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Literature summary for 2.3.1.51 extracted from

  • Yu, X.H.; Prakash, R.R.; Sweet, M.; Shanklin, J.
    Coexpressing Escherichia coli cyclopropane synthase with Sterculia foetida lysophosphatidic acid acyltransferase enhances cyclopropane fatty acid accumulation (2014), Plant Physiol., 164, 455-465.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.51

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Arabidopsis thaliana Sterculia foetida

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Sterculia foetida 5783
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43723
-
 x * 43723, calculated from amino acid sequence Sterculia foetida

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate Sterculia foetida
-
 CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
 ?
additional information Sterculia foetida the enzyme has preference for cyclopropene fatty acids ?
-
 ?

Organism

Organism UniProt Comment Textmining
Sterculia foetida V9TK35
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acyl-CoA + 1-acyl-sn-glycerol 3-phosphate
-
 Sterculia foetida CoA + 1,2-diacyl-sn-glycerol 3-phosphate
-
 ?
additional information the enzyme has preference for cyclopropene fatty acids Sterculia foetida ?
-
 ?

Subunits

Subunits Comment Organism
? x * 43723, calculated from amino acid sequence Sterculia foetida

Synonyms

Synonyms Comment Organism
acyl-CoA:lysophosphatidic acid acyltransferase
-
 Sterculia foetida
LPAT
-
 Sterculia foetida
lysophosphatidic acid acyltransferase
-
 Sterculia foetida

pI Value

Organism Comment pI Value Maximum pI Value
Sterculia foetida calculated from amino acid sequence
-
 9.6