ArticleThe Biochemical journal2002
Characterization and expression of human bifunctional 3'-phosphoadenosine 5'-phosphosulphate synthase isoforms.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 70 citations in OpenAlex.
- Bone Phenotype is Always Present But Androgen Excess is Less Frequently Seen in PAPSS2 DeficiencyJournal of clinical research in pediatric endocrinology · 2024Review
- Genome-wide CRISPR screen for HSV-1 host factors reveals PAPSS1 contributes to heparan sulfate synthesis.Communications biology · 2022Article
- GRASP depletion-mediated Golgi fragmentation impairs glycosaminoglycan synthesis, sulfation, and secretion.Cellular and molecular life sciences : CMLS · 2022Article
- Role of aspartic acid residues D87 and D89 in APS kinase domain of human 3'-phosphoadenosine 5'-phosphosulfate synthase 1 and 2b: A commonality with phosphatases/kinases.Biochemistry and biophysics reports · 2021Article
- Review
- Congenital Disorders of Deficiency in Glycosaminoglycan Biosynthesis.Frontiers in genetics · 2021Review
- An Overview ofFrontiers in cell and developmental biology · 2021Review
- Enzyme Kinetics of PAPS-Sulfotransferase.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Skeletal Dysplasias Caused by Sulfation Defects.International journal of molecular sciences · 2020Review
- Sulfation pathways from red to green.The Journal of biological chemistry · 2019Review
- Enhanced PAPSS2/VCAN sulfation axis is essential for Snail-mediated breast cancer cell migration and metastasis.Cell death and differentiation · 2019Article
- Human DHEA sulfation requires direct interaction between PAPS synthase 2 and DHEA sulfotransferase SULT2A1.The Journal of biological chemistry · 2018Article
- Determinants of Glycosaminoglycan (GAG) Structure.Biomolecules · 2015Review
- Crystal structures of the kinase domain of the sulfate-activating complex in Mycobacterium tuberculosis.PloS one · 2015Article
- Heparan sulfate biosynthesis: regulation and variability.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2012Review
- 3'-Phosphoadenosine 5'-phosphosulfate (PAPS) synthases, naturally fragile enzymes specifically stabilized by nucleotide binding.The Journal of biological chemistry · 2012Article
- Quantitative proteomics analysis of chondrogenic differentiation of C3H10T1/2 mesenchymal stem cells by iTRAQ labeling coupled with on-line two-dimensional LC/MS/MS.Molecular & cellular proteomics : MCP · 2010Article
- Sulfate activation enzymes: phylogeny and association with pyrophosphatase.Journal of molecular evolution · 2009Article
- The host cell sulfonation pathway contributes to retroviral infection at a step coincident with provirus establishment.PLoS pathogens · 2008Article
- Elucidation of the active conformation of the APS-kinase domain of human PAPS synthetase 1.Journal of molecular biology · 2007Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
Sulphonation, a fundamental process essential for normal growth and development, requires the sulphonate donor molecule 3'-phosphoadenosine 5'-phosphosulphate (PAPS), which is produced from ATP and inorganic sulphate by the bifunctional enzyme PAPS synthase. In humans, two genes encode isoenzymes that are 77% identical at the amino acid level, and alternative splicing creates two subtypes of PAPS synthase 2. The question as to whether distinctions in amino acid composition are reflected in differences in activity has been examined. The specific activity of the PAPS synthase 2 subtypes is 10- to 15-fold higher than that for PAPS synthase 1. The greater catalytic efficiency of the PAPS synthase 2 subtypes is demonstrated further by the 3- to 6-fold higher k(cat)/K(m) ratios for ATP and inorganic sulphate as compared with the ratios for PAPS synthase 1. In humans, PAPS synthase 1 is expressed ubiquitously, and is the dominant isoform in most tissues, whereas expression of the PAPS synthase 2 subtypes is variable and tissue-specific. It is noteworthy that, similar to other human tissues, PAPS synthase 1 also appears to be the dominant isoform expressed in cartilage. The latter finding initially created a conundrum, since there is a specific human dwarfing disorder that is known to be caused by a mutation in the PAPS synthase 2 gene. This apparent enigma would seem to be resolved by examination of cartilage from guinea-pigs as an animal model. Similar to humans, cartilage from mature animals predominantly expresses PAPS synthase 1. In contrast, expression of PAPS synthase 1 is relatively low in the cartilage of immature guinea-pigs, including the growth plate of long bones, whereas PAPS synthase 2 is the highly expressed isoenzyme.
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