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Literature summary for 1.14.13.1 extracted from

  • Zhou, F.; Last, R.L.; Pichersky, E.
    Degradation of salicylic acid to catechol in Solanaceae by SA 1-hydroxylase (2021), Plant Physiol., 185, 876-891 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene Solyc08g063130, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, transient recombinant expression in Nicotiana benthamiana leaves Solanum lycopersicum

Protein Variants

Protein Variants Comment Organism
additional information generation of SlSA1H antisense knockdown transgenic tomato plants. In three analyzed SlSA1H RNAi lines (RNAi-23, RNAi-4, and RNAi-22), mRNA levels of SlSA1H relative to wild-type are reduced by 54%, 59%, and 56% in stems, respectively, and by 35%, 55%, and 66% in leaves, respectively. Whereas no significant morphological changes are observed in these plants, the guaiacol levels relative to wild-type are reduced by 47%, 52%, and 60% in stems, respectively, and by 22%, 24%, and 65% in leaves, respectively. Veratrole cannot be detected in any of these three RNAi lines Solanum lycopersicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0091
-
salicylate recombinant enzyme, pH and temperature not specified in the publication Solanum lycopersicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
salicylate + NADH + 2 H+ + O2 Solanum lycopersicum
-
catechol + NAD+ + H2O + CO2
-
?

Organism

Organism UniProt Comment Textmining
Solanum lycopersicum A0A3Q7IJD4
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Solanum lycopersicum
-
additional information transcript levels of SlSA1H are highest in stems and its expression is correlated with the formation of the methylated catechol derivatives guaiacol and veratrole Solanum lycopersicum
-
stem
-
Solanum lycopersicum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the recombinant SlSA1H enzyme shows high substrate specificity. Poor activity with 6-methylsalicylate, no activity with 3-hydroxybenzoate, 4-hydroxybenzoate, 2-methoxybenzoate, 2-coumarate, gallate, shikimate, 2,3-dihydroxybenzoate, 2,4-dihydroxybenzoate, 2,5-dihydroxybenzoate, 2,6-dihydroxybenzoate, 3,4-dihydroxybenzoate, 3,5-dihydroxybenzoate, 3-methylsalicylate, 4-methylsalicylate, and 5-methylsalicylate Solanum lycopersicum ?
-
-
salicylate + NADH + 2 H+ + O2
-
Solanum lycopersicum catechol + NAD+ + H2O + CO2
-
?

Synonyms

Synonyms Comment Organism
FAD/NADH-dependent SA 1-hydroxylase
-
Solanum lycopersicum
SA 1-decarboxylase/hydroxylase
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Solanum lycopersicum
SA 1-hydroxylase
-
Solanum lycopersicum
SA1H
-
Solanum lycopersicum
salcylic acid 1-hydroxylase UniProt Solanum lycopersicum
SlSA 1H
-
Solanum lycopersicum
SlSA1H
-
Solanum lycopersicum
Solyc08g063130
-
Solanum lycopersicum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0783
-
salicylate recombinant enzyme, pH and temperature not specified in the publication Solanum lycopersicum

Cofactor

Cofactor Comment Organism Structure
FAD
-
Solanum lycopersicum
NADH
-
Solanum lycopersicum

General Information

General Information Comment Organism
evolution the NahG homologue from tomato (SlSA1H) belongs to the FAD/NAD(P)-binding oxidoreductase family and is capable of catalyzing the oxidative decarboxylation (i.e. 1-hydroxylation) of SA to catechol both in vitro and in planta. Phylogenetic tree, overview Solanum lycopersicum
physiological function in plants, salicylate (SA) is best known as an important phytohormone involved in the activation of defense response against a wide range of biotic and abiotic stresses. Besides its role in immune responses, SA also plays crucial roles in plant growth and developmental processes such as photosynthesis, flowering, and senescence. Because of its chemical reactivity, lipophilicity, and phytotoxicity, most of the SA synthesized in plants is further modified into different derivatives to fine-tune its storage, function, and/or mobility. These modifications include glycosylation, methylation, sulfonation, amino acid conjugation, and hydroxylation. Enzyme SlSA1H may play an important role in the homeostasis of SA in vivo Solanum lycopersicum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
8.6
-
salicylate recombinant enzyme, pH and temperature not specified in the publication Solanum lycopersicum