Apparent equilibrium constant and mass-action ratio for sucrose-phosphate synthase in seeds of <i>Pisum sativum</i>

Lunn, John E.; Rees, Tom ap

doi:10.1042/bj2670739

Cited by 50 publications

(34 citation statements)

References 13 publications

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“…The sucrose phosphate phosphatase (SPP) family is closely related to the previous family and catalyzes the dephosphorylation of sucrose phosphate to form sucrose. 185,186 The SPP plant versions additionally have a highly conserved C-terminal domain (At2g35840 _ At in Figure 9), which we show belongs to the NTF2 class of α+β domains. 187 These domains have been previously found in a variety of enzymes, such as the steroid delta-isomerase and scytalone dehydratase, as well as small moleculebinding proteins such as the orange carotenoid protein.…”

Section: C2 Caps: the Cof Phosphatase Assemblage And Its Constituent mentioning

confidence: 75%

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Evolutionary Genomics of the HAD Superfamily: Understanding the Structural Adaptations and Catalytic Diversity in a Superfamily of Phosphoesterases and Allied Enzymes

Burroughs¹,

Allen²,

Dunaway‐Mariano³

et al. 2006

Journal of Molecular Biology

387

520

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The HAD (haloacid dehalogenase) superfamily includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates. The availability of numerous crystal structures of representatives belonging to diverse branches of the HAD superfamily provides us with a unique opportunity to reconstruct their evolutionary history and uncover the principal determinants that led to their diversification of structure and function. To this end we present a comprehensive analysis of the HAD superfamily that identifies their unique structural features and provides a detailed classification of the entire superfamily. We show that at the highest level the HAD superfamily is unified with several other superfamilies, namely the DHH, receiver (CheY-like), von Willebrand A, TOPRIM, classical histone deacetylases and PIN/FLAP nuclease domains, all of which contain a specific form of the Rossmannoid fold. These Rossmannoid folds are distinguished from others by the presence of equivalently placed acidic catalytic residues, including one at the end of the first core β-strand of the central sheet. The HAD domain is distinguished from these related Rossmannoid folds by two key structural signatures, a "squiggle" (a single helical turn) and a "flap" (a beta hairpin motif) located immediately downstream of the first β-strand of their core Rossmanoid fold. The squiggle and the flap motifs are predicted to provide the necessary mobility to these enzymes for them to alternate between the "open" and "closed" conformations. In addition, most members of the HAD superfamily contains inserts, termed caps, occurring at either of two positions in the core Rossmannoid fold. We show that the cap modules have been independently inserted into these two stereotypic positions on multiple occasions in evolution and display extensive evolutionary diversification independent of the core catalytic domain. The first group of caps, the C1 caps, is directly inserted into the flap motif and regulates access of reactants to the active site. The second group, the C2 caps, forms a roof over the active site, and access to their internal cavities might be in part regulated by the movement of the flap. The diversification of the cap module was a major factor in the exploration of a vast substrate space in the course of the evolution of this superfamily. We show that the HAD superfamily contains 33 major families distributed across the three superkingdoms of life. Analysis of the phyletic patterns suggests that at least five distinct HAD proteins are traceable to the last universal common ancestor (LUCA) of all extant organisms. While these prototypes diverged prior to the emergence Abbreviations used: HAD, haloacid dehalogenase; PNKP, polynucleotide kinase phosphatase; KDO 8-P, deoxy-Dmannose-octulosonate 8-phosphate; CTD, carboxyl-terminal domain; PNKP, polynucleotide kinase phosphatase; LUCA, last universal common ancestor.E-mail address of the corresponding author: aravind@ncbi.nlm.nih.gov of the LUCA, t...

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Section: C2 Caps: the Cof Phosphatase Assemblage And Its Constituent mentioning

confidence: 75%

“…Some of these innovations were transmitted via lateral gene transfers to the eukaryotes at various points in their evolution, and used as is (e.g. sucrose phosphate phosphatase 185,186 ) or recruited for new functions (e.g. the chronophin subfamily 171 ).…”

Section: Post-luca Evolution Of Had Superfamilymentioning

confidence: 99%

Evolutionary Genomics of the HAD Superfamily: Understanding the Structural Adaptations and Catalytic Diversity in a Superfamily of Phosphoesterases and Allied Enzymes

Burroughs¹,

Allen²,

Dunaway‐Mariano³

et al. 2006

Journal of Molecular Biology

387

520

View full text Add to dashboard Cite

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“…Suc6P is produced by sucrose-phosphate synthase (SPS; EC 2.4.1.14), and the irreversible hydrolysis of Suc6P by SPP is essential to pull the reversible SPS reaction in the direction of sucrose synthesis (Lunn and ap Rees, 1990a). In most plants, sucrose is the main product of photosynthesis that is exported from the leaves to fuel growth and synthesis of storage reserves, such as starch and oil, and sucrose itself is often accumulated by plant cells to protect against the effects of dehydration under drought, salinity, or cold stress.…”

Section: Introductionmentioning

confidence: 99%

The Structure of a Cyanobacterial Sucrose-Phosphatase Reveals the Sugar Tongs That Release Free Sucrose in the Cell

et al. 2005

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Sucrose-phosphatase (SPP) catalyzes the final step in the pathway of sucrose biosynthesis in both plants and cyanobacteria, and the SPPs from these two groups of organisms are closely related. We have crystallized the enzyme from the cyanobacterium Synechocystis sp PCC 6803 and determined its crystal structure alone and in complex with various ligands. The protein consists of a core domain containing the catalytic site and a smaller cap domain that contains a glucose binding site. Two flexible hinge loops link the two domains, forming a structure that resembles a pair of sugar tongs. The glucose binding site plays a major role in determining the enzyme's remarkable substrate specificity and is also important for its inhibition by sucrose and glucose. It is proposed that the catalytic reaction is initiated by nucleophilic attack on the substrate by Asp9 and involves formation of a covalent phospho-Asp9-enzyme intermediate. From modeling based on the SPP structure, we predict that the noncatalytic SPP-like domain of the Synechocystis sucrose-phosphate synthase could bind sucrose-6 F -phosphate and propose that this domain might be involved in metabolite channeling between the last two enzymes in the pathway of sucrose synthesis.

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“…The reaction catalysed by SPS is not strongly irreversible, but removal of its product by sucrose phosphate phosphatase means that it is the first committed reaction in the pathway of sucrose synthesis (Lunn & apRees 1990;Krause & Stitt 1991). SPS is regulated in a sophisticated manner by a variety of mechanisms that operate at different levels and in different time frames (Stitt et al 1987;Huber, Huber & McMichael 1992;Huber & Huber 1996).…”

Section: Introductionmentioning

confidence: 99%

Potato plants contain multiple forms of sucrose phosphate synthase, which differ in their tissue distributions, their levels during development, and their responses to low temperature

Reimholz¹,

Geiger²,

Haake³

et al. 1997

Plant Cell & Environment

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Antibodies raised against a peptide fragment (residues 60-456) of potato sucrose phosphate synthase (SPS) were used to investigate whether potato plants contain multiple forms of SPS. When a partially purified preparation of SPS from cold-stored potato tubers was separated on 5 % polyacrylamide gel electrophoresis (PAGE), four immunopositive bands were found with estimated molecular weights of 125, 127, 135 and 145 kDa. These bands were also found in rapidly prepared extracts and were termed SPS-la, SPS-lb, SPS-2 and SPS-3, respectively. Direct evidence that SPS-la and SPS-lb represent active SPS was provided by the finding that both are greatly reduced in plants expressing an antisense sequence derived from the potato leaf SPS gene. SPS-2 was not decreased in the antisense plants, indicating that it has a significantly different sequence. Evidence that SPS-2 represents active SPS was obtained by showing that the amount of SPS-la and SPS-lb protein remaining in the leaves and tubers of antisense potato plants was too low to account for the remaining SPS activity. The four immunopositive SPS forms had different tissue distributions. SPS-la was the major form in all tissues except petals, sepals and stamens. SPS-lb and SPS-2 were absent in very young growing tissues hut were present as minor forms in source leaves and sprouting tubers. The SPS-lh level was especially high in petals and sepals, and the SPS-

show abstract

Apparent equilibrium constant and mass-action ratio for sucrose-phosphate synthase in seeds of Pisum sativum

Cited by 50 publications

References 13 publications

Evolutionary Genomics of the HAD Superfamily: Understanding the Structural Adaptations and Catalytic Diversity in a Superfamily of Phosphoesterases and Allied Enzymes

Evolutionary Genomics of the HAD Superfamily: Understanding the Structural Adaptations and Catalytic Diversity in a Superfamily of Phosphoesterases and Allied Enzymes

The Structure of a Cyanobacterial Sucrose-Phosphatase Reveals the Sugar Tongs That Release Free Sucrose in the Cell

Potato plants contain multiple forms of sucrose phosphate synthase, which differ in their tissue distributions, their levels during development, and their responses to low temperature

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