Roles of Ala-149 in the catalytic activity of diadenosine tetraphosphate phosphorylase from Mycobacterium tuberculosis H37Rv
Roles of Ala-149 in the catalytic activity of diadenosine tetraphosphate phosphorylase from Mycobacterium tuberculosis H37Rv
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Ala-149 在结核分枝杆菌 H37Rv 二腺苷四磷酸磷酸化酶催化活性中的作用
DOI：
10.1080/09168451.2014.973364
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发表时间：
2014
期刊：
影响因子：
--
通讯作者：
Shibayama K
中科院分区：
文献类型：
--
作者：
Mori S;Kim H;Rimbara E;Arakawa Y;Shibayama K
结核分枝杆菌H37 Rv（MtAPA）的二腺苷5′，5 ′-P1，P4-四磷酸（Ap 4A）磷酸化酶属于组氨酸三联体（HIT）超家族，但它是唯一一个在149位（Ala-149）有丙氨酸残基的酶。酶促分析显示，Ala-149缺失突变体对二腺苷5′，5 ′-P1，P5-五磷酸显示出底物特异性，并且对Ap 4A和野生型酶所利用的其他底物无活性。
Diadenosine 5′,5′′′-P1,P4-tetraphosphate (Ap4A) phosphorylase fromMycobacterium tuberculosisH37Rv (MtAPA) belongs to the histidine triad motif (HIT) superfamily, but is the only member with an alanine residue at position 149 (Ala-149). Enzymatic analysis revealed that the Ala-149 deletion mutant displayed substrate specificity for diadenosine 5′,5′′′-P1,P5-pentaphosphate and was inactive on Ap4A and other substrates that are utilized by the wild-type enzyme.