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GOT2 is a dimer containing two identical subunits that hold overlapping subunit regions. The top and sides of the enzyme are made up of helices , while the bottom is formed by strands of beta sheets and extended hairpin loops.
Each subunit is composed of a large and a small domain, as well as a third domain consisting of the N-terminal residues 3-14; these few residues form a strand, which links and stabilizes the two subunits of the dimer. The large domain, which includes residues 48-325, binds the PLP cofactor via an aldimine linkage to the ε-amino group of Lys258.
14718 Ensembl ENSG00000120053 ENSMUSG00000025190 UniProt P17174 P05201 RefSeq (mRNA) NM_002079 NM_010324 RefSeq (protein) NP_002070 NP_034454 Location (UCSC) Chr 10: 99.4 – 99.43 Mb Chr 19: 43.49 – 43.51 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Aspartate aminotransferase, cytoplasmic is an enzyme that in humans is encoded by the GOT1 gene. Glutamic-oxaloacetic transaminase ...
Glutamate dehydrogenase (GLDH, GDH) is an enzyme observed in both prokaryotes and eukaryotic mitochondria.The aforementioned reaction also yields ammonia, which in eukaryotes is canonically processed as a substrate in the urea cycle.
The GTP form of the α subunit of transducin (G t) activates the cyclic GMP phosphodiesterase from retinal rod outer segments, [3] and the GTP form of the α subunit of the stimulatory G protein (G s) activates hormone-sensitive adenylate cyclase. [4] [5] More than one type of G protein co-exist in the same tissue. For example, in adipose ...
In enzymology, a glutamine-pyruvate transaminase (EC 2.6.1.15) is an enzyme that catalyzes the chemical reaction. L-glutamine + pyruvate 2-oxoglutaramate + L-alanine. Thus, the two substrates of this enzyme are L-glutamine and pyruvate, whereas its two products are 2-oxoglutaramate and L-alanine.
The bull market of the past year or more has reinvigorated investors' interest across a range of industries, and the performance of many top stocks reflects this reality. DexCom (NASDAQ: DXCM) is ...
RabGGTase’s secondary structure is largely composed of alpha helices; the alpha subunit is 74% helical with no beta sheets, while the beta subunit is 51% helical and 5% beta sheet. There are 28 alpha helices total (15 in the alpha subunit and 13 in the beta subunit) and 15 very short (no more than 4 residues) beta sheets.