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Literature summary for 3.5.1.93 extracted from

  • Anandan, A.; Vallet, C.; Coyle, T.; Moustafa, I.M.; Vrielink, A.
    Crystallization and preliminary diffraction analysis of an engineered cephalosporin acylase (2010), Acta Crystallogr. Sect. F, 66, 808-810.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
full-length wild-type enzyme or the double mutant variant H296S/H309S are transformed in Escherichia coli BL21 Pseudomonas sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
preliminary crystals of the double mutant can be grown from 4% PEG 8000, 100 mM Tris-HCl, pH 8.5, carried out by vapour diffusion using hanging-drop method at 17.85°C, 1.57 A resolution Pseudomonas sp.

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
N176
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
double mutant H296S/H309S exhibits 22fold enhanced specificity and reactivity for cephalosporin C over the natural substrate glutaryl-7-aminocephalosporanic acid Pseudomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cephalosporin C + H2O double mutant H296S/H309S exhibits 22fold enhanced specificity and reactivity for cephalosporin C over the natural substrate glutaryl-7-aminocephalosporanic acid Pseudomonas sp. cephalosporanic acid + 2-amino-5-hydroxypentanoate
-
?
glutaryl-7-aminocephalosporanic acid + H2O double mutant H296S/H309S exhibits 22fold enhanced specificity and reactivity for cephalosporin C over the natural substrate glutaryl-7-aminocephalosporanic acid Pseudomonas sp. 7-aminocephalosporanic acid + glutarate
-
?

Synonyms

Synonyms Comment Organism
cephalorin acylase
-
Pseudomonas sp.