Substrate stereoselectivity of poly(Asp) hydrolase-1 capable of cleaving β-amide bonds as revealed by investigation of enzymatic hydrolysis of stereoisomeric β-tri(Asp)s.
作者： Tomohiro Hiraishi , Hideki Abe , Mizuo Maeda
DOI: 10.1186/S13568-015-0118-3
关键词:
摘要: We previously reported that poly(Asp) hydrolase-1 (PahZ1KP-2) from Pedobacter sp. KP-2 selectively, but not completely, cleaved the amide bonds between β-Asp units in thermally synthesized (tPAA). In present study, enzymatic hydrolysis of stereoisomeric β-tri(Asp)s by PahZ1KP-2 was investigated to clarify substrate stereoselectivity tPAA. The results suggest following structural features at its binding site: (1) active site contains four subsites (2, 1, −1, and −2), three which need be occupied Asp for cleavage occur; (2) proceed, subsite 1 should an l-Asp unit, whereas other may accept both l- d-Asp units; (3) two central occurs, (l-Asp)-(d-Asp) sequence is most favorable cleavage.
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