2'-phosphotransferase

Thus, the two substrates of this enzyme are [[2'-phospho-[ligated tRNA]]] and NAD⁺, whereas its 4 products are mature tRNA, ADP-ribose 1'',2''-phosphate, nicotinamide, and H₂O.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is 2'-phospho-[ligated tRNA]:NAD+ phosphotransferase. Other names in common use include yeast 2'-phosphotransferase, Tpt1, Tpt1p, and 2'-phospho-tRNA:NAD+ phosphotransferase.

References

Steiger MA, Kierzek R, Turner DH, Phizicky EM (2001). "Substrate recognition by a yeast 2'-phosphotransferase involved in tRNA splicing and by its Escherichia coli homolog". Biochemistry. 40 (46): 14098–105. doi:10.1021/bi011388t. PMID 11705403.
Spinelli SL, Kierzek R, Turner DH, Phizicky EM (1999). "Transient ADP-ribosylation of a 2'-phosphate implicated in its removal from ligated tRNA during splicing in yeast". J. Biol. Chem. 274 (5): 2637–44. doi:10.1074/jbc.274.5.2637. PMID 9915792.
Culver GM, McCraith SM, Consaul SA, Stanford DR, Phizicky EM (1997). "A 2'-phosphotransferase implicated in tRNA splicing is essential in Saccharomyces cerevisiae". J. Biol. Chem. 272 (20): 13203–10. doi:10.1074/jbc.272.20.13203. PMID 9148937.
McCraith SM, Phizicky EM (1991). "An enzyme from Saccharomyces cerevisiae uses NAD+ to transfer the splice junction 2'-phosphate from ligated tRNA to an acceptor molecule". J. Biol. Chem. 266 (18): 11986–92. PMID 2050693.
Hu QD, Lu H, Huo K, Ying K, Li J, Xie Y, Mao Y, Li YY (2003). "A human homolog of the yeast gene encoding tRNA 2'-phosphotransferase: cloning, characterization and complementation analysis". Cell. Mol. Life. Sci. 60 (8): 1725–32. doi:10.1007/s00018-003-3107-7. PMID 14504659.
Steiger MA, Jackman JE, Phizicky EM (2005). "Analysis of 2'-phosphotransferase (Tpt1p) from Saccharomyces cerevisiae: evidence for a conserved two-step reaction mechanism". RNA. 11 (1): 99–106. doi:10.1261/rna.7194605. PMC 1370695. PMID 15611300.
Sawaya R, Schwer B, Shuman S (2005). "Structure-function analysis of the yeast NAD+-dependent tRNA 2'-phosphotransferase Tpt1". RNA. 11 (1): 107–13. doi:10.1261/rna.7193705. PMC 1370696. PMID 15611301.
Kato-Murayama M, Bessho Y, Shirouzu M, Yokoyama S (2005). "Crystal structure of the RNA 2'-phosphotransferase from Aeropyrum pernix K1". J. Mol. Biol. 348 (2): 295–305. doi:10.1016/j.jmb.2005.02.049. PMID 15811369.

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)

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

Guanylyltransferase

mRNA capping enzyme

Other

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

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)

This article is issued from Wikipedia - version of the 8/10/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.