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Information on EC 3.4.11.25 - beta-peptidyl aminopeptidase
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EC Tree
3.4.11.25 beta-peptidyl aminopeptidaseSpecify your search results
Word Map
- 3.4.11.25
- synthesis
-
beta-amino
- beta-peptides
-
alpha-amino
- rrna
-
l-configuration
- preproteins
- aminopeptidases
-
anthropi
-
ochrobactrum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
cleaves N-terminal beta-homoamino acids from peptides composed of 2 to 6 amino acids
Synonyms
beta-peptidyl aminopeptidase, 3-2w4 bapa, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-2W4 BapA
Y2 BapA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cleaves N-terminal beta-homoamino acids from peptides composed of 2 to 6 amino acids
-
-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(beta-homoAla-beta-homoLys-beta-homoPhe)2 + H2O
beta-homoAla + beta-homoLys + beta-homoPhe
2 beta-homoGly 4-nitroanilide
beta-homoGly-beta-homoGly 4-nitroanilide + 4-nitroaniline
-
product of mutant S237C, synthesized efficiently without degradation
-
?
beta-homoGly 4-nitroanilide + H2O
beta-homoGly + 4-nitroaniline
-
wild-type enzyme shows beta-homoGly-beta-homoGly-4-nitroanilide synthetic activity, but the product vanishes in a few min and converts to free beta-homoGly
-
?
beta-homoVal-Ile-Tyr + H2O
beta-homoVal + Ile-Tyr
only the N-terminal beta-homoVal is released. Hydrolysis at 32% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
insulin + rac-3-aminobutanamide
?
enatioselectivity for beta-alanine is more than 300:1
-
-
r
Val-Ile-Tyr + H2O
beta-homoVal + Ile-Tyr
only the N-terminal beta-homoVal is released. Preferred substrate
-
-
?
(beta-homoAla-beta-homoLys-beta-homoPhe)2 + H2O
beta-homoAla + beta-homoLys + beta-homoPhe
completely degraded to the corresponding beta-homoamino acids within 312 h
-
-
?
(beta-homoAla-beta-homoLys-beta-homoPhe)2 + H2O
beta-homoAla + beta-homoLys + beta-homoPhe
completely degraded to the corresponding beta-homoamino acids within 312 h
-
-
?
(beta-homoAla-beta-homoLys-beta-homoPhe)2 + H2O
beta-homoAla + beta-homoLys + beta-homoPhe
completely degraded to the corresponding beta-homoamino acids within 312 h
-
-
?
(beta-homoAla-beta-homoLys-beta-homoPhe)2 + H2O
beta-homoAla + beta-homoLys + beta-homoPhe
completely degraded to the corresponding beta-homoamino acids within 312 h
-
-
?
beta-Ala-Ile-beta-homoTyr + H2O
beta-Ala + Ile-beta-homoTyr
1.5% of the activity with beta-homoAla-beta-homoLeu
-
-
?
beta-Ala-Ile-beta-homoTyr + H2O
beta-Ala + Ile-beta-homoTyr
hydrolysis at 1.5% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-Ala-Ile-beta-homoTyr + H2O
beta-Ala + Ile-beta-homoTyr
hydrolysis at 1.5% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-Ala-Ile-beta-homoTyr + H2O
beta-Ala + Ile-beta-homoTyr
1.5% of the activity with beta-homoAla-beta-homoLeu
-
-
?
beta-Ala-Ile-beta-homoTyr + H2O
beta-Ala + Ile-beta-homoTyr
0.3% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-Ala-Ile-beta-homoTyr + H2O
beta-Ala + Ile-beta-homoTyr
hydrolysis at 0.3% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-Ala-Ile-beta-homoTyr + H2O
beta-Ala + Ile-beta-homoTyr
hydrolysis at 0.3% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-Ala-Ile-beta-homoTyr + H2O
beta-Ala + Ile-beta-homoTyr
0.3% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
i.e. carnosine, 2% of the activity with beta-homoAla-beta-homoLeu
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
i.e. carnosine. Hydrolysis at 2% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
i.e. carnosine. Hydrolysis at 2% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
i.e. carnosine, 2% of the activity with beta-homoAla-beta-homoLeu
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
i.e. carnosine, 0.8% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
i.e. carnosine. Hydrolysis at 0.7% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
i.e. carnosine. Hydrolysis at 0.7% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-Ala-L-His + H2O
beta-Ala + L-His
i.e. carnosine, 0.8% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-Ala-p-nitroanilide + H2O
beta-Ala + p-nitroaniline
-
-
-
?
beta-Ala-p-nitroanilide + H2O
beta-Ala + p-nitroaniline
-
-
-
?
beta-Ala-p-nitroanilide + H2O
beta-Ala + p-nitroaniline
-
-
-
?
beta-Ala-p-nitroanilide + H2O
beta-Ala + p-nitroaniline
-
-
-
?
beta-homoAla-beta-homoLeu + H2O
beta-homoAla + beta-homoLeu
preferred substrate
-
-
?
beta-homoAla-beta-homoLeu + H2O
beta-homoAla + beta-homoLeu
preferred substrate
-
-
?
beta-homoAla-beta-homoLeu + H2O
beta-homoAla + beta-homoLeu
-
-
-
?
beta-homoAla-beta-homoLeu + H2O
beta-homoAla + beta-homoLeu
35% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-homoAla-beta-homoLeu + H2O
beta-homoAla + beta-homoLeu
hydrolysis at 31% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-homoAla-beta-homoLeu + H2O
beta-homoAla + beta-homoLeu
35% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-homoAla-beta-homoLeu + H2O
beta-homoAla + beta-homoLeu
-
-
-
?
beta-homoAla-p-nitroanilide + H2O
beta-homoAla + p-nitroaniline
-
-
-
?
beta-homoAla-p-nitroanilide + H2O
beta-homoAla + p-nitroaniline
-
-
-
?
beta-homoArg-Ile-beta-homoTyr + H2O
beta-homoArg + Ile-beta-homoTyr
3.4% of the activity with beta-homoAla-beta-homoLeu
-
-
?
beta-homoArg-Ile-beta-homoTyr + H2O
beta-homoArg + Ile-beta-homoTyr
hydrolysis at 0.35% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-homoArg-Ile-beta-homoTyr + H2O
beta-homoArg + Ile-beta-homoTyr
0.2% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-homoArg-Ile-beta-homoTyr + H2O
beta-homoArg + Ile-beta-homoTyr
hydrolysis at 0.2% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-homoGln-Ile-beta-homoTyr + H2O
beta-homoGln + Ile-beta-homoTyr
0.3% of the activity with beta-homoAla-beta-homoLeu
-
-
?
beta-homoGln-Ile-beta-homoTyr + H2O
beta-homoGln + Ile-beta-homoTyr
hydrolysis at 0.25% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-homoGln-Ile-beta-homoTyr + H2O
beta-homoGln + Ile-beta-homoTyr
0.2% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-homoGln-Ile-beta-homoTyr + H2O
beta-homoGln + Ile-beta-homoTyr
hydrolysis at 0.2% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-homoHis-Ile-beta-homoTyr + H2O
beta-homoHis + Ile-beta-homoTyr
0.4% of the activity with beta-homoAla-beta-homoLeu
-
-
?
beta-homoHis-Ile-beta-homoTyr + H2O
beta-homoHis + Ile-beta-homoTyr
hydrolysis at 0.35% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-homoHis-Ile-beta-homoTyr + H2O
beta-homoHis + Ile-beta-homoTyr
0.3% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-homoHis-Ile-beta-homoTyr + H2O
beta-homoHis + Ile-beta-homoTyr
hydrolysis at 0.2% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-homoLeu-Ile-beta-homoTyr + H2O
beta-homoLeu + Ile-beta-homoTyr
12% of the activity with beta-homoAla-beta-homoLeu
-
-
?
beta-homoLeu-Ile-beta-homoTyr + H2O
beta-homoLeu + Ile-beta-homoTyr
hydrolysis at 12% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-homoLeu-Ile-beta-homoTyr + H2O
beta-homoLeu + Ile-beta-homoTyr
61% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-homoLeu-Ile-beta-homoTyr + H2O
beta-homoLeu + Ile-beta-homoTyr
hydrolysis at 54% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-homoLys-Ile-beta-homoTyr + H2O
beta-homoLys + Ile-beta-homoTyr
0.5% of the activity with beta-homoAla-beta-homoLeu
-
-
?
beta-homoLys-Ile-beta-homoTyr + H2O
beta-homoLys + Ile-beta-homoTyr
hydrolysis at 0.48% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-homoLys-Ile-beta-homoTyr + H2O
beta-homoLys + Ile-beta-homoTyr
0.5% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-homoLys-Ile-beta-homoTyr + H2O
beta-homoLys + Ile-beta-homoTyr
hydrolysis at 0.5% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-homoPhe-Ile-beta-homoTyr + H2O
beta-homoPhe + Ile-beta-homoTyr
15% of the activity with beta-homoAla-beta-homoLeu
-
-
?
beta-homoPhe-Ile-beta-homoTyr + H2O
beta-homoPhe + Ile-beta-homoTyr
hydrolysis at 15% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-homoPhe-Ile-beta-homoTyr + H2O
beta-homoPhe + Ile-beta-homoTyr
22% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-homoPhe-Ile-beta-homoTyr + H2O
beta-homoPhe + Ile-beta-homoTyr
hydrolysis at 19% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-homoPhe-p-nitroanilide + H2O
beta-homoPhe + p-nitroaniline
-
-
-
?
beta-homoPhe-p-nitroanilide + H2O
beta-homoPhe + p-nitroaniline
-
-
-
?
beta-homoSer-Ile-beta-homoTyr + H2O
beta-homoSer + Ile-beta-homoTyr
13% of the activity with beta-homoAla-beta-homoLeu
-
-
?
beta-homoSer-Ile-beta-homoTyr + H2O
beta-homoSer + Ile-beta-homoTyr
hydrolysis at 12% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-homoSer-Ile-beta-homoTyr + H2O
beta-homoSer + Ile-beta-homoTyr
3% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-homoSer-Ile-beta-homoTyr + H2O
beta-homoSer + Ile-beta-homoTyr
hydrolysis at 2.7% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-homoThr-Ile-beta-homoTyr + H2O
beta-homoThr + Ile-beta-homoTyr
1.6% of the activity with beta-homoAla-beta-homoLeu
-
-
?
beta-homoThr-Ile-beta-homoTyr + H2O
beta-homoThr + Ile-beta-homoTyr
hydrolysis at 1.6% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-homoThr-Ile-beta-homoTyr + H2O
beta-homoThr + Ile-beta-homoTyr
2% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-homoThr-Ile-beta-homoTyr + H2O
beta-homoThr + Ile-beta-homoTyr
hydrolysis at 1.9% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-homoTrp-Ile-beta-homoTyr + H2O
beta-homoTrp + Ile-beta-homoTyr
1.3% of the activity with beta-homoAla-beta-homoLeu
-
-
?
beta-homoTrp-Ile-beta-homoTyr + H2O
beta-homoTrp + Ile-beta-homoTyr
hydrolysis at 1.2% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-homoTrp-Ile-beta-homoTyr + H2O
beta-homoTrp + Ile-beta-homoTyr
1.5% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-homoTrp-Ile-beta-homoTyr + H2O
beta-homoTrp + Ile-beta-homoTyr
hydrolysis at 1.3% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-homoTyr-Ile-beta-homoTyr + H2O
beta-homoTyr + Ile-beta-homoTyr
7% of the activity with beta-homoAla-beta-homoLeu
-
-
?
beta-homoTyr-Ile-beta-homoTyr + H2O
beta-homoTyr + Ile-beta-homoTyr
hydrolysis at 7% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-homoTyr-Ile-beta-homoTyr + H2O
beta-homoTyr + Ile-beta-homoTyr
15% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-homoTyr-Ile-beta-homoTyr + H2O
beta-homoTyr + Ile-beta-homoTyr
hydrolysis at 13% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-homoVal-beta-homoAla-beta-homoLeu + H2O
beta-homoVal + beta-homoAla-beta-homoLeu
27% of the activity with beta-homoAla-beta-homoLeu
-
-
?
beta-homoVal-beta-homoAla-beta-homoLeu + H2O
beta-homoVal + beta-homoAla-beta-homoLeu
hydrolysis at 27% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-homoVal-beta-homoAla-beta-homoLeu + H2O
beta-homoVal + beta-homoAla-beta-homoLeu
-
-
-
?
beta-homoVal-beta-homoAla-beta-homoLeu + H2O
beta-homoVal + beta-homoAla-beta-homoLeu
preferred substrate
-
-
?
beta-homoVal-beta-homoAla-beta-homoLeu + H2O
beta-homoVal + beta-homoAla-beta-homoLeu
hydrolysis at 89% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-homoVal-beta-homoAla-beta-homoLeu + H2O
beta-homoVal + beta-homoAla-beta-homoLeu
-
-
-
?
beta-homoVal-beta-homoArg-beta-homoArg + H2O
beta-homoVal + beta-homoArg-beta-homoArg
hydrolysis at 0.2% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-homoVal-beta-homoArg-beta-homoArg + H2O
beta-homoVal + beta-homoArg-beta-homoArg
hydrolysis at 1.4% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-homoVal-beta-homoIle-beta-homoTyr + H2O
beta-homoVal + beta-homoIle + beta-homoTyr
completely hydrolyzed. Hydrolysis at 5% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-homoVal-beta-homoIle-beta-homoTyr + H2O
beta-homoVal + beta-homoIle + beta-homoTyr
completely hydrolyzed. Hydrolysis at 15% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
beta-homoVal-beta-homoIle-Tyr + H2O
beta-homoVal + beta-homoIle + Tyr
completely hydrolyzed. Hydrolysis at 5% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-homoVal-beta-homoIle-Tyr + H2O
beta-homoVal + beta-homoIle + Tyr
completely hydrolyzed. Hydrolysis at 20% compared to hydrolysis of beta-(3-homoVal)-Ile-Tyr
-
-
?
beta-homoVal-Ile-beta-homoTyr + H2O
beta-homoVal + Ile-beta-homoTyr
15% of the activity with beta-homoAla-beta-homoLeu
-
-
?
beta-homoVal-Ile-beta-homoTyr + H2O
beta-homoVal + Ile-beta-homoTyr
only the N-terminal beta-homoVal is released. Hydrolysis at 15% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
beta-homoVal-Ile-beta-homoTyr + H2O
beta-homoVal + Ile-beta-homoTyr
32% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
beta-homoVal-Ile-beta-homoTyr + H2O
beta-homoVal + Ile-beta-homoTyr
only the N-terminal beta-homoVal is released. Hydrolysis at 28% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
D-beta-homoVal-Ile-beta-homoTyr + H2O
D-beta-homoVal + Ile-beta-homoTyr
hydrolysis at 0.5% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
D-beta-homoVal-Ile-beta-homoTyr + H2O
D-beta-homoVal + Ile-beta-homoTyr
the rate of cleavage is slower by factor 28 as compared to the L-enantiomer. 0.5% of the activity with beta-homoAla-beta-homoLeu
-
-
?
D-beta-homoVal-Ile-beta-homoTyr + H2O
D-beta-homoVal + Ile-beta-homoTyr
hydrolysis at 0.8% compared to hydrolysis of beta-homoVal-Ile-Tyr
-
-
?
D-beta-homoVal-Ile-beta-homoTyr + H2O
D-beta-homoVal + Ile-beta-homoTyr
the rate of cleavage is slower by factor 35 as compared to the L-enantiomer. 0.9% of the activity with beta-homoVal-beta-homoAla-beta-homoLeu
-
-
?
additional information
?
-
all peptides carrying a beta-homoamino acid at the N-terminus are hydrolyzed. Tripeptides with an N-terminal alpha-amino acid are not degraded
-
-
?
additional information
?
-
in the reverse direction the enzyme catalyzes the oligomerization of beta-amino acids and the synthesis of mixed peptides with N-terminal beta-amino acid residues. As substrates the beta-homoamino acid derivatives beta-Ala-p-nitroanilide, beta-homoAla-p-nitroanilide, (R)-beta-homoAla-p-nitroanilide, beta-homoPhe-p-nitroanilide, (R)-beta-homoPhe-p-nitroanilide, and beta-homoLeu-p-nitroanilide are utilized
-
-
?
additional information
?
-
-
in the reverse direction the enzyme catalyzes the oligomerization of beta-amino acids and the synthesis of mixed peptides with N-terminal beta-amino acid residues. As substrates the beta-homoamino acid derivatives beta-Ala-p-nitroanilide, beta-homoAla-p-nitroanilide, (R)-beta-homoAla-p-nitroanilide, beta-homoPhe-p-nitroanilide, (R)-beta-homoPhe-p-nitroanilide, and beta-homoLeu-p-nitroanilide are utilized
-
-
?
additional information
?
-
the alpha-tripeptide Val-Ala-Leu and bestatin are not accepted as substrates. No degradation of DL-pyroglutamic acid-p-nitroanilide
-
-
?
additional information
?
-
all peptides carrying a beta-homoamino acid at the N-terminus are hydrolyzed. Tripeptides with an N-terminal alpha-amino acid are not degraded
-
-
?
additional information
?
-
in the reverse direction the enzyme catalyzes the oligomerization of beta-amino acids and the synthesis of mixed peptides with N-terminal beta-amino acid residues. As substrates the beta-homoamino acid derivatives beta-Ala-p-nitroanilide, beta-homoAla-p-nitroanilide, (R)-beta-homoAla-p-nitroanilide, beta-homoPhe-p-nitroanilide, (R)-beta-homoPhe-p-nitroanilide, and beta-homoLeu-p-nitroanilide are utilized
-
-
?
additional information
?
-
the alpha-tripeptide Val-Ala-Leu and bestatin are not accepted as substrates. No degradation of DL-pyroglutamic acid-p-nitroanilide
-
-
?
additional information
?
-
all peptides carrying a beta-homoamino acid at the N-terminus are hydrolyzed. Tripeptides with an N-terminal alpha-amino acid are not degraded
-
-
?
additional information
?
-
in the reverse reaction the enzyme catalyzes the oligomerization of beta-amino acids and the synthesis of mixed peptides with N-terminal beta-amino acid residues. As substrates the beta-homoamino acid derivatives beta-Ala-p-nitroanilide, beta-homoAla-p-nitroanilide, (R)-beta-homoAla-p-nitroanilide, beta-homoPhe-p-nitroanilide, (R)-beta-homoPhe-p-nitroanilide, and beta-homoLeu-p-nitroanilide are utilized
-
-
?
additional information
?
-
-
in the reverse reaction the enzyme catalyzes the oligomerization of beta-amino acids and the synthesis of mixed peptides with N-terminal beta-amino acid residues. As substrates the beta-homoamino acid derivatives beta-Ala-p-nitroanilide, beta-homoAla-p-nitroanilide, (R)-beta-homoAla-p-nitroanilide, beta-homoPhe-p-nitroanilide, (R)-beta-homoPhe-p-nitroanilide, and beta-homoLeu-p-nitroanilide are utilized
-
-
?
additional information
?
-
the alpha-tripeptide Val-Ala-Leu and bestatin are not accepted as substrates. No degradation of DL-pyroglutamyl-p-nitroanilide
-
-
?
additional information
?
-
all peptides carrying a beta-homoamino acid at the N-terminus are hydrolyzed. Tripeptides with an N-terminal alpha-amino acid are not degraded
-
-
?
additional information
?
-
in the reverse reaction the enzyme catalyzes the oligomerization of beta-amino acids and the synthesis of mixed peptides with N-terminal beta-amino acid residues. As substrates the beta-homoamino acid derivatives beta-Ala-p-nitroanilide, beta-homoAla-p-nitroanilide, (R)-beta-homoAla-p-nitroanilide, beta-homoPhe-p-nitroanilide, (R)-beta-homoPhe-p-nitroanilide, and beta-homoLeu-p-nitroanilide are utilized
-
-
?
additional information
?
-
-
in the reverse reaction the enzyme catalyzes the oligomerization of beta-amino acids and the synthesis of mixed peptides with N-terminal beta-amino acid residues. As substrates the beta-homoamino acid derivatives beta-Ala-p-nitroanilide, beta-homoAla-p-nitroanilide, (R)-beta-homoAla-p-nitroanilide, beta-homoPhe-p-nitroanilide, (R)-beta-homoPhe-p-nitroanilide, and beta-homoLeu-p-nitroanilide are utilized
-
-
?
additional information
?
-
the alpha-tripeptide Val-Ala-Leu and bestatin are not accepted as substrates. No degradation of DL-pyroglutamyl-p-nitroanilide
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
no activating effects are observed when the enzyme assay is performed in the presence of 1 mM of CaCl2, MgCl2, ZnCl2, CoCl2, FeCl2, MnCl2 or CuCl2
additional information
-
no activating effects are observed when the enzyme assay is performed in the presence of 1 mM of CaCl2, MgCl2, ZnCl2, CoCl2, FeCl2, MnCl2 or CuCl2
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Pefabloc SC
0.4 mM and 4 mM, complete inhibition of hydrolysis of beta-homoVal-beta-homoAla-beta-homoLeu
Pefabloc SC
0.4 mM and 4 mM, complete inhibition of hydrolysis of beta-homoVal-beta-homoAla-beta-homoLeu
additional information
no inhibition: EDTA (0.1 mM, 1 mM and 10 mM), leupeptin (0.01 mM, 0.1 mM and 1 mM), phenylmethanesulfonyl fluoride (1 mM and 10 mM), bestatin (0.01 mM and 0.1 mM), and 1,10-phenanthroline (1 mM and 10 mM)
-
additional information
no inhibition: EDTA (0.1 mM, 1 mM and 10 mM), leupeptin (0.01 mM, 0.1 mM and 1 mM), phenylmethanesulfonyl fluoride (1 mM and 10 mM), bestatin (0.01 mM and 0.1 mM), and 1,10-phenanthroline (1 mM and 10 mM)
-
additional information
no inhibitory effects are observed when the enzyme assay is performed in the presence of 1 mM of EDTA, CaCl2, MgCl2, ZnCl2, CoCl2, FeCl2, MnCl2, CuCl2, beta-mercaptoethanol, 1,4-dithio-DL-threitol, or phenylmethylsulfonyl fluoride
-
additional information
-
no inhibitory effects are observed when the enzyme assay is performed in the presence of 1 mM of EDTA, CaCl2, MgCl2, ZnCl2, CoCl2, FeCl2, MnCl2, CuCl2, beta-mercaptoethanol, 1,4-dithio-DL-threitol, or phenylmethylsulfonyl fluoride
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no activating effects are observed when the enzyme assay is performed in the presence of 1 mM of EDTA, beta-mercaptoethanol, 1,4-dithio-DL-threitol, or phenylmethylsulfonyl fluoride
-
additional information
-
no activating effects are observed when the enzyme assay is performed in the presence of 1 mM of EDTA, beta-mercaptoethanol, 1,4-dithio-DL-threitol, or phenylmethylsulfonyl fluoride
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9
beta-homoVal-beta-homoAla-beta-homoLeu
pH 8.0, 25°C
39
beta-homoVal-beta-homoAla-beta-homoLeu
pH 8.0, 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.3
beta-homoVal-beta-homoAla-beta-homoLeu
pH 8.0, 25°C
6
beta-homoVal-beta-homoAla-beta-homoLeu
pH 8.0, 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.11
beta-homoVal-beta-homoAla-beta-homoLeu
pH 8.0, 25°C
0.67
beta-homoVal-beta-homoAla-beta-homoLeu
pH 8.0, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.2
pH 8.0, 25°C, substrate: beta-Ala-p-nitroanilide
0.62
pH 8.0, 25°C, substrate: beta-Ala-p-nitroanilide
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
Sphingosinicella xenopeptidilytica strain 3-2W4 is able to utilize the beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu as sole carbon and energy sources
metabolism
-
Sphingosinicella xenopeptidilytica strain 3-2W4 is able to utilize the beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu as sole carbon and energy sources
-
Show AA Sequence and Transmembrane Helices (138 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
130000
13144
alpha4beta4, 4 * 13144 + 4 * 25333, calculated from sequence
13168
alpha4beta4, 4 * 13168 + 4 * 25465, MALDI-TOF MS
25333
alpha4beta4, 4 * 13144 + 4 * 25333, calculated from sequence
25465
alpha4beta4, 4 * 13168 + 4 * 25465, MALDI-TOF MS
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
octamer
octamer
alpha4beta4, 4 * 13144 + 4 * 25333, calculated from sequence
octamer
alpha4beta4, 4 * 13168 + 4 * 25465, MALDI-TOF MS
octamer
-
alpha4beta4, 4 * 13144 + 4 * 25333, calculated from sequence
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
cleavage of the Y2 BapA preprotein between the conserved residues N275 and S276
proteolytic modification
-
cleavage of the Y2 BapA preprotein between the conserved residues N275 and S276
-
proteolytic modification
the gene encodes a beta-peptidyl aminopeptidase (BapA) of 402 amino acids that is synthesized as preprotein with a signal sequence of 29 amino acids. The enzyme is cleaved into two subunits (residues 30 to 278 and 279 to 402)
proteolytic modification
-
the gene encodes a beta-peptidyl aminopeptidase (BapA) of 402 amino acids that is synthesized as preprotein with a signal sequence of 29 amino acids. The enzyme is cleaved into two subunits (residues 30 to 278 and 279 to 402)
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S237C
mutant synthesizes beta-homoGly-beta-homoGly-4-nitroanilide from beta-homoGly-4-nitroanilide efficiently without degradation, indicating that because of the mutation, the enzyme came to recognize only the amine group as an acyl acceptor instead of water. When using cysteamine as an acyl acceptor, beta-homoGly-cysteamine is synthesized by the mutant only in the reaction using S237C. Mutant S237C is unable to synthesize beta-homoGly-cystamine when using cystamine as an acyl acceptor, although it is synthesized by wild-type
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
70
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
attachment of a beta-amino acid to the N-terminus of a natural alpha-peptide. N-terminal beta-amino acid residues may be considered as protective groups against proteolytic enzymes in vitro and in vivo
synthesis
attachment of a beta-amino acid to the N-terminus of a natural alpha-peptide. N-terminal beta-amino acid residues may be considered as protective groups against proteolytic enzymes in vitro and in vivo
synthesis
BapA catalyzes reversible protein acylation at the N-terminus. The selective modification can also be applied for protein labeling and tagging and should be generally useful, also to protect peptides and proteins from attack by common aminopeptidase
synthesis
-
attachment of a beta-amino acid to the N-terminus of a natural alpha-peptide. N-terminal beta-amino acid residues may be considered as protective groups against proteolytic enzymes in vitro and in vivo
-
synthesis
-
attachment of a beta-amino acid to the N-terminus of a natural alpha-peptide. N-terminal beta-amino acid residues may be considered as protective groups against proteolytic enzymes in vitro and in vivo
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heck, T.; Limbach, M.; Geueke, B.; Zacharias, M.; Gardiner, J.; Kohler, H.P.; Seebach, D.
Enzymatic degradation of beta- and mixed alpha,beta-oligopeptides
Chem. Biodivers.
3
1325-1348
2006
Sphingosinicella microcystinivorans (A0MTQ2), Sphingosinicella xenopeptidilytica (Q52VH2), Sphingosinicella xenopeptidilytica 3-2W4 (Q52VH2), Sphingosinicella microcystinivorans Y2 (A0MTQ2)
brenda
Heck, T.; Kohler, H.P.; Limbach, M.; Flgel, O.; Seebach, D.; Geueke, B.
Enzyme-catalyzed formation of beta-peptides: beta-peptidyl aminopeptidases BapA and DmpA acting as beta-peptide-synthesizing enzymes
Chem. Biodivers.
4
2016-2030
2007
Sphingosinicella microcystinivorans (A0MTQ2), Sphingosinicella microcystinivorans, Sphingosinicella xenopeptidilytica (Q52VH2), Sphingosinicella xenopeptidilytica, Sphingosinicella xenopeptidilytica 3-2W4 (Q52VH2), Sphingosinicella xenopeptidilytica 3-2W4, Sphingosinicella microcystinivorans Y2 (A0MTQ2)
brenda
Geueke, B.; Heck, T.; Limbach, M.; Nesatyy, V.; Seebach, D.; Kohler, H.P.
Bacterial beta-peptidyl aminopeptidases with unique substrate specificities for beta-oligopeptides and mixed beta,alpha-oligopeptides
FEBS J.
273
5261-5272
2006
Sphingosinicella microcystinivorans (A0MTQ2), Sphingosinicella xenopeptidilytica (Q52VH2), Sphingosinicella xenopeptidilytica 3-2W4 (Q52VH2), Sphingosinicella microcystinivorans Y2 (A0MTQ2)
brenda
Geueke, B.; Namoto, K.; Seebach, D.; Kohler, H.P.
A novel beta-peptidyl aminopeptidase (BapA) from strain 3-2W4 cleaves peptide bonds of synthetic beta-tri- and beta-dipeptides
J. Bacteriol.
187
5910-5917
2005
Sphingosinicella xenopeptidilytica (Q52VH2), Sphingosinicella xenopeptidilytica, Sphingosinicella xenopeptidilytica 3-2W4 (Q52VH2)
brenda
Arima, J.; Tanaka, A.; Morimoto, M.; Mori, N.
Mutation of active site serine residue with cysteine displays change in acyl-acceptor preference of beta-peptidyl aminopeptidase from Pseudomonas aeruginosa PAO1
Appl. Microbiol. Biotechnol.
98
1631-1640
2014
Pseudomonas aeruginosa (Q9I3M6)
brenda
Kolesinska, B.; Wasko, J.; Kaminski, Z.; Geueke, B.; Kohler, H.; Seebach, D.
Labeling and protecting N-terminal protein positions by beta-peptidyl aminopeptidase-catalyzed attachment of beta-amino-acid residues - insulin as a first example
Helv. Chim. Acta
101
e1700259
2018
Sphingosinicella xenopeptidilytica (Q52VH2)
-
brenda
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Release 2023.1 (January 2023)
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