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In contrast, archaeal H2 producers have a unique enzyme, GAP oxidoreductase (GAPOR), which oxidizes GAP generating one Fdred but no ATP.
Coat disassembly is triggered by an ARF-GTPase activating enzyme (GAP) [22], [26].
This tool was then used to search for functional activity related to missing enzyme (Gap) in the metabolic reaction.
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With the growing myriad of connexin interacting proteins, including cytoskeletal elements, junctional proteins, and enzymes, gap junctions are now perceived, not only as channels between neighboring cells, but as signaling complexes that regulate cell function and transformation.
However, this activity is very weak and needs to be up-regulated by GTPase activating enzymes (GAPs).
In resting neurons that are not releasing neurotransmitters, synaptotagmin ('yin') binds to an enzyme called GAP and prevents it from converting GTP an energy-storage molecule into GDP.
However, there is no information about the role of this enzyme on GAP-43 deacylation.
Besides the significantly enhanced expression of VAL-A biosynthetic genes as previously detected [ 4], a few key enzymes (Pfk-Gap-Pyk-GntK-CitE) for central carbon metabolism were differentially expressed to redirect carbon metabolic flux into the pentose phosphate pathway, which generates more carbon precursors for VAL-A production.
In a previous study, we constructed an ATP/ADP-balanced chimeric Embden-Meyerhof (EM) pathway by swapping the enzyme couple of GAP dehydrogenase and phosphoglycerate kinase in the bacterial/eukaryotic EM pathway with the non-phosphorylating GAP dehydrogenase (GAPNTk) involved in the modified EM pathway of a hyperthermophilic archaeon, Thermococcus kodakarensis[5].
This disrupts its interaction with the GAP enzyme, which thus becomes free to convert the GTP molecule bound to Rab3 into GDP.
Unlike what happens with Ras, the glutamine residue in the switch II motif in Rab33 does not contribute directly to the catalysis of GTP hydrolysis: instead it is involved in the interaction between the Rab33 enzyme and the GAP protein.
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