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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and characterization of the dehydrogenase domain from rat peroxisomal multifunctional enzyme type 1.
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Crystallization and characterization of the dehydrogenase domain from rat peroxisomal multifunctional enzyme type 1.

机译：结晶和表征从老鼠的酶脱氢酶域多功能酶1型。

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摘要

Peroxisomal multifunctional enzyme type 1 from rat (perMFE-1) is a monomeric multidomain protein shown to have 2-enoyl-CoA hydratase/Delta(3)-Delta(2)-enoyl-CoA isomerase and (3S)-hydroxyacyl-CoA dehydrogenase domains followed by a C-terminal extension of 130 amino acids with unknown function apart from being a carrier of the peroxisomal targeting signal type 1. The truncated perMFE-1 without the N-terminal hydratase/isomerase domain (perMFE-1DH; residues 260-722) was overexpressed as an enzymatically active recombinant protein, purified and characterized. Using (3S)-hydroxydecanoyl-CoA as a substrate, the specific enzymatic activity of perMFE-1DH was determined to be 2.2 micromol min(-1) mg(-1), comparable with that of perMFE-1 purified from rat liver (2.8 micromol min(-1) mg(-1)). The protein was crystallized in the apo form by the hanging-drop method and a complete data set to 2.45 A resolution was collected using a rotating-anode X-ray source. The crystals have primitive tetragonal symmetry, with unit-cell parameters a = b = 125.9, c = 60.2 A.
机译：过氧化物酶病1型多功能酶从老鼠(perMFE-1)是一个单体的多畴的蛋白质证明有2-enoyl-CoA水合酶/δ(3)-它(2)-enoyl-CoA异构酶和(3 s) -hydroxyacyl-CoA脱氢酶域紧随其后的是一个c端130个氨基酸的延伸酸和未知函数除了一个过氧化物酶病目标信号的载波类型1. 水合酶/异构酶域(perMFE-1DH;260 - 722)是作为酶过表达活跃的重组蛋白纯化,为特征。底物的特定酶活性2.2 micromol perMFE-1DH决心分钟(1)毫克(1),与perMFE-1可比纯化大鼠肝脏(2.8 micromol min (1)毫克(1))。由悬滴法和一个完整的形式分辨率收集使用数据集到2.45旋转阳极x射线源。原始的正方对称,单胞参数a = b = 125.9, c = 60.2。

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