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EC Number	Recommended Name	Application	Commentary
1.3.3.4	protoporphyrinogen oxidase	more	light intensity-dependent degradation of reduced and oxidized porphyrins prevents severe photodynamic leaf damage, moreover, under high-light conditions, elevated contents of reduced and total low-molecular-weight antioxidants, which contribute to the protection against photosensitizing porphyrins
1.3.3.4	protoporphyrinogen oxidase	more	metabolic homeostasis by antifouling herbicide Irgarol 1051, which includes cnidarian PPO, decreases in ferrochelatase and increases in PPO and heme oxygenase suggest adverse impacts on porphyrin synthesis, damage to porphyrins, and increased porphyrin degradation
1.3.3.4	protoporphyrinogen oxidase	more	no consistent beneficial effects on sugarcane from applications of different PPOase inhibitor herbicides, herbicide treatments result in plant injury
1.3.3.4	protoporphyrinogen oxidase	more	no consistent effects from herbicide treatments on disease parameters
1.3.3.4	protoporphyrinogen oxidase	more	PPO and FeC are each encoded by a single gene in the green alga, multiplicity of genes for PPO and FeC in higher plants could be related to differential expression in differently developing tissues rather than to targeting of different gene products to different organelles
1.3.3.4	protoporphyrinogen oxidase	more	presence of the plastidal transit sequence neither excludes the intrinsic ability of subcellular translocation of Protox nor changes herbicide resistance in TTS lines
1.3.3.4	protoporphyrinogen oxidase	more	transgenic rice lines are resistant to the herbicides carfentrazone-ethyl and oxyfluorfen
1.3.3.5	bilirubin oxidase	more	redox potential of the T1 site of BOD is > 650 mV vs. NHE, redox potential of the T2 site is near 390 mV vs. NHE
1.3.3.5	bilirubin oxidase	more	redox potential of the T1 site of BOD is close to 670 mV vs. NHE, redox potential of the T2 site is near 390 mV vs. NHE
1.3.3.5	bilirubin oxidase	more	BODs have a high efficiency of decolorizing compounds such as Trypan blue and Remazol brilliant blue R under mild pH conditions
1.3.3.5	bilirubin oxidase	more	the purified bilirubin oxidase in Myrothecium verrucaria strain has potential application in dye effluent decolorization. Extracellular bilirubin oxidase decolorizes indigo carmine, biosorption and biodegradation of the dye is achieved with more than 98% decolorization efficiency after 7 days at 26°C. Additionally, the crude bilirubin oxidase can efficiently decolorize indigo carmine at 30°C to 50°C and pH 5.5-9.5 with dye concentrations of 50-200 mg/ml
1.3.3.5	bilirubin oxidase	more	usage of the enzyme for a bilirubin oxidase-based air breathing cathode, evaluation by constant monitoring over 45 days, analysis of effect of electrolyte composition on the cathode oxygen reduction reaction output, and of deactivation of the electrocatalytic activity of the enzyme in phosphate buffer saline solution and in activated sludge. BOx electrochemical response as a function of presence of pollutants, solids and bacteria, overview
1.3.3.5	bilirubin oxidase	more	the enzyme is used to decolorize recalcitrant dyes
1.3.3.6	acyl-CoA oxidase	more	ACOX1 alternative splicing isoforms play a key conserved role in the vertebrate fatty acid metabolism, tissue-specific modulation of ACOX1 activity by exchanging exon 3 duplicated isoforms containing amino acid sequences that are potentially implicated in fatty acyl chain specificity
1.3.3.6	acyl-CoA oxidase	more	inability of ACX1, ACX3, and ACX4 to fully compensate for one another in indole-3-butyric acid-mediated root elongation inhibition and ability of ACX2 and ACX5 to contribute to indole-3-butyric acid response suggests that indole-3-butyric acid-response defects in acx mutants may reflect indirect blocks in peroxisomal metabolism and indole-3-butyric acid beta-oxidation, rather than direct enzymatic activity of ACX isozymes on indole-3-butyric acid-CoA
1.3.3.6	acyl-CoA oxidase	more	isomerase activity of rat peroxisomal acyl-CoA oxidase I, is probably due to a spontaneous process driven by thermodynamic equilibrium with formation of a conjugated structure after deprotonation of substrate alpha-proton
1.3.3.6	acyl-CoA oxidase	more	nervonic acid is discharged from the spore into the external medium during firing along with the catalase and ACOX enzymes
1.3.3.6	acyl-CoA oxidase	more	novel Pex5pM is functional and a seven amino acids-insertion, which is present in the L isoform but absent in the M isoform, plays some role in the process of maturation of Aox
1.3.3.6	acyl-CoA oxidase	more	solvent-accessible acyl binding pocket is not required for oxygen reactivity, the oligomeric state plays a role in substrate pocket architecture but is not linked to oxygen reactivity
1.3.3.6	acyl-CoA oxidase	more	three distinct ACX genes, ACX1 is upregulated by wounding, both locally and systemically, ACX1 may play a role in the synthesis of jasmonic acid in response to wounding
1.3.3.6	acyl-CoA oxidase	more	three distinct ACX genes, expression of ACX2 remains unchanged by wounding, ACX2 may be involved in providing germinating seeds with sugar and energy
1.3.3.6	acyl-CoA oxidase	more	three distinct ACX genes, expression of ACX3 remains unchanged by wounding
1.3.5.2	dihydroorotate dehydrogenase (quinone)	more	kinetic isotope effects on flavin reduction in anaerobic stopped-flow experiments, are about 3fold for DHO labeled at the 5-position, about 4fold for DHO labeled at the 6-position, and about 6-7fold for DHO labeled at both the 5- and 6-positions, at a pH value above the pKa controlling reduction, no isotope effect was observed for DHO deuterated at the 5-position, which is consistent with a stepwise reaction, above the kinetic pKa, the deprotonation of C5 is fast enough that it does not contribute to the observed rate constant and, therefore, is not isotopically sensitive
1.3.5.2	dihydroorotate dehydrogenase (quinone)	more	kinetic isotope effects on flavin reduction in anaerobic stopped-flow experiments, pKa near 9.4 controlling reduction, similar to that previously reported for the Escherichia coli enzyme
1.3.5.2	dihydroorotate dehydrogenase (quinone)	more	three types of hydrogen bonding pathways, hydrogen bonding of the active base serine to a water molecule, which is hydrogen bonded to the substrate carboxylate group or a threonine residue, the threonine residue is positioned to enable proton transfer to another water molecule leading to the bulk solvent
1.3.7.3	phycoerythrobilin:ferredoxin oxidoreductase	more	metabolic engineering of bacteria for the production of various bilins for assembly into phytochromes will facilitate the molecular analysis of photoreceptors
1.3.7.5	phycocyanobilin:ferredoxin oxidoreductase	more	co-expression of heme oxygenase in a single operon in conjunction with apophytochrome, is a system to produce phytochromes with various chromophores in Escherichia coli, metabolic engineering of bacteria for the production of various bilins for assembly into phytochromes will facilitate the molecular analysis of photoreceptors
1.3.7.5	phycocyanobilin:ferredoxin oxidoreductase	more	conserved histidine and aspartate residues essential for the catalytic activity of the enzyme, direct role of the His85-Asp102 pair in exovinyl reduction of biliverdin IXa
1.3.7.5	phycocyanobilin:ferredoxin oxidoreductase	more	phycocyanobilin-CpcB(C155I) and phycocyanobilin-PecB(C155I) are also biosynthesized heterologously in vivo, when cpeS is introduced into Escherichia coli with cpcB(C155I) or pecB(C155I), respectively, together with genes ho1 and pcyA
1.3.8.1	short-chain acyl-CoA dehydrogenase	more	common variant SCAD enzymes and their potential contribution to clinical disease in humans
1.3.8.1	short-chain acyl-CoA dehydrogenase	more	development of a novel surface plasmon resonance assay to measure substrate binding
1.3.8.1	short-chain acyl-CoA dehydrogenase	more	overall high degree of thermodynamic modulation of wild-type SCAD, substrate binding appears to make a larger contribution than does product to thermodynamic modulation, substrate redox activation leading to a large enzyme midpoint potential shift
1.3.8.1	short-chain acyl-CoA dehydrogenase	more	type I strain has the same clustered genes with the same arrangement as type II strain, deduced amino acid sequences of these enzymes do not greatly differ between the two strains, and even between Butyrivibrio fibrisolvens and clostridia. Amino acid identity appears to be higher within the same type than between types I and II, clustered genes are cotranscribed, and constitutively transcribed without being affected significantly by culture conditions
1.3.8.7	medium-chain acyl-CoA dehydrogenase	more	acyl-CoA dehydrogenase LipB is involved in the introduction of the unusual Dcis3 double bond into the acyl residue of friulimicin
1.3.8.7	medium-chain acyl-CoA dehydrogenase	more	AFT10-1, which encodes an acyl-CoA dehydrogenase, is involved in the formation of the 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid moiety of the host-specific AF-toxin molecule
1.3.8.7	medium-chain acyl-CoA dehydrogenase	more	development of fluorogenic and fluoromorphic probes for the enzyme as indicators for selective and sensetive detection of MCAD activity in tissue homogenates
1.3.8.7	medium-chain acyl-CoA dehydrogenase	more	highly homologous to human very-long-chain acyl-CoA dehydrogenase
1.3.8.8	long-chain acyl-CoA dehydrogenase	more	CTE-II expression is induced during embryogenesis in association with neuronal differentiation, and persists after terminal differentiation in neurons at postnatal stages, resulting in constitutive high expression in the adult brain in a neuron-specific manner
1.3.98.1	dihydroorotate dehydrogenase (fumarate)	more	an ancient common ancestor of Euglenozoa had a mitochondrial DHOD whose descendant exists in Euglena gracilis
1.3.98.1	dihydroorotate dehydrogenase (fumarate)	more	Bodo saliens has an ACT/DHOD gene fusion encoding aspartate carbamoyltransferase, the second enzyme of the de novo pyrimidine pathway, and DHOD
1.3.98.1	dihydroorotate dehydrogenase (fumarate)	more	significant heterogeneity in the catalytic behaviors of individual dimer molecules, very similar reaction rates in both the reductive and oxidative half-reactions for different DHODA dimers, single-molecule data provide strong evidence for half-sites reactivity, in which only one subunit reacts at a time
1.3.98.1	dihydroorotate dehydrogenase (fumarate)	more	species-specific preferential inhibitor binding, different binding mode for the same inhibitor in the two catalytically identical enzymes human DHODH and Plasmodium DHODH
1.3.98.1	dihydroorotate dehydrogenase (fumarate)	more	the cytosolic DHOD gene acquired may have contributed to adaptation to anaerobiosis in the kinetoplastid lineage and further contributes to the subsequent establishment of parasitism in a trypanosomatid ancestor
1.3.98.1	dihydroorotate dehydrogenase (fumarate)	more	the gene LMjF16.0530 possesses a dihydroorotate oxidase activity using fumarate as oxidizing agent
1.3.99.4	3-oxosteroid 1-dehydrogenase	more	ksdD-1 and ksdD-2 display respectively high (78%) and low (33%) amino acid sequence identity with the putative ksdD gene of Mycobacterium tuberculosis
1.3.99.4	3-oxosteroid 1-dehydrogenase	more	the two putative Mycobacterium tuberculosis KsdDs, MT3641 and MT0809, complement the Mycobacterium smegmatis deltaksdD-1 deltaksdD-2 double mutant
1.3.99.4	3-oxosteroid 1-dehydrogenase	more	3-oxosteroid DELAT1-dehydrogenases are of particular interest for the etiology of some infectious diseases, for the production of starting materials for the pharmaceutical industry, and for environmental bioremediation applications
1.3.99.17	quinoline 2-oxidoreductase	more	the gene cluster involved in quinoline degradation is transcribed from the quinoline-dependent promoters PoxoO, Porf3, PqorM, and PoxoR in the presence of oxoS. The oxoS gene coding for a quinoline-responsive transcriptional activator of the XylS family is expressed independently of quinoline
1.3.99.23	all-trans-retinol 13,14-reductase	more	conserved function but altered specificity of RetSat in vertebrates
1.4.1.1	alanine dehydrogenase	more	alanine dehydrogenase activity is necessary for an adequate cellular response to nitrogen starvation, is required for efficient degradation of phycobilisomes only during nitrogen starvation
1.4.1.2	glutamate dehydrogenase	more	GDH gene expression and translation are apparently subject to complex regulation
1.4.1.2	glutamate dehydrogenase	more	glutamine synthetase-GOGAT pathway and GDH play distinct roles in the source-sink nitrogen cycle of tobacco leaves, regardless of leaf age, [15N]ammonium does not depend on GDH
1.4.1.2	glutamate dehydrogenase	more	high sequence similarity to GDH genes from the Bacteroides, GDH is an anabolic enzyme catalysing the assimilation of ammonia by Entodinium caudatum in the rumen, the gene is probably acquired by lateral gene transfer from a ruminal bacterium
1.4.1.2	glutamate dehydrogenase	more	induction of GDH1 and GDH2 transcripts along the root do not coincide with that of NADH-GOGAT expression
1.4.1.2	glutamate dehydrogenase	more	large modulation of GDH beta-subunit titre does not affect plant viability under ideal growing conditions, GDH gene expression and translation are apparently subject to complex regulation
1.4.1.2	glutamate dehydrogenase	more	possible role of enzyme under Hg-stress
1.4.1.2	glutamate dehydrogenase	more	Q144R can be used as a template gene to modify the substrate specificity of Bacillus subtilis GluDH for industrial use
1.4.1.2	glutamate dehydrogenase	more	reactivation of D165N is a consequence of the catalytic chemistry of the enzymes active site
1.4.1.2	glutamate dehydrogenase	more	shift in GDH cellular compartmentation is important during leaf nitrogen remobilization
1.4.1.2	glutamate dehydrogenase	more	subunit rearrangement, i.e., a change in the quaternary structure of the hexameric recombinant GDH, is essential for activation of the enzyme
1.4.1.3	glutamate dehydrogenase [NAD(P)+]	more	C323 plays an important role in catalysis by human GDH isozymes
1.4.1.4	glutamate dehydrogenase (NADP+)	more	in order for the wild-type nitrogen assimilation control protein to exert strong repression of gdhA, it must form a tetramer that bridges the two sites at gdhA, similar to other DNA looping models, the negative control mutants of nitrogen assimilation control protein fail to tetramerize and cannot form this loop, thus fail to exert the strong repression at gdhA
1.4.1.4	glutamate dehydrogenase (NADP+)	more	lack of a structure called antenna, NAD(P)-binding motif GAGNVA, and a second putative coenzyme-binding motif GVLTGKG together with the four residues Lys, Ser, Arg and Thr involved in the binding of the reduced form of NADP, key role of GDH4 in ammonium assimilation
1.4.1.4	glutamate dehydrogenase (NADP+)	more	minor role in ammonium assimilation in ectomycorrhizal fungi
1.4.1.4	glutamate dehydrogenase (NADP+)	more	minor role in ammonium assimilation in ectomycorrhizal fungi, NADPH-GDH activity detected in ectomycorrhizas formed with Pseudotsuga menziesii
1.4.1.14	glutamate synthase (NADH)	more	possible relationship between NADH-GOGAT, IDH and GDH, IDH is a good candidate to generate the 2-oxoglutarate required for NH4+-induced NADH-GOGAT activity in rice roots, GDH shows no significant differences in its localization between the conditions with or without NH4+ application
1.4.1.21	aspartate dehydrogenase	more	first report of an archaeal L-aspartate dehydrogenase, within the archaeal domain, homologues in many methanogenic species, but not in Thermococcales or Sulfolobales species
1.4.3.2	L-amino-acid oxidase	more	a helical domain is exclusively responsible for the unusual dimerisation mode of the enzyme and is not found in other members of the family so far. Most groups present at the active site are involved in substrate recognition, binding and fixation, i.e. they direct the trajectory of the interacting orbitals. In this mode of catalysis orbital steering/interactions are the predominant factors for the chemical step(s). A mirrorsymmetrical relationship between the two substrate-binding sites of D and L-amino acid oxidases is observed which facilitates enantiomeric selectivity while preserving a common arrangement of the residues in the active site
1.4.3.2	L-amino-acid oxidase	more	expressed LAAO exhibits the same electrophoretic mobility as native LAAO and exhibits approximately the same extent of glycosylation as authentic LAAO from snake venom. Catalytic properties and substrate specificity of recombinant LAAO are similar to those of native enzyme
1.4.3.2	L-amino-acid oxidase	more	LAAO causes cell death by induction of apoptosis in yeast. Lower concentrations of hydrogen peroxide accompanied by leucine deficiency may have a role in enhancing cell death in leucine auxotrophic yeast strain. LAAO interacts with the cell surface of yeast. Depletion of leucine from the medium by LAAO and the interaction of LAAO with yeast cells are shown to be the major factors responsible for cell demise in the presence of catalase
1.4.3.2	L-amino-acid oxidase	more	LAAO contributes to competitive edge of Streptococcus oligofermentans over Streptococcus mutans in mixed-species biofilm with peptone
1.4.3.2	L-amino-acid oxidase	more	LAAO dose-dependently induces aggregation of washed human platelets. It induces tyrosine phosphorylation of a number of platelet proteins including Src kinase, spleen tyrosine kinase, and phospholipase C gamma2. Both H2O2 production and binding to platelet membrane proteins may be involved in its action. The enzyme binds to the platelet membrane to enhance the sensitivity of platelets to H2O2. At the same time, H2O2 released by the enzyme activates platelets by an unknown mechanism
1.4.3.2	L-amino-acid oxidase	more	LAO is a macromolecule with antimicrobial activity, shows broad substrate specificity
1.4.3.2	L-amino-acid oxidase	more	LAO is a potential candidate for a mechanism that catalyses nitrogen mineralization from amino acids at the ecosystem level
1.4.3.2	L-amino-acid oxidase	more	LAO is involved in the innate immunity of fish skin. Shows potent antibacterial activity against fish pathogens, specifically Gram-negative bacteria such as Aeromonas hydrophila, Aeromonas salmonicida and Photobacterium damselae ssp. piscicida
1.4.3.2	L-amino-acid oxidase	more	potent and effective activity of SSAP against waterborne virulent pathogens. Shows antibacterial activity, acts selectively on Gram-negative bacteria. SSAP inhibits potently the growth of Aeromonas salmonicida, Photobacterium damselae subsp. piscicida and Vibrio parahaemolyticus with a minimum inhibitory concentration of 0.078, 0.16 and 0.63 microg/mL, respectively. Bacteria binding activity may be involved in the bacterial cell selectivity of SSAP. Treatments with SSAP induce cell surface damage to Aeromonas salmonicida, remarkable elongation of Photobacterium damselae subsp. piscicida bodies and pores into Vibrio parahaemolyticus cells
1.4.3.2	L-amino-acid oxidase	more	SSAP is predominantly synthesized in skin and gill and probably functions as an antibacterial LAO in both tissues. It shows antibacterial activity against Photobacterium damselae subsp. piscicida
1.4.3.2	L-amino-acid oxidase	more	the enzyme has antibacterial activity inhibiting the growth of Gram-positive (Bacillus subtilis) and Gram-negative (Escherichia coli) bacteria. LAAO dose-dependently inhibits ADP- or collagen-induced platelet aggregation with IC50 of 0.094 micromol and 0.036 micromol, respectively
1.4.3.16	L-aspartate oxidase	more	is essential for plant growth and development
1.4.4.2	glycine dehydrogenase (aminomethyl-transferring)	more	GDC is dispensable for cyanobacterial metabolism
1.4.4.2	glycine dehydrogenase (aminomethyl-transferring)	more	GDC is not necessary for cell viability under standard conditions. GDC is dispensable for Synechocystis
1.5.1.18	ephedrine 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
1.5.1.34	6,7-dihydropteridine reductase	more	the purified recombinant enzyme from Escherichia coli is used for 5,6,7,8-tetrahydropteridine (BH4) regeneration to alleviate 7,8-dihydropteridine (BH2) inhibition of L-tyrosine hydroxylation by crude tyrosine hydroxylase (SrTH) from Streptosporangium roseum DSM 43021 as part of a combined whole-cell catalyst, and a series of tyrosine hydroxylase/sepiapterin reductase (TH/SPR) synthesis systems, overview
1.6.2.4	NADPH-hemoprotein reductase	more	the CPR activity in different recombinant enzyme preparations is crucial for in vitro CYP3A5-mediated clearance of midazolam. The level of CPR affects both the affinity/binding of midazolam to the CYP enzyme and the velocity of the metabolic reaction
1.6.3.1	NAD(P)H oxidase (H2O2-forming)	more	NADPH oxidase but not myeloperoxidase is required for host defense in lymphopenic mice. Lymphocytes and NADPH oxidase may compensate for each other's deficiency in providing resistance to spontaneous bacterial infections
1.6.5.2	NAD(P)H dehydrogenase (quinone)	more	ERbeta and hPMC2 are required for trans-hydroxytamoxifen-dependent recruitment of coactivators such as PARP-1 to the electrophile response element of NQO1 resulting in the induction of the antioxidative enzyme and subsequent protection against oxidative DNA damage
1.6.5.2	NAD(P)H dehydrogenase (quinone)	more	oxidative stress-type cytotoxicity of chromate in FLK cells may be partly attributed to its reduction by NQO1, but not by glutathione reductase
1.6.5.2	NAD(P)H dehydrogenase (quinone)	more	PIFI is a novel component essential for NDH-mediated nonphotochemical reduction of the plastoquinone pool in chlororespiratory electron transport
1.6.5.2	NAD(P)H dehydrogenase (quinone)	more	WrbA bridges flavodoxins and oxidoreductases. WrbA shows a close relationship to mammalian Nqo1
1.7.1.6	azobenzene reductase	more	health protection, the activity of the pure oxidoreductase YhdA can be used for efficient bioremediation of Cr(VI), it counteracts the cytotoxic and genotoxic effects of oxygen radicals induced by intracellular factors and those generated during reduction of hexavalent chromium. Oxidoreductases that possess the ability to reduce Cr(VI) to Cr(III), avoiding the intermediates Cr(V) and Cr(IV), are of significant biotechnological value
1.7.1.17	FMN-dependent NADH-azoreductase	more	the enzyme can be applied for textile wastewater treatment
1.7.2.8	hydrazine dehydrogenase	more	anaerobic ammonium oxidation is a very good alternative for treatment of high strength nitrogenous waste streams. The introduction of anaerobic ammonium oxidation to N-removal would lead to a 90% reduction in operational costs. Anammox would replace the conventional denitrification step and would also save half of the nitrification aeration costs
1.7.2.8	hydrazine dehydrogenase	more	the application of anammox to nitrogen removal would lead to a reduction of operational costs of up to 90%. The process targets wastewaters that contain much ammonium and little organic material, such as sludge digestor effluents. Anammox would replace the conventional denitrification step completely and would also save half of the nitrification aeration costs
1.8.1.4	dihydrolipoyl dehydrogenase	more	a mutation in LPD leads to a pyruvate dehydrogenase complex that is less sensitive to inhibition by NADH, allowing the enzyme to function in an anaerobic culture, which changes the fermentation profile of the mutant. Presence and functional activity of such an NADH-insensitive pyruvate dehydrogenase may have significant unexplored physiological and biotechnological applications
1.8.1.4	dihydrolipoyl dehydrogenase	more	high stability of rBfmBC may make it useful for practical use
1.8.1.4	dihydrolipoyl dehydrogenase	more	metabolic context(s) of DLDHs remains an open question
1.8.1.4	dihydrolipoyl dehydrogenase	more	the lipoyl protein domain (but not lipoic acid alone) plays a regulatory role in the enzymatic characteristics of pneumococcal DLDH
1.8.1.12	trypanothione-disulfide reductase	more	modeled structure of trypanothione reductase shows different active site from glutathione reductase, a specific inhibitor against trypanothione reductase can be designed without interfering with host glutathione reductase activity
1.8.2.1	sulfite dehydrogenase (cytochrome)	more	N-terminal amino acid sequence of the mature SorA from Cupriavidus necator H16 is currently unique
1.8.2.1	sulfite dehydrogenase (cytochrome)	more	the N-terminal amino acid sequence of the mature SorA from Delftia acidovorans SPH-1 is found in about 500 proteins

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