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

BRENDA support

Literature summary for 4.1.99.1 extracted from

  • Pioselli, B.; Bettati, S.; Demidkina, T.V.; Zakomirdina, L.N.; Phillips, R.S.; Mozzarelli, A.
    Tyrosine phenol-lyase and tryptophan indole-lyase encapsulated in wet nanoporous silica gels: Selective stabilization of tertiary conformations (2004), Protein Sci., 13, 913-924.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
biotechnology encapsulation of enzyme in wet nanoporous silica gels to selectively stabilize tertiary and quarternary protein conformations and to develop bioreactors and biosensors Proteus vulgaris

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.18
-
S-(o-nitrophenyl)-L-cysteine pH 8.0, 25°C Proteus vulgaris
16
-
S-methyl-L-cysteine pH 8.0, 25°C Proteus vulgaris

Organism

Organism UniProt Comment Textmining
Proteus vulgaris
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-(o-nitrophenyl)-L-cysteine
-
Proteus vulgaris ?
-
?
S-methyl-L-cysteine
-
Proteus vulgaris ?
-
?