enzyme_display_name: cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose)

organism: Dianthus caryophyllus

assay_conditions_summary: pH 6; 303.15 K; buffer 0.1 M citrate

column_label: Results prose page 3380, recombinant Dc AA5GT clause of the kinetic parameter sentence: 'kcat for Cy3G = 0.07 s^-1' and 'Km for Cy3G = 6.5 uM'; Results prose page 3381, recombinant Dc AA5GT sentence: '5-O-glucosyltransferase activity for Cy3G (kcat/Km = 1.0 x 10^4)', in the s^-1 M^-1 unit the article states for kcat/Km on page 3380.

normalized_value_unit_evidence: kcat: printed value 0.07 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.07 s^(-1). Km: printed value 6.5 uM; 6.5 / 1000 = 0.0065 mM. kcat/Km: printed value 1.0 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 10000 / 1000 = 10.0 s^-1 mM^-1; the export carries no kcat_over_km field for this row, so the printed value is recorded as evidence only and no ratio is written.

raw_value_unit_evidence: Results prose, page 3380, recombinant Dc AA5GT clause: kcat for Cy3G = 0.07 s^-1; Km for Cy3G = 6.5 uM. Results prose, page 3381, recombinant Dc AA5GT sentence: printed kcat/Km for Cy3G = 1.0 x 10^4 s^-1 M^-1.

row_label: page-3380 kinetic parameter sentence, recombinant Dc AA5GT clause, Cy3G acceptor values; page-3381 recombinant Dc AA5GT efficiency sentence, Cy3G value

table_label: Results prose, pages 3380 and 3381, section 'Kinetic Properties and Substrate Preferences of Acceptor and Donor Molecules of Dc AA5GT and Dg AA7GT' (The Plant Cell 2010, 22:3374-3389); the article has no kinetic table, the sentences cite the online-only Supplemental Table 3


enzyme_display_name: beta-lactamase

organism: Citrobacter diversus

substrate_name: Cephalothin

verification_status: verified

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: as published (see paper)

km_unit: mM

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

column_label: Table 4 (Substrate profile of C. diversus beta-lactamases), 'Form II' group, substrate row 'Cephalothin'; column 'Km (uM)' = 41 +/- 2; column 'kcat (s-1)' = 55 +/- 6; column 'kcat/Km (M-1 s-1)' = (1.30 +/- 0.20) x 10^6.

normalized_value_unit_evidence: Km: printed Table 4 cell 41 +/- 2 uM; 41 / 1000 = 0.041 mM; the exported value is 0.041 mM. kcat: printed Table 4 cell 55 +/- 6 s^-1; the cell is already in s^-1, so no unit conversion applies here; the exported value is 55 s^(-1). kcat/Km: printed Table 4 cell (1.30 +/- 0.20) x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1300000 / 1000 = 1300 s^-1 mM^-1; the catalog identity keeps no catalytic-efficiency value, so this printed cell is carried here as typed provenance only.

raw_value_unit_evidence: Table 4, 'Form II' group, substrate row 'Cephalothin': Km = 41 +/- 2 uM; kcat = 55 +/- 6 s^-1; printed kcat/Km = (1.30 +/- 0.20) x 10^6 M^-1 s^-1.

table_label: Table 4: Substrate profile of C. diversus beta-lactamases (Biochemical Journal 1988, 254:885-890)

enzyme: beta-lactamase

substrate: Cephalothin

status: verified


substrate_name: Cephalosporin C

column_label: Table 4 (Substrate profile of C. diversus beta-lactamases), 'Form II' group, substrate row 'Cephalosporin C'; column 'Km (uM)' = 123 +/- 13; column 'kcat (s-1)' = 23 +/- 9; column 'kcat/Km (M-1 s-1)' = (0.19 +/- 0.09) x 10^6.

normalized_value_unit_evidence: Km: printed Table 4 cell 123 +/- 13 uM; 123 / 1000 = 0.123 mM; the exported value is 0.123 mM. kcat: printed Table 4 cell 23 +/- 9 s^-1; the cell is already in s^-1, so no unit conversion applies here; the exported value is 23 s^(-1). kcat/Km: printed Table 4 cell (0.19 +/- 0.09) x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 190000 / 1000 = 190 s^-1 mM^-1; the catalog identity keeps no catalytic-efficiency value, so this printed cell is carried here as typed provenance only.

raw_value_unit_evidence: Table 4, 'Form II' group, substrate row 'Cephalosporin C': Km = 123 +/- 13 uM; kcat = 23 +/- 9 s^-1; printed kcat/Km = (0.19 +/- 0.09) x 10^6 M^-1 s^-1.

substrate: Cephalosporin C


enzyme_display_name: aldehyde dehydrogenase (NAD(+))

organism: Homo sapiens

substrate_name: acetaldehyde

verification_status: unverified

smiles: CC=O

enzyme: aldehyde dehydrogenase (NAD(+))

substrate: acetaldehyde

status: unverified


substrate_name: propanal

smiles: CCC=O

substrate: propanal


substrate_name: pentanal

smiles: CCCCC=O

substrate: pentanal


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: heptanal

smiles: CCCCCCC=O

substrate: heptanal


substrate_name: decanal

smiles: CCCCCCCCCC=O

substrate: decanal


substrate_name: o-nitro-

substrate: o-nitro-


substrate_name: p-nitro-

substrate: p-nitro-


substrate_name: p-methyl-

substrate: p-methyl-


substrate_name: m-methyl-

substrate: m-methyl-


substrate_name: p-(dimethylamino)-

substrate: p-(dimethylamino)-


substrate_name: m-methoxy-

substrate: m-methoxy-


substrate_name: o-methoxy-

substrate: o-methoxy-


substrate_name: o-methyl-

substrate: o-methyl-


substrate_name: o-hydroxy-

substrate: o-hydroxy-


enzyme_display_name: L-iditol 2-dehydrogenase

organism: Ovis aries

substrate_name: (meso)-erythritol

enzyme: L-iditol 2-dehydrogenase

substrate: (meso)-erythritol


substrate_name: (meso)-ribitol

substrate: (meso)-ribitol


substrate_name: (meso)-xylitol

substrate: (meso)-xylitol


substrate_name: D-glucitol (sorbitol)

substrate: D-glucitol (sorbitol)


substrate_name: D-glycero-D-manno-heptitol (volemitol)

substrate: D-glycero-D-manno-heptitol (volemitol)


substrate_name: 1,2,3-hexanetriol (mixture of D-, L- and meso forms)

smiles: CCCC(C(CO)O)O


enzyme_display_name: ferredoxin--nitrite reductase

organism: Nicotiana tabacum

substrate_name: nitrite

source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

enzyme: ferredoxin--nitrite reductase

substrate: nitrite

source: skid


sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.


organism: Oryza sativa

substrate_name: methyl viologen

source_db: brenda

kcat_display: Not reported

source_license: CC BY 4.0

substrate: methyl viologen

source: brenda


enzyme_display_name: nitroalkane oxidase

organism: Streptomyces ansochromogenes

source_license: CC BY 4.0; CC BY-NC-ND 4.0

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.

proof_lines:
pH 8.0, 28°C
Raw SKiD Env: Temp=28°C, pH=8

source_databases_merged: brenda skid

enzyme: nitroalkane oxidase


enzyme_display_name: ferredoxin--nitrate reductase

organism: Haloferax mediterranei

enzyme: ferredoxin--nitrate reductase


organism: Pyropia yezoensis


enzyme_display_name: hydroxylamine reductase

organism: Pseudomonas aeruginosa

enzyme: hydroxylamine reductase


enzyme_display_name: trypanothione-disulfide reductase

organism: Leishmania donovani

substrate_name: trypanothione disulfide

assay_conditions_summary: cofactor NADPH

enzyme: trypanothione-disulfide reductase

substrate: trypanothione disulfide


organism: Rhodobacter capsulatus

substrate_name: methyl viologen (at pH 9.3 and 40 degrees Celsius)

source_db: uniprot

sequence_variant_note: Source notes indicate a mutant or variant enzyme, but no machine-applicable substitution signature was available.

source: uniprot


organism: Trypanosoma brucei


organism: Euglena gracilis


organism: Trypanosoma congolense


substrate_name: trypanothione

sequence_source: Trusted canonical UniProt P13110 sequence evidence, reusable per the supplied identity-reuse summary.

data_origin: experimental

substrate: trypanothione


enzyme_display_name: CoA-disulfide reductase

organism: Pyrococcus horikoshii

substrate_name: H+; NADH; CoA-disulfide

source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org)

sequence_source: UniProtKB:O58308 direct accession lookup

enzyme: CoA-disulfide reductase

substrate: H+; NADH; CoA-disulfide


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: NADPH

substrate: NADPH


organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)


enzyme_display_name: glutathione amide reductase

organism: Marichromatium gracile

substrate_name: glutathione amide disulfide (GASSAG) for the reverse reaction (in the presence of 100 uM NADH)

enzyme: glutathione amide reductase


verification_status: corrected

km_display: Not reported

sequence_source: UniProtKB/Swiss-Prot O58308; PubMed 15720393 identity/function anchor

assay_conditions_summary: 348.15 K; cofactor NADPH

status: corrected


assay_conditions_summary: pH 7.1; 298.15 K; cofactor NADPH


enzyme_display_name: NAD(P)H sulfur oxidoreductase (CoA-dependent)


organism: Rhodococcus erythropolis

smiles: C(CC(=O)[O-])CSSCCCC(=O)[O-]

assay_conditions_summary: pH 8; 310.15 K; cofactor NADH


organism: Xanthobacter autotrophicus

source_db: oed

smiles: CC(=O)CSCCS(=O)(=O)O

mutation_type: substitution

source: oed


organism: Xanthobacter sp.

substrate_name: acetoacetate

substrate: acetoacetate


enzyme_display_name: glutathione-disulfide reductase

organism: Caenorhabditis elegans

substrate_name: glutathione disulfide (at 25 degrees Celsius)

enzyme: glutathione-disulfide reductase


organism: Acidithiobacillus ferrooxidans

substrate_name: GSSG

substrate: GSSG


organism: Enterococcus faecalis

substrate_name: H+; NADPH; Glutathione disulfide

substrate: H+; NADPH; Glutathione disulfide


organism: Escherichia coli

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH


enzyme_display_name: cystine reductase

organism: Homo sapiens

substrate_name: L-cystine

enzyme: cystine reductase

substrate: L-cystine


substrate_name: NADP+

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADP+

substrate: NADP+


organism: Haemonchus contortus

substrate_name: glutathione disulfide

assay_conditions_summary: pH 7.8; 310.15 K; cofactor FAD

substrate: glutathione disulfide


substrate_name: reduced glutathione

substrate: reduced glutathione


assay_conditions_summary: pH 7.8; 310.15 K; cofactor NADPH


organism: Mus musculus

substrate_name: Oxidized glutathione

substrate: Oxidized glutathione


organism: Escherichia coli (strain K12)


organism: Euglena gracilis


substrate_name: NADPH; Glutathione disulfide; H+

substrate: NADPH; Glutathione disulfide; H+


organism: Oryza sativa


organism: Phycomyces blakesleeanus


organism: Neospora caninum

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH


organism: Trypanosoma congolense


enzyme_display_name: protein-disulfide reductase

organism: Methanosarcina acetivorans

substrate_name: coenzyme M

assay_conditions_summary: pH 6.8; 323.15 K; cofactor CoA

enzyme: protein-disulfide reductase

substrate: coenzyme M


enzyme_display_name: thioredoxin-disulfide reductase (NADPH)

organism: Aeropyrum pernix

substrate_name: 5,5'-dithiobis(2-nitrobenzoic acid)

enzyme: thioredoxin-disulfide reductase (NADPH)

substrate: 5,5'-dithiobis(2-nitrobenzoic acid)


organism: Sus scrofa


organism: Leptospira interrogans serovar Copenhageni

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH


substrate_name: thioredoxin disulfide

substrate: thioredoxin disulfide


organism: Rattus norvegicus

assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADPH


organism: Arabidopsis thaliana

substrate_name: thioredoxin

substrate: thioredoxin


organism: Deinococcus radiophilus

assay_conditions_summary: pH 7; 295.15 K; buffer context (50 mM potassium phosphate; cofactor NADPH

proof_lines: in 50 mM potassium phosphate buffer (pH 7.0), at 22°C


organism: Plasmodium falciparum (isolate FCH-5)

substrate_name: NADPH (at 20 degrees Celsius and pH 7.4)

assay_conditions_summary: pH 7.4; cofactor NADPH


organism: Taenia crassiceps


enzyme_display_name: sulfite dehydrogenase (cytochrome)

organism: Starkeya novella

substrate_name: sulfite

enzyme: sulfite dehydrogenase (cytochrome)

substrate: sulfite


organism: Thermotoga maritima

substrate_name: benzyl viologen

assay_conditions_summary: pH 9.5; 353.15 K; cofactor NADPH

proof_lines:
at pH 9.5 and 80°C
at pH 6.5 and 80°C

substrate: benzyl viologen


enzyme_display_name: thiosulfate dehydrogenase

organism: Pseudomonas sp.

substrate_name: thiosulfate

enzyme: thiosulfate dehydrogenase

substrate: thiosulfate


enzyme_display_name: thiol oxidase

organism: Aspergillus oryzae

smiles: OCCS

enzyme: thiol oxidase


enzyme_display_name: sulfide-cytochrome-c reductase (flavocytochrome c)

organism: Allochromatium vinosum

substrate_name: Sulfide

assay_conditions_summary: pH 8.5; 293.15 K; buffer 10 mM Tris-HCl

proof_lines: in 10 mM Tris-HCl buffer, pH 8.5, at 20°C

substrate: Sulfide


substrate_name: N-acetylcysteine

substrate: N-acetylcysteine


substrate_name: D-Cys

substrate: D-Cys


enzyme_display_name: methanethiol oxidase

organism: Hyphomicrobium sp.

enzyme: methanethiol oxidase


enzyme_display_name: prenylcysteine oxidase

enzyme: prenylcysteine oxidase


enzyme_display_name: formylglycine-generating enzyme

organism: Thermomonospora curvata

enzyme: formylglycine-generating enzyme


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: 5'-adenylyl sulfate (at pH 8.5 and 30 degrees Celsius)


enzyme_display_name: glutathione oxidase

enzyme: glutathione oxidase


enzyme_display_name: L-methionine (S)-S-oxide reductase

organism: Escherichia coli B

substrate_name: L-methionine (S)-S-oxide

enzyme: L-methionine (S)-S-oxide reductase

substrate: L-methionine (S)-S-oxide


enzyme_display_name: L-methionine (R)-S-oxide reductase

organism: Escherichia coli

substrate_name: L-Methionine (R)-S-oxide; Reduced thioredoxin

kcat_over_km_origin: calculated

source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org); CC BY-NC-ND 4.0

source_databases_merged: sabio_rk brenda skid

enzyme: L-methionine (R)-S-oxide reductase


organism: Escherichia coli (strain K12)

substrate_name: L-methionine-(R)-S-oxide

substrate: L-methionine-(R)-S-oxide


organism: Saccharomyces cerevisiae

substrate_name: Reduced thioredoxin; L-Methionine (R)-S-oxide

sequence_source: UniProtKB REST direct lookup P36088; UniProtKB reviewed (Swiss-Prot)


organism: Mus musculus

substrate_name: H2O; O2; Methanethiol

substrate: H2O; O2; Methanethiol


organism: Thermoplasma acidophilum

substrate_name: L-methionine (R)-S-oxide

sequence_source: UniProt REST Q9HJW5 canonical sequence; not accepted as row-specific evidence for the unspecified variant

smiles: CS(=O)CCC(C(=O)O)N

substrate: L-methionine (R)-S-oxide


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: 3-HSA (with FAD at pH 7 and at 25 degrees Celsius)

assay_conditions_summary: cofactor FAD


enzyme_display_name: glutathione dehydrogenase (ascorbate)

organism: Homo sapiens

substrate_name: dehydroascorbate

sequence_source: UniProtKB REST accession Q9H4Y5 direct lookup on 2026-06-05

enzyme: glutathione dehydrogenase (ascorbate)

substrate: dehydroascorbate


enzyme_display_name: respiratory dimethylsulfoxide reductase

substrate_name: 2-mercaptopyridine N-oxide

enzyme: respiratory dimethylsulfoxide reductase

substrate: 2-mercaptopyridine N-oxide


substrate_name: 2-chloropyridine N-oxide (at pH 5 and at 30 degrees Celsius)


enzyme_display_name: glutathionyl-hydroquinone reductase

organism: Sphingobium chlorophenolicum

enzyme: glutathionyl-hydroquinone reductase


substrate_name: glutathione

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

proof_lines:
pH 8.0, 23°C
Raw SKiD Env: Temp=23°C, pH=8
Raw SKiD Env: Temp=-----, pH=7.5

substrate: glutathione


enzyme_display_name: assimilatory sulfite reductase (ferredoxin)

organism: Limnospira platensis

substrate_name: S-Sulfoglutathione

substrate: S-Sulfoglutathione


enzyme_display_name: chlorate reductase

organism: Haloferax mediterranei

substrate_name: Chlorate

enzyme: chlorate reductase

substrate: Chlorate


enzyme_display_name: sulfiredoxin

substrate_name: ATP

assay_conditions_summary: pH 7; 303.15 K; buffer activity measured in TK; cofactor ATP

enzyme: sulfiredoxin

substrate: ATP


organism: Stutzerimonas chloritidismutans

sequence: LNMLEPVGETLASEYPYXK

wild_type_sequence: LNMLEPVGETLASEYPYXK


enzyme_display_name: nitrate reductase (cytochrome)

organism: Cereibacter sphaeroides f. sp. denitrificans

substrate_name: nitrate

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

enzyme: nitrate reductase (cytochrome)

substrate: nitrate


enzyme_display_name: homocysteine S-methyltransferase

organism: Arabidopsis thaliana

substrate_name: S-methylmethionine

enzyme: homocysteine S-methyltransferase

substrate: S-methylmethionine


substrate_name: L-homocysteine

substrate: L-homocysteine


organism: Brassica oleracea var. italica

substrate_name: DL-homocysteine

substrate: DL-homocysteine


enzyme_display_name: phosphoethanolamine N-methyltransferase

organism: Plasmodium vivax

substrate_name: Ethanolamine phosphate

sequence_source: UniProtKB:A5K867 direct lookup

smiles: C(COP(=O)(O)O)N

enzyme: phosphoethanolamine N-methyltransferase

substrate: Ethanolamine phosphate


enzyme_display_name: caffeoyl-CoA O-methyltransferase

organism: Petroselinum crispum

substrate_name: caffeoyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: caffeoyl-CoA O-methyltransferase

substrate: caffeoyl-CoA


organism: Pyrus x bretschneideri

assay_conditions_summary: pH 4; 310.15 K; cofactor CoA


organism: Triticum aestivum

substrate_name: S-Adenosyl-L-methionine; Caffeoyl-CoA

source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org)

substrate: S-Adenosyl-L-methionine; Caffeoyl-CoA


organism: Vanilla planifolia

substrate_name: tricetin

substrate: tricetin


enzyme_display_name: tryptophan 2-C-methyltransferase

organism: Kitasatospora setae

substrate_name: L-tryptophan

enzyme: tryptophan 2-C-methyltransferase

substrate: L-tryptophan


enzyme_display_name: eukaryotic sulfide quinone oxidoreductase

substrate_name: sulfide (with sulfite as electron acceptor)


organism: Pseudomonas denitrificans


organism: Methanobacterium ivanovii

sequence_source: UniProtKB reviewed accession P29564


organism: Aspergillus parasiticus

substrate_name: dihydrodemethylsterigmatocystin

substrate: dihydrodemethylsterigmatocystin


organism: Pseudomonas denitrificans (nom. rej.)

substrate_name: uroporphyrinogen III

substrate: uroporphyrinogen III


enzyme_display_name: alcohol dehydrogenase

organism: Homo sapiens

substrate_name: all-trans-Retinal

enzyme: alcohol dehydrogenase

substrate: all-trans-Retinal


enzyme_display_name: sterigmatocystin 8-O-methyltransferase

substrate_name: sterigmatocystin

enzyme: sterigmatocystin 8-O-methyltransferase

substrate: sterigmatocystin


organism: Thalictrum flavum

substrate_name: (R,S)-Norreticuline

substrate: (R,S)-Norreticuline


substrate_name: S-Adenosyl-L-methionine

substrate: S-Adenosyl-L-methionine


enzyme_display_name: (S)-scoulerine 9-O-methyltransferase

organism: Coptis japonica

substrate_name: (S)-scoulerine

enzyme: (S)-scoulerine 9-O-methyltransferase

substrate: (S)-scoulerine


enzyme_display_name: methionine S-methyltransferase

organism: Wollastonia biflora

substrate_name: L-Met

smiles: CSCCC(C(=O)O)N

enzyme: methionine S-methyltransferase

substrate: L-Met


substrate_name: S-Adenosyl-L-methionine; (S)-Scoulerine

substrate: S-Adenosyl-L-methionine; (S)-Scoulerine


organism: Eschscholzia californica


enzyme_display_name: methionine synthase

organism: Escherichia coli

substrate_name: S-adenosyl-L-methionine

enzyme: methionine synthase

substrate: S-adenosyl-L-methionine


substrate_name: (S)-Stylopine

substrate: (S)-Stylopine


substrate_name: (R,S)-stylopine

substrate: (R,S)-stylopine


organism: Dehalococcoides mccartyi

substrate_name: L-homocysteine

smiles: C(CS)C(C(=O)O)N

substrate: L-homocysteine


organism: Rattus norvegicus

assay_conditions_summary: pH 7.4; 310.15 K; buffer 50 mM phosphate

proof_lines: in 50 mM phosphate buffer, pH 7.4, at 37°C


organism: Thermus thermophilus

sequence_source: UniProt REST Q5SKM5 canonical sequence


organism: Sus scrofa

ki_unit: mM


organism: Papaver bracteatum

substrate_name: (R,S)-Stylopine

substrate: (R,S)-Stylopine


organism: Papaver somniferum


enzyme_display_name: chlorophenol O-methyltransferase

organism: Trichoderma longibrachiatum

substrate_name: 2,4,6-trichlorophenol (2,4,6-TCP)

enzyme: chlorophenol O-methyltransferase

substrate: 2,4,6-trichlorophenol (2,4,6-TCP)


enzyme_display_name: arsenite methyltransferase

substrate_name: S-Adenosyl-L-methionine; Arsenite

enzyme: arsenite methyltransferase

substrate: S-Adenosyl-L-methionine; Arsenite


substrate_name: sodium arsenite

substrate: sodium arsenite


enzyme_display_name: (S)-coclaurine-N-methyltransferase

organism: Stephania intermedia

substrate_name: (R)-coclaurine

enzyme: (S)-coclaurine-N-methyltransferase

substrate: (R)-coclaurine


enzyme_display_name: columbamine O-methyltransferase

substrate_name: S-Adenosyl-L-methionine; Columbamine

enzyme: columbamine O-methyltransferase

substrate: S-Adenosyl-L-methionine; Columbamine


enzyme_display_name: jasmonate O-methyltransferase

organism: Arabidopsis thaliana

enzyme: jasmonate O-methyltransferase


substrate_name: (RS)-coclaurine

sequence_source: Selected-batch preserved sequence; compact direct UniProt REST check of Q948P7 confirmed it is length 358 and byte-identical to the live unreviewed canonical Q948P7_COPJA sequence.

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=8

substrate: (RS)-coclaurine


organism: Brassica rapa subsp. oleifera

substrate_name: jasmonate

substrate: jasmonate


substrate_name: (-)-Jasmonic acid

substrate: (-)-Jasmonic acid


organism: Thalictrum flavum subsp. glaucum

substrate_name: (R,S)-norreticuline

substrate: (R,S)-norreticuline


organism: Humulus lupulus

substrate_name: chalconaringenin

substrate: chalconaringenin


organism: Medicago sativa

substrate_name: isoliquiritigenin

substrate: isoliquiritigenin


organism: Aphanothece halophytica

substrate_name: S-adenosyl-L-homocysteine (at pH 8.8 and at 37 degrees Celsius)


enzyme_display_name: glycine/sarcosine N-methyltransferase

organism: Halorhodospira halochloris

substrate_name: sarcosine (at pH 7.4 and at 37 degrees Celsius)

smiles: CNCC(=O)O

enzyme: glycine/sarcosine N-methyltransferase


enzyme_display_name: theobromine synthase

organism: Coffea arabica

enzyme: theobromine synthase


organism: Camellia ptilophylla

substrate_name: 7-methylxanthine (in the presence of 50 uM S-adenosyl-L-methionine)


organism: Camellia irrawadiensis

substrate: 7-methylxanthine (in the presence of 50 uM S-adenosyl-L-methionine)


organism: Parasynechococcus marenigrum (strain WH8102)

substrate_name: AdoMet (with glycine at pH 8.2 and at 37 degrees Celsius)

assay_conditions_summary: pH 8


organism: Theobroma cacao


substrate_name: AdoMet (with dimethylglycine at pH 7.4 and at 37 degrees Celsius)


enzyme_display_name: caffeine synthase

organism: Camellia sinensis

enzyme: caffeine synthase


substrate_name: 7-methylxanthine for the recombinant protein


substrate_name: paraxanthine

substrate: paraxanthine


enzyme_display_name: tricin synthase

organism: Oryza sativa subsp. japonica

substrate_name: tricetin

enzyme: tricin synthase

substrate: tricetin


organism: Oryza sativa

substrate_name: S-Adenosyl-L-methionine; Tricetin

substrate: S-Adenosyl-L-methionine; Tricetin


organism: Zea mays


organism: Bacillus subtilis

substrate_name: S-adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature N192A to reconstruct the assayed variant sequence.

substrate: S-adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K197A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K133A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature N200A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K204A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K197A/N200A/E202A/K204A/K205A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, mutant enzyme K197A/N200A/E202A/K204A/K205A


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature E202A to reconstruct the assayed variant sequence.


sequence_source: uniprot


enzyme_display_name: carnosine N-methyltransferase

organism: Gallus gallus

substrate_name: carnosine

enzyme: carnosine N-methyltransferase

substrate: carnosine


organism: Saccharomyces cerevisiae

substrate_name: S-Adenosyl-L-methionine; Carnosine

sequence_source: UniProtKB P53934 direct accession lookup; sequence matched the accession reuse cache.

substrate: S-Adenosyl-L-methionine; Carnosine


organism: Methanocaldococcus jannaschii

substrate_name: S-Adenosyl-L-methionine; tRNA guanine

proof_lines: SABIO-RK modifier species: tRNA (guanine37-N1)-methyltransferase(Enzyme) mutant Y176A His-tag

substrate: S-Adenosyl-L-methionine; tRNA guanine


proof_lines: SABIO-RK modifier species: tRNA (guanine37-N1)-methyltransferase(Enzyme) mutant R144A His-tag


organism: Streptomyces azureus


enzyme_display_name: mycinamicin VI 2''-O-methyltransferase

organism: Micromonospora griseorubida

substrate_name: mycinamicin VI

enzyme: mycinamicin VI 2''-O-methyltransferase

substrate: mycinamicin VI


enzyme_display_name: flavonoid 4'-O-methyltransferase

organism: Artemisia annua

substrate_name: kaempferol

enzyme: flavonoid 4'-O-methyltransferase

substrate: kaempferol


enzyme_display_name: [methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M

organism: Methanosarcina barkeri


organism: Methanosarcina barkeri (strain Fusaro / DSM 804)

substrate_name: dimethylamine

smiles: CNC

substrate: dimethylamine


enzyme_display_name: mycinamicin III 3''-O-methyltransferase

substrate_name: mycinamicin III

sequence_source: uniprot_ec_organism_unique; direct reviewed UniProtKB accession check: Q49492

enzyme: mycinamicin III 3''-O-methyltransferase

substrate: mycinamicin III


enzyme_display_name: salicylate carboxymethyltransferase

organism: Clarkia breweri

substrate_name: salicylate

enzyme: salicylate carboxymethyltransferase

substrate: salicylate


organism: Pisum sativum


enzyme_display_name: phenylethanolamine N-methyltransferase

organism: Macaca mulatta

substrate_name: normetanephrine

enzyme: phenylethanolamine N-methyltransferase

substrate: normetanephrine


enzyme_display_name: selenocysteine Se-methyltransferase

organism: Astragalus bisulcatus

enzyme: selenocysteine Se-methyltransferase


enzyme_display_name: phenylpyruvate C(3)-methyltransferase

organism: Streptomyces hygroscopicus

enzyme: phenylpyruvate C(3)-methyltransferase


enzyme_display_name: emodin O-methyltransferase

organism: Aspergillus terreus

substrate_name: emodin

enzyme: emodin O-methyltransferase

substrate: emodin


enzyme_display_name: trans-anol O-methyltransferase

organism: Acorus calamus

substrate_name: resveratrol

enzyme: trans-anol O-methyltransferase

substrate: resveratrol


organism: Amycolatopsis mediterranei

substrate_name: 27-O-demethylrifamycin SV

substrate: 27-O-demethylrifamycin SV


enzyme_display_name: carminomycin 4-O-methyltransferase

organism: Streptomyces sp.

substrate_name: carminomycin

enzyme: carminomycin 4-O-methyltransferase

substrate: carminomycin


enzyme_display_name: mitomycin 6-O-methyltransferase

organism: Streptomyces lavendulae

proof_lines:
pH 7.4, 30°C
Raw SKiD Env: Temp=30°C, pH=7.4

enzyme: mitomycin 6-O-methyltransferase


organism: Saccharomyces cerevisiae


enzyme_display_name: type I protein arginine methyltransferase

organism: Homo sapiens

substrate_name: AdoMet

substrate: AdoMet


organism: Rattus norvegicus

enzyme: type I protein arginine methyltransferase


organism: Sphingobium sp.

substrate_name: vanillate

sequence_source: UniProtKB reviewed accession G2IQS7; canonical sequence preserved in the selected batch

substrate: vanillate


enzyme_display_name: mRNA m(6)A methyltransferase

enzyme: mRNA m(6)A methyltransferase


organism: Mycobacterium abscessus

sequence_source: UniProtKB reviewed accession B1MCE2 fetched by direct accession lookup


organism: Eubacterium limosum

substrate_name: L-carnitine

substrate: L-carnitine


substrate_name: gamma-butyrobetaine

substrate: gamma-butyrobetaine


enzyme_display_name: norajmaline N-methyltransferase

organism: Rauvolfia serpentina

substrate_name: norajmaline

enzyme: norajmaline N-methyltransferase

substrate: norajmaline


enzyme_display_name: ajmaline N-methyltransferase

enzyme: ajmaline N-methyltransferase


enzyme_display_name: acetylserotonin O-methyltransferase

organism: Arabidopsis thaliana

substrate_name: N-acetylserotonin

enzyme: acetylserotonin O-methyltransferase

substrate: N-acetylserotonin


organism: Bos taurus

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Oncorhynchus tshawytscha


enzyme_display_name: mycothione reductase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

enzyme: mycothione reductase

substrate: NADPH


organism: Oryza sativa

sequence_source: UniProtKB REST direct accession check for Q6ZD89 on 2026-06-24


enzyme_display_name: flavone 3'-O-methyltransferase

organism: Chrysosplenium americanum

substrate_name: quercetin

enzyme: flavone 3'-O-methyltransferase

substrate: quercetin


enzyme_display_name: Transferred entry: 2.1.1.354

substrate_name: S-Adenosyl-L-methionine

enzyme: Transferred entry: 2.1.1.354

substrate: S-Adenosyl-L-methionine


enzyme_display_name: thymidylate synthase

organism: Crithidia fasciculata

enzyme: thymidylate synthase


organism: Enterococcus faecalis

substrate_name: methylenetetrahydrofolate

substrate: methylenetetrahydrofolate


organism: Lactobacillus casei

substrate_name: dUMP

substrate: dUMP


enzyme_display_name: peroxidase

organism: Burkholderia pseudomallei

assay_conditions_summary: pH 4.5; 298.15 K; cofactor NADH

enzyme: peroxidase


enzyme_display_name: sterol 24-C-methyltransferase

organism: Glycine max

substrate_name: Cycloartenol; S-Adenosyl-L-methionine

sequence_source: UniProtKB Q43445 REST JSON, active TrEMBL entry for Glycine max; canonical sequence evidence is preserved in the selected batch.

enzyme: sterol 24-C-methyltransferase

substrate: Cycloartenol; S-Adenosyl-L-methionine


organism: Leishmania major


enzyme_display_name: isoflavone 4'-O-methyltransferase

organism: Glycyrrhiza echinata

enzyme: isoflavone 4'-O-methyltransferase


organism: Pisum sativum


organism: Medicago truncatula


enzyme_display_name: indolepyruvate C-methyltransferase

organism: Streptomyces griseus

substrate_name: indolepyruvate (at 30 degrees Celsius and pH 7.6)

enzyme: indolepyruvate C-methyltransferase


organism: Mus musculus

substrate_name: S-methyl-L-methionine

substrate: S-methyl-L-methionine


organism: Rattus norvegicus

substrate_name: L-homocysteine

sequence_source: UniProtKB O09171 direct lookup

substrate: L-homocysteine


organism: Sus scrofa

sequence_source: UniProtKB Q95332 direct lookup; entry flagged Fragment


substrate_name: glycine betaine

substrate: glycine betaine


enzyme_display_name: putrescine N-methyltransferase

organism: Datura stramonium

enzyme: putrescine N-methyltransferase


organism: Solanum lycopersicum

substrate_name: putrescine

substrate: putrescine


enzyme_display_name: mRNA (guanine-N(7))-methyltransferase

organism: Encephalitozoon cuniculi (strain GB-M1)

substrate_name: GTP

enzyme: mRNA (guanine-N(7))-methyltransferase

substrate: GTP


organism: Saccharomyces cerevisiae

substrate_name: GpppA

substrate: GpppA


enzyme_display_name: methyltransferase cap1

organism: Homo sapiens

enzyme: methyltransferase cap1


organism: Orthopoxvirus vaccinia


enzyme_display_name: catechol O-methyltransferase

substrate_name: S-Adenosyl-L-methionine; L-Adrenaline

enzyme: catechol O-methyltransferase

substrate: S-Adenosyl-L-methionine; L-Adrenaline


organism: Sus scrofa domesticus


enzyme_display_name: calmodulin-lysine N-methyltransferase

enzyme: calmodulin-lysine N-methyltransferase


enzyme_display_name: nicotinate N-methyltransferase

substrate_name: nicotinate

enzyme: nicotinate N-methyltransferase

substrate: nicotinate


organism: Aquilegia coerulea

substrate_name: S-Adenosyl-L-methionine; Nicotinate

substrate: S-Adenosyl-L-methionine; Nicotinate


substrate_name: Nicotinate; S-Adenosyl-L-methionine

substrate: Nicotinate; S-Adenosyl-L-methionine


organism: Theobroma cacao


organism: Bos taurus

substrate_name: S-adenosyl-L-methionine

assay_conditions_summary: pH 10

substrate: S-adenosyl-L-methionine


organism: Arabidopsis thaliana


organism: Enterobacteria phage T4

substrate_name: S-adenosylmethionine

substrate: S-adenosylmethionine


organism: Escherichia phage T1


organism: Pyrococcus horikoshii


organism: Enterococcus faecalis


organism: Pinus massoniana


organism: Caenorhabditis elegans


enzyme_display_name: histamine N-methyltransferase

enzyme: histamine N-methyltransferase


organism: Cavia porcellus

substrate_name: histamine

substrate: histamine


organism: Mus musculus


organism: Rattus rattus

substrate_name: S-Adenosyl-L-methionine; Histamine

substrate: S-Adenosyl-L-methionine; Histamine


enzyme_display_name: apigenin 4'-O-methyltransferase

organism: Plagiochasma appendiculatum

substrate_name: apigenin

enzyme: apigenin 4'-O-methyltransferase

substrate: apigenin


organism: Rattus norvegicus


organism: Papaver somniferum

substrate_name: (S)-scoulerine

substrate: (S)-scoulerine


organism: Coptis japonica


enzyme_display_name: thiol S-methyltransferase

organism: Phaeodactylum tricornutum

substrate_name: thiocyanate

enzyme: thiol S-methyltransferase

substrate: thiocyanate


organism: Homo sapiens

substrate_name: hydrogen sulfide

smiles: S

substrate: hydrogen sulfide


enzyme_display_name: aminomethyltransferase

organism: Gallus gallus

substrate_name: tetrahydrofolate

enzyme: aminomethyltransferase

substrate: tetrahydrofolate


substrate_name: NAD+; Glycine; 5,6,7,8-Tetrahydrofolate

assay_conditions_summary: cofactor NAD+

substrate: NAD+; Glycine; 5,6,7,8-Tetrahydrofolate


organism: Oryctolagus cuniculus


organism: Pisum sativum


organism: Canis familiaris


organism: Mycobacterium tuberculosis


enzyme_display_name: methionyl-tRNA formyltransferase

organism: Enterococcus faecalis

enzyme: methionyl-tRNA formyltransferase


organism: Escherichia coli (strain K12)


enzyme_display_name: D-alanine 2-hydroxymethyltransferase

organism: Ensifer sp. AJ110404

smiles: CC(CO)(C(=O)O)N

enzyme: D-alanine 2-hydroxymethyltransferase


organism: Streptomyces niveus

substrate_name: decarbamoylnovobiocin

substrate: decarbamoylnovobiocin


enzyme_display_name: acetyl-CoA carboxytransferase

substrate_name: malonyl-CoA

enzyme: acetyl-CoA carboxytransferase

substrate: malonyl-CoA


enzyme_display_name: aspartate carbamoyltransferase

organism: Methanocaldococcus jannaschii

substrate_name: L-aspartate

sequence_source: UniProtKB Q58976 direct accession lookup; entry PYRB_METJA; reviewed Swiss-Prot; fetched 2026-06-03.

proof_lines:
Raw SKiD Env: Temp=37°C, pH=-----
Raw SKiD Env: Temp=55°C, pH=-----
Raw SKiD Env: Temp=15°C, pH=-----

enzyme: aspartate carbamoyltransferase

substrate: L-aspartate


organism: Pyrococcus abyssi

substrate_name: Carbamoyl phosphate

sequence_source: UniProtKB P77918 direct accession lookup; entry PYRB_PYRAB; reviewed Swiss-Prot; fetched 2026-06-03.

proof_lines:
Raw SKiD Env: Temp=37°C, pH=-----
Raw SKiD Env: Temp=30°C, pH=-----
Raw SKiD Env: Temp=55°C, pH=-----

substrate: Carbamoyl phosphate


enzyme_display_name: ornithine carbamoyltransferase

organism: Bos taurus

substrate_name: ornithine

smiles: C(CC(C(=O)O)N)CN

proof_lines:
at pH 7.2
at pH 8.5

enzyme: ornithine carbamoyltransferase

substrate: ornithine


substrate_name: L-citrulline

smiles: C(CC(C(=O)O)N)CNC(=O)N

proof_lines:
at 25°C and pH 8.4
at 25°C and pH 7.1

substrate: L-citrulline


substrate_name: Phosphate

smiles: O=P(O)(O)O

substrate: Phosphate


substrate_name: Carbamoyl phosphate; L-Ornithine

substrate: Carbamoyl phosphate; L-Ornithine


substrate_name: L-Citrulline

substrate: L-Citrulline


substrate_name: L-Ornithine; Carbamoyl phosphate

substrate: L-Ornithine; Carbamoyl phosphate


smiles: NC(=O)OP(=O)(O)O


substrate_name: L-Ornithine

substrate: L-Ornithine


organism: Mycoplasma arthritidis

substrate_name: L-Citrulline; Phosphate

substrate: L-Citrulline; Phosphate


organism: Pseudomonas aeruginosa


organism: Agrobacterium tumefaciens


organism: Pseudomonas syringae phaseolicola


enzyme_display_name: putrescine carbamoyltransferase

substrate_name: putrescine

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature Y230V/G231S/L232M/Y233G to reconstruct the assayed variant sequence.

smiles: C(CCN)CN

proof_lines: recombinant PTC mutant Y230V/G231S/L232M/Y233G, pH 8.5, 37°C

enzyme: putrescine carbamoyltransferase

substrate: putrescine


organism: Sus scrofa


enzyme_display_name: transketolase

organism: Cyberlindnera jadinii

substrate_name: thiamine diphosphate

enzyme: transketolase

substrate: thiamine diphosphate


organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

substrate_name: fructose 6-phosphate (at pH 7.0 and 37 degrees Celsius)

smiles: C(C(C(C(C(=O)CO)O)O)O)OP(=O)(O)O

assay_conditions_summary: pH 7


organism: Homo sapiens

substrate_name: D-Ribose 5-phosphate; D-Xylulose 5-phosphate


organism: Leishmania mexicana

proof_lines:
pH 7.5
Raw SKiD Env: Temp=-----, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----


organism: Saccharomyces cerevisiae

substrate_name: D-Ribose 5-phosphate

substrate: D-Ribose 5-phosphate


organism: Rattus norvegicus

substrate: D-Ribose 5-phosphate; D-Xylulose 5-phosphate


substrate_name: D-Xylulose 5-phosphate

substrate: D-Xylulose 5-phosphate


organism: Rhodobacter sphaeroides


organism: Scheffersomyces stipitis


substrate_name: Hydroxypyruvate

substrate: Hydroxypyruvate


substrate_name: sedoheptulose 7-phosphate

substrate: sedoheptulose 7-phosphate


organism: Spinacia oleracea

substrate_name: D-ribose 5-phosphate

substrate: D-ribose 5-phosphate


substrate_name: xylulose 5-phosphate

smiles: C(C(C(C(=O)CO)O)O)OP(=O)(O)O

substrate: xylulose 5-phosphate


enzyme_display_name: ubiquinol oxidase (non-electrogenic)

organism: Arabidopsis thaliana

enzyme: ubiquinol oxidase (non-electrogenic)


enzyme_display_name: lignostilbene alphabeta-dioxygenase

organism: Sphingomonas paucimobilis

enzyme: lignostilbene alphabeta-dioxygenase


enzyme_display_name: flavanone 3-dioxygenase

organism: Oryza sativa subsp. japonica

substrate_name: S-eriodictyol

enzyme: flavanone 3-dioxygenase

substrate: S-eriodictyol


enzyme_display_name: vinorine hydroxylase

organism: Rauvolfia serpentina

substrate_name: vinorine

enzyme: vinorine hydroxylase

substrate: vinorine


enzyme_display_name: methyl farnesoate epoxidase

organism: Diploptera punctata

substrate_name: methyl (2E,6E)-farnesoate (with purified enzyme)

enzyme: methyl farnesoate epoxidase


enzyme_display_name: (E)-2-methylbutanal oxime monooxygenase

organism: Manihot esculenta

substrate_name: (Z)-2-methylbutanal oxime

enzyme: (E)-2-methylbutanal oxime monooxygenase

substrate: (Z)-2-methylbutanal oxime


enzyme_display_name: methanethiol oxidase

substrate_name: methanethiol

enzyme: methanethiol oxidase

substrate: methanethiol


organism: Hyphomicrobium sp


organism: Mus musculus


enzyme_display_name: sphingoid base N-palmitoyltransferase

substrate_name: sphinganine (d18:0)

enzyme: sphingoid base N-palmitoyltransferase

substrate: sphinganine (d18:0)


substrate_name: sphinganine

substrate: sphinganine


enzyme_display_name: laccase

organism: Bacillus sp. SL-1

substrate_name: Syringaldazine; O2

sequence_source: UniProtKB A0A165W3F6 canonical FASTA fetched during exact accession lookup; UniProt entry is Laccase, EC 1.10.3.2, Bacillus sp. SL-1, sequence length 513.

assay_conditions_summary: buffer conditions and no primary measurement location

enzyme: laccase

substrate: Syringaldazine; O2


organism: Bacteroides thetaiotaomicron


substrate_name: Syringaldazine

substrate: Syringaldazine


organism: Escherichia coli


organism: Fomitopsis pinicola

substrate_name: guaiacol

sequence_source: UniProtKB:S8FGV1 direct FASTA; reviewed Swiss-Prot laccase EC 1.10.3.2; PMID:34116754 reference.

assay_conditions_summary: pH 5; 303.15 K; buffer sodium-citrate

substrate: guaiacol


organism: basidiomycete PM1

sequence_source: UniProt REST direct accession lookup, Q12571, 2026-05-24


organism: Lentinus brumalis

assay_conditions_summary: pH 4; 303.15 K; buffer their

proof_lines:
in McIlvaine buffer (pH 4.0), at 30°C
in McIlvaine buffer (pH 5.0), at 30°C


organism: Meiothermus ruber


organism: Caldalkalibacillus thermarum

substrate_name: O2; 2,6-Dimethoxyphenol

substrate: O2; 2,6-Dimethoxyphenol


organism: Aquifex aeolicus


organism: Phoma sp.

substrate_name: syringaldazine

substrate: syringaldazine


organism: Pseudomonas putida

sequence_source: UniProtKB exact accession Q88C03 REST lookup, retrieved 2026-07-01


enzyme_display_name: trans-4-coumaroyl-CoA 2'-hydroxylase

organism: Ipomoea batatas

substrate_name: feruloyl-CoA

assay_conditions_summary: pH 7.2; cofactor CoA

proof_lines: kcat is 0.28 sec(-1) with feruloyl-CoA as substrate. kcat is 0.28 sec(-1) with p-Coumaroyl-CoA as substrate.

enzyme: trans-4-coumaroyl-CoA 2'-hydroxylase

substrate: feruloyl-CoA


proof_lines: kcat is 0.35 sec(-1) with feruloyl-CoA as substrate. kcat is 0.33 sec(-1) with p-Coumaroyl-CoA as substrate.


proof_lines: kcat is 0.55 sec(-1) with feruloyl-CoA as substrate. kcat is 0.64 sec(-1) with p-Coumaroyl-CoA as substrate.


organism: Ruta graveolens

proof_lines: kcat is 0.46 sec(-1) with feruloyl-CoA as substrate (PubMed:22168819). kcat is 0.71 sec(-1) with p-coumaroyl-CoA as substrate (PubMed:22168819).


enzyme_display_name: methylphosphonate hydroxylase

organism: Gimesia maris (strain ATCC 29201 / DSM 8797 / 534-30)

substrate_name: methylphosphonate

proof_lines: kcat is 0.36 sec(-1) with methylphosphonate as substrate. kcat is 0.42 sec(-1) with 2-oxoglutarate as substrate.

enzyme: methylphosphonate hydroxylase

substrate: methylphosphonate


enzyme_display_name: methane monooxygenase (particulate)

organism: Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)

substrate_name: Unknown

assay_conditions_summary: cofactor NADH

proof_lines: Kinetic parameters have been established with the pMMO heteromeric complex.

enzyme: methane monooxygenase (particulate)

substrate: Unknown


enzyme_display_name: lupanine 17-hydroxylase (cytochrome c)

organism: Pseudomonas sp

substrate_name: sparteine (at 25 degrees Celsius and at pH 8.5)

proof_lines: kcat is 217 sec(-1) with lupanine as substrate and 11.8 sec(-1) with sparteine as substrate.

enzyme: lupanine 17-hydroxylase (cytochrome c)


enzyme_display_name: isopiperitenol dehydrogenase

organism: Mentha piperita

substrate_name: (-)-trans-carveol (at pH 7.5)

assay_conditions_summary: pH 7.5; cofactor NADP+

proof_lines: kcat is 0.02 sec(-1) with (-)-trans-carveol as substrate (at pH 7.5), kcat is 0.06 sec(-1) with (-)-trans-carveol as substrate (at pH 10), kcat is 0.002 sec(-1) with (-)-trans-isopiperitenol as substrate (at pH 7.5).

enzyme: isopiperitenol dehydrogenase

substrate: (-)-trans-carveol (at pH 7.5)


enzyme_display_name: tyramine N-methyltransferase

organism: Lophophora williamsii

substrate_name: mescaline

proof_lines: kcat is 0.0001 sec(-1) with mescaline as substrate (PubMed:37675639). kcat is 0.130 sec(-1) with 4-hydroxy-3,5-dimethoxyphenethylamine as substrate (PubMed:37675639).

enzyme: tyramine N-methyltransferase

substrate: mescaline


enzyme_display_name: trans-anol O-methyltransferase

organism: Pimpinella anisum

substrate_name: isoeugenol (at pH 7.5 and 25 degrees Celsius)

assay_conditions_summary: pH 7.5; buffer or captured segment for the populated kcat 0

enzyme: trans-anol O-methyltransferase


enzyme_display_name: phenylpyruvate C(3)-methyltransferase

organism: Streptomyces hygroscopicus

substrate_name: S-adenosyl-L-methionine

proof_lines: kcat is 0.8 sec(-1) with S-adenosyl-L-methionine as substrate. kcat is 8.15 sec(-1) with phenylpyruvic acid as substrate.

enzyme: phenylpyruvate C(3)-methyltransferase

substrate: S-adenosyl-L-methionine


organism: Pyrobaculum aerophilum

sequence_source: UniProtKB exact accession Q8ZWA8 REST lookup, retrieved 2026-07-01


organism: Streptomyces viridochromogenes

sequence_source: UniProtKB exact accession lookup J9S5G3, retrieved 2026-05-24


organism: Shiraia sp. SUPER-H168


organism: Streptomyces ipomoeae

sequence_source: UniProtKB REST A3QVH2, checked 2026-05-30


organism: Streptomyces coelicolor


organism: Corynebacterium glutamicum


organism: Streptomyces sviceus


organism: Mus musculus


enzyme_display_name: sphingoid base N-stearoyltransferase

enzyme: sphingoid base N-stearoyltransferase


enzyme_display_name: RING-type E3 ubiquitin transferase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: ATP

assay_conditions_summary: cofactor ATP

enzyme: RING-type E3 ubiquitin transferase

substrate: ATP


organism: Escherichia coli

substrate_name: UDP-Glc

substrate: UDP-Glc


enzyme_display_name: quinolinate synthase

organism: Bacillus subtilis (strain 168)

substrate_name: dihydroxyacetone phosphate

enzyme: quinolinate synthase

substrate: dihydroxyacetone phosphate


organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)


enzyme_display_name: pyridinol guanylyltransferase

organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

substrate_name: GTP

enzyme: pyridinol guanylyltransferase

substrate: GTP


organism: Cricetulus griseus

substrate_name: L-serine

substrate: L-serine


organism: Homo sapiens

substrate_name: serine (in the presence of 1 mM PE)

substrate: serine (in the presence of 1 mM PE)


substrate_name: serine (in the presence of 2 mM PC)

substrate: serine (in the presence of 2 mM PC)


enzyme_display_name: isoamyl acetate esterase

substrate_name: 3-methylbutyl acetate

enzyme: isoamyl acetate esterase

substrate: 3-methylbutyl acetate


enzyme_display_name: catechol oxidase

organism: Malus domestica

substrate_name: O2; Caffeoyl quinic acid

enzyme: catechol oxidase

substrate: O2; Caffeoyl quinic acid


organism: Bacillus licheniformis


organism: Geobacter metallireducens

sequence_source: UniProtKB:Q39TP1 direct FASTA; unreviewed TrEMBL multicopper oxidase type 2.

smiles: O=O


organism: Bacillus clausii

sequence_source: UniProtKB:Q5WEM6 canonical sequence retrieved by direct lookup on 2026-05-30


organism: Melanocarpus albomyces


organism: Halobacterium volcanii

sequence_source: UniProtKB direct lookup D4GPK6, reviewed Swiss-Prot entry LACC_HALVD


sequence_source: UniProtKB REST direct accession check on 2026-07-01: D4GPK6


organism: Meiothermus ruber

sequence_source: UniProtKB exact accession D3PLX1 REST lookup, retrieved 2026-07-01


enzyme_display_name: deacetoxycephalosporin-C synthase

organism: Streptomyces clavuligerus

substrate_name: ampicillin

enzyme: deacetoxycephalosporin-C synthase

substrate: ampicillin


proof_lines:
mutant C281Y, pH 7.4, 30°C
mutant enzyme C281Y


proof_lines:
mutant I305M, pH 7.4, 30°C
mutant enzyme I305M


substrate_name: Ampicillin

substrate: Ampicillin


substrate_name: Penicillin G

substrate: Penicillin G


proof_lines: pH 7.5, cosubstrate 2-oxohexanoate, recombinant mutants R258H and R258A


substrate_name: 2-Oxoglutarate; O2; Penicillin G

proof_lines: recombinant His-tagged enzyme, pH 7.5, 30°C

proof_lines: recombinant FF2 derived from gene shuffling

proof_lines: recombinant clone FF8 derived from gene shuffling

substrate: 2-Oxoglutarate; O2; Penicillin G


proof_lines: pH 7.5, cosubstrate 2-oxohexanoate, recombinant mutant R258A

proof_lines: pH 7.5, cosubstrate 2-oxo-4-methyl-pentanoate, recombinant mutant R258A


proof_lines: pH 7.5, cosubstrate 2-oxo-4-methyl-pentanoate, recombinant mutant R258Q

proof_lines: pH 7.5, cosubstrate 2-oxohexanoate, recombinant mutant R258Q


proof_lines: pH 7.5, cosubstrate 2-oxo-4-methyl-pentanoate, recombinant mutant R258L

proof_lines: pH 7.5, cosubstrate 2-oxohexanoate, recombinant mutant R258L


substrate_name: penicillin G

proof_lines: pH 7.5, cosubstrate 2-oxo-4-methyl-pentanoate, recombinant mutant R258F

proof_lines: pH 7.5, cosubstrate 2-oxohexanoate, recombinant mutant R258F

substrate: penicillin G


proof_lines: pH 7.5, cosubstrate 2-oxohexanoate, recombinant mutants R258A and R258Q


proof_lines: pH 7.5, cosubstrate 2-oxo-4-methyl-pentanoate, recombinant mutants R258H and R258Q


proof_lines: pH 7.5, cosubstrate 2-oxo-4-methyl-pentanoate, recombinant mutants R258A and R258F


proof_lines: pH 7.5, cosubstrate 2-oxoglutarate, recombinant wild-type enzyme


substrate_name: Penicillin N

substrate: Penicillin N


proof_lines:
mutant V275I, pH 7.4, 30°C
mutant enzyme V275I


proof_lines:
mutant enzyme L277Q
mutant L277Q


proof_lines:
mutant enzyme M188V
mutant M188V


proof_lines:
mutant enzyme C155Y
mutant C155Y


mutation_type: deletion


proof_lines: pH 7.5, cosubstrate 2-oxoglutarate, recombinant mutant R258K

proof_lines: pH 7.5, cosubstrate 2-oxohexanoate, recombinant mutant R258K

proof_lines: pH 7.5, cosubstrate 2-oxo-4-methyl-pentanoate, recombinant mutant R258K


proof_lines: pH 7.5, cosubstrate 2-oxohexanoate, recombinant mutants R258L and R258F


proof_lines: pH 7.5, cosubstrate 2-oxo-4-methyl-pentanoate, recombinant mutant R258H

proof_lines: pH 7.5, cosubstrate 2-oxohexanoate, recombinant mutant R258H

proof_lines: pH 7.5, cosubstrate 2-oxohexanoate, recombinant mutants R258H


proof_lines: pH 7.5, cosubstrate 2-oxo-4-methyl-pentanoate, recombinant mutants R258K, R258A, and R258L


proof_lines: pH 7.5, cosubstrate 2-oxohexanoate, recombinant mutants R258A and R258H


proof_lines:
mutant N304K, pH 7.4, 30°C
mutant enzyme N304K


proof_lines:
mutant V275I/I305M, pH 7.4, 30°C
mutant enzyme V275I/I305M


proof_lines:
mutant V275I7N304K, pH 7.4, 30°C
mutant C281Y7N304R, pH 7.4, 30°C


proof_lines:
mutant R306L, pH 7.4, 30°C
mutant R306L, 30°C


proof_lines:
mutant enzyme T91A
mutant T91A


proof_lines:
mutant enzyme H244Q
mutant H244Q


proof_lines:
mutant enzyme C155Y/Y184H/V275I/C281Y
mutant C155Y/Y184H/V275I/C281Y


proof_lines:
mutant enzyme Y184H
mutant Y184H


proof_lines: mutant enzyme C155Y/Y184H/V275I/C281Y/L305M, at pH 7.4 and 25°C


proof_lines: mutant enzyme C155Y/Y184H/V275I/C281Y/I305M/T213V/M73T, at pH 7.4 and 25°C


proof_lines: mutant enzyme C155Y/Y184H, at pH 7.4 and 25°C


enzyme_display_name: ferredoxin--NADP(+) reductase

organism: Anabaena sp.

substrate_name: reduced flavodoxin

assay_conditions_summary: pH 8; 286.15 K; cofactor NADPH

proof_lines:
pH 8.0, 13°C, wild-type enzyme
wild-type enzyme, pH 8.0
wild type enzyme of Anabaena sp.

enzyme: ferredoxin--NADP(+) reductase

substrate: reduced flavodoxin


substrate_name: NADH

assay_conditions_summary: cofactor NADP+

proof_lines: mutant T155G/A160T/L263P/Y303S, called PP3CT

substrate: NADH


proof_lines: mutant T155G/A160T/S223D/L263P/R264P/G265P, called AMP1PP5


organism: Plasmodium falciparum

substrate_name: NADPH

proof_lines: in an assay using K3Fe(CN)6 as electron acceptor for mutant H286K

proof_lines: in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286K

substrate: NADPH


proof_lines: in an assay using K3Fe(CN)6 as electron acceptor for mutant H286L


organism: Rhodobacter capsulatus

assay_conditions_summary: pH 8; cofactor NADPH

proof_lines:
diaphorase activity, pH 8.0
pH 8.0


enzyme_display_name: pyranose oxidase

organism: Lyophyllum shimeji

substrate_name: L-sorbose

proof_lines: using D-glucose as cosubstrate, at 30°C, pH 6.5

enzyme: pyranose oxidase

substrate: L-sorbose


organism: Peniophora sp.

substrate_name: D-glucose

substrate: D-glucose


organism: Phanerodontia chrysosporium

substrate_name: ferricyanide

proof_lines: substrate ferricyanide (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2-azinobis(3-ethylbenzthiazolinesulfo

proof_lines: substrate 2-chloro-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2-azinobis(3-ethylbenzth

proof_lines: substrate 2-methyl-1,4-benzoquinone (constant D-glucose concentration, 20 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2-azinobis(3-ethylbenzth

substrate: ferricyanide


organism: Phlebiopsis gigantea

proof_lines: pH 7.3, 22°C, mutant enzyme E540K with a C-terminal His6-tag


proof_lines: pH 7.3, 22°C, recombinant wild-type enzyme


substrate_name: D-allose

proof_lines: pH 7.3, 22°C, mutant enzyme K312E with a C-terminal His6-tag

substrate: D-allose


organism: Trametes ochracea

substrate_name: ferricenium ion

proof_lines: E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: E542R mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

substrate: ferricenium ion


proof_lines: L537G/E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 3

proof_lines: L537G/E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,

proof_lines: L537G/E542R mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5


assay_conditions_summary: pH 6.5; 303.15 K; buffer 50 mM phosphate

proof_lines: E542K mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: E542K mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: mutant enzyme E542K, in 50 mM phosphate buffer (pH 6.5) at 60°C


assay_conditions_summary: pH 6.5; 303.15 K; cofactor FAD

proof_lines: L537W/E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,

proof_lines: L537W/E542R mutant, substrate 1,4-benzoquinone (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5

proof_lines: L537W/E542R mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,


proof_lines: L537G/E542K mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537G/E542K mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,

proof_lines: L537G/E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,


proof_lines: L537G mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537G mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537G mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C


substrate_name: D-galactose

proof_lines: L537W mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537W mutant, substrate D-glucose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537W mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

substrate: D-galactose


proof_lines: L537W/E542K mutant, substrate 1,4-benzoquinone (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5,

proof_lines: L537W/E542K mutant, substrate D-galactose (O2 concentration constant), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

proof_lines: L537W/E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 3


assay_conditions_summary: pH 6.5; 323.15 K; cofactor FAD

proof_lines: T169G/E542K/V546C, mutant, 50°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2-azinobis(3-ethylbenzthiazolinesulfonic acid) assay

proof_lines: T169G/E542K/V546C, mutant, 50°C, substrate D-galactose (1,4-benzoquinone saturated), pH 6.5, standard 2,2-azinobis(3-ethylbenzthiazolinesulfonic acid) assay

proof_lines: T169G/E542K/V546C, mutant, 50°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2-azinobis(3-ethylbenzthiazolinesulfonic acid) assay


assay_conditions_summary: cofactor FAD

proof_lines: R472L, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: R472L, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: Q448N, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: Q448N, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: V546P/T169G, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: V546P/T169G, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: T169S, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: T169S, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: V546C/T169N, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: V546C/T169N, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: Q448S, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: Q448S, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: T169N, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: T169N, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: H548R, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: H548R, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: H548I, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: H548I, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


assay_conditions_summary: pH 6.5; 333.15 K; buffer 50 mM phosphate; cofactor FAD

proof_lines: V546C, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: mutant enzyme V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C

proof_lines: mutant enzyme V546C, pH and temperature not specified in the publication


proof_lines: R472G, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: R472G, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: V546G/T169G, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: V546G/T169G, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: Q448C, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: Q448C, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: V546P, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: V546P, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: V546G, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: V546G, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: N593R, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: N593R, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: mutant enzyme H450G/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C

proof_lines: mutant enzyme H450G/V546C, pH and temperature not specified in the publication


proof_lines: mutant enzyme H450G, in 50 mM phosphate buffer (pH 6.5) at 60°C

proof_lines: mutant enzyme H450G, pH and temperature not specified in the publication


assay_conditions_summary: pH 6.5; 333.15 K; buffer 50 mM phosphate

proof_lines: mutant enzyme H450G/E542K/V546C, in 50 mM phosphate buffer (pH 6.5) at 60°C


assay_conditions_summary: pH 6.5; 303.15 K; buffer 50 mM KH2PO4

proof_lines: wild type enzyme, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: wild-type, mutant, 30°C, substrate D-glucose (O2 saturated), pH 6.5, standard 2,2-azinobis(3-ethylbenzthiazolinesulfonic acid) assay

proof_lines: wild-type, mutant, 30°C, substrate D-galactose (O2 saturated), pH 6.5, standard 2,2-azinobis(3-ethylbenzthiazolinesulfonic acid) assay


proof_lines: mutant enzyme F454A/S455A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454A/S455A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454A/S455A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


proof_lines: mutant enzyme F454A/Y456A, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454A/Y456A, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454A/Y456A, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


proof_lines: mutant enzyme F454N, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454N, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454N, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


substrate_name: D-melibiose

proof_lines: mutant enzyme H450Q, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme H450Q, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme H450Q, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

substrate: D-melibiose


proof_lines: mutant enzyme Y456W, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme Y456W, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme Y456W, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


proof_lines: mutant enzyme F454P, using O2 as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454P, using D-galactose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C

proof_lines: mutant enzyme F454P, using D-glucose as cosubstrate, in 50 mM KH2PO4 buffer (pH 6.5), at 30°C


proof_lines: mutant enzyme T196G/V546C, pH and temperature not specified in the publication


proof_lines: mutant enzyme T169G, pH and temperature not specified in the publication

proof_lines: T169G, mutant, substrate D-galactose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay

proof_lines: T169G, mutant, substrate D-glucose, 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)-peroxidase assay


proof_lines: mutant enzyme H167A, pH and temperature not specified in the publication


proof_lines: mutant enzyme Q448H, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme Q448H, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme Q448H, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C


proof_lines: mutant T155G/A160T/L263P/R264P/G265P, called PP5


proof_lines: mutant T155G/A160T/S223D/Y235F/L263P/R264P/G265P, called AMP2PP5


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

proof_lines: with 2,6-dichlorophenolindophenol as cosubstrate, at pH 7.0 and 25°C


organism: Bacillus subtilis

substrate_name: oxidized [2Fe-2S]-[rubredoxin]

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

substrate: oxidized [2Fe-2S]-[rubredoxin]


organism: Chlorobaculum tepidum

proof_lines:
cosubstrate NADH, pH 7, 25°C
pH 7, 25°C
cosubstrate NADPH, pH 7, 25°C


organism: Escherichia coli

substrate_name: Fe(III)-EDTA

proof_lines: in the presence of 0.15 mM Fe(III)-EDTA, in the absence of free flavin, in 50 mM sodium phosphate (pH 7.0), at 25°C

proof_lines: in the presence of 0.15 mM Fe(III)-EDTA, in the presence of 0.15 mM FAD, in 50 mM sodium phosphate (pH 7.0), at 25°C

substrate: Fe(III)-EDTA


substrate_name: oxidized ferredoxin

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

substrate: oxidized ferredoxin


organism: Lathyrus oleraceus

proof_lines: mutant lacking the beta-hairpin, pH 8.0, 30°C

proof_lines: mutant with additional tryptophan residue at the C-terminus, pH 8.0, 30°C


proof_lines: in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286Q

proof_lines: in an assay using K3Fe(CN)6 as electron acceptor for mutant H286Q


proof_lines: in an assay using K3Fe(CN)6 as electron acceptor for mutant H286A

proof_lines: in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286A


assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+

proof_lines: in an assay using 2,6-dichlorophenolindophenol as electron acceptor

proof_lines: using 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloride as electron acceptor

proof_lines: in an assay using K3Fe(CN)6 as electron acceptor


proof_lines: recombinant mutant S261M, pH not specified in the publication, 30°C


proof_lines: mutant I305M/T213V, pH and temperature not specified in the publication


proof_lines: mutant I305M/S261M, pH and temperature not specified in the publication


proof_lines: mutant C155Y/Y184H/V275I/C281Y, pH and temperature not specified in the publication


proof_lines: mutant I305L, pH and temperature not specified in the publication


enzyme_display_name: cathepsin B

organism: Homo sapiens

proof_lines: pH 6.0, 25°C, mutant H110A in presence of heparin

enzyme: cathepsin B


proof_lines: pH 6.0, 25°C, mutant H111A in presence of heparin


assay_conditions_summary: pH 6; 298.15 K; buffer 0.4 M sodium potassium phosphate

proof_lines: pH 6.0, 25°C, wild-type enzyme in presence of heparin

proof_lines: wild type enzyme, in 0.4 M sodium potassium phosphate buffer (pH 6.0) containing 8 mM dithiothreitol and 4 mM EDTA, at 37°C


proof_lines: recombinant mutant S261A, pH not specified in the publication, 30°C


proof_lines: recombinant mutant Y184A, pH not specified in the publication, 30°C


proof_lines: recombinant mutant Q126M, pH not specified in the publication, 30°C


proof_lines: recombinant mutant T213V, pH not specified in the publication, 30°C


organism: Hapsidospora chrysogena


proof_lines: wild-type enzyme, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: isocitrate dehydrogenase (NAD(+))

organism: Xylella fastidiosa

substrate_name: NADP+

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

enzyme: isocitrate dehydrogenase (NAD(+))

substrate: NADP+


substrate_name: NAD+

proof_lines: mutant enzymeD268K/I269Y/A275V, at pH 8.0 and 25°C

substrate: NAD+


proof_lines: mutant enzyme D268K/I269Y, at pH 8.0 and 25°C


organism: Streptomyces clavuligerus

substrate_name: penicillin G

proof_lines: mutant I305M, pH and temperature not specified in the publication

substrate: penicillin G


proof_lines: mutant I305M/T213V/S261M, pH and temperature not specified in the publication


proof_lines: mutantI305M/T213V/M73T, pH and temperature not specified in the publication


substrate_name: Penicillin N

proof_lines: pH 6.5, 30°C, recombinant mutant V275I/I305M

proof_lines: pH 6.5, 30°C, recombinant mutants V275I and I305M

substrate: Penicillin N


proof_lines: pH 6.5, 30°C, recombinant mutants G79E and I305M


proof_lines: pH 6.5, 30°C, recombinant wild-type enzyme

proof_lines: wild-type enzyme, pH and temperature not specified in the publication

proof_lines: recombinant wild-type enzyme, pH not specified in the publication, 30°C


proof_lines: 30°C, double mutant with truncation at residue 310 and M306I


proof_lines: 30°C, triple mutant with truncation at residue 310, M306I and N305L


proof_lines: mutant R308I, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant R308L, pH not specified in the publication, temperature not specified in the publication


substrate_name: NAD+; Isocitrate

substrate: NAD+; Isocitrate


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NAD+


organism: Campylobacter curvus

assay_conditions_summary: 298.15 K; cofactor NADP+


organism: Campylobacter sp.

proof_lines: pH 75, 25°C, recombinant His6-tagged enzyme


assay_conditions_summary: 298.15 K; cofactor NAD+


proof_lines: pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R


organism: Congregibacter litoralis

assay_conditions_summary: pH 7.5; 308.15 K; cofactor NAD+


assay_conditions_summary: pH 7.5; 308.15 K; cofactor NADP+


proof_lines: mutant D487R/L488H, with Mn2+, pH 7.5, 35°C


proof_lines: wild-type enzyme, with Mg2+, pH 7.5, 35°C

proof_lines: wild-type enzyme, with Mn2+, pH 7.5, 35°C


enzyme_display_name: laccase

organism: Geobacter metallireducens

enzyme: laccase


organism: Lentinus brumalis

assay_conditions_summary: pH 4; 303.15 K; buffer McIlvaine

proof_lines:
in McIlvaine buffer (pH 4.0), at 30°C
in McIlvaine buffer (pH 5.0), at 30°C


organism: Panus rudis


enzyme_display_name: peroxidase

organism: Amycolatopsis sp.

substrate_name: H2O2; 2,4-Dichlorophenol

enzyme: peroxidase

substrate: H2O2; 2,4-Dichlorophenol


organism: Armoracia rusticana


substrate_name: 2-Chloro-4-methoxyphenol; H2O2

substrate: 2-Chloro-4-methoxyphenol; H2O2


substrate_name: L-Dopa; H2O2

substrate: L-Dopa; H2O2


organism: Bacillus altitudinis

substrate_name: H2O2; Sinapate

substrate: H2O2; Sinapate


enzyme_display_name: phenylalanine 4-monooxygenase

assay_conditions_summary: pH 7; 298.15 K; buffer 100 mM Na-HEPES

proof_lines: mutant enzyme R155H, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C

enzyme: phenylalanine 4-monooxygenase


proof_lines: mutant enzyme D143G, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


substrate_name: L-phenylalanine

assay_conditions_summary: pH 6.8; 310.15 K; buffer 50 mM potassium phosphate

proof_lines: mutant enzyme R68S, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme R68S, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme R68S, using S-carboxymethyl-L-cysteine as cosubstrate

substrate: L-phenylalanine


proof_lines: mutant enzyme V388M, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme V388M, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme V388M, using S-carboxymethyl-L-cysteine as cosubstrate


proof_lines: mutant enzyme I65T, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme I65T, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme I65T, using S-carboxymethyl-L-cysteine as cosubstrate


proof_lines: mutant enzyme R261Q, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme R261Q, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme R261Q, using S-carboxymethyl-L-cysteine as cosubstrate


proof_lines: mutant enzyme Y414C, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C

proof_lines: mutant enzyme Y414C, using L-phenylalanine as cosubstrate

proof_lines: mutant enzyme Y414C, using S-carboxymethyl-L-cysteine as cosubstrate


substrate_name: tetrahydrobiopterin

substrate: tetrahydrobiopterin


organism: Rattus norvegicus

source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org); CC BY-NC-ND 4.0


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


organism: Trametes ochracea

substrate_name: D-glucose

substrate: D-glucose


organism: Cephalosporium acremonium

substrate_name: Penicillin G; 2-Oxoglutarate; O2

substrate: Penicillin G; 2-Oxoglutarate; O2


proof_lines: pH 7.5, 30°C, recombinant wild-type enzyme


proof_lines: pH 7.5, 30°C, recombinant mutant DELTA310/N305L/M306I


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: Penicillin N; 2-Oxoglutarate; O2

substrate: Penicillin N; 2-Oxoglutarate; O2


proof_lines: mutant enzyme DELTAI305-310, DELTAR306-310 and mutant DELTAR307-310


organism: Bos taurus


organism: Burkholderia pseudomallei


organism: Cucumis sativus

substrate_name: H2O2; 4-Methoxy-alpha-naphthol

substrate: H2O2; 4-Methoxy-alpha-naphthol


organism: Euphorbia characias


organism: Caenorhabditis elegans


organism: Dictyostelium discoideum


organism: Homo sapiens


proof_lines: pH 7.0, 25°C, recombinant enzyme, versus (6R)-tetrahydrobiopterin


proof_lines: mutant enzyme R408W, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


proof_lines: mutant enzyme L348V, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


proof_lines: mutant enzyme P416Q, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C


proof_lines: wild type enzyme, in 100 mM Na-HEPES buffer, pH 7.0, at 25°C

proof_lines: wild type enzyme, in 50 mM potassium phosphate buffer, pH 6.8, at 37°C

proof_lines: wild type enzyme, in 50 mM potassium phosphate buffer (pH 6.8), at 37°C


proof_lines: V546C/T169G/L537W mutant, substrate D-glucose (constant O2 concentration), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2-azinobis(3-ethylbenzthiazo

proof_lines: V546C/T169G/L537W mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled ass

proof_lines: mutant enzyme V546C/T169G/L537W, at pH 6.5 and 30°C


proof_lines: V546C/E542K mutant, substrate 1,4-benzoquinone (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using 2,2-azinobis(3

proof_lines: V546C/E542K mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay usi

proof_lines: mutant enzyme V546C/E542K, at pH 6.5 and 30°C


substrate_name: ferricenium hexafluorophosphate

proof_lines: V546C/T169G mutant, substrate ferricenium hexafluorophosphate (constant D-galactose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay usi

proof_lines: mutant enzyme V546C/T169G, at pH 6.5 and 30°C

proof_lines: V546C/T169G mutant, substrate ferricenium hexafluorophosphate (constant D-glucose concentration, 100 mM), activity determined spectrophotometrically at 420 nm by measuring formation of H2O2 with a horse-radish peroxidase-coupled assay using

substrate: ferricenium hexafluorophosphate


organism: Saccharomyces cerevisiae

substrate_name: D-isocitrate

assay_conditions_summary: pH 7.4; 297.15 K; cofactor NAD+

proof_lines: octameric enzyme IDH1G15D/IDH2 with AMP, without DTT, pH 7.4, 24°C

proof_lines: octameric enzyme IDH1G15D/IDH2 with AMP and DTT, pH 7.4, 24°C

proof_lines: octameric enzyme IDH1G15D/IDH2 without AMP, with DTT, pH 7.4, 24°C

substrate: D-isocitrate


substrate_name: NAD+

assay_conditions_summary: pH 7.2; cofactor NAD+

proof_lines: pH 7.2, alpha-subunit mutant enzyme D181N

substrate: NAD+


proof_lines: pH 7.2, gamma-subunit mutant enzyme D190N


proof_lines: pH 7.2, beta-subunit mutant enzyme D192N


substrate_name: D-galactose

proof_lines: pH 7.0, 25°C, reductive half-reaction, mutant T169S

proof_lines: mutant enzyme T169S, in 50 mM sodium phosphate (pH 7.0), at 25°C

proof_lines: mutant enzyme T169S, in 50 mM sodium phosphate (pH 7.0), at 4°C

substrate: D-galactose


proof_lines: pH 7.0, 25°C, reductive half-reaction, mutant T169N

proof_lines: mutant enzyme T169N, in 50 mM sodium phosphate (pH 7.0), at 4°C

proof_lines: mutant enzyme T169N, using D-glucose as cosubstrate, in 50 mM sodium phosphate (pH 7.0), at 4°C


proof_lines: pH 7.0, 25°C, reductive half-reaction, mutant T169G

proof_lines: mutant enzyme T169G, in 50 mM sodium phosphate (pH 7.0), at 25°C

proof_lines: mutant enzyme T169G, in 50 mM sodium phosphate (pH 7.0), at 4°C


proof_lines: pH 7.0, 25°C, reductive half-reaction, wild-type enzyme

proof_lines: wild type enzyme F454Y, at pH 6.5 and 30°C

proof_lines: wild type enzyme, in 50 mM sodium phosphate (pH 7.0), at 4°C


organism: Ostreococcus tauri

assay_conditions_summary: pH 7.6; cofactor NADP+

proof_lines: pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mg2+

proof_lines: pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mn2+


substrate_name: NADP+

proof_lines: pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R/M345H, with Mn2+

substrate: NADP+


proof_lines: pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R, with Mn2+


organism: Campylobacter concisus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

proof_lines: mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C


substrate_name: NAD+; Isocitrate

assay_conditions_summary: cofactor NAD+

substrate: NAD+; Isocitrate


enzyme_display_name: vanillyl-alcohol oxidase

organism: Penicillium simplicissimum

enzyme: vanillyl-alcohol oxidase


proof_lines:
pH 7.5, 25°C, mutant enzyme E502G
pH 10, 25°C, mutant enzyme E502G
pH 8, 25°C, mutant enzyme E502G


substrate_name: creosol

proof_lines:
pH 10, 25°C, mutant enzyme I237T/M437L
pH 8, 25°C, mutant enzyme I237T/M437L

substrate: creosol


substrate_name: Eugenol

substrate: Eugenol


substrate_name: O2; Vanillyl alcohol

substrate: O2; Vanillyl alcohol


substrate_name: eugenol

proof_lines:
pH 7.5, 25°C, mutant enzyme F454Y
pH 8, 25°C, mutant enzyme F454Y
pH 10, 25°C, mutant enzyme F454Y

substrate: eugenol


proof_lines:
pH 10, 25°C, mutant enzyme T505S
pH 7.5, 25°C, mutant enzyme T505S
pH 8, 25°C, mutant enzyme T505S


organism: Rhodomicrobium vannielii

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+


organism: Streptococcus suis

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+


organism: Sus scrofa


proof_lines: mutant enzyme L545C, with O2 as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme L545C, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme L545C, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C


proof_lines: mutant enzyme T166R, with O2 as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme T166R, with ferrocenium ion as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme T166R, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C


proof_lines: mutant enzyme L547R, with O2 as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme L547R, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme L547R, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C


proof_lines: mutant enzyme N593C, with 1 ferrocenium ion as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme N593C, with 1,4-benzoquinone as electron acceptor, at pH 6.5 and 30°C

proof_lines: mutant enzyme N593C, with 2,6-dichlorophenolindophenol as electron acceptor, at pH 6.5 and 30°C


assay_conditions_summary: pH 10.5; buffer the publication 100 mM ethanolamine

proof_lines: pH and temperature not specified in the publication

proof_lines: recombinant protein with a hexa-histidine tag, 0.1 M ethanolamine buffer at pH 10.5


organism: Trametes sp.


organism: Hydrogenobacter thermophilus

assay_conditions_summary: pH 7.5; 343.15 K; cofactor NADP+


assay_conditions_summary: cofactor NADP+


organism: Micromonas commoda

assay_conditions_summary: 298.15 K; cofactor NADP+


proof_lines: pH 75, 25°C, recombinant His6-tagged enzyme


organism: Ostreococcus sp. 'lucimarinus'


proof_lines: pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H


organism: Phycomyces blakesleeanus

source_protein_accession: complex


organism: Methylovorus sp. MP688

substrate_name: Vanillyl alcohol

substrate: Vanillyl alcohol


assay_conditions_summary: pH 7.5; 298.15 K; cofactor FAD


organism: Acidithiobacillus thiooxidans

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

proof_lines:
pH 9.0, 30°C, native enzyme
Raw SKiD Env: Temp=30°C, pH=9


organism: Bifidobacterium longum

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


organism: Bos taurus


organism: Campylobacter curvus


organism: Homo sapiens


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NAD+


substrate_name: chavicol

substrate: chavicol


enzyme_display_name: phenylalanine dehydrogenase

organism: Bacillus badius

substrate_name: L-tyrosine

enzyme: phenylalanine dehydrogenase

substrate: L-tyrosine


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


substrate_name: NAD+; H2O; L-Phenylalanine

substrate: NAD+; H2O; L-Phenylalanine


organism: Lysinibacillus sphaericus

substrate_name: L-Norleucine

substrate: L-Norleucine


substrate_name: phenylpyruvate

substrate: phenylpyruvate


smiles: CCC(C)C(=O)C(=O)O


organism: Pyrococcus furiosus

assay_conditions_summary: pH 8; 343.15 K; cofactor NADP+

proof_lines: pH 8.0, 70°C, the Km-value for NADP+ is about 65fold higher than the KM-value for NAD+


organism: Rattus norvegicus

substrate_name: D-threo-Isocitrate; NAD+

substrate: D-threo-Isocitrate; NAD+


substrate_name: L-Methionine

substrate: L-Methionine


substrate_name: L-Leucine

substrate: L-Leucine


substrate_name: L-Isoleucine

substrate: L-Isoleucine


smiles: CSCCC(=O)C(=O)O


substrate_name: L-Tyrosine

substrate: L-Tyrosine


substrate_name: alpha-Ketovaline

smiles: CC(C)C(=O)C(=O)O

substrate: alpha-Ketovaline


substrate_name: L-Norvaline

sequence_source: UniProt P23307 direct lookup: canonical sequence exists; not row-specific mutant proof.

substrate: L-Norvaline


substrate_name: L-Valine

sequence_source: UniProt P23307 direct lookup: canonical sequence exists; accession context only.

substrate: L-Valine


organism: Penicillium simplicissimum

substrate_name: creosol

proof_lines:
pH 10, 25°C, mutant enzyme I238T
pH 7.5, 25°C, mutant enzyme I238T
pH 8, 25°C, mutant enzyme I238T

substrate: creosol


proof_lines:
pH 7.5, 25°C, wild-type enzyme
pH 10, 25°C, wild-type enzyme
wild-type, pH 7.5, 25°C


proof_lines: pH 10, 25°C, mutant enzyme F93Y/P189S/I238T


substrate_name: Eugenol

substrate: Eugenol


proof_lines:
pH 8, 25°C, mutant enzyme A429V
pH 10, 25°C, mutant enzyme A429V


assay_conditions_summary: pH 8.6; 298.15 K; cofactor NADH


assay_conditions_summary: pH 10.4; 298.15 K; cofactor NADH


smiles: CCCCC(=O)C(=O)O


proof_lines: His-tagged recombinant enzyme, pH 7.5, 25°C


organism: Rhodococcus jostii

proof_lines:
pH 7.5, 25°C
Raw SKiD Env: Temp=25°C, pH=7.5


substrate_name: Vanillyl alcohol

substrate: Vanillyl alcohol


substrate_name: vanillylamine

substrate: vanillylamine


assay_conditions_summary: pH 10.4; 298.15 K; cofactor NAD+


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


organism: Escherichia coli

substrate_name: But-2-enoyl-[acyl-carrier protein]

smiles: CC=CC(=O)S

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH

substrate: But-2-enoyl-[acyl-carrier protein]


substrate_name: crotonoyl-CoA

substrate: crotonoyl-CoA


organism: Haemophilus influenzae

substrate_name: NADH; H+; But-2-enoyl-[acyl-carrier protein]

assay_conditions_summary: cofactor NADH


organism: Mycobacterium tuberculosis

substrate_name: NADH

assay_conditions_summary: pH 6.8; 298.15 K; cofactor NADH

proof_lines:
pH 6.8, 25°C, mutant enzyme I21V
I21V mutant enoyl-ACP reductase

substrate: NADH


proof_lines:
pH 6.8, 25°C, mutant enzyme Y158F
mutant Y158F, pH 6.8, 30°C
mutant enzyme Y158F, pH 6.8, 25°C


assay_conditions_summary: pH 6.8; 298.15 K; cofactor CoA


enzyme_display_name: shikimate dehydrogenase (NADP+)

organism: Arabidopsis thaliana

substrate_name: NADP+

assay_conditions_summary: pH 8.8; 295.15 K; cofactor NADP+

enzyme: shikimate dehydrogenase (NADP+)

substrate: NADP+


substrate_name: shikimate

assay_conditions_summary: pH 8.8; 295.15 K; cofactor NADPH

substrate: shikimate


organism: Burkholderia pseudomallei


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


organism: Candidatus Liberibacter asiaticus

assay_conditions_summary: pH 7.5; 301.15 K; cofactor NADH

proof_lines: with respect to NADH, at pH 7.5 and 28°C

proof_lines: with respect to crotonyl-CoA, at pH 7.5 and 28°C


organism: Eimeria tenella

assay_conditions_summary: pH 7.2; buffer 0.1 mM Tris-HCl; cofactor NADH

proof_lines: recombinant enzyme, in the absence of enoyl-CoA as scosubstrate, in 0.1 mM Tris-HCl buffer (pH 7.2)


assay_conditions_summary: pH 8; 298.15 K; cofactor NADH


proof_lines:
25°C, pH 8.0
pH 7.5, 22°C
Raw SKiD Env: Temp=25°C, pH=8


organism: Corynebacterium glutamicum

assay_conditions_summary: pH 8.6; 303.15 K; cofactor NADP+

proof_lines:
with NADPH, pH 8.6, 30°C
with NADP+, pH 9.0, 30°C
pH 7.0, 30°C


substrate_name: NADP+; Shikimate

assay_conditions_summary: pH 7.5; 298.15 K; buffer notes; cofactor NADP+

proof_lines: 25°potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH

substrate: NADP+; Shikimate


assay_conditions_summary: pH 9; 293.15 K; cofactor NADP+


assay_conditions_summary: pH 9; 298.15 K; cofactor NADPH


assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+

proof_lines: pH 9.0, 25°C, recombinant wild-type enzyme


substrate_name: NAD+

proof_lines: pH 9.0, 25°C, recombinant mutant S131A/L135A/N149D/V152F

substrate: NAD+


proof_lines: pH 9.0, 25°C, recombinant mutant N149D/V152F


proof_lines: pH 9.0, 25°C, recombinant mutant S131A/N149D/V152F


organism: Eucalyptus camaldulensis


assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

proof_lines: pH 9.0, temperature not specified in the publication

proof_lines: pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation

proof_lines: pH 6.5, temperature not specified in the publication


substrate_name: NADPH

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH

substrate: NADPH


enzyme_display_name: uronate dehydrogenase

organism: Chromohalobacter israelensis

substrate_name: beta-D-galacturonate

enzyme: uronate dehydrogenase

substrate: beta-D-galacturonate


substrate_name: beta-D-glucuronate

proof_lines: mutant enzyme N99K/L100H/K102V/P103K/I105V, at pH 8.0 and 25°C

substrate: beta-D-glucuronate


proof_lines: mutant enzyme T113V/M175I/D246N, at pH 8.0 and 25°C


proof_lines: mutant enzyme T113V/A172V/D246N, at pH 8.0 and 25°C


organism: Chromohalobacter salexigens


organism: Pseudomonas putida KT2440

substrate_name: D-glucuronate

assay_conditions_summary: cofactor NAD+

substrate: D-glucuronate


organism: Pseudomonas syringae pv. tomato

substrate_name: D-Mannuronate

assay_conditions_summary: pH 8; 298.15 K; buffer recombinant His-tagged enzyme; cofactor NAD+

proof_lines: recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer

proof_lines: recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer

substrate: D-Mannuronate


organism: Thermobispora bispora

substrate_name: D-glucuronic acid from a beechwood xylan

assay_conditions_summary: pH 7; 333.15 K; cofactor NAD+


organism: Aquifex aeolicus

proof_lines:
25°C, pH 9.0
with shikimate, pH 9.0, 25°C
with NADP+, pH 9.0, 25°C


proof_lines:
pH 8.8, 22°C, with shikimate
pH 8.8, 22°C, with NADP+
Raw SKiD Env: Temp=-----, pH=-----


proof_lines: pH and temperature not specified in the publication, mutant S338G/T381G


substrate_name: L-quinate

proof_lines: pH and temperature not specified in the publication, mutant T381S

substrate: L-quinate


proof_lines: pH and temperature not specified in the publication, mutant T381A


proof_lines: pH and temperature not specified in the publication, mutant T381G


proof_lines: pH and temperature not specified in the publication, mutant S338G


proof_lines: pH and temperature not specified in the publication, wild-type enzyme


organism: Agrobacterium tumefaciens

assay_conditions_summary: buffer separate potassium phosphate and Tris; cofactor NAD+


proof_lines: mutant enzyme L158A/N159C/I160V, at pH 8.0 and 25°C


proof_lines: mutant enzyme T113V/A172V/M175I, at pH 8.0 and 25°C


proof_lines: mutant enzyme T113V/A172V/M175I/D236N, at pH 8.0 and 25°C


organism: Pseudomonas putida

assay_conditions_summary: pH 8.8; cofactor NADP+

proof_lines:
pH 8.8, presence of 2 mM quinate
pH 8.8, presence of 2 mM NAD+
pH 8.8, presence of 2 mM shikimate


proof_lines:
pH 8.8, presence of 2 mM NAD+
pH 8.8, presence of 2 mM shikimate
pH 8.8, presence of 2 mM NADP+


assay_conditions_summary: pH 8.8; 298.15 K; cofactor NADP+

proof_lines:
pH 8.8, 25°C, with shikimate
pH 8.8, 25°C, with NADP+
pH 8.8, presence of 2 mM NADP+


assay_conditions_summary: cofactor NADP+

proof_lines:
in the presence of 2 mM NAD+
in the presence of shikimate
in the presence of 2 mM NADP+


proof_lines:
in the presence of 2 mM NADP+
in the presence of shikimate
in the presence of 2 mM NAD+


organism: Staphylococcus epidermidis

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

proof_lines:
pH 7.0, 25°C, with NADP+
pH 7.0, 25°C, with shikimate


organism: Staphylococcus epidermidis RP62A


organism: Toxoplasma gondii

proof_lines:
pH 8.8, 25°C, with NADP+
pH 8.8, 25°C, with shikimate


organism: Vitis vinifera


organism: Archaeoglobus fulgidus

assay_conditions_summary: pH 7.3; 360.15 K; cofactor NADP+

proof_lines:
with shikimate, pH 7.3, 87°C
with NADP+, pH 7.3, 87°C


organism: Aspergillus nidulans

substrate_name: NADPH; 3-Dehydroshikimate; H+

proof_lines:
with NADP+, pH 7.0, 25°C
with shikimate, pH 7.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7

substrate: NADPH; 3-Dehydroshikimate; H+


organism: Camellia sinensis

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADP+

proof_lines: pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with shikimate

proof_lines: pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with 3-dehydroshikimate

proof_lines: pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADP+


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH


organism: Corynebacterium glutamicum

assay_conditions_summary: pH 10; 303.15 K; cofactor NADP+


assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+


proof_lines: pH 7.0, 30°C, recombinant isozyme VvSDH3

proof_lines: pH 9.0, 30°C, recombinant isozyme VvSDH3


proof_lines: pH 9.0, 30°C, recombinant isozyme VvSDH4

proof_lines: pH 7.0, 30°C, recombinant isozyme VvSDH4


proof_lines: pH 7.0, 30°C, recombinant isozyme VvSDH1

proof_lines: pH 9.0, 30°C, recombinant isozyme VvSDH1


organism: Alistipes finegoldii

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

proof_lines: K0.5 value, Hill coefficient 2.4, pH 8, 30°C

proof_lines: K0.5 value, Hill coefficient 1.5, pH 8, 30°C


organism: Arabidopsis thaliana

substrate_name: NADH; H+; Crotonoyl-CoA

substrate: NADH; H+; Crotonoyl-CoA


organism: Bacillus subtilis

assay_conditions_summary: cofactor NADPH


organism: Burkholderia mallei

assay_conditions_summary: pH 7.9; 298.15 K; cofactor NADH


organism: Eucalyptus camaldulensis

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

proof_lines: pH 9.0, temperature not specified in the publication

proof_lines: pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation


assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADP+

proof_lines: pH 8.5, temperature not specified in the publication


organism: Haemophilus influenzae

assay_conditions_summary: pH 7.5; cofactor NADP+


assay_conditions_summary: pH 8.8; 303.15 K; cofactor NADP+


organism: Helicobacter pylori

assay_conditions_summary: pH 8; 333.15 K; cofactor NADP+


organism: Mycobacterium tuberculosis

proof_lines:
pH 7.0, 25°C, recombinant AroE
25°C, pH 7.3


assay_conditions_summary: pH 7.3; 298.15 K; cofactor NADPH


assay_conditions_summary: pH 6.8; 303.15 K; cofactor NADH

proof_lines:
wild-type, pH 6.8, 30°C
pH 7.5, 25°C, wild-type enzyme
pH 6.8, 25°C, wild-type enzyme


organism: Mycolicibacterium smegmatis

assay_conditions_summary: pH 6.8; 298.15 K; cofactor NADH


proof_lines:
pH 6.8, 25°C, mutant enzyme M161V
mutant enzyme M161V, pH 6.8, 25°C


organism: Plasmodium falciparum

substrate_name: H+; NADH; Crotonoyl-CoA

substrate: H+; NADH; Crotonoyl-CoA


substrate_name: Unknown

substrate: Unknown


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH

proof_lines:
25°C, pH 7.4
Raw SKiD Env: Temp=25°C, pH=7.4


substrate_name: 2-trans-Dodecenoyl-CoA; NADH; H+

assay_conditions_summary: cofactor NADH

substrate: 2-trans-Dodecenoyl-CoA; NADH; H+


substrate_name: NADH

proof_lines: I16T mutantwild type enoyl-ACP reductase

substrate: NADH


assay_conditions_summary: pH 6.8; cofactor NADH

proof_lines: pH 6.8, temperature not specified in the publication


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


substrate_name: octenoyl-CoA

substrate: octenoyl-CoA


substrate_name: crotonoyl-CoA

substrate: crotonoyl-CoA


organism: Lysinibacillus sphaericus

substrate_name: L-Isoleucine

substrate: L-Isoleucine


substrate_name: L-Methionine

substrate: L-Methionine


substrate_name: L-Norleucine

substrate: L-Norleucine


substrate_name: NAD+; H2O; L-Phenylalanine

assay_conditions_summary: cofactor NAD+

substrate: NAD+; H2O; L-Phenylalanine


substrate_name: L-Norvaline

substrate: L-Norvaline


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


substrate_name: phenylpyruvate

substrate: phenylpyruvate


organism: Pseudobacillus badius

substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: L-tyrosine

substrate: L-tyrosine


organism: Rhodococcus sp.

substrate_name: phenylacetone

substrate: phenylacetone


organism: Yersinia pestis


substrate_name: L-Valine

assay_conditions_summary: pH 10.4; 298.15 K; cofactor NADH

substrate: L-Valine