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Literature summary for 1.14.13.83 extracted from

  • Heldt, D.; Lawrence, A.D.; Lindenmeyer, M.; Deery, E.; Heathcote, P.; Rigby, S.E.; Warren, M.J.
    Aerobic synthesis of vitamin B12: ring contraction and cobalt chelation (2005), Biochem. Soc. Trans., 33, 815-819.
    View publication on PubMed
Search for more literature for 1.14.13.83

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the enzyme contains both a non-haem iron and an Fe-S centre Rhodobacter capsulatus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
precorrin-3A + NADH + O2 Rhodobacter capsulatus the enzyme is involved in ring contraction, whereby an integral carbon atom of the tetrapyrrole-derived macrocycle is removed, and cobalt chelation during aerobic synthesis of vitamin B12, the catalytic cycle of CobZ, overview precorrin-3B + NAD+ + H2O
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 ?

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus
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 in bacteria such as Rhodobacter capsulatus CobG is substituted by an isofunctional protein called CobZ
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Reaction

Reaction Comment Organism Reaction ID
precorrin-3A + NADH + H+ + O2 = precorrin-3B + NAD+ + H2O reaction mechanism of CobZ Rhodobacter capsulatus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
precorrin-3A + NADH + O2 the enzyme is involved in ring contraction, whereby an integral carbon atom of the tetrapyrrole-derived macrocycle is removed, and cobalt chelation during aerobic synthesis of vitamin B12, the catalytic cycle of CobZ, overview Rhodobacter capsulatus precorrin-3B + NAD+ + H2O
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 ?
precorrin-3A + NADH + O2 the enzyme generates a hydroxy lactone intermediate Rhodobacter capsulatus precorrin-3B + NAD+ + H2O
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 ?

Synonyms

Synonyms Comment Organism
CobZ
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 Rhodobacter capsulatus

Cofactor

Cofactor Comment Organism Structure
flavin enzyme-bound Rhodobacter capsulatus