5-Aminolevulinic acid synthase: mechanism, mutations and medicine. - Wikidata - awgldk - TriplyDB

5-Aminolevulinic acid synthase: mechanism, mutations and medicine.

5-Aminolevulinic acid synthase: mechanism, mutations and medicine.

http://www.wikidata.org/entity/Q34189589

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Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans.Inhibitory effects of palm tocotrienol-rich fraction supplementation on bilirubin-metabolizing enzymes in hyperbilirubinemic adult rats An ATP and oxalate generating variant tricarboxylic acid cycle counters aluminum toxicity in Pseudomonas fluorescens.Serine 254 enhances an induced fit mechanism in murine 5-aminolevulinate synthase.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.Asn-150 of Murine Erythroid 5-Aminolevulinate Synthase Modulates the Catalytic Balance between the Rates of the Reversible Reaction The glycine deportation system and its pharmacological consequences.The power plant of the cell is also a smithy: the emerging role of mitochondria in cellular iron homeostasis.Current evaluation and management of anemia in patients with inflammatory bowel disease.A novel hemizygous I418S mutation in the ALAS2 gene in a young Korean man with X-linked sideroblastic anemia.Occurrence of two 5-aminolevulinate biosynthetic pathways in Streptomyces nodosus subsp. asukaensis is linked with the production of asukamycin.Arg-85 and Thr-430 in murine 5-aminolevulinate synthase coordinate acyl-CoA-binding and contribute to substrate specificity.Detection and characterization of a thermophilic biotin biosynthetic enzyme, 7-keto-8-aminopelargonic acid synthase, from various thermophiles.A novel mutation, Ile289Thr, in the ALAS2 gene in a family with pyridoxine responsive sideroblastic anaemia.Investigating the bifunctionality of cyclizing and "classical" 5-aminolevulinate synthases.Arg452 substitution of the erythroid-specific 5-aminolaevulinate synthase, a hot spot mutation in X-linked sideroblastic anaemia, does not itself affect enzyme activity.Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme.Insulin resistance and glycine metabolism in humans.Birth, death and horizontal transfer of the fumonisin biosynthetic gene cluster during the evolutionary diversification of Fusarium.Suicide inhibition of α-oxamine synthases: structures of the covalent adducts of 8-amino-7-oxononanoate synthase with trifluoroalanine

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P2860

5-Aminolevulinic acid synthase: mechanism, mutations and medicine.

http://www.wikidata.org/entity/Q34189589

description

2003 nî lūn-bûn

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2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2003 թվականի ապրիլին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

5-Aminolevulinic acid synthase: mechanism, mutations and medicine.

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5-Aminolevulinic acid synthase: mechanism, mutations and medicine.

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5-Aminolevulinic acid synthase: mechanism, mutations and medicine.

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5-Aminolevulinic acid synthase: mechanism, mutations and medicine.

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5-Aminolevulinic acid synthase: mechanism, mutations and medicine.

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5-Aminolevulinic acid synthase: mechanism, mutations and medicine.

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5-Aminolevulinic acid synthase: mechanism, mutations and medicine.

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5-Aminolevulinic acid synthase: mechanism, mutations and medicine.

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5-Aminolevulinic acid synthase: mechanism, mutations and medicine.

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S1570-9639(03)00095-5

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Biochimica et Biophysica Acta

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5-Aminolevulinic acid synthase: mechanism, mutations and medicine.

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Dmitriy Alexeev

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I Donald Kahari

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Ipsita Roy

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Lindsay Sawyer

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Muhammad Sarwar

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Peter M Shoolingin-Jordan

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Robert L Baxter

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Shu-Fen Wang

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Sooad Al-Daihan

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Sylvia S Bottomley

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361-366

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scholarly article

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10.1016/S1570-9639(03)00095-5

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1-2

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