BRENDA - Enzyme Database show
show all sequences of 3.4.11.25

Enzyme-catalyzed formation of beta-peptides: beta-peptidyl aminopeptidases BapA and DmpA acting as beta-peptide-synthesizing enzymes

Heck, T.; Kohler, H.P.; Limbach, M.; Flgel, O.; Seebach, D.; Geueke, B.; Chem. Biodivers. 4, 2016-2030 (2007)

Data extracted from this reference:

Application
Application
Commentary
Organism
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
Sphingosinicella microcystinivorans
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
Sphingosinicella xenopeptidilytica
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sphingosinicella microcystinivorans
A0MTQ2
-
-
Sphingosinicella microcystinivorans Y2
A0MTQ2
-
-
Sphingosinicella xenopeptidilytica
Q52VH2
-
-
Sphingosinicella xenopeptidilytica 3-2W4
Q52VH2
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
708080
Sphingosinicella microcystinivorans
?
-
-
-
-
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
708080
Sphingosinicella xenopeptidilytica
?
-
-
-
-
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
708080
Sphingosinicella xenopeptidilytica 3-2W4
?
-
-
-
-
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
708080
Sphingosinicella microcystinivorans Y2
?
-
-
-
-
Application (protein specific)
Application
Commentary
Organism
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
Sphingosinicella microcystinivorans
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
Sphingosinicella xenopeptidilytica
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
708080
Sphingosinicella microcystinivorans
?
-
-
-
-
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
708080
Sphingosinicella xenopeptidilytica
?
-
-
-
-
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
708080
Sphingosinicella xenopeptidilytica 3-2W4
?
-
-
-
-
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
708080
Sphingosinicella microcystinivorans Y2
?
-
-
-
-
Other publictions for EC 3.4.11.25
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
731203
Arima
Mutation of active site serine ...
Pseudomonas aeruginosa
Appl. Microbiol. Biotechnol.
98
1631-1640
2014
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1
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1
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3
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3
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1
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2
1
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2
3
2
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1
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1
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1
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3
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3
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2
1
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2
3
2
-
1
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-
-
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-
708080
Heck
Enzyme-catalyzed formation of ...
Sphingosinicella microcystinivorans, Sphingosinicella microcystinivorans Y2, Sphingosinicella xenopeptidilytica, Sphingosinicella xenopeptidilytica 3-2W4
Chem. Biodivers.
4
2016-2030
2007
-
2
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13
-
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4
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2
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4
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708078
Heck
Enzymatic degradation of beta- ...
Sphingosinicella microcystinivorans, Sphingosinicella microcystinivorans Y2, Sphingosinicella xenopeptidilytica, Sphingosinicella xenopeptidilytica 3-2W4
Chem. Biodivers.
3
1325-1348
2006
-
-
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-
-
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6
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9
-
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2
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60
-
2
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6
2
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6
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2
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60
-
2
-
-
6
2
-
-
-
-
-
-
-
6
6
708467
Geueke
Bacterial beta-peptidyl aminop ...
Sphingosinicella microcystinivorans, Sphingosinicella microcystinivorans Y2, Sphingosinicella xenopeptidilytica, Sphingosinicella xenopeptidilytica 3-2W4
FEBS J.
273
5261-5272
2006
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-
-
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4
6
-
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8
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9
-
1
2
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-
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2
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46
1
2
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4
6
4
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4
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6
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8
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1
2
-
-
2
-
46
1
2
-
4
6
4
-
-
-
-
-
-
-
8
8
708917
Geueke
A novel beta-peptidyl aminopep ...
Sphingosinicella xenopeptidilytica, Sphingosinicella xenopeptidilytica 3-2W4
J. Bacteriol.
187
5910-5917
2005
1
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1
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1
2
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8
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1
1
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1
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4
1
1
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1
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1
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1
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1
2
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1
1
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1
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4
1
1
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1
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1
1
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