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Literature summary for 3.5.2.B2 extracted from

  • Wang, J.; Zhao, H.; Zhao, G.; Chen, D.; Tao, Y.; Wu, S.
    Enhancing the atypical esterase promiscuity of the gamma-lactamase Sspg from Sulfolobus solfataricus by substrate screening (2019), Appl. Microbiol. Biotechnol., 103, 4077-4087 .
    View publication on PubMed
Search for more literature for 3.5.2.B2

Application

Application Comment Organism
synthesis mutant enzyme Q192S/L223Y can be employed for the preparation of (-)-gamma-lactam and also for that of (2S,3R)-ethyl 3-phenylglycidate Saccharolobus solfataricus

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli TOP10 cells Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
C145A mutant enzyme retains 51% of activities relative to the wild-type enzyme Saccharolobus solfataricus
K96A mutant enzyme loses entire hydrolysis activities Saccharolobus solfataricus
Q192N no improvement of activity as compared to wild-type enzyme Saccharolobus solfataricus
Q192R no improvement of activity as compared to wild-type enzyme Saccharolobus solfataricus
Q192S/L223Y high activity and enantioselectivity to phenylglycidate analogs such as methyl 3-methoxyphenylglycidate and methyl 3-phenylglycidate. It shows moderate enantioselectivity to several other chiral compounds. The mutant shows the highest activity towards methyl 2-methylbutyrate but poor enantioselectivity. Catalytic efficiency for gamma-lactamase activity (kcat/Km) of the mutant enzyme shows a slight decrease (about 15%) when compared to that of the wild-type enzyme. When compared to wild-type enzyme, the stability of the mutant enzyme does not change considerably at 50°C. The study employs a three-step method to successfully convert a (+)-gamma-lactamase into an esterase. This three-step method includes the combination of the sequence alignment to recommend the possible substrate, substrate screening to expand the substrate scope, and substrate-enzyme docking to enhance esterase activity Saccharolobus solfataricus
S171A mutant enzyme loses entire hydrolysis activities Saccharolobus solfataricus
S195A mutant enzyme loses entire hydrolysis activities Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus P95896
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Saccharolobus solfataricus ATCC 35092 P95896
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Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the wild-type enzyme cannot hydrolyze classical esterase p-nitrophenyl substrates such as p-nitrophenylbutyrate. It shows weak hydrolysis activizy of (+)-trans-enantiomer of ethyl chrysanthemate. It shows very low activity with ethyl 2-phenylcyclopropanecarboxylate. The wild-type enzyme can hydrolyze ethyl 3-phenylglycidate with high enantioselectivity (hydrolysis of (2S,3R)-ethyl-3-phenylglycidate, enantiomeric excess: 99.5%) but low activity Saccharolobus solfataricus ?
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 ?
additional information the wild-type enzyme cannot hydrolyze classical esterase p-nitrophenyl substrates such as p-nitrophenylbutyrate. It shows weak hydrolysis activizy of (+)-trans-enantiomer of ethyl chrysanthemate. It shows very low activity with ethyl 2-phenylcyclopropanecarboxylate. The wild-type enzyme can hydrolyze ethyl 3-phenylglycidate with high enantioselectivity (hydrolysis of (2S,3R)-ethyl-3-phenylglycidate, enantiomeric excess: 99.5%) but low activity Saccharolobus solfataricus ATCC 35092 ?
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 ?

Synonyms

Synonyms Comment Organism
Sspg
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 Saccharolobus solfataricus