EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
3.1.2.14 | 751804 |
A new herbicidal site of action Cinmethylin binds to acyl-ACP thioesterase and inhibits plant fatty acid biosynthesis |
Pestic. Biochem. Physiol. |
148 |
116-125 |
2018 |
Lemna |
29891362 |
3.1.2.14 | 751897 |
Acyl carrier proteins from sunflower (Helianthus annuus L.) seeds and their influence on FatA and FatB acyl-ACP thioesterase activities |
Planta |
244 |
479-490 |
2016 |
Helianthus annuus |
27095109 |
3.1.2.14 | 750653 |
Cellular and molecular responses of Dunaliella tertiolecta by expression of a plant medium chain length fatty acid specific acyl-ACP thioesterase |
Front. Microbiol. |
9 |
619 |
2018 |
Cinnamomum camphora |
29670594 |
3.1.2.14 | 749676 |
Chimeric fatty acyl-acyl carrier protein thioesterases provide mechanistic insight into enzyme specificity and expression |
Appl. Environ. Microbiol. |
84 |
e02868-17 |
2018 |
Cuphea palustris |
29549102 |
3.1.2.14 | 751885 |
Elucidating the substrate specificities of acyl-lipid thioesterases from diverse plant taxa |
Plant Physiol. Biochem. |
127 |
104-118 |
2018 |
Zea mays |
29571003 |
3.1.2.14 | 751885 |
Elucidating the substrate specificities of acyl-lipid thioesterases from diverse plant taxa |
Plant Physiol. Biochem. |
127 |
104-118 |
2018 |
Arabidopsis thaliana |
29571003 |
3.1.2.14 | 751156 |
Expression of the heterologous Dunaliella tertiolecta fatty acyl-ACP thioesterase leads to increased lipid production in Chlamydomonas reinhardtii |
J. Biotechnol. |
247 |
60-67 |
2017 |
Dunaliella tertiolecta |
28279815 |
3.1.2.14 | 749480 |
Highly active C8-acyl-ACP thioesterase variant isolated by a synthetic selection strategy |
ACS Synth. Biol. |
7 |
2205-2215 |
2018 |
Cuphea palustris |
30064208 |
3.1.2.14 | 749859 |
Identification of active site residues implies a two-step catalytic mechanism for acyl-ACP thioesterase |
Biochem. J. |
475 |
3861-3873 |
2018 |
Cocos nucifera |
30409825 |
3.1.2.14 | 749859 |
Identification of active site residues implies a two-step catalytic mechanism for acyl-ACP thioesterase |
Biochem. J. |
475 |
3861-3873 |
2018 |
Cuphea viscosissima |
30409825 |