Biology:3-hydroxydecanoyl-(acyl-carrier-protein) dehydratase

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Short description: Class of enzymes
3-hydroxydecanoyl-(acyl-carrier-protein) dehydratase
Identifiers
EC number4.2.1.60
CAS number9030-79-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

3-hydroxydecanoyl-(acyl-carrier-protein) dehydratase (EC 4.2.1.60, D-3-hydroxydecanoyl-[acyl-carrier protein] dehydratase, 3-hydroxydecanoyl-acyl carrier protein dehydrase, 3-hydroxydecanoyl-acyl carrier protein dehydratase, β-hydroxydecanoyl thioester dehydrase, β-hydroxydecanoate dehydrase, beta-hydroxydecanoyl thiol ester dehydrase, FabA, β-hydroxyacyl-acyl carrier protein dehydratase, HDDase, β-hydroxyacyl-ACP dehydrase, (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] hydro-lyase) is an enzyme with systematic name (3R)-3-hydroxydecanoyl-(acyl-carrier protein) hydro-lyase.[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction

(1) a (3R)-3-hydroxydecanoyl-[acyl-carrier protein] [math]\displaystyle{ \rightleftharpoons }[/math] a trans-dec-2-enoyl-[acyl-carrier protein] + H2O
(2) a (3R)-3-hydroxydecanoyl-[acyl-carrier protein] [math]\displaystyle{ \rightleftharpoons }[/math] a cis-dec-3-enoyl-[acyl-carrier protein] + H2O

This enzyme is specific for C10 chain length.

References

  1. "Beta-hydroxydecanoyl thioester dehydrase. I. Purification and properties". The Journal of Biological Chemistry 242 (19): 4418–31. October 1967. PMID 4863739. 
  2. "Beta-hydroxydecanoyl thioester dehydrase. II. Mode of action". The Journal of Biological Chemistry 242 (19): 4432–40. October 1967. PMID 4863740. 
  3. "Crystallization and preliminary X-ray analysis of beta-hydroxydecanoyl thiol ester dehydrase from Escherichia coli". The Journal of Biological Chemistry 265 (9): 5110–2. March 1990. PMID 2180957. 
  4. "Regulation of fatty acid biosynthesis in Escherichia coli". Microbiological Reviews 57 (3): 522–42. September 1993. PMID 8246839. 
  5. "Enzymatic synthesis of monounsaturated fatty acids". Acc. Chem. Res. 2: 193–202. 1969. doi:10.1021/ar50019a001. 
  6. "Functional replacement of the FabA and FabB proteins of Escherichia coli fatty acid synthesis by Enterococcus faecalis FabZ and FabF homologues". The Journal of Biological Chemistry 279 (33): 34489–95. August 2004. doi:10.1074/jbc.M403874200. PMID 15194690. 
  7. Neidhardt, F.C., ed (1996). "Biosynthesis of membrane lipids". Escherichia coli and Salmonella: Cellular and Molecular Biology. 1 (2nd ed.). Washington, DC: ASM Press. pp. 612–636. 

External links