Search by BoMiProt ID - Bomi6882


Primary Information

BoMiProt ID Bomi6882
Protein Name L-serine dehydratase/L-threonine deaminase/L-serine deaminase/L-threonine dehydratase/SDH
Organism Bos taurus
Uniprot IdQ0VCW4
Milk FractionWhey,MFGM
Ref Sequence Id NP_001069130.1
Aminoacid Length 327
Molecular Weight 34441
Fasta Sequence https://www.uniprot.org/uniprot/Q0VCW4.fasta
Gene Name SDS/SDH
Gene Id 514346
Protein Existence Status reviewed

Secondary Information

Protein Function involved in the pathway gluconeogenesis.
Biochemical Properties pyridoxal 5'-phosphate (P-5-P) dependent enzyme,affinity for 2 substrates L-serine and L-threonine to form a-ketobutyrate and pyruvate, respectively.L-Threonine deaminase is specifically inhibited by L-cysteine, D-cysteine.The Km values for serine and threonine of the recombinant enzyme were 67 and 50 mM,respectively
Significance in milk associated with milk cholesterol (CHL) metabolism
PTMs proteolytic cleavage from N terminal
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
NA
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs In E. coli, the N-terminal methionine residue is removed from the enzyme by posttranslational modification.
Additional Comments L-Threonine deaminase is under hormonal control and is clearly enhanced by amino acid diet.
Bibliography 1.Pagani R, Leoncini R, Pizzichini M, Vannoni D, Tabucchi A, Marinello E. Properties of rat liver L-threonine deaminase. Enzyme Protein. 1994-1995;48(2):90-7. doi: 10.1159/000474974. PMID: 7581747. 2.Pagani R, Leoncini R, Pizzichini M, Vannoni D, Tabucchi A, Marinello E. Properties of rat liver L-threonine deaminase. Enzyme Protein. 1994-1995;48(2):90-7. doi: 10.1159/000474974. PMID: 7581747.