Compounds > malyl-coenzyme a

malyl-coenzyme a and coenzyme a

malyl-coenzyme a has been researched along with coenzyme a in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19901 (33.33)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's2 (66.67)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Dekker, EE; Gupta, SC1
Nolte, JC; Schepers, CL; Schürmann, M; Steinbüchel, A; Vogel, E; Wübbeler, JH1
Chen, JC; González, JM; Marti-Arbona, R; Unkefer, CJ1

Other Studies

3 other study(ies) available for malyl-coenzyme a and coenzyme a

ArticleYear
Malyl-CoA formation in the NAD-, CoASH-, and alpha-ketoglutarate dehydrogenase-dependent oxidation of 2-keto-4-hydroxyglutarate. Possible coupled role of this reaction with 2-keto-4-hydroxyglutarate aldolase activity in a pyruvate-catalyzed cyclic oxidati
    The Journal of biological chemistry, 1984, Aug-25, Volume: 259, Issue:16

    Topics: Acyl Coenzyme A; Animals; Coenzyme A; Escherichia coli; Glyoxylates; Hydroxylamine; Hydroxylamines; Ketoglutarate Dehydrogenase Complex; Ketoglutaric Acids; Ketone Oxidoreductases; Kinetics; Myocardium; NAD; Oxidation-Reduction; Oxo-Acid-Lyases; Swine

1984
Novel characteristics of succinate coenzyme A (Succinate-CoA) ligases: conversion of malate to malyl-CoA and CoA-thioester formation of succinate analogues in vitro.
    Applied and environmental microbiology, 2014, Volume: 80, Issue:1

    Topics: Acyl Coenzyme A; Alcaligenaceae; Alcanivoraceae; Coenzyme A; Escherichia coli; Esters; Kinetics; Malates; Substrate Specificity; Succinate-CoA Ligases; Sulfur Compounds

2014
Structure of Methylobacterium extorquens malyl-CoA lyase: CoA-substrate binding correlates with domain shift.
    Acta crystallographica. Section F, Structural biology communications, 2017, Feb-01, Volume: 73, Issue:Pt 2

    Topics: Acyl Coenzyme A; Amino Acid Sequence; Bacterial Proteins; Catalytic Domain; Cations, Divalent; Cloning, Molecular; Coenzyme A; Crystallography, X-Ray; Escherichia coli; Gene Expression; Magnesium; Methylobacterium extorquens; Models, Molecular; Oxalic Acid; Oxo-Acid-Lyases; Plasmids; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; Protein Structure, Quaternary; Recombinant Proteins; Rhodobacter sphaeroides; Substrate Specificity

2017