Adenosylcobinamide kinase
| adenosylcobinamide kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.156 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
In enzymology, an adenosylcobinamide kinase (EC 2.7.1.156) is an enzyme that catalyzes the chemical reaction
- RTP + adenosylcobinamide adenosylcobinamide phosphate + RDP
Thus, the two substrates of this enzyme are RTP and adenosylcobinamide, whereas its two products are adenosylcobinamide phosphate and RDP.
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 RTP:adenosylcobinamide phosphotransferase. Other names in common use include CobU, adenosylcobinamide kinase/adenosylcobinamide-phosphate, guanylyltransferase, and AdoCbi kinase/AdoCbi-phosphate guanylyltransferase. This enzyme participates in porphyrin and chlorophyll metabolism.
References
- O'Toole GA, Escalante-Semerena JC (1995). "Purification and characterization of the bifunctional CobU enzyme of Salmonella typhimurium LT2. Evidence for a CobU-GMP intermediate". J. Biol. Chem. 270 (40): 23560–9. doi:10.1074/jbc.270.40.23560. PMID 7559521.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - Thompson TB, Thomas MG, Escalante-Semerena JC, Rayment I (1998). "Three-dimensional structure of adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase from Salmonella typhimurium determined to 2.3 A resolution". Biochemistry. 37 (21): 7686–95. CiteSeerX 10.1.1.565.1238. doi:10.1021/bi973178f. PMID 9601028.
- Thompson TB, Thomas MG, Escalante-Semerena JC, Rayment I (1999). "Three-dimensional structure of adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase (CobU) complexed with GMP: evidence for a substrate-induced transferase active site". Biochemistry. 38 (40): 12995–3005. doi:10.1021/bi990910x. PMID 10529169.
- Thomas MG, Thompson TB, Rayment I, Escalante-Semerena JC (2000). "Analysis of the adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase (CobU) enzyme of Salmonella typhimurium LT2. Identification of residue His-46 as the site of guanylylation". J. Biol. Chem. 275 (36): 27576–86. doi:10.1074/jbc.M000977200. PMID 10869342.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC (2002). "The biosynthesis of adenosylcobalamin (vitamin B12)". Nat. Prod. Rep. 19 (4): 390–412. doi:10.1039/b108967f. PMID 12195810.
