PAPSS1 - Encyclopedia Information

From Wikipedia, the free encyclopedia

PAPSS1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1X6V, 1XJQ, 1XNJ, 2OFW, 2OFX, 2PEY, 2PEZ, 2QJF

Identifiers

PAPSS1, ATPSK1, PAPSS, SK1, 3'-phosphoadenosine 5'-phosphosulfate synthase 1

External IDs

OMIM: 603262; MGI: 1330587; HomoloGene: 81740; GeneCards: PAPSS1; OMA: PAPSS1 - orthologs

Gene location ( Human)

Chr.	Chromosome 4 (human)^[1]

Band	4q25	Start	107,590,276 bp^[1]
Band	4q25	End	107,720,234 bp^[1]

Gene location ( Mouse)

Chr.	Chromosome 3 (mouse)^[2]

Band	3 G3\|3 61.05 cM	Start	131,270,529 bp^[2]
Band	3 G3\|3 61.05 cM	End	131,349,432 bp^[2]

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

inferior ganglion of vagus nerve

secondary oocyte

pons

bronchial epithelial cell

subthalamic nucleus

pylorus

corpus callosum

endometrium

superior vestibular nucleus

Brodmann area 46

Top expressed in

vestibular membrane of cochlear duct

left colon

submandibular gland

vestibular sensory epithelium

lacrimal gland

migratory enteric neural crest cell

medullary collecting duct

ileum

human fetus

utricle

More reference expression data


More reference expression data

Gene ontology
Molecular function	transferase activity nucleotide binding nucleotidyltransferase activity catalytic activity ATP binding kinase activity sulfate adenylyltransferase (ATP) activity protein homodimerization activity adenylylsulfate kinase activity
Cellular component	cytosol
Biological process	skeletal system development metabolism phosphorylation sulfate assimilation 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process
Sources: Amigo / QuickGO

Species

Human

Mouse


9061


23971


ENSG00000138801


ENSMUSG00000028032


O43252


Q60967

RefSeq (mRNA)


NM_005443


NM_001289477 NM_001289478 NM_001289479 NM_011863

RefSeq (protein)


NP_005434


NP_001276406 NP_001276407 NP_001276408 NP_035993

Location (UCSC)

Chr 4: 107.59 – 107.72 Mb

Chr 3: 131.27 – 131.35 Mb

PubMed search

^[3]

^[4]

View/Edit Human

View/Edit Mouse

Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 is an enzyme that in humans is encoded by the PAPSS1 gene.^[5]^[6]^[7]

Three-prime-phosphoadenosine 5-prime-phosphosulfate ( PAPS) is the sulfate donor cosubstrate for all sulfotransferase (SULT) enzymes (Xu et al., 2000). SULTs catalyze the sulfate conjugation of many endogenous and exogenous compounds, including drugs and other xenobiotics. In humans, PAPS is synthesized from adenosine 5-prime triphosphate (ATP) and inorganic sulfate by 2 isoforms, PAPSS1 and PAPSS2 (MIM 603005).[supplied by OMIM]^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000138801 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028032 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Girard JP, Baekkevold ES, Amalric F (May 1998). "Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase". FASEB J. 12 (7): 603–12. doi: 10.1096/fasebj.12.7.603. PMID 9576487. S2CID 19530341.
^ ul Haque MF, King LM, Krakow D, Cantor RM, Rusiniak ME, Swank RT, Superti-Furga A, Haque S, Abbas H, Ahmad W, Ahmad M, Cohn DH (Oct 1998). "Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse". Nat Genet. 20 (2): 157–62. doi: 10.1038/2458. PMID 9771708. S2CID 13108930.
^ ^a ^b "Entrez Gene: PAPSS1 3'-phosphoadenosine 5'-phosphosulfate synthase 1".

Further reading

Venkatachalam KV (2004). "Human 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase: biochemistry, molecular biology and genetic deficiency". IUBMB Life. 55 (1): 1–11. doi: 10.1080/1521654031000072148. PMID 12716056. S2CID 37733913.
Yanagisawa K, Sakakibara Y, Suiko M, et al. (1998). "cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme". Biosci. Biotechnol. Biochem. 62 (5): 1037–40. doi: 10.1271/bbb.62.1037. PMID 9648242.
Venkatachalam KV, Akita H, Strott CA (1998). "Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains". J. Biol. Chem. 273 (30): 19311–20. doi: 10.1074/jbc.273.30.19311. PMID 9668121.
Kurima K, Warman ML, Krishnan S, et al. (1998). "A member of a family of sulfate-activating enzymes causes murine brachymorphism". Proc. Natl. Acad. Sci. U.S.A. 95 (15): 8681–5. Bibcode: 1998PNAS...95.8681K. doi: 10.1073/pnas.95.15.8681. PMC 21136. PMID 9671738.
Venkatachalam KV, Fuda H, Koonin EV, Strott CA (1999). "Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase". J. Biol. Chem. 274 (5): 2601–4. doi: 10.1074/jbc.274.5.2601. PMID 9915785.
Besset S, Vincourt JB, Amalric F, Girard JP (2000). "Nuclear localization of PAPS synthetase 1: a sulfate activation pathway in the nucleus of eukaryotic cells". FASEB J. 14 (2): 345–54. doi: 10.1096/fasebj.14.2.345. PMID 10657990. S2CID 9024784.
Xu ZH, Otterness DM, Freimuth RR, et al. (2000). "Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization". Biochem. Biophys. Res. Commun. 268 (2): 437–44. doi: 10.1006/bbrc.2000.2123. PMID 10679223.
Fuda H, Shimizu C, Lee YC, et al. (2002). "Characterization and expression of human bifunctional 3'-phosphoadenosine 5'-phosphosulphate synthase isoforms". Biochem. J. 365 (Pt 2): 497–504. doi: 10.1042/BJ20020044. PMC 1222679. PMID 11931637.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode: 2002PNAS...9916899M. doi: 10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Harjes S, Scheidig A, Bayer P (2004). "Expression, purification and crystallization of human 3'-phosphoadenosine-5'-phosphosulfate synthetase 1". Acta Crystallogr. D. 60 (Pt 2): 350–2. doi: 10.1107/S0907444903027628. PMID 14747722.
Lansdon EB, Fisher AJ, Segel IH (2004). "Human 3'-phosphoadenosine 5'-phosphosulfate synthetase (isoform 1, brain): kinetic properties of the adenosine triphosphate sulfurylase and adenosine 5'-phosphosulfate kinase domains". Biochemistry. 43 (14): 4356–65. doi: 10.1021/bi049827m. PMID 15065880.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi: 10.1101/gr.2596504. PMC 528928. PMID 15489334.
Harjes S, Bayer P, Scheidig AJ (2005). "The crystal structure of human PAPS synthetase 1 reveals asymmetry in substrate binding". J. Mol. Biol. 347 (3): 623–35. doi: 10.1016/j.jmb.2005.01.005. PMID 15755455.
Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi: 10.1016/j.cell.2005.08.029. hdl: 11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi: 10.1101/gr.4039406. PMC 1356129. PMID 16344560.
Sekulic N, Konrad M, Lavie A (2007). "Structural mechanism for substrate inhibition of the adenosine 5'-phosphosulfate kinase domain of human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 and its ramifications for enzyme regulation". J. Biol. Chem. 282 (30): 22112–21. doi: 10.1074/jbc.M701713200. hdl: 11858/00-001M-0000-0012-E08D-D. PMID 17540769.

PDB gallery

1x6v: The crystal structure of human 3'-phosphoadenosine-5'-phosphosulfate synthetase 1
1xjq: ADP Complex OF HUMAN PAPS SYNTHETASE 1
1xnj: APS complex of human PAPS synthetase 1
2ofw: Crystal structure of the APSK domain of human PAPSS1 complexed with 2 APS molecules
2ofx: crystal structure of the APSK domain of human PAPSS1 in complex with ADPMg and PAPS
2pey: Crystal structure of deletion mutant of APS-kinase domain of human PAPS-synthetase 1
2pez: Crystal structure of deletion mutant of APS-kinase domain of human PAPS-synthetase 1 in complex with cyclic PAPS and dADP

Transferases: phosphorus-containing groups ( EC 2.7)

2.7.1-2.7.4:
phosphotransferase/ kinase
( PO₄)

2.7.1: OH acceptor	Hexo- Gluco- Fructo- Hepatic Galacto- Phosphofructo- 1 Liver Muscle Platelet 2 Riboflavin Shikimate Thymidine ADP-thymidine NAD⁺ Glycerol Pantothenate Mevalonate Pyruvate Deoxycytidine PFP Diacylglycerol Phosphoinositide 3 Class I PI 3 Class II PI 3 Sphingosine Glucose-1,6-bisphosphate synthase
2.7.2: COOH acceptor	Phosphoglycerate Aspartate kinase
2.7.3: N acceptor	Creatine
2.7.4: PO₄ acceptor	Phosphomevalonate Adenylate Nucleoside-diphosphate Uridylate Guanylate Thiamine-diphosphate

2.7.6: diphosphotransferase
( P₂O₇)

2.7.7: nucleotidyltransferase
( PO₄-nucleoside)

DNA polymerase	DNA-directed DNA polymerase I/A γ θ ν T7 Taq II/B α δ ε ζ Pfu III/C IV/X β λ μ TDT V/Y η ι κ RNA-directed DNA polymerase Reverse transcriptase Telomerase
RNA polymerase	Template-directed RNA polymerase I II III IV V ssRNAP POLRMT Primase 1 2 PrimPol RNA-dependent RNA polymerase Polyadenylation PAP PNPase

Phosphorolytic
3' to 5' exoribonuclease

Nucleotidyltransferase

Guanylyltransferase

mRNA capping enzyme

Other

Recombinase ( Integrase)
Transposase

2.7.8: miscellaneous

Phosphatidyltransferases	CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase CDP-diacylglycerol—serine O-phosphatidyltransferase CDP-diacylglycerol—inositol 3-phosphatidyltransferase CDP-diacylglycerol—choline O-phosphatidyltransferase
Glycosyl-1-phosphotransferase	N-acetylglucosamine-1-phosphate transferase

2.7.10-2.7.13: protein kinase
( PO₄; protein acceptor)

2.7.10: protein-tyrosine	see tyrosine kinases
2.7.11: protein-serine/threonine	see serine/threonine-specific protein kinases
2.7.12: protein-dual-specificity	see serine/threonine-specific protein kinases
2.7.13: protein-histidine	Protein-histidine pros-kinase Protein-histidine tele-kinase Histidine kinase

glycosaminoglycan anabolism

Heparan sulfate: EXT1; EXT2

Chondroitin sulfate: PAPSS1; PAPSS2

glycosaminoglycan catabolism

Hunter, Hurler	Iduronate-2-sulfatase Iduronidase
Sanfilippo, Sly	Heparan sulfamidase N-acetyltransferase Alpha-N-acetylglucosaminidase Glucuronidase N-acetylglucosamine-6-sulfatase
Morquio/ Maroteaux-Lamy	Arylsulfatase B Galactosamine-6 sulfatase Beta-galactosidase ( GLB1)

This article on a gene on human chromosome 4 is a stub. You can help Wikipedia by expanding it.

Retrieved from " https://en.wikipedia.org/?title=PAPSS1&oldid=1215911978"

Hidden categories:

From Wikipedia, the free encyclopedia

PAPSS1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1X6V, 1XJQ, 1XNJ, 2OFW, 2OFX, 2PEY, 2PEZ, 2QJF

Identifiers

PAPSS1, ATPSK1, PAPSS, SK1, 3'-phosphoadenosine 5'-phosphosulfate synthase 1

External IDs

OMIM: 603262; MGI: 1330587; HomoloGene: 81740; GeneCards: PAPSS1; OMA: PAPSS1 - orthologs

Gene location ( Human)

Chr.	Chromosome 4 (human)^[1]

Band	4q25	Start	107,590,276 bp^[1]
Band	4q25	End	107,720,234 bp^[1]

Gene location ( Mouse)

Chr.	Chromosome 3 (mouse)^[2]

Band	3 G3\|3 61.05 cM	Start	131,270,529 bp^[2]
Band	3 G3\|3 61.05 cM	End	131,349,432 bp^[2]

RNA expression pattern

Human

Mouse (ortholog)

Top expressed in

inferior ganglion of vagus nerve

secondary oocyte

pons

bronchial epithelial cell

subthalamic nucleus

pylorus

corpus callosum

endometrium

superior vestibular nucleus

Brodmann area 46

Top expressed in

vestibular membrane of cochlear duct

left colon

submandibular gland

vestibular sensory epithelium

lacrimal gland

migratory enteric neural crest cell

medullary collecting duct

ileum

human fetus

utricle

More reference expression data


More reference expression data

Gene ontology
Molecular function	transferase activity nucleotide binding nucleotidyltransferase activity catalytic activity ATP binding kinase activity sulfate adenylyltransferase (ATP) activity protein homodimerization activity adenylylsulfate kinase activity
Cellular component	cytosol
Biological process	skeletal system development metabolism phosphorylation sulfate assimilation 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process
Sources: Amigo / QuickGO

Species

Human

Mouse


9061


23971


ENSG00000138801


ENSMUSG00000028032


O43252


Q60967

RefSeq (mRNA)


NM_005443


NM_001289477 NM_001289478 NM_001289479 NM_011863

RefSeq (protein)


NP_005434


NP_001276406 NP_001276407 NP_001276408 NP_035993

Location (UCSC)

Chr 4: 107.59 – 107.72 Mb

Chr 3: 131.27 – 131.35 Mb

PubMed search

^[3]

^[4]

View/Edit Human

View/Edit Mouse

Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 is an enzyme that in humans is encoded by the PAPSS1 gene.^[5]^[6]^[7]

Three-prime-phosphoadenosine 5-prime-phosphosulfate ( PAPS) is the sulfate donor cosubstrate for all sulfotransferase (SULT) enzymes (Xu et al., 2000). SULTs catalyze the sulfate conjugation of many endogenous and exogenous compounds, including drugs and other xenobiotics. In humans, PAPS is synthesized from adenosine 5-prime triphosphate (ATP) and inorganic sulfate by 2 isoforms, PAPSS1 and PAPSS2 (MIM 603005).[supplied by OMIM]^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000138801 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028032 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Girard JP, Baekkevold ES, Amalric F (May 1998). "Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase". FASEB J. 12 (7): 603–12. doi: 10.1096/fasebj.12.7.603. PMID 9576487. S2CID 19530341.
^ ul Haque MF, King LM, Krakow D, Cantor RM, Rusiniak ME, Swank RT, Superti-Furga A, Haque S, Abbas H, Ahmad W, Ahmad M, Cohn DH (Oct 1998). "Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse". Nat Genet. 20 (2): 157–62. doi: 10.1038/2458. PMID 9771708. S2CID 13108930.
^ ^a ^b "Entrez Gene: PAPSS1 3'-phosphoadenosine 5'-phosphosulfate synthase 1".

Further reading

Venkatachalam KV (2004). "Human 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase: biochemistry, molecular biology and genetic deficiency". IUBMB Life. 55 (1): 1–11. doi: 10.1080/1521654031000072148. PMID 12716056. S2CID 37733913.
Yanagisawa K, Sakakibara Y, Suiko M, et al. (1998). "cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme". Biosci. Biotechnol. Biochem. 62 (5): 1037–40. doi: 10.1271/bbb.62.1037. PMID 9648242.
Venkatachalam KV, Akita H, Strott CA (1998). "Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains". J. Biol. Chem. 273 (30): 19311–20. doi: 10.1074/jbc.273.30.19311. PMID 9668121.
Kurima K, Warman ML, Krishnan S, et al. (1998). "A member of a family of sulfate-activating enzymes causes murine brachymorphism". Proc. Natl. Acad. Sci. U.S.A. 95 (15): 8681–5. Bibcode: 1998PNAS...95.8681K. doi: 10.1073/pnas.95.15.8681. PMC 21136. PMID 9671738.
Venkatachalam KV, Fuda H, Koonin EV, Strott CA (1999). "Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase". J. Biol. Chem. 274 (5): 2601–4. doi: 10.1074/jbc.274.5.2601. PMID 9915785.
Besset S, Vincourt JB, Amalric F, Girard JP (2000). "Nuclear localization of PAPS synthetase 1: a sulfate activation pathway in the nucleus of eukaryotic cells". FASEB J. 14 (2): 345–54. doi: 10.1096/fasebj.14.2.345. PMID 10657990. S2CID 9024784.
Xu ZH, Otterness DM, Freimuth RR, et al. (2000). "Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization". Biochem. Biophys. Res. Commun. 268 (2): 437–44. doi: 10.1006/bbrc.2000.2123. PMID 10679223.
Fuda H, Shimizu C, Lee YC, et al. (2002). "Characterization and expression of human bifunctional 3'-phosphoadenosine 5'-phosphosulphate synthase isoforms". Biochem. J. 365 (Pt 2): 497–504. doi: 10.1042/BJ20020044. PMC 1222679. PMID 11931637.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode: 2002PNAS...9916899M. doi: 10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Harjes S, Scheidig A, Bayer P (2004). "Expression, purification and crystallization of human 3'-phosphoadenosine-5'-phosphosulfate synthetase 1". Acta Crystallogr. D. 60 (Pt 2): 350–2. doi: 10.1107/S0907444903027628. PMID 14747722.
Lansdon EB, Fisher AJ, Segel IH (2004). "Human 3'-phosphoadenosine 5'-phosphosulfate synthetase (isoform 1, brain): kinetic properties of the adenosine triphosphate sulfurylase and adenosine 5'-phosphosulfate kinase domains". Biochemistry. 43 (14): 4356–65. doi: 10.1021/bi049827m. PMID 15065880.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi: 10.1101/gr.2596504. PMC 528928. PMID 15489334.
Harjes S, Bayer P, Scheidig AJ (2005). "The crystal structure of human PAPS synthetase 1 reveals asymmetry in substrate binding". J. Mol. Biol. 347 (3): 623–35. doi: 10.1016/j.jmb.2005.01.005. PMID 15755455.
Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi: 10.1016/j.cell.2005.08.029. hdl: 11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi: 10.1101/gr.4039406. PMC 1356129. PMID 16344560.
Sekulic N, Konrad M, Lavie A (2007). "Structural mechanism for substrate inhibition of the adenosine 5'-phosphosulfate kinase domain of human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 and its ramifications for enzyme regulation". J. Biol. Chem. 282 (30): 22112–21. doi: 10.1074/jbc.M701713200. hdl: 11858/00-001M-0000-0012-E08D-D. PMID 17540769.

PDB gallery

1x6v: The crystal structure of human 3'-phosphoadenosine-5'-phosphosulfate synthetase 1
1xjq: ADP Complex OF HUMAN PAPS SYNTHETASE 1
1xnj: APS complex of human PAPS synthetase 1
2ofw: Crystal structure of the APSK domain of human PAPSS1 complexed with 2 APS molecules
2ofx: crystal structure of the APSK domain of human PAPSS1 in complex with ADPMg and PAPS
2pey: Crystal structure of deletion mutant of APS-kinase domain of human PAPS-synthetase 1
2pez: Crystal structure of deletion mutant of APS-kinase domain of human PAPS-synthetase 1 in complex with cyclic PAPS and dADP

Transferases: phosphorus-containing groups ( EC 2.7)

2.7.1-2.7.4:
phosphotransferase/ kinase
( PO₄)

2.7.1: OH acceptor	Hexo- Gluco- Fructo- Hepatic Galacto- Phosphofructo- 1 Liver Muscle Platelet 2 Riboflavin Shikimate Thymidine ADP-thymidine NAD⁺ Glycerol Pantothenate Mevalonate Pyruvate Deoxycytidine PFP Diacylglycerol Phosphoinositide 3 Class I PI 3 Class II PI 3 Sphingosine Glucose-1,6-bisphosphate synthase
2.7.2: COOH acceptor	Phosphoglycerate Aspartate kinase
2.7.3: N acceptor	Creatine
2.7.4: PO₄ acceptor	Phosphomevalonate Adenylate Nucleoside-diphosphate Uridylate Guanylate Thiamine-diphosphate

2.7.6: diphosphotransferase
( P₂O₇)

2.7.7: nucleotidyltransferase
( PO₄-nucleoside)

DNA polymerase	DNA-directed DNA polymerase I/A γ θ ν T7 Taq II/B α δ ε ζ Pfu III/C IV/X β λ μ TDT V/Y η ι κ RNA-directed DNA polymerase Reverse transcriptase Telomerase
RNA polymerase	Template-directed RNA polymerase I II III IV V ssRNAP POLRMT Primase 1 2 PrimPol RNA-dependent RNA polymerase Polyadenylation PAP PNPase

Phosphorolytic
3' to 5' exoribonuclease

Nucleotidyltransferase

Guanylyltransferase

mRNA capping enzyme

Other

Recombinase ( Integrase)
Transposase

2.7.8: miscellaneous

Phosphatidyltransferases	CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase CDP-diacylglycerol—serine O-phosphatidyltransferase CDP-diacylglycerol—inositol 3-phosphatidyltransferase CDP-diacylglycerol—choline O-phosphatidyltransferase
Glycosyl-1-phosphotransferase	N-acetylglucosamine-1-phosphate transferase

2.7.10-2.7.13: protein kinase
( PO₄; protein acceptor)

2.7.10: protein-tyrosine	see tyrosine kinases
2.7.11: protein-serine/threonine	see serine/threonine-specific protein kinases
2.7.12: protein-dual-specificity	see serine/threonine-specific protein kinases
2.7.13: protein-histidine	Protein-histidine pros-kinase Protein-histidine tele-kinase Histidine kinase

glycosaminoglycan anabolism

Heparan sulfate: EXT1; EXT2

Chondroitin sulfate: PAPSS1; PAPSS2

glycosaminoglycan catabolism

Hunter, Hurler	Iduronate-2-sulfatase Iduronidase
Sanfilippo, Sly	Heparan sulfamidase N-acetyltransferase Alpha-N-acetylglucosaminidase Glucuronidase N-acetylglucosamine-6-sulfatase
Morquio/ Maroteaux-Lamy	Arylsulfatase B Galactosamine-6 sulfatase Beta-galactosidase ( GLB1)

This article on a gene on human chromosome 4 is a stub. You can help Wikipedia by expanding it.

Retrieved from " https://en.wikipedia.org/?title=PAPSS1&oldid=1215911978"

Hidden categories:

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