PMID- 10329704
OWN - NLM
STAT- MEDLINE
DCOM- 19990709
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 21
DP  - 1999 May 21
TI  - Human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase is a
      single-domain multifunctional enzyme. Characterization of a novel
      17beta-hydroxysteroid dehydrogenase.
PG  - 15014-9
AB  - Human brain short chain L-3-hydroxyacyl-CoA dehydrogenase (SCHAD) was found to
      catalyze the oxidation of 17beta-estradiol and dihydroandrosterone as well as
      alcohols. Mitochondria have been demonstrated to be the proper location of this
      NAD+-dependent dehydrogenase in cells, although its primary structure is
      identical to an amyloid beta-peptide binding protein reportedly associated with
      the endoplasmic reticulum (ERAB). This fatty acid beta-oxidation enzyme was
      identified as a novel 17beta-hydroxysteroid dehydrogenase responsible for the
      inactivation of sex steroid hormones. The catalytic rate constant of the purified
      enzyme was estimated to be 0.66 min-1 with apparent Km values of 43 and 50 microM
      for 17beta-estradiol and NAD+, respectively. The catalytic efficiency of this
      enzyme for the oxidation of 17beta-estradiol was comparable with that of
      peroxisomal 17beta-hydroxysteroid dehydrogenase type 4. As a result, the human
      SCHAD gene product, a single-domain multifunctional enzyme, appears to function
      in two different pathways of lipid metabolism. Because the catalytic functions of
      human brain short chain L-3-hydroxyacyl-CoA dehydrogenase could weaken the
      protective effects of estrogen and generate aldehydes in neurons, it is proposed 
      that a high concentration of this enzyme in brain is a potential risk factor for 
      Alzheimer's disease.
FAU - He, X Y
AU  - He XY
AD  - Departments of Pharmacology, New York State Institute for Basic Research in
      Developmental Disabilities, Staten Island, New York 10314, USA.
FAU - Merz, G
AU  - Merz G
FAU - Mehta, P
AU  - Mehta P
FAU - Schulz, H
AU  - Schulz H
FAU - Yang, S Y
AU  - Yang SY
LA  - eng
GR  - DK47392/DK/NIDDK NIH HHS/United States
GR  - HL30847/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Alcohols)
RN  - EC 1.1.- (17-Hydroxysteroid Dehydrogenases)
RN  - EC 1.1.1.- (3-Hydroxyacyl CoA Dehydrogenases)
RN  - EC 1.1.1.35 (HSD17B10 protein, human)
SB  - IM
MH  - 17-Hydroxysteroid Dehydrogenases/*isolation & purification
MH  - 3-Hydroxyacyl CoA Dehydrogenases/*chemistry/metabolism
MH  - Alcohols/metabolism
MH  - Amino Acid Sequence
MH  - Brain/cytology/*enzymology
MH  - Humans
MH  - Molecular Sequence Data
MH  - Oxidation-Reduction
EDAT- 1999/05/18 00:00
MHDA- 1999/05/18 00:01
CRDT- 1999/05/18 00:00
PHST- 1999/05/18 00:00 [pubmed]
PHST- 1999/05/18 00:01 [medline]
PHST- 1999/05/18 00:00 [entrez]
AID - 10.1074/jbc.274.21.15014 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 May 21;274(21):15014-9. doi: 10.1074/jbc.274.21.15014.