N-アシルノイラミン酸シチジルトランスフェラーゼ
WordNet
- the 14th letter of the Roman alphabet (同)n
PrepTutorEJDIC
- nitrogenの化学記号
- neodymiumの化学記号
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/02/19 14:30:45」(JST)
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| N-acylneuraminate cytidylyltransferase |
| Identifiers |
| EC number |
2.7.7.43 |
| CAS number |
9067-82-7 |
| Databases |
| IntEnz |
IntEnz view |
| BRENDA |
BRENDA entry |
| ExPASy |
NiceZyme view |
| KEGG |
KEGG entry |
| MetaCyc |
metabolic pathway |
| PRIAM |
profile |
| PDB structures |
RCSB PDB PDBe PDBsum |
| Gene Ontology |
AmiGO / EGO |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI |
proteins |
|
In enzymology, a N-acylneuraminate cytidylyltransferase (EC 2.7.7.43) is an enzyme that catalyzes the chemical reaction
- CTP + N-acylneuraminate diphosphate + CMP-N-acylneuraminate
Thus, the two substrates of this enzyme are CTP and N-acylneuraminate, whereas its two products are diphosphate and CMP-N-acylneuraminate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:N-acylneuraminate cytidylyltransferase. Other names in common use include CMP-sialate pyrophosphorylase, CMP-sialate synthase, cytidine 5'-monophosphosialic acid synthetase, CMP-Neu5Ac synthetase, CMP-NeuAc synthetase, acylneuraminate cytidyltransferase, CMP-N-acetylneuraminate synthetase, CMP-N-acetylneuraminate synthase, CMP-N-acetylneuraminic acid synthase, CMP-NANA synthetase, CMP-sialate synthetase, CMP-sialic synthetase, cytidine 5'-monophospho-N-acetylneuraminic acid synthetase, cytidine 5-monophosphate N-acetylneuraminic acid synthetase, cytidine monophosphosialic acid synthetase, cytidine monophosphoacetylneuraminic synthetase, cytidine monophosphosialate pyrophosphorylase, cytidine monophosphosialate synthetase, and acetylneuraminate cytidylyltransferase. This enzyme participates in aminosugars metabolism.
Structural studies
As of late 2007, three structures have been solved for this class of enzymes, with PDB accession codes 1EYR, 1EZI, and 1QWJ.
References
- Kean EL, Roseman S (1966). "The sialic acids. X. Purification and properties of cytidine 5'-monophosphosialic acid synthetase". J. Biol. Chem. 241 (23): 5643–50. PMID 4288894.
|
Transferases: phosphorus-containing groups (EC 2.7)
|
|
2.7.1-2.7.4:
phosphotransferase/kinase
(PO4) |
| 2.7.1: OH acceptor |
- Hexo-
- Gluco-
- Fructo-
- Galacto-
- Phosphofructo-
- 1
- Liver
- Muscle
- Platelet
- 2
- Riboflavin
- Shikimate
- 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 |
|
|
| 2.7.4: PO4 acceptor |
- Phosphomevalonate
- Adenylate
- Nucleoside-diphosphate
- Uridylate
- Guanylate
- Thiamine-diphosphate
|
|
|
2.7.6: diphosphotransferase
(P2O7) |
- Ribose-phosphate diphosphokinase
- Thiamine diphosphokinase
|
|
2.7.7: nucleotidyltransferase
(PO4-nucleoside) |
| Polymerase |
| DNA polymerase |
- DNA-directed DNA polymerase
- I
- II
- III
- IV
- V
- RNA-directed DNA polymerase
- Reverse transcriptase
- Telomerase
- DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase
|
|
| RNA nucleotidyltransferase |
- RNA polymerase/DNA-directed RNA polymerase
- RNA polymerase I
- RNA polymerase II
- RNA polymerase III
- RNA polymerase IV
- Primase
- RNA-dependent RNA polymerase
- PNPase
|
|
|
Phosphorolytic
3' to 5' exoribonuclease |
|
|
| Nucleotidyltransferase |
- UTP—glucose-1-phosphate uridylyltransferase
- Galactose-1-phosphate uridylyltransferase
|
|
| Guanylyltransferase |
|
|
| 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 |
|
|
| 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
|
|
|
|
Proteins: enzymes
|
|
| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
|
|
| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
|
|
| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
|
|
| Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
|
|
English Journal
- Extension of the Legionella pneumophila sequence-based typing scheme to include strains carrying a variant of the N-acylneuraminate cytidylyltransferase gene.
- Mentasti M1, Underwood A, Lück C, Kozak-Muiznieks NA, Harrison TG, Fry NK.
- Clinical microbiology and infection : the official publication of the European Society of Clinical Microbiology and Infectious Diseases.Clin Microbiol Infect.2014 Jul;20(7):O435-41. doi: 10.1111/1469-0691.12459. Epub 2013 Dec 12.
- Sequence-based typing (SBT) combined with monoclonal antibody subgrouping of Legionella pneumophila isolates is at present considered to be the reference standard during epidemiological investigation of Legionnaires' disease outbreaks. In some isolates of L. pneumophila, the seventh allele of the st
- PMID 24245827
- The role of Drosophila cytidine monophosphate-sialic acid synthetase in the nervous system.
- Islam R1, Nakamura M, Scott H, Repnikova E, Carnahan M, Pandey D, Caster C, Khan S, Zimmermann T, Zoran MJ, Panin VM.
- The Journal of neuroscience : the official journal of the Society for Neuroscience.J Neurosci.2013 Jul 24;33(30):12306-15. doi: 10.1523/JNEUROSCI.5220-12.2013.
- While sialylation plays important functions in the nervous system, the complexity of glycosylation pathways and limitations of genetic approaches preclude the efficient analysis of these functions in mammalian organisms. Drosophila has recently emerged as a promising model for studying neural sialyl
- PMID 23884937
- Immunoproteomic analysis of the protective response obtained with subunit and commercial vaccines against Glässer's disease in pigs.
- Martínez-Martínez S1, Frandoloso R, Rodríguez Ferri EF, Gil C, Hernández-Haro C, Yubero S, Gutiérrez Martín CB.
- Veterinary immunology and immunopathology.Vet Immunol Immunopathol.2013 Feb 15;151(3-4):235-47. doi: 10.1016/j.vetimm.2012.11.014. Epub 2012 Dec 1.
- An immunoproteomic analysis of the protective response of subunit and commercial vaccines in colostrum-deprived pigs against Glässer's disease was carried out. A mixture of proteins with affinity to porcine transferrin (PAPT) from Haemophilus parasuis Nagasaki strain (serovar 5) was inoculated intr
- PMID 23266097
Related Links
- In enzymology, a N-acylneuraminate cytidylyltransferase (EC 2.7.7.43) is an enzyme that catalyzes the chemical reaction ... Thus, the two substrates of this enzyme are CTP and N-acylneuraminate, whereas its two products are diphosphate ...
Related Pictures
★リンクテーブル★
[★]
- 英
- N-acylneuraminate cytidylyltransferase
[★]
- 関
- number of experiment、sample size
- pの前の[n]はmと記載する。synptom→symptom
[★]
[★]
ネオジム neodymium