BRENDA - Enzyme Database
show all sequences of 1.2.1.95

Regulation of alpha-aminoadipate reductase from Penicillium chrysogenum in relation to the flux from alpha-aminoadipate into penicillin biosynthesis

Lu, Y.; Mach, R.; Affenzeller, K.; Kubicek, C.; Can. J. Microbiol. 38, 758-763 (1992)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
L-lysine
in strains Q176, D6/1014/A, and P2, in vivo activity of alpha-aminoadipate reductase from superior penicillin producer strains is more strongly inhibited by lysine, and this is related to their ability to accumulate increased amounts of alpha-aminoadipate, and hence penicillin
Penicillium chrysogenum
Organism
Organism
UniProt
Commentary
Textmining
Penicillium chrysogenum
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
additional information
in strains Q176, D6/1014/A, and P2, the enzyme exhibits decreasing affinity for alpha-aminoadipate with increasing capacity of the respective strain to produce penicillin
733601
Penicillium chrysogenum
?
-
-
-
?
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
L-lysine
in strains Q176, D6/1014/A, and P2, in vivo activity of alpha-aminoadipate reductase from superior penicillin producer strains is more strongly inhibited by lysine, and this is related to their ability to accumulate increased amounts of alpha-aminoadipate, and hence penicillin
Penicillium chrysogenum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
additional information
in strains Q176, D6/1014/A, and P2, the enzyme exhibits decreasing affinity for alpha-aminoadipate with increasing capacity of the respective strain to produce penicillin
733601
Penicillium chrysogenum
?
-
-
-
?
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
Synonyms
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
-
-
1
-
1
-
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-
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2
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1
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1
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1
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742278
Kalb
Activity of alpha-aminoadipat ...
Gelatoporia subvermispora
ChemBioChem
16
1426-1430
2015
-
-
1
-
1
-
-
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-
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1
1
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1
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1
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1
1
4
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2
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1
2
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1
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1
1
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1
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1
1
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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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2
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9
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657420
Guo
Posttranslational activation, ...
Schizosaccharomyces pombe
Yeast
21
1279-1288
2004
-
-
1
-
4
-
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-
-
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8
-
1
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656194
Hijarrubia
Domain structure characterizat ...
Penicillium chrysogenum
J. Biol. Chem.
278
8250-8256
2003
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-
-
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-
1
3
-
3
3
-
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4
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1
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2
3
1
1
1
1
2
1
1
1
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1
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3
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3
3
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1
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-
2
3
1
1
1
2
1
1
1
-
-
-
-
-
-
-
-
656800
Guo
Site-directed mutational analy ...
Candida albicans
Mol. Genet. Genomics
269
271-279
2003
-
-
1
-
61
-
-
-
-
1
-
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7
-
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1
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1
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1
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1
1
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61
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1
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1
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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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4
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1
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2
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2
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2
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288204
Guo
Novel posttranslational activa ...
Candida albicans
J. Bacteriol.
183
7120-7125
2001
-
-
1
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7
-
-
-
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1
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5
-
1
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1
1
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1
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7
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1
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1
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1
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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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1
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4
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1
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4
1
1
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4
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5
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1
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1
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4
1
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4
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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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1
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1
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7
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1
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1
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1
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-
733601
Lu
Regulation of alpha-aminoadipa ...
Penicillium chrysogenum
Can. J. Microbiol.
38
758-763
1992
-
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1
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4
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1
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1
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733888
Affenzeller
-
Lysine biosynthesis in Penicil ...
Penicillium chrysogenum
FEMS Microbiol. Lett.
58
293-297
1989
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3
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