the steady state concentration of the acetyl-enzyme intermediate
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Acetyl coenzyme A: arylamine acetyltransferase. Measurement of the steady state concentration of the acetyl-enzyme intermediate

Jencks, W P ; Gresser, M ; Valenzuela, M S ; Huneeus, F C

The Journal of biological chemistry, 1972-06, Vol.247 (12), p.3756 [Periódico revisado por pares]

United States

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7
The kinetics for the phosphoryl transfer steps of the sarcoplasmic reticulum calcium ATPase are the same with strontium and with calcium bound to the transport sites
The kinetics for the phosphoryl transfer steps of the sarcoplasmic reticulum calcium ATPase are the same with strontium and with calcium bound to the transport sites
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The kinetics for the phosphoryl transfer steps of the sarcoplasmic reticulum calcium ATPase are the same with strontium and with calcium bound to the transport sites

FUJIMORI, T ; JENCKS, WP

The Journal of biological chemistry, 1992-09, Vol.267 (26), p.18466-18474 [Periódico revisado por pares]

BETHESDA: American Society for Biochemistry and Molecular Biology

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8
Allosteric inhibition of methylenetetrahydrofolate reductase by adenosylmethionine. Effects of adenosylmethionine and NADPH on the equilibrium between active and inactive forms of the enzyme and on the kinetics of approach to equilibrium
Allosteric inhibition of methylenetetrahydrofolate reductase by adenosylmethionine. Effects of adenosylmethionine and NADPH on the equilibrium between active and inactive forms of the enzyme and on the kinetics of approach to equilibrium
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Allosteric inhibition of methylenetetrahydrofolate reductase by adenosylmethionine. Effects of adenosylmethionine and NADPH on the equilibrium between active and inactive forms of the enzyme and on the kinetics of approach to equilibrium

Jencks, D.A. ; Mathews, R.G.

The Journal of biological chemistry, 1987-02, Vol.262 (6), p.2485-2493 [Periódico revisado por pares]

United States: Elsevier Inc

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9
Lanthanum inhibits steady-state turnover of the sarcoplasmic reticulum calcium ATPase by replacing magnesium as the catalytic ion
Lanthanum inhibits steady-state turnover of the sarcoplasmic reticulum calcium ATPase by replacing magnesium as the catalytic ion
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Lanthanum inhibits steady-state turnover of the sarcoplasmic reticulum calcium ATPase by replacing magnesium as the catalytic ion

Fujimori, T ; Jencks, W P

The Journal of biological chemistry, 1990-09, Vol.265 (27), p.16262-16270 [Periódico revisado por pares]

United States: Elsevier Inc

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10
Acetyl phosphate as a substrate for the calcium ATPase of sarcoplasmic reticulum
Acetyl phosphate as a substrate for the calcium ATPase of sarcoplasmic reticulum
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Acetyl phosphate as a substrate for the calcium ATPase of sarcoplasmic reticulum

Bodley, A L ; Jencks, W P

The Journal of biological chemistry, 1987-10, Vol.262 (29), p.13997-14004 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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