Adenosylcobinamide-phosphate guanylyltransferase
| adenosylcobinamide-phosphate guanylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.7.62 | ||||||||
| 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 | ||||||||
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In enzymology, an adenosylcobinamide-phosphate guanylyltransferase (EC 2.7.7.62) is an enzyme that catalyzes the chemical reaction
- GTP + adenosylcobinamide phosphate diphosphate + adenosylcobinamide-GDP
Thus, the two substrates of this enzyme are GTP and adenosylcobinamide phosphate, whereas its two products are diphosphate and adenosylcobinamide-GDP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is GTP:adenosylcobinamide-phosphate guanylyltransferase. 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&ndash, 9. doi:10.1074/jbc.270.40.23560. PMID 7559521.
- 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&ndash, 95. 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&ndash, 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&ndash, 86. doi:10.1074/jbc.M000977200. PMID 10869342.
- Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC (2002). "The biosynthesis of adenosylcobalamin (vitamin B12)". Nat. Prod. Rep. 19 (4): 390&ndash, 412. doi:10.1039/b108967f. PMID 12195810.