EC Number |
Recommended Name |
Reaction Type |
Organism |
Primary Accession No. |
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1.7.3.3 | factor-independent urate hydroxylase |
More |
the enzyme catalyzes the degradation of urate to [S]-allantoin through 5-hydroxyisourate as a metastable intermediate |
Aspergillus flavus |
Q00511 |
1.8.1.2 | assimilatory 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 |
- |
1.8.1.2 | assimilatory 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 |
- |
1.8.1.9 | thioredoxin-disulfide reductase |
More |
the enzyme utilizes oxygen, requires NADH or NADPH, and readily generates the reduced paraquat radical |
Mus musculus |
- |
1.8.3.1 | sulfite oxidase |
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the enzyme also functions as a selenite oxidase |
Arabidopsis thaliana |
- |
1.8.7.1 | assimilatory sulfite reductase (ferredoxin) |
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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 |
- |
1.8.7.1 | assimilatory 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 |
- |
3.1.3.18 | phosphoglycolate phosphatase |
More |
- |
Nicotiana tabacum |
- |
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 |
- |
3.1.3.43 | [pyruvate dehydrogenase (acetyl-transferring)]-phosphatase |
More |
PDP1 belongs to the PPM family of protein serine/threonine phosphatases |
Rattus norvegicus |
O88483 |
3.1.3.45 | 3-deoxy-manno-octulosonate-8-phosphatase |
More |
KDO-phosphatase is not essential for viability of Escherichia coli |
Escherichia coli |
- |
3.1.3.53 | [myosin-light-chain] phosphatase |
More |
cardiac derived MYPT2 and smooth muscle derived MYPT2 have similar properties |
Mammalia |
- |
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 |
- |
3.1.3.60 | phosphoenolpyruvate phosphatase |
More |
PEP phosphatase increases as active Fe decreases |
Vitis labrusca x Vitis vinifera |
- |
3.1.4.12 | sphingomyelin 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 |
- |
3.4.21.22 | coagulation factor IXa |
More |
amidolytic activity |
Homo sapiens |
- |
3.4.22.61 | caspase-8 |
More |
caspase-8 also regulates cell motility |
Mus musculus |
O89110 |
3.4.24.81 | ADAM10 endopeptidase |
More |
ADAM10 mediates the epidermal growth factor-induced CD44 cleavage by the small monomeric GTPase Rac1 |
Homo sapiens |
- |
3.6.5.3 | protein-synthesizing GTPase |
More |
anti-association activity for splitted 70S ribosomes subunits |
Escherichia coli |
- |
3.6.5.3 | protein-synthesizing GTPase |
More |
influence on translation initiation pathway and ribosomal subunit joining |
Saccharomyces cerevisiae |
- |
3.6.5.3 | protein-synthesizing GTPase |
More |
together with ribosome recycling factor and GTP transient split of 70S ribosomes into subunits |
Escherichia coli |
- |
4.1.3.43 | 4-hydroxy-2-oxohexanoate aldolase |
More |
BphI exhibits a compulsory order mechanism, with pyruvate binding first |
Paraburkholderia xenovorans |
- |
4.1.99.26 | 3-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 |
4.2.1.84 | nitrile hydratase |
More |
a new biocatalytic mechanism is proposed, that is based on crystallographic data of the active center |
Rhodococcus erythropolis |
- |
4.2.2.5 | chondroitin AC lyase |
More |
no beta-elimination |
Pedobacter heparinus |
- |
4.2.2.7 | heparin lyase |
More |
random endolytic attack |
Pedobacter heparinus |
- |
4.2.2.7 | heparin lyase |
More |
random endolytic attack |
Rattus norvegicus |
- |
4.2.3.22 | germacradienol synthase |
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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 |
- |
4.2.3.22 | germacradienol synthase |
More |
putative function is as a germacradienol synthase/terpene cyclase |
Streptomyces peucetius |
B0FLN6 |
4.2.3.4 | 3-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 |
- |
4.2.99.18 | DNA-(apurinic or apyrimidinic site) lyase |
More |
APE1 possesses endonuclease, exonuclease and phosphodiesterase activity |
Homo sapiens |
- |
4.4.1.13 | cysteine-S-conjugate beta-lyase |
More |
- |
Fusobacterium varium |
- |
4.4.1.13 | cysteine-S-conjugate beta-lyase |
More |
- |
Homo sapiens |
- |
4.4.1.13 | cysteine-S-conjugate beta-lyase |
More |
- |
Rattus norvegicus |
- |
4.4.1.13 | cysteine-S-conjugate beta-lyase |
More |
identical with glutamine transaminase K |
Rattus norvegicus |
- |
4.4.1.13 | cysteine-S-conjugate beta-lyase |
More |
kynureninase reaction and beta-elimination |
Rattus norvegicus |
- |
4.4.1.13 | cysteine-S-conjugate beta-lyase |
More |
shows identity with a soluble kynurenine aminotransferase from rat brain |
Rattus norvegicus |
- |
4.4.1.14 | 1-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 |
4.4.1.14 | 1-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 |
- |
4.4.1.14 | 1-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 |
4.4.1.14 | 1-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 |
4.4.1.14 | 1-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 |
4.4.1.20 | leukotriene-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 |
4.4.1.21 | S-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 |
4.4.1.21 | S-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 |
4.8.1.2 | aliphatic 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) |
- |
4.8.1.2 | aliphatic 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. |
- |
4.8.1.2 | aliphatic 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 |
- |
5.1.3.2 | UDP-glucose 4-epimerase |
More |
catalyses the interconversion of UDP-Gal and UDPGlc |
Escherichia coli |
- |
5.1.3.2 | UDP-glucose 4-epimerase |
More |
catalyses the interconversion of UDP-Gal and UDPGlc |
Hordeum vulgare |
Q58IJ6 |
5.1.3.2 | UDP-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 |
6.3.2.1 | pantoate-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 |
- |
6.3.4.15 | biotin-[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 |