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Literature summary 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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.22 0.00832
-
oleoyl-CoA pH and temperature not specified in the publication Arachis hypogaea
2.3.1.22 0.01481
-
1-oleoyl-sn-glycerol pH and temperature not specified in the publication Arachis hypogaea

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.22 Arachis hypogaea H9LBH7
-
-

Substrates and Products (Substrate)

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.22 30
-
-
Arachis hypogaea

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.3.1.22 7 8 maximum activity Arachis hypogaea

General Information

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