Johnson E A, Burke S K, Forage R G, Lin E C
J Bacteriol. 1984 Oct;160(1):55-60. doi: 10.1128/jb.160.1.55-60.1984.
Dihydroxyacetone (DHA) kinase of Klebsiella pneumoniae, a gene product of the dha regulon responsible for fermentative dissimilation of glycerol and DHA, was purified 120-fold to a final specific activity of 10 mumol X min-1 X mg of protein-1 at 30 degrees C. The enzyme, a dimer of a 53,000 +/- 5,000-dalton polypeptide, is highly specific for DHA (Km, ca.4 microM). Glycerol is not a substrate at 1 mM and is not an inhibitor even at 100 mM. The enzyme is not inhibited by 5 mM fructose-1,6-diphosphate. Ca2+ gives a higher enzyme activity than Mg2+ as a cationic cofactor. Escherichia coli glycerol kinase acts on both glycerol and DHA and is allosterically inhibited by fructose-1,6-diphosphate. Antibodies raised against E. coli glycerol kinase cross-reacted with K. pneumoniae glycerol kinase but not with K. pneumoniae DHA kinase.
肺炎克雷伯菌的二羟基丙酮（DHA）激酶是dha操纵子的基因产物，负责甘油和DHA的发酵异化作用，该酶在30℃下纯化了120倍，最终比活性为10 μmol·min⁻¹·mg蛋白质⁻¹。该酶是一种由53,000±5,000道尔顿多肽组成的二聚体，对DHA具有高度特异性（Km约为4 μM）。1 mM甘油不是底物，即使在100 mM时也不是抑制剂。该酶不受5 mM果糖-1,6-二磷酸的抑制。作为阳离子辅因子，Ca²⁺比Mg²⁺能赋予更高的酶活性。大肠杆菌甘油激酶作用于甘油和DHA，并受到果糖-1,6-二磷酸的变构抑制。针对大肠杆菌甘油激酶产生的抗体与肺炎克雷伯菌甘油激酶发生交叉反应，但不与肺炎克雷伯菌DHA激酶发生交叉反应。
