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Literature summary 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

EC Number Protein Variants Comment Organism
3.5.1.93 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.93 additional information
-
 additional information Michaelis-Menten kinetics of free and immobilized wild-type and mutant enzymes, overview Pseudomonas sp.
3.5.1.93 0.041
-
 (7R)-7-(4-carboxybutanamido)cephalosporanate pH 8.5, 37°C, free mutant enzyme Pseudomonas sp.
3.5.1.93 0.043
-
 (7R)-7-(4-carboxybutanamido)cephalosporanate pH 8.5, 37°C, free wild-type enzyme Pseudomonas sp.
3.5.1.93 0.0438
-
 (7R)-7-(4-carboxybutanamido)cephalosporanate pH 8.5, 37°C, immobilized mutant enzyme Pseudomonas sp.
3.5.1.93 0.0484
-
 (7R)-7-(4-carboxybutanamido)cephalosporanate pH 8.5, 37°C, immobilized wild-type enzyme Pseudomonas sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.93 (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O Pseudomonas sp.
-
 (7R)-7-aminocephalosporanate + glutarate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.93 Pseudomonas sp. P15557
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.93 (7R)-7-(4-carboxybutanamido)cephalosporanate + H2O
-
 Pseudomonas sp. (7R)-7-aminocephalosporanate + glutarate
-
 ?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
3.5.1.93 CCA
-
 Pseudomonas sp.
3.5.1.93 cephalosporin C acylase
-
 Pseudomonas sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.93 37
-
 assay at Pseudomonas sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.93 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.93 8.5
-
 assay at Pseudomonas sp.

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.5.1.93 5.5
-
 the enzyme activities of both free and immobilized enzymes are greatly reduced at pH 5.5 Pseudomonas sp.

General Information

EC Number General Information Comment Organism
3.5.1.93 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.