Converting tissue plasminogen activator to a zymogen: a regulatory triad of Asp-His-Ser.
Converting tissue plasminogen activator to a zymogen: a regulatory triad of Asp-His-Ser.
复制标题
将组织纤溶酶原激活剂转化为酶原:Asp-His-Ser 的调节三联体。
作者:
E. Madison;A. Kobe;M. Gething;J. Sambrook;E. Goldsmith
Unlike most serine proteases of the chymotrypsin family, tissue-type plasminogen activator (tPA) is secreted from cells as an active, single-chain enzyme with a catalytic efficiency only slightly lower than that of the proteolytically cleaved form. A zymogenic mutant of tPA has been engineered that displays a reduction in catalytic efficiency by a factor of 141 in the single-chain form while retaining full activity in the cleaved form. The residues introduced in the mutant, serine 292 and histidine 305, are proposed to form a hydrogen-bonded network with aspartate 477, similar to the aspartate 194-histidine 40-serine 32 network found to stabilize the zymogen chymotrypsinogen.
影响因子:
20.3
作者:
Silverberg,M;Kaplan,AP
通讯作者:
Kaplan,AP
DOI:
10.1016/0002-9343(88)90586-4
发表时间:
1988
期刊:
The American journal of medicine
影响因子:
--
作者:
Califf,RM;Topol,EJ;George,BS;Boswick,JM;Abbottsmith,C;Sigmon,KN;Candela,R;Masek,R;Kereiakes,D;O'Neill,WW
通讯作者:
O'Neill,WW