Results 191 to 200 of about 9,205 (218)

Structural genomics of bacterial drug targets: Application of a high-throughput pipeline to solve 58 protein structures from pathogenic and related bacteria. [PDF]

Microbiol Resour Announc
Inniss NL, Minasov G, Chang C, Tan K, Kim Y, Maltseva N, Stogios P, Filippova E, Michalska K, Osipiuk J, Jaroszewki L, Godzik A, Savchenko A, Joachimiak A, Anderson WF, Satchell KJF, Center for Structural Biology of Infectious Diseases Team members.   +16 more
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Refolding of the human dihydrolipoamide dehydrogenase

Biochemical Engineering Journal, 2009
Abstract A refolding procedure was optimized for human dihydrolipoamide dehydrogenase (LADH) that can serve as a complementary method to isolation protocols for cytosolic or periplasmic expression of the enzyme. The reported procedure is especially useful if part of the protein is precipitated into inclusion bodies during expression and higher ...
Vera Adam-Vizi, Attila Ambrus, Beáta Töröcsik   +2 more
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The moonlighting activities of dihydrolipoamide dehydrogenase: Biotechnological and biomedical applications

Journal of Molecular Recognition, 2021
AbstractDihydrolipoamide dehydrogenase (DLDH) is a homodimeric flavin‐dependent enzyme that catalyzes the NAD+‐dependent oxidation of dihydrolipoamide. The enzyme is part of several multi‐enzyme complexes such as the Pyruvate Dehydrogenase system that transforms pyruvate into acetyl‐co‐A.
Gideon Fleminger, Avraham Dayan
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Dihydrolipoamide dehydrogenase in the Trypanosoma subgenus, Trypanozoon

Molecular and Biochemical Parasitology, 1994
The enzyme dihydrolipoamide dehydrogenase has been discovered and characterised in four salivarian trypanosomes of the subgenus trypanozoon: Trypanosoma brucei brucei, T. b. gambiense, T. b. rhodesiense, and Trypanosoma evansi. The three T. brucei species, which have insect procyclic forms biochemically distinct from their mammalian bloodstream forms ...
Anthony J. Else, Michael J. Danson, Anthony Willis, Simon A. Jackman, David W. Hough, James F. Clarke   +5 more
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A structural model for human dihydrolipoamide dehydrogenase

Proteins: Structure, Function, and Bioinformatics, 1992
AbstractThe hypothesis that dihydrolipoamide dehydrogenases (E3s) have tertiary structures very similar to that of human glutathione reductase (GR) was tested in detail by three separate criteria: (1) by analyzing each putative secondary structural element for conservation of appropriate polar/nonpolar regions, (2) by detailed comparison of putative ...
Menachem Shoham, Darren Hurst, Joyce E. Jentoft, Mulchand S. Patel   +3 more
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[20] Dihydrolipoamide dehydrogenase: Activity assays

1995
We have described the most commonly used assay procedures determination of the DHLipDH activities from prokaryotic and eukaryotic cells. We have also described the procedures for the preparation of tissue extracts to determine the enzymatic activity.
Nataraj N. Vettakkorumakankav, Te-Chung Liu, Mulchand S. Patel   +2 more
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Dihydrolipoamide dehydrogenase from Haloferax volcanii: gene cloning, complete primary structure, and comparison to other dihydrolipoamide dehydrogenases

Biochemistry and Cell Biology, 1992
We used the N-terminal amino acid sequence of dihydrolipoamide dehydrogenase from Haloferax volcanii, to design and synthesize two oligonucleotide probes that were used to identify and clone a 4.3 kilobase pair (kbp) fragment from MboI restriction endonuclease digestion of Hf. volcanii genomic DNA.
Kenneth J. Stevenson, Nataraj Vettakkorumakankav   +1 more
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Expression and purification of the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase subunits of the Escherichia coli pyruvate dehydrogenase multienzyme complex: a mass spectrometric assay for reductive acetylation of dihydrolipoamide acetyltransferase

Protein Expression and Purification, 2003
Plasmids were constructed for overexpression of the Escherichia coli dihydrolipoamide acetyltransferase (1-lip E2, with a single hybrid lipoyl domain per subunit) and dihydrolipoamide dehydrogenase (E3). A purification protocol is presented that yields homogeneous recombinant 1-lip E2 and E3 proteins.
Frank Jordan, Natalia S. Nemeria, Hong Li, Wen Wei   +3 more
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