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Biotin synthase

  • Crystallographic Snapshots of Sulfur Insertion by Lipoyl Synthase

    Crystallographic Snapshots of Sulfur Insertion by Lipoyl Synthase

  • Letters to Nature

    Letters to Nature

  • Mitochondrial Serine Acetyltransferase Functions As a Pacemaker of Cysteine Synthesis in Plant Cells1[C][W][OA]

    Mitochondrial Serine Acetyltransferase Functions As a Pacemaker of Cysteine Synthesis in Plant Cells1[C][W][OA]

  • Product Sheet Info

    Product Sheet Info

  • The Crystal Structure of Biotin Synthase, an S-Adenosylmethionine-Dependent Radical Enzyme F

    The Crystal Structure of Biotin Synthase, an S-Adenosylmethionine-Dependent Radical Enzyme F

  • Dependent Enzyme Moaa and Its Implications for Molybdenum Cofactor Deficiency in Humans

    Dependent Enzyme Moaa and Its Implications for Molybdenum Cofactor Deficiency in Humans

  • 12) United States Patent (10

    12) United States Patent (10

  • Radical-Sam Enzymes with Two Iron-Sulfur Clusters: Cofactor

    Radical-Sam Enzymes with Two Iron-Sulfur Clusters: Cofactor

  • Cysteine Catabolism and Glucosinolate Turnover in Arabidopsis Thaliana

    Cysteine Catabolism and Glucosinolate Turnover in Arabidopsis Thaliana

  • Cysteine: an Overlooked Energy and Carbon Source

    Cysteine: an Overlooked Energy and Carbon Source

  • Cluster Accompanies Formation of the Intermediate 9-Mercaptodethiobiotin in Escherichia Coli Biotin Synthase Andrew M

    Cluster Accompanies Formation of the Intermediate 9-Mercaptodethiobiotin in Escherichia Coli Biotin Synthase Andrew M

  • Genetic and Biochemical Characterization of Yrkf, a Novel

    Genetic and Biochemical Characterization of Yrkf, a Novel

  • Genome Wide Analysis Identifies Sphingolipid Metabolism As a New Target of Valproic Acid

    Genome Wide Analysis Identifies Sphingolipid Metabolism As a New Target of Valproic Acid" (2016)

  • All Enzymes in BRENDA™ the Comprehensive Enzyme Information System

    All Enzymes in BRENDA™ the Comprehensive Enzyme Information System

  • The Multifaceted Bacterial Cysteine Desulfurases: from Metabolism to Pathogenesis

    The Multifaceted Bacterial Cysteine Desulfurases: from Metabolism to Pathogenesis

  • Mechanistic Studies on Biotin Biosynthesis

    Mechanistic Studies on Biotin Biosynthesis

  • Row Labels Gene Name GLU 1 GLU 2 GLU 3 RF 1 RF 2 RF 3

    Row Labels Gene Name GLU 1 GLU 2 GLU 3 RF 1 RF 2 RF 3

  • S-Adenosylmethionine As an Oxidant: the Radical SAM Superfamily

    S-Adenosylmethionine As an Oxidant: the Radical SAM Superfamily

Top View
  • Springer Handbook of Enzymes
  • Are Shown B Gene Numbera
  • The Role of the Energy Conserving Hydrogenase B in Autotrophy And
  • Crystallographic Snapshots of Sulfur Insertion by Lipoyl Synthase
  • Okonji Et Al (6).Cdr
  • Supplementary Table 2 - in Silico Reconstruction of the Metabolic Pathways of S
  • Supplemental Table 1.Predicted Enzymes of S. Oneidensis MR-1 and Their Closest Homolog by Darwin Analysis. the Microbial Genomes
  • Sulfur Metabolism in Escherichia Coli and Related Bacteria: Facts and Fiction
  • Roles of Vitamins B5, B8, B9, B12 and Molybdenum Cofactor at Cellular and Organismal Levels†
  • This Diagram Was Automatically Generated by SRI International Pathway Tools Version 19.0, Authors S. Paley and P.D. Karp
  • Myosin Light Chain Kinase
  • Reducing the Mysteries of Sulfur Metabolism in Mycobacterium Tuberculosis
  • Structure-Function Studies of Escherichia Coli Biotin Synthase Via a Chemical Modification and Site-Directed Mutagenesis Approach1
  • Molecular Genetic Studies of Acetyl-Coa Carboxylase and 3-Methylcrotonyl-Coa Carboxylase in Plants Hui-Rong Qian Iowa State University
  • A [3Fe-4S] Cluster Is Required for Trna Thiolation in Archaea and Eukaryotes
  • The Role of Mitochondria in Cellular Iron – Sulfur Protein Biogenesis
  • Structures of Lipoyl Synthase Reveal a Compact Active Site for Controlling Sequential Sulfur Insertion Reactions Jenny E
  • Structural Biology of Enzymes Involved in NAD and Molybdenum Cofactor Biosynthesis Menico Rizzi* and Hermann Schindelin†


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