Results 201 to 210 of about 9,205 (218)

Elevated plasma citrulline: look for dihydrolipoamide dehydrogenase deficiency

European Journal of Pediatrics, 2013
The E3 subunit of the pyruvate dehydrogenase complex (dihydrolipoamide dehydrogenase/dihydrolipoyl dehydrogenase/DLD/lipoamide dehydrogenase/LAD), is a mitochondrial matrix enzyme and also a part of the branched-chain ketoacid dehydrogenase and alpha-ketoglutarate dehydrogenase complexes.
Ann Saada, Corinne Belaiche, Avraham Zeharia, Yishai Haimi Cohen, Ruby Haviv   +4 more
openaire   +3 more sources

Roles of dihydrolipoamide dehydrogenase Lpd1 in Candida albicans filamentation

Fungal Genetics and Biology, 2010
Acetyl coenzyme A, a key intermediate of the mitochondrial carbon metabolism, is formed by the mitochondrial pyruvate dehydrogenase complex (PDC). The dihydrolipoamide dehydrogenase Lpd1 is a catalytic component of PDC. Lpd1 has been recovered during 2D-PAGE screening for the hypha-specific proteins in Candida albicans.
Jinmi Kim, Seung-Yeop Kim
openaire   +3 more sources

Dihydrolipoamide dehydrogenase moonlighting activity as a DNA chelating agent

Proteins: Structure, Function, and Bioinformatics, 2020
AbstractDihydrolipoamide dehydrogenase (DLDH) is a mitochondrial enzyme that comprises an essential component of the pyruvate dehydrogenase complex. Lines of evidence have shown that many dehydrogenases possess unrelated actions known as moonlightings in addition to their oxidoreductase activity.
Gideon Fleminger, Adva Yeheskel, Avraham Dayan, Raphael Lamed, Osnat Ashur-Fabian, Osnat Ashur-Fabian   +5 more
openaire   +2 more sources

Cloning and sequence analysis of the genes encoding the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus

European Journal of Biochemistry, 1990
A 2641‐bp EcoRl fragment of DNA that encodes the C‐terminal part of the dihydrolipoyl acetyltransferase (E2) component and the dihydrolipoamide dehydrogenase (E3) component of the pyruvate dehydrogenase complex of Bacillus stearothermophilus has been cloned in Escherichia coli. Its nucleotide sequence was determined.
Adolfo Borges, Leonard C. Packman, Christopher F. Hawkins, Richard N. Perham   +3 more
openaire   +3 more sources

Thermally Induced Disintegration of theBacillus stearothermophilusDihydrolipoamide Dehydrogenase

Bioscience, Biotechnology, and Biochemistry, 2000
Upon heat treatment of the pyruvate dehydrogenase complex from Bacillus stearothermophilus, the most thermostable component is a dihydrolipoamide dehydrogenase (E3c). To understand this stability, the thermal disintegration of E3 dissociated from the complex (E3d) was examined, comparing with that of E3c. Judging from residual activity and inactivation
Yasuaki Hiromasa, Kohji Meno, Shoji Yamashita, Yoichi Aso   +3 more
openaire   +3 more sources

Lipoic Acid and Dihydrolipoamide Dehydrogenase in Halophilic Archaeobacteria

1991
We have discovered the presence of dihydrolipoamide dehydrogenase (DHLipDH) in the halophilic archaeobacteria, despite the fact that these organisms lack the multienzyme complexes with which this enzyme is associated in eubacteria and eucaryotes. We will discuss (a) the discovery, purification and characterisation of the halophilic DHLipDH, (b) the ...
David W. Hough, Nataraj Vettakkorumakankav, Michael J. Danson, Kenneth J. Stevenson   +3 more
openaire   +2 more sources

Cloning, sequencing, and expression of Trypanosoma brucei dihydrolipoamide dehydrogenase

European Journal of Biochemistry, 1993
A gene encoding dihydrolipoamide dehydrogenase was isolated from Trypanosoma brucei genomic DNA by using a combination of polymerase chain reaction and screening of a λ EMBL3 library. The DNA sequence reveals that it encodes a protein of 478 amino acids (Mr 49935) highly similar to previously sequenced dihydrolipoamide dehydrogenases.
Michael J. Danson, David W. Hough, Anthony J. Else   +2 more
openaire   +3 more sources

Identification and purification of a distinct dihydrolipoamide dehydrogenase from pea chloroplasts

Planta, 1996
Two distinct dihydrolipoamide dehydrogenases (E3s, EC 1.8.1.4) have been detected in pea (Pisum sativum L. cv. Little Marvel) leaf extracts and purified to at or near homogeneity. The major enzyme, a homodimer with an apparent subunit M(r) value 56,000 (80-90% of overall activity), corresponded to the mitochondrial isoform studied previously, as ...
Tino Krell, Lindsay Jg, Conner M
openaire   +3 more sources

Dihydrolipoamide dehydrogenase: a ‘new’ function for an old enzyme? [PDF]

Biochemical Society Transactions, 1988
openaire   +2 more sources

Serum Dihydrolipoamide Dehydrogenase Is a Labile Enzyme.

Journal of biochemical and pharmacological research
Dihydrolipoamide dehydrogenase (DLDH) is a multifunctional oxidoreductase and is well known as an essential component of four mammalian mitochondrial multienzyme complexes: pyruvate dehydrogenase, α-ketoglutarate dehydrogenase, branched chain α-keto acid dehydrogenase, and the glycine cleavage system. However, existence of extracellular DLDH in mammals,
Liang-Jun, Yan, Nopporn, Thangthaeng, Nathalie, Sumien, Michael J, Forster   +3 more
openaire   +1 more source