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Literature summary for 2.3.1.198 extracted from

  • Petit, J.; Bres, C.; Mauxion, J.P.; Tai, F.W.; Martin, L.B.; Fich, E.A.; Joubes, J.; Rose, J.K.; Domergue, F.; Rothan, C.
    The glycerol-3-phosphate acyltransferase GPAT6 from tomato plays a central role in fruit cutin biosynthesis (2016), Plant Physiol., 171, 894-913 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene SlGPAT6, located on chromosome 9, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of SlGPAT6 wild-type and DELTASlGPAT6 mutant carrying the G163R mutation in a Saccharomyces cerevisiae gat1DELTA mutant strain with a GAT1 knockout Solanum lycopersicum

Protein Variants

Protein Variants Comment Organism
G163R isolation of a set of fruit brightness mutants (named glossy mutants) with abnormal fruit cutin amounts/compositions from the EMS-mutagenized tomato mutant population (cv Micro-Tom). The glossy mutant line P23F12 exhibits enhanced fruit brightness and a reduced cutin load. Whole-genome sequencing and gene mapping show that a single G613A nucleotide transition in the first exon leading to a G163R nonsynonymous mutation in gene SlGPAT (Solyc09g014350) is responsible for the mutant glossy fruit phenotype, i.e. mutant gpat6-a, overview. The inactive mutant gpat6-a has a fruit cuticle that shows reduced levels of C16 cutin monomers. No differences are observed in total wax load between wild-type and gpat6-a fruits, but differences in wax composition are apparent, such as increased or decreased levels of several minor C25 to C30 alkanes in the gpat6-a mutant. Since both even- and odd-numbered alkanes display similar trends, these variations are likely independent of the alkane biosynthetic pathways. The most striking wax compositional change in the gpat6-a mutant is an approximately 5fold increase in delta- and alpha-amyrin levels and to a lesser extent in beta-amyrin levels. In contrast to waxes, the total cutin load in gpat6-a is reduced by almost 3fold. MapMan-based general overview of genes differentially expressed between wild-type and gpat6-a mutant fruit Solanum lycopersicum

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
Solanum lycopersicum 5783
-
membrane a transmembrane enzyme Solanum lycopersicum 16020
-
microsome
-
Solanum lycopersicum
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Solanum lycopersicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
9(10),16-dihydroxyhexadecanoyl-CoA + sn-glycerol 3-phosphate Solanum lycopersicum the principal putative substrate of SlGPAT6 is 9(10),16-dihydroxyhexadecanoic acid (C16:0 diOH) is the major cutin monomer present in tomato fruit cuticles CoA + 2-(9(10),16-dihydroxyhexadecanoyl)-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate Solanum lycopersicum
-
CoA + 2-acyl-sn-glycerol 3-phosphate
-
?

Organism

Organism UniProt Comment Textmining
Solanum lycopersicum A0A3Q7I0S2 cv. Micro-Tom, a EMS-mutagenized tomato mutant population
-

Source Tissue

Source Tissue Comment Organism Textmining
fruit
-
Solanum lycopersicum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
16-hydroxyhexadecanoyl-CoA + sn-glycerol 3-phosphate
-
Solanum lycopersicum CoA + 2-(16-hydroxyhexadecanoyl)-sn-glycerol 3-phosphate
-
?
9(10),16-dihydroxyhexadecanoyl-CoA + sn-glycerol 3-phosphate
-
Solanum lycopersicum CoA + 2-(9(10),16-dihydroxyhexadecanoyl)-sn-glycerol 3-phosphate
-
?
9(10),16-dihydroxyhexadecanoyl-CoA + sn-glycerol 3-phosphate the principal putative substrate of SlGPAT6 is 9(10),16-dihydroxyhexadecanoic acid (C16:0 diOH) is the major cutin monomer present in tomato fruit cuticles Solanum lycopersicum CoA + 2-(9(10),16-dihydroxyhexadecanoyl)-sn-glycerol 3-phosphate
-
?
acyl-CoA + sn-glycerol 3-phosphate
-
Solanum lycopersicum CoA + 2-acyl-sn-glycerol 3-phosphate
-
?
hexadecane-1,16-dioyl-CoA + sn-glycerol 3-phosphate
-
Solanum lycopersicum CoA + 2-hexadecane-1,16-dioyl-sn-glycerol 3-phosphate
-
?
hexadecanoyl-CoA + sn-glycerol 3-phosphate
-
Solanum lycopersicum CoA + 2-hexadecanoyl-sn-glycerol 3-phosphate
-
?
additional information analysis of SlGPAT6 substrate specificity of wild-type and mutant enzymes, overview Solanum lycopersicum ?
-
-

Synonyms

Synonyms Comment Organism
GPAT6
-
Solanum lycopersicum
SlGPAT6
-
Solanum lycopersicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Solanum lycopersicum

General Information

General Information Comment Organism
malfunction the G163R mutation in gpat6-a confers a loss of SlGPAT6-mediated GPAT activity leading to P23F12 glossy mutant line with with abnormal fruit cutin amounts/compositions and increased fruit brightness. Loss of SlGPAT6 function leads to altered expression of genes involved in cuticle and cell wall formation and remodeling Solanum lycopersicum
additional information structural modeling of SlGPAT6, based on the Methanococcus jannaschii phospho-Ser phosphatase template and restricted to the N-terminal 17 to 207 amino acid region, generated in silico, revealing that the G-to-R amino acid substitution at position 163 is close to the cluster of residues that are essential for the catalytic activity and Mg2+ binding of GPAT6 Solanum lycopersicum
physiological function glycerol-3-phosphate acyltransferase GPAT6 from tomato plays a central role in fruit cutin biosynthesis. Wild-type SlGPAT6 has the dual acyltransferase and phosphatase activities expected from a GPAT enzyme involved in cutin monomer biosynthesis Solanum lycopersicum