EC Number   |
General Information |
Reference |
|---|
    5.4.4.2 | physiological function |
Arabidopsis ICS1 represents a divergent isoform for inducible salicylic acid synthesis during defense |
706530 |
| 5.4.4.2 | physiological function |
chorismate-utilizing enzymes (CUE) such as chorismate mutase, anthranilate synthase, chorismate pyruvate-lyase, 4-amino-4-deoxychorismate synthase, isochorismate synthase and salicylate synthase are responsible for converting chorismate into various products necessary for the survival of bacteria |
747617 |
| 5.4.4.2 | metabolism |
enzyme ICS does not act as isochorismate pyruvate lyase (IPL, EC 4.2.99.21) and bifunctional salicylate synthase, it does not convert chorismate into salicylate. In Arabidopsis thaliana, salicylate is synthesized from chorismic acid, derived from the shikimic acid pathway, occuring in the plastid |
747030 |
| 5.4.4.2 | more |
enzyme structure comparisons and analysis, active site structure, overview. Ala304 plays an important role in positioning the peptide-bond carbonyl, enabling the formation of a proper hydrogen bond to the isochorismate C2 hydroxyl |
-, 726636 |
| 5.4.4.2 | more |
enzyme three-dimensional structure analysis, the lysine residue, Lys190, might be involved in the activation of water molecules and the subsequent nucleophilic attack on the C2 carbon of chorismate without directly involving the magnesium ion, participation of the Lys residue during the activation of the substrate or nucleophilic agent |
747617 |
| 5.4.4.2 | evolution |
genes ATICS1 and AtICS2 are both located on chromosome 1 on different sides of the centromere, and they are likely a result of a duplication event, since they are bordered by similar genes. At the DNA sequence level, the protein-coding regions of the two genes share a high degree of similarity, but this does not extend into the untranslated regions |
747030 |
| 5.4.4.2 | more |
homology modeling of isozymes ICS1 and ICS2 using Serratia marcescens anthranilate synthase (TrpE, PDB ID 1I7Q) as reference structure |
747030 |
| 5.4.4.2 | metabolism |
isochorismate synthase 1 is a key enzyme in salicylate biosynthesis in Arabidopsis thaliana. The TCP family transcription factor AtTCP8 is a regulator of isozyme ICS1, it binds to a typical TCP binding site in the ICS1 promoter. Expression patterns of TCP8 and its corresponding gene TCP9 largely overlap with ICS1 under pathogen attack. Strong interactions between TCP8 and SAR deficient 1 (SARD1), WRKY family transcription factor 28 (WRKY28), NAC (NAM/ATAF1, ATAF2/CUC2) family transcription factor 019 (NAC019), as well as among TCP8, TCP9 and TCP20, implying a complex coordinated regulatory mechanism underlying ICS1 expression. There is a strong negative regulatory region between -128 and -316 bp, and the binding of repressor(s) to this region may be necessary for suppression of ICS1 expression during plant growth and development, TCP8 can bind at this region, while TCP5, TCP11 and TCP19 appear not to bind to the promoter region. TCP8 specifically binds to the TCP binding site in the ICS1 promoter in vitro and in vivo. Trans-activation capability of TCP8. TCP8/TCP9 positively regulate ICS1 expression with redundancy upon pathogen infection, and TCPs are involved in maintaining ICS1 expression, yeast one-hybrid (Y1H) screening and transactivation activity assay, detailed overview |
-, 748946 |
| 5.4.4.2 | physiological function |
isochorismate synthase 1 is required for salicylate biosynthesis. SUMO homeostasis influences salicylate biosynthesis in wild-type plants, and also demonstrate that elevated levels of salicylate strongly increase the abundance of SUMO conjugates |
748944 |
| 5.4.4.2 | physiological function |
isozyme AtICS1 is required for increased salicylate biosynthesis in response to pathogens, and its expression can be stimulated throughout the leaf by virus infection and exogenous salicylate. Isozymes AtICS1 and AtICS2 can be successful in competing for chorismate in vivo |
747030 |
