Oleate hydratase

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is (R)-10-hydroxystearate 10-hydro-lyase (oleate-forming). This enzyme is also called (R)-10-hydroxystearate 10-hydro-lyase.

References

Davis EN, Wallen LL, Goodwin JC, Rohwedder WK, Rhodes RA (1969). "Microbial hydration of cis-9-alkenoic acids". Lipids. 4 (5): 356–62. doi:10.1007/BF02531006. PMID 5823715.
Gotouda H, Takatori T, Terazawa K, Nagao M, Tarao H (1988). "The mechanism of experimental adipocere formation: hydration and dehydrogenation in microbial synthesis of hydroxy and oxo fatty acids". Forensic Sci. Int. 37 (4): 249–57. doi:10.1016/0379-0738(88)90233-2. PMID 3410394.
Jr; Torkelson, A; Kisic, A; Bednarczyk, DJ; Schroepfer Jr, GJ (1970). "Stereospecific hydration of the delta-9 double bond of oleic acid". J. Biol. Chem. 245 (15): 3790–7. PMID 5492948.

Carbon-oxygen lyases (EC 4.2) (primarily dehydratases)

4.2.1: Hydro-Lyases	Carbonic anhydrase Fumarase Aconitase Enolase Alpha Enolase 2 Enoyl-CoA hydratase/3-Hydroxyacyl ACP dehydrase Methylglutaconyl-CoA hydratase Tryptophan synthase Cystathionine beta synthase Porphobilinogen synthase 3-Isopropylmalate dehydratase Urocanase Uroporphyrinogen III synthase Nitrile hydratase

4.2.2: Acting on polysaccharides	Hyaluronate lyase

4.2.3: Acting on phosphates	Threonine synthase

4.2.99: Other	Carboxymethyloxysuccinate lyase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

This article is issued from Wikipedia - version of the Thursday, March 31, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.