Search by BoMiProt ID - Bomi47

Primary Information

BoMiProt ID Bomi47
Protein Name 3-hydroxybutyrate dehydrogenase type 2
Organism Bos taurus
Uniprot IDQ3T046
Milk FractionExosome
Ref Sequence ID NP_001029660.1
Aminoacid Length 245
Molecular Weight 26662
FASTA Sequence Download
Gene Name BDH2
Gene ID 515321
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondary Information

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
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
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
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
PTMs Phosphorylation at Ser
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Additional Comments increase in 3-hydroxybutyrate dehydrogenase activity in the brain of ketonaemic rats and sheep
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.
2. Bionaz, M., & Loor, J. J. (2008). Gene networks driving bovine milk fat synthesis during the lactation cycle. BMC Genomics, 9.