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Literature summary for 2.3.1.22 extracted from

  • Vijayaraj, P.; Jashal, C.B.; Vijayakumar, A.; Rani, S.H.; Venkata Rao, D.K.; Rajasekharan, R.
    A bifunctional enzyme that has both monoacylglycerol acyltransferase and acyl hydrolase activities (2012), Plant Physiol., 160, 667-683.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.22

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00832
-
 oleoyl-CoA pH and temperature not specified in the publication Arachis hypogaea
0.01481
-
 1-oleoyl-sn-glycerol pH and temperature not specified in the publication Arachis hypogaea

Organism

Organism UniProt Comment Textmining
Arachis hypogaea H9LBH7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oleoyl-CoA + 1,2-dioleoyl-sn-glycerol
-
 Arachis hypogaea ?
-
 ?
oleoyl-CoA + 1-oleoyl-sn-glycerol preferred substrate Arachis hypogaea CoA + 1,2-dioleoyl-sn-glycerol
-
 ?
oleoyl-CoA + 2-oleoyl-sn-glycerol
-
 Arachis hypogaea ?
-
 ?

Synonyms

Synonyms Comment Organism
MGAT enzyme shows bifunctional activities: monoacylglycerol and lysophosphatidylcholine hydrolytic activities Arachis hypogaea

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
 Arachis hypogaea

pH Range

pH Minimum pH Maximum Comment Organism
7 8 maximum activity Arachis hypogaea

General Information

General Information Comment Organism
metabolism overexpression of the MGAT gene in yeast (Saccharomyces cerevisiae) causes an increase in triacylglycerol accumulation Arachis hypogaea