Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.13.1 extracted from

  • Hao, G.; Naumann, T.; Vaughan, M.; McCormick, S.; Usgaard, T.; Kelly, A.; Ward, T.
    Characterization of a Fusarium graminearum salicylate hydroxylase (2019), Front. Microbiol., 10, 3219 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.13.1

Cloned(Commentary)

Cloned (Comment) Organism
gene shy1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative RT-PCR enzyme expression analysis Fusarium graminearum
gene shyC, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative RT-PCR enzyme expression analysis Fusarium graminearum

Protein Variants

Protein Variants Comment Organism
additional information generation of a disruption mutant of Fusarium graminearum strain NRRL 46422 gene shyC, replacement of FgShyC is confirmed by genome sequencing and analysis Fusarium graminearum
additional information generation of enzyme deletion mutants. The wild-type strain PH-1 degrades approximately 80% of the added salicylate (SA) whereas Fgshy1 deletion mutants are significantly reduced in their ability to degrade SA in liquid culture. Compared to media control, Fgshy1-M1 and M2 mutants are able to degrade 10 and 11% of the SA, respectively, but mutant Fgshy1-M18 is almost inactive. With addition of SA at concentrations of 1 and 2 mM, the Fgshy1 mutant grows slightly slower than the wild-type PH-1 and the hyphae turn yellow. But no significant growth difference between Fgshy1 mutant and PH-1 is found by statistical analysis. Disruption of FgShy1 does not significantly affect Fusarium graminearum Fusarium graminearum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
salicylate + NADH + 2 H+ + O2 Fusarium graminearum
-
 catechol + NAD+ + H2O + CO2
-
 ?
salicylate + NADH + 2 H+ + O2 Fusarium graminearum NRRL 31084
-
 catechol + NAD+ + H2O + CO2
-
 ?
salicylate + NADH + 2 H+ + O2 Fusarium graminearum CBS 123657
-
 catechol + NAD+ + H2O + CO2
-
 ?
salicylate + NADH + 2 H+ + O2 Fusarium graminearum PH-1
-
 catechol + NAD+ + H2O + CO2
-
 ?
salicylate + NADH + 2 H+ + O2 Fusarium graminearum ATCC MYA-4620
-
 catechol + NAD+ + H2O + CO2
-
 ?
salicylate + NADH + 2 H+ + O2 Fusarium graminearum FGSC 9075
-
 catechol + NAD+ + H2O + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Fusarium graminearum A0A455ZJ87 Fusarium graminearum
-
Fusarium graminearum I1RIL9 Fusarium graminearum
-
Fusarium graminearum ATCC MYA-4620 I1RIL9 Fusarium graminearum
-
Fusarium graminearum CBS 123657 I1RIL9 Fusarium graminearum
-
Fusarium graminearum FGSC 9075 I1RIL9 Fusarium graminearum
-
Fusarium graminearum NRRL 31084 I1RIL9 Fusarium graminearum
-
Fusarium graminearum NRRL 46422 A0A455ZJ87 Fusarium graminearum
-
Fusarium graminearum PH-1 I1RIL9 Fusarium graminearum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the ability of wild-type from strain 46422 and the FgshyC mutant to metabolize salicylate (SA) is tested. When SA is added to liquid cultures of either wild-type strain 46422 or the FgShyC mutant, it is degraded similarly. This demonstrates that Fusarium graminearum produces salicylate hydroxylases and argues against this role for FgShyC. In addition, recombinant FgShyC protein expressed in Escherichia coli does not convert SA to catechol in a colorimetric plate assay. Although FgShyC has sequence homology with salicylic hydroxylase genes, it does not function as a salicylate hydroxylase in our assays Fusarium graminearum ?
-
-
additional information the ability of wild-type from strain 46422 and the FgshyC mutant to metabolize salicylate (SA) is tested. When SA is added to liquid cultures of either wild-type strain 46422 or the FgShyC mutant, it is degraded similarly. This demonstrates that Fusarium graminearum produces salicylate hydroxylases and argues against this role for FgShyC. In addition, recombinant FgShyC protein expressed in Escherichia coli does not convert SA to catechol in a colorimetric plate assay. Although FgShyC has sequence homology with salicylic hydroxylase genes, it does not function as a salicylate hydroxylase in our assays Fusarium graminearum NRRL 46422 ?
-
-
salicylate + NADH + 2 H+ + O2
-
 Fusarium graminearum catechol + NAD+ + H2O + CO2
-
 ?
salicylate + NADH + 2 H+ + O2
-
 Fusarium graminearum NRRL 31084 catechol + NAD+ + H2O + CO2
-
 ?
salicylate + NADH + 2 H+ + O2
-
 Fusarium graminearum CBS 123657 catechol + NAD+ + H2O + CO2
-
 ?
salicylate + NADH + 2 H+ + O2
-
 Fusarium graminearum PH-1 catechol + NAD+ + H2O + CO2
-
 ?
salicylate + NADH + 2 H+ + O2
-
 Fusarium graminearum ATCC MYA-4620 catechol + NAD+ + H2O + CO2
-
 ?
salicylate + NADH + 2 H+ + O2
-
 Fusarium graminearum FGSC 9075 catechol + NAD+ + H2O + CO2
-
 ?

Synonyms

Synonyms Comment Organism
FAD_binding_3 domain-containing protein UniProt Fusarium graminearum
FGSG_03657
-
 Fusarium graminearum
FgShy1
-
 Fusarium graminearum
FgShyC
-
 Fusarium graminearum
SA hydroxylase
-
 Fusarium graminearum
salicylate hydroxylase
-
 Fusarium graminearum
Shy1
-
 Fusarium graminearum
ShyC
-
 Fusarium graminearum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Fusarium graminearum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Fusarium graminearum

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Fusarium graminearum
NADH
-
 Fusarium graminearum

Expression

Organism Comment Expression
Fusarium graminearum the enzyme is highly induced by salicylate. FgShy1 expression is induced about fourfold during wheat head infection up
Fusarium graminearum the enzyme is only very slightly induced by salicylate up

General Information

General Information Comment Organism
evolution phylogenetic analysis and tree, salicylate hydroxylase homologue FgShy1 is most closely related to NahG from Pseudomonas putida and Shy1 from Ustilago maydis Fusarium graminearum
evolution phylogenetic analysis and tree, salicylate hydroxylase homologue FgShyC is unique to the North American population 2 (NA2), FgShyC is present only in NA2 strains Fusarium graminearum
physiological function FgShy1 is not essential for the growth of Fusarium graminearum on agar medium with SA, suggesting additional enzymes or other SA degradation pathways exist Fusarium graminearum