Kim Hyun-Soo, Golyshin Peter N, Timmis Kenneth N
Department of Environmental Microbiology, The Helmholtz Center for Infection Research, Braunschweig, Germany.
J Ind Microbiol Biotechnol. 2007 Nov;34(11):715-21. doi: 10.1007/s10295-007-0245-1. Epub 2007 Aug 1.
A metalloprotease induced by chitin in a new chitinolytic bacterium Serratia sp. Strain KCK was purified and characterized. Compared with other Serratia enzymes, it exhibited a rather broad pH activity range (pH 5.0-8.0), and thermostability. The cognate ORF, mpr, was cloned and expressed. Its deduced amino acid sequence showed high similarity to those of bacterial zinc-binding metalloproteases and a well-conserved serralysin family motif. Pretreatment of chitin with the Mpr protein promoted chitin degradation by chitinase A, which suggests that Mpr participates in, and facilitates, chitin degradation by this microorganism.
一种由几丁质诱导产生的金属蛋白酶在新型几丁质分解细菌粘质沙雷氏菌KCK菌株中得到了纯化和表征。与其他沙雷氏菌酶相比，它表现出相当宽的pH活性范围（pH 5.0 - 8.0）以及热稳定性。同源开放阅读框mpr被克隆并表达。其推导的氨基酸序列与细菌锌结合金属蛋白酶的序列高度相似，并且具有一个保守性良好的丝氨酸蛋白酶家族基序。用Mpr蛋白对几丁质进行预处理可促进几丁质酶A对几丁质的降解，这表明Mpr参与并促进了这种微生物对几丁质的降解。
