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Literature summary for 1.14.11.21 extracted from

  • Zhou, J.; Kelly, W.L.; Bachmann, B.O.; Gunsior, M.; Townsend, C.A.; Solomon, E.I.
    Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional a-KG-dependent non-heme iron enzyme: correlation with mchanisms and reactivities (2001), J. Am. Chem. Soc., 123, 7388-7398.
    View publication on PubMed
Search for more literature for 1.14.11.21

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ required Streptomyces clavuligerus
Fe2+ conformation during catalytic reaction Streptomyces clavuligerus
Fe2+ isozyme CS2, five and six-coordinate ferrous species in the enzyme-substrate complexes, structural model of conversion for the different reactions Streptomyces clavuligerus
Fe2+ isozyme CS2, a single ferrous active site Streptomyces clavuligerus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
deoxyamidinoproclavaminate + 2-oxoglutarate + O2 Streptomyces clavuligerus
-
 amidinoproclavaminate + succinate + CO2 + H2O
-
 ?
deoxyguanidinoproclavaminate + 2-oxoglutarate + O2 Streptomyces clavuligerus
-
 guanidinoproclavaminate + succinate + CO2 + H2O
-
 ?
dihydroclavaminate + 2-oxoglutarate + O2 Streptomyces clavuligerus
-
 clavaminate + succinate + CO2 + H2O
-
 ?
proclavaminate + 2-oxoglutarate + O2 Streptomyces clavuligerus
-
 dihydroclavaminate + succinate + CO2 + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Streptomyces clavuligerus Q05581 recombinant purifed isozyme CS2
-

Reaction

Reaction Comment Organism Reaction ID
dihydroclavaminate + 2-oxoglutarate + O2 = clavaminate + succinate + CO2 + H2O reaction mechanism Streptomyces clavuligerus
a
proclavaminate + 2-oxoglutarate + O2 = dihydroclavaminate + succinate + CO2 + H2O reaction mechanism Streptomyces clavuligerus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + O2 in absence or presence of the substrate proclavaminate, inactivation of the enzyme Streptomyces clavuligerus ? + H2O2
-
 ?
2-oxoglutarate + O2 molecular mechanism Streptomyces clavuligerus ? + H2O2
-
 ?
2-oxoglutarate + O2 varying amounts of unsaturated six-coordinate ferrous species exist in the substrate complexes which correlate to this uncoupled reaction Streptomyces clavuligerus ? + H2O2
-
 ?
deoxyamidinoproclavaminate + 2-oxoglutarate + O2
-
 Streptomyces clavuligerus amidinoproclavaminate + succinate + CO2 + H2O
-
 ?
deoxyguanidinoproclavaminate + 2-oxoglutarate + O2
-
 Streptomyces clavuligerus guanidinoproclavaminate + succinate + CO2 + H2O
-
 ?
deoxyguanidinoproclavaminate + 2-oxoglutarate + O2 hydroxylation Streptomyces clavuligerus guanidinoproclavaminate + succinate + CO2 + H2O
-
 ?
dihydroclavaminate + 2-oxoglutarate + O2
-
 Streptomyces clavuligerus clavaminate + succinate + CO2 + H2O
-
 ?
dihydroclavaminate + 2-oxoglutarate + O2 cyclization Streptomyces clavuligerus clavaminate + succinate + CO2 + H2O
-
 ?
additional information structure-function correlation Streptomyces clavuligerus ?
-
 ?
proclavaminate + 2-oxoglutarate + O2
-
 Streptomyces clavuligerus dihydroclavaminate + succinate + CO2 + H2O
-
 ?
proclavaminate + 2-oxoglutarate + O2 saturation Streptomyces clavuligerus dihydroclavaminate + succinate + CO2 + H2O
-
 ?