BRENDA - Enzyme Database show
show all sequences of 1.1.1.192

Biosynthesis of 4-methylproline in cyanobacteria: cloning of nosE and nosF genes and biochemical characterization of the encoded dehydrogenase and reductase activities

Luesch, H.; Hoffmann, D.; Hevel, J.M.; Becker, J.E.; Golakoti, T.; Moore, R.E.; J. Org. Chem. 68, 83-91 (2003)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene nosE, overexpression in Escherichia coli BL21(DE3) as N-terminally His-tagged enzyme
Nostoc sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.24
-
(2S,4S)-5-hydroxyleucine
pH 10.0, 42°C, recombinant enzyme
Nostoc sp.
1.2
-
(2S)-5-hydroxy-2-aminovaleric acid
pH 10.0, 42°C, recombinant enzyme
Nostoc sp.
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
dependent on
Nostoc sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
x * 35000, about, recombinant enzyme, SDS-PAGE
Nostoc sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(2S,4S)-5-hydroxyleucine + NAD+ + H2O
Nostoc sp.
enzyme reaction is part of the biosynthesis of (2S,4S)-4-methylproline
(4S)-5-oxo-L-leucine + NADH
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Nostoc sp.
-
GSV224, gene nosE
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme by nickel affinity chromatography
Nostoc sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2S)-5-hydroxy-2-aminovaleric acid + NAD+ + H2O
no activity with the (2R)-isomer
656603
Nostoc sp.
(2S)-2-amino-5-oxopentanoate + NADH
-
-
-
?
(2S,4S)-5-hydroxyleucine + NAD+ + H2O
-
656603
Nostoc sp.
(4S)-5-oxo-L-leucine + NADH
-
-
-
r
(2S,4S)-5-hydroxyleucine + NAD+ + H2O
enzyme reaction is part of the biosynthesis of (2S,4S)-4-methylproline
656603
Nostoc sp.
(4S)-5-oxo-L-leucine + NADH
-
-
-
r
additional information
stereospecific abstraction of the 5pro-S hydrogen
656603
Nostoc sp.
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 35000, about, recombinant enzyme, SDS-PAGE
Nostoc sp.
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
42
-
-
Nostoc sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
10
-
-
Nostoc sp.
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
specific for the A-side of NAD+, no activity with NADP+
Nostoc sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
gene nosE, overexpression in Escherichia coli BL21(DE3) as N-terminally His-tagged enzyme
Nostoc sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
specific for the A-side of NAD+, no activity with NADP+
Nostoc sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.24
-
(2S,4S)-5-hydroxyleucine
pH 10.0, 42°C, recombinant enzyme
Nostoc sp.
1.2
-
(2S)-5-hydroxy-2-aminovaleric acid
pH 10.0, 42°C, recombinant enzyme
Nostoc sp.
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
dependent on
Nostoc sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
35000
-
x * 35000, about, recombinant enzyme, SDS-PAGE
Nostoc sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(2S,4S)-5-hydroxyleucine + NAD+ + H2O
Nostoc sp.
enzyme reaction is part of the biosynthesis of (2S,4S)-4-methylproline
(4S)-5-oxo-L-leucine + NADH
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme by nickel affinity chromatography
Nostoc sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2S)-5-hydroxy-2-aminovaleric acid + NAD+ + H2O
no activity with the (2R)-isomer
656603
Nostoc sp.
(2S)-2-amino-5-oxopentanoate + NADH
-
-
-
?
(2S,4S)-5-hydroxyleucine + NAD+ + H2O
-
656603
Nostoc sp.
(4S)-5-oxo-L-leucine + NADH
-
-
-
r
(2S,4S)-5-hydroxyleucine + NAD+ + H2O
enzyme reaction is part of the biosynthesis of (2S,4S)-4-methylproline
656603
Nostoc sp.
(4S)-5-oxo-L-leucine + NADH
-
-
-
r
additional information
stereospecific abstraction of the 5pro-S hydrogen
656603
Nostoc sp.
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 35000, about, recombinant enzyme, SDS-PAGE
Nostoc sp.
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
42
-
-
Nostoc sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
10
-
-
Nostoc sp.
Other publictions for EC 1.1.1.192
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)
712962
Liu
Two novel metal-independent lo ...
Geobacillus thermodenitrificans, Geobacillus thermodenitrificans NG80-2
Microbiology
155
2078-2085
2009
1
-
1
-
-
-
10
5
-
3
4
-
-
4
-
-
-
-
-
-
-
-
26
1
1
-
1
3
1
1
-
4
-
-
-
1
-
2
6
-
-
-
-
19
-
5
-
5
4
-
-
-
-
-
-
-
-
-
26
1
2
-
2
3
2
2
-
-
-
-
-
-
5
5
656603
Luesch
Biosynthesis of 4-methylprolin ...
Nostoc sp.
J. Org. Chem.
68
83-91
2003
-
-
1
-
-
-
-
2
-
1
1
1
-
4
-
-
1
-
-
-
-
-
4
1
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
2
-
1
1
1
-
-
-
1
-
-
-
-
4
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
347799
Nagashima
-
Long-chain n-alkanol dehydroge ...
Pseudomonas putida
J. Ferment. Bioeng.
82
328-333
1996
-
-
-
-
-
-
-
11
-
1
2
-
-
1
-
-
1
-
-
-
-
-
9
2
1
-
2
-
2
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
11
-
1
2
-
-
-
-
1
-
-
-
-
9
2
1
-
2
-
2
-
-
-
-
-
-
-
-
-
288324
Van Ophem
NAD-linked, factor-dependent f ...
Amycolatopsis methanolica
Eur. J. Biochem.
206
511-518
1992
-
-
-
-
-
-
5
7
-
1
2
1
-
7
-
-
-
-
-
-
-
-
7
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
7
-
1
2
1
-
-
-
-
-
-
-
-
7
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
347798
Ribas de Pouplana
-
Structural properties of long- ...
Equus caballus
Biochem. J.
276
433-438
1991
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
347795
Ueda
Long-chain alcohol dehydrogena ...
Candida tropicalis, Yarrowia lipolytica
Methods Enzymol.
188
171-175
1990
-
-
-
-
-
6
-
-
-
-
-
4
-
4
-
-
-
-
-
-
-
-
9
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
6
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
9
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
347796
Yamada
Subcellular localization of lo ...
Candida tropicalis
Arch. Microbiol.
128
145-151
1980
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
3
-
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-
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-
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-
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2
-
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-
-
-
-
-
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3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
347794
Lee
Characterization of fatty alco ...
Rattus norvegicus
J. Biol. Chem.
254
2892-2896
1979
1
-
-
-
-
-
3
1
-
-
-
1
-
1
-
-
-
-
-
1
-
-
4
-
1
-
-
-
2
-
-
1
-
-
-
1
-
-
1
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
-
1
-
-
4
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
347800
Eklund
Three-dimensional structure of ...
Equus caballus
J. Mol. Biol.
102
27-59
1976
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
1
-
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-
-
-
-
-
-
-
-
-
-
-
-
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1
-
-
-
-
-
-
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