Information on EC 2.3.1.118 - N-hydroxyarylamine O-acetyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
2.3.1.118
-
RECOMMENDED NAME
GeneOntology No.
N-hydroxyarylamine O-acetyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
acetyl-CoA + an N-hydroxyarylamine = CoA + an N-acetoxyarylamine
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:N-hydroxyarylamine O-acetyltransferase
The enzyme from liver, but not that from bacteria, can also catalyse N-acetylation of arylamines and N,O-acetylation of arylhydroxamates.
CAS REGISTRY NUMBER
COMMENTARY hide
100984-92-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain C57BL/67
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Manually annotated by BRENDA team
strain C57BL/67
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Manually annotated by BRENDA team
Sprague-Dawley strain
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Manually annotated by BRENDA team
Sprague-Dawley strain
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + 2-aminofluorene
CoA + 2-acetyloxyaminofluorene
show the reaction diagram
-
N-acetyltransferase activity
-
?
acetyl-CoA + 2-aminofluorene
CoA + N-acetyl-2-aminofluorene
show the reaction diagram
-
-
-
-
?
acetyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-acetoxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
show the reaction diagram
acetyl-CoA + 3-hydroxyamino-1-methyl-pyrido[4,3-b]-indole
CoA + N-acetoxy-amino-1-methyl-pyrido[4,3-b]-indole
show the reaction diagram
acetyl-CoA + 4-aminoveratrole
CoA + N-acetyl-4-aminoveratrole
show the reaction diagram
acetyl-CoA + 4-anisidine
CoA + N-acetyl-4-anisidine
show the reaction diagram
acetyl-CoA + 4-iodoaniline
CoA + N-acetyl-4-iodoaniline
show the reaction diagram
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
show the reaction diagram
acetyl-CoA + aniline
CoA + N-acetylaniline
show the reaction diagram
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N-acetyltransferase activity, ping-pong bi bi mechanism
-
?
acetyl-CoA + isoniazid
CoA + N-acetyl-isoniazid
show the reaction diagram
-
N-acetyltransferase activity, ping-pong bi bi mechanism
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?
acetyl-CoA + m-aminophenol
CoA + N-acetyl-m-aminophenol
show the reaction diagram
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N-acetyltransferase activity, ping-pong bi bi mechanism
-
?
acetyl-CoA + N-hydroxy-2-aminofluorene
CoA + N-acetoxyaminofluorene
show the reaction diagram
acetyl-CoA + N-hydroxy-2-aminofluorene
CoA + N-acetylxy-2-aminofluorene
show the reaction diagram
acetyl-CoA + N-hydroxy-3,2'-dimethyl-4-aminobiphenyl
CoA + N-acetoxy-3,2'-dimethyl-4-aminobiphenyl
show the reaction diagram
-
-
-
?
acetyl-CoA + N-hydroxy-4-aminobiphenyl
CoA + N-acetoxyaminobiphenyl
show the reaction diagram
acetyl-CoA + o-aminobenzoic acid
CoA + N-acetyl-o-aminobenzoic acid
show the reaction diagram
acetyl-CoA + o-aminophenol
CoA + N-acetyl-o-aminophenol
show the reaction diagram
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N-acetyltransferase activity, ping-pong bi bi mechanism
-
?
acetyl-CoA + o-anisidine
CoA + N-acetyl-o-anisidine
show the reaction diagram
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N-acetyltransferase activity, ping-pong bi bi mechanism
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?
acetyl-CoA + p-aminobenzoic acid
CoA + N-acetyl-p-aminobenzoic acid
show the reaction diagram
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N-acetyltransferase activity, ping-pong bi bi mechanism
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?
acetyl-CoA + p-aminophenol
CoA + N-acetyl-p-aminophenol
show the reaction diagram
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N-acetyltransferase activity, ping-pong bi bi mechanism
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?
acetyl-CoA + p-aminotoluene
CoA + N-acetyl-p-aminotoluene
show the reaction diagram
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N-acetyltransferase activity, ping-pong bi bi mechanism
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?
acetyl-CoA + p-anisidine
CoA + N-acetyl-p-anisidine
show the reaction diagram
-
N-acetyltransferase activity, ping-pong bi bi mechanism
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?
butyryl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-(butyryloxy)-6-methylpyrido[3',2':4,5]imidazo[1,2-a]pyridin-2-amine
show the reaction diagram
hexanoyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-hexanoyloxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
show the reaction diagram
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1.3% of the activity compared to acetyl-CoA as acyl donor
-
?
malonyl-CoA + 2-hydroxy-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-malonyloxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
show the reaction diagram
p-aminobenzoic acid + acetyl-CoA
N-acetyl-p-aminobenzoic acid + CoA
show the reaction diagram
-
-
-
-
?
propionyl-CoA + 2-hydroxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
CoA + N-propionyloxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
show the reaction diagram
sulfadiazine + acetyl-CoA
N-acetyl-sulfadiazine + CoA
show the reaction diagram
-
-
-
-
?
sulfamethazine + acetyl-CoA
N-acetyl-sulfamethazine + CoA
show the reaction diagram
-
-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + an N-hydroxyarylamine
CoA + an N-acetoxyarylamine
show the reaction diagram
acetyl-CoA + o-aminobenzoic acid
CoA + N-acetyl-o-aminobenzoic acid
show the reaction diagram
-
o-aminobenzoic acid is intermediate in the synthesis of tryptophane in E. coli
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?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-naphthol
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1-Nitro-2-naphthol
2,6 dichloro-4-nitrophenol
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2-amino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole
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2-Aminofluorene
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2-naphthol
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Acetylsalicylic acid
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Harmaline
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harmine
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iodoacetamide
N-ethylmaleimide
Paraoxon
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no significant effect
Pentachlorophenol
salicylic acid
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thiolactomycin
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.238 - 0.857
2-Aminofluorene
0.0033 - 0.37
acetyl-CoA
0.55
aniline
-
-
0.59
Isoniazid
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1.71
m-aminophenol
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-
0.27
N-Hydroxy-2-acetylaminofluorene
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0.48
o-aminobenzoic acid
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1.94
o-aminophenol
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0.41
o-anisidine
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-
0.36 - 687
p-Aminobenzoic acid
0.54
p-Aminophenol
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0.63
p-aminotoluene
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-
0.83
p-anisidine
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3.1 - 5.8
Sulfadiazine
136
sulfamethazine
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recombinant isoform NAT2*4, pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0008
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substrate sulfamethazine, recombinant isoform NAT2*4, pH 7.5
0.001
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N-acetylation of p-aminobenzoic acid
0.00196
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kidney
0.0024
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intestine
0.0029
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substrate sulfadiazine, recombinant isoform NAT2*4, pH 7.5
0.0058
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liver
0.0064
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substrate p-aminobenzoic aicd, recombinant isoform NAT1*3, pH 7.5
0.0183
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substrate sulfadiazine, recombinant isoform NAT1*3, pH 7.5
0.06
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p-aminobenzoic acid
0.09
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aniline
0.1
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o-anisidine
0.126
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2-hydroxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole as substrate
0.17
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isoniazid
0.25
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p-aminotoluene
0.28
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m-aminophenol
0.3
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o-aminobenzoic acid
0.33
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p-aminophenol
0.47
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p-anisidine
0.517
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N-acetylation of 2-aminofluorene
0.67
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o-aminophenol
0.82
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2-hydroxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole as substrate
1.31
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2-hydroxyamino-6-methyldipyrido[1,2-a: 3',2'-d]imidazole as substrate
3.9
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N,O-acetyltransferase assay
7.8
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O-acetyltransferase assay
74
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N-acetyltransferase assay
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Mycobacterium abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
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SDS PAGE
32180
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calculated from nucleotide sequence
33000
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gel filtration
33500
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SDS PAGE
33570
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electrospray mass spectrometry
60000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 33000 SDS-PAGE
dimer
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2 * 34000, SDS-PAGE and DNA sequence
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sodium potassium tartrate and X-ray diffraction
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol 50% v/v, stabilizes during storage
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50 mM Tris-HCl, pH: 7.8, 10% glycerol, 1 month
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-80C, glycerol 50% v/v, stabilizes during storage
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, ion exchange chromatography, gel filtration, immunoaffinity chromatograpy with protein A Sepharose columns
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copurifies and may be identical with N-acetyltransferase EC 2.3.1.5
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copurifies with arylamine acetyltransferase and arylhydroxamic acid N,O-acetyltransferase; purification by ammonium sulfate followed by DEAE cellulose, gel filtration on GCL-2000 and HPKB-hydroxyapatite chromatography
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monomeric isozyme
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Ni-NTA column chromatography
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nickel affinity column chromatography, SDS-PAGE
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partial, by ammonium sulfate precipitation, DEAE-cellulose and Sephadex-G150 column chromatography; streptomycin, ammonium sulfate precipitation, DEAE Cellulose, Sephadex G-150 chromatograpy
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partial, using DEAE Cellulose and Sephacryl S-200 chromatography
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single step immobilized metal ion chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
16 recombinant NAT2 allozymes expressed in Escherichia coli JM105 expression system
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cloned and expression of wild type and two mutant enzymes in Escherichia coli XL-1-Blue maxi cells, plasmid pYG122
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construction of 2 oat-null mutants specifically disrupted by replacing the oat gene with the chloramphenicol resistance gene using the preligation method
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expressed in Escherichia coli AD494 and BL21(DE3) cells
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expression as a hystidine tagged fusion protein
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G127A
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mutation has no obvious effect on enzymatic activity
K214R
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the mutant exhibits an about 25% decrease in enzyme activity compared to the wild type enzyme
K214R/K281R
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the mutant exhibits an about 25% decrease in enzyme activity compared to the wild type enzyme
K281R
-
the mutant exhibits an about 12% decrease in enzyme activity compared to the wild type enzyme
G127A
-
mutation has no obvious effect on enzymatic activity
-
K214R
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the mutant exhibits an about 25% decrease in enzyme activity compared to the wild type enzyme
-
K214R/K281R
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the mutant exhibits an about 25% decrease in enzyme activity compared to the wild type enzyme
-
K281R
-
the mutant exhibits an about 12% decrease in enzyme activity compared to the wild type enzyme
-
I238T
-
about 30% of wild-type activity
K185N
-
about 40% of wild-type activity
N172I
-
about 20% of wild-type activity
N245I
-
enzymic activity comparable to wild-type, slight increase in Km-value
W77R
-
about 25% of wild-type activity
A69C
-
reduces enzyme activity without affecting stability and mobility on SDS-PAGE
A69R
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reduces enzyme activity without affecting stability and mobility on SDS-PAGE
A69C
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reduces enzyme activity without affecting stability and mobility on SDS-PAGE
-
A69R
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reduces enzyme activity without affecting stability and mobility on SDS-PAGE
-
A69C
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reduces enzyme activity without affecting stability and mobility on SDS-PAGE
-
A69R
-
reduces enzyme activity without affecting stability and mobility on SDS-PAGE
-
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