Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Awodi, U.; Ronan, J.; Masschelein, J.; De Los Santos, E.; Challis, G.
    Thioester reduction and aldehyde transamination are universal steps in actinobacterial polyketide alkaloid biosynthesis (2016), Chem. Sci., 8, 411-415 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.281 expression in Escherichia coli Streptomyces coelicolor
2.6.1.115 expression in Escherichia coli Streptomyces coelicolor

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.281 Streptomyces coelicolor
-
-
-
2.3.1.281 Streptomyces coelicolor M145
-
-
-
2.6.1.115 Streptomyces coelicolor
-
-
-
2.6.1.115 Streptomyces coelicolor M145
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.115 recombinant protein Streptomyces coelicolor

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.281 6 malonyl-CoA + 5 NADPH + NADH + 6 H+
-
 Streptomyces coelicolor (2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal + 6 CoA + 5 NADP+ + NAD+ + 6 CO2 + 4 H2O
-
 ?
2.3.1.281 6 malonyl-CoA + 5 NADPH + NADH + 6 H+
-
 Streptomyces coelicolor M145 (2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal + 6 CoA + 5 NADP+ + NAD+ + 6 CO2 + 4 H2O
-
 ?
2.3.1.281 additional information the isolated subunit CpkC reduces octanoyl-CoA to octanal and further to 1-octanol in presence of NADH Streptomyces coelicolor ?
-
 ?
2.3.1.281 additional information the isolated subunit CpkC reduces octanoyl-CoA to octanal and further to 1-octanol in presence of NADH Streptomyces coelicolor M145 ?
-
 ?
2.6.1.115 (2E,5S,6E,8E,10E)-1-aminododeca-2,6,8,10-tetraen-5-ol + pyruvate
-
 Streptomyces coelicolor (2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal + L-alanine
-
 ?
2.6.1.115 (2E,5S,6E,8E,10E)-1-aminododeca-2,6,8,10-tetraen-5-ol + pyruvate
-
 Streptomyces coelicolor M145 (2E,5S,6E,8E,10E)-5-hydroxydodeca-2,6,8,10-tetraenal + L-alanine
-
 ?
2.6.1.115 1,1-dicyclopentylmethanamine + 2-oxoglutarate
-
 Streptomyces coelicolor 1-dicyclopentylmethanal + L-glutamate
-
 ?
2.6.1.115 1,1-dicyclopentylmethanamine + 2-oxoglutarate
-
 Streptomyces coelicolor M145 1-dicyclopentylmethanal + L-glutamate
-
 ?
2.6.1.115 2-methylpropan-1-amine + 2-oxoglutarate
-
 Streptomyces coelicolor 2-methylpropanal + L-glutamate
-
 ?
2.6.1.115 butan-1-amine + 2-oxoglutarate
-
 Streptomyces coelicolor butanal + L-glutamate
-
 ?
2.6.1.115 additional information enzyme displays broad substrate tolerance. Highest level of activity is observed for octylamine using pyruvate as the cosubstrate. Only L-alanine is formed from pyruvate Streptomyces coelicolor ?
-
 ?
2.6.1.115 additional information enzyme displays broad substrate tolerance. Highest level of activity is observed for octylamine using pyruvate as the cosubstrate. Only L-alanine is formed from pyruvate Streptomyces coelicolor M145 ?
-
 ?
2.6.1.115 octanal + L-alanine
-
 Streptomyces coelicolor octyl-1-amine + pyruvate
-
 r
2.6.1.115 octyl-1-amine + pyruvate
-
 Streptomyces coelicolor octanal + L-alanine
-
 r
2.6.1.115 phenylamine + 2-oxoglutarate
-
 Streptomyces coelicolor benzaldehyde + L-glutamate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.6.1.115 cpkG
-
 Streptomyces coelicolor

General Information

EC Number General Information Comment Organism
2.3.1.281 physiological function the C-terminal thioester reductase domain of the PKS and an omega-transaminase are responsible for release of the polyketide chain as an aldehyde and its subsequent reductive amination Streptomyces coelicolor