| Adenosylcobinamide-phosphate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.1.10 | ||||||||
| CAS no. | 905988-16-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Adenosylcobinamide-phosphate synthase ( EC 6.3.1.10, CbiB) is an enzyme with systematic name adenosylcobyric acid:(R)-1-aminopropan-2-yl phosphate ligase (ADP-forming). [1] [2] This enzyme catalyses the following chemical reaction
- (1) ATP + adenosylcobyric acid + (R)-1-aminopropan-2-yl phosphate ADP + phosphate + adenosylcobinamide phosphate
- (2) ATP + adenosylcobyric acid + (R)-1-aminopropan-2-ol ADP + phosphate + adenosylcobinamide
One of the substrates, (R)-1-aminopropan-2-yl phosphate, is produced by CobD ( EC 4.1.1.81). This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria.
- ^ Cheong CG, Bauer CB, Brushaber KR, Escalante-Semerena JC, Rayment I (April 2002). "Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica". Biochemistry. 41 (15): 4798–808. CiteSeerX 10.1.1.564.9386. doi: 10.1021/bi012111w. PMID 11939774.
- ^ Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC (August 2002). "The biosynthesis of adenosylcobalamin (vitamin B12)". Natural Product Reports. 19 (4): 390–412. doi: 10.1039/b108967f. PMID 12195810.
- Adenosylcobinamide-phosphate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| Adenosylcobinamide-phosphate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 6.3.1.10 | ||||||||
| CAS no. | 905988-16-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Adenosylcobinamide-phosphate synthase ( EC 6.3.1.10, CbiB) is an enzyme with systematic name adenosylcobyric acid:(R)-1-aminopropan-2-yl phosphate ligase (ADP-forming). [1] [2] This enzyme catalyses the following chemical reaction
- (1) ATP + adenosylcobyric acid + (R)-1-aminopropan-2-yl phosphate ADP + phosphate + adenosylcobinamide phosphate
- (2) ATP + adenosylcobyric acid + (R)-1-aminopropan-2-ol ADP + phosphate + adenosylcobinamide
One of the substrates, (R)-1-aminopropan-2-yl phosphate, is produced by CobD ( EC 4.1.1.81). This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria.
- ^ Cheong CG, Bauer CB, Brushaber KR, Escalante-Semerena JC, Rayment I (April 2002). "Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica". Biochemistry. 41 (15): 4798–808. CiteSeerX 10.1.1.564.9386. doi: 10.1021/bi012111w. PMID 11939774.
- ^ Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC (August 2002). "The biosynthesis of adenosylcobalamin (vitamin B12)". Natural Product Reports. 19 (4): 390–412. doi: 10.1039/b108967f. PMID 12195810.
- Adenosylcobinamide-phosphate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)