Literature summary extracted from
Leesong, M.; Henderson, B.S.; Gillig, J.R.; Schwab, J.M.; Smith, J.L.
Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site (1996), Structure, 4, 253-264.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
5.3.3.14 |
free enzyme and modified by inhibitor 3-decynoyl-N-acteylcysteamine |
Escherichia coli |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
5.3.3.14 |
Escherichia coli |
- |
multifunctional enzyme, catalyzing in addition reaction of EC 4.2.1.60 |
- |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
5.3.3.14 |
a trans-dec-2-enoyl-[acyl-carrier protein] = a cis-dec-3-enoyl-[acyl-carrier protein] |
the reactions of EC 4.2.1.60 and EC 5.3.3.14 are carried out by the same active site carrying a His and a Asp residue in a hydrophobic environment |
Escherichia coli |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
5.3.3.14 |
dimer |
crystallization data |
Escherichia coli |