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Literature summary for 3.5.2.B2 extracted from

  • Ren, L.; Zhu, S.; Shi, Y.; Gao, S.; Zheng, G.
    Enantioselective resolution of gamma-lactam by a novel thermostable type II (+)-gamma-lactamase from the hyperthermophilic archaeon Aeropyrum pernix (2015), Appl. Biochem. Biotechnol., 176, 170-184.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
-
 Aeropyrum pernix

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular modeling. Structure does not show similartity to the domain structure of known gamma-lactamases, leading to gamma lactamase type II Aeropyrum pernix

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47000
-
 x * 47000, SDS-PAGE Aeropyrum pernix

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one + H2O
-
 Aeropyrum pernix (1R,4S)-4-aminocyclopent-2-ene-1-carbaldehyde enzyme specifically hydrolyzes the (+)-lactam, (1S,4R)-2-azabicyclo[2.2.1]hept-5-en-3-one, without any actin against the (-)-isomer. Yield is 48%, 97% enantiomeric excess ?

Subunits

Subunits Comment Organism
? x * 47000, SDS-PAGE Aeropyrum pernix

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
100
-
-
 Aeropyrum pernix

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
100
-
 12 h, no loss of activity Aeropyrum pernix

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
 Aeropyrum pernix