TY - JOUR
T1 - Purification and characterization of D(-)-β-hydroxybutyrate dehydrogenase from Azospirillum brasilense Cd
AU - Tal, S.
AU - Smirnoff, P.
AU - Okon, Y.
PY - 1990
Y1 - 1990
N2 - D(-)-β-hydroxybutyrate dehydrogenase (BOHB-DH) (EC 1.1.1.30) was purified 991-fold from Azospirillum brasilense Cd. Its specific activity was 5650 units (mg protein)-1 min-1. The enzyme is a tetramer, with identical subunits and a total molecular mass of 100 kDa. BOHB-DH is not a glycoprotein. It is acidic and contains six disulphide bonds without free -SH groups. Under the assay conditions used, BOHB-DH activity was maximal at pH 8.0 and at 36°C. The enzyme is an NAD+ oxidoreductase, and is inhibited by NADPH and NADH. It has high affinity for β-hydroxybutyrate: the K(m) value for the β-hydroxybutyrate substrate is 1 mM. Adenosine phosphates, pyruvate, acetyl-coenzyme A, oxaloacetate and 2-oxoglutarate inhibited purified BOHB-DH.
AB - D(-)-β-hydroxybutyrate dehydrogenase (BOHB-DH) (EC 1.1.1.30) was purified 991-fold from Azospirillum brasilense Cd. Its specific activity was 5650 units (mg protein)-1 min-1. The enzyme is a tetramer, with identical subunits and a total molecular mass of 100 kDa. BOHB-DH is not a glycoprotein. It is acidic and contains six disulphide bonds without free -SH groups. Under the assay conditions used, BOHB-DH activity was maximal at pH 8.0 and at 36°C. The enzyme is an NAD+ oxidoreductase, and is inhibited by NADPH and NADH. It has high affinity for β-hydroxybutyrate: the K(m) value for the β-hydroxybutyrate substrate is 1 mM. Adenosine phosphates, pyruvate, acetyl-coenzyme A, oxaloacetate and 2-oxoglutarate inhibited purified BOHB-DH.
UR - http://www.scopus.com/inward/record.url?scp=0025219730&partnerID=8YFLogxK
U2 - 10.1099/00221287-136-4-645
DO - 10.1099/00221287-136-4-645
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AN - SCOPUS:0025219730
SN - 0022-1287
VL - 136
SP - 645
EP - 649
JO - Journal of General Microbiology
JF - Journal of General Microbiology
IS - 4
ER -