Berghäuser J, Schirmer R H
Biochim Biophys Acta. 1978 Dec 20;537(2):428-35. doi: 10.1016/0005-2795(78)90527-5.
Adenylate kinase (ATP:AMP phosphotransferase, EC 2.7.4.3) isolated from porcine skeletal and heart muscle and from rabbit muscle are inactivated when a single arginine residue is modified. In adenylate kinase from pig the modified residue was identified as Arg-97 by peptide-mapping. In native adenylate kinase Arg-97 is located at the bottom of the active site cleft. The protein fluorescence of modified adenylate kinase is reduced. Whereas the addition of AMP, ADP and MgATP quench the fluorescence of native adenylate kinase, the fluorescence of phenylglyoxal-modified adenylate kinase is only affected by ADP and MgATP. This finding is discussed in connection with the structural isomerization observed in native adenylate kinase by X-ray diffraction analysis.
从猪骨骼肌、心肌以及兔肌肉中分离出的腺苷酸激酶(ATP:AMP磷酸转移酶,EC 2.7.4.3),当单个精氨酸残基被修饰时会失活。通过肽图分析,在猪的腺苷酸激酶中,被修饰的残基被鉴定为精氨酸-97。在天然腺苷酸激酶中,精氨酸-97位于活性位点裂隙的底部。修饰后的腺苷酸激酶的蛋白质荧光降低。虽然添加AMP、ADP和MgATP会淬灭天然腺苷酸激酶的荧光,但苯乙二醛修饰的腺苷酸激酶的荧光仅受ADP和MgATP影响。结合通过X射线衍射分析在天然腺苷酸激酶中观察到的结构异构化对这一发现进行了讨论。