BRENDA - Enzyme Database
show all sequences of 5.3.3.18

Crystal structure of phenylacetic acid degradation protein PaaG from Thermus thermophilus HB8

Kichise, T.; Hisano, T.; Takeda, K.; Miki, K.; Proteins 76, 779-786 (2009)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization (Commentary)
Organism
to 1.85 A resolution. Enzyme consists of three identical subunits related by local three-fold symmetry. The monomer is comprised of a spiral and a helical domain with a fold characteristic of the crotonase superfamily. A putative active site residue, Asp136, is situated in an active site cavity and surrounded by several hydrophobic and hydrophilic residues. The active site cavity is sufficiently large to accommodate a ring substrate. Two conformations are observed for helix H2 located adjacent to the active site. Helix H2 is kinked at Asn81 in two subunits, whereas it is kinked at Leu77 in the other subunit, and the side chain of Tyr80 is closer to Asp136. This indicates that catalytic reaction of PaaG may proceed with large conformational changes at the active site
Thermus thermophilus
Organism
Organism
UniProt
Commentary
Textmining
Thermus thermophilus
Q5SLK3
-
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q5SLK3
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-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
additional information
enzyme may undergo isomerization or a ring-opening reaction via a Delta3,Delta2-enoyl-CoA isomerase-like mechanism
723737
Thermus thermophilus
?
-
-
-
-
additional information
enzyme may undergo isomerization or a ring-opening reaction via a Delta3,Delta2-enoyl-CoA isomerase-like mechanism
723737
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
?
-
-
-
-
Crystallization (Commentary) (protein specific)
Crystallization
Organism
to 1.85 A resolution. Enzyme consists of three identical subunits related by local three-fold symmetry. The monomer is comprised of a spiral and a helical domain with a fold characteristic of the crotonase superfamily. A putative active site residue, Asp136, is situated in an active site cavity and surrounded by several hydrophobic and hydrophilic residues. The active site cavity is sufficiently large to accommodate a ring substrate. Two conformations are observed for helix H2 located adjacent to the active site. Helix H2 is kinked at Asn81 in two subunits, whereas it is kinked at Leu77 in the other subunit, and the side chain of Tyr80 is closer to Asp136. This indicates that catalytic reaction of PaaG may proceed with large conformational changes at the active site
Thermus thermophilus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
additional information
enzyme may undergo isomerization or a ring-opening reaction via a Delta3,Delta2-enoyl-CoA isomerase-like mechanism
723737
Thermus thermophilus
?
-
-
-
-
additional information
enzyme may undergo isomerization or a ring-opening reaction via a Delta3,Delta2-enoyl-CoA isomerase-like mechanism
723737
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
?
-
-
-
-
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
Synonyms
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
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716755
Teufel
Bacterial phenylalanine and ph ...
Pseudomonas sp., Pseudomonas sp. Y2
Proc. Natl. Acad. Sci. USA
107
14390-14395
2010
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723737
Kichise
Crystal structure of phenylace ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Proteins
76
779-786
2009
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714891
Ismail
Functional genomics by NMR spe ...
Escherichia coli
Eur. J. Biochem.
270
3047-3054
2003
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