Recent Results on the Assimilatory Sulfate Reduction: APS-Kinase and the Reduction of APS to Cysteine in Higher Plants

Schwenn, Jens D.; Urlaub, Herbert

doi:10.1007/978-3-642-67919-3_29

Cited by 6 publications

(2 citation statements)

References 21 publications

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“…Assimilatory SO 4 2− reduction is a unique and complex process that requires the binding of SO 4 2− oxyanions to a variety of specific transporters and the distribution of these oxyanions between subcellular compartments. The first step is controlled by an ATP sulfurylase enzyme that releases adenosine‐5′‐phosphosulfate (APS), allowing the activation and reduction of SO 4 2− by two enzymatic systems working in succession to release APS‐sulfhydryl (APS‐SH) as an end product . The molecule is then transferred by APS‐kinase to O‐acetyl‐serine, whose C skeleton becomes cysteine (Cys) after the binding of an S atom through the mediation of a thiol‐lyase .…”

Section: Sulfur In the Plant Kingdommentioning

confidence: 99%

“…The first step is controlled by an ATP sulfurylase enzyme that releases adenosine-5′-phosphosulfate (APS), allowing the activation and reduction of SO4 2by two enzymatic systems working in succession to release APS-sulfhydryl (APS-SH) as an end product. 18 The molecule is then transferred by APS-kinase to O-acetylserine, whose C skeleton becomes cysteine (Cys) after the binding of an S atom through the mediation of a thiollyase. 17 Cys operates as the precursor of methionine (Met) and of most S-containing compounds (g-glutamylcysteine-glycine or glutathione [GSH], S-adenosylmethionine [SAM], hormones, vitamins, cofactors) except for taurine (Tau), which is virtually absent from the plant kingdom.…”

Section: Sulfur In the Plant Kingdommentioning

confidence: 99%

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Nutritional essentiality of sulfur in health and disease

Ingenbleek¹,

Kimura

2013

Nutr Rev

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Sulfur is the seventh most abundant element measurable in the human body and is supplied mainly by the intake of methionine (Met), an indispensable amino acid found in plant and animal proteins. Met controls the initiation of protein synthesis, governs major metabolic and catalytic activities, and may undergo reversible redox processes safeguarding protein integrity. Withdrawal of Met from customary diets causes the greatest downsizing of lean body mass following either unachieved replenishment (malnutrition) or excessive losses (inflammation). These physiopathologically unrelated morbidities nevertheless stimulate comparable remethylation reactions from homocysteine, indicating that Met homeostasis benefits from high metabolic priority. Inhibition of cystathionine-β-synthase activity causes the upstream sequestration of homocysteine and the downstream drop in cysteine and glutathione. Consequently, the enzymatic production of hydrogen sulfide and the nonenzymatic reduction of elemental sulfur to hydrogen sulfide are impaired. Sulfur operates as cofactor of several enzymes critically involved in the regulation of oxidative processes. A combination of malnutrition and nutritional deprivation of sulfur maximizes the risk of cardiovascular disorders and stroke, constituting a novel clinical entity that threatens plant-eating population groups.

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Section: Sulfur In the Plant Kingdommentioning

confidence: 99%

Section: Sulfur In the Plant Kingdommentioning

confidence: 99%

Nutritional essentiality of sulfur in health and disease

Ingenbleek¹,

Kimura

2013

Nutr Rev

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The Reduction of Sulfate and the Oxidation of Sulfide

Huxtable

1986

Biochemistry of Sulfur

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Properties of the purified APS-kinase from Escherichia coli and Saccharomyces cerevisiae

Schriek

Schwenn

1986

Arch. Microbiol.

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Adenylylsulphate kinase (EC 2.7.1.25, ATP:adenylylsulphate 3'-phosphotransferase) has been isolated from Escherichia coli and from Saccharomyces cerevisiae. As major steps of purification, affinity chromatography on Sepharose CL 6B ("blue" or "red") and chromatofocusing on polybuffer PBE 94tm were employed. The proteins were obtained in nearly homogeneous state after five chromatographic steps. The isolated enzymes from both sources appeared predominantly to exist as dimers. Upon reduction of the protein with dithiothreitol, it disintegrated into assumingly identical smaller subunits (E. coli rom Mr 90-85,000 to 45-40,000 and S. cerevisiae from 52-49,500 to 28-29,500). Both forms, dimer and monomer were found catalytically active. Preincubation of the isolated enzyme from either source in the presence of thioredoxin plus DTT, reduced glutathione or DTT increased the activity significantly. Treatment of the enzyme with SH-blocking reagents inactivated the enzyme irreversibly as compared to the inactivation caused by oxidants (2,6-dichlorophenol-indophenol, ferricyanide or oxydized glutathione). This oxidant induced inactivation was less pronounced for the fungal enzyme than for the bacterial protein. The enzyme from E. coli required thioredoxin in order to alleviate the GSSG-induced inactivation.

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Recent Results on the Assimilatory Sulfate Reduction: APS-Kinase and the Reduction of APS to Cysteine in Higher Plants

Cited by 6 publications

References 21 publications

Nutritional essentiality of sulfur in health and disease

Nutritional essentiality of sulfur in health and disease

The Reduction of Sulfate and the Oxidation of Sulfide

Properties of the purified APS-kinase from Escherichia coli and Saccharomyces cerevisiae

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