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Literature summary for 3.5.1.87 extracted from

  • Mei, Y.Z.; Wan, Y.M.; He, B.F.; Ying, H.J.; Ouyang, P.K.
    New gene cluster from the thermophile Bacillus fordii MH602 in the conversion of DL-5-substituted hydantoins to L-amino acids (2009), J. Microbiol. Biotechnol., 19, 1497-1505.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 Siminovitchia fordii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44000
-
SDS-PAGE Siminovitchia fordii

Organism

Organism UniProt Comment Textmining
Siminovitchia fordii
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MH602, thermophile bacterium
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
the activity of the recombinant enzyme is lower than the wild-type strain MH602. The expressed proteins are mainly present in the insoluble fraction, indicating the formation of inclusion bodies Siminovitchia fordii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-carbamoyl-L-phenylalanine + H2O the recombinant L-carbamoylase from Escherichia coli harboring the pET-Case is L-stereospecific Siminovitchia fordii L-phenylalanine + CO2 + NH3
-
?

Synonyms

Synonyms Comment Organism
hyuC gene name, from the hyu gene cluster containing four genes with novel cluster organization characteristics Siminovitchia fordii
L-carbamoylase
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Siminovitchia fordii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
assay at Siminovitchia fordii