EC Number |
Recommended Name |
Application |
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7.1.1.2 | NADH:ubiquinone reductase (H+-translocating) |
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crucial role for mitochondrial nitric oxide synthase in oxidative stress caused by mitochondrial complex I inactivation |
7.1.1.2 | NADH:ubiquinone reductase (H+-translocating) |
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if phosphorylation occurs in vivo, effects on complex I activity are significant |
7.1.1.2 | NADH:ubiquinone reductase (H+-translocating) |
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missense mutation in the MT-ND5 subunit of NADH dehydrogenase in Tibet chicken breed. Significant differences between animals carrying mitochondria with the EF493865.1:m.1627A versus EF493865.1:m.1627C alleles for respiratory control ratio and enzyme activity. MT-ND5 gene variation is significantly associated with brain mitochondrial respiratory function in Tibet chicken embryos under hypoxia, which identifies MT-ND5 as a candidate gene for adaptation to hypoxia (or high hatchability under hypoxia) in Tibet chickens |
7.1.1.2 | NADH:ubiquinone reductase (H+-translocating) |
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reduction in complex I activity results in a decrease in mitochondrial movement which is compensated for by an increase in mitochondrial length and degree of branching and an enhanced diffusion of matrix constituents |
7.1.1.2 | NADH:ubiquinone reductase (H+-translocating) |
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two variants of the mitochondrial complex I subunit NDUFA10. A D/N substitution at position 120 resulting from a 353A/G transition in the coding gene is the biochemical difference between the two most abundant NDUFA10 isoforms |
7.1.1.8 | quinol-cytochrome-c reductase |
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the complex from the alpha-proteobacterium Paracoccus denitrificans is a model for the medically relevant mitochondrial complexes |
7.1.1.9 | cytochrome-c oxidase |
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100% homology among cox1 sequences from morphotype 1 (females presenting caudal tips smooth without spines) and morphotype 2 (females presenting caudal tips smooth with spines) of Filaria martis collected from beech martens, thus indicating that the shape of female posterior edge may vary among specimens |
7.1.1.9 | cytochrome-c oxidase |
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an assembled complex IV helps to maintain complex I (NADH-ubiquinone oxidoreductase) in mammalian cells |
7.1.1.9 | cytochrome-c oxidase |
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Arabidopsis thaliana COX19 genes encode functional homologues of the yeast metal chaperone. Smaller COX19-1 isoform, but not the larger one, is able to restore growth on non-fermentable carbon sources when expressed in a yeast cox19 null mutant. Induction by biotic and abiotic stress factors may indicate a relevant role of this protein in the biogenesis of cytochrome c oxidase to replace damaged forms of the enzyme. COX19 has additional functions besides its participation in COX assembly as, for example, metal transport, detoxification, or general protection against oxidative stress |
7.1.1.9 | cytochrome-c oxidase |
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counteracting relationship exists between the effects of withdrawal and 17beta-estradiol on the activity of COX in a subunit specific manner, which may not alter protein synthesis |
7.1.1.9 | cytochrome-c oxidase |
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cytochrome c oxidase is involved in mercury reduction in Acidithiobacillus ferrooxidans cells. Levels of mercury resistance in Acidithiobacillus ferrooxidans strains correspond well with the levels of mercury resistance of cytochrome c oxidase |
7.1.1.9 | cytochrome-c oxidase |
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inhibition of COX activity is rather caused by ischemia-induced modification of COX polypeptides than by inhibition of mitochondrial translation |
7.1.1.9 | cytochrome-c oxidase |
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mean nucleotide variation within the Steganinae subfamily is 8.1% |
7.1.1.9 | cytochrome-c oxidase |
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mean nucleotide variation within the Steganinae subfamily is 8.1%, variation within Amiota spp. is 21.8% |
7.1.1.9 | cytochrome-c oxidase |
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mean nucleotide variation within the Steganinae subfamily is 8.1%, with a variation within Phortica spp. of 1.6% |
7.1.1.9 | cytochrome-c oxidase |
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molecular phylogenic analysis based on COXI indicates Gobiocypris rarus belongs to Gobioninae. Comparison of DNA with cDNA shows that RNA editing phenomenon does not occur in the COXI of Gobiocypris rarus |
7.1.1.9 | cytochrome-c oxidase |
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permeabilization of the outer mitochondrial membrane during apoptosis functions not just to release cytochrome c but also to maintain it oxidized via cytochrome oxidase, thus maximizing caspase activation |
7.1.1.9 | cytochrome-c oxidase |
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prion protein may not be involved in regulation of cytochrome c oxidase |
7.1.1.9 | cytochrome-c oxidase |
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simple and rapid isolation of COX by immunocapture |
7.1.1.9 | cytochrome-c oxidase |
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the MCOX2e region is unique to unionoidean bivalve male genomes. MCOX2e is functional and is likely the result of a single insertion event that took place over 65 MYA, the predicted transmembrane helices/interhelical loops number, length and position variability likely stems from substitution-based processes rather than the typically implicated insertion/deletion events. MCOX2e has relatively high rates of evolution in its primary and secondary structures. MCOX2e displays evidence suggestive of site-specific positive selection. MCOX2e has an overall pattern of purifying selection that leads to the preservation of the transmembrane helices/interhelical loops and hydrophilic C-terminus tail sub-regions, and the more conserved C-terminus tail (relative to the transmembrane helices/interhelical loops sub-region of MCOX2e) is likely biologically active because it contains functional motifs. MCOX2e may have a novel reproductive function within unionoidean bivalves |
7.1.1.9 | cytochrome-c oxidase |
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the monomeric form of Rhodobacter sphaeroides COX when reconstituted into a phospholipid bilayer is completely functionally active in its ability to perform electron transfer and proton pumping activities of the enzyme |
7.1.2.2 | H+-transporting two-sector ATPase |
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cleavage of the gamma subunit of the ATP synthase by trypsin prevents inhibition of ATPase activity by the sigma subunit, but only partially overcomes Mg2+-ADP inhibition during assay |
7.1.2.2 | H+-transporting two-sector ATPase |
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formation of an active alpha3beta3EG hybrid complex by co-reconstitution of subunits alpha and beta of the F1-ATPase and of subunits E and G of Saccharomyces cerevisiae V-ATPase, the coupling subunit gamma inside the alpha3beta3 oligomer of F1 can be effectively replaced by subunit E of the V-ATPase, the E and gamma subunit are structurally similiar, but their genes do not show homology |
7.1.2.2 | H+-transporting two-sector ATPase |
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incorporation of F1F0 into soybean liposomes yields well-coupled and highly active proteoliposomes |
7.1.2.2 | H+-transporting two-sector ATPase |
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simple and inexpensive method to grow yeast to high density and purify the mitochondrial F1-ATPase quickly and efficiently |
7.1.2.2 | H+-transporting two-sector ATPase |
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site-specific spin-labeling of single cysteine mutations within mutant of subunit b of the ATP-synthase and employed electron spin resonance indicate tight binding interaction between b2 and F1, different binding interactions of b to F1 in the presence or absence of sigma, b preperations spin-labeled between amino acid position 101 and 114 are indicative of either two populations of b subunits with different packing interactions or to helical bending within this region |
7.1.2.2 | H+-transporting two-sector ATPase |
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the catalytic site at the alphaTP-betaTP interface is loaded first upon addition of nucleotides to nucleotide-depleted F1-ATPases |
7.2.2.10 | P-type Ca2+ transporter |
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determination of enzyme activity and Ca2+ transport rates in different human muscles types are important for the local anesthetics strategy in dentistry |
7.2.2.19 | H+/K+-exchanging ATPase |
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beta1 subunit is the predominant isoform in nongastric H-K-ATPase |
7.2.2.19 | H+/K+-exchanging ATPase |
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binding and release steps of K+ and H+ in both principal conformations of the ion pump, E1 and P-E2, are electrogenic, whereas the conformation transitions do not contribute significantly to a charge movement wihtin the membrane dielectric |
7.2.2.19 | H+/K+-exchanging ATPase |
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carboxy-terminus of the H+,K+-ATPase alpha subunit facilitates the proper folding of the H+,K+-ATPase alpha/beta1 subunit complex allowing translocation to the plasma membrane where K+ uptake occurs, otherwise the complex is destined for degradation |
7.2.2.19 | H+/K+-exchanging ATPase |
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CD63 functions as a negative regulator of the colonic H+-K+-ATPase, specifically interacts with carboxy terminus of the enzyme, supression of CD63 protein synthesis in HEK-293 cells increases Rb+ uptake by the HKalpha2/NKbeta1 complex |
7.2.2.19 | H+/K+-exchanging ATPase |
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enzyme expression increases during freshwater acclimation but not exposure to hypercapnia |
7.2.2.19 | H+/K+-exchanging ATPase |
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infrared spectra on multilayer stacks of native gastric tubulovesicle membranes, membrane tilt does not significantly contribute to the infrared dichroism, even for the largest thicknesses tested |
7.2.2.19 | H+/K+-exchanging ATPase |
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Na+,K+-ATPase is likely to represent the most physiologic and efficient subunit for H+,K+-ATPase alpha subunit assembly in distal colon |
7.2.2.19 | H+/K+-exchanging ATPase |
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presence of fucosyl residues in N-linked oligosaccharidic chains in glyocoproteins of beta-H,K-ATPase subunits |
7.2.2.19 | H+/K+-exchanging ATPase |
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role of the beta subunit in stabilizing conformations of the enzyme with occluded K+ ions, alpha/beta subunit interactions may be required to compensate for the tendency of occluded K+ ions to destabalize the trans-membrane segments and are effective only in the context of correct phospholipid-protein interactions |
7.2.2.19 | H+/K+-exchanging ATPase |
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strong evidence that the catalytic unit of C12E8-solubilized gastric H/K-ATPase is a tetraprotomer |
7.2.2.19 | H+/K+-exchanging ATPase |
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the non-gastric H,K-ATPase contains similar sorting motifs in close proximity to the 4th transmembrane spanning domain than the gastric H,K-ATPase, short extracellular loop between the third and the 4th transmembrane spanning domain is critical for the pump´s apical delivery |
7.2.2.19 | H+/K+-exchanging ATPase |
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the salt bridge between Glu820 and Lys791 is essential for high-affinity K+ binding and the E2 preference of the enzyme |
7.3.2.5 | ABC-type molybdate transporter |
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specifically binds MoO42-/WO42- but not SO42-, mainly because the desolvation penalty of MoO42-/WO42- is significantly less than that of SO42- and, to a lesser extent, because the large and rigid cavity in these proteins attenuates ligand interactions with SO42-, as compared to MoO42-, exclusion of positively charged Lys/Arg side chains in the anion-binding sites of ModA, because Lys/Arg do not contribute to the selectivity of the binding pocket and substantially stabilize the complex between the oxyanion and protein ligands, which in turn would prohibit the rapid release of the bound oxyanion at a certain stage during the transport process |
7.3.2.5 | ABC-type molybdate transporter |
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transcription of modABC genes is repressed by molybdate |
7.4.2.1 | ABC-type polar-amino-acid transporter |
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BcaP is required for optimal growth in media containing free amino acids as the sole amino acid source |
7.4.2.1 | ABC-type polar-amino-acid transporter |
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conformational changes within HisP that are dependent on the presence of ATP in the binding pocket of the protein, changes are predominantely confined to the alpha-helical subdomain, considerable conformational flexibility in a conserved glutamine-containing loop |
7.4.2.1 | ABC-type polar-amino-acid transporter |
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identification of a GTPase-containing complex for Gap1p sorting in the endosomes, which has a key role in trafficking Gap1p out of the late endosome and may serve as coat proteins in this process, the complex contains the GTPases Gtr1p and Gtr2p, delivery of Gap1p to the plasma membrane depends on specific nucleotide-bound states of the GTPases, Gtr2p interacts with the C-terminal cytosolic domain of Gap1p, a tyrosine-containing motif in this domain is necessary both to bind Gtr2p and to direct sorting of Gap1p to the plasma membrane |
7.4.2.1 | ABC-type polar-amino-acid transporter |
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role of ubiquitination appears to be a signal for delivery of Gap1p to the multivesicular endosome, whereas amino acid abundance appears to control the cycling of Gap1p from the multivesicular endosome to the plasma membrane, Gap1p recycling does not depend on other known pathways for recycling proteins from the endosome to Golgi compartments |
7.4.2.1 | ABC-type polar-amino-acid transporter |
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the aromatic and neutral aliphatic amino acid permease PcMtr is unrelated to the amino acid permease family, which includes most amino acid permeases in fungi |
7.4.2.1 | ABC-type polar-amino-acid transporter |
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UfAAT3 encodes a protein with a high degree of sequence similarity to fungal amino acid permeases |
7.4.2.1 | ABC-type polar-amino-acid transporter |
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VfAAP1 expression increases seed sink strength for nitrogen, improves plant nitrogen status, and leads to higher seed protein |
7.4.2.2 | ABC-type nonpolar-amino-acid transporter |
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N-I permease is necessary for normal growth of Anabaena sp. on N2, plays a role in the diazotrophic filament specifically in vegetative cells, the products of Anabaena open reading frames all1046, all1047, all1284, alr1834 and all2912 are putative elements of the neutral amino acid permease |
7.4.2.2 | ABC-type nonpolar-amino-acid transporter |
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the aromatic and neutral aliphatic amino acid permease PcMtr is unrelated to the amino acid permease family, which includes most amino acid permeases in fungi |
7.4.2.3 | mitochondrial protein-transporting ATPase |
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mtHsp70 and Escherichia coli DnaK display different conformational and biochemical properties, chimeric Hsp70s can not complement DnaK function in vivo |
7.4.2.3 | mitochondrial protein-transporting ATPase |
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Pam16 is selectively required for preprotein translocation into the matrix, but not for protein insertion into the inner membrane, Pam16 interacts with Pam18 and is needed for the association of Pam18 with the presequence translocase and for formation of a mtHsp70-Tim44 complex |
7.4.2.3 | mitochondrial protein-transporting ATPase |
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Pam16's J-like domain strongly interacts with Pam18's J domain, leading to a productive interaction of Pam18 with mtHsp70 at the import channel |
7.4.2.3 | mitochondrial protein-transporting ATPase |
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Pam16-Pam18 complex regulates the ATpase activity of mtHsp70, Pam17 is required for the correct organization of the Pam16-Pam18 complex and thus contributes to regulation of mtHsp70 activity |
7.4.2.3 | mitochondrial protein-transporting ATPase |
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Tam41 faciliates mitochondrial protein import by maintaining the functional integrity of the TIM23 protein translocator complex, TIM44 provides an anchor for mtHsp70 to bind to the translocating polypeptide that emerges from the outlet of the TIM23 channel |
7.4.2.3 | mitochondrial protein-transporting ATPase |
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the TIM23 complex is not a static complex but switches between TOM tethering and PAM binding, including the subunit mtHsp70, in a reaction cycle involving Tim21 and Tim17 |
7.4.2.3 | mitochondrial protein-transporting ATPase |
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Tim15/Zim17 cooperates with mtHsp70 to faciliate import of presequence-containing proteins into the matrix |
7.4.2.3 | mitochondrial protein-transporting ATPase |
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TIM44 binds to the peptide-binding domain of Hsp70 and thereby recruits it to the outlet of the translocation pore, so that mtHsp70 can bind to the incoming polypeptide chain as soon as it emerges from the channel |
7.4.2.3 | mitochondrial protein-transporting ATPase |
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truncation of the N terminus of TIM17, a subunit of the TIM23 complex, severely diminishes mitochondrial import of preproteins, mitochondrial Hsp70 mediates the vectorial translocation of the preprotein into the matrix |
7.6.2.1 | P-type phospholipid transporter |
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Drs2p deficiency causes a markedly increased rate of cholesterol transport from the plasma membrane to the endoplasmic reticulum and redistribution of endogenous ergosterol to intracellular membranes |
7.6.2.9 | ABC-type quaternary amine transporter |
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betaine and carnitine transport upon low temperature exposure is mediated via three osmolyte transporters including OpuC, carnitine uptake for cryoprotective purposes, OpuB shows no significant contribution to listeral chill tolerance |
7.6.2.9 | ABC-type quaternary amine transporter |
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functional re-association of a substrate-binding protein-dependent ABC-transporter starting from the isolated subunits |
7.6.2.9 | ABC-type quaternary amine transporter |
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Na+-betaine symporter that contributes to the salt stress tolerance at alkaline pH |
7.6.2.9 | ABC-type quaternary amine transporter |
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osmotic control of the OpuA operon allows the cell to sensitively adjust the number of the OpuA transporter to the physiological need of the cell |
7.6.2.9 | ABC-type quaternary amine transporter |
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the cystathionine beta-synthase module in OpuA constitutes the ionic strength sensor whose activity is modulated by the C-terminal anionic tail |