| 词条 | Cob(I)yrinic acid a,c-diamide adenosyltransferase |
| 释义 |
| Name = ATP:corrinoid adenosyltransferase | EC_number = 2.5.1.17 | CAS_number = 37277-84-2 | IUBMB_EC_number = 2/5/1/17 | GO_code = 0008817 | image = Protein MMAB PDB 2idx.png | width = | caption = Human mitochondrial Cob(I)yrinic acid a,c-diamide adenosyltransferase, MMAB.[1] }}{{Infobox protein family | Symbol = CobA_CobO_BtuR | Name = ATP:corrinoid adenosyltransferase | image = PDB 1g5t EBI.jpg | width = | caption = the three-dimensional structure of atp:corrinoid adenosyltransferase from salmonella typhimurium. apo-atp form | Pfam = PF02572 | Pfam_clan = CL0023 | InterPro = IPR003724 | SMART = | PROSITE = | MEROPS = | SCOP = 1g64 | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }}{{Infobox protein family | Symbol = Cob_adeno_trans | Name = Cobalamin adenosyltransferase (PduO/EutT) | image = PDB 1nog EBI.jpg | width = | caption = crystal structure of conserved protein 0546 from thermoplasma acidophilum | Pfam = PF01923 | Pfam_clan = | InterPro = IPR002779 | SMART = | PROSITE = | MEROPS = | SCOP = 1nog | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} In molecular biology, cob(I)yrinic acid a,c-diamide adenosyltransferase (also known as ATP:cob(I)alamin adenosyltransferase or ATP:corrinoid adenosyltransferase) {{EC number|2.5.1.17}} is an enzyme which catalyses the conversion of cobalamin (vitamin B12) into one of its coenzyme forms, adenosylcobalamin (coenzyme B12, AdoCbl).[2][3] Adenosylcobalamin is required as a cofactor for the activity of certain enzymes. AdoCbl contains an adenosyl moiety liganded to the cobalt ion of cobalamin via a covalent Co-C bond. ATP:cob(I)alamin adenosyltransferases are classed into three groups: CobA-type,[4] EutT-type [5] and PduO-type.[6] Each of the three enzyme types appears to be specialised for particular AdoCbl-dependent enzymes or for the de novo synthesis of AdoCbl. PduO and EutT are distantly related, sharing short conserved motifs, while CobA is evolutionarily unrelated and is an example of convergent evolution. The CobA group includes the ATP:cob(I)alamin adenosyltransferases CobA (Salmonella typhimurium), CobO (Pseudomonas denitrificans), and ButR (Escherichia coli). There is a high degree of sequence identity between these proteins.[7] CobA is responsible for attaching the adenosyl moiety from ATP to the cobalt ion of the corrin ring, necessary for the conversion of cobalamin to adenosylcobalamin.[3][4] PduO functions to convert cobalamin to AdoCbl for 1,2-propanediol degradation,[8] while EutT produces AdoCbl for ethanolamine utilisation.[9] SynonymsThis enzyme is also known as:
References1. ^{{cite journal |vauthors=Schubert HL, Hill CP | title = Structure of ATP-bound human ATP:cobalamin adenosyltransferase | journal = Biochemistry | volume = 45 | issue = 51 | pages = 15188–96 |date=December 2006 | pmid = 17176040 | pmc = 2532598 | doi = 10.1021/bi061396f }} {{Alkyl and aryl transferases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{InterPro content|IPR003724}}{{InterPro content|IPR002779}}2. ^{{cite journal |vauthors=Mera PE, Escalante-Semerena JC | title = Multiple roles of ATP:cob(I)alamin adenosyltransferases in the conversion of B12 to coenzyme B12 | journal = Appl. Microbiol. Biotechnol. | volume = 88 | issue = 1 | pages = 41–8 |date=September 2010 | pmid = 20677021 | pmc = 3034633 | doi = 10.1007/s00253-010-2773-2 }} 3. ^1 {{cite journal |vauthors=Sheppard DE, Penrod JT, Bobik T, Kofoid E, Roth JR | title = Evidence that a B12-adenosyl transferase is encoded within the ethanolamine operon of Salmonella enterica | journal = J. Bacteriol. | volume = 186 | issue = 22 | pages = 7635–44 |date=November 2004 | pmid = 15516577 | pmc = 524904 | doi = 10.1128/JB.186.22.7635-7644.2004 | url = }} 4. ^1 {{cite journal |vauthors=Buan NR, Rehfeld K, Escalante-Semerena JC | title = Studies of the CobA-type ATP:Co(I)rrinoid adenosyltransferase enzyme of Methanosarcina mazei strain Go1 | journal = J. Bacteriol. | volume = 188 | issue = 10 | pages = 3543–50 |date=May 2006 | pmid = 16672609 | pmc = 1482872 | doi = 10.1128/JB.188.10.3543-3550.2006 | url = }} 5. ^{{cite journal |vauthors=Buan NR, Suh SJ, Escalante-Semerena JC | title = The eutT gene of Salmonella enterica Encodes an oxygen-labile, metal-containing ATP:corrinoid adenosyltransferase enzyme | journal = J. Bacteriol. | volume = 186 | issue = 17 | pages = 5708–14 |date=September 2004 | pmid = 15317775 | pmc = 516830 | doi = 10.1128/JB.186.17.5708-5714.2004 | url = }} 6. ^{{cite journal |vauthors=Johnson CL, Pechonick E, Park SD, Havemann GD, Leal NA, Bobik TA | title = Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene | journal = J. Bacteriol. | volume = 183 | issue = 5 | pages = 1577–84 |date=March 2001 | pmid = 11160088 | pmc = 95042 | doi = 10.1128/JB.183.5.1577-1584.2001 | url = }} 7. ^{{cite journal |vauthors=Suh SJ, Escalante-Semerena JC | title = Cloning, sequencing and overexpression of cobA which encodes ATP:corrinoid adenosyltransferase in Salmonella typhimurium | journal = Gene | volume = 129 | issue = 1 | pages = 93–7 |date=July 1993 | pmid = 7916712 | doi = 10.1016/0378-1119(93)90701-4 }} 8. ^{{cite journal |vauthors=Luers F, Seyfried M, Daniel R, Gottschalk G | title = Glycerol conversion to 1,3-propanediol by Clostridium pasteurianum: cloning and expression of the gene encoding 1,3-propanediol dehydrogenase | journal = FEMS Microbiol. Lett. | volume = 154 | issue = 2 | pages = 337–45 |date=September 1997 | pmid = 9311132 | doi = 10.1016/s0378-1097(97)00351-0}} 9. ^{{cite journal |vauthors=Buan NR, Escalante-Semerena JC | title = Purification and initial biochemical characterization of ATP:Cob(I)alamin adenosyltransferase (EutT) enzyme of Salmonella enterica | journal = J. Biol. Chem. | volume = 281 | issue = 25 | pages = 16971–7 |date=June 2006 | pmid = 16636051 | doi = 10.1074/jbc.M603069200 }} 2 : Protein families|EC 2.5.1 |
| 随便看 |
|
开放百科全书收录14589846条英语、德语、日语等多语种百科知识，基本涵盖了大多数领域的百科知识，是一部内容自由、开放的电子版国际百科全书。