From Surf Wiki (app.surf) — the open knowledge base
Cob(I)yrinic acid a,c-diamide adenosyltransferase
Class of enzymes
Class of enzymes
| Field | Value |
|---|---|
| Name | ATP:corrinoid adenosyltransferase |
| EC_number | 2.5.1.17 |
| CAS_number | 37277-84-2 |
| GO_code | 0008817 |
| image | Protein MMAB PDB 2idx.png |
| caption | Human mitochondrial Cob(I)yrinic acid a,c-diamide adenosyltransferase, MMAB. |
In molecular biology, cob(I)yrinic acid a,c-diamide adenosyltransferase (also known as ATP:cob(I)alamin adenosyltransferase or ATP:corrinoid adenosyltransferase) is an enzyme which catalyses the conversion of cobalamin (vitamin B12) into one of its coenzyme forms, adenosylcobalamin (coenzyme B12, AdoCbl). 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, EutT-type and PduO-type. 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. 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. PduO functions to convert cobalamin to AdoCbl for 1,2-propanediol degradation, while EutT produces AdoCbl for ethanolamine utilisation.
Synonyms
This enzyme is also known as:
- Cobalamin adenosyltransferase
- ATP:cob(I)alamin adenosyltransferase
- ATP:corrinoid adenosyltransferase
References
References
- (December 2006). "Structure of ATP-bound human ATP:cobalamin adenosyltransferase". Biochemistry.
- (September 2010). "Multiple roles of ATP:cob(I)alamin adenosyltransferases in the conversion of B12 to coenzyme B12". Appl. Microbiol. Biotechnol..
- (November 2004). "Evidence that a B12-adenosyl transferase is encoded within the ethanolamine operon of Salmonella enterica". J. Bacteriol..
- (May 2006). "Studies of the CobA-type ATP:Co(I)rrinoid adenosyltransferase enzyme of Methanosarcina mazei strain Go1". J. Bacteriol..
- (September 2004). "The eutT gene of Salmonella enterica Encodes an oxygen-labile, metal-containing ATP:corrinoid adenosyltransferase enzyme". J. Bacteriol..
- (March 2001). "Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene". J. Bacteriol..
- (July 1993). "Cloning, sequencing and overexpression of cobA which encodes ATP:corrinoid adenosyltransferase in Salmonella typhimurium". Gene.
- (September 1997). "Glycerol conversion to 1,3-propanediol by Clostridium pasteurianum: cloning and expression of the gene encoding 1,3-propanediol dehydrogenase". FEMS Microbiol. Lett..
- (June 2006). "Purification and initial biochemical characterization of ATP:Cob(I)alamin adenosyltransferase (EutT) enzyme of Salmonella enterica". J. Biol. Chem..
This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page.
Ask Mako anything about Cob(I)yrinic acid a,c-diamide adenosyltransferase — get instant answers, deeper analysis, and related topics.
Research with MakoFree with your Surf account
Create a free account to save articles, ask Mako questions, and organize your research.
Sign up freeThis content may have been generated or modified by AI. CloudSurf Software LLC is not responsible for the accuracy, completeness, or reliability of AI-generated content. Always verify important information from primary sources.
Report