The Role of Electrostatics at the Catalytic Metal Binding Site in Xylose Isomerase Action
作者： B. Asbóth , Z. Böcskei , M. Fuxreiter , G. Náray-Szabó
DOI: 10.1007/978-94-011-5171-9_19
关键词:
摘要: D-xylose isomerase (EC 5.3.1.5) catalyses the reversible conversion of to D-xylulose and is also capable converting other sugars from aldose ketose [1]. It latter activity on glucose fructose, that accounts for fact it one most widely used industrial enzymes. active in oligomeric forms requires Mg2+, Co2+ or Mn2+ activation while divalent cations, e.g Zn2+, Ba2+ Cu2+ Ca2+ inhibit catalysis [2]. The effect cation practical importance since a preceding enzyme starch bioconversion process, α-amylase, only presence calcium ions, removal which an ion exchange step.
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