来自海洋无脊椎动物的三磷酸腺苷激活的腺苷酸脱氨酶。沙蠋（Arenicola cristata）体壁肌肉中该酶的性质。
Adenosine triphosphate-activated adenylate deaminase from marine invertebrate animals. Properties of the enzyme from lugworm (Arenicola cristata) body-wall muscle.
作者信息
Gibbs K L, Bishop S H
出版信息
Biochem J. 1977 Jun 1;163(3):511-6. doi: 10.1042/bj1630511.
Adenylate deaminase (AMP aminohydrolase, EC 3.5.4.6) from lugworm (Arenicola cristata) body-wall muscle was partially purified by extraction in KCl solutions and chromatography on phosphocellulose. Enzyme activity was eluted from the column at two salt concentrations. Both forms show co-operative binding of AMP (Hill coefficient, h, 2.85) with s0.5 values of 20 mM and 15.6 mM. ATP and ADP act as positive effectors lowering h to 1.07 and s0.5 to 2mM. The apparent Ka (activation) for ATP was 1.5mM. GTP is an inhibitor with an apparent Ki of 0.12 mM. In vivo the ATP-activated adenylate deaminase is in the active form and may be regulated by changes in GTP concentrations. Adenylate deaminase may act as a primary ammonia-forming enzyme in ammonotelic marine invertebrates with the purine nucleotide cycle.
通过在氯化钾溶液中提取并在磷酸纤维素上进行色谱分离，对沙蠋（Arenicola cristata）体壁肌肉中的腺苷酸脱氨酶（AMP氨基水解酶，EC 3.5.4.6）进行了部分纯化。酶活性在两个盐浓度下从柱上洗脱下来。两种形式均显示出AMP的协同结合（希尔系数，h，2.85），s0.5值分别为20 mM和15.6 mM。ATP和ADP作为正效应物，将h降低至1.07，s0.5降低至2 mM。ATP的表观Ka（激活）为1.5 mM。GTP是一种抑制剂，表观Ki为0.12 mM。在体内，ATP激活的腺苷酸脱氨酶处于活性形式，可能受GTP浓度变化的调节。在具有嘌呤核苷酸循环的排氨型海洋无脊椎动物中，腺苷酸脱氨酶可能作为主要的产氨酶。
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