Yildirim, S.; Zezula, J.; Hudlicky, T.; Witholt, B.; Schmid, A.
Asymmetric dihydroxylation of cinnamonitrile to trans-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-acrylonitrile using chlorobenzene dioxygenase in Escherichia coli (pTEZ30) (2004), Adv. Synth. Catal., 346, 933-942 .
No PubMed abstract available
Application
Application |
Comment |
Organism |
synthesis |
asymmetric dihydroxylation of non-natural cinnamonitrile to trans-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-acrylonitrile by chlorobenzene dioxygenase in recombinant Escherichia coli JM101 (pTEZ30). Recombinant hosts with a strong expression system, such as Escherichia coli JM101 (pTEZ30), can be used to produce dioxygenases efficiently to performcis-dihydroxylations up to technical scales. The cells should be maintained in ametabolically active state duringthe biotransformation in order to increase and maintain the volumetric productivity for long-term reactions |
Pseudomonas sp. P51 |
Cloned(Commentary)
Cloned (Comment) |
Organism |
chlorobenzene dioxygenase genes tcbAa, tcbAb, tcbAc, and tcbAd are expressed in Escherichia coli JM101 (pTEZ30) under the control of the alk regulatory system of Pseudomonas oleovorans GPo1 |
Pseudomonas sp. P51 |
Organism
Organism |
UniProt |
Comment |
Textmining |
Pseudomonas sp. P51 |
Q52383 AND Q52384 AND Q52385 AND Q52386 |
Q52383: large subunit (tcbAa), Q52384: small subunit (tcbAb), Q52385: ferredoxin (tcbAc), Q52386: NADH-ferredoxin reductase (tcbAd) |
- |
Substrates and Products (Substrate)
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
cinnamonitrile + NADH + H+ + O2 |
- |
Pseudomonas sp. P51 |
trans-3-[(5S,6R)-5,6-dihydroxycyclohexa-1,3-dienyl]-acrylonitrile + NAD+ |
- |
? |
|
Synonyms
Synonyms |
Comment |
Organism |
CDO |
- |
Pseudomonas sp. P51 |