Literature summary for 3.5.4.23 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.

Search for more literature for 3.5.4.23

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Organism

Organism	UniProt	Comment	Textmining
Aspergillus terreus	P0C2P0	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
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)

Renatured (Comment)	Organism
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)

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

Subunits

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

Synonyms

Synonyms	Comment	Organism
blasticidin S deaminase	-	Aspergillus terreus
BS deaminase	-	Aspergillus terreus
BSD	-	Aspergillus terreus

Temperature Stability [°C]

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

Turnover Number [1/s]

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

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Release 2023.1 (January 2023)