2015
DOI: 10.1074/jbc.m115.655399
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Asn-150 of Murine Erythroid 5-Aminolevulinate Synthase Modulates the Catalytic Balance between the Rates of the Reversible Reaction

Abstract: Background: 5-Aminolevulinate synthase (ALAS) catalyzes the initial step of mammalian heme biosynthesis. Results: N150H and N150F mutations significantly reduced the rate of quinonoid intermediate formation in the forward direction, while increasing the reverse reaction rate. Conclusion: Asn-150 is essential for establishing a catalytic balance between the forward and reverse reactions. Significance: This is the first report of an ALAS region modulating the ALA synthesis-breakdown balance.

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Cited by 5 publications
(1 citation statement)
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“…As an enzyme belongs to α-oxoamine synthase (AOS) family, ALAS adapts asparagine instead of histidine and phenylalanine which are widely observed at analogous site in the structure. The unusual amino acid usage is assumed that histidine and phenylalanine may impede the 5-ALA release and even result in balance shift to reverse reaction (Stojanovski and Ferreira 2015 ).…”
Section: Production Of 5-ala Via C4 Pathway In Escherichia ...mentioning
confidence: 99%
“…As an enzyme belongs to α-oxoamine synthase (AOS) family, ALAS adapts asparagine instead of histidine and phenylalanine which are widely observed at analogous site in the structure. The unusual amino acid usage is assumed that histidine and phenylalanine may impede the 5-ALA release and even result in balance shift to reverse reaction (Stojanovski and Ferreira 2015 ).…”
Section: Production Of 5-ala Via C4 Pathway In Escherichia ...mentioning
confidence: 99%