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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2017, Volume 114, Issue 38, pp. E8045 - E8052
Journal Article
Biochemistry, ISSN 0006-2960, 09/2015, Volume 54, Issue 36, pp. 5617 - 5631
Journal Article
Journal Article
Journal Article
Structure, ISSN 0969-2126, 04/2018, Volume 26, Issue 4, pp. 580 - 589.e4
5-Aminolevulinic acid synthase (ALAS) catalyzes the first step in heme biosynthesis. We present the crystal structure of a eukaryotic ALAS from Saccharomyces... 
ClpX | AAA+ unfoldase | porphyria | XLSA | XLPP | α-oxoamine family | sideroblastic anemia | BIOCHEMISTRY & MOLECULAR BIOLOGY | LINKED SIDEROBLASTIC ANEMIA | 5-AMINOLEVULINATE SYNTHASE | GLYCINE LOOP | FEATURES | CELL BIOLOGY | PHOSPHATE COFACTOR-BINDING | BIOPHYSICS | METABOLISM | SUCCINYL-COA SYNTHETASE | PURIFICATION | MUTATIONS | DOMINANT PROTOPORPHYRIA | Pyridoxal Phosphate - chemistry | Mitochondria - enzymology | Aminolevulinic Acid - chemistry | Saccharomyces cerevisiae - genetics | Protein Multimerization | Substrate Specificity | Crystallography, X-Ray | Protein Subunits - metabolism | Pyridoxal Phosphate - metabolism | Coenzymes - metabolism | Heme - chemistry | Mitochondria - genetics | Aminolevulinic Acid - metabolism | Heme - biosynthesis | Cloning, Molecular | Escherichia coli - metabolism | 5-Aminolevulinate Synthetase - metabolism | Protein Interaction Domains and Motifs | Coenzymes - chemistry | Mitochondria - chemistry | Protein Subunits - genetics | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Catalytic Domain | Gene Expression | Genetic Vectors - chemistry | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | 5-Aminolevulinate Synthetase - chemistry | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Saccharomyces cerevisiae - chemistry | Amino Acid Motifs | Protein Conformation, beta-Strand | Escherichia coli - genetics | 5-Aminolevulinate Synthetase - genetics | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Saccharomyces cerevisiae - enzymology | Protein Subunits - chemistry | Kinetics | Mutation | Amino Acid Substitution | Saccharomyces cerevisiae Proteins - chemistry | Phosphates | Enzymes | Anemia | Analysis | Heme | Crystals | Hemoglobin synthesis | Structure | AAA+ | unfoldase | Sideroblastic anemia
Journal Article
Scientific Reports, ISSN 2045-2322, 12/2018, Volume 8, Issue 1, pp. 14228 - 13
Journal Article
Molecular Genetics and Metabolism, ISSN 1096-7192, 11/2019, Volume 128, Issue 3, pp. 178 - 189
Journal Article
Journal Article
Archives of Biochemistry and Biophysics, ISSN 0003-9861, 2011, Volume 511, Issue 1, pp. 107 - 117
► Product release, and not its formation, is rate-determining in wild-type ALAS dimer. ► The two active sites of a single chain dimeric ALAS have different... 
8-Amino-7-oxononanoate synthase | 5-Aminolevulinate | Pyridoxal 5′-phosphate | 5-Aminolevulinate synthase | α-Oxoamine synthase family | COA-CONDENSING ENZYME | HEME-BIOSYNTHESIS | PYRIDOXAL-PHOSPHATE COFACTOR | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | alpha-Oxoamine synthase family | BIOPHYSICS | ASPARTATE-AMINOTRANSFERASE | REACTION-MECHANISM | ESCHERICHIA-COLI K-12 | SERINE PALMITOYLTRANSFERASE | Pyridoxal 5 '-phosphate | CIRCULAR PERMUTATION | AMINOLEVULINATE SYNTHASE | Acyltransferases - metabolism | Acyltransferases - genetics | Recombinant Fusion Proteins - metabolism | Protein Structure, Quaternary | 5-Aminolevulinate Synthetase - metabolism | Protein Interaction Domains and Motifs | Dimerization | Escherichia coli - enzymology | Mutagenesis, Site-Directed | Catalytic Domain - genetics | Models, Molecular | Spectrometry, Fluorescence | Escherichia coli Proteins - metabolism | 5-Aminolevulinate Synthetase - chemistry | Recombinant Fusion Proteins - chemistry | Animals | Escherichia coli - genetics | 5-Aminolevulinate Synthetase - genetics | Escherichia coli Proteins - genetics | Recombinant Fusion Proteins - genetics | Acyltransferases - chemistry | Mice | Kinetics | Escherichia coli Proteins - chemistry | Spectrophotometry | Amino Acid Substitution | Phosphates | pyridoxal 5′ phosphate | α-oxoamine synthase family | 5-aminolevulinate synthase | 8-amino-7-oxononanoate synthase
Journal Article
BBA - Molecular Basis of Disease, ISSN 0925-4439, 02/2017, Volume 1863, Issue 2, pp. 428 - 439
Mutations in the C-terminus of human erythroid 5-aminolevulinate synthase (hALAS2), a pyridoxal 5′-phosphate (PLP)-dependent enzyme, are associated with two... 
Porphyria | Enzyme inhibitors | Anemia | Heme | Pyridoxal 5′-phosphate | 5-Aminolevulinate synthase | Enzyme stuctures | HEME-BIOSYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | SIDEROBLASTIC ANEMIA | PYRIDOXINE-RESPONSIVE ANEMIA | ENZYME | BIOPHYSICS | LIVER-INJURY | SUCCINYL-COA SYNTHETASE | DRUGS | Pyridoxal 5 '-phosphate | MUTATIONS | DOMINANT PROTOPORPHYRIA | BINDING | 5-Aminolevulinate Synthetase - deficiency | Isoniazid - pharmacology | Protoporphyria, Erythropoietic - drug therapy | Genetic Diseases, X-Linked - enzymology | Protoporphyria, Erythropoietic - blood | Humans | Enzyme Inhibitors - pharmacology | Protoporphyrins - blood | 5-Aminolevulinate Synthetase - chemistry | 5-Aminolevulinate Synthetase - antagonists & inhibitors | Vitamin B Complex - pharmacology | Enzyme Inhibitors - therapeutic use | Pyridoxal Phosphate - metabolism | Genetic Diseases, X-Linked - drug therapy | Protein Binding - drug effects | Anemia, Sideroblastic - enzymology | Isoniazid - therapeutic use | 5-Aminolevulinate Synthetase - metabolism | Protoporphyria, Erythropoietic - enzymology | HeLa Cells | 5-Aminolevulinate Synthetase - blood | Genetic Diseases, X-Linked - blood | Protein Structure, Tertiary - drug effects | Pyridoxine - pharmacology | Phosphates | Enzymes | Medical research | Medicine, Experimental | Isoniazid | Fluorescence microscopy | Fluorescence
Journal Article
Journal Article