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Information on EC 3.4.11.25 - beta-peptidyl aminopeptidase and Organism(s) Sphingosinicella microcystinivorans and UniProt Accession A0MTQ2
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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 taxonomic range for the selected organisms is: Sphingosinicella microcystinivorans
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
completely degraded to the corresponding beta-homoamino acids within 312 h
-
-
?
beta-Ala-p-nitroanilide + H2O
beta-Ala + p-nitroaniline
-
-
-
?
beta-homoAla-beta-homoLeu + H2O
beta-homoAla + beta-homoLeu
preferred substrate
-
-
?
beta-homoAla-p-nitroanilide + H2O
beta-homoAla + p-nitroaniline
-
-
-
?
beta-homoPhe-p-nitroanilide + H2O
beta-homoPhe + p-nitroaniline
-
-
-
?
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-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-Tyr + H2O
beta-homoVal + beta-homoIle + Tyr
completely hydrolyzed. Hydrolysis at 5% compared to hydrolysis of beta-homoAla-beta-homoLeu
-
-
?
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
-
-
?
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-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-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-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-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-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-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-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-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-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-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-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-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-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
-
-
?
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
-
-
?
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
-
-
?
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
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)
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
39
beta-homoVal-beta-homoAla-beta-homoLeu
pH 8.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.3
beta-homoVal-beta-homoAla-beta-homoLeu
pH 8.0, 25°C
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.2
pH 8.0, 25°C, substrate: beta-Ala-p-nitroanilide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
octamer
octamer
alpha4beta4, 4 * 13144 + 4 * 25333, calculated from sequence
octamer
alpha4beta4, 4 * 13168 + 4 * 25465, MALDI-TOF MS
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
cleavage of the Y2 BapA preprotein between the conserved residues N275 and S276
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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 microcystinivorans Y2 (A0MTQ2), Sphingosinicella xenopeptidilytica (Q52VH2), Sphingosinicella xenopeptidilytica 3-2W4 (Q52VH2)
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 microcystinivorans Y2 (A0MTQ2), Sphingosinicella xenopeptidilytica (Q52VH2), Sphingosinicella xenopeptidilytica, Sphingosinicella xenopeptidilytica 3-2W4 (Q52VH2), Sphingosinicella xenopeptidilytica 3-2W4
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 microcystinivorans Y2 (A0MTQ2), Sphingosinicella xenopeptidilytica (Q52VH2), Sphingosinicella xenopeptidilytica 3-2W4 (Q52VH2)
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