BRENDA - Enzyme Database show
show all sequences of 5.3.3.18

Bacterial phenylalanine and phenylacetate catabolic pathway revealed

Teufel, R.; Mascaraque, V.; Ismail, W.; Voss, M.; Perera, J.; Eisenreich, W.; Haehnel, W.; Fuchs, G.; Proc. Natl. Acad. Sci. USA 107, 14390-14395 (2010)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas sp.
-
-
-
Pseudomonas sp. Y2
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA
enzyme acts as a ring 1,2-epoxyphenylacetyl-CoA isomerase forming oxepin-CoA. It mediates the formation and stabilization of the enolate form by abstracting a proton from the side chain at C2 of ring 1,2-epoxyphenylacetyl-CoA. Addition of the abstracted proton to C8, which becomes C4, of the ring leads to a rearrangement of the double bonds and results in a C-C cleavage of the two epoxy-C-O bonds, yielding the oxepin
716755
Pseudomonas sp.
2-oxepin-2(3H)-ylideneacetyl-CoA
-
-
-
?
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA
enzyme acts as a ring 1,2-epoxyphenylacetyl-CoA isomerase forming oxepin-CoA. It mediates the formation and stabilization of the enolate form by abstracting a proton from the side chain at C2 of ring 1,2-epoxyphenylacetyl-CoA. Addition of the abstracted proton to C8, which becomes C4, of the ring leads to a rearrangement of the double bonds and results in a C-C cleavage of the two epoxy-C-O bonds, yielding the oxepin
716755
Pseudomonas sp. Y2
2-oxepin-2(3H)-ylideneacetyl-CoA
-
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA
enzyme acts as a ring 1,2-epoxyphenylacetyl-CoA isomerase forming oxepin-CoA. It mediates the formation and stabilization of the enolate form by abstracting a proton from the side chain at C2 of ring 1,2-epoxyphenylacetyl-CoA. Addition of the abstracted proton to C8, which becomes C4, of the ring leads to a rearrangement of the double bonds and results in a C-C cleavage of the two epoxy-C-O bonds, yielding the oxepin
716755
Pseudomonas sp.
2-oxepin-2(3H)-ylideneacetyl-CoA
-
-
-
?
2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA
enzyme acts as a ring 1,2-epoxyphenylacetyl-CoA isomerase forming oxepin-CoA. It mediates the formation and stabilization of the enolate form by abstracting a proton from the side chain at C2 of ring 1,2-epoxyphenylacetyl-CoA. Addition of the abstracted proton to C8, which becomes C4, of the ring leads to a rearrangement of the double bonds and results in a C-C cleavage of the two epoxy-C-O bonds, yielding the oxepin
716755
Pseudomonas sp. Y2
2-oxepin-2(3H)-ylideneacetyl-CoA
-
-
-
?
Other publictions for EC 5.3.3.18
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
727930
Grishin
Protein-protein interactions i ...
Thermus thermophilus
J. Biol. Chem.
287
37986-37996
2012
-
-
-
1
-
-
-
-
-
-
2
1
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
1
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
716755
Teufel
Bacterial phenylalanine and ph ...
Pseudomonas sp., Pseudomonas sp. Y2
Proc. Natl. Acad. Sci. USA
107
14390-14395
2010
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
723737
Kichise
Crystal structure of phenylace ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Proteins
76
779-786
2009
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
714891
Ismail
Functional genomics by NMR spe ...
Escherichia coli
Eur. J. Biochem.
270
3047-3054
2003
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-