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

BRENDA support

Literature summary extracted from

  • Kimura, M.; Furuichi, M.; Yamamoto, M.; Kumasaka, T.; Mizuno, H.; Miyano, M.; Yamaguchi, I.
    The flexible C-terminal region of Aspergillus terreus blasticidin S deaminase: identification of its functional roles with deletion enzymes (2002), Biochem. Biophys. Res. Commun., 290, 421-426.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.4.23 expression of deletion mutants as soluble enzymes in Escherichia coli Aspergillus terreus

Protein Variants

EC Number Protein Variants Comment Organism
3.5.4.23 additional information construction of 5 C-terminal deletion mutants, i.e. DELTA130, DELTA126-130, DELTA127-130, DELTA128-130, and DELTA129-130 Aspergillus terreus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.4.23 additional information the wild-type and deletion mutant enzymes are highly resistant to protease digestions Aspergillus terreus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.4.23 1
-
 blasticidin S wild-type enzyme, 30°C Aspergillus terreus
3.5.4.23 8.1
-
 blasticidin S deletion mutant DELTA130, 30°C Aspergillus terreus
3.5.4.23 9.6
-
 blasticidin S deletion mutant DELTA129-130, 30°C Aspergillus terreus
3.5.4.23 20
-
 blasticidin S deletion mutants DELTA128-130, DELTA127-130, DELTA126-130, 30°C Aspergillus terreus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.4.23 Zn2+ tightly bound catalytic zinc, 1 zinc ion per subunit, coordinative role in enzyme tetrameric structure stabilization and protein folding, overview Aspergillus terreus

Organism

EC Number Organism UniProt Comment Textmining
3.5.4.23 Aspergillus terreus P0C2P0
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.5.4.23 blasticidin S + H2O = deaminohydroxyblasticidin S + NH3 the C-terminal flexible region appears to be directly involved in enzyme-substrate interaction facilitating the access of substrate to the active site, Tyr126, Trp128, and Gly130 are key residues Aspergillus terreus
a

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.5.4.23 wild-type and deletion mutant apoenzymes, prepared by zinc removal via EDTA, exhibit similar physical properties in thermodynamic refolding into the stable tetramer conformation, reconstitution with zinc Aspergillus terreus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.4.23 blasticidin S + H2O
-
 Aspergillus terreus deaminohydroxyblasticidin S + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.4.23 More the C-terminus of the enzyme is flexible Aspergillus terreus
3.5.4.23 tetramer the 4 polypeptides are tightly coordinated to the structurally and catalytically important zinc atom of each subunit Aspergillus terreus

Synonyms

EC Number Synonyms Comment Organism
3.5.4.23 blasticidin S deaminase
-
 Aspergillus terreus
3.5.4.23 BS deaminase
-
 Aspergillus terreus
3.5.4.23 BSD
-
 Aspergillus terreus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.4.23 65
-
 half-lives of wild-type and mutant enzymes Aspergillus terreus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.4.23 71
-
 blasticidin S deletion mutant DELTA126-130, 30°C Aspergillus terreus
3.5.4.23 320
-
 blasticidin S deletion mutant DELTA127-130, 30°C Aspergillus terreus
3.5.4.23 390
-
 blasticidin S deletion mutant DELTA128-130, 30°C Aspergillus terreus
3.5.4.23 770
-
 blasticidin S wild-type enzyme, 30°C Aspergillus terreus
3.5.4.23 860
-
 blasticidin S deletion mutant DELTA130, 30°C Aspergillus terreus
3.5.4.23 890
-
 blasticidin S deletion mutant DELTA129-130, 30°C Aspergillus terreus