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

BRENDA support

Literature summary for 3.5.1.4 extracted from

  • Giordano, C.; Ammendola, S.
    Characterization of mutants of Sulfolobus solfataricus signature amidase able to hydrolyse R-ketoprofen amide (2008), Protein Pept. Lett., 15, 617-623.
    View publication on PubMed
Search for more literature for 3.5.1.4

Application

Application Comment Organism
synthesis the enzyme is useful for production of optically pure S-arylpropionic acids Saccharolobus solfataricus

Cloned(Commentary)

Cloned (Comment) Organism
-
 Saccharolobus solfataricus
expression of gene SsAH in Escherichia coli strain BL21(DE3) as soluble, active protein, sequence comparison of wild-type and mutants enzymes, overview Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
additional information identification of three independent SsAH mutants, SsAH-7, SsAH-14 and SsAH-15, that hydrolyze R-ketoprofen amide, although the mutations do not specifically affect residues near the active site, or directly interacting with the substrate, computational models of their three-dimensional structure, overview. Sequence comparison of wild-type and mutants enzymes, overview Saccharolobus solfataricus
additional information after random mutagenesis 3 mutants are characterized Saccharolobus solfataricus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000096
-
 ketoprofen amide
-
 Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-
Saccharolobus solfataricus
-
 gene SsAH
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus
recombinant enzyme 2.35fold from Escherichia coli strain BL21(DE3) by anion exchange chromatography Saccharolobus solfataricus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.19
-
 >99% enantiomeric excess Saccharolobus solfataricus
0.52
-
-
 Saccharolobus solfataricus
16
-
 purified recombinant wild-type enzyme Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R,S)-2-(3-benzoylphenyl)propanamide + H2O enantioselective for the S-enantiomer Saccharolobus solfataricus (S)-2-(3-benzoylphenyl)propanoic acid + NH3
-
 ?
(R,S)-ketoprofen amide + H2O the enzyme hydrolyzes S-ketoprofen amide to its corresponding acid in an absolutely enantioselective manner Saccharolobus solfataricus (S)-ketoprofen + NH3
-
 ?
(S)-2-(3-benzoylphenyl)propanamide + H2O ketoprofen amide, R-amide is not converted Saccharolobus solfataricus (S)-2-(3-benzoylphenyl)propanoic acid + NH3 ketoprofen ?
(S)-ibuprofen amide + H2O
-
 Saccharolobus solfataricus (S)-ibuprofen + NH3
-
 ?
benzamide + H2O
-
 Saccharolobus solfataricus benzoic acid + NH3
-
 ?
ibuprofen amide + H2O
-
 Saccharolobus solfataricus ibuprofen + NH3
-
 ?
additional information the amidase shows high enantioselectivity for (S)-arylpropionic amides, it is active on nitriles, molecular modelling, overview Saccharolobus solfataricus ?
-
 ?

Synonyms

Synonyms Comment Organism
amidase
-
 Saccharolobus solfataricus
signature amidase
-
 Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
 assay at Saccharolobus solfataricus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
887
-
 ketoprofen amide
-
 Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Saccharolobus solfataricus