The activation and inactivation of the acyl phosphatase activity of glyceraldehyde-3-phosphate dehydrogenase

Allison, William S.; Connors, Michael J.

doi:10.1016/0003-9861(70)90209-2

Cited by 39 publications

(13 citation statements)

References 31 publications

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“…The discovery that the specific conversion of Cys-149 in GAPDH to corresponding sulfenic acid converts the enzyme from dehydrogenase to an acyl phosphatase was probably the first to hint at a biological role for protein sulfenic acid [68,72,73]. Another study demonstrated oxidation of the lone free thiol in albumin upon incubation with xanthine oxidase [74].…”

Section: Sulfenic Acids In Proteinsmentioning

confidence: 99%

Sulfenic acid chemistry, detection and cellular lifetime

Gupta

Carroll

2014

Biochimica et Biophysica Acta (BBA) - General Subjects

383

399

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Background Reactive oxygen species-mediated cysteine sulfenic acid modification has emerged as an important regulatory mechanism in cell signaling. The stability of sulfenic acid in proteins is dictated by the local microenvironment and ability of antioxidants to reduce this modification. Several techniques for detecting this cysteine modification have been developed, including direct and in situ methods. Scope of review This review presents a historical discussion of sulfenic acid chemistry and highlights key examples of this modification in proteins. A comprehensive survey of available detection techniques with advantages and limitations is discussed. Finally, issues pertaining to rates of sulfenic acid formation, reduction, and chemical trapping methods are also covered. Major conclusions Early chemical models of sulfenic acid yielded important insights into the unique reactivity of this species. Subsequent pioneering studies led to the characterization of sulfenic acid formation in proteins. In parallel, the discovery of oxidant-mediated cell signaling pathways and pathological oxidative stress has led to significant interest in methods to detect these modifications. Advanced methods allow for direct chemical trapping of protein sulfenic acids directly in cells and tissues. At the same time, many sulfenic acids are short-lived and the reactivity of current probes must be improved to sample these species, while at the same time, preserving their chemical selectivity. Inhibitors with binding scaffolds can be rationally designed to target sulfenic acid modifications in specific proteins. General significance Ever increasing roles for protein sulfenic acids have been uncovered in physiology and pathology. A more complete understanding of sulfenic acid-mediated regulatory mechanisms will continue to require rigorous and new chemical insights. This article is part of a Special Issue entitled Current methods to study reactive oxygen species - pros and cons and biophysics of membrane proteins. Guest Editor: Christine Winterbourn.

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Section: Sulfenic Acids In Proteinsmentioning

confidence: 99%

Sulfenic acid chemistry, detection and cellular lifetime

Gupta

Carroll

2014

Biochimica et Biophysica Acta (BBA) - General Subjects

383

399

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“…Several early studies of protein-SOH formation demonstrated the ability of mild reducing agents to reverse this modification and, in turn, regenerate the cysteine thiol at the site of modification (figure 3a). Trivalent arsenicals such as sodium arsenite and phenyl arsene oxide reduced GAPDH-SOH and the specificity of these reductants for SOH versus disulfides was a strong early indication for the existence of protein-SOH (17, 19, 102). Other mild reducing agents like sodium borohydride, ascorbate and azide were also shown to reverse the SOH modification (19, 103).…”

Section: Reactivity Of Protein-soh Intermediatesmentioning

confidence: 99%

Formation, Reactivity, and Detection of Protein Sulfenic Acids

Kettenhofen

Wood

2010

Chem. Res. Toxicol.

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It has become clear in recent decades that the post-translational modification of protein cysteine residues is a crucial regulatory event in biology. Evidence supports the reversible oxidation of cysteine thiol groups as a mechanism of redox-based signal transduction while the accumulation of proteins with irreversible thiol oxidations is a hallmark of stress-induced cellular damage. The initial formation of cysteine sulfenic acid (SOH) derivatives, along with the reactive properties of this functional group, serves as a crossroads whereby the local redox environment may dictate the progression of either regulatory or pathological outcomes. Protein-SOH are established as transient intermediates in the formation of more stable cysteine oxidation products both under basal conditions and in response to several redox-active extrinsic compounds. This review details both direct and multi-step chemical routes proposed to generate protein-SOH, the spectrum of secondary reactions that may follow their initial formation and the arsenal of experimental tools available for their detection. Both the pioneering studies that have provided a framework for our current understanding of protein-SOH as well as state-of-the-art proteomic strategies designed for global assessments of this post-translational modification are highlighted.

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“…Acylphosphatase activity of GAPDH was discovered by Allison et al (5)(6)(7). However, it was considered as an alternative activity of GAPDH resulting from oxidation of the essential Cys 149 of the enzyme by o-iodozobenzoate, iodine monochloride, or trinitroglycerine into a sulfenic acid derivative.…”

Section: Introductionmentioning

confidence: 99%

Mildly Oxidized Glyceraldehyde‐3‐Phosphate Dehydrogenase as a Possible Regulator of Glycolysis

et al. 2001

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SummaryIn uence of H 2 O 2 on glycolysis was investigated. A hypothesis previously formulated was tested according to which a mild oxidation of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) results in uncoupling of oxidation and phosphorylation at this step of glycolysis due to acylphosphatase activity of the oxidized enzyme. Incubation of a mixture of puri ed glycolytic enzymes, as well as a muscle extract, in the presence of 10 -100 ¹M H 2 O 2 was shown to result in an increase in the rate of glycolysis.

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The activation and inactivation of the acyl phosphatase activity of glyceraldehyde-3-phosphate dehydrogenase

Cited by 39 publications

References 31 publications

Sulfenic acid chemistry, detection and cellular lifetime

Sulfenic acid chemistry, detection and cellular lifetime

Formation, Reactivity, and Detection of Protein Sulfenic Acids

Mildly Oxidized Glyceraldehyde‐3‐Phosphate Dehydrogenase as a Possible Regulator of Glycolysis

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