ATP Sulfurylase from Higher Plants: Kinetic and Structural Characterization of the Chloroplast and Cytosol Enzymes from Spinach Leaf

Renosto, Franco; Patel, Harshila; Martin, Robert L.; Thomassian, C.; Zimmerman, G.; Segel, Irwin H.

doi:10.1006/abbi.1993.1590

Cited by 88 publications

(74 citation statements)

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“…However, since most of the total ATP sulfurylase is plastid localized (Lunn et al, 1990;Renosto et al, 1993; this study) and ATP sulfurylase activity is present in excess over that required for normal rates of sulfate assimilation (Lee, 1999) it is difficult to imagine the conditions under which cytosolic ATP sulfurylase might contribute significantly toward sulfate reduction or why the level of this enzyme increases just at the time when APS reductase is declining. More likely is the idea that cytosolic ATP sulfurylase has a specialized function.…”

Section: Discussionmentioning

confidence: 99%

“…However, all known sulfotransferases that carry out sulfate esterification are cytosolic enzymes (Varin et al, 1997), indicating the need for activated sulfate in the cytosol. A cytosolic isoenzyme of ATP sulfurylase has been reported in some plant species (Lunn et al, 1990;Renosto et al, 1993). Two catalytically distinct forms of ATP sulfurylase have been purified from Euglena gracilis, one of which exists in mitochondria (Li et al, 1991).…”

Section: Cys Is Formed When Sulfide Reacts With O-acetyl Ser (Oas) Mementioning

confidence: 99%

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Differential Subcellular Localization and Expression of ATP Sulfurylase and 5′-Adenylylsulfate Reductase during Ontogenesis of Arabidopsis Leaves Indicates That Cytosolic and Plastid Forms of ATP Sulfurylase May Have Specialized Functions

2000

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ATP sulfurylase and 5Ј-adenylylsulfate (APS) reductase catalyze two reactions in the sulfate assimilation pathway. Cell fractionation of Arabidopsis leaves revealed that ATP sulfurylase isoenzymes exist in the chloroplast and the cytosol, whereas APS reductase is localized exclusively in chloroplasts. During development of Arabidopsis plants the total activity of ATP sulfurylase and APS reductase declines by 3-fold in leaves. The decline in APS reductase can be attributed to a reduction of enzyme during aging of individual leaves, the highest activity occurring in the youngest leaves and the lowest in fully expanded leaves. By contrast, total ATP sulfurylase activity declines proportionally in all the leaves. The distinct behavior of ATP sulfurylase can be attributed to reciprocal expression of the chloroplast and cytosolic isoenzymes. The chloroplast form, representing the more abundant isoenzyme, declines in parallel with APS reductase during aging; however, the cytosolic form increases over the same period. In total, the results suggest that cytosolic ATP sulfurylase plays a specialized function that is probably unrelated to sulfate reduction. A plausible function could be in generating APS for sulfation reactions.

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Section: Discussionmentioning

confidence: 99%

Section: Cys Is Formed When Sulfide Reacts With O-acetyl Ser (Oas) Mementioning

confidence: 99%

Differential Subcellular Localization and Expression of ATP Sulfurylase and 5′-Adenylylsulfate Reductase during Ontogenesis of Arabidopsis Leaves Indicates That Cytosolic and Plastid Forms of ATP Sulfurylase May Have Specialized Functions

2000

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“…Because of ATP-Sase's position as the initial enzyme in S04'^ metabolism, and due to its enzyme kinetics, it is often examined for rate and pathway regulation in S reduction. The enzyme ATP-Sase is found predominantly in leaf chloroplasts near a ready ATP supply (Brunold, 1990;Renosto et al, 1993); however, it can also be found in root cytoplasms (Leustek, 1996;Lappartient and Touraine, 1997) were ATP is generally not considered to be in excess. Root ATP-Sase in Brassica napus is inhibited by GHS (Lappartient and Touraine, 1997).…”

Section: Sulfate Activationmentioning

confidence: 99%

Distribution and Mobilization of Sulfur during Soybean Reproduction

Naeve

Shibles

2005

Crop Science

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This manuscript has been reproduced from the microfilm master. UMI films the text directly from the original or copy submitted. Thus, some thesis and dissertation copies are in typewriter face, while others may be from any type of computer printer.The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleedthrough, substandard margins, and improper alignment can adversely aflFect reproduction.In the unlikely event that the author did not send UMI a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyright material had to be removed, a note will indicate the deletion.Oversize materials (e.g., maps, drawings, charts) are reproduced by sectioning the original, beginning at the upper left-hand comer and continuing from left to right in equal sections with small overiaps. Each original is also photographed in one exposure and is included in reduced form at the back of the book.Photographs included in the original manuscript have been reproduced xerographically in this copy. Higher quality 6" x 9" black and white photographic prints are available for any photographs or illustrations appearing in this copy for an additional charge. Contact UMI directly to order. UMI GENERAL INTRODUCTION Dissertation OrganizationA discussion of results obtained from studies conducted on soybean sulfur metabolism is presented here as two manuscripts for the eventual submission for publication in Crop Science. A general introduction precedes these manuscripts giving a broad overview of plant sulfur metabolism, sulfur transpon, and soybean seed protein accumulation. A general conclusion chapter follows, summarizing findings of the two studies presented here.References cited in this dissertation are coalesced and listed at the end of the dissertation.The first manuscript paper discusses the distribution and mobilization of sulfur acquired by soybean during seed development, while the second takes up nitrogen and sulfur stress effects on mobilization of sulfur to developing soybean seed. RationaleSoybean seed is an important source of dietary protein for livestock and humans;however, soybean seed protein itself contains low, potentially growth-limiting concentrations of the sulfur-containing amino acids, methionine (met) and cysteine (cys), when used as the sole protein source for monogastric mammals. Methionine and cys are considered "essential amino acids" indicating that they cannot be synthesized de novo by monogastric mammals (Food and Agricultural Organization and World Health Organization, 1989). Methionine is the primary essential amino acid that is deficient in legume proteins (DeLumen et al., 1997), and soybean seed proteins contain about half of the met found in FAO's (Food and 2 Agricultural Organization) egg protein standard (Burton et al., 1982). This limitation reveals itself in high protein rations when the majority of the ingested protein is derived from soybean....

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“…ATP sulfurylase isoforms are localized to different organelles with the chloroplast form associated with reductive sulfate assimilation and accounting for the highest portion of enzyme activity (35,36). For example, soybean contains four isoforms (GmATPS1-4), all of which are predicted to localize to the chloroplast (5).…”

mentioning

confidence: 99%

“…For example, soybean contains four isoforms (GmATPS1-4), all of which are predicted to localize to the chloroplast (5). Expression of ATP sulfurylase is highest in young leaves, the early stages of seed development, and the elongation zone of roots (19,(35)(36)(37)(38). Traditionally, ATP sulfurylase has not been considered to be important for the control of flux through the sulfate assimilation pathway (39).…”

mentioning

confidence: 99%

Structure and Mechanism of Soybean ATP Sulfurylase and the Committed Step in Plant Sulfur Assimilation

Herrmann

Ravilious

McKinney

et al. 2014

Journal of Biological Chemistry

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Background: ATP sulfurylase catalyzes the energetically unfavorable formation of adenosine 5Ј-phosphosulfate in plant sulfur assimilation. Results: Structural and kinetic analyses identifies key active site residues. Conclusion: A reaction mechanism involving distortion of nucleotide conformation and stabilizing interactions is proposed. Significance: These results provide the first molecular insights on a plant ATP sulfurylase and the committed step of plant sulfur assimilation.

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ATP Sulfurylase from Higher Plants: Kinetic and Structural Characterization of the Chloroplast and Cytosol Enzymes from Spinach Leaf

Cited by 88 publications

References 0 publications

Differential Subcellular Localization and Expression of ATP Sulfurylase and 5′-Adenylylsulfate Reductase during Ontogenesis of Arabidopsis Leaves Indicates That Cytosolic and Plastid Forms of ATP Sulfurylase May Have Specialized Functions

Differential Subcellular Localization and Expression of ATP Sulfurylase and 5′-Adenylylsulfate Reductase during Ontogenesis of Arabidopsis Leaves Indicates That Cytosolic and Plastid Forms of ATP Sulfurylase May Have Specialized Functions

Distribution and Mobilization of Sulfur during Soybean Reproduction

Structure and Mechanism of Soybean ATP Sulfurylase and the Committed Step in Plant Sulfur Assimilation

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