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Literature summary extracted from

  • Kalinger, R.S.; Rowland, O.
    Determinants of substrate specificity in a catalytically diverse family of acyl-ACP thioesterases from plants (2023), BMC Plant Biol., 23, 0001.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
3.1.2.14 Arabidopsis thaliana Q8W583 isoform ALT3
-
3.1.2.14 Arabidopsis thaliana F4HX80 isoform ALT4
-
3.1.2.14 Medicago truncatula G7K1I0 isoform ALT1
-
3.1.2.14 Zea mays A0A1D6HF47 isoform ALT3
-

Synonyms

EC Number Synonyms Comment Organism
3.1.2.14 acyl-lipd thioesterase
-
 Zea mays
3.1.2.14 acyl-lipid thioesterase
-
 Medicago truncatula
3.1.2.14 acyl-lipid thioesterase
-
 Arabidopsis thaliana
3.1.2.14 ALT1
-
 Medicago truncatula
3.1.2.14 ALT3
-
 Zea mays
3.1.2.14 ALT3
-
 Arabidopsis thaliana
3.1.2.14 ALT4
-
 Arabidopsis thaliana
3.1.2.14 pollen thioesterase
-
 Zea mays

General Information

EC Number General Information Comment Organism
3.1.2.14 physiological function exchange of regions of amino acid sequence between ALT-type thioesterases from Arabidopsis thaliana, Medicago truncatula, and Zea mays to create chimeric ALT proteins. The presence of a 31-CQH[G/C]RH-36 motif on the central alpha-helix shifts chain-length specificity towards 12-14 carbon chains, and is a core determinant of substrate specificity in ALT-type thioesterases with preference for 12-14 carbon 3-hydroxyacyl- and beta-ketoacyl-ACP substrates. To be functional, an additional 108-KXXA-111 motif and compatible sequence spanning aa77-93 of the surrounding beta-sheet must also be present. Amino acis 77-93 play a significant role in dictating whether an ALT will prefer up to 10-carbon or above 12-carbon acyl chain-lengths, and aa91-96 influence selectivity for substrates of fully or partially reduced oxidation states. Amino acids 64-67 on the hot dog-fold beta-sheet are important for enabling an ALT to act on 3-hydroxy fatty acyl-ACP substrates Medicago truncatula
3.1.2.14 physiological function exchange of regions of amino acid sequence between ALT-type thioesterases from Arabidopsis thaliana, Medicago truncatula, and Zea mays to create chimeric ALT proteins. The presence of a 31-CQH[G/C]RH-36 motif on the central alpha-helix shifts chain-length specificity towards 12-14 carbon chains, and is a core determinant of substrate specificity in ALT-type thioesterases with preference for 12-14 carbon 3-hydroxyacyl- and beta-ketoacyl-ACP substrates. To be functional, an additional 108-KXXA-111 motif and compatible sequence spanning aa77-93 of the surrounding beta-sheet must also be present. Amino acis 77-93 play a significant role in dictating whether an ALT will prefer up to 10-carbon or above 12-carbon acyl chain-lengths, and aa91-96 influence selectivity for substrates of fully or partially reduced oxidation states. Amino acids 64-67 on the hot dog-fold beta-sheet are important for enabling an ALT to act on 3-hydroxy fatty acyl-ACP substrates Zea mays
3.1.2.14 physiological function exchange of regions of amino acid sequence between ALT-type thioesterases from Arabidopsis thaliana, Medicago truncatula, and Zea mays to create chimeric ALT proteins. The presence of a 31-CQH[G/C]RH-36 motif on the central alpha-helix shifts chain-length specificity towards 12-14 carbon chains, and is a core determinant of substrate specificity in ALT-type thioesterases with preference for 12-14 carbon 3-hydroxyacyl- and beta-ketoacyl-ACP substrates. To be functional, an additional 108-KXXA-111 motif and compatible sequence spanning aa77-93 of the surrounding beta-sheet must also be present. Amino acis 77-93 play a significant role in dictating whether an ALT will prefer up to 10-carbon or above 12-carbon acyl chain-lengths, and aa91-96 influence selectivity for substrates of fully or partially reduced oxidation states. Amino acids 64-67 on the hot dog-fold beta-sheet are important for enabling an ALT to act on 3-hydroxy fatty acyl-ACP substrates Arabidopsis thaliana