Primary Information |
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BoMiProt ID | Bomi47 |
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Protein Name | 3-hydroxybutyrate dehydrogenase type 2 |
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Organism | Bos taurus |
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Uniprot ID | Q3T046 |
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Milk Fraction | Exosome |
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Ref Sequence ID | NP_001029660.1 |
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Aminoacid Length | 245 |
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Molecular Weight | 26662 |
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FASTA Sequence |
Download |
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Gene Name | BDH2 |
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Gene ID | 515321 |
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Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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Presence in other biological fluids/tissue/cells | very low activity in
sheep liver mitochondria, whereas appreciable activity in the cytoplasmic
fraction of sheep liver and kidney |
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Protein Function | catalyses the reversible NAD-linked
oxidation of 3-h_ydroxybutyrate to acetoacetate; essential
for the last step in the production and the first
step in the utilization of D(-)-3-hydroxybutyrate |
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Biochemical Properties | enzyme is tightly bound to the mitochondrial membrane,
and when freed from this membrane has a
requirement for phosphatidylcholine; In sheep
kidney, this 'cytoplasmic 3-hydroxybutyrate dehydrogenase'
has been shown to react readily with L(+)-
3-hydroxybutyrate
and is
identical with L-gulonate-NAD oxidoreductase; enzymes extracted from liver, rumen epithelium and
kidney of sheep reacted with
acetoacetate; for the liver enzyme, the rate was
appreciably lower than with D(-)-3-hydroxybutyrate; enzyme activity is inhibited by phosphatidylcholine; The optimum pH for assay of the cytoplasmic
enzyme in sheep liver was 8.5 which is the same as
for the particulate enzyme in rat liver |
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Significance in milk | β-hydroxybutyrate is the major ketone body produced in bovine species by mammary gland - 3-hydroxybutyrate dehydrogenase catalyzes this substrate's utilization in mitochondria; the large increase in expression and relative mRNA abundance during lactation correspond with their enzymatic activity level in lactating rat mammary tissue |
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PTMs | Phosphorylation at Ser |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| |
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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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Additional Comments | increase in 3-hydroxybutyrate dehydrogenase
activity in the brain of ketonaemic rats and
sheep |
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Bibliography | 1. Watson, H. R., & Lindsay, D. B. (1972). 3-hydroxybutyrate dehydrogenase in tissues from normal and ketonaemic sheep. The Biochemical Journal, 128(1), 53–57. https://doi.org/10.1042/bj1280053. 2. Bionaz, M., & Loor, J. J. (2008). Gene networks driving bovine milk fat synthesis during the lactation cycle. BMC Genomics, 9. https://doi.org/10.1186/1471-2164-9-366. |