BRENDA - Enzyme Database show
show all sequences of 1.5.1.9

Isolation and characterization of enzymes involved in lysine catabolism from sorghum seeds

Fornazier, R.F.; Gaziola, S.A.; Helm, C.V.; Lea, P.J.; Azevedo, R.A.; J. Agric. Food Chem. 53, 1791-1798 (2005)

Data extracted from this reference:

General Stability
General Stability
Organism
very unstable during the isolation and purification procedure
Sorghum bicolor
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Sorghum bicolor
-
Moench
-
Sorghum bicolor Moench
-
Moench
-
Purification (Commentary)
Commentary
Organism
partial
Sorghum bicolor
Source Tissue
Source Tissue
Commentary
Organism
Textmining
endosperm
-
Sorghum bicolor
-
seed
only immature
Sorghum bicolor
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.54
-
-
Sorghum bicolor
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
655777
Sorghum bicolor
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
655777
Sorghum bicolor Moench
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
pH-optimum above pH 8.5
Sorghum bicolor
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Sorghum bicolor
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Sorghum bicolor
General Stability (protein specific)
General Stability
Organism
very unstable during the isolation and purification procedure
Sorghum bicolor
Purification (Commentary) (protein specific)
Commentary
Organism
partial
Sorghum bicolor
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
endosperm
-
Sorghum bicolor
-
seed
only immature
Sorghum bicolor
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.54
-
-
Sorghum bicolor
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
655777
Sorghum bicolor
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
?
N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O
-
655777
Sorghum bicolor Moench
L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+
-
-
-
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
pH-optimum above pH 8.5
Sorghum bicolor
Other publictions for EC 1.5.1.9
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)
743526
Schmidt
Lysine metabolism in antisens ...
Hordeum vulgare
Plant Physiol. Biochem.
87
73-83
2015
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743575
Wan
Pathways of amino acid degrad ...
Nilaparvata lugens
PLoS ONE
10
e0127789
2015
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725019
Serrano
Lysine degradation through the ...
Nostoc punctiforme, Nostoc punctiforme ATCC 29133, Ruegeria pomeroyi
FEBS Lett.
586
905-911
2012
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2
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712041
Leon-Ramirez
A molecular probe for Basidiom ...
Ustilago maydis
FEMS Microbiol. Lett.
312
77-83
2010
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724672
Anderson
Structural and transcriptional ...
Triticum turgidum
BMC Plant Biol.
10
113
2010
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700907
Battur
LKR/SDH plays important roles ...
Haemaphysalis longicornis
PLoS ONE
4
e7136
2009
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1
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7
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694615
Schildhauer
Supply of nitrogen can reverse ...
Arabidopsis thaliana, Hordeum vulgare
Plant Biol.
10 Suppl 1
76-84
2008
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655777
Fornazier
Isolation and characterization ...
Sorghum bicolor, Sorghum bicolor Moench
J. Agric. Food Chem.
53
1791-1798
2005
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1
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2
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1
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654174
Cunha Lima
Isolation of the bifunctional ...
Phaseolus vulgaris
Amino Acids
24
179-186
2003
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657056
Stepansky
Synthesis of the Arabidopsis b ...
Arabidopsis sp.
Plant Physiol.
133
1407-1415
2003
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396550
Zhu
Characterization of the two sa ...
Arabidopsis thaliana
Plant Physiol.
124
1363-1371
2000
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1
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8
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392370
Gaziola
The enzymology of lysine catab ...
Oryza sativa
Eur. J. Biochem.
247
364-371
1997
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2
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1
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1
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392371
Miron
-
In vitro dephosphorylation inh ...
Glycine max
Plant J.
12
1453-1458
1997
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396547
Goncalves-Butruille
Purification and Characterizat ...
Zea mays
Plant Physiol.
110
765-771
1996
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2
1
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392366
Blemings
Lysine-alpha-ketoglutarate red ...
Rattus norvegicus
J. Nutr.
124
1215-1221
1994
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396544
Mukhopadhyay
Comparison of lysine and trypt ...
Bos taurus, Rattus norvegicus
Experientia
46
874-876
1990
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392365
Markovitz
The bifunctional aminoadipic s ...
Bos taurus
J. Biol. Chem.
262
9353-9358
1987
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1
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392364
Markovitz
Familial hyperlysinemias. Puri ...
Bos taurus, Papio hamadryas
J. Biol. Chem.
259
11643-11646
1984
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2
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2
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2
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392361
Hutzler
Lysine-ketoglutarate reductase ...
Homo sapiens
Biochim. Biophys. Acta
377
42-51
1975
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396540
Fjellstedt
Properties of partially purifi ...
Homo sapiens
Arch. Biochem. Biophys.
171
191-196
1975
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4
2
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1
1
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2
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392363
Fellows
Lysine metabolism in mammals ...
Bos taurus, Canis lupus familiaris, Felis catus, Homo sapiens, Ovis aries, Rattus norvegicus, Sus scrofa
Biochem. J.
136
329-334
1973
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7
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8
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7
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7
7
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16
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7
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7
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7
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8
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7
7
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16
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396543
Hutzler
Saccharopine cleavage by a deh ...
Homo sapiens
Biochim. Biophys. Acta
206
205-214
1970
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4
2
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3
-
1
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1
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1
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1
1
2
2
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1
1
2
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1
1
1
2
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2
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4
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2
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3
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1
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1
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1
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2
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1
1
2
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1
1
1
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