BRENDA - Enzyme Database show
show all sequences of 1.11.1.1

Characterization of leaf apoplastic peroxidases and metabolites in Vigna unguiculata in response to toxic manganese supply and silicon

Fuehrs, H.; Goetze, S.; Specht, A.; Erban, A.; Gallien, S.; Heintz, D.; Van Dorsselaer, A.; Kopka, J.; Braun, H.P.; Horst, W.J.; J. Exp. Bot. 60, 1663-1678 (2009)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
Benzoic acid
enhances NADH-peroxidase activity in the presence of Mn2+
Vigna unguiculata
ferulic acid
enhances NADH-peroxidase activity in the presence of Mn2+
Vigna unguiculata
p-coumaric acid
enhances NADH-peroxidase activity in the presence of Mn2+
Vigna unguiculata
vanillic acid
enhances NADH-peroxidase activity in the presence of Mn2+
Vigna unguiculata
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mn2+
-
Vigna unguiculata
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
NADH + H+ + H2O2
Vigna unguiculata
four peroxidase isoenzymes are isolated, catalyse both H2O2-consuming and H2O2-producing activity
NAD+ + H2O
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Vigna unguiculata
-
-
-
Purification (Commentary)
Commentary
Organism
separation of proteins on a 1D blue-native gel followed by electroelution, four isoenzymes elutes from the blue-native gels
Vigna unguiculata
Source Tissue
Source Tissue
Commentary
Organism
Textmining
leaf
-
Vigna unguiculata
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
NADH + H+ + H2O2
four peroxidase isoenzymes are isolated, catalyse both H2O2-consuming and H2O2-producing activity
699261
Vigna unguiculata
NAD+ + H2O
-
-
-
r
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
activity assay
Vigna unguiculata
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5.5
6.5
four peroxidase isoenzymes
Vigna unguiculata
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
Benzoic acid
enhances NADH-peroxidase activity in the presence of Mn2+
Vigna unguiculata
ferulic acid
enhances NADH-peroxidase activity in the presence of Mn2+
Vigna unguiculata
p-coumaric acid
enhances NADH-peroxidase activity in the presence of Mn2+
Vigna unguiculata
vanillic acid
enhances NADH-peroxidase activity in the presence of Mn2+
Vigna unguiculata
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mn2+
-
Vigna unguiculata
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
NADH + H+ + H2O2
Vigna unguiculata
four peroxidase isoenzymes are isolated, catalyse both H2O2-consuming and H2O2-producing activity
NAD+ + H2O
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
separation of proteins on a 1D blue-native gel followed by electroelution, four isoenzymes elutes from the blue-native gels
Vigna unguiculata
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
leaf
-
Vigna unguiculata
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
NADH + H+ + H2O2
four peroxidase isoenzymes are isolated, catalyse both H2O2-consuming and H2O2-producing activity
699261
Vigna unguiculata
NAD+ + H2O
-
-
-
r
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
activity assay
Vigna unguiculata
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5.5
6.5
four peroxidase isoenzymes
Vigna unguiculata
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
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1
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1
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1
1
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699261
Fuehrs
Characterization of leaf apopl ...
Vigna unguiculata
J. Exp. Bot.
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1663-1678
2009
4
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1
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1
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2
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4
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1
1
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672012
Yeh
Peptergents: peptide detergent ...
Enterococcus casseliflavus
Biochemistry
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2
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Simonovicova
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Hordeum vulgare
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Enterococcus faecalis
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2002
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658146
Davydova
Antioxidative enzymes of sulfa ...
Desulfovibrio desulfuricans
Biochemistry (Moscow)
67
822-825
2002
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660156
Lin
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Osmotic stress-induced changes ...
Oryza sativa
Plant Growth Regul.
37
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2002
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395344
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Analysis of the kinetic and re ...
Enterococcus faecalis
Biochemistry
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2000
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6
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395333
Yeh
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Enterococcus faecalis
Biochemistry
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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
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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 ...
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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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395346
Parsonage
Analysis of the kinetic and re ...
Enterococcus faecalis 10C1, Enterococcus faecalis
Biochemistry
34
435-441
1995
-
-
1
-
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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1
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2
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1
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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
-
1
1
-
-
1
1
-
-
2
-
-
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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-
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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
-
-
2
-
-
-
-
1
-
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1
-
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1
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1
1
1
-
-
-
-
-
-
-
-
-
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
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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