caa a22 4500 475746333 CHVBK 20180406123514.0 cr unu---uuuuu 170329e20000701xx s 000 0 eng 10.1007/s002840010094 doi (NATIONALLICENCE)springer-10.1007/s002840010094 News & Notes: Specificity of a Neutral Zn-Dependent Proteinase from Thermoactinomyces sacchari Toward the Oxidized Insulin B Chain [Elektronische Daten] [Dessislava N. Georgieva, Stanka Stoeva, Veneta Ivanova, Adriana Gusterova, Wolfgang Voelter] Abstract.: The proteolytic specificity of the neutral Zn-dependent proteinase from Thermoactinomyces sacchari was determined by analysis of the peptides obtained after incubation with the oxidized insulin B chain as a substrate. The enzyme is an endopeptidase with broad specificity. In total, 12 peptide bonds in the B chain of insulin were hydrolyzed. The major requirement is that a hydrophobic residue such as Leu, Val, or Phe should participate with the α-amino group in the bond to be cleaved. However, hydrolysis of bonds at the N-terminal side of His, Thr, and Gly was also observed. The peptide bond Leu 15-Tyr 16 in the oxidized insulin B chain, which is the major cleavage site for the alkaline microbial proteinases, is resistant to the attacks of the enzyme from Thermoactinomyces sacchari and other neutral proteinases. The proteolytic activity of the Zn-dependent proteinase from T. sacchari is different from those of other metalloendopeptidases from microorganisms. Springer-Verlag New York Inc., 2000 Georgieva Dessislava N. Institute of Organic Chemistry, Bulgarian Academy of Sciences, Sofia 1113, Bulgaria, BG aut Stoeva Stanka Abteilung für Physikalische Biochemie, Physiologisch-chemisches Institut der Universität Tübingen, Hoppe-Seyler-Str. 4, D-72076 Tübingen, Germany, DE aut Ivanova Veneta Institute of Microbiology, Bulgarian Academy of Sciences, Sofia 1113, Bulgaria, BG aut Gusterova Adriana Institute of Microbiology, Bulgarian Academy of Sciences, Sofia 1113, Bulgaria, BG aut Voelter Wolfgang Abteilung für Physikalische Biochemie, Physiologisch-chemisches Institut der Universität Tübingen, Hoppe-Seyler-Str. 4, D-72076 Tübingen, Germany, DE aut https://doi.org/10.1007/s002840010094 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s002840010094 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Georgieva Dessislava N. Institute of Organic Chemistry, Bulgarian Academy of Sciences, Sofia 1113, Bulgaria, BG aut NATIONALLICENCE 700 1- Stoeva Stanka Abteilung für Physikalische Biochemie, Physiologisch-chemisches Institut der Universität Tübingen, Hoppe-Seyler-Str. 4, D-72076 Tübingen, Germany, DE aut NATIONALLICENCE 700 1- Ivanova Veneta Institute of Microbiology, Bulgarian Academy of Sciences, Sofia 1113, Bulgaria, BG aut NATIONALLICENCE 700 1- Gusterova Adriana Institute of Microbiology, Bulgarian Academy of Sciences, Sofia 1113, Bulgaria, BG aut NATIONALLICENCE 700 1- Voelter Wolfgang Abteilung für Physikalische Biochemie, Physiologisch-chemisches Institut der Universität Tübingen, Hoppe-Seyler-Str. 4, D-72076 Tübingen, Germany, DE aut Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer