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BDH1  -  3-hydroxybutyrate dehydrogenase, type 1

Bos taurus

 
 
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High impact information on BDH1

 

Biological context of BDH1

  • The above results suggest that N3-NAD can be used for photoaffinity labeling of BDH at the active site [6].
 

Anatomical context of BDH1

  • D(-)beta-hydroxybutyrate dehydrogenase (BDH) purified from bovine heart mitochondria contains essential thiol and carboxyl groups [7].
  • The apparent Km for the negatively charged substrates of D-beta-hydroxybutyrate dehydrogenase increased as the membranes were reacted with phospholipase D. There was a 10-fold increase in the apparent Km for NADH when the content of acidic phospholipids was increased by 24% [8].
  • This study shows that apo-BDH, purified from bovine-heart mitochondria, and phospholipid-reconstituted BDH appear to be polydisperse [9].
 

Associations of BDH1 with chemical compounds

  • A tryptic BDH peptide labeled at an essential thiol with [3H]N-ethylmaleimide (NEM), and another tryptic peptide labeled at an essential carboxyl with N,N'-dicyclohexyl [14C]carbodiimide (DCCD), were isolated and sequenced [7].
  • The photoinhibition of BDH in the presence of N3-NAD was prevented nearly completely by addition of NADH, NAD plus beta-hydroxybutyrate, or NAD plus 2-methylmalonate and partially by addition of NAD [6].
  • Data presented in this paper suggest that D-(-)-beta-hydroxybutyrate dehydrogenase (BDH) purified from bovine heart mitochondria contains an essential carboxyl group and an essential histidyl residue at or near the active site [4].
  • In the dark, arylazido-beta-alanylnicotinamide adenine dinucleotide (N3-NAD) can replace NAD as cofactor for D-(-)-beta-hydroxybutyrate dehydrogenase (BDH) purified from bovine heart mitochondria [5].
  • Moreover, the presence of NADH prevented, and prior partial modification of BDH at the NAD(H)-protectable site by N-ethylmaleimide decreased, the incorporation of radioactivity into BDH from photoirradiated [3H]N3-NAD [6].
 

Analytical, diagnostic and therapeutic context of BDH1

  • The role of phospholipid in the binding of coenzyme, NAD(H), to 3-hydroxybutyrate dehydrogenase, a lipid-requiring membrane enzyme, has been studied with the ultrafiltration binding method, which we optimized to quantitate weak ligand binding (KD in the range 10-100 microM) [10].

References

  1. Preparation of a homogeneous soluble D-beta-hydroxybutyrate apodehydrogenase from mitochondria. Bock, H., Fleischer, S. J. Biol. Chem. (1975) [Pubmed]
  2. Effect of selective thiol-group derivatization on enzyme kinetics of (R)-3-hydroxybutyrate dehydrogenase. Dalton, L.A., McIntyre, J.O., Fleischer, S. Biochem. J. (1993) [Pubmed]
  3. Cooperativity in lipid activation of 3-hydroxybutyrate dehydrogenase: role of lecithin as an essential allosteric activator. Cortese, J.D., McIntyre, J.O., Duncan, T.M., Fleischer, S. Biochemistry (1989) [Pubmed]
  4. Inactivation of D-(-)-beta-hydroxybutyrate dehydrogenase by modifiers of carboxyl and histidyl groups. Prasad, P.V., Hatefi, Y. Biochemistry (1986) [Pubmed]
  5. Amino acid sequence of the nucleotide-binding site of D-(-)-beta-hydroxybutyrate dehydrogenase labeled with arylazido-beta-[3-3H]alanylnicotinamide adenine dinucleotide. Yamaguchi, M., Chen, S., Hatefi, Y. Biochemistry (1986) [Pubmed]
  6. Photoaffinity labeling of D-(-)-beta-hydroxybutyrate dehydrogenase by (arylazido)-beta-alanyl-substituted nicotinamide adenine dinucleotide. Yamaguchi, M., Chen, S., Hatefi, Y. Biochemistry (1985) [Pubmed]
  7. Amino acid sequences of two tryptic peptides from D(-)-beta-hydroxybutyrate dehydrogenase radiolabeled at essential carboxyl and sulfhydryl groups. Prasad, P.V., Hatefi, Y. Biochem. Int. (1986) [Pubmed]
  8. Use of phospholipase D to alter the surface charge of membranes and its effect on the enzymatic activity of D-beta-hydroxybutyrate dehydrogenase. Clancy, R.M., Wissenberg, A.R., Glaser, M. Biochemistry (1981) [Pubmed]
  9. Role of phospholipids in activation of mitochondrial D(-)-beta-hydroxybutyrate dehydrogenase. Prasad, P.V., Yamaguchi, M., Hatefi, Y. Biochem. Int. (1986) [Pubmed]
  10. Coenzyme binding by 3-hydroxybutyrate dehydrogenase, a lipid-requiring enzyme: lecithin acts as an allosteric modulator to enhance the affinity for coenzyme. Rudy, B., Dubois, H., Mink, R., Trommer, W.E., McIntyre, J.O., Fleischer, S. Biochemistry (1989) [Pubmed]
 
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