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Results 1 - 53 of 53
EC Number Recommended Name Reaction Type Commentary Organism Primary Accession No.
Show all pathways known for 1.7.3.3Display the word mapDisplay the reaction diagram Show all sequences 1.7.3.3factor-independent urate hydroxylase More the enzyme catalyzes the degradation of urate to [S]-allantoin through 5-hydroxyisourate as a metastable intermediate Aspergillus flavus Q00511
Show all pathways known for 1.8.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.2assimilatory sulfite reductase (NADPH) More sodium salts of thiosulfate and sulfate do not serve as the electron acceptor for reduced F420 oxidation by Fsr. Also, Fsr can not use NADH and NADPH for the reduction of sulfite. Methanocaldococcus jannaschii -
Show all pathways known for 1.8.1.2Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.2assimilatory sulfite reductase (NADPH) More the N-terminal half of Fsr represents a H2F420 dehydrogenase and the C-terminal half a dissimilatory-type siroheme sulfite reductase, and Fsr catalyzes the corresponding partial reactions Methanocaldococcus jannaschii -
Show all pathways known for 1.8.1.9Display the word mapDisplay the reaction diagram Show all sequences 1.8.1.9thioredoxin-disulfide reductase More the enzyme utilizes oxygen, requires NADH or NADPH, and readily generates the reduced paraquat radical Mus musculus -
Show all pathways known for 1.8.3.1Display the word mapDisplay the reaction diagram Show all sequences 1.8.3.1sulfite oxidase More the enzyme also functions as a selenite oxidase Arabidopsis thaliana -
Show all pathways known for 1.8.7.1Display the word mapDisplay the reaction diagram Show all sequences 1.8.7.1assimilatory sulfite reductase (ferredoxin) More sodium salts of thiosulfate and sulfate does not serve as the electron acceptor for reduced F420 oxidation by Fsr. Also, Fsr can not use NADH and NADPH for the reduction of sulfite. Methanocaldococcus jannaschii -
Show all pathways known for 1.8.7.1Display the word mapDisplay the reaction diagram Show all sequences 1.8.7.1assimilatory sulfite reductase (ferredoxin) More the N-terminal half of Fsr represents a H2F420 dehydrogenase and the C-terminal half a dissimilatory-type siroheme sulfite reductase, and Fsr catalyzes the corresponding partial reactions Methanocaldococcus jannaschii -
Show all pathways known for 3.1.3.18Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.18phosphoglycolate phosphatase More - Nicotiana tabacum -
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.43[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase More PDP activity and protein content is higher in fast-twitch oxidative glycolytic muscles, food deprivation decreases PDP activity in all muscle types, PDP2 declines in fast-twitch oxidative glycolytic muscle Rattus norvegicus -
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.43[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase More PDP1 belongs to the PPM family of protein serine/threonine phosphatases Rattus norvegicus O88483
Show all pathways known for 3.1.3.45Display the reaction diagram Show all sequences 3.1.3.453-deoxy-manno-octulosonate-8-phosphatase More KDO-phosphatase is not essential for viability of Escherichia coli Escherichia coli -
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.53[myosin-light-chain] phosphatase More cardiac derived MYPT2 and smooth muscle derived MYPT2 have similar properties Mammalia -
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.53[myosin-light-chain] phosphatase More MYTP1 binds the catalytic subunit of type 1 phosphatase delta, binds many proteins like myosin II, ezrin, radixin, moesin, a-adducin, tau, MAP, elongation factor-1a, ZIP kinase, RhoA-GTP, key reaction is dephosphorylation of myosin II but also in cell migration, cell division Mammalia -
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.60phosphoenolpyruvate phosphatase More PEP phosphatase increases as active Fe decreases Vitis labrusca x Vitis vinifera -
Display the word mapDisplay the reaction diagram Show all sequences 3.1.4.12sphingomyelin phosphodiesterase More SMase belongs to the family of interfacial enzymes that carry out processive catalytic turnover at the interface, SMase binds rapidly and avidly to sphingomyelin vesicles and it is fully active as a monomer at the interface Bacillus cereus -
Display the word mapDisplay the reaction diagram Show all sequences 3.4.21.22coagulation factor IXa More amidolytic activity Homo sapiens -
Display the word mapDisplay the reaction diagram Show all sequences 3.4.22.61caspase-8 More caspase-8 also regulates cell motility Mus musculus O89110
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.81ADAM10 endopeptidase More ADAM10 mediates the epidermal growth factor-induced CD44 cleavage by the small monomeric GTPase Rac1 Homo sapiens -
Display the word mapDisplay the reaction diagram Show all sequences 3.6.5.3protein-synthesizing GTPase More anti-association activity for splitted 70S ribosomes subunits Escherichia coli -
Display the word mapDisplay the reaction diagram Show all sequences 3.6.5.3protein-synthesizing GTPase More influence on translation initiation pathway and ribosomal subunit joining Saccharomyces cerevisiae -
Display the word mapDisplay the reaction diagram Show all sequences 3.6.5.3protein-synthesizing GTPase More together with ribosome recycling factor and GTP transient split of 70S ribosomes into subunits Escherichia coli -
Show all pathways known for 4.1.3.43Display the reaction diagram Show all sequences 4.1.3.434-hydroxy-2-oxohexanoate aldolase More BphI exhibits a compulsory order mechanism, with pyruvate binding first Paraburkholderia xenovorans -
Display the reaction diagram Show all sequences 4.1.99.263-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethylpyrrolidin-2-one synthase More enzyme MftC catalyzes two distinct chemistries in the same active, an oxidative decarboxylation of the C-terminus and a subsequent redox neutral C-C bond formation Mycobacterium ulcerans A0PM49, A0PM49
Show all pathways known for 4.2.1.84Display the word mapDisplay the reaction diagram Show all sequences 4.2.1.84nitrile hydratase More a new biocatalytic mechanism is proposed, that is based on crystallographic data of the active center Rhodococcus erythropolis -
Show all pathways known for 4.2.2.5Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.5chondroitin AC lyase More no beta-elimination Pedobacter heparinus -
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.7heparin lyase More random endolytic attack Pedobacter heparinus -
Display the word mapDisplay the reaction diagram Show all sequences 4.2.2.7heparin lyase More random endolytic attack Rattus norvegicus -
Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.22germacradienol synthase More germacradienol/geosmin synthase is a bifunctional enzyme in which the N-terminal domain of the protein converts farnesyl diphosphate, while the C-terminal domain catalyzes the transformation of germacradienol to geosmin Streptomyces coelicolor -
Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.22germacradienol synthase More putative function is as a germacradienol synthase/terpene cyclase Streptomyces peucetius B0FLN6
Show all pathways known for 4.2.3.4Display the word mapDisplay the reaction diagram Show all sequences 4.2.3.43-dehydroquinate synthase More DHQS itself is of interest because it apparently catalyzes five individual reactions, alcohol oxidation, phosphate omega-elimination, carbonyl reduction, ring opening and intramolecular aldol condensation, in a single active site as well as being a drug target Xanthomonas oryzae -
Display the word mapDisplay the reaction diagram Show all sequences 4.2.99.18DNA-(apurinic or apyrimidinic site) lyase More APE1 possesses endonuclease, exonuclease and phosphodiesterase activity Homo sapiens -
Show all pathways known for 4.4.1.13Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.13cysteine-S-conjugate beta-lyase More - Fusobacterium varium -
Show all pathways known for 4.4.1.13Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.13cysteine-S-conjugate beta-lyase More - Homo sapiens -
Show all pathways known for 4.4.1.13Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.13cysteine-S-conjugate beta-lyase More - Rattus norvegicus -
Show all pathways known for 4.4.1.13Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.13cysteine-S-conjugate beta-lyase More identical with glutamine transaminase K Rattus norvegicus -
Show all pathways known for 4.4.1.13Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.13cysteine-S-conjugate beta-lyase More kynureninase reaction and beta-elimination Rattus norvegicus -
Show all pathways known for 4.4.1.13Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.13cysteine-S-conjugate beta-lyase More shows identity with a soluble kynurenine aminotransferase from rat brain Rattus norvegicus -
Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.141-aminocyclopropane-1-carboxylate synthase More 14-3-3 protein may inhibit binding to ethylene overproducer 1 proteins, resulting in 1-aminocyclopropane-1-carboxylate and ethylene synthesis Oryza sativa Q10DK7
Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.141-aminocyclopropane-1-carboxylate synthase More by Agrobacterium mediated transformation, two transgenic pineapple lines have been produced containing co-suppression constructs designed to down-regulate the expression of the ACACS2 gene Ananas comosus -
Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.141-aminocyclopropane-1-carboxylate synthase More high levels of expression of CyACS1 in the necrotic inflorescences of wild-type Cymbidium at high temperatures, no bud necrosis in the mericlone mutant, but application of exogenous ACC or ethephon to the young inflorescences of nhn restored the high-temperature necrosis response Cymbidium hybrid cultivar A0JBY6
Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.141-aminocyclopropane-1-carboxylate synthase More LE-ACS3 shows a strong interaction with the protein ethylene overproducer 1, the C-terminal tail of ACS is essential for the interaction with ethylene overproducer 1 and signals the proteasome-dependent protein destabilization Solanum lycopersicum Q42881
Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.141-aminocyclopropane-1-carboxylate synthase More two introns are in the genomic DNA sequence, Southern blot analysis suggests that there might be a multi-gene family encoding for ACC synthase, alignment analysis shows a close association with the wound-inducible ACS of citrus Gossypium hirsutum A9NIT9
Show all pathways known for 4.4.1.20Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.20leukotriene-C4 synthase More multiple constructs encoding fusion proteins of green fluorescent protein as the N-terminal part and various truncated variants of human LTC4S as C-terminal part were prepared and transfected into HEK 293/T or COS-7 cells Homo sapiens Q16873
Show all pathways known for 4.4.1.21Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.21S-ribosylhomocysteine lyase More absorption and electron paramagnetic resonance spectroscopic studies reveals that the active form of LuxS contains a metal-bound water and a thiolate ion at Cys-83, an invariant Arg-39 in the active site is partially responsible for stabilizing the thiolate anion of Cys-83 Escherichia coli P45578
Show all pathways known for 4.4.1.21Display the word mapDisplay the reaction diagram Show all sequences 4.4.1.21S-ribosylhomocysteine lyase More Bacillus subtilis can use methionine as sole sulfur source, the BsluxS knockout mutant grows poorly in the presence of methionine compared to the wild-type strain, methionine utilization requires first its conversion to homocysteine Bacillus subtilis O34667
Show all pathways known for 4.8.1.2Display the word mapDisplay the reaction diagram Show all sequences 4.8.1.2aliphatic aldoxime dehydratase More electronic absorption, resonance Raman spectroscopy, electronic paramagnetic resonance and rapid scanning spectroscopy shows that ferric OxdB contains a six-coordinate high-spin heme, the substrate is bound to the ferric heme via its oxygen atom, the coordination structure of the heme-aldoxime complex changes redox-dependent Bacillus sp. (in: Bacteria) -
Show all pathways known for 4.8.1.2Display the word mapDisplay the reaction diagram Show all sequences 4.8.1.2aliphatic aldoxime dehydratase More electronic absorption, resonance Raman spectroscopy, electronic paramagnetic resonance and rapid scanning spectroscopy shows that ferric OxdB contains a six-coordinate high-spin heme, the substrate is bound to the ferric heme via its oxygen atom, the coordination structure of the heme-aldoxime complex changes redox-dependent Rhodococcus sp. -
Show all pathways known for 4.8.1.2Display the word mapDisplay the reaction diagram Show all sequences 4.8.1.2aliphatic aldoxime dehydratase More resonance Raman spectroscopy shows that an reaction intermediate of the hemecontaining enzyme with a highly oxidized heme is formed concomitantly upon direct binding of a substrate Pseudomonas chlororaphis -
Show all pathways known for 5.1.3.2Display the word mapDisplay the reaction diagram Show all sequences 5.1.3.2UDP-glucose 4-epimerase More catalyses the interconversion of UDP-Gal and UDPGlc Escherichia coli -
Show all pathways known for 5.1.3.2Display the word mapDisplay the reaction diagram Show all sequences 5.1.3.2UDP-glucose 4-epimerase More catalyses the interconversion of UDP-Gal and UDPGlc Hordeum vulgare Q58IJ6
Show all pathways known for 5.1.3.2Display the word mapDisplay the reaction diagram Show all sequences 5.1.3.2UDP-glucose 4-epimerase More HvUGE also catalyses the interconversion of UDP-GalNAc and UDP-GlcNAc, although it is not known if this has any biological significance. Hordeum vulgare Q58IJ6
Show all pathways known for 6.3.2.1Display the word mapDisplay the reaction diagram Show all sequences 6.3.2.1pantoate-beta-alanine ligase (AMP-forming) More pantothenate synthetase catalyzes the formation of a pantoyl-adenylate intermediate upon the ordered addition of ATP and pantoate Mycobacterium tuberculosis -
Show all pathways known for 6.3.4.15Display the word mapDisplay the reaction diagram Show all sequences 6.3.4.15biotin-[biotin carboxyl-carrier protein] ligase More biotinylation, mediates attachment of biotin to a fusion protein of a biotin acceptor peptide and GLuc, EC 1.13.12.5 Escherichia coli K-12 P06709
Results 1 - 53 of 53