Literature summary for 3.4.11.24 extracted from

Hershcovitz, Y.F.; Gilboa2, R.; Reiland, V.; Shoham, G.; Shoham, Y.
Catalytic mechanism of SGAP, a double-zinc aminopeptidase from Streptomyces griseus (2007), FEBS J., 274, 3864-3876.

Search for more literature for 3.4.11.24

Protein Variants

Protein Variants	Comment	Organism
E131D	a general acid-base mutant, thermodynamic parameters for the reaction are similar to the wild-type enzyme, but the kcat of the mutant is 4fold reduced, while the activation energy is elevated compared to the wild-type enzyme	Streptomyces griseus

Inhibitors

Inhibitors	Comment	Organism	Structure
fluoride	noncompetitive inhibitor at pH 5.9-8.0, fluoride ion interacts equally with the free enzyme as with the enzyme-substrate complex	Streptomyces griseus
phosphate	-	Streptomyces griseus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics,enzyme-substrate interaction, overview	Streptomyces griseus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	activates	Streptomyces griseus
Zn2+	double-zinc aminopeptidase	Streptomyces griseus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
30000	-	1 * 30000	Streptomyces griseus

Organism

Organism	UniProt	Comment	Textmining
Streptomyces griseus	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues	catalytic reaction mechanism, a single proton transfer is involved in catalysis at pH 8.0, whereas two proton transfers are implicated at pH 6.5, involvement of a zinc-bound hydroxide as the reaction nucleophile, Tyr246 polarizes the carbonyl carbon and stabilizes the transition state, enzyme-substrate interaction, overview	Streptomyces griseus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-leucine 4-nitroanilide + H2O	-	Streptomyces griseus	L-leucine + 4-nitroaniline	-	?
additional information	the thermostable enzyme prefers large hydrophobic N-terminal residues in its peptide and protein substrates, a single proton transfer is involved in catalysis at pH 8.0, whereas two proton transfers are implicated at pH 6.5	Streptomyces griseus	?	-	?

Subunits

Subunits	Comment	Organism
monomer	1 * 30000	Streptomyces griseus

Synonyms

Synonyms	Comment	Organism
double-zinc aminopeptidase	-	Streptomyces griseus
SGAP	-	Streptomyces griseus

Temperature Range [°C]

Temperature Minimum [°C]	Temperature Maximum [°C]	Comment	Organism
19	56	-	Streptomyces griseus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.5	8	assay at	Streptomyces griseus

pH Range

pH Minimum	pH Maximum	Comment	Organism
additional information	-	a single proton transfer is involved in catalysis at pH 8.0, whereas two proton transfers are implicated at pH 6.5	Streptomyces griseus

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
11.4	-	fluoride	pH 8.0	Streptomyces griseus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)