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Literature summary for 3.5.1.93 extracted from

  • Luo, H.; Zhao, H.; Chang, Y.; Wang, Q.; Yu, H.; Shen, Z.
    Oriented immobilization and characterization of a poly-lysine-tagged cephalosporin C acylase on glyoxyl agarose support (2014), Appl. Biochem. Biotechnol., 175, 2114-2123.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information the enzyme is mutated by PCR method to add a 3G3K tag to the C-terminal of the beta-subunit, the wild-type and mutated enzyme have nearly equal specific activity. The mutant enzyme has a 20% higher expressed activity than its wild-type counterpart. Immobilization of mutated and wild-type enzyme on glyoxyl agarose support via surface lysine or the poly-lysine tag, respectively Pseudomonas sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics of free and immobilized wild-type and mutant enzymes, overview Pseudomonas sp.
0.041
-
(7R)-7-(4-carboxybutanamido)cephalosporanate pH 8.5, 37°C, free mutant enzyme Pseudomonas sp.
0.043
-
(7R)-7-(4-carboxybutanamido)cephalosporanate pH 8.5, 37°C, free wild-type enzyme Pseudomonas sp.
0.0438
-
(7R)-7-(4-carboxybutanamido)cephalosporanate pH 8.5, 37°C, immobilized mutant enzyme Pseudomonas sp.
0.0484
-
(7R)-7-(4-carboxybutanamido)cephalosporanate pH 8.5, 37°C, immobilized wild-type enzyme Pseudomonas sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(7R)-7-(4-carboxybutanamido)cephalosporanate + H2O Pseudomonas sp.
-
(7R)-7-aminocephalosporanate + glutarate
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas sp. P15557
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(7R)-7-(4-carboxybutanamido)cephalosporanate + H2O
-
Pseudomonas sp. (7R)-7-aminocephalosporanate + glutarate
-
?

Subunits

Subunits Comment Organism
heterodimer alphabeta structure, but not linked via disulfide bridge and not separable by SDS-PAGE Pseudomonas sp.

Synonyms

Synonyms Comment Organism
CCA
-
Pseudomonas sp.
cephalosporin C acylase
-
Pseudomonas sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Pseudomonas sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
free wild-type and mutant enzymes: pH 8.5, inactivation after 1 h, immobilized wild-type and mutant enzymes: pH 8.5, 30% and 10% activity remaing after 4 h Pseudomonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Pseudomonas sp.

pH Stability

pH Stability pH Stability Maximum Comment Organism
5.5
-
the enzyme activities of both free and immobilized enzymes are greatly reduced at pH 5.5 Pseudomonas sp.

General Information

General Information Comment Organism
additional information the protein structure of Pseudomonas SE83 CCA is obtained through the computational modeling with X-ray crystal structure of Pseudomonas N176 CCA (PDB accession code 4HST) as the template, three-dimensional structure, homology modeling, overview. The key residue of the enzyme, 1Ser of beta-subunit, is located in the active-site cavity, which is on the opposite side to the C-terminal of beta-subunit Pseudomonas sp.