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Literature summary for 2.6.1.B3 extracted from

  • 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 (2010), J. Biotechnol., 145, 120-129.
    View publication on PubMed
Search for more literature for 2.6.1.B3

Application

Application Comment Organism
food industry enzymatic detoxification of fumonisins in animal feed and potentially also in foodstuffs intended for human consumption, improvement of food and feed safety Sphingopyxis macrogoltabida

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Sphingopyxis macrogoltabida

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
46300
-
 x * 46300, SDS-PAGE Sphingopyxis macrogoltabida

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol + pyruvate Sphingopyxis macrogoltabida (2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol i.e. aminopentoln (3S,5R,10S,12R,14R,15S,16S)-3,5,10,14,15-pentahydroxy-12,16-dimethylicosan-2-one + L-alanine
-
 ?

Organism

Organism UniProt Comment Textmining
Sphingopyxis macrogoltabida D2D3B2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol + pyruvate (2S,3S,5R,10S,12R,14R,15S,16S)-2-amino-12,16-dimethylicosane-3,5,10,14,15-pentol i.e. aminopentoln Sphingopyxis macrogoltabida (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 (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 Sphingopyxis macrogoltabida (3S,5R,10S,12R,14R,15S,16S)-3,5,10,14,15-pentahydroxy-12,16-dimethylicosan-2-one + L-alanine
-
 ?

Subunits

Subunits Comment Organism
? x * 46300, SDS-PAGE Sphingopyxis macrogoltabida

Synonyms

Synonyms Comment Organism
aminopentol:pyruvate aminotransferase
-
 Sphingopyxis macrogoltabida
FumI
-
 Sphingopyxis macrogoltabida
HFB1 deaminating activity
-
 Sphingopyxis macrogoltabida

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Sphingopyxis macrogoltabida

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Sphingopyxis macrogoltabida

Cofactor

Cofactor Comment Organism Structure
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 Sphingopyxis macrogoltabida