Leibniz Institute on Aging - Fritz Lipmann Institute, Beutenbergstr. 11, D-07745, Jena, Germany.
Pharmaceutical Biochemistry and Bioanalytics, Pharmaceutical Institute, University of Bonn, An der Immenburg 4, D-53121, Bonn, Germany.
Sci Rep. 2018 Feb 6;8(1):2474. doi: 10.1038/s41598-018-20841-z.
Cystathionine-β-synthase (CBS) belongs to a large family of pyridoxal 5'-phosphate (PLP)-dependent enzymes, responsible for the sulfur metabolism. The heme-dependent protein CBS is part of regulatory pathways also involving the gasotransmitter hydrogen sulfide. Malfunction of CBS can lead to pathologic conditions like cancer, cardiovascular and neurodegenerative disorders. Truncation of residues 1-40, absent in X-ray structures of CBS, reduces but does not abolish the activity of the enzyme. Here we report the NMR resonance assignment and heme interaction studies for the N-terminal peptide stretch of CBS. We present NMR-spectral evidence that residues 1-40 constitute an intrinsically disordered region in CBS and interact with heme via a cysteine-proline based motif.
胱硫醚-β-合酶（CBS）属于吡哆醛 5′-磷酸（PLP）依赖性酶大家族，负责硫代谢。依赖血红素的蛋白 CBS 是涉及气体递质硫化氢的调节途径的一部分。CBS 的功能障碍可导致病态，如癌症、心血管和神经退行性疾病。残基 1-40 的截断，在 CBS 的 X 射线结构中不存在，降低但没有消除酶的活性。本文报道了 CBS 中 N 端肽段的 NMR 共振分配和血红素相互作用研究。我们提供了 NMR 光谱证据，表明残基 1-40 构成 CBS 中的一个固有无序区域，并通过基于半胱氨酸-脯氨酸的基序与血红素相互作用。
