Primary Information |
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| BoMiProt ID | Bomi6882 |
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| Protein Name | L-serine dehydratase/L-threonine deaminase/L-serine deaminase/L-threonine dehydratase/SDH |
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| Organism | Bos taurus |
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| Uniprot ID | Q0VCW4 |
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| Milk Fraction | Whey,MFGM |
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| Ref Sequence ID | NP_001069130.1 |
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| Aminoacid Length | 327 |
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| Molecular Weight | 34441 |
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| FASTA Sequence |
Download |
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| Gene Name | SDS/SDH |
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| Gene ID | 514346 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | involved in the pathway gluconeogenesis. |
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| 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 |
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| Significance in milk | associated with milk cholesterol (CHL) metabolism |
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| PTMs | proteolytic cleavage from N terminal |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| NA |
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | In E. coli, the N-terminal methionine residue is removed from the enzyme by posttranslational modification. |
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| Additional Comments | L-Threonine deaminase is under hormonal control and is clearly enhanced by amino acid diet. |
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| 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. |
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