The Hydrolytic Activity of Glyceraldehyde-3-Phosphate Dehydrogenase

Park, Jane Harting; Koshland, Daniel E.

doi:10.1016/s0021-9258(18)64691-5

Cited by 79 publications

(16 citation statements)

References 22 publications

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“…For example, the acid-and basecatalyzed hydrolysis of AcP reactions have been shown to take place by cleavage of the C−O bonds, while the uncatalyzed reaction and the pyridine-catalyzed reaction proceed by O−P bond splitting. 13 In one drug development project at Merck & Co., Inc. (Kenilworth, NJ, USA), enzymatic phosphorylation is used as an important step for the synthesis of an active pharmaceutical ingredient. Propionyl phosphate (PrP) was chosen as the phosphate donor because of the benefits for the downstream biocatalytic process.…”

Section: Introductionmentioning

confidence: 99%

“…Also, there have been studies investigating the specific location of the oxygen bond broken during the hydrolysis reaction of AcP. For example, the acid- and base-catalyzed hydrolysis of AcP reactions have been shown to take place by cleavage of the C–O bonds, while the uncatalyzed reaction and the pyridine-catalyzed reaction proceed by O–P bond splitting …”

Section: Introductionmentioning

confidence: 99%

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Characterization of Propionyl Phosphate Hydrolysis Kinetics by Data-Rich Experiments and In-Line Process Analytical Technology

Yang

Feng

Stone

2021

Org. Process Res. Dev.

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In-depth characterization of reaction kinetics often requires a considerable amount of experimental results under various conditions. Recent advances in data-rich experimentation enable the collection of sufficient data to investigate reactions with only a limited number of experiments. In this study, we developed a cost-efficient, robust approach by utilizing data-rich experimentation to characterize propionyl phosphate hydrolysis reaction kinetics. Specifically, an Fourier transform infrared (FTIR)-based process analytical technology (PAT) and off-line NMR calibration allowed the establishment of a quantitative FTIR multivariant model. This PAT was then integrated with repeated temperature scanning (RTS) to generate a massive database in a single experiment. The data were subsequently used for kinetic analysis, and two key characteristic reaction parameters (the activation energy and pre-exponential factor) were determined on the basis of the assumption of first-order kinetics. We envision that the integrative platform developed in this study can be broadly applied to investigations of the kinetics of a wide range of similar liquid-phase reactions.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization of Propionyl Phosphate Hydrolysis Kinetics by Data-Rich Experiments and In-Line Process Analytical Technology

Yang

Feng

Stone

2021

Org. Process Res. Dev.

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“…It is known that aldehyde dehydrogenase has carboxyl esterase- and phosphatase-like activities, wherein the enzyme catalyzes hydrolysis of carboxyl esters and phosphoesters in the presence of NADH. − It is believed that both dehydrogenase and esterase activities of aldehyde dehydrogenase occur at its same active site and that ester hydrolysis begins with an attack to the carbonyl carbon of the ester by the nucleophile at the active site of the enzyme–NADH complex. , Importantly, the authors have demonstrated that DT-D [NAD(P)H dehydrogenase (quinone)] from Bacillus stearothermophilus (EC 1.6.99.-) also shows high phosphatase-like activity . Because DT-D is a bifunctional (type 3) enzyme, triple signal amplification is readily achieved.…”

mentioning

confidence: 99%

Carboxyl Esterase-Like Activity of DT-Diaphorase and Its Use for Signal Amplification

Nandhakumar

Ichzan

Lee³

et al. 2019

ACS Sens.

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Carboxyl esterases show limited use as catalytic labels in bioassays because of slow enzymatic reaction. We report that DT-diaphorase from Bacillus stearothermophilus (DT-D, EC 1.6.99.-) shows high carboxyl esterase-like activity in the presence of reduced β-nicotinamide adenine dinucleotide (NADH) and may be used as a better catalytic label than carboxyl esterases. DT-D is a redox enzyme and can participate in signal-amplifying redox cycling. Thus, an electrochemical immunosensor using a DT-D label allows for triple signal amplification based on (i) hydrolysis of a carboxyl ester, (ii) electrochemical–chemical (EC) redox cycling involving an electrode, a hydrolysis product, and NADH, and (iii) electrochemical–enzymatic (EN) redox cycling involving an electrode, a hydrolysis product, DT-D, and NADH. Ester hydrolysis by DT-D is confirmed via spectrophotometric measurement of a chromogenic substrate (4-nitrophenyl acetate) and 1H NMR spectra. Among two phenyl acetates and four naphthyl acetates considered, 4-aminonaphthalene-1-yl acetate (4-NH2-NAc) is chosen as the best acetyl ester substrate because 4-NH2-NAc is stable, its hydrolysis is slow in the absence of DT-D, its hydrolysis is very fast in the presence of DT-D, and EC and EN redox cycling involving the hydrolysis product (4-amino-1-naphthol) is rapid. However, hydrolysis of 4-NH2-NAc by esterase from porcine liver (EC 3.1.1.1.) is very slow. When DT-D is applied to sandwich-type detection of thyroid-stimulating hormone in artificial serum, the detection limit is ∼2 pg/mL, indicating that the developed immunosensor is highly sensitive because of triple signal amplification. DT-D may be used as a catalytic label in sensitive and stable bioassays instead of common alkaline phosphatase and horseradish peroxidase.

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“…The mechanism of the inhibition of the phosphatase reaction is discussed, and the effects of photooxidation on the various enzymatic activities are compared. dized by air and acquired an acetylphosphatase activity (Harting, 1954; Park and Koshland, 1958). Rafter and Colo wick (1957) found that this slow rate of hydrolysis of acetyl phosphate or 1,3-diphosphoglyceric acid could be markedly increased by oxidizing the enzyme with iodosobenzoate under strictly controlled conditions (Rafter, 1957;Rafter and Colowick, 1957).…”

mentioning

confidence: 99%

“…Rafter and Colo wick (1957) found that this slow rate of hydrolysis of acetyl phosphate or 1,3-diphosphoglyceric acid could be markedly increased by oxidizing the enzyme with iodosobenzoate under strictly controlled conditions (Rafter, 1957;Rafter and Colowick, 1957). The phosphatase activity can be inhibited by sulfhydryl compounds, i.e., cysteine or glutathione, and the dehydrogenase activity thereby restored (Harting, 1954;Park and Koshland, 1958). It has been demonstrated that cysteine-149 in the monomer of 332 amino acids was the active-site residue which was responsible for the reversible interconversion of the dehydrogenase and phosphatase activities (Harris et al, 1963;Harris and Perham, 1965).…”

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confidence: 99%

Effects of photooxidation of histidine-38 on the acetylphosphatase activity of glyceraldehyde 3-phosphate dehydrogenase

Francis¹,

Meriwether²,

Park³

1973

Biochemistry

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The Hydrolytic Activity of Glyceraldehyde-3-Phosphate Dehydrogenase

Cited by 79 publications

References 22 publications

Characterization of Propionyl Phosphate Hydrolysis Kinetics by Data-Rich Experiments and In-Line Process Analytical Technology

Characterization of Propionyl Phosphate Hydrolysis Kinetics by Data-Rich Experiments and In-Line Process Analytical Technology

Carboxyl Esterase-Like Activity of DT-Diaphorase and Its Use for Signal Amplification

Effects of photooxidation of histidine-38 on the acetylphosphatase activity of glyceraldehyde 3-phosphate dehydrogenase

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