BRENDA - Enzyme Database
show all sequences of 4.3.2.5

Kinetic and inhibition studies on substrate channelling in the bifunctional enzyme catalysing C-terminal amidation

Moore, A.B.; May, S.W.; Biochem. J. 341, 33-40 (1999)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in cultured Sf9 insect cells
Xenopus laevis
Inhibitors
Inhibitors
Commentary
Organism
Structure
acetylmethionyl pyruvate
competitive inhibition of PGL domain of full expressed enzyme: AE and monofunctional lyase: PGL
Xenopus laevis
acetylphenylalanyl pyruvate
competitive inhibition of PGL domain of full expressed enzyme: AE and monofunctional lyase: PGL
Xenopus laevis
acetyltyrosyl pyruvate
competitive inhibition of PGL domain of full expressed enzyme: AE and monofunctional lyase: PGL
Xenopus laevis
additional information
-
Bos taurus
additional information
the inhibitors of PAM: acetyl-L-Phe-acetic acid and [(4-methoxybenzoyl)oxy]acetic acid show no effect of the KM of the monofunctional lyase: PGL
Xenopus laevis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.014
-
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
37°C, pH 6.6, PGL domain of transmembrane truncated enzyme: dAE
Xenopus laevis
0.018
-
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
37°C, pH 6.6, PGL domain of full expressed enzyme: AE
Xenopus laevis
0.019
-
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
37°C, pH 6.6, monofunctional lyase: PGL
Xenopus laevis
0.033
-
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
37°C, pH 6.6
Bos taurus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bos taurus
-
-
-
Xenopus laevis
-
-
-
Purification (Commentary)
Commentary
Organism
-
Xenopus laevis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
23000
-
PGL domain of full expressed enzyme: AE
Xenopus laevis
76000
-
PGL domain of transmembrane truncated enzyme: dAE
Xenopus laevis
180000
-
monofunctional lyase: PGL
Xenopus laevis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
-
648705
Bos taurus
trinitrophenyl-D-Tyr-L-Val-NH2 + glyoxylate
-
-
-
?
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
-
648705
Xenopus laevis
trinitrophenyl-D-Tyr-L-Val-NH2 + glyoxylate
-
-
-
?
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.049
-
acetylphenylalanyl pyruvate
37°C, pH 6.6, monofunctional lyase: PGL
Xenopus laevis
0.071
-
acetylphenylalanyl pyruvate
37°C, pH 6.6, PGL domain of full expressed enzyme: AE
Xenopus laevis
0.55
-
acetyltyrosyl pyruvate
37°C, pH 6.6, monofunctional lyase: PGL
Xenopus laevis
0.92
-
acetyltyrosyl pyruvate
37°C, pH 6.6, PGL domain of full expressed enzyme: AE
Xenopus laevis
3.2
-
acetylmethionyl pyruvate
37°C, pH 6.6, monofunctional lyase: PGL
Xenopus laevis
4.8
-
acetylmethionyl pyruvate
37°C, pH 6.6, PGL domain of full expressed enzyme: AE
Xenopus laevis
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in cultured Sf9 insect cells
Xenopus laevis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
acetylmethionyl pyruvate
competitive inhibition of PGL domain of full expressed enzyme: AE and monofunctional lyase: PGL
Xenopus laevis
acetylphenylalanyl pyruvate
competitive inhibition of PGL domain of full expressed enzyme: AE and monofunctional lyase: PGL
Xenopus laevis
acetyltyrosyl pyruvate
competitive inhibition of PGL domain of full expressed enzyme: AE and monofunctional lyase: PGL
Xenopus laevis
additional information
-
Bos taurus
additional information
the inhibitors of PAM: acetyl-L-Phe-acetic acid and [(4-methoxybenzoyl)oxy]acetic acid show no effect of the KM of the monofunctional lyase: PGL
Xenopus laevis
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.049
-
acetylphenylalanyl pyruvate
37°C, pH 6.6, monofunctional lyase: PGL
Xenopus laevis
0.071
-
acetylphenylalanyl pyruvate
37°C, pH 6.6, PGL domain of full expressed enzyme: AE
Xenopus laevis
0.55
-
acetyltyrosyl pyruvate
37°C, pH 6.6, monofunctional lyase: PGL
Xenopus laevis
0.92
-
acetyltyrosyl pyruvate
37°C, pH 6.6, PGL domain of full expressed enzyme: AE
Xenopus laevis
3.2
-
acetylmethionyl pyruvate
37°C, pH 6.6, monofunctional lyase: PGL
Xenopus laevis
4.8
-
acetylmethionyl pyruvate
37°C, pH 6.6, PGL domain of full expressed enzyme: AE
Xenopus laevis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.014
-
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
37°C, pH 6.6, PGL domain of transmembrane truncated enzyme: dAE
Xenopus laevis
0.018
-
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
37°C, pH 6.6, PGL domain of full expressed enzyme: AE
Xenopus laevis
0.019
-
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
37°C, pH 6.6, monofunctional lyase: PGL
Xenopus laevis
0.033
-
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
37°C, pH 6.6
Bos taurus
Purification (Commentary) (protein specific)
Commentary
Organism
-
Xenopus laevis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
23000
-
PGL domain of full expressed enzyme: AE
Xenopus laevis
76000
-
PGL domain of transmembrane truncated enzyme: dAE
Xenopus laevis
180000
-
monofunctional lyase: PGL
Xenopus laevis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
-
648705
Bos taurus
trinitrophenyl-D-Tyr-L-Val-NH2 + glyoxylate
-
-
-
?
trinitrophenyl-D-Tyr-L-Val-alpha-hydroxy-Gly
-
648705
Xenopus laevis
trinitrophenyl-D-Tyr-L-Val-NH2 + glyoxylate
-
-
-
?
Other publictions for EC 4.3.2.5
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)
730684
Yin
Probing the production of amid ...
Mus musculus, Mus musculus C57/BL6J
PLoS ONE
6
e28679
2011
-
-
-
-
-
-
-
-
-
-
-
4
-
61
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
691012
Takahashi
Involvement of metals in enzym ...
Homo sapiens
Biochemistry
48
1654-1662
2009
-
-
-
-
-
-
-
3
-
7
-
1
-
1
-
-
-
-
-
-
1
-
1
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
7
-
1
-
-
-
-
-
-
1
-
1
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
664714
Park
Ap-let neurons-a peptidergic c ...
Drosophila melanogaster
Dev. Biol.
269
95-108
2004
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
3
-
-
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-
-
-
-
-
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-
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-
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-
-
-
-
-
-
-
3
-
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-
-
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-
-
-
-
-
-
-
-
-
-
-
666112
Han
Drosophila uses two distinct n ...
Drosophila melanogaster, Rattus norvegicus
J. Neurochem.
90
129-141
2004
4
-
2
-
-
-
1
3
3
4
4
3
-
3
-
-
2
-
-
3
-
-
6
1
-
-
-
-
2
-
-
-
-
-
-
6
-
2
-
-
-
-
-
2
-
3
4
6
4
3
-
-
-
2
-
5
-
-
6
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
648703
Satani
Expression and characterizatio ...
Homo sapiens
Protein Expr. Purif.
28
293-302
2003
-
-
1
-
-
-
2
-
1
-
-
-
-
3
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
648704
Kolhekar
Essential features of the cata ...
Rattus norvegicus
Biochemistry
41
12384-12394
2002
-
-
1
-
12
-
6
7
1
1
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
1
-
-
12
-
-
6
-
7
1
1
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
648706
Garmendia
Immunocytochemical finding of ...
Homo sapiens, Mus musculus, Rattus norvegicus
J. Histochem. Cytochem.
50
1401-1415
2002
-
-
-
-
-
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3
-
-
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-
-
3
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-
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3
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
648705
Moore
Kinetic and inhibition studies ...
Bos taurus, Xenopus laevis
Biochem. J.
341
33-40
1999
-
-
1
-
-
-
5
4
-
-
-
-
-
3
-
-
1
-
-
-
3
-
2
-
-
-
-
-
-
-
-
-
6
-
-
-
-
1
-
-
-
-
-
5
6
4
-
-
-
-
-
-
-
1
-
-
3
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
438594
Francisco
Kinetic mechanism and intrinsi ...
Rattus norvegicus
Biochemistry
37
8244-8252
1998
-
-
1
-
-
-
-
-
-
-
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1
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-
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-
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-
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-
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1
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-
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-
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-
438592
Ping
Reaction versus subsite stereo ...
Bos taurus
J. Biol. Chem.
270
29250-29255
1995
-
-
-
-
-
-
3
8
-
-
-
-
-
1
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-
1
-
-
1
-
-
8
-
-
-
-
-
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-
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3
-
-
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-
-
-
-
-
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3
3
8
-
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-
-
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-
-
1
-
1
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
648693
Husten
Use of endoproteases to identi ...
Bos taurus, Rattus norvegicus
J. Biol. Chem.
268
9709-9717
1993
-
-
1
-
-
-
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2
1
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-
-
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2
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1
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-
4
-
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-
-
2
-
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-
-
1
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-
-
-
-
-
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2
1
-
-
-
-
-
-
1
-
-
-
-
4
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
648694
Ping
-
Tandem stereochemistry of pept ...
Bos taurus
J. Am. Chem. Soc.
114
3998-4000
1992
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-
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1
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1
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1
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2
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-
-
-
438571
Merkler
Recombinant type A rat 75-kDa ...
Rattus norvegicus
Arch. Biochem. Biophys.
289
192-196
1991
-
-
1
-
-
-
-
2
2
-
1
-
-
1
-
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-
-
-
1
2
-
1
-
1
-
-
-
-
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-
1
-
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-
-
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-
-
2
2
-
1
-
-
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-
-
1
2
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
648692
Katopodis
Functional and structural char ...
Bos taurus
Biochemistry
30
6189-6194
1991
-
-
1
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-
-
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-
1
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-
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1
-
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1
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1
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1
1
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1
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1
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1
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1
-
1
1
-
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-
-
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-
-
-
-
-
-
-
-
-
648695
Husten
The membrane-bound bifunctiona ...
Rattus norvegicus
J. Biol. Chem.
266
17004-17010
1991
-
-
-
-
-
-
-
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1
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1
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1
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1
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1
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1
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1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
648697
Eipper
Peptidyl-alpha-hydroxyglycine ...
Bos taurus
J. Biol. Chem.
266
7827-7833
1991
-
-
-
-
-
-
5
1
-
-
1
-
-
1
-
-
1
-
-
2
-
-
1
-
-
-
-
1
1
-
-
-
-
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-
-
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-
-
-
-
-
-
5
-
1
-
-
1
-
-
-
-
1
-
2
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
438567
Perkins
The 108-kDA peptidylglycine al ...
Bos taurus
Biochem. Biophys. Res. Commun.
171
926-932
1990
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
438569
Suzuki
Elucidation of amidating react ...
Xenopus laevis
EMBO J.
9
4259-4265
1990
-
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1
-
-
-
-
-
-
-
-
-
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1
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-
-
-
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1
-
1
-
-
-
-
-
-
-
-
-
-
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-
-
-
1
-
-
-
-
-
-
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-
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-
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-
1
-
1
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
648691
Katopodis
A novel enzyme from bovine neu ...
Bos taurus
Biochemistry
29
6115-6120
1990
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
1
2
-
2
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
1
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648700
Takahashi
Peptidylglycine alpha-amidatin ...
Bos taurus, Rattus norvegicus
Biochem. Biophys. Res. Commun.
169
524-530
1990
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648701
Kato
Two enzymes concerned in pepti ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
172
197-203
1990
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