Precorrin-3B synthase

precorrin-3B synthase
Identifiers
EC no.	1.14.13.83
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
Search PMC articles PubMed articles NCBI proteins

In enzymology, a precorrin-3B synthase (EC 1.14.13.83) is an enzyme that catalyzes the chemical reaction

precorrin-3A + NADH + H⁺ + O₂ $\rightleftharpoons$ precorrin-3B + NAD⁺ + H₂O

The 4 substrates of this enzyme are precorrin 3A, NADH, H⁺, and O₂, whereas its 3 products are precorrin 3B, NAD⁺, and H₂O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is precorrin-3A,NADH:oxygen oxidoreductase (20-hydroxylating). Other names in common use include precorrin-3X synthase, and CobG. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B₁₂) in aerobic bacteria.

See also

• Cobalamin biosynthesis

References

• Debussche L, Thibaut D, Cameron B, Crouzet J, Blanche F (1993). "Biosynthesis of the corrin macrocycle of coenzyme B12 in Pseudomonas denitrificans". J. Bacteriol. 175 (22): 7430–40. PMC 206888. PMID 8226690.
• Scott AI, Roessner CA, Stolowich NJ, Spencer JB, Min C, Ozaki SI (1993). "Biosynthesis of vitamin B12. Discovery of the enzymes for oxidative ring contraction and insertion of the fourth methyl group". FEBS Lett. 331 (1–2): 105–8. doi:10.1016/0014-5793(93)80306-F. PMID 8405386.
• 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.