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Characterization of Recombinant L-Amino Acid Deaminase of Proteus mirabilis

机译：变形菌变形杆菌L-氨基酸脱氨酶的表征

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摘要

L-amino acid deaminases catalyze the deamination of L-amino acids. Up until now, two types of L-amino acid deaminase have been identified in Proteus species. To investigate enzymatic characteristics of L-amino acid deaminase from Proteus mirabilis, L-amino acid deaminase encoding gene (pmta) was cloned from P. mirabilis T-l. Prokaryotic expression system was established to express recombinant Pmta. Enzymatic characteristics of the enzymes were analyzed. Results showed that recombinant Pmta exhibited function of second type of L-amino acid deaminase. The Km and Vmax value of Pmta for histidine was 10.57 mmol/L and 202.06 μmol/min/mg, respectively. The optimal temperature and pH of recombinant Pmta was 40 °C and 7.0. The enzymatic characteristics of Pmta were different from those of Pml discovered in P. mirabilis KCTC, which was probably due to different amino acid sequences. The Pmta deaminase will be very useful in the preparation of commercially valuable materials including urocanic acid and 3-mercaptopyruvic acid.
机译：L-氨基酸脱氨基酶催化L-氨基酸的脱氨基。迄今为止，在变形杆菌属中已鉴定出两种类型的L-氨基酸脱氨酶。为了研究奇异变形杆菌的L-氨基酸脱氨酶的酶学特征，从奇异假单胞菌T-1克隆了L-氨基酸脱氨酶编码基因（pmta）。建立了表达重组Pmta的原核表达系统。分析了酶的酶学特征。结果表明重组Pmta表现出第二种类型的L-氨基酸脱氨酶的功能。组氨酸的Pmta的Km和Vmax值分别为10.57 mmol / L和202.06μmol/ min / mg。重组Pmta的最佳温度和pH为40°C和7.0。 Pmta的酶学特征不同于奇异假单胞菌KCTC中发现的Pml的酶学特征，这可能是由于氨基酸序列不同所致。 Pmta脱氨酶在制备包括尿烷酸和3-巯基丙酮酸的商业上有价值的材料中将非常有用。

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