Biochemical characterization of TyrA enzymes from Ignicoccus hospitalis and Haemophilus influenzae: A comparative study of the bifunctional and monofunctional dehydrogenase forms

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• 作者：Irina Shlaifer ; Peter Kojo Quashie¹ ; Hyun Young Kim² ; Joanne L. Turnbull ; ^{Joanne.Turnbull@concordia.ca}
• 关键词：Chorismate mutase ; Prephenate dehydrogenase ; Ignicoccus hospitalis ; Aromatic amino acid biosynthesis ; TyrA ; Haemophilus influenzae
• 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：1865
• 期：3
• 页码：312-320
• 全文大小：1044 K
• 卷排序：1865

文摘

Bifunctional TyrA enzymes from 2 different organisms were expressed, and purified. An active, stable monofunctional dehydrogenase domain was identified and expressed. TyrAs differed with respect to thermal stability, cofactor preference and regulation. I. hospitalis TyrA may represent a unique class of prephenate dehydrogenases.