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Journal Abstract Search

176 related items for PubMed ID: 12686158

  • 1. 5-Aminolevulinic acid synthase: mechanism, mutations and medicine.
    Shoolingin-Jordan PM, Al-Daihan S, Alexeev D, Baxter RL, Bottomley SS, Kahari ID, Roy I, Sarwar M, Sawyer L, Wang SF.
    Biochim Biophys Acta; 2003 Apr 11; 1647(1-2):361-6. PubMed ID: 12686158
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  • 3. Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans.
    Astner I, Schulze JO, van den Heuvel J, Jahn D, Schubert WD, Heinz DW.
    EMBO J; 2005 Sep 21; 24(18):3166-77. PubMed ID: 16121195
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  • 6. Unstable reaction intermediates and hysteresis during the catalytic cycle of 5-aminolevulinate synthase: implications from using pseudo and alternate substrates and a promiscuous enzyme variant.
    Stojanovski BM, Hunter GA, Jahn M, Jahn D, Ferreira GC.
    J Biol Chem; 2014 Aug 15; 289(33):22915-22925. PubMed ID: 24920668
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  • 11. Murine erythroid 5-aminolevulinate synthase: Adenosyl-binding site Lys221 modulates substrate binding and catalysis.
    Stojanovski BM, Ferreira GC.
    FEBS Open Bio; 2015 Aug 15; 5():824-31. PubMed ID: 26605136
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  • 15. Elucidating the Role of Human ALAS2 C-terminal Mutations Resulting in Loss of Function and Disease.
    Taylor JL, Ayres-Galhardo PH, Brown BL.
    Biochemistry; 2024 Jul 02; 63(13):1636-1646. PubMed ID: 38888931
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  • 17. Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme.
    Brown BL, Kardon JR, Sauer RT, Baker TA.
    Structure; 2018 Apr 03; 26(4):580-589.e4. PubMed ID: 29551290
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  • 19. Investigating the bifunctionality of cyclizing and "classical" 5-aminolevulinate synthases.
    Liu J, Kaganjo J, Zhang W, Zeilstra-Ryalls J.
    Protein Sci; 2018 Feb 03; 27(2):402-410. PubMed ID: 29027286
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  • 20. Aspartate-279 in aminolevulinate synthase affects enzyme catalysis through enhancing the function of the pyridoxal 5'-phosphate cofactor.
    Gong J, Hunter GA, Ferreira GC.
    Biochemistry; 1998 Mar 10; 37(10):3509-17. PubMed ID: 9521672
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