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show all sequences of 1.2.1.95

Activity of alpha-aminoadipate reductase depends on the N-terminally extending domain

Kalb, D.; Lackner, G.; Rappe, M.; Hoffmeister, D.; ChemBioChem 16, 1426-1430 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant expression of N-terminally His6-tagged truncated NPS3 enzyme mutant lacking the 247 amino acids of the N-terminal ADA domain from pET21a-based expression plasmid pMR1, recombinant expression of N-terminally His6-tagged truncated NPS3 enzyme mutant lacking the 152 amino acids of the N-terminal ADA domain from expression plasmid pDK22, and recombinant expression of the 102.8 kDa ADA-A didomain (lacking the C-terminal 515 amino acids) and the 75.7 kDa standalone NPS3A domain, respectively, in which the first 247 and terminal 515 amino acids are absent, from plasmids pDK24 and pDK25, both based on expression vector pET28a, all in Escherichia coli strain KRX
Gelatoporia subvermispora
Engineering
Amino acid exchange
Commentary
Organism
additional information
truncated enzymes based on NPS3, the L-alpha-aminoadipic acid reductase of the basidiomycete Ceriporiopsis subvermispora, lacking the ADA domain either partially or entirely are tested for activity in vitro, together with an ADA-adenylation didomain and the ADA domain-less adenylation domain
Gelatoporia subvermispora
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
132600
-
about, recombinant truncated enzyme, sequence calculation
Gelatoporia subvermispora
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-2-aminoadipate + NADPH + H+ + ATP
Gelatoporia subvermispora
-
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Gelatoporia subvermispora
A0A0S2LUS1
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged truncated enzyme mutants from Escherichia coli strain KRX by nickel affinity chromatography and gel filtration
Gelatoporia subvermispora
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-2-aminoadipate + NADPH + H+ + ATP
-
742278
Gelatoporia subvermispora
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
the enzyme has a multidomain composition but features a unique domain of elusive function, termed the adenylation activating (ADA) domain, that extends the reductase N-terminally. The activity of alpha-aminoadipate reductase depends on the N-terminally extending domain
Gelatoporia subvermispora
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
required
Gelatoporia subvermispora
NADPH
-
Gelatoporia subvermispora
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression of N-terminally His6-tagged truncated NPS3 enzyme mutant lacking the 247 amino acids of the N-terminal ADA domain from pET21a-based expression plasmid pMR1, recombinant expression of N-terminally His6-tagged truncated NPS3 enzyme mutant lacking the 152 amino acids of the N-terminal ADA domain from expression plasmid pDK22, and recombinant expression of the 102.8 kDa ADA-A didomain (lacking the C-terminal 515 amino acids) and the 75.7 kDa standalone NPS3A domain, respectively, in which the first 247 and terminal 515 amino acids are absent, from plasmids pDK24 and pDK25, both based on expression vector pET28a, all in Escherichia coli strain KRX
Gelatoporia subvermispora
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
required
Gelatoporia subvermispora
NADPH
-
Gelatoporia subvermispora
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
truncated enzymes based on NPS3, the L-alpha-aminoadipic acid reductase of the basidiomycete Ceriporiopsis subvermispora, lacking the ADA domain either partially or entirely are tested for activity in vitro, together with an ADA-adenylation didomain and the ADA domain-less adenylation domain
Gelatoporia subvermispora
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
132600
-
about, recombinant truncated enzyme, sequence calculation
Gelatoporia subvermispora
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-2-aminoadipate + NADPH + H+ + ATP
Gelatoporia subvermispora
-
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged truncated enzyme mutants from Escherichia coli strain KRX by nickel affinity chromatography and gel filtration
Gelatoporia subvermispora
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-2-aminoadipate + NADPH + H+ + ATP
-
742278
Gelatoporia subvermispora
(S)-2-amino-6-oxohexanoate + NADP+ + AMP + diphosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
the enzyme has a multidomain composition but features a unique domain of elusive function, termed the adenylation activating (ADA) domain, that extends the reductase N-terminally. The activity of alpha-aminoadipate reductase depends on the N-terminally extending domain
Gelatoporia subvermispora
General Information
General Information
Commentary
Organism
metabolism
the enzyme is involved in the fungal de novo L-lysine biosynthesis via ATP- and NADPH-dependent reduction of the intermediate L-alpha-aminoadipic acid into L-alpha-aminoadipate 6-semialdehyde as a multifunctional aminoacyl-adenylate-forming reductase, pathway overview
Gelatoporia subvermispora
additional information
the enzyme has a multidomain composition but features a unique domain of elusive function, termed the adenylation activating (ADA) domain, that extends the reductase N-terminally. The activity of alpha-aminoadipate reductase and A domain depends on the N-terminally extending domain. ADA domain sequence comparison and protein interaction analysis, homology modeling, overview
Gelatoporia subvermispora
physiological function
L-alpha-aminoadipic acid reductases catalyze the ATP- and NADPH-dependent reduction of L-alpha-aminoadipic acid to the corresponding 6-semialdehyde during fungal L-lysine biosynthesis
Gelatoporia subvermispora
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the enzyme is involved in the fungal de novo L-lysine biosynthesis via ATP- and NADPH-dependent reduction of the intermediate L-alpha-aminoadipic acid into L-alpha-aminoadipate 6-semialdehyde as a multifunctional aminoacyl-adenylate-forming reductase, pathway overview
Gelatoporia subvermispora
additional information
the enzyme has a multidomain composition but features a unique domain of elusive function, termed the adenylation activating (ADA) domain, that extends the reductase N-terminally. The activity of alpha-aminoadipate reductase and A domain depends on the N-terminally extending domain. ADA domain sequence comparison and protein interaction analysis, homology modeling, overview
Gelatoporia subvermispora
physiological function
L-alpha-aminoadipic acid reductases catalyze the ATP- and NADPH-dependent reduction of L-alpha-aminoadipic acid to the corresponding 6-semialdehyde during fungal L-lysine biosynthesis
Gelatoporia subvermispora
Other publictions for EC 1.2.1.95
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)
733659
Kalb
Activity of alpha-aminoadipate ...
Gelatoporia subvermispora, Gelatoporia subvermispora B
ChemBioChem
16
1426-1430
2015
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742278
Kalb
Activity of alpha-aminoadipat ...
Gelatoporia subvermispora
ChemBioChem
16
1426-1430
2015
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3
3
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695274
Yan
Cloning, sequencing and charac ...
Saccharomycopsis fibuligera, Saccharomycopsis fibuligera PD70
Yeast
24
189-199
2007
1
1
1
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1
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6
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657420
Guo
Posttranslational activation, ...
Schizosaccharomyces pombe
Yeast
21
1279-1288
2004
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1
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4
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7
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1
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656194
Hijarrubia
Domain structure characterizat ...
Penicillium chrysogenum
J. Biol. Chem.
278
8250-8256
2003
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1
3
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3
3
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2
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1
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3
1
1
1
2
1
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1
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656800
Guo
Site-directed mutational analy ...
Candida albicans
Mol. Genet. Genomics
269
271-279
2003
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61
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5
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61
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288203
Hijarrubia
Characterization of the lys2 g ...
Acremonium chrysogenum, Acremonium chrysogenum ATCC 48272
Mol. Gen. Genet.
264
755-762
2001
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288204
Guo
Novel posttranslational activa ...
Candida albicans
J. Bacteriol.
183
7120-7125
2001
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1
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7
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288201
Ehmann
Lysine biosynthesis in Sacchar ...
Saccharomyces cerevisiae
Biochemistry
38
6171-6177
1999
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1
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5
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4
4
288198
Ford
Molecular properties of the ly ...
Schizosaccharomyces pombe, Schizosaccharomyces pombe 972
Curr. Genet.
28
131-137
1995
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733601
Lu
Regulation of alpha-aminoadipa ...
Penicillium chrysogenum
Can. J. Microbiol.
38
758-763
1992
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733888
Affenzeller
-
Lysine biosynthesis in Penicil ...
Penicillium chrysogenum
FEMS Microbiol. Lett.
58
293-297
1989
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