Murine erythroid 5-aminolevulinate synthase: Truncation of a disordered N-terminal extension is not detrimental for catalysis
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- 作者：Bosko M. Stojanovskia ; bstojano@health.usf.edu" class="auth_mail" title="E-mail the corresponding author ; Leonid Breydoa ; b ; Vladimir N. Uverskya ; b ; Gloria C. Ferreiraa ; c ; gferreir@health.usf.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：ALA ; 5-aminolevulinic acid ; ALAS1 ; non-specific isoform of 5-aminolevulinate synthase ; ALAS2 ; erythroid-specific isoform of 5-aminolevulinate synthase ; mALAS2 ; erythroid-specific isoform of murine 5-aminolevulinate synthase ; ΔmALAS2 ; erythroid-specific isoform of 5-aminolevulinate synthase with an N-terminal truncation ; hALAS1 ; non-specific isoform of human 5-aminolevulinate synthase ; hALAS2 ; erythroid-specific isoform of human 5-aminolevulinate synthase ; PLP ; pyridoxal 5&prime ; -phosphate ; SDS-P
- 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 出版年：2016
- 出版时间：May 2016
- 年：2016
- 卷：1864
- 期：5
- 页码：441-452
- 全文大小：2122 K
文摘
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Intrinsically disordered regions were identified in the N-terminus of mALAS2.
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Truncation of the N-terminal region subtly reduced the tertiary structure rigidity.
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Thermal denaturation analyses revealed a 4.3 °C reduction in the Tm of ΔmALAS2.
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The steady-state kinetic properties of mALAS2 are largely unperturbed.
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The N-terminal truncation modulates the active site PLP microenvironment.