Literature summary for 3.5.1.4 extracted from

Andrade, J.; Karmali, A.; Carrondo, M.A.; Frazao, C.
Structure of amidase from Pseudomonas aeruginosa showing a trapped acyl transfer reaction intermediate state (2007), J. Biol. Chem., 282, 19598-19605.

Crystallization (Commentary)

Crystallization (Comment)	Organism
high resolution crystallographic structure shows that each amidase monomer is formed by a globular four-layer alphabetbetaalpha sandwich domain with an additional 81-residue long C-terminal segment. This wraps arm-in-arm with a homologous C-terminal chain of another monomer, producing a strongly packed dimer. In the crystal, the biological active homo-hexameric amidase is built grouping three such dimers around a crystallographic 3fold axis	Pseudomonas aeruginosa
purified wild-type enzyme, 25 mg/ml protein in 50 mM Tris-HCl, pH 7.2, containing 5 mM DTT and 1 mM EDTA, hexagonal crystals, X-ray diffraction structure determination and analysis at 1.25-1.4 A resolution, modeling	Pseudomonas aeruginosa

Crystallization (Comment)

Organism

high resolution crystallographic structure shows that each amidase monomer is formed by a globular four-layer alphabetbetaalpha sandwich domain with an additional 81-residue long C-terminal segment. This wraps arm-in-arm with a homologous C-terminal chain of another monomer, producing a strongly packed dimer. In the crystal, the biological active homo-hexameric amidase is built grouping three such dimers around a crystallographic 3fold axis

Pseudomonas aeruginosa

purified wild-type enzyme, 25 mg/ml protein in 50 mM Tris-HCl, pH 7.2, containing 5 mM DTT and 1 mM EDTA, hexagonal crystals, X-ray diffraction structure determination and analysis at 1.25-1.4 A resolution, modeling

Pseudomonas aeruginosa

Protein Variants

Protein Variants	Comment	Organism
additional information	the constitutive mutant strain L10 is isolated by mutagenesis from the wild-type strain 8602	Pseudomonas aeruginosa

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
38000	-	6 * 38000, SDS-PAGE	Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	-	-	-
Pseudomonas aeruginosa	-	gene amiE, inducible enzyme	-

Purification (Commentary)

Purification (Comment)	Organism
-	Pseudomonas aeruginosa

Reaction

Reaction	Comment	Organism	Reaction ID
a monocarboxylic acid amide + H2O = a monocarboxylate + NH3	the enzyme contains a nitrilase catalytic triad at the bottom of a 13-A deep, funnel-shaped pocket, accessible from the solvent through a narrow neck with 3-A diameter	Pseudomonas aeruginosa	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
additional information	optimal growth at 37°C	Pseudomonas aeruginosa	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme catalyses the hydrolysis of small aliphatic amides	Pseudomonas aeruginosa	?	-	?

Subunits

Subunits	Comment	Organism
hexamer	6 * 38000, SDS-PAGE	Pseudomonas aeruginosa
More	each amidase monomer is formed by a globular four-layer alphabetabetaalpha sandwich domain with an additional 81-residue long C-terminal segment, this wraps arm-in-arm with a homologous C-terminal chain of another monomer, producing a strongly packed dimer, the active homo-hexameric amidase is built grouping three such dimers around a crystallographic 3fold axis, structure analysis and comparisons, overview	Pseudomonas aeruginosa

Synonyms

Synonyms	Comment	Organism
More	the enzyme belongs to the thiol nitrilases family	Pseudomonas aeruginosa

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Pseudomonas aeruginosa

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
55	-	wild-type enzyme, stable	Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.2	-	assay at	Pseudomonas aeruginosa