BRENDA - Enzyme Database
show all sequences of 1.11.1.1

Pyridine nucleotide oxidizing enzymes of Lactobacillus casei. II. Oxidase and peroxidase

Walker, G.A.; Kilgour, G.L.; Arch. Biochem. Biophys. 111, 534-539 (1965)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
N-ethylmaleimide
50% inhibition at 1 mM
Lactobacillus casei
p-hydroxymercuribenzoate
100% inhibition at 1 mM
Lactobacillus casei
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Lactobacillus casei
-
-
-
Purification (Commentary)
Commentary
Organism
partial, peroxidase activity cannot be separated from oxidase acitivity
Lactobacillus casei
Storage Stability
Storage Stability
Organism
5°C, pH 7.0, 1 month
Lactobacillus casei
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ferricyanide + H2O2
-
395332
Lactobacillus casei
ferrocyanide + H2O
-
-
-
?
additional information
H2O2 cannot be replaced by methylene blue, indophenol, or benzoquinone
395332
Lactobacillus casei
?
-
-
-
-
NADH + H2O2
NADPH is only 8% as active as NADH
395332
Lactobacillus casei
NAD+ + H2O
-
-
-
?
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
5
-
1 month
Lactobacillus casei
50
-
5 min
Lactobacillus casei
60
-
5 min, 20% loss of activity
Lactobacillus casei
70
-
complete loss of activity
Lactobacillus casei
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.4
-
-
Lactobacillus casei
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
2.8
-
complete loss of activity after 2 h
Lactobacillus casei
3
-
19% of enzyme activity after 2 h
Lactobacillus casei
3.25
-
86% of enzyme activity after 2 h
Lactobacillus casei
3.5
-
no loss of enzyme activity after 2 h
Lactobacillus casei
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
-
Lactobacillus casei
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
-
Lactobacillus casei
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
N-ethylmaleimide
50% inhibition at 1 mM
Lactobacillus casei
p-hydroxymercuribenzoate
100% inhibition at 1 mM
Lactobacillus casei
Purification (Commentary) (protein specific)
Commentary
Organism
partial, peroxidase activity cannot be separated from oxidase acitivity
Lactobacillus casei
Storage Stability (protein specific)
Storage Stability
Organism
5°C, pH 7.0, 1 month
Lactobacillus casei
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ferricyanide + H2O2
-
395332
Lactobacillus casei
ferrocyanide + H2O
-
-
-
?
additional information
H2O2 cannot be replaced by methylene blue, indophenol, or benzoquinone
395332
Lactobacillus casei
?
-
-
-
-
NADH + H2O2
NADPH is only 8% as active as NADH
395332
Lactobacillus casei
NAD+ + H2O
-
-
-
?
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
5
-
1 month
Lactobacillus casei
50
-
5 min
Lactobacillus casei
60
-
5 min, 20% loss of activity
Lactobacillus casei
70
-
complete loss of activity
Lactobacillus casei
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.4
-
-
Lactobacillus casei
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
2.8
-
complete loss of activity after 2 h
Lactobacillus casei
3
-
19% of enzyme activity after 2 h
Lactobacillus casei
3.25
-
86% of enzyme activity after 2 h
Lactobacillus casei
3.5
-
no loss of enzyme activity after 2 h
Lactobacillus casei
Other publictions for EC 1.11.1.1
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)
742429
Keirsse-Haquin
Modulation of the flavin-prot ...
Enterococcus faecalis
Eur. Biophys. J.
FEHLT
0000
2017
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743331
Wang
Mimicking horseradish peroxid ...
synthetic construct
Nano Lett.
17
2043-2048
2017
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724862
Achary
Aluminum induces oxidative bur ...
Allium cepa
Environ. Mol. Mutagen.
53
550-560
2012
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2
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1
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1
1
1
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699261
Fuehrs
Characterization of leaf apopl ...
Vigna unguiculata
J. Exp. Bot.
60
1663-1678
2009
4
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1
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4
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1
1
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700055
Riebe
Pathway for H2O2 and O2 detoxi ...
Clostridium acetobutylicum
Microbiology
155
16-24
2009
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1
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-
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3
1
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3
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1
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4
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1
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4
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1
1
1
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1
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1
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1
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-
689049
La Carbona
Comparative study of the physi ...
Enterococcus faecalis
Mol. Microbiol.
66
1148-1163
2007
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3
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676593
Fecht-Christoffers
The role of hydrogen peroxide- ...
Vigna unguiculata
Plant Physiol.
140
1451-1463
2006
1
-
-
-
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1
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2
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672012
Yeh
Peptergents: peptide detergent ...
Enterococcus casseliflavus
Biochemistry
44
16912-16919
2005
-
-
1
-
-
1
-
-
-
-
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-
-
2
2
-
1
1
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2
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1
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2
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674247
Fernandez
Bacterial cyanide oxygenase is ...
Pseudomonas fluorescens
J. Bacteriol.
187
6396-6402
2005
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4
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3
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1
1
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658242
Simonovicova
-
Effect of aluminum on oxidativ ...
Hordeum vulgare
Biol. Plant.
48
261-266
2004
-
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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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395349
Yeh
Crystal structures of oxidized ...
Enterococcus faecalis
Methods Enzymol.
353
44-54
2002
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1
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1
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658146
Davydova
Antioxidative enzymes of sulfa ...
Desulfovibrio desulfuricans
Biochemistry (Moscow)
67
822-825
2002
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3
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1
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4
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660156
Lin
-
Osmotic stress-induced changes ...
Oryza sativa
Plant Growth Regul.
37
177-184
2002
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1
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1
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395344
Crane
Analysis of the kinetic and re ...
Enterococcus faecalis
Biochemistry
39
10353-10364
2000
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1
1
2
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6
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1
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1
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1
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3
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1
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6
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1
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395342
Coulter
NADH peroxidase activity of ru ...
Clostridium perfringens, Desulfovibrio vulgaris
Biochem. Biophys. Res. Commun.
255
317-323
1999
-
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-
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2
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7
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2
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2
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2
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395333
Yeh
Structure of the native cystei ...
Enterococcus faecalis
Biochemistry
35
9951-9957
1996
-
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1
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2
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395348
Sakamoto
-
Aerobic growth of and activiti ...
Enterococcus faecium, Lactobacillus brevis, Lactobacillus buchneri, Lactobacillus casei, Lactobacillus coryniformis, Lactobacillus delbrueckii, Lactobacillus mali, Lactobacillus plantarum, Lactobacillus rhamnosus, Leuconostoc lactis, Leuconostoc mesenteroides, Pediococcus acidilactici, Pediococcus pentosaceus, Streptococcus thermophilus
J. Ferment. Bioeng.
82
210-216
1996
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14
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16
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16
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395343
Crane
Analysis of the kinetic mechan ...
Enterococcus faecalis
Biochemistry
34
14114-14124
1995
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1
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1
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395345
Mande
Crystallographic analyses of N ...
Enterococcus faecalis
Biochemistry
34
6985-6992
1995
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1
1
2
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1
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2
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1
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1
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395346
Parsonage
Analysis of the kinetic and re ...
Enterococcus faecalis 10C1, Enterococcus faecalis
Biochemistry
34
435-441
1995
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1
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2
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8
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1
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2
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3
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2
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3
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395347
Parsonage
Purification and analysis of s ...
Enterococcus faecalis 10C1, Enterococcus faecalis
J. Biol. Chem.
268
3161-3167
1993
1
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1
1
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1
1
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2
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10
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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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1
1
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2
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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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395337
Claiborne
-
The Streptococcal NADH peroxid ...
Enterococcus faecalis
Flavins and Flavoproteins (Proc. Int. Symp. , 10th, Meeting Date 1990, Curti, B. , Ronchi S. , Zanetti, G. , eds. ) de Gruyter, Berlin, New York
667-670
1991
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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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The structure of NADH peroxida ...
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Sequence fingerprints for the ...
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Heterogeneity among the flavin ...
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The non-flavin redox center of ...
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