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Literature summary extracted from

  • Yang, W.; Pollard, M.; Li-Beisson, Y.; Ohlrogge, J.
    Quantitative analysis of glycerol in dicarboxylic acid-rich cutins provides insights into Arabidopsis cutin structure (2016), Phytochemistry, 130, 159-169 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.198 gene gpat4 Arabidopsis thaliana
2.3.1.198 gene gpat8 Arabidopsis thaliana

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.198 additional information glycerol content is strongly reduced in both stem and leaf cutin from all Arabidopsis thaliana mutants analyzed (gpat4/gpat8). Knocking out of these genes individually or as a pair (gpat4/gpat8) leads to large reductions in Arabidopsis thaliana cutin monomer loads, especially in the major monomer octadeca-6,9-diene-1,18-dioate (C18:2 DCA) Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.198 acyl-CoA + sn-glycerol 3-phosphate Arabidopsis thaliana
-
 CoA + 2-acyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.198 acyl-CoA + sn-glycerol 3-phosphate Arabidopsis thaliana Col-0
-
 CoA + 2-acyl-sn-glycerol 3-phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.198 Arabidopsis thaliana
-
-
-
2.3.1.198 Arabidopsis thaliana Q5XF03
-
-
2.3.1.198 Arabidopsis thaliana Col-0
-
-
-
2.3.1.198 Arabidopsis thaliana Col-0 Q5XF03
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.198 leaf
-
 Arabidopsis thaliana
-
2.3.1.198 stem
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.198 acyl-CoA + sn-glycerol 3-phosphate
-
 Arabidopsis thaliana CoA + 2-acyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.198 acyl-CoA + sn-glycerol 3-phosphate isozyme GPAT4 acylates glycerol-3-phosphate at the sn-2 position Arabidopsis thaliana CoA + 2-acyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.198 acyl-CoA + sn-glycerol 3-phosphate isozyme GPAT8 acylates glycerol-3-phosphate at the sn-2 position Arabidopsis thaliana CoA + 2-acyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.198 acyl-CoA + sn-glycerol 3-phosphate
-
 Arabidopsis thaliana Col-0 CoA + 2-acyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.198 acyl-CoA + sn-glycerol 3-phosphate isozyme GPAT4 acylates glycerol-3-phosphate at the sn-2 position Arabidopsis thaliana Col-0 CoA + 2-acyl-sn-glycerol 3-phosphate
-
 ?
2.3.1.198 acyl-CoA + sn-glycerol 3-phosphate isozyme GPAT8 acylates glycerol-3-phosphate at the sn-2 position Arabidopsis thaliana Col-0 CoA + 2-acyl-sn-glycerol 3-phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.198 glycerol-3-phosphate 2-O-acyltransferases
-
 Arabidopsis thaliana
2.3.1.198 GPAT4
-
 Arabidopsis thaliana
2.3.1.198 GPAT8
-
 Arabidopsis thaliana
2.3.1.198 sn-2-GPAT
-
 Arabidopsis thaliana

General Information

EC Number General Information Comment Organism
2.3.1.198 malfunction glycerol content is strongly reduced in both stem and leaf cutin from all Arabidopsis thaliana mutants analyzed (gpat4/gpat8). Knocking out any of these genes individually, or as a pair (gpat4/gpat8), leads to large reductions in Arabidopsis thaliana cutin monomer loads, especially in the major monomer octadeca-6,9-diene-1,18-dioate (C18:2 DCA). sn-2-GPATs play pivotal roles in providing glycerol as a structural monomer for cutin through regiospecific sn-2 acylation of glycerol-3-phosphate. The double-knockout gpat4/gpat8 has an overall 60-70% reduction of aliphatic monomers in stem and leaf cutin, and the most pronounced decrease occurs in its major monomer, C18:2 dicarboxylic acyl-CoA (DCA) Arabidopsis thaliana
2.3.1.198 metabolism isozymes GPAT4 and GPAT8 are glycerol-3-phosphate 2-O acyltransferases that catalyze the first step in leaf and stem cutin acylglycerol assembly Arabidopsis thaliana
2.3.1.198 physiological function glycerol-3-phosphate 2-O-acyltransferases (sn-2-GPATs) are essential for cutin biosynthesis and involved in cutin polymerization, cutin structures and compositions in plant tissues, detailed overview Arabidopsis thaliana
2.3.1.198 physiological function the enzyme is involved in cutin polymerization, cutin structures and compositions in plant tissues, detailed overview Arabidopsis thaliana