Cobalt chelatase
| cobalt chelatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| File:EVWong CC2XVX raytraced.png
Putative cobalt chelatase monomer from Desulvobrio vulgaris.[1]
|
|||||||||
| Identifiers | |||||||||
| EC number | 6.6.1.2 | ||||||||
| CAS number | Template:CAS | ||||||||
| 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 / EGO | ||||||||
|
|||||||||
| Cobalt chelatase, CobT subunit | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | CobT | ||||||||
| Pfam | PF06213 | ||||||||
| InterPro | IPR006538 | ||||||||
|
|||||||||
Cobalt chelatase (EC 6.6.1.2) is an enzyme that catalyzes the chemical reaction
- ATP + hydrogenobyrinic acid a,c-diamide + Co2+ + H2O
ADP + phosphate + cob(II)yrinic acid a,c-diamide + H+
The 4 substrates of this enzyme are ATP, hydrogenobyrinic acid a,c-diamide, Co2+, and H2O, whereas its 4 products are ADP, phosphate, cob(II)yrinic acid a,c-diamide, and H+.
The aerobic cobalt chelatase (aerobic cobalamin biosynthesis pathway)[2][3] consists of three subunits, CobT, CobN (IPR003672) and CobS (IPR006537).
Cobalamin (vitamin B12) can be complexed with metal via the ATP-dependent reactions (aerobic pathway) (e.g., in Pseudomonas denitrificans) or via ATP-independent reactions (anaerobic pathway) (e.g., in Salmonella typhimurium).[4][5] The corresponding cobalt chelatases are not homologous. However, aerobic cobalt chelatase subunits CobN and CobS are homologous to Mg-chelatase subunits BchH and BchI, respectively.[5] CobT, too, has been found to be remotely related to the third subunit of Mg-chelatase, BchD (involved in bacteriochlorophyll synthesis, e.g., in Rhodobacter capsulatus).[5]
This enzyme belongs to the family of ligases, specifically those forming nitrogen-D-metal bonds in coordination complexes. The systematic name of this enzyme class is hydrogenobyrinic-acid-a,c-diamide:cobalt cobalt-ligase (ADP-forming). Other names in common use include hydrogenobyrinic acid a,c-diamide cobaltochelatase, CobNST, and CobNCobST. This enzyme participates in porphyrin and chlorophyll metabolism.
References
<templatestyles src="Reflist/styles.css" />
Cite error: Invalid <references> tag; parameter "group" is allowed only.
<references />, or <references group="..." />Further reading
- Lua error in package.lua at line 80: module 'strict' not found.
- Lua error in package.lua at line 80: module 'strict' not found.
This article incorporates text from the public domain Pfam and InterPro IPR006538
<templatestyles src="Asbox/styles.css"></templatestyles>
- ↑ Romao CV, Ladakis D, Lobo SAL, Carrondo MA, Brindley AA, Deery E, Matias PM, Pickersgill RW, Saravia LM, Warren MJ. Evolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerization. (2011) Proc. Natl. Acad. Sci. USA. 108, 97-102. http://www.pnas.org/content/108/1/97.full.pdf+html?sid=d820d5c4-9e1e-459e-ad22-a24df13b0485. Image drawn in PyMOL.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ 5.0 5.1 5.2 Lua error in package.lua at line 80: module 'strict' not found.
