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Information on EC 2.6.1.29 - diamine transaminase
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2.6.1.29 diamine transaminaseSpecify your search results
Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
pcata, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)-selective ATA
alpha,omega-diamine transaminase
alpha,omega-DTA
amine transaminase
-
-
-
-
amine-ketoacid transaminase
-
-
-
-
aminotransferase, diamine
-
-
-
-
bifunctional di-amine transaminase
bifunctional mono- and di-amine transaminase
diamine aminotransferase
-
-
-
-
diamine-ketoglutaric transaminase
-
-
-
-
omega-diamine aminotransferase
Pa-SpuC
Pf-SpuC
SpuC
bifunctional mono- and di-amine transaminase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an alpha,omega-diamine + 2-oxoglutarate = an omega-aminoaldehyde + L-glutamate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
diamine:2-oxoglutarate aminotransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9031-83-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(+)-1,4-diaminobutan-2-ol + 2-oxoglutarate
?
-
30% of the activity with putrescine
-
-
?
1,6-diaminohexane + 2-oxoglutarate
6-aminohexanal + L-glutamate
-
-
-
?
1,7-diaminoheptane + 2-oxoglutarate
7-aminoheptanal + L-glutamate
-
30% of the activity with putrescine
-
?
1,7-diaminoheptane + 2-oxoglutarate
7-aminoheptanal + L-glutamate
-
30% of the activity with putrescine
-
?
1-phenylpentane-2,4-dione + cadaverine
?
-
43% conversion at 5 mM cadaverine, 80% at 15 mM cadaverine
-
-
?
1-phenylpentane-2,4-dione + cadaverine
?
-
54% conversion at 5 mM cadaverine, 78% at 15 mM cadaverine
-
-
?
1-phenylpentane-2,4-dione + cadaverine
?
-
53% conversion at 5 mM cadaverine, 75% at 15 mM cadaverine
-
-
?
1-phenylpentane-2,4-dione + cadaverine
?
-
75% conversion at 5 mM cadaverine, 99% at 15 mM cadaverine
-
-
?
1-phenylpentane-2,4-dione + o-xylylenediamine
?
-
23% conversion
-
-
?
1-phenylpentane-2,4-dione + o-xylylenediamine
?
-
35% conversion
-
-
?
1-phenylpentane-2,4-dione + putrescine
?
-
20% conversion
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
-
-
?
4-aminobutanoate + 2-oxoglutarate
4-oxobutanoate + L-glutamate
-
11% of the activity with putrescine
-
?
4-phenylbutan-2-one + cadaverine
?
-
14% conversion
-
-
?
4-phenylbutan-2-one + o-xylylenediamine
?
-
8% conversion
-
-
?
4-phenylbutan-2-one + putrescine
?
-
6% conversion
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
equally active as putrescine
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
equally active as putrescine
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
additional information
?
-
-
inactive with 1,3-diaminopropane, lysine, ornithine, spermidine
-
-
?
additional information
?
-
-
inactive with 1,3-diaminopropane, lysine, ornithine, spermidine
-
-
?
additional information
?
-
-
inactive with histamine, tyramine, 4-aminobutanol, beta-alanine
-
-
?
additional information
?
-
-
development of a whole-cell system for the co-production of an omega-TA and sacrificial smart amine donor. Optimization of reaction conditions, 5 mM amine substrate concentration. No activity with benzaldehyde as amine acceptor
-
-
-
additional information
?
-
-
development of a whole-cell system for the co-production of an omega-TA and sacrificial smart amine donor. Optimization of reaction conditions, 5 mM amine substrate concentration. No activity with putrescine as amine donor and benzaldehyde as amine acceptor
-
-
-
additional information
?
-
-
development of a whole-cell system for the co-production of an omega-TA and sacrificial smart amine donor. Optimization of reaction conditions, 5 mM amine substrate concentration. No activity with benzaldehyde as amine acceptor
-
-
-
additional information
?
-
-
development of a whole-cell system for the co-production of an omega-transaminase and sacrificial smart amine donor. Optimization of reaction conditions, 5 mM amine substrate concentration. No activity with benzaldehyde as amine acceptor
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
an alpha,omega-diamine + 2-oxoglutarate
an omega-aminoaldehyde + L-glutamate
-
-
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
cadaverine + 2-oxoglutarate
5-aminopentanal + L-glutamate
-
enzyme catalyzes the second step in lysine catabolism
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
purified enzyme normally active without added pyridoxal phosphate, absolute requirement when irradiated with UV light or treated with 2 mM phenylhydrazine and then with Norite
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Coronary Artery Disease
Determinants of Pericoronary Adipose Tissue Attenuation on Computed Tomography Angiography in Coronary Artery Disease.
Coronary Artery Disease
Impact of pericoronary adipose tissue inflammation on left ventricular hypertrophy and regional physiological indices in stable coronary artery disease patients with preserved systolic function.
Coronary Artery Disease
Prognostic Value of RCA Pericoronary Adipose Tissue CT-Attenuation Beyond High-Risk Plaques, Plaque Volume, and Ischemia.
Myocardial Ischemia
Prognostic Value of RCA Pericoronary Adipose Tissue CT-Attenuation Beyond High-Risk Plaques, Plaque Volume, and Ischemia.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00064
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 10.5
-
almost completely inactive at pH 7, pH 8 about 40% of maximum activity, pH 10.5 about 20% of maximum activity
additional information
additional information
-
the ATA retains less than 20% activity in the intracellular neutral pH
additional information
-
the ATA retains less than 20% activity in the intracellular neutral pH
additional information
-
the ATA retains less than 20% activity in the intracellular neutral pH
additional information
-
the ATA retains less than 20% activity in the intracellular neutral pH
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Show AA Sequence and Transmembrane Helices (1386 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
precipitation with ammonium sulphate followed by column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene spuC, recombinant overexpression in Escherichia coli strain BL21(DE3)
recombinant expression in Corynebacterium glutamicum
gene spuC, recombinant overexpression in Escherichia coli strain BL21(DE3)
gene spuC, recombinant overexpression in Escherichia coli strain BL21(DE3)
gene spuC, recombinant overexpression in Escherichia coli strain BL21(DE3)
gene spuC, recombinant overexpression in Escherichia coli strain BL21(DE3)
recombinant expression in Corynebacterium glutamicum
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
biocatalytic transamination with near-stoichiometric inexpensive amine donors mediated by bifunctional mono- and di-amine transaminases. Both monoamine and diamine transaminase activity is reported, allowing conversion of a wide range of target ketone substrates with just a small excess of amine donor. The diamine co-substrates (putrescine, cadaverine or spermidine) are bio-derived and the enzyme system results in very little waste, making it a greener strategy for the production of valuable amine fine chemicals and pharmaceuticals
synthesis
biocatalytic transamination with near-stoichiometric inexpensive amine donors mediated by bifunctional mono- and di-amine transaminases. Both monoamine and diamine transaminase activity is reported, allowing conversion of a wide range of target ketone substrates with just a small excess of amine donor. The diamine co-substrates (putrescine, cadaverine or spermidine) are bio-derived and the enzyme system results in very little waste, making it a greener strategy for the production of valuable amine fine chemicals and pharmaceuticals
synthesis
biocatalytic transamination with near-stoichiometric inexpensive amine donors mediated by bifunctional mono- and di-amine transaminases. Both monoamine and diamine transaminase activity is reported, allowing conversion of a wide range of target ketone substrates with just a small excess of amine donor. The diamine co-substrates (putrescine, cadaverine or spermidine) are bio-derived and the enzyme system results in very little waste, making it a greener strategy for the production of valuable amine fine chemicals and pharmaceuticals
synthesis
biocatalytic transamination with near-stoichiometric inexpensive amine donors mediated by bifunctional mono- and di-amine transaminases. Both monoamine and diamine transaminase activity is reported, allowing conversion of a wide range of target ketone substrates with just a small excess of amine donor. The diamine co-substrates (putrescine, cadaverine or spermidine) are bio-derived and the enzyme system results in very little waste, making it a greener strategy for the production of valuable amine fine chemicals and pharmaceuticals
synthesis
-
diamine donors are used for effective equilibrium displacement of transaminase-mediated biotransformations. Whole-cell biotransformation using engineered Corynebacterium glutamicum cells, that produce diamine donors, is evaluated
synthesis
-
diamine donors are used for effective equilibrium displacement of transaminase-mediated biotransformations. Whole-cell biotransformation using engineered Corynebacterium glutamicum cells, that produce diamine donors, is evaluated
synthesis
-
diamine donors are used for effective equilibrium displacement of transaminase-mediated biotransformations. Whole-cell biotransformation using engineered Corynebacterium glutamicum cells, that produce diamine donors, is evaluated
synthesis
-
diamine donors are used for effective equilibrium displacement of transaminase-mediated biotransformations. Whole-cell biotransformation using engineered Corynebacterium glutamicum cells, that produce diamine donors, is evaluated
synthesis
-
biocatalytic transamination with near-stoichiometric inexpensive amine donors mediated by bifunctional mono- and di-amine transaminases. Both monoamine and diamine transaminase activity is reported, allowing conversion of a wide range of target ketone substrates with just a small excess of amine donor. The diamine co-substrates (putrescine, cadaverine or spermidine) are bio-derived and the enzyme system results in very little waste, making it a greener strategy for the production of valuable amine fine chemicals and pharmaceuticals
-
synthesis
-
biocatalytic transamination with near-stoichiometric inexpensive amine donors mediated by bifunctional mono- and di-amine transaminases. Both monoamine and diamine transaminase activity is reported, allowing conversion of a wide range of target ketone substrates with just a small excess of amine donor. The diamine co-substrates (putrescine, cadaverine or spermidine) are bio-derived and the enzyme system results in very little waste, making it a greener strategy for the production of valuable amine fine chemicals and pharmaceuticals
-
synthesis
-
biocatalytic transamination with near-stoichiometric inexpensive amine donors mediated by bifunctional mono- and di-amine transaminases. Both monoamine and diamine transaminase activity is reported, allowing conversion of a wide range of target ketone substrates with just a small excess of amine donor. The diamine co-substrates (putrescine, cadaverine or spermidine) are bio-derived and the enzyme system results in very little waste, making it a greener strategy for the production of valuable amine fine chemicals and pharmaceuticals
-
synthesis
-
biocatalytic transamination with near-stoichiometric inexpensive amine donors mediated by bifunctional mono- and di-amine transaminases. Both monoamine and diamine transaminase activity is reported, allowing conversion of a wide range of target ketone substrates with just a small excess of amine donor. The diamine co-substrates (putrescine, cadaverine or spermidine) are bio-derived and the enzyme system results in very little waste, making it a greener strategy for the production of valuable amine fine chemicals and pharmaceuticals
-
synthesis
-
biocatalytic transamination with near-stoichiometric inexpensive amine donors mediated by bifunctional mono- and di-amine transaminases. Both monoamine and diamine transaminase activity is reported, allowing conversion of a wide range of target ketone substrates with just a small excess of amine donor. The diamine co-substrates (putrescine, cadaverine or spermidine) are bio-derived and the enzyme system results in very little waste, making it a greener strategy for the production of valuable amine fine chemicals and pharmaceuticals
-
synthesis
-
biocatalytic transamination with near-stoichiometric inexpensive amine donors mediated by bifunctional mono- and di-amine transaminases. Both monoamine and diamine transaminase activity is reported, allowing conversion of a wide range of target ketone substrates with just a small excess of amine donor. The diamine co-substrates (putrescine, cadaverine or spermidine) are bio-derived and the enzyme system results in very little waste, making it a greener strategy for the production of valuable amine fine chemicals and pharmaceuticals
-
synthesis
-
biocatalytic transamination with near-stoichiometric inexpensive amine donors mediated by bifunctional mono- and di-amine transaminases. Both monoamine and diamine transaminase activity is reported, allowing conversion of a wide range of target ketone substrates with just a small excess of amine donor. The diamine co-substrates (putrescine, cadaverine or spermidine) are bio-derived and the enzyme system results in very little waste, making it a greener strategy for the production of valuable amine fine chemicals and pharmaceuticals
-
synthesis
-
biocatalytic transamination with near-stoichiometric inexpensive amine donors mediated by bifunctional mono- and di-amine transaminases. Both monoamine and diamine transaminase activity is reported, allowing conversion of a wide range of target ketone substrates with just a small excess of amine donor. The diamine co-substrates (putrescine, cadaverine or spermidine) are bio-derived and the enzyme system results in very little waste, making it a greener strategy for the production of valuable amine fine chemicals and pharmaceuticals
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, K.H.
Purification and properties of a diamine alpha-ketoglutarate transaminase from Escherichia coli
J. Biol. Chem.
239
783-786
1964
Escherichia coli
brenda
Kim, K.H.; Tchen, T.T.
Diamine-alpha-ketoglutarate aminotransferase (Escherichia coli)
Methods Enzymol.
17B
812-815
1971
Escherichia coli
-
brenda
Bascarn, V.; Snchez, L.; Hardisson, C.; Braa, A.F.
Stringent response and initiation of secondary metabolism in Streptomyces clavuligerus
J. Gen. Microbiol.
137
1625-1634
1991
Streptomyces clavuligerus
brenda
Madduri, K.; Stuttard, C.; Vining, L.C.
Lysine catabolism in Streptomyces spp. is primarily through cadaverine: beta-lactam producers also make alpha-aminoadipate
J. Bacteriol.
171
299-302
1989
Streptomyces phaeochromogenes, Amycolatopsis lactamdurans, Streptomyces clavuligerus, Streptomyces glaucescens, Streptomyces griseus, Streptomyces lividans, Streptomyces parvulus, Streptomyces rimosus, Streptomyces venezuelae, Streptomyces viridochromogenes, Streptomyces glaucescens GLAO, Streptomyces viridochromogenes CUB416, Streptomyces phaeochromogenes B2196, Streptomyces parvulus ISP5048, Streptomyces lividans TK24, Streptomyces clavuligerus NRRL 3585, Streptomyces griseus NRRL 3851, Streptomyces venezuelae ISP5230, Amycolatopsis lactamdurans NRRL 3802, Streptomyces rimosus NRRL 2234
brenda
Galman, J.; Slabu, I.; Weise, N.; Iglesias, C.; Parmeggiani, F.; Lloyd, R.; Turner, N.
Biocatalytic transamination with near-stoichiometric inexpensive amine donors mediated by bifunctional mono- and di-amine transaminases
Green Chem.
19
361-366
2017
Pseudomonas chlororaphis subsp. aureofaciens (A0A290U4C9), Pseudomonas putida (A0A4P8GNL5), Pseudomonas fluorescens (G8Q4R3), Pseudomonas aeruginosa (Q9I6J2), Pseudomonas aeruginosa ATCC 15692 (Q9I6J2), Pseudomonas fluorescens F113 (G8Q4R3), Pseudomonas aeruginosa 1C (Q9I6J2), Pseudomonas aeruginosa PRS 101 (Q9I6J2), Pseudomonas aeruginosa DSM 22644 (Q9I6J2), Pseudomonas aeruginosa CIP 104116 (Q9I6J2), Pseudomonas aeruginosa LMG 12228 (Q9I6J2), Pseudomonas aeruginosa JCM 14847 (Q9I6J2)
-
brenda
Grigoriou, S.; Kugler, P.; Kulcinskaja, E.; Walter, F.; King, J.; Hill, P.; Wendisch, V.F.; O'Reilly, E.
Development of a Corynebacterium glutamicum bio-factory for self-sufficient transaminase reactions
Green Chem.
22
4128-4132
2020
Pseudomonas putida, Pseudomonas chlororaphis subsp. aureofaciens, Pseudomonas fluorescens, Ruegeria pomeroyi
-
brenda
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