Compounds > udp-n-acetylglucosamine-enolpyruvate
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udp-n-acetylglucosamine-enolpyruvate and nadp

udp-n-acetylglucosamine-enolpyruvate has been researched along with nadp in 5 studies

Compound Research Comparison

Studies
(udp-n-acetylglucosamine-enolpyruvate)		Trials
(udp-n-acetylglucosamine-enolpyruvate)		Recent Studies (post-2010)
(udp-n-acetylglucosamine-enolpyruvate)		Studies
(nadp)		Trials
(nadp)		Recent Studies (post-2010) (nadp)
110421,608253,484

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (60.00)18.2507
2000's0 (0.00)29.6817
2010's2 (40.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Dhalla, AM; Falk, PJ; Ho, HT; Robertson, JG; Villafranca, JJ; Yanchunas, J1
Benson, TE; Hogle, JM; Walsh, CT1
Axley, MJ; Fairman, R; Robertson, JG; Villafranca, JJ; Yanchunas, J1
Chen, MW; Lescar, J; Lohkamp, B; Schneider, G; Schnell, R1
Bajpai, U; Dharavath, S; Eniyan, K; Gourinath, S; Vijayan, R1

Other Studies

5 other study(ies) available for udp-n-acetylglucosamine-enolpyruvate and nadp

ArticleYear
Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase.
    Biochemistry, 1995, Apr-25, Volume: 34, Issue:16

    Topics: Anaerobiosis; Carbohydrate Dehydrogenases; Cloning, Molecular; Escherichia coli; Flavin-Adenine Dinucleotide; Genes, Bacterial; Glucosamine; Kinetics; Mathematics; NADP; Recombinant Proteins; Ribonucleotides; Uridine Diphosphate; Uridine Diphosphate N-Acetylglucosamine

1995
The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls.
    Structure (London, England : 1993), 1996, Jan-15, Volume: 4, Issue:1

    Topics: Bacterial Proteins; Binding Sites; Carbohydrate Dehydrogenases; Cell Wall; Crystallography, X-Ray; Flavin-Adenine Dinucleotide; Hydrogen Bonding; Models, Chemical; Models, Molecular; Molecular Structure; NADP; Oxidation-Reduction; Protein Binding; Protein Conformation; Tyrosine; Uridine Diphosphate N-Acetylglucosamine

1996
Spectroscopic properties of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase.
    Biochemistry, 1997, Jan-28, Volume: 36, Issue:4

    Topics: Anaerobiosis; Carbohydrate Dehydrogenases; Circular Dichroism; Deuterium Oxide; Escherichia coli; Flavin-Adenine Dinucleotide; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; NADP; Oxidation-Reduction; Photochemistry; Protein Denaturation; Protein Folding; Protons; Solvents; Spectrophotometry; Spectrophotometry, Ultraviolet; Substrate Specificity; Uridine Diphosphate N-Acetylglucosamine

1997
Substrate Channel Flexibility in Pseudomonas aeruginosa MurB Accommodates Two Distinct Substrates.
    PloS one, 2013, Volume: 8, Issue:6

    Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Catalytic Domain; Crystallography, X-Ray; Escherichia coli; Flavin-Adenine Dinucleotide; Molecular Dynamics Simulation; NADP; Oxidoreductases; Potassium; Pseudomonas aeruginosa; Recombinant Proteins; Sequence Alignment; Substrate Specificity; Uridine Diphosphate N-Acetylglucosamine

2013
Crystal structure of UDP-N-acetylglucosamine-enolpyruvate reductase (MurB) from Mycobacterium tuberculosis.
    Biochimica et biophysica acta. Proteins and proteomics, 2018, Volume: 1866, Issue:3

    Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Biocatalysis; Catalytic Domain; Crystallography, X-Ray; Molecular Dynamics Simulation; Mycobacterium tuberculosis; NADP; Protein Binding; Protein Domains; Protein Multimerization; Sequence Homology, Amino Acid; Uridine Diphosphate N-Acetylglucosamine

2018