Active-site geometry of proteinase K
作者： Christian Betzel , Gour P. Pal , Mark Struck , Klaus-Dieter Jany , Wolfram Saenger
DOI: 10.1016/0014-5793(86)80307-6
关键词: Beta sheet 、 Ketone 、 Stereochemistry 、 Crystallography 、 Dipeptide 、 Chemistry 、 Proteinase K 、 Oxyanion hole 、 Active site 、 Endopeptidase K 、 Subtilisin
摘要: Proteinase K (EC 3.4.21.14) from the fungus Tritirachium album Limber is most active known serine endopeptidase. The sequence of its 275-residue long polypeptide chain and three-dimensional folding show a high degree homology with bacterial subtilisin proteases. Using difference Fourier methods, binding mode synthetic carbobenzoxy-Ala-Ala-chloromethyl ketone inhibitor to site proteinase was determined. In several cycles restrained least-squares, enzyme-inhibitor complex refined current R = 22% for 9400 X-ray diffraction data between 2.2 5.0 A resolution. attached by two covalent bonds: one methylene carbon N epsilon 2 catalytic His 68, other atom O gamma Ser 221. addition, hydrogen bonds donated peptide NH 221 side NH2 Asn 160 hold hemiketal O- in oxyanion hole. further bonded three-stranded antiparallel pleated sheet.
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