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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: epithiospecifier protein

Gene: AT1G54040

Species: Arabidopsis thaliana col

Summary:
An ESP cDNA (AT1G54040) from Arabidopsis thaliana, ecotype Col, was heterologously expressed in Escherichia coli. The un-purified protein was then assayed in the presence of myrosinase. The Arabidopsis ESP catalyzes the conversion of alkenylglucosinolates to epithionitriles, whereas nonalkenylglucosinolates were converted to simple nitriles. The enzyme activity is not dependent on Fe2+, although Fe2+ can increase nitrile formation. Without Fe2+, the formation of epithionitriles was 75% of the maximum. 37% enzyme activity was retained in the presence of 1 mM EDTA [Lambrix01].

In another report [Zabala05], the Arabidopsis ESP is ferrous ion dependent. The discrepancy of the observations is not clear. Ectopic expression of this cDNA in Col-5 background significantly changed the profile of glucosinolate hydrolysis products in this ecotype. The wild type Col-5 produces mostly isothiocynates, whereas the transformed plants produce significant amounts of nitriles [Zabala05].

Molecular Weight of Polypeptide: 37.0 kD (from nucleotide sequence)

pI: 5.65 [Lambrix01]

Unification Links: PhylomeDB:Q8RY71 , Pride:Q8RY71 , Protein Model Portal:Q8RY71 , SMR:Q8RY71 , String:Q8RY71 , TAIR:AT1G54040 , UniProt:Q8RY71

Relationship Links: InterPro:IN-FAMILY:IPR006652 , InterPro:IN-FAMILY:IPR015915 , Pfam:IN-FAMILY:PF01344 , Smart:IN-FAMILY:SM00612

Gene-Reaction Schematic: ?


Enzymatic reaction of: thiohydroximate-O-sulfate sulfohydrolase (nitrile-forming) (epithiospecifier protein)

a thiohydroximate-O-sulfate without a terminal alkene <=> a nitrile + sulfate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

In Pathways: glucosinolate breakdown

Cofactors or Prosthetic Groups: Fe2+ [Lambrix01]


Enzymatic reaction of: alkenyl thiohydroximate-O-sulfate sulfohydrolase (epithionitrile-forming) (epithiospecifier protein)

a thiohydroximate-O-sulfate with a terminal alkene <=> an epithionitrile + sulfate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

In Pathways: glucosinolate breakdown

Cofactors or Prosthetic Groups: Fe2+ [Lambrix01]


References

Lambrix01: Lambrix V, Reichelt M, Mitchell-Olds T, Kliebenstein DJ, Gershenzon J (2001). "The Arabidopsis epithiospecifier protein promotes the hydrolysis of glucosinolates to nitriles and influences Trichoplusia ni herbivory." Plant Cell 13(12);2793-807. PMID: 11752388

Zabala05: Zabala Mde T, Grant M, Bones AM, Bennett R, Lim YS, Kissen R, Rossiter JT (2005). "Characterisation of recombinant epithiospecifier protein and its over-expression in Arabidopsis thaliana." Phytochemistry 66(8);859-67. PMID: 15845404


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, BIOCYC14A.