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Transketolase (abbreviated as TK) is an enzyme that, in humans, is encoded by the TKT gene. [1] It participates in both the pentose phosphate pathway in all organisms and the Calvin cycle of photosynthesis. Transketolase catalyzes two important reactions, which operate in opposite directions in these two pathways.
Transketolase-like-1 (TKTL1) is a gene closely related to the transketolase gene (TKT). It emerged in mammals during the course of evolution and, according to the latest research findings, is considered one of the key genes that distinguishes modern humans ( Homo sapiens ) from Neanderthals .
In enzymology, a formaldehyde transketolase (EC 2.2.1.3) is an enzyme that catalyzes the chemical reaction D-xylulose 5-phosphate + formaldehyde ⇌ {\displaystyle \rightleftharpoons } glyceraldehyde 3-phosphate + glycerone
74419 Ensembl ENSG00000151005 ENSMUSG00000025519 UniProt Q9H0I9 Q9D4D4 RefSeq (mRNA) NM_032136 NM_001271574 NM_028927 RefSeq (protein) NP_115512 NP_001258503 NP_083203 Location (UCSC) Chr 4: 163.47 – 163.47 Mb Chr 8: 66.96 – 66.97 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Transketolase-like protein 2 is an enzyme that in humans is encoded by the TKTL2 gene. References ^ a b ...
Dehydrogenase E1 and transketolase domain containing 1 is a protein that in humans is encoded by the DHTKD1 gene. This gene encodes a component of a mitochondrial 2-oxoglutarate-dehydrogenase-complex-like protein involved in the degradation pathways of several amino acids , including lysine .
In several reactions, including that of pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase, and transketolase, TPP catalyses the reversible decarboxylation reaction (aka cleavage of a substrate compound at a carbon-carbon bond connecting a carbonyl group to an adjacent reactive group—usually a carboxylic acid or an alcohol).
In the non-oxidative branch of the pentose phosphate pathway, xylulose-5-phosphate acts as a donor of two-carbon ketone groups in transketolase reactions. [1] Xylulose-5-phosphate also plays a crucial role in the regulation of glycolysis through its interaction with the bifunctional enzyme PFK2/FBPase2.
It is formed by transketolase and acted upon by transaldolase. Sedoheptulokinase is an enzyme that uses sedoheptulose and ATP to produce ADP and sedoheptulose 7-phosphate. Sedoheptulose-bisphosphatase is an enzyme that uses sedoheptulose 1,7-bisphosphate and H 2 O to produce sedoheptulose 7-phosphate and phosphate.
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