EC Number   |
Recommended Name   |
Application   |
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  1.1.1.3 | homoserine dehydrogenase |
more |
HOM6 deletion reduces Candida albicans cell adhesion to polystyrene, which is a common plastic used in many medical devices |
 1.1.1.12 | L-arabinitol 4-dehydrogenase |
more |
covalent immobilization of purified enzyme HjLAD onto glutaraldehyde-activated silicon oxide nanoparticles shows the a high immobilization efficiency of 94.7%, comparative characterization of free and immobilized enzyme HjLAD, including its thermostability and kinetic parameters, overview. Thermostability of immobilized enzyme is 14.2-fold higher than for free HjLAD, the t1/2 of HjLAD at 25°C is enhanced from 190 min (free) to 45 h (immobilized). The immobilized HjLAD retains 94% of its initial activity after 10 cycles. Immobilization efficiencies of HjLAD onto different supports, silicon oxide nanoparticles (4830HT) show the highest efficiency, method optimization, overview |
  1.1.1.28 | D-lactate dehydrogenase |
more |
protocol for undergraduate molecular biology and biochemistry laboratory courses spanning two semesters that is organized around the LdhA gene from the yogurt-fermenting bacterium Lactobacillus bulgaricus, using commercially available yogurt. Curriculum starts with cloning the LdhA gene into a prokaryotic expression vector, followed by mRNA isolation and characterization of recombinant gene expression levels using RT-PCR. The biochemistry module begins with overexpression of the cloned LdhA gene and guides students through the process of affinity purification, biochemical characterization of the purified LdhA protein, and analysis of enzyme kinetics using various substrates and an inhibitor, concluding with a guided inquiry investigation of structure-function relationships in the three-dimensional structure of LdhA using molecular visualization software |
  1.1.1.31 | 3-hydroxyisobutyrate dehydrogenase |
more |
3-HIBADH may play a role in biosynthesis of 3-hydroxypropionate as a biological source |
  1.1.1.42 | isocitrate dehydrogenase (NADP+) |
more |
IDPm siRNA functions as a potentially useful agent for targeting chemo- and radio-resistant hypoxic cells within solid tumors through inhibition of HIF-1alpha expression |
  1.1.1.42 | isocitrate dehydrogenase (NADP+) |
more |
future clinical and bioengineering applications of hICDH can be in the development of techniques to regulate the growth of glioblastomas and to capture and store carbon dioxide |
 1.1.1.43 | phosphogluconate 2-dehydrogenase |
more |
usage of isozymes as marker for chromosome identification and evaluation of introgression of genes in apomictic mode of reproduction of Tripsacum dactyloides into Zea mays |
  1.1.1.44 | phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating) |
more |
the enzyme can be used for power production in biobatteries. Mutant N32E/R33I/T34I versus the wild-type 6PGDH are evaluated electrochemically in an anodic reaction system containing two enzymes: 6PGDH and diaphorase, a coenzyme (NADP+ or NAD+), an electron mediator AQDS, and a 6-phosphogluconate substrate. Cyclic voltammetry results clearly show that both enzymes produce significant oxidation current peaks at -0.3 V versus Ag/AgCl. The mutant N32E/R33I/T34I exhibits a current density 25% higher than that generated by the wild-type |
  1.1.1.49 | glucose-6-phosphate dehydrogenase (NADP+) |
more |
evaluation and optimization of enzyme production in Candida guilliermondii, modeling, overview |
  1.1.1.49 | glucose-6-phosphate dehydrogenase (NADP+) |
more |
because isoenzyme replacement of G6PDH in the cytosol of tobacco is beneficial under various kinds of cues, this strategy may be a tool to enhance stress tolerance in general |
  1.1.1.49 | glucose-6-phosphate dehydrogenase (NADP+) |
more |
loss of cytosolic G6PDH activity affects the metabolism of developing seeds by increasing carbon substrates for synthesis of storage compounds rather than by decreasing the NADPH supply specifically for fatty acid synthesis |
  1.1.1.80 | isopropanol dehydrogenase (NADP+) |
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the enzyme is an ideal candidate biocatalyst in the construction of coenzyme regeneration system and the enzymatic bioconversion of high value alcohols or other compounds |
  1.1.1.118 | glucose 1-dehydrogenase (NAD+) |
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application in NADPH regeneration for the asymmetric reduction of haloketone by a carbonyl reductase in organic solvent/buffer system |
  1.1.1.195 | cinnamyl-alcohol dehydrogenase |
more |
CAD is a useful tool to improve lignin digestibility and/or to lower the lignin levels in plants. Enzyme knockout modification targeted directly to block lignin synthesis causes not only reduced lignin level in fibre, but also affects amount and organization of cellulose and pectin. The process of retting in the transgenic straw is more uniform, which might contribute to an improvement in the fibre quality. Such plants can be successfully cultivated in a field |
 1.1.1.243 | carveol dehydrogenase |
more |
supply of a mixture of (-)-trans- and (-)-cis-carveol to the organism delivers pure (-)-carvone and pure (-)-cis-carveol |
  1.1.1.267 | 1-deoxy-D-xylulose-5-phosphate reductoisomerase |
more |
the enzyme is a target for development of antibacterial drugs, determination of the antimicrobial activities of various essential oils against different microbials |
 1.1.1.306 | S-(hydroxymethyl)mycothiol dehydrogenase |
more |
thiol formation and detection of MSH-dependent formaldehyde dehydrogenase activity in cell extracts are relevant to the possible modulation of nitric oxide toxicity generated by strain NRRL 5646 |
 1.1.1.324 | 8-hydroxygeraniol dehydrogenase |
more |
plant (4aR,7S,7aS)-nepetalactone can be used for synthesis of (4aR,7S,7aS)-nepetalactol, an aphid pheromone, useful in aphid control |
1.1.1.422 | pseudoephedrine dehydrogenase |
more |
both (R,S)-(-)-ephedrine and (S,S)-(+)-pseudoephedrine are constituents of various over-the-counter (OTC) drugs and are also used as decongestants and stimulants. Arthrobacter sp. TS-15 and its isolated ephedrine-oxidizing enzymes have potential for use in decontamination and synthetic applications |
  1.1.2.4 | D-lactate dehydrogenase (cytochrome) |
more |
carbon paste electrode-based biosensor with immobilized D-LCR seems to be optimal for analysis, representing significant advantage due to simplification of the whole device, i.e., the sensor exerts lower limit of detection under supposed concentration of D-lactate in real samples, low material demands, simplicity of D-LCR biosensor and short total time of analysis of about 2 min, pointing at the sensor possibilities in commercial applications |
 1.1.3.4 | glucose oxidase |
more |
GOx bioactive paper is fabricated, which can potentially be used as food packaging paper |
 1.1.3.4 | glucose oxidase |
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despite the broad range of applications for glucose oxidase, the effectiveness of glucose oxidase is restricted by the narrow substrate range of this enzyme and susceptibility to H2O2 inactivation |
 1.1.3.5 | hexose oxidase |
more |
the enzyme is a good candidate for bioelectrochemical applications. Electrochemical study of electron transfer reactions and bioelectrocatalysis of glucose oxidation by enzyme HOX immobilized on graphite electrodes |
 1.1.3.7 | aryl-alcohol oxidase |
more |
a two-enzyme system comprising a dye decolorizing peroxidase (DyP, EC 1.11.1.19) from Mycetinis scorodonius and the Pleurotus sapidus AAO enzyme is successfully employed to bleach the anthraquinone dye Reactive Blue 5. The aryl-alcohol oxidase provides the required H2O2 |
 1.1.3.17 | choline oxidase |
more |
enzyme is of both biotechnological and medical interest, since glycine betaine can be accumulated in the cytoplasm of cells to prevent dehydration and plasmolysis in adverse hyperosmotic environments in pathogenic bacteria |
 1.1.5.5 | alcohol dehydrogenase (quinone) |
more |
applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview |
 1.1.5.5 | alcohol dehydrogenase (quinone) |
more |
applications of PQQ-ADH in bioelectrocatalyst for biosensors and biofuel cells, amperometric determination of ethanol is a potential application for the PQQ-ADH electrode, overview. Development of a DET-based biofuel system by combination of electrodes coated with FAD-dependent fructose dehydrogenase of Gluconobacter sp. as an anode and laccase of mushroom as a cathode |
  1.1.7.1 | 4-hydroxybenzoyl-CoA reductase |
more |
contains three open reading frames coding for proteins with very high similiarities to 4-HBCR from Thauera aromatica with 85%, 70% and 91% identities respectively |
  1.2.1.3 | aldehyde dehydrogenase (NAD+) |
more |
enzyme ALD6 can potentially be used to treat hazardous substances to remove formaldehyde |
  1.2.1.5 | aldehyde dehydrogenase [NAD(P)+] |
more |
ALDH2 may have antioxidant properties. Yeast ALDH significantly and dose-dependently attenuates HX/XO-generated O2S- signal |
  1.2.1.5 | aldehyde dehydrogenase [NAD(P)+] |
more |
reduced ALDH-2 activity and expression leads to decreased nitroglycerin bioconversion. ALDH is an important physiological inhibitory factor of superoxide production |
  1.2.1.8 | betaine-aldehyde dehydrogenase |
more |
BADH isolated from spinach is successfully utilised for selection of chloroplast transformation of tobacco in order to prevent the risk of transferring antibiotic resistance genes to gut microbes or the environment |
  1.2.1.8 | betaine-aldehyde dehydrogenase |
more |
nitric oxide and light co-regulate glycine betaine homeostasis in sunflower seedling cotyledons by modulating betaine aldehyde dehydrogenase transcript levels and activity |
  1.2.1.11 | aspartate-semialdehyde dehydrogenase |
more |
enzyme is an attractive target for development of antibacterial, fungicidal, or herbicidal compounds |
  1.2.1.12 | glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) |
more |
selective inhibition of GAPDHS, one of the glycolytic isozymes with restricted expression during spermatogenesis, is a potential strategy for the development of a non-hormonal contraceptive that directly blocks sperm function. Detailed structural comparisons of sperm-specific glyceraldehyde 3-phosphate dehydrogenase, spermatogenic (GAPDHS) and the somatic glyceraldehyde 3-phosphate dehydrogenase (GAPDH) isozyme can facilitate the identification of selective GAPDHS inhibitors for contraceptive development |
 1.2.1.15 | malonate-semialdehyde dehydrogenase |
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iolA is indispensable for myo-inositol fermentation |
  1.2.1.16 | succinate-semialdehyde dehydrogenase [NAD(P)+] |
more |
the NADP+-dependent succinate semialdehyde dehydrogenase activity encoded by gabD appears to be important for nitrogen metabolism under N limitation conditions |
  1.2.1.19 | aminobutyraldehyde dehydrogenase |
more |
AMADH may participate in processes of adaptation to stress events caused by mechanical injury, which involve polyamine catabolism, GABA production and lignification |
  1.2.1.24 | succinate-semialdehyde dehydrogenase (NAD+) |
more |
genomic copy of the SSADH gene contains two introns. Multiple SSADH gene copies are present in the genome |
  1.2.1.24 | succinate-semialdehyde dehydrogenase (NAD+) |
more |
genomic copy of the SSADH gene is devoid of introns. Multiple SSADH gene copies are present in the genome |
  1.2.1.24 | succinate-semialdehyde dehydrogenase (NAD+) |
more |
in the world population, the c.538C variant of SSADH is proceeding to replace the ancestral c.538T, shared with primates. A significant correlation between the frequencies of the derived alleles in SSADH and microcephalin, which show concerted changes worldwide and, at least in Asian populations, also on a restricted geographical scale |
  1.2.1.24 | succinate-semialdehyde dehydrogenase (NAD+) |
more |
yneI, responsible for NAD+/NADP+-dependent SSADH activity, plays a unique physiological role in the general nitrogen metabolism of Escherichia coli. The yneI gene has an important, but not essential, role during growth on arginine and probably has an essential function during growth on putrescine as the nitrogen source. The yneI-encoded activity functions primarily as a valve to prevent toxic accumulation of succinate semialdehyde |
  1.2.1.26 | 2,5-dioxovalerate dehydrogenase |
more |
the ALDH branch including ycbD protein is designated the KGSADH subclass (type III) |
  1.2.1.26 | 2,5-dioxovalerate dehydrogenase |
more |
three different types of KGSADH appear in the bacterial evolutional stage convergently |
  1.2.1.32 | aminomuconate-semialdehyde dehydrogenase |
more |
codG encoding 2-hydroxymuconic semialdehyde dehydrogenase shows a higher degree of similarity to those genes in classical bacteria |
 1.2.1.36 | retinal dehydrogenase |
more |
Raldh3 is a zebrafish ortholog of mammalian Raldh3. The predicted protein encoded by zebrafish raldh3 exhibits 70.0% amino acid identity with mouse Raldh3 |
 1.2.1.36 | retinal dehydrogenase |
more |
Raldh4 is a zebrafish ortholog of mammalian Raldh4. The predicted protein encoded by zebrafish raldh4 exhibits 73.5% amino acid identity with mouse Raldh4 |
 1.2.1.36 | retinal dehydrogenase |
more |
RDH13 is significantly different from related RDH11, RDH12 and RDH14 in that it is targeted to the mitochondria, but at the same time, RDH13 is very similar to the members of the RDH11-14 cluster of short-chain dehydrogenases/reductases in terms of its substrate and cofactor preferences. It may function to protect mitochondria against oxidative stress associated with the highly reactive retinaldehyde produced from dietary beta-carotene |
 1.2.1.36 | retinal dehydrogenase |
more |
similar localization of Rdh12 and RDH12 proteins in mouse and human photoreceptors, respectively, which may indicate an analogous physiological role of the enzymes in both species |
  1.2.1.38 | N-acetyl-gamma-glutamyl-phosphate reductase |
more |
rapid, highly sensitive, and reproducible coupled enzyme assays for AGS, AGK, and GAT using recombinant Escherichia coli AGK and AGPR as coupling enzymes |
  1.2.1.41 | glutamate-5-semialdehyde dehydrogenase |
more |
the genes proH encoding pyrroline-5-carboxylate reductase, proJ encoding glutamate-5-kinase, and proA encoding glutamate-5-semialdehyde dehydrogenase form a transcriptional unit. This pro operon is involved in salinity-induced proline biosynthesis |
  1.2.1.44 | cinnamoyl-CoA reductase |
more |
CCR1 is present as a single-copy gene in the wheat genome. It groups together with other monocot CCR sequences while it diverges from CCR2. It may be involved in the regulation of lignin biosynthesis during stem maturity and may contribute to stem strength support in wheat |
  1.2.1.44 | cinnamoyl-CoA reductase |
more |
the thioacidolysis monomer 1,2,2-trithioethyl ethylguaiacol is a general marker for incorporation of ferulic acid into the lignification process, and is an indicator that can be used judiciously for CCR downregulation in a variety of plants as long as the background levels in control materials are measured |
1.2.1.61 | 4-hydroxymuconic-semialdehyde dehydrogenase |
more |
HapE shows 45% sequence identity with CymC, a p-cumic aldehyde dehydrogenase, from Pseudomonas putida |
 1.2.1.65 | salicylaldehyde dehydrogenase |
more |
two genes code for salicylaldehyde dehydrogenase. NahF resides in the naphthalene degradation upper pathway operon as the meta-cleavage pathway gene, whereas NahV is situated outside of this operon. NahF-like genes occur in all naphthalene-degradation bacteria, whereas nahV-like genes are present in only some naphthalene-degrading bacteria |
 1.2.1.65 | salicylaldehyde dehydrogenase |
more |
two genes code for salicylaldehyde dehydrogenase. NahF resides in the naphthalene degradation upper pathway operon as the meta-cleavage pathway gene, whereas NahV is situated outside of this operon. NahF-like genes occurr in all naphthalene-degradation bacteria, whereas nahV-like genes are present in only some naphthalene-degrading bacteria |
  1.2.1.70 | glutamyl-tRNA reductase |
more |
the function of GluTR is regulated by mechanisms that involve the steady-state level of the protein or the activity of the enzyme in response to the cellular heme status |
  1.2.1.70 | glutamyl-tRNA reductase |
more |
the tetrapyrrole biosynthetic pathway is controlled by HEMA2 and FC1, which normally functions for heme biosynthesis in nonphotosynthetic tissues, but is induced in photosynthetic tissues under oxidative conditions to supply heme for defensive hemoproteins outside plastids |
 1.2.1.95 | L-2-aminoadipate reductase |
more |
the sequence of the Saccharomycopsis fibuligera alpha-aminoadipate reductase gene Lys2p has the highest identity of 53% with the AAR of Candida albicans SC5314 and an identity of 51% with that of Saccharomyces cerevisiae. Expression of the ORF of SfLYS2 in a lys2- strain of Saccharomyces cerevisiae can functionally complement the lysine mutant of the Saccharomyces cerevisiae strain. Cloning of SfLYS2 may provide a general tool in developing genetics-based studies not only with Saccharomycopsis fibuligera but also with Saccharomyces cerevisiae |
  1.2.1.105 | 2-oxoglutarate dehydrogenase system |
more |
alpha-ketoglutarate-involving reactions belong to the backbone of high-flux reactions, which is rather conserved in evolution |
  1.2.1.105 | 2-oxoglutarate dehydrogenase system |
more |
in post-mortem mice brain samples the activity is quickly lost, whereas the activity of another TPP-dependent enzyme, PDH, remains unalterd for at least 24 h |
 1.2.3.1 | aldehyde oxidase |
more |
96% amino acid identity with those of human enzyme. Two forms of aldehyde oxidase in monkey are the expression products by a single gene due to possibly existence of two aldehyde oxidase isoforms or two active sites in a single enzyme |
 1.2.3.1 | aldehyde oxidase |
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aldehyde oxidase is involved in the chemo-reception of pheromonal stimuli in the antennae |
 1.2.3.1 | aldehyde oxidase |
more |
despite divergent evolution, AOXs from the molybdo-flavoenzyme family can share a common function in insects and vertebrates, i.e. the control of the duration and/or strength of olfactory stimuli |
 1.2.3.1 | aldehyde oxidase |
more |
rat strains with low aldehyde oxidase activity show only a monomer, whereas strains with high activity overwhelmingly exhibit a dimer. Expression levels of aldehyde oxidase homodimer are primarily responsible for rat strain differences in aldehyde oxidase activity |
 1.2.3.1 | aldehyde oxidase |
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variations in the levels of aldehyde oxidase activity in different strains of experimental animals |
 1.2.3.1 | aldehyde oxidase |
more |
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOH1 by androgens and estrogens |
 1.2.3.1 | aldehyde oxidase |
more |
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 and AOH1 by androgens and estrogens |
 1.2.3.1 | aldehyde oxidase |
more |
variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Gender-specific regulation of AOX1 by androgens and estrogens |
 1.2.3.1 | aldehyde oxidase |
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variations in the levels of aldehyde oxidase activity in different strains of experimental animals. Rat strains with low aldehyde oxidase activity lack the ability to produce the catalytically active dimer and express only the monomeric form of the enzyme |
 1.2.3.3 | pyruvate oxidase |
more |
aerobiosis makes the concerted action of lactate oxidase and pyruvate oxidase possible, enabling cells of Streptococcus pneumoniae to gain more ATP from glucose than under anaerobiosis |
 1.2.3.3 | pyruvate oxidase |
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development of a biosensor based on POX enzyme for the investigation of the effect of thiamine (vitamin B1) molecule on the activity of the enzyme |
 1.2.3.3 | pyruvate oxidase |
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optimization of the medium for PyOD production by recombinant Escherichia coli using shake flask method |
 1.2.3.3 | pyruvate oxidase |
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pyruvate oxidase is not only a stationary-phase enzyme. Removal of the poxB gene affects the central metabolism at the enzyme level |
1.2.3.6 | pyruvate oxidase (CoA-acetylating) |
more |
pneumococcal spxB gene influences competence, the mechanism remains elusive |
1.2.3.6 | pyruvate oxidase (CoA-acetylating) |
more |
spxB transcription is regulated by both cis- and trans-acting regulatory elements |
 1.2.4.4 | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) |
more |
activation of the translational regulators by leucine is partly regulated by the activity of BCKDH complex |
 1.2.4.4 | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) |
more |
NMR techniques to determine the structure of hbSBD and dynamics of several truncated constructs from the E2 component, including hbLBD (residues 184), hbSBD (residues 111149), and a di-domain (hbDD) (residues 1166) comprising hbLBD, hbSBD and the interdomain linker, the presence of the interdomain linker restricts the motional freedom of the hbSBD more significantly than hbLBD, the linker region likely exists as a soft rod rather than a flexible string in solution |
 1.2.4.4 | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) |
more |
regulation of BCKD kinase expression by nutritional, hormonal, and pathological factors |
 1.2.4.4 | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) |
more |
use of a microRNA to exert control on a metabolic pathway of amino acid catabolism |
  1.3.1.3 | DELTA4-3-oxosteroid 5beta-reductase |
more |
5beta-POR is highly conserved within the genus Digitalis and the respective genes and proteins share considerable homology to putative progesterone reductases from other plant species |
  1.3.1.3 | DELTA4-3-oxosteroid 5beta-reductase |
more |
inspection of the MAD-phased electron-density map shows that 5beta-POR is a Rossmann-type reductase and the quality of the map is such that it is anticipated that a complete atomic model of 5beta-POR may readily be built |
  1.3.1.3 | DELTA4-3-oxosteroid 5beta-reductase |
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P5betaR belongs to the short-chain dehydrogenase/reductase (SDR) superfamily, bearing no structural homology to its mammalian counterpart, which is a member of the aldo-keto reductase (AKR) superfamily |
  1.3.1.3 | DELTA4-3-oxosteroid 5beta-reductase |
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significant homology to the putative progesterone 5beta-reductases isolated from other plant species, such as Digitalis lanata (ca. 98% identical) and Arabidopsis thaliana (ca. 69% identical) |
  1.3.1.12 | prephenate dehydrogenase |
more |
Mycobacterium tuberculosis PDH is a monofunctional protein, does not possess any chorismate mutase activity unlike many other enteric bacteria |
  1.3.1.22 | 3-oxo-5alpha-steroid 4-dehydrogenase (NADP+) |
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two isoenzymes of 5alphaR is probably characteristic of the whole plant kingdom |
  1.3.1.24 | biliverdin reductase |
more |
BVR regualtes cellular levels of biliverdin, a potent gene regulator and determinant factor for dorsal axis development in Xenopus larva |
  1.3.1.24 | biliverdin reductase |
more |
interacts with the insulin receptor kinase domain, key factor in the MAPK pathway and the PI3K pathway as well as regulating PKC isoforms that link the two pathways, plays a role in the mechanism of insulin resistance |
  1.3.1.24 | biliverdin reductase |
more |
potential function in propagation of signals relayed through protein kinase C, binds to protein kinase C betaII, increases its phosphorylation, and is a substrate for the kinase, increases PMA-dependent c-fos activation and protein kinase C translocation to the membrane |
  1.3.1.24 | biliverdin reductase |
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potential role in the insulin signaling pathway, BVR is both a substrate for insulin receptor tyrosine kinase activity and a kinase for serine phosphorylation of insulin receptor substrate 1 |
  1.3.1.24 | biliverdin reductase |
more |
regulates oxidative response and HO-1 expression |
  1.3.1.32 | maleylacetate reductase |
more |
graDAFCBE genes are responsible as an operon for the growth of Rhizobium sp. strain MTP-10005 on gamma-resorcylate and are probably regulated by GraR at the transcriptional level, first report of the gamma-resorcylate catabolic pathway in an aerobic bacterium |
  1.3.2.3 | L-galactonolactone dehydrogenase |
more |
ascorbate, which fulfils well recognized, signalling functions in plants, decliney in a regulated manner during nodule development, indicates a development-related shift in redox-linked metabolite cross-talk that underpins the development and aging processes |
  1.3.2.3 | L-galactonolactone dehydrogenase |
more |
despite limitations on L-GalL synthesis by regulation of early steps in the ascorbic acid synthesis pathway, the regulation of L-GalLDH activity via the interaction of light and respiratory controls is a crucial determinant of the overall ability of leaves to produce and accumulate ascorbic acid |
  1.3.2.3 | L-galactonolactone dehydrogenase |
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GalLDH protein and activity cannot be used as an indicator for changes in the capacity for ascorbate biosynthesis, thus ascorbic acid biosynthesis is constrained by other factors under stress |
  1.3.2.3 | L-galactonolactone dehydrogenase |
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possibility of the generation of plants that have resistance to environmental stresses by increasing their L-ascorbic acid content |
  1.3.3.3 | coproporphyrinogen oxidase |
more |
cloned KlHEM13 is functional and able to replace its homologous gene in Saccharomyces cerevisiae |
  1.3.3.3 | coproporphyrinogen oxidase |
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cpx1 and cpx2 genes encode almost identical, catalytically active enzymes with distinctive N-terminal peptide sequences, cpx1 encodes a plastid transit peptide, whereas this region is deleted from the cpx2 gene, the 5' regions of both messenger RNAs are highly similar, but the cpx2 gene has an open-reading frame that can encode a new targeting signal |
  1.3.3.3 | coproporphyrinogen oxidase |
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functions as a homodimer in solution |
  1.3.3.4 | protoporphyrinogen oxidase |
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in rice plants, outstanding resistance to Protox-inhibiting herbicides can be achieved by expression of Myxococcus xanthus Protox |