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Information on EC 2.3.2.6 - lysine/arginine leucyltransferase
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EC Tree
2.3.2.6 lysine/arginine leucyltransferaseIUBMB Comments
Requires a univalent cation. The enzyme participates in the N-end rule protein degradation pathway in certain bacteria, by attaching the primary destabilizing residue L-leucine to the N-termini of proteins that have an N-terminal L-arginine or L-lysine residue. Once modified, the proteins are recognized by EC 3.4.21.92, the ClpAP/ClpS endopeptidase system. The enzyme also transfers L-phenylalanine in vitro, but this has not been observed in vivo . cf. EC 2.3.2.29, aspartate/glutamate leucyltransferase, and EC 2.3.2.8, arginyltransferase.
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Word Map
- 2.3.2.6
- aminoacyl-trnas
- diphtheria
- toxin
- aa
-
eubacterial
-
ribosylation
-
n-termini
- peptidoglycan
-
trna-dependent
-
cycloaddition
-
non-ribosomal
- puromycin
-
n-degrons
-
alkyne
-
transferase-mediated
-
toxin-dependent
- leu-trnaleu
- synthesis
- analysis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
+
N-terminal L-lysyl-[protein]
=
+
N-terminal L-leucyl-L-lysyl-[protein]
+
N-terminal L-arginyl-[protein]
=
+
N-terminal L-leucyl-L-arginyl-[protein]
Synonyms
l/f-transferase, l/f transferase, leucyl/phenylalanyl-trna-protein transferase, aminoacyl transferase, lf-transferase, leucyl/phenylalanyl-trna protein transferase, l/f-trna-protein transferase, leucyltransferase, leucyl/phenylalanyl trna protein transferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L/F transferase
L/F-transferase
leucyl, phenylalanine-tRNA-protein transferase
-
-
-
-
leucyl, phenylalanyl transfer ribonucleic acid-protein transferase
-
-
-
-
leucyl-phenylalanine-transfer ribonucleate-protein aminoacyltransferase
-
-
-
-
leucyl-phenylalanine-transfer ribonucleate-protein transferase
-
-
-
-
leucyl/phenylalanyl tRNA protein transferase
leucyl/phenylalanyl-tRNA protein transferase
leucyl/phenylalanyl-tRNA-protein transferase
L/F-transferase
-
-
-
-
leucyl/phenylalanyl-tRNA-protein transferase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-leucyl-tRNALeu + N-terminal L-arginyl-[protein] = tRNALeu + N-terminal L-leucyl-L-arginyl-[protein]
(2)
-
-
-
L-leucyl-tRNALeu + N-terminal L-lysyl-[protein] = tRNALeu + N-terminal L-leucyl-L-lysyl-[protein]
L-leucyl-tRNALeu + N-terminal L-lysyl-[protein] = tRNALeu + N-terminal L-leucyl-L-lysyl-[protein]
the electron relay from Asp 186 to Gln 188 helps Gln 188 to attract a proton from the a-amino group of the N-terminal Arg of the acceptor peptide. This generates the attacking nucleophile for the carbonyl carbon of the aminoacyl bond of the aminoacyl-tRNA, thus facilitating peptide-bond formation
L-leucyl-tRNALeu + N-terminal L-lysyl-[protein] = tRNALeu + N-terminal L-leucyl-L-lysyl-[protein]
(1)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aminoacyl group transfer
aminoacyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-leucyl-tRNALeu:[protein] N-terminal L-lysine/L-arginine leucyltransferase
Requires a univalent cation. The enzyme participates in the N-end rule protein degradation pathway in certain bacteria, by attaching the primary destabilizing residue L-leucine to the N-termini of proteins that have an N-terminal L-arginine or L-lysine residue. Once modified, the proteins are recognized by EC 3.4.21.92, the ClpAP/ClpS endopeptidase system. The enzyme also transfers L-phenylalanine in vitro, but this has not been observed in vivo [5]. cf. EC 2.3.2.29, aspartate/glutamate leucyltransferase, and EC 2.3.2.8, arginyltransferase.
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CAS REGISTRY NUMBER
COMMENTARY
37257-22-0
-
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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
1-naphthylalanyl-tRNA + L-Lys-SoCBM13
1-naphthylalanyl-L-Lys-SoCBM13 + tRNA
-
a xylan binding domain with N-terminal Lys. Introduction of 1-naphthylalanine is more difficult than of 2-naphthylalanine
-
-
?
2-naphthylalanyl-tRNA + L-Lys-SoCBM13
2-naphthylalanyl-L-Lys-SoCBM13 + tRNA
-
a xylan binding domain with N-terminal Lys. Introduction of 1-naphthylalanine is more difficult than of 2-naphthylalanine
-
-
?
3-nitrotyrosyl-tRNA + L-Arg-casein
3-nitrotyrosyl-L-Arg-casein + tRNA
-
-
-
-
?
3-nitrotyrosyl-tRNA + L-Lys-glutathione S-transferase
3-nitrotyrosyl-L-Lys-glutathione S-transferase + tRNA
-
-
-
-
?
3-nitrotyrosyl-tRNA + L-Lys-SoCBM13
3-nitrotyrosyl-L-Lys-SoCBM13 + tRNA
-
a xylan binding domain with N-terminal Lys
-
-
?
L-leucyl-tRNALeu + N-terminal L-arginyl-[protein]
tRNALeu + N-terminal L-leucyl-L-arginyl-[protein]
-
-
-
?
L-leucyl-tRNALeu + N-terminal L-lysyl-[protein]
tRNALeu + N-terminal L-leucyl-L-lysyl-[protein]
-
-
-
?
L-leucyl-tRNALeu + putrescine aminotransferase
tRNALeu + L-leucyl-[putrescine aminotransferase]
-
posttranslationally modification of PATase to generate a primary N-degron
-
-
?
L-phenylalanyl-tRNA + KAC-acrydonylalanine
tRNA + L-phenylalanyl-KAC-acrydonylalanine
-
-
-
-
?
L-phenylalanyl-tRNA + KPC-acrydonylalanine
tRNA + L-phenylalanyl-KPC-acrydonylalanine
-
-
-
-
?
L-phenylalanyl-tRNA + KQC-acrydonylalanine
tRNA + L-phenylalanyl-KQC-acrydonylalanine
-
-
-
-
?
L-phenylalanyl-tRNA + putrescine aminotransferase
tRNA + L-phenylalanyl-putrescine aminotransferase
-
posttranslationally modification of PATase to generate a primary N-degron
-
-
?
L-phenylalanyl-tRNA + REPGLCTWQSLR
tRNA + FREPGLCTWQSLR
-
substrate peptide
-
-
?
L-phenylalanyl-tRNA(Leu) + L-arginyl-peptide
tRNA(Leu) + L-phenylalanyl-L-arginyl-protein
-
-
-
?
L-phenylalanyl-tRNA(Phe) + L-arginyl-peptide
tRNA(Phe) + L-phenylalanyl-L-arginyl-protein
-
-
-
?
L-phenylalanyl-tRNAPhe + N-terminal L-arginyl-[protein]
tRNAPhe + N-terminal L-phenylalanyl-L-arginyl-[protein]
-
-
-
?
L-phenylalanyl-tRNAPhe + N-terminal L-leucyl-[protein]
tRNAPhe + N-terminal L-phenylalanyl-L-leucyl-[protein]
-
-
-
?
L-phenylalanyl-tRNAPhe + N-terminal L-lysyl-[protein]
tRNAPhe + N-terminal L-phenylalanyl-L-lysyl-[protein]
-
-
-
?
L-phenylalanyl-tRNAPhe + protein
tRNAPhe + L-phenylalanyl-[protein]
-
-
-
-
?
L-Trp-tRNATrp + acceptor protein
tRNATrp + L-Trp-[acceptor protein]
-
-
-
-
?
O-(2-fluoroethyl)- L-tyrosyl-tRNA + acceptor protein
tRNA + O-(2-fluoroethyl)-L-tyrosyl-protein
-
-
-
-
?
O-(2-fluoromethyl)-L-tyrosinyl-tRNA + N-terminal L-leucyl-[protein]
tRNA + N-terminal O-(2-fluoromethyl)-L-tyrosinyl-L-leucyl-[protein]
-
-
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
acceptor protein: bovine serum albumin
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
acceptor protein: bovine serum albumin
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
acceptor protein: alphaS1-casein
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
incorporation of Leu into the peptide linkage with the amino-terminal aspartic acid of albumin
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
all peptides containing a NH2-terminal L-Arg or Lys residue function as acceptor, however D-Arg-D-Val is inactive
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
the association of the Leu-tRNA-enzyme complex is diffusion controlled
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
acceptors with arginine or lysine as initial NH2-terminal residue
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
basic NH2-terminal is absolute determinant of specificity
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
basic NH2-terminal is absolute determinant of specificity
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
dipeptide specificity
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
the major portion of L-Leu incorporation is an addition of amino acid to the NH2 group of a preformed acceptor or to a Lys NH2 group in the internal linkage, The NH2 group addition involving ribosomes is dependent on aminoacyl S-RNA, soluble enzymes, and the acceptor substance on ribosomes
-
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
the major portion of L-Leu incorporation is an addition of amino acid to the NH2 group of a preformed acceptor or to a Lys NH2 group in the internal linkage. The NH2 group addition involving ribosomes is dependent on aminoacyl S-RNA, soluble enzymes, and the acceptor substance on ribosomes
-
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
Escherichia coli B / ATCC 11303
-
acceptor protein: bovine serum albumin
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
Escherichia coli B / ATCC 11303
-
acceptor protein: bovine serum albumin
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
Escherichia coli B / ATCC 11303
-
incorporation of Leu into the peptide linkage with the amino-terminal aspartic acid of albumin
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
Escherichia coli B / ATCC 11303
-
acceptor protein: alphaS1-casein
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
Escherichia coli B / ATCC 11303
-
all peptides containing a NH2-terminal L-Arg or Lys residue function as acceptor, however D-Arg-D-Val is inactive
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
Escherichia coli B / ATCC 11303
-
basic NH2-terminal is absolute determinant of specificity
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
Escherichia coli B / ATCC 11303
-
basic NH2-terminal is absolute determinant of specificity
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
Escherichia coli B / ATCC 11303
-
dipeptide specificity
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-[protein]
-
strongly preferred substrate
-
-
?
L-methionyl-tRNA + acceptor protein
tRNA + L-methionyl-protein
-
-
-
-
?
L-methionyl-tRNA + acceptor protein
tRNA + L-methionyl-protein
-
wild-type Met-tRNAMetm (CAU anticodon) and mischarged Met-tRNAVal-1 (CAU anticodon) are substrates for LF-transferase during the NH2-terminal aminoacylation of alpha-casein
-
-
?
L-methionyl-tRNA + acceptor protein
tRNA + L-methionyl-protein
-
methionyl-tRNAmMet preferred to methionyl-tRNAfMet. Peptides containing a basic amino acid at the NH2-terminus function as acceptors
-
-
?
L-methionyl-tRNA + acceptor protein
tRNA + L-methionyl-protein
Escherichia coli B / ATCC 11303
-
methionyl-tRNAmMet preferred to methionyl-tRNAfMet. Peptides containing a basic amino acid at the NH2-terminus function as acceptors
-
-
?
L-phenylalanyl + acceptor protein
tRNA + L-phenylalanyl-protein
-
the major portion of L-Phe incorporation is an addition of amino acid to the NH2 group of a preformed acceptor or to a Lys NH2 group in the internal linkage. The NH2 group addition involving ribosomes is dependent on aminoacyl S-RNA, soluble enzymes, and the acceptor substance on ribosomes
-
-
?
L-phenylalanyl-tRNA + acceptor protein
tRNA + L-phenylalanyl-protein
-
-
-
-
?
L-phenylalanyl-tRNA + acceptor protein
tRNA + L-phenylalanyl-protein
-
incorporation of Phe into the peptide linkage with the amino-terminal aspartic acid of albumin
-
-
?
L-phenylalanyl-tRNA + acceptor protein
tRNA + L-phenylalanyl-protein
Escherichia coli B / ATCC 11303
-
-
-
-
?
L-phenylalanyl-tRNA + acceptor protein
tRNA + L-phenylalanyl-protein
Escherichia coli B / ATCC 11303
-
incorporation of Phe into the peptide linkage with the amino-terminal aspartic acid of albumin
-
-
?
L-phenylalanyl-tRNA + acceptor protein
tRNA + L-phenylalanyl-protein
Escherichia coli B / ATCC 11303
-
-
-
-
?
additional information
?
-
-
substrate recognition. Vatiants of the enzyme, lacking either 33 or 78 N-terminal residues, retain measurable peptidyltransferase activity and wild type substrate specificity
-
-
?
additional information
?
-
-
no activity with Val-tRNAVal-1 (UAC anticodon), Val-tRNAMetm (UAC anticodon), and Arg-tRNAMetm
-
-
?
additional information
?
-
-
L-methionyl-tRNAMet is a very poor substrate
-
-
?
additional information
?
-
in vivo, the dominating modification is leucylation of the N-terminus of the substrate protein
-
-
-
additional information
?
-
-
in vivo, the dominating modification is leucylation of the N-terminus of the substrate protein
-
-
-
additional information
?
-
in vitro, the L/F transferase catalyzes the transfer of Leu or Phe (1° destabilizing) or Met (2° destabilizing) from an aminoacyl-tRNA to the N-terminus of a substrate protein bearing an N-terminal Arg or Lys (2° destabilizing) or Met (1° destabilizing) residue, substrate recognition and proposed mechanism for the generation of N-end rule substrates, structure-function relationship, overview. Design of an improved aminoacyl-tRNA substrate analogue
-
-
-
additional information
?
-
-
in vitro, the L/F transferase catalyzes the transfer of Leu or Phe (1° destabilizing) or Met (2° destabilizing) from an aminoacyl-tRNA to the N-terminus of a substrate protein bearing an N-terminal Arg or Lys (2° destabilizing) or Met (1° destabilizing) residue, substrate recognition and proposed mechanism for the generation of N-end rule substrates, structure-function relationship, overview. Design of an improved aminoacyl-tRNA substrate analogue
-
-
-
additional information
?
-
various non-natural amino acids as artificial substrates can be enzymatically introduced only at the basic N-terminus of any kind of acceptor peptides/proteins by using Escherichia coli leucyl/phenylalanyl-tRNA-protein transferase (L/F-transferase) without any engineering of its catalytic pocket. Extension of this L/F-transferase-mediated functionalization of peptides/proteins in combination with aminoacyl-tRNA synthetase (ARS) mutant. Fast enzymatic introduction of a positron emission tomography (PET) probe into acceptor peptides/proteins, it is site-specifically introduced at the basic N-terminus of the acceptors by using L/F-transferase in combination with aminoacyl-tRNA synthetase, namely the NEXT-A/PET reaction. Estimated from kinetic analysis, the transfer efficiency of O-(2-fluoromethyl)-L-tyrosine as an artificial amino acid PET probe mediated by the wild-type transferase is almost as good as that of the natural substrate, phenylalanine. About 90 % of Lys-Ala-7-amino-4-methylcoumarin peptide or of Lys-bradykinin peptide are labeled by O-(2-fluoromethyl)-L-tyrosine (FMT), the model protein Lys-SoCBM13 is also labeled by FMT
-
-
-
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NATURAL SUBSTRATE
NATURAL 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
L-leucyl-tRNALeu + N-terminal L-arginyl-[protein]
tRNALeu + N-terminal L-leucyl-L-arginyl-[protein]
-
-
-
?
L-leucyl-tRNALeu + N-terminal L-lysyl-[protein]
tRNALeu + N-terminal L-leucyl-L-lysyl-[protein]
-
-
-
?
L-phenylalanyl-tRNA(Leu) + L-arginyl-peptide
tRNA(Leu) + L-phenylalanyl-L-arginyl-protein
-
-
-
?
L-phenylalanyl-tRNA(Phe) + L-arginyl-peptide
tRNA(Phe) + L-phenylalanyl-L-arginyl-protein
-
-
-
?
L-phenylalanyl-tRNAPhe + protein
tRNAPhe + L-phenylalanyl-[protein]
-
-
-
-
?
additional information
?
-
in vivo, the dominating modification is leucylation of the N-terminus of the substrate protein
-
-
-
additional information
?
-
-
in vivo, the dominating modification is leucylation of the N-terminus of the substrate protein
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
NH4+
-
monovalent cation required, stimulation of Leu transfer is somewhat greater than that of Phe
K+
-
monovalent cation required, stimulation of Leu transfer is somewhat greater than that of Phe
K+
-
monovalent cation required, maximal activity is 0.15 M KCl for the transfer of Phe and 0.2 M for the transfer of Leu
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
puromycin
-
aminonucleoside derivative, which lacks the aminoacyl analogus structure, fails to inhibit the reaction
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Diphtheria
A proposed mechanism for ADP ribosylation of aminoacyl transferase II by diphtheria toxin.
Diphtheria
Adenosine diphosphate ribosylation of aminoacyl transferase II and inhibition of protein synthesis by diphtheria toxin.
Diphtheria
Diphtheria toxin-dependent adenosine diphosphate ribosylation of aminoacyl transferase II and inhibition of protein synthesis.
Diphtheria
Diphtheria toxin: requirement for active protein synthesis for inactivation of aminoacyl transferase II in the intact mammalian cell.
Diphtheria
Interaction of aminoacyl transferase II and guanosine triphosphate: inhibition by diphtheria toxin and nicotinamide adenine dinucleotide.
Diphtheria
Studies on diphtheria toxin. The effect of GTP on the toxin-dependent adenosine diphosphate ribosylation of rat liver aminoacyl transferase. II.
Diphtheria
The diphtheria toxin-dependent adenosine diphosphate ribosylation of rat liver aminoacyl transferase. II. General characteristics and mechanism of the reaction.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetic analysis of L/F-transferase
-
2.2
REPGLCTWQSLR
-
amino acid residue on the aminoacyl-tRNA(Phe) transferred to the peptide substrate, 4-azido phenylalanine, Km apparent
3.2
REPGLCTWQSLR
-
amino acid residue on the aminoacyl-tRNA(Phe) transferred to the peptide substrate, phenylalanine, Km apparent
4.3
REPGLCTWQSLR
-
amino acid residue on the aminoacyl-tRNA(Phe) transferred to the peptide substrate, 4-bromo phenylalanine, Km apparent
18
REPGLCTWQSLR
-
amino acid residue on the aminoacyl-tRNA(Phe) transferred to the peptide substrate, 4-acetyl-N-(tert-butoxycarbonyl)-L-phenylalanine, Km apparent
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00183
REPGLCTWQSLR
-
amino acid residue on the aminoacyl-tRNA(Phe) transferred to the peptide substrate, 4-azido phenylalanine, Kcat apparent
0.00283
REPGLCTWQSLR
-
amino acid residue on the aminoacyl-tRNA(Phe) transferred to the peptide substrate, 4-acetyl-N-(tert-butoxycarbonyl)-L-phenylalanine, Kcat apparent
0.00333
REPGLCTWQSLR
-
amino acid residue on the aminoacyl-tRNA(Phe) transferred to the peptide substrate, 4-bromo phenylalanine, Kcat apparent
0.00367
REPGLCTWQSLR
-
amino acid residue on the aminoacyl-tRNA(Phe) transferred to the peptide substrate, phenylalanine, Kcat apparent
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5
Arginine methyl ester
-
inhibition of reaction with alphaS1-casein as acceptor
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM