EC IUBMB specificity_promiscuity_comment KEGG reaction_typing 5.1.1.8 Also interconverts trans-4-hydroxy-D-proline and cis-4-hydroxy-L-proline. stereisomer promiscuity single NA 5.1.1.9 NA NA multi NA 5.1.1.10 NA NA multi generic 5.1.1.13 Also acts, at half the rate, on L-alanine. substrate promiscuity single NA 5.1.1.14 NA NA multi NA 5.1.1.15 Also racemises 2-aminopentano-5-lactam (α-amino-δ-valerolactam) and 2-amino-4-thiahexano-6-lactam (where S replaces CH2 of C-4). It does not catalyse the racemisation of α-amino acids but has some transaminase activity with them. substrate promiscuity and substrate specificity single NA 5.1.1.16 The enzyme specifically interconverts the configuration of Ser-46 of the peptide ω-agatoxin-KT, found in the venom of the funnel web spider, Agelenopsis aperta, but not that of the other serine residue, Ser-28. substrate promiscuity and substrate specificity single NA 5.1.1.18 The reaction can also occur in the reverse direction but does so more showly at physiological serine concentrations reversibility single NA 5.1.1.20 In vitro the enzyme from E.coli epimerizes several L-Ala-L-X dipeptides with broader specificity than the enzyme from B.subtilis. substrate promiscuity and species specificity single NA 5.1.1.21 The enzyme, characterized from the bacterium Lactobacillus buchneri, specifically catalyses racemization of nonpolar amino acids at the C-2 position. substrate specificity single NA 5.1.2.2 NA NA multi different reactants 5.1.3.1 The enzyme also converts D-erythrose 4-phosphate into D-erythrulose 4-phosphate and D-threose 4-phosphate. substrate promiscuity single NA 5.1.3.2 Also acts on UDP-2-deoxyglucose. substrate promiscuity multi different reactants 5.1.3.3 Also acts on L-arabinose, D-xylose, D-galactose, maltose and lactose. substrate promiscuity multi generic 5.1.3.9 NA NA multi generic 5.1.3.11 The enzyme catalyses the interconversion between D-glucose and D-mannose residues at the reducing end of β-1,4-linked disaccharides by epimerizing the hydroxyl group at the C-2 position of the glucose moiety. substrate promiscuity multi generic 5.1.3.14 This bacterial enzyme catalyses the reversible interconversion of UDP-GlcNAc and UDP-ManNAc. reversibility multi partial 5.1.3.17 It does not act on glucuronate residues that are O-sulfated or are adjacent to N-acetylglucosamine residues that are O-sulfated at the 6 position. Thus the epimerization from D-glucuronate to L-iduronate occurs after N-sulfation of glucosamine residues but before O-sulfation. substrate specificity single NA 5.1.3.21 The enzyme catalyses the interconversion of α and β anomers of maltose more effectively than those of disaccharides such as lactose and cellobiose. substrate promiscuity single NA 5.1.3.23 The enzyme is highly specific as UDP-α-D-GlcNAc, UDP-α-D-GlcNAcA (UDP-2-acetamido-2-deoxy-α-D-glucuronic acid) and UDP-α-D-GlcNAc3NAc (UDP-2,3-diacetamido-2,3-dideoxy-α-D-glucose) cannot act as substrates. substrate specificity single NA 5.1.3.29 This enzyme shows no 1-epimerase activity with D-glucose, L-rhamnose and D-fucose substrate specificity single NA 5.1.3.30 The enzyme is highly specific for D-psicose and shows very low activity with D-tagatose. substrate specificity single NA 5.1.3.31 The enzymes isolated from the bacteria Pseudomonas cichorii, Pseudomonas sp. ST-24, Rhodobacter sphaeroides and Mesorhizobium loti catalyse the epimerization of various ketoses at the C3 position, interconverting D-fructose and D-psicose, D-tagatose and D-sorbose, D-ribulose and D-xylulose, and L-ribulose and L-xylulose. The specificity depends on the species. substrate promiscuity and species specificity multi different reactants 5.1.3.32 The enzyme is specific for L-rhamnopyranose. substrate specificity single NA 5.1.3.36 Unlike EC 5.1.3.17, heparosan-N-sulfate-glucuronate 5-epimerase, it shows no activity with D-glucuronate residues in heparosan-N-sulfate. substrate specificity single NA 5.1.3.37 The enzyme epimerizes the C-5 bond in some β-D-mannuronate residues in mannuronan, converting them to α-L-guluronate residues, and thus modifying the mannuronan into alginate. substrate promiscuity single NA 5.1.99.1 NA NA multi different reactants 5.1.99.4 α-methyl-branched acyl-CoA derivatives with chain lengths of more than C10 are substrates. Also active towards some aromatic compounds (e.g. ibuprofen) and bile acid intermediates, such as trihydroxycoprostanoyl-CoA. Not active towards free acids. substrate promiscuity multi generic 5.1.99.5 The enzyme from Pseudomonas sp. (HyuE) has a preference for hydantoins with aliphatic substituents, e.g. D- and L-5-(2-methylthioethyl)hydantoin, whereas that from Arthrobacter aurescens shows highest activity with arylalkyl substituents, especially 5-benzylhydantoin, at the 5-position. substrate promiscuity and species specificity single NA 5.1.99.6 The enzyme can use either (R)-NADH-hydrate or (R)-NADPH-hydrate as a substrate. substrate promiscuity multi different reactants 5.1.99.7 The enzyme, found in gammaproteobacteria, has almost no activity with 7,8-dihydroneopterin. substrate specificity and species specificity single NA 5.1.99.8 The enzyme, which has been characterized in bacteria and plants, also has the activity of EC 4.1.2.25, dihydroneopterin aldolase. The enzyme from the bacterium Mycobacterium tuberculosis has an additional oxygenase function (EC 1.13.11.81, 7,8-dihydroneopterin oxygenase). reaction promiscuity single NA 5.2.1.2 Also acts on maleylpyruvate. substrate promiscuity multi different reactants 5.3.1.3 The enzyme catalyses the aldose-ketose isomerization of several sugars. Most enzymes also catalyse the reaction of EC 5.3.1.25, L-fucose isomerase [3]. The enzyme from the bacterium Falsibacillus pallidus also converts D-altrose to D-psicose [4]. cf. EC 5.3.1.4, L-arabinose isomerase. reaction promiscuity and species specificity multi different reactants 5.3.1.4 The enzyme can also convert D-galactose to D-tagatose with lower efficiency substrate promiscuity single NA 5.3.1.5 The enzyme catalyses the interconversion of aldose and ketose sugars with broad substrate specificity substrate promiscuity multi generic and different reactants 5.3.1.6 Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate. substrate promiscuity multi different reactants 5.3.1.7 Also acts on D-lyxose and D-rhamnose. substrate promiscuity single NA 5.3.1.8 NA NA multi generic 5.3.1.9 Also catalyses the anomerization of D-glucose 6-phosphate reaction promiscuity multi generic and different types of reactions 5.3.1.12 Also converts D-galacturonate to D-tagaturonate. substrate promiscuity multi different reactants 5.3.1.14 While the enzyme from the bacterium Escherichia coli is specific for L-rhamnose, the enzyme from the bacterium Pseudomonas stutzeri has broad substrate specificity and catalyses the interconversion of L-mannose and L-fructose, L-lyxose and L-xylulose, D-ribose and D-ribulose, and D-allose and D-psicose substrate promiscuity and species specificity single NA 5.3.1.20 Also acts on L-lyxose and L-rhamnose. substrate promiscuity single NA 5.3.1.21 An epimerization at C-20 and C-21 is probably catalysed by the same enzyme. reaction promiscuity single NA 5.3.1.25 The enzyme from Escherichia coli can also convert D-arabinose to D-ribulose. The enzyme from the thermophilic bacterium Caldicellulosiruptor saccharolyticus also converts D-altrose to D-psicose and L-galactose to L-tagatose substrate promiscuity and species specificity single NA 5.3.1.27 NA NA multi generic 5.3.1.28 NA NA multi generic 5.3.2.1 Also acts on other arylpyruvates. substrate promiscuity multi different reactants 5.3.2.8 It catalyses the interconversion of two of the tautomers of 4-oxalomesaconate, a reaction that can also occur spontaneously. tautomer promiscuity single NA 5.3.3.1 NA NA multi different reactants and different types of reactions 5.3.3.3 Also acts on 3-methyl-vinylacetyl-CoA. substrate promiscuity single NA 5.3.3.4 NA NA multi generic 5.3.3.5 NA NA multi different reactants 5.3.3.8 Also catalyses the interconversion of 3-acetylenic fatty acyl thioesters and (+)-2,3-dienoyl fatty acyl thioesters, with fatty acid chain lengths C6 to C12. substrate promiscuity multi different reactants 5.3.3.10 NA NA multi different reactants 5.3.3.12 Stereospecific for L-dopachrome. Dopachrome methyl ester is a substrate, but dopaminochrome (2,3-dihydroindole-5,6-quinone) is not substrate promiscuity and substrate specificity single NA 5.3.3.13 The enzyme from the red alga Ptilota filicina catalyses the isomerization of skip dienes (methylene-interrupted double bonds) in a broad range of fatty acids and fatty-acid analogues, such as arachidonate and γ-linolenate, to yield a conjugated triene. substrate promiscuity and species specificity single NA 5.3.3.14 While the enzyme from Escherichia coli is highly specific for the 10-carbon enoyl-ACP, the enzyme from Streptococcus pneumoniae can also use the 12-carbon enoyl-ACP as substrate in vitro but not 14- or 16-carbon enoyl-ACPs. ACP can be replaced by either CoA or N-acetylcysteamine thioesters. substrate promiscuity and species specificity single NA 5.3.3.18 The enzyme catalyses the reversible isomerization of 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA to the unusual unsaturated, oxygen-containing, seven-member heterocyclic enol ether 2-oxepin-2(3H)-ylideneacetyl-CoA, as part of an aerobic phenylacetate degradation pathway. reversibility single NA 5.3.3.19 The enzyme can interconvert the (E) isomer formed in the reaction into the (Z) isomer reaction promiscuity single NA 5.3.99.7 Highly specific. substrate specificity multi generic 5.3.99.8 This multifunctional enzyme is induced during chromoplast differentiation in plants NA multi partial 5.3.99.9 NA NA multi different reactants 5.4.1.3 The enzyme, purified from the bacterium Chloroflexus aurantiacus, acts as an intramolecular CoA transferase and does not transfer CoA to free mesaconate substrate specificity single NA 5.4.2.2 NA NA multi generic and different reactants 5.4.2.5 NA NA multi generic 5.4.2.7 Also converts 2-deoxy-α-D-ribose 1-phosphate into 2-deoxy-D-ribose 5-phosphate. substrate promiscuity multi different reactants 5.4.2.10 It can also catalyse the interconversion of α-D-glucose 1-phosphate and glucose 6-phosphate, although at a much lower rate. substrate promiscuity single NA 5.4.4.3 NA NA multi different reactants 5.4.4.5 The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyse two separate reactions. Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (cf. EC 1.13.11.60, linoleate 8R-lipoxygenase), which is subsequently isomerized to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate within the C-terminal P450 heme thiolate domain. reaction promiscuity and species specificity single NA 5.4.4.6 The bifunctional enzyme from Gaeumannomyces graminis catalyses the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate (cf. EC 1.13.11.60, linoleate 8R-lipoxygenase), which is then isomerized to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate. reaction promiscuity single NA 5.4.4.7 The enzyme from mammals accepts a range of hydroperoxy icosatetraenoates producing one or several different hydroxy epoxy icosatrienoates. The human enzyme has highest activity with (12R)-HPETE producing (5Z,8R,9E,11R,12R,14Z)-8-hydroxy-11,12-epoxyicosa-5,9,14-trienoate, followed by (12S)-HPETE producing (5Z,8Z,10R,11S,12S,14Z)-10-hydroxy-11,12-epoxyicosa-5,8,14-trienoate and (5Z,8R,9E,11S,12S,14Z)-8-hydroxy-11,12-epoxyicosa-5,9,14-trienoate. The mouse enzyme has highest activity with (8S)-HPETE, producing (5Z,8S,9S,10R,11Z,14Z)-10-hydroxy-8,9-epoxyicosa-5,11,14-trienoate. The enzymes also have the activity of EC 4.2.1.152, hydroperoxy icosatetraenoate dehydratase. reaction promiscuity, substrate promiscuity and species specificity single NA 5.4.99.3 Also converts 2-aceto-2-hydroxybutanoate to 3-hydroxy-3-methyl-2-oxopentanoate substrate promiscuity multi generic and different reactants 5.4.99.9 NA NA multi different reactants 5.4.99.11 The enzyme simultaneously produces isomaltulose (6-O-α-D-glucopyranosyl-D-fructose) and smaller amounts of trehalulose (1-O-α-D-glucopyranosyl-β-D-fructose) from sucrose. reaction promiscuity single NA 5.4.99.12 The uridylate residues at positions 38, 39 and 40 of nearly all tRNAs are isomerized to pseudouridine. TruA specifically modifies uridines at positions 38, 39, and/or 40 in the anticodon stem loop of tRNAs with highly divergent sequences and structures substrate promiscuity single NA 5.4.99.15 Not active towards maltose substrate specificity single NA 5.4.99.17 The enzyme also produces the cyclization product hopan-22-ol by addition of water (cf. EC 4.2.1.129, squalene—hopanol cyclase). Hopene and hopanol are formed at a constant ratio of 5:1. reaction promiscuity single NA 5.4.99.19 The enzyme is specific for uridine516 in 16S rRNA. In vitro, the enzyme does not modify free 16S rRNA. The preferred substrate is a 5'-terminal fragment of 16S rRNA complexed with 30S ribosomal proteins substrate specificity single NA 5.4.99.20 The enzyme modifies uridine2457 in a stem of 23S RNA in Escherichia coli. substrate specificity and species specificity single NA 5.4.99.21 The enzyme is not completely specific for uridine2604 and can, to a small extent, also react with uridine2605 substrate promiscuity single NA 5.4.99.22 Pseudouridine synthase RluB converts uridine2605 of 23S rRNA to pseudouridine. substrate specificity single NA 5.4.99.23 Pseudouridine synthase RluD converts uridines at positions 1911, 1915, and 1917 of 23S rRNA to pseudouridines. substrate specificity single NA 5.4.99.24 The enzyme converts uridines at position 955, 2504 and 2580 of 23S rRNA to pseudouridines. substrate specificity single NA 5.4.99.25 Pseudourine synthase TruB from Escherichia coli specifically modifies uridine55 synthase in tRNA molecules. The bifunctional archaeal enzyme also catalyses the pseudouridylation of uridine54. It is not known whether the enzyme from Escherichia coli can also act on position 54 in vitro, since this position is occupied in Escherichia coli tRNAs by thymine. substrate promiscuity and species specificity single NA 5.4.99.26 TruC specifically modifies uridines at positions 65 in tRNA substrate specificity single NA 5.4.99.27 Pseudouridine synthase PusS from Escherichia coli specifically acts on uridine13 in tRNA. The Pus7 protein from Saccharomyces cerevisiae is a multisite-multisubstrate pseudouridine synthase that is able to modify uridine13 in several yeast tRNAs, uridine35 in the pre-tRNATyr, uridine35 in U2 small nuclear RNA, and uridine50 in 5S rRNA. substrate promiscuity and species specificity single NA 5.4.99.28 The dual-specificity enzyme also catalyses the formation of pseudouridine746 in 23S rRNA. cf. EC 5.4.99.29 (23S rRNA pseudouridine746 synthase). substrate promiscuity single NA 5.4.99.29 RluA is the sole protein responsible for the in vivo formation of 23S RNA pseudouridine746. The dual-specificity enzyme also catalyses the formation of uridine32 in tRNA. cf. EC 5.4.99.28 (tRNA pseudouridine32 synthase). substrate promiscuity single NA 5.4.99.34 The enzyme produces germanicol, β-amyrin and lupeol in the ratio 63:33:4. reaction promiscuity single NA 5.4.99.35 The enzyme gives taraxerol, β-amyrin and lupeol in the ratio 70:17:13. reaction promiscuity single NA 5.4.99.38 The product is 97% camelliol, 2% achilleol A and 0.2% β-amyrin. reaction promiscuity single NA 5.4.99.39 Some organism possess a monofunctional β-amyrin synthase, other have a multifunctional enzyme that also catalyses the synthesis of α-amyrin (EC 5.4.99.40) or lupeol (EC 5.4.99.41). reaction promiscuity single NA 5.4.99.40 A multifunctional enzyme which produces both α- and β-amyrin (see EC 5.4.99.39, β-amyrin synthase). reaction promiscuity single NA 5.4.99.41 Also forms some β-amyrin. The recombinant enzyme from Arabidopsis thaliana [3] gives a 1:1 mixture of lupeol and lupan-3β,20-diol with small amounts of β-amyrin, germanicol, taraxasterol and ψ-taraxasterol. reaction promiscuity single NA 5.4.99.42 The enzyme specifically acts on uridine31 in tRNA. reaction promiscuity single NA 5.4.99.43 The enzyme specifically acts on uridine2819 in 21S rRNA. substrate specificity single NA 5.4.99.44 The mitochondrial enzyme Pus2p is specific for position 27 or 28 in mitochondrial tRNA. substrate specificity single NA 5.4.99.45 The enzyme from Saccharomyces cerevisiae is active only towards uridine38 and uridine39, and shows no activity with uridine40 (cf. EC 5.4.99.12, tRNA pseudouridine38-40 synthase). In vitro the enzyme from mouse is active on uridine39 and very slightly on uridine38 (human tRNALeu) substrate promiscuity and species specificity single NA 5.4.99.46 The enzyme gives traces of four other triterpenoids. reaction promiscuity single NA 5.4.99.47 The enzyme from rice (Oryza sativa) produces parkeol as a single product reaction promiscuity single NA 5.4.99.49 The enzyme from Kalanchoe daigremontiana also gives traces of other triterpenoids. reaction promiscuity and species specificity single NA 5.4.99.50 The enzyme from Kalanchoe daigremontiana also gives traces of other triterpenoids. reaction promiscuity and species specificity single NA 5.4.99.51 The enzyme from Stevia rebaudiana also gives traces of other triterpenoids. reaction promiscuity and species specificity single NA 5.4.99.52 The enzyme from Arabidopsis thaliana is multifunctional and produces about equal amounts of α- and β-seco-amyrin. See EC 5.4.99.54, β-seco-amyrin synthase. reaction promiscuity and species specificity single NA 5.4.99.54 The enzyme from Arabidopsis thaliana is multifunctional and produces about equal amounts of α- and β-seco-amyrin. See EC 5.4.99.52, α-seco-amyrin synthase. reaction promiscuity and species specificity single NA 5.4.99.55 The enzyme from tomato (Solanum lycopersicum) gives 48% δ-amyrin, 18% α-amyrin, 13% β-amyrin and traces of three or four other triterpenoid alcohols. See also EC 5.4.99.40, α-amyrin synthase and EC 5.4.99.39, β-amyrin synthase. reaction promiscuity and species specificity single NA 5.4.99.56 The product from Arabidopsis thaliana is 85% tirucalla-7,24-dien-3β-ol with trace amounts of other triterpenoids. reaction promiscuity and species specificity single NA 5.4.99.57 The enzyme from Arabidopsis thaliana also produces traces of 22 other triterpenoids. reaction promiscuity and species specificity single NA 5.4.99.62 The enzyme also catalyzes the conversion between β-allofuranose and β-allopyranose. substrate promiscuity single NA 5.5.1.1 Also acts (in the reverse reaction) on 3-methyl-cis,cis-hexadienedioate and, very slowly, on cis,trans-hexadienedioate. substrate promiscuity multi different types of reaction, partial reaction and different reactants 5.5.1.6 NA NA multi different reactants 5.5.1.7 NA NA multi different types of reaction, partial reaction and different reactants 5.5.1.8 The enzyme from Salvia officinalis (sage) can also use (3R)-linalyl diphosphate or more slowly neryl diphosphate in vitro. The reaction proceeds via isomeration of geranyl diphosphate to (3R)-linalyl diphosphate. substrate promiscuity and species specificity single NA 5.5.1.9 Opens the cyclopropane ring of a number of related 4α-methyl-9β-19-cyclosterols, but not those with a 4β-methyl group, with formation of an 8(9) double bond. substrate promiscuity and substrate specificity single NA 5.5.1.11 The product of cyclisomerization of dichloro-cis,cis-muconate spontaneously eliminates chloride to produce cis-4-carboxymethylene-3-chlorobut-2-en-4-olide. Also acts, in the reverse direction, on cis,cis-muconate and its monochloro-derivatives, but with lower affinity. substrate promiscuity multi different types of reactions and partial reaction 5.5.1.12 In some plants, such as Salvia miltiorrhiza, this enzyme is monofunctional. In other plants this activity is often a part of a bifunctional enzyme. reaction promiscuity and species specificity single NA 5.5.1.13 Part of a bifunctional enzyme involved in the biosynthesis of kaurene reaction promiscuity single NA 5.5.1.18 NA NA multi partial reaction and different reactants 5.5.1.19 NA NA multi partial reaction and different reactants 5.5.1.20 The bifunctional enzyme catalyses the oxidation of prosolanapyrone II and the subsequent Diels Alder cycloisomerization of the product prosolanapyrone III to (-)-solanapyrone A (cf. EC 1.1.3.42, prosolanapyrone II oxidase). reaction promiscuity single NA 5.5.1.22 The enzyme from Tanacetum vulgare (tansey) can also use (3S)-linalyl diphosphate or more slowly neryl diphosphate in vitro. substrate promiscuity single NA 5.5.1.24 The enzyme has been described from plants and cyanobacteria. It has similar activity with all four listed benzoquinol substrates. substrate promiscuity and species specificity multi different reactants 5.5.1.27 The enzyme, characterized from the bacterium Agrobacterium fabrum strain C58, is involved in degradation of D-galacturonate and D-glucuronate. Activity with D-galactaro-1,4-lactone is 4-fold higher than with D-glucaro-1,4-lactone. substrate promiscuity multi different reactants