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5.3.3.14: trans-2-decenoyl-[acyl-carrier protein] isomerase

This is an abbreviated version!
For detailed information about trans-2-decenoyl-[acyl-carrier protein] isomerase, go to the full flat file.

Reaction

a trans-dec-2-enoyl-[acyl-carrier protein]
=
a cis-dec-3-enoyl-[acyl-carrier protein]

Synonyms

FabM

ECTree

     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.3 Transposing C=C bonds
                5.3.3.14 trans-2-decenoyl-[acyl-carrier protein] isomerase

Reference

Reference on EC 5.3.3.14 - trans-2-decenoyl-[acyl-carrier protein] isomerase

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kass, L.R.; Brock, D.J.H.; Bloch, K.
beta-Hydroxydecanoyl thioester dehydrase
J. Biol. Chem.
242
4418-4431
1967
Escherichia coli
Manually annotated by BRENDA team
Helmkamp, G.H.; Bloch, K.
beta-Hydroxydecanoyl thioester dehydrase. Studies on molecular structure and active site
J. Biol. Chem.
244
6014-6022
1969
Escherichia coli
Manually annotated by BRENDA team
Helmkamp, G.; Rando, R.R.; Brock, D.J.H.; Bloch, K.
beta-Hydroxydecanoyl thioester dehydrase
J. Biol. Chem.
243
3229-3231
1968
Escherichia coli
Manually annotated by BRENDA team
Endo, K.; Helmkamp, G.M.; Bloch, K.
Mode of inhibition of beta-hydroxydecanoyl thioester dehydrase by 3-decynoyl-N-acetylcysteamine
J. Biol. Chem.
245
4293-4296
1970
Escherichia coli
Manually annotated by BRENDA team
Cronan, J.E.; Li, W.B.; Coleman, R.; Narasimhan, M.; De Mendoza, D.; Schwab, J.M.
Derived amino acid sequence and identification of active site residues of Escherichia coli beta-hydroxydecanoyl thioester dehydrase
J. Biol. Chem.
263
4641-4646
1988
Escherichia coli (P0A6Q3)
Manually annotated by BRENDA team
Guerra, D.J.; Browse, J.A.
Escherichia coli beta-hydroxydecanoyl thioester dehydrase reacts with native C10 acyl-acyl-carrier proteins of plant and bacterial origin
Arch. Biochem. Biophys.
280
336-345
1990
Escherichia coli
Manually annotated by BRENDA team
Fozo, E.M.; Quivey, R.G., Jr.
The fabM gene product of Streptococcus mutans is responsible for the synthesis of monounsaturated fatty acids and is necessary for survival at low pH
J. Bacteriol.
186
4152-4158
2004
Streptococcus mutans
Manually annotated by BRENDA team
Rando, R.R.; Bloch, K.
Mechanism of action of beta-hydroxydecanoyl thioester dehydrase
J. Biol. Chem.
243
5627-5634
1968
Escherichia coli
Manually annotated by BRENDA team
Marrakchi, H.; Choi, K.H.; Rock, C.O.
A new mechanism for anaerobic unsaturated fatty acid formation in Streptococcus pneumoniae
J. Biol. Chem.
277
44809-44816
2002
Streptococcus pneumoniae
Manually annotated by BRENDA team
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
Structure
4
253-264
1996
Escherichia coli
Manually annotated by BRENDA team