The dihydrolipoamide dehydrogenase from the crenarchaeon Acidianus ambivalens [PDF]
A dihydrolipoamide dehydrogenase (DLDH) was purified and characterized for the first time from a crenarchaeon, Acidianus ambivalens. The holoenzyme consists of two identical subunits with a molecular mass of 45.4 kDa per monomer. It contains FAD as a prosthetic group and uses NAD+ as the preferential substrate, but can also reduce NADP+.
Arnulf Kletzin+2 more
openaire +3 more sources
Electrochemical tuning of alcohol oxidase and dehydrogenase catalysis via biosensing towards butanol-1 detection in fermentation media [PDF]
A novel approach for electrochemical tuning of alcohol oxidase (AOx) and alcohol dehydrogenase (ADH) biocatalysis towards butanol-1 oxidation by incorporating enzymes in various designs of amperometric biosensors is presented. The biosensors were developed by using commercial graphene oxide-based screen-printed electrodes and varying enzyme producing ...
arxiv +1 more source
DHTKD1 is a lesser-studied E1 enzyme among the family of 2-oxoacid dehydrogenases. In complex with E2 (dihydrolipoamide succinyltransferase, DLST) and E3 (dihydrolipoamide dehydrogenase, DLD) components, DHTKD1 is involved in lysine and tryptophan ...
Gustavo A. Bezerra+10 more
doaj +1 more source
Nucleotide sequence for yeast dihydrolipoamide dehydrogenase. [PDF]
Rabbit antiserum to the dihydrolipoamide dehydrogenase (dihydrolipoamide:NAD+ oxidoreductase, EC 1.8.1.4) component of the pyruvate dehydrogenase complex from bakers' yeast was used to screen plaques produced by a lambda gt11 yeast cDNA library.
Karen S. Browning+2 more
openaire +3 more sources
Pyruvate dehydrogenase (PDH) and 2‐oxoglutarate dehydrogenase (ODH) are critical enzymes in central carbon metabolism. In Corynebacterium glutamicum, an unusual hybrid complex consisting of CgE1p (thiamine diphosphate‐dependent pyruvate dehydrogenase ...
Hirokazu Kinugawa+5 more
doaj +1 more source
Protein–protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of dihydrolipoamide acetyltransferase [PDF]
The ubiquitous pyruvate dehydrogenase multienzyme complex is built around an octahedral or icosahedral core of dihydrolipoamide acetyltransferase (E2) chains, to which multiple copies of pyruvate decarboxylase (E1) and dihydrolipoamide dehydrogenase (E3) bind tightly but non-covalently.
Sharmila S. Mande+4 more
openaire +3 more sources
The nicotinamide cofactor specificity of enzymes plays a key role in regulating metabolic processes and attaining cellular homeostasis. Multiple studies have used enzyme engineering tools or a directed evolution approach to switch the cofactor preference
Madeleine Bouzon+12 more
doaj +1 more source
Variation in the organization and subunit composition of the mammalian pyruvate dehydrogenase complex E2/E3BP core assembly [PDF]
The final version of this article is available at the link below.Crucial to glucose homoeostasis in humans, the hPDC (human pyruvate dehydrogenase complex) is a massive molecular machine comprising multiple copies of three distinct enzymes (E1–E3) and an
Alan Cooper+44 more
core +3 more sources
Large yellow croaker (Larimichthys crocea), an economically important marine fish in China, has suffered from serious vibriosis, which has resulted in great economic losses for the large yellow croaker industry.
Xiaomeng Li+6 more
doaj +1 more source
Characterization and epitope mapping of human monoclonal antibodies to PDC-E2, the immunodominant autoantigen of primary biliary cirrhosis [PDF]
Further to define the epitopes of PDC-E2, the major autoantigen in primary biliary cirrhosis (PBC), we have developed and characterized five human monoclonal antibodies. These antibodies were derived by fusing a regional hepatic lymph node from a patient
Bassendine+49 more
core +1 more source