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Information on EC 2.6.1.B3 - aminopentol:pyruvate aminotransferase FumI
for references in articles please use BRENDA:EC2.6.1.B3preliminary BRENDA-supplied EC number
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2.6.1.B3 aminopentol:pyruvate aminotransferase FumISpecify your search results
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
aminotransferase fumi, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FumI
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol + pyruvate = (3S,5R,10S,12R,14R,15S,16S)-3,5,10,14,15-pentahydroxy-12,16-dimethylicosan-2-one + L-alanine
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol:pyruvate aminotransferase
-
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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
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol + oxaloacetate
(3S,5R,10S,12R,14R,15S,16S)-3,5,10,14,15-pentahydroxy-12,16-dimethylicosan-2-one + L-aspartate
-
-
-
-
?
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol + pyruvate
(3S,5R,10S,12R,14R,15S,16S)-3,5,10,14,15-pentahydroxy-12,16-dimethylicosan-2-one + L-alanine
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol + pyruvate
(3S,5R,10S,12R,14R,15S,16S)-3,5,10,14,15-pentahydroxy-12,16-dimethylicosan-2-one + L-alanine
the enzyme is involved in degradation of fumonisin B1. Fumonisin B1 is a mycotoxin produced by different phytopathogenic filamentous fungi
-
-
?
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol + pyruvate
(3S,5R,10S,12R,14R,15S,16S)-3,5,10,14,15-pentahydroxy-12,16-dimethylicosan-2-one + L-alanine
recombinant aminotransferase is able to deaminate HFB1 in the presence of pyruvate and pyridoxal 5'-phosphate
-
-
?
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol + pyruvate
(3S,5R,10S,12R,14R,15S,16S)-3,5,10,14,15-pentahydroxy-12,16-dimethylicosan-2-one + L-alanine
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol i.e. aminopentoln
-
-
?
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol + pyruvate
(3S,5R,10S,12R,14R,15S,16S)-3,5,10,14,15-pentahydroxy-12,16-dimethylicosan-2-one + L-alanine
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol i.e. aminopentol, i.e. hydrolyzed fumonisin B1. The enzyme is independent of oxygen
-
-
?
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol + pyruvate
(3S,5R,10S,12R,14R,15S,16S)-3,5,10,14,15-pentahydroxy-12,16-dimethylicosan-2-one + L-alanine
-
-
-
-
?
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol + pyruvate
(3S,5R,10S,12R,14R,15S,16S)-3,5,10,14,15-pentahydroxy-12,16-dimethylicosan-2-one + L-alanine
-
activity observed with glyoxylate and 2-oxobutyrate, no activity detectable with 2-oxogluarate, substrates hydrolyzed fumonisin B2 and B3 also used
-
-
?
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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
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol + pyruvate
(3S,5R,10S,12R,14R,15S,16S)-3,5,10,14,15-pentahydroxy-12,16-dimethylicosan-2-one + L-alanine
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol + pyruvate
(3S,5R,10S,12R,14R,15S,16S)-3,5,10,14,15-pentahydroxy-12,16-dimethylicosan-2-one + L-alanine
the enzyme is involved in degradation of fumonisin B1. Fumonisin B1 is a mycotoxin produced by different phytopathogenic filamentous fungi
-
-
?
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol + pyruvate
(3S,5R,10S,12R,14R,15S,16S)-3,5,10,14,15-pentahydroxy-12,16-dimethylicosan-2-one + L-alanine
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol i.e. aminopentoln
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
heterologously expressed aminotransferase deaminates hydrolyzed fumonisin B1 ((2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol) in the presence of pyruvate and pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
recombinant aminotransferase is able to deaminate (2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol in the presence of pyruvate and pyridoxal 5'-phosphate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol
-
substrate inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0011
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol
-
pH 8.0, 35°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.73
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol
-
pH 8.0, 35°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
activity reduced at pH 6.5 or less (1 h, 35°C), activity reduced at pH 8.0 (1 h)
724058
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged protein: immobilized metal ion affinity chromatography (Ni2+), maltose binding protein fusion protein: affinity chromatography (dextrin sepharose), cleavage of the fusion protein
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
His-tagged protein and maltose binding protein fusion protein expressed in different Escherichia coli (DE3) strains at different temeratures and different expression levels
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His-tagged protein expressed in Escherichia coli ArcticExpress (DE3), His-tag does not affect the enzymatic activity
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
enzymatic detoxification of fumonisins in animal feed and potentially also in foodstuffs intended for human consumption, improvement of food and feed safety
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heinl, S.; Hartinger, D.; Thamhesl, M.; Schatzmayr, G.; Moll, W.-D.; Grabherr, R.
An aminotransferase from bacterium ATCC 55552 deaminates hydrolyzed fumonisin B1
Biodegradation
22
25-30
2011
bacterium ATCC 55552 (E2E0Q4)
brenda
Heinl, S.; Hartinger, D.; Thamhesl, M.; Vekiru, E.; Krska, R.; Schatzmayr, G.; Moll, W.D.
Grabherr, R.: Degradation of fumonisin B1 by the consecutive action of two bacterial enzymes
J. Biotechnol.
145
120-129
2010
Sphingopyxis macrogoltabida (D2D3B2)
brenda
Hartinger, D.; Schwartz, H.; Hametner, C.; Schatzmayr, G.; Haltrich, D.; Moll, W.D.
Enzyme characteristics of aminotransferase FumI of Sphingopyxis sp. MTA144 for deamination of hydrolyzed fumonisin B1
Appl. Microbiol. Biotechnol.
91
757-768
2011
Sphingopyxis sp.
brenda
Hartinger, D.; Heinl, S.; Schwartz, H.E.; Grabherr, R.; Schatzmayr, G.; Haltrich, D.; Moll, W.D.
Enhancement of solubility in Escherichia coli and purification of an aminotransferase from Sphingopyxis sp. MTA144 for deamination of hydrolyzed fumonisin B1
Microb. Cell Fact.
9
62
2010
Sphingopyxis sp.
brenda
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Release 2023.1 (January 2023)
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