sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9FK25 and applied mutation signature C296F/Q310L/V314T to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic analysis of AtCOMT WT and mutants towards NAS; row Table 2 row C296F-Q310L-V314T; columns Km (mM), kcat (s^-1), kcat/Km (10^3 s^-1 M^-1).


enzyme_display_name: caffeate O-methyltransferase

organism: Arabidopsis thaliana

substrate_name: N-acetylserotonin

source_db: oed

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q310L to reconstruct the assayed variant sequence.

mutation_type: substitution

data_origin: experimental

enzyme: caffeate O-methyltransferase

substrate: N-acetylserotonin

status: unverified

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V314T to reconstruct the assayed variant sequence.


mutation_signature: Unknown

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


enzyme_display_name: thymidylate synthase (FAD)

organism: Chlamydia trachomatis

verification_status: corrected

assay_conditions_summary: pH 7.2; 310.15 K; cofactor NADPH

raw_value_unit_evidence: Apparent Km for CH2H4folate = 22.66 +/- 2.02 uM; kcat = 39.98 +/- 1.77 min^-1; kcat/Km not separately printed

row_label: CH2H4folate / CH2-H4folate

table_label: Saturation Kinetics / Fig. 5

enzyme: thymidylate synthase (FAD)

status: corrected


substrate_name: dUMP

raw_value_unit_evidence: Apparent Km for dUMP = 5.99 +/- 0.54 uM; kcat = 39.98 +/- 1.77 min^-1; kcat/Km not separately printed

row_label: dUMP

substrate: dUMP


substrate_name: NADPH

raw_value_unit_evidence: Apparent Km for NADPH = 60.80 +/- 4.86 uM; kcat = 39.98 +/- 1.77 min^-1; kcat/Km not separately printed

row_label: NADPH

substrate: NADPH


organism: Ocimum basilicum

substrate_name: S-Adenosyl-L-methionine

verification_status: verified

column_label: Table 1 row COMT1 with Km for SAM column 64 uM and kcat column 1.3 x 10^-2 s^-1; exported substrate is SAM, so kcat/Km is derived from normalized kcat and SAM Km cells.

normalized_value_unit_evidence: kcat normalized value: 0.013; normalized unit: s^-1; km normalized value: 0.064; normalized unit: mM; kcat_over_km normalized value: 0.203125; normalized unit: s^-1 mM^-1

raw_value_unit_evidence: Table 1 COMT1 row: Km for SAM 64 uM; substrate Caffeic acid; kcat 1.3 x 10^-2 s^-1.

row_label: COMT1 / SAM Km column in Caffeic acid assay row

table_label: Table 1. Properties of Basil Phenylpropanoid OMTs

substrate: S-Adenosyl-L-methionine

status: verified


substrate_name: caffeic acid

column_label: Table 1 row COMT1 / Caffeic acid; columns Km for substrate (47 uM) and kcat (1.3 x 10^-2 s^-1); kcat/Km calculated from normalized kcat and Km cells.

normalized_value_unit_evidence: kcat normalized value: 0.013; normalized unit: s^-1; km normalized value: 0.047; normalized unit: mM; kcat_over_km normalized value: 0.2765957446808511; normalized unit: s^-1 mM^-1

raw_value_unit_evidence: Table 1 COMT1 / Caffeic acid: Km for substrate 47 uM; kcat 1.3 x 10^-2 s^-1; printed kcat/Km column 0.27.

row_label: COMT1 / Caffeic acid

substrate: caffeic acid


substrate_name: catechol

column_label: Table 1 row COMT1 / Catechol; exported value set does not exactly match the explicit table row/cell values preserved here.

normalized_value_unit_evidence: paper_kcat_s^-1: 0.0046; paper_km_mM: 0.29; paper_kcat_over_km_s^-1_mM^-1: 0.02

raw_value_unit_evidence: Export has kcat 0.005 and derived kcat/Km 0.01724137931034483, but Table 1 reports kcat 4.6 x 10^-3 and kcat/Km column 0.02 for COMT1 / Catechol.

row_label: COMT1 / Catechol

substrate: catechol


enzyme_display_name: tocopherol C-methyltransferase

substrate_name: delta-tocopherol

source_db: brenda

kcat_display: Not reported

kcat_over_km_display: Not reported

enzyme: tocopherol C-methyltransferase

substrate: delta-tocopherol

source: brenda


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


substrate_name: gamma-tocopherol

proof_lines:
Arabidopsis thaliana
gamma-tocopherol methyltransferase
substrate specificities

substrate: gamma-tocopherol


enzyme_display_name: tricin synthase

organism: Zea mays

substrate_name: tricetin

sequence_source: multiple

source_databases_merged: brenda uniprot

enzyme: tricin synthase

substrate: tricetin


enzyme_display_name: Caffeic acid 3-O-methyltransferase

substrate_name: luteolin

source_db: uniprot

enzyme: Caffeic acid 3-O-methyltransferase

substrate: luteolin

source: uniprot


organism: Coptis japonica

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


enzyme_display_name: cycloartenol 24-C-methyltransferase

organism: Glycine max

substrate_name: S-Adenosyl-L-methionine; Cycloartenol

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

enzyme: cycloartenol 24-C-methyltransferase

substrate: S-Adenosyl-L-methionine; Cycloartenol


enzyme_display_name: 24-methylenesterol C-methyltransferase

enzyme: 24-methylenesterol C-methyltransferase


enzyme_display_name: trans-aconitate 2-methyltransferase

organism: Escherichia coli

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

enzyme: trans-aconitate 2-methyltransferase


enzyme_display_name: trans-aconitate 3-methyltransferase

organism: Saccharomyces cerevisiae

enzyme: trans-aconitate 3-methyltransferase


enzyme_display_name: (iso)eugenol O-methyltransferase

organism: Clarkia breweri

substrate_name: Isoeugenol; S-Adenosyl-L-methionine

enzyme: (iso)eugenol O-methyltransferase

substrate: Isoeugenol; S-Adenosyl-L-methionine


enzyme_display_name: thioether S-methyltransferase

organism: Mus musculus

substrate_name: dimethyl selenide

smiles: C[Se]C

enzyme: thioether S-methyltransferase

substrate: dimethyl selenide


substrate_name: Dimethyl sulfide

smiles: CSC

substrate: Dimethyl sulfide


substrate_name: S-adenosylmethionine

substrate: S-adenosylmethionine


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: N-acetyl-S-farnesyl-L-cysteine (AFC)

substrate: N-acetyl-S-farnesyl-L-cysteine (AFC)


organism: Rattus norvegicus

substrate_name: N-acetyl-S-(E,E)-farnesyl-L-cysteine

substrate: N-acetyl-S-(E,E)-farnesyl-L-cysteine


substrate_name: N-acetyl-S-(E)-geranyl-L-cysteine

smiles: CC(=CCCC(=CCSCC(C(=O)O)NC(=O)C)C)C

substrate: N-acetyl-S-(E)-geranyl-L-cysteine


enzyme_display_name: macrocin O-methyltransferase

organism: Streptomyces fradiae

substrate_name: macrocin

enzyme: macrocin O-methyltransferase

substrate: macrocin


substrate_name: lactenocin

substrate: lactenocin


substrate_name: (R,S)-norlaudanosoline

column_label: Abstract reports Km values of 2.23 mM and 3.95 mM for (R,S)-norlaudanosoline and S-adenosyl-L-methionine, respectively.

raw_value_unit_evidence: Km raw_value=2.23 mM raw_unit=mM

row_label: Coptis norcoclaurine 6-O-methyltransferase / (R,S)-norlaudanosoline

table_label: PubMed XML abstract PMID 7925429

substrate: (R,S)-norlaudanosoline


raw_value_unit_evidence: Km raw_value=3.95 mM raw_unit=mM

row_label: Coptis norcoclaurine 6-O-methyltransferase / S-adenosyl-L-methionine


substrate_name: Cycloartenol

proof_lines:
cyclobranol 8A
cycloartenol
soybean SMT1

substrate: Cycloartenol


substrate_name: cyclobranol

substrate: cyclobranol


organism: Thalictrum flavum subsp. glaucum

assay_conditions_summary: pH 8


substrate_name: norcoclaurine

substrate: norcoclaurine


organism: Paramecium bursaria Chlorella virus-1

substrate_name: dUMP

substrate: dUMP


proof_lines:
5,10-methylenetetrahydrofolate
ThyX
methylene group


organism: Medicago sativa

substrate_name: isoliquiritigenin

substrate: isoliquiritigenin


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Escherichia coli (strain K12)

proof_lines: kcat is 1.52 min(-1) with tRNA(fMet1) as substrate. kcat is 1.42 min(-1) with tRNA(fMet2) as substrate. kcat is 1.31 min(-1) with tRNA(Trp1) as substrate. kcat is 1.20 min(-1) with tRNA(Gln1) as substrate. kcat is 1.41 min(-1) with tRNA(Gln


enzyme_display_name: tRNA (cytosine38-C5)-methyltransferase

organism: Schizosaccharomyces pombe

substrate_name: cytosine38 in Q34tRNAAsp

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: tRNA (cytosine38-C5)-methyltransferase

substrate: cytosine38 in Q34tRNAAsp


enzyme_display_name: UniProt P51580

organism: Homo sapiens

source_db: skid

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

source_databases_merged: skid uniprot

enzyme: UniProt P51580

source: skid


km_display: Not reported


enzyme_display_name: Ribosomal RNA small subunit methyltransferase E

substrate_name: 16S rRNA within 30S ribosomal subunits

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

substrate: 16S rRNA within 30S ribosomal subunits


organism: Lathyrus oleraceus

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


organism: Glycyrrhiza echinata


organism: Medicago truncatula


organism: Pisum sativum


column_label: Abstract reports this enzyme activity uses S-adenosyl-L-methionine as the methyl donor (Km = 2.1 microM).

raw_value_unit_evidence: Km raw_value=2.1 microM raw_unit=microM

row_label: rat liver membrane C-terminal protein carboxyl methyltransferase / S-adenosyl-L-methionine

table_label: PubMed XML abstract PMID 2398053


organism: Spodoptera frugiperda

proof_lines: Icmt AdoMet


organism: Ammi majus

substrate_name: bergaptol

substrate: bergaptol


assay_conditions_summary: pH 8; 315.15 K; buffer potassium phosphate

column_label: Abstract reports recombinant AmBMT showed narrow substrate specificity with Km SAM 6.5 micro m.

raw_value_unit_evidence: Km raw_value=6.5 microM raw_unit=microM

row_label: Recombinant AmBMT / S-adenosyl-L-methionine

table_label: PubMed XML abstract PMID 15009205


enzyme_display_name: UniProt Q29U70

column_label: Paper labels 2,7,4'-trihydroxyisoflavanone Km 73.3 uM for Mt HI4OMT.

table_label: Results prose: steady-state kinetic parameters

enzyme: UniProt Q29U70


column_label: Paper labels S-adenosyl-L-methionine as the cosubstrate kinetic parameter with Km 99.8 uM.

raw_value_unit_evidence: SAM Km 99.8 uM; Vmax 23.9 nmol mg^-1 min^-1

row_label: Mt HI4OMT: S-adenosyl-L-methionine cosubstrate


enzyme_display_name: Isoflavone 4'-O-methyltransferase

column_label: Paper labels 6a-hydroxymaackiain Km 62.1 uM for Mt HI4OMT.

raw_value_unit_evidence: 6a-hydroxymaackiain Km 62.1 uM

row_label: Mt HI4OMT: 6a-hydroxymaackiain

enzyme: Isoflavone 4'-O-methyltransferase


enzyme_display_name: UniProt Q9BV86

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q9BV86


enzyme_display_name: UniProt O55060

enzyme: UniProt O55060


organism: Nicotiana sp.

column_label: PMID 16668531 PDF text page 1 lines 34-36 and page 5 line 328; AdoMet/S-adenosyl-L-methionine Km = 10 micromolar.

raw_value_unit_evidence: Abstract reports apparent Km values of 10 micromolar for S-adenosyl-L-methionine and 18 micromolar for ribulose-P2 carboxylase; Results text reports apparent Km for AdoMet was 10 uM.

row_label: AdoMet substrate Km

table_label: Abstract and kinetic analysis prose


enzyme_display_name: Macrocin O-methyltransferase

substrate_name: AdoMet

enzyme: Macrocin O-methyltransferase

substrate: AdoMet


substrate_name: S-Adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E281Q with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

substrate: S-Adenosyl-L-methionine


enzyme_display_name: Trans-aconitate 2-methyltransferase

substrate_name: trans-aconitate

enzyme: Trans-aconitate 2-methyltransferase

substrate: trans-aconitate


enzyme_display_name: flavonoid 3',5'-methyltransferase

organism: Solanum lycopersicum

substrate_name: luteolin

enzyme: flavonoid 3',5'-methyltransferase

substrate: luteolin


substrate_name: eriodictyol

substrate: eriodictyol


column_label: Full text reports the KM value determined for SAM was 26.7 +/- 0.4 microM.

raw_value_unit_evidence: Km raw_value=26.7 +/- 0.4 microM raw_unit=microM

row_label: His-RsmE / SAM varied with 30S subunits present

table_label: Official PMC full-text Results prose: In vitro activity of RsmE

enzyme: Ribosomal RNA small subunit methyltransferase E


enzyme_display_name: thymidylate synthase (FAD)

organism: Thermotoga maritima

substrate_name: NADPH

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

enzyme: thymidylate synthase (FAD)

substrate: NADPH


organism: Clostridioides difficile

substrate_name: Cobalamin

substrate: Cobalamin


organism: Bacillus cereus

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA


substrate_name: hydroxycobalamin

assay_conditions_summary: pH 5.1; 298.15 K; cofactor CoA

proof_lines: recombinant enzyme, in 0.1 M MES, at pH 5.1 and 25°C

substrate: hydroxycobalamin


organism: Vitis vinifera

substrate_name: resveratrol

substrate: resveratrol


substrate_name: resveratrol monomethyl ether

substrate: resveratrol monomethyl ether


organism: Perilla frutescens

substrate_name: chrysin

substrate: chrysin


substrate_name: kaempferol

substrate: kaempferol


substrate_name: apigenin

substrate: apigenin


substrate_name: naringenin

substrate: naringenin


organism: Oryza sativa

substrate_name: tricetin

proof_lines:
isoform ROMT-17
isoform ROMT-15

substrate: tricetin


substrate_name: myricetin

proof_lines:
isoform ROMT-17
pH 7.5, 37°C
isoform ROMT-15

substrate: myricetin


substrate_name: caffeoyl-coenzyme A

assay_conditions_summary: cofactor CoA

substrate: caffeoyl-coenzyme A


proof_lines:
isoform ROMT-15
isoform ROMT-17


organism: Citrus reticulata

substrate_name: quercetin

proof_lines:
pH 8.0, 37°C
at pH 8.0 and 37°C

substrate: quercetin


substrate_name: baicalein

substrate: baicalein


substrate_name: caffeic acid

substrate: caffeic acid


substrate_name: luteolin

substrate: luteolin


organism: Torenia hybrid cultivar

substrate_name: cyanidin 3-O-glucoside

substrate: cyanidin 3-O-glucoside


substrate_name: delphinidin 3,5-O-diglucoside

substrate: delphinidin 3,5-O-diglucoside


substrate_name: delphinidin 3-O-glucoside

substrate: delphinidin 3-O-glucoside


substrate_name: cyanidin 3,5-O-diglucoside

substrate: cyanidin 3,5-O-diglucoside


organism: synthetic construct

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


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Paeonia suffruticosa

substrate_name: luteolin 7-O-glucoside

proof_lines: recombinant enzyme, pH 7.5, temperature not specified in the publication

substrate: luteolin 7-O-glucoside


substrate_name: quercetin 3-O-rutinoside

substrate: quercetin 3-O-rutinoside


enzyme_display_name: UniProt Q4FP21

organism: Candidatus Pelagibacter ubique

substrate_name: tetrahydrofolate

enzyme: UniProt Q4FP21

substrate: tetrahydrofolate


enzyme_display_name: UniProt Q9SPV4

organism: Clarkia breweri

substrate_name: salicylate

enzyme: UniProt Q9SPV4

substrate: salicylate


enzyme_display_name: Flavonoid 3',5'-methyltransferase

substrate_name: cyanidin 3-glucoside

proof_lines: kcat is 0.090 sec(-1) with cyanidin 3-glucoside (PubMed:19525322). kcat is 2.3825 sec(-1) with cyanidin 3-glucoside (PubMed:20580386). kcat is 0.118 sec(-1) with delphinidin 3-glucoside (PubMed:19525322). kcat is 0.1 sec(-1) with quercetin

enzyme: Flavonoid 3',5'-methyltransferase

substrate: cyanidin 3-glucoside


substrate_name: delphinidin 3-glucoside

substrate: delphinidin 3-glucoside


substrate_name: quercetin 3-glucoside

substrate: quercetin 3-glucoside


substrate_name: cyanidin

substrate: cyanidin


substrate_name: quercetin

substrate: quercetin


substrate_name: myricetin

substrate: myricetin


enzyme_display_name: [Fructose-bisphosphate aldolase]-lysine N-methyltransferase, chloroplastic

organism: Arabidopsis thaliana

substrate_name: fructose-bisphosphate aldolase 2

substrate: fructose-bisphosphate aldolase 2


organism: Aspergillus fumigatus


enzyme_display_name: squalene methyltransferase

organism: Botryococcus braunii

substrate_name: Squalene; S-Adenosyl-L-methionine

enzyme: squalene methyltransferase

substrate: Squalene; S-Adenosyl-L-methionine


substrate_name: S-Adenosyl-L-methionine; Squalene

substrate: S-Adenosyl-L-methionine; Squalene


enzyme_display_name: botryococcene C-methyltransferase

enzyme: botryococcene C-methyltransferase


enzyme_display_name: Myricetin 3'/5'-O-methyltransferase 1

organism: Solanum habrochaites

substrate_name: myricetin (in the presence of S-adenosylmethionine)

column_label: PMC table reports Myricetin Km 0.46 +/- 0.05 uM, Kcat 1.59 +/- 0.15 s^-1, and Kcat/Km 3.46 +/- 0.38 uM^-1*s^-1; this row requires only Km

normalized_value_unit_evidence: Km normalized_value=0.00046 normalized_unit=mM; current_export_km=0.00046 mM

raw_value_unit_evidence: Km raw_value=0.46 +/- 0.05 raw_unit=uM for myricetin

row_label: Myricetin row; Km column

table_label: PMID 21343428 PMC HTML ShMOMT1 kinetic table

enzyme: Myricetin 3'/5'-O-methyltransferase 1


substrate_name: laricitrin (in the presence of S-adenosylmethionine)

column_label: PMC table reports Laricitrin Km 0.21 +/- 0.04 uM, Kcat 0.45 +/- 0.01 s^-1, and Kcat/Km 2.14 +/- 0.27 uM^-1*s^-1; this row requires only Km

normalized_value_unit_evidence: Km normalized_value=0.00021 normalized_unit=mM; current_export_km=0.00021 mM

raw_value_unit_evidence: Km raw_value=0.21 +/- 0.04 raw_unit=uM for laricitrin

row_label: Laricitrin row; Km column


organism: Streptomyces coelicolor

proof_lines: pH and temperature not specified in the publication

source_databases_merged: brenda skid uniprot


substrate_name: geranyl diphosphate

smiles: CC(=CCCC(=CCOP(=O)(O)OP(=O)(O)O)C)C

substrate: geranyl diphosphate


organism: Solanum lycopersicum

substrate_name: quercetin 3-O-beta-D-glucoside

assay_conditions_summary: pH 7

column_label: Table 3 row Quercetin 3-glucoside; AnthOMT columns KM (uM), kcat (min^-1), kcat/KM (uM^-1 min^-1)

row_label: Quercetin 3-glucoside -> Isorhamnetin 3-glucoside; AnthOMT columns

table_label: Table 3. Kinetic parameters of CCoAOMT and AnthOMT enzymes in the presence of S-adenosyl L-methionine as methyl donor and using various substrates

substrate: quercetin 3-O-beta-D-glucoside


column_label: Table 3 row Quercetin; AnthOMT columns KM (uM), kcat (min^-1), kcat/KM (uM^-1 min^-1)

row_label: Quercetin -> Isorhamnetin; AnthOMT columns


substrate_name: delphinidin 3-O-beta-D-glucoside

column_label: Table 3 row Delphinidin 3-glucoside; AnthOMT columns KM (uM), kcat (min^-1), kcat/KM (uM^-1 min^-1)

row_label: Delphinidin 3-glucoside -> Petunidin 3-glucoside; AnthOMT columns

substrate: delphinidin 3-O-beta-D-glucoside


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

proof_lines:
pH 7.0, 37°C, recombinant enzyme
Raw SKiD Env: Temp=37°C, pH=7

source_databases_merged: sabio_rk brenda skid


organism: Lathyrus oleraceus

substrate_name: [large subunit of spinach Rubisco-human carbonic anhydrase II fusion protein]-L-lysine

proof_lines: in 100 mM Bicine, 20 mM MgCl2 pH 8.0, at 30°C

proof_lines: kcat is 0.047 sec(-1) for S-adenosyl-L-methionine. kcat is 0.038 sec(-1) for rubisco.


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


substrate_name: S-adenosyl-L-methionine (in the presence of myricetin)

proof_lines: kcat is 1.59 sec(-1) with myricetin as substrate (in the presence of S-adenosylmethionine) (PubMed:21343428). kcat is 0.45 sec(-1) with laricitrin as substrate (in the presence of S-adenosylmethionine) (PubMed:21343428). kcat is 0.47 sec(-1


enzyme_display_name: Squalene methyltransferase 1

substrate_name: squalene

enzyme: Squalene methyltransferase 1

substrate: squalene


enzyme_display_name: Squalene methyltransferase 2

enzyme: Squalene methyltransferase 2


organism: Streptomyces carzinostaticus

column_label: Table 1; acid 8; product 9; Km and kcat columns; relative kcat/Km column is not an absolute unit column.

raw_value_unit_evidence: Table 1 acid 8/product 9: Km=206 +/- 49 uM; kcat=0.69 +/- 0.05 min^-1; relative kcat/Km=1.

row_label: acid 8 / product 9

table_label: Table 1


column_label: Table 1; acid 15; product 18; Km column.

normalized_value_unit_evidence: normalized required Km-only paper value: 24 uM = 0.024 mM.

raw_value_unit_evidence: Table 1 acid 15/product 18: Km=24 +/- 11 uM.

row_label: acid 15 / product 18


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R11W to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; buffer pH 6

column_label: Table 2. Kinetics of NcsB1 and mutant constructs; row_label: Arg11Trp/3; columns KM (uM), kcat (min^-1), and printed relative kcat/KM; absolute kcat/KM is locked from the same-row kcat and KM cells, not from the relative column.

normalized_value_unit_evidence: KM 0.4 mM; kcat 0.01 s^-1; absolute kcat/KM 0.025 s^-1 mM^-1 locked from same-row kcat and KM cells.

raw_value_unit_evidence: Table 2 row Arg11Trp/3: KM 400 +/- 68 uM; kcat 0.60 +/- 0.03 min^-1; printed relative kcat/KM 0.45.


column_label: Table 2. Kinetics of NcsB1 and mutant constructs; row_label: WT/3; columns KM (uM), kcat (min^-1), and printed relative kcat/KM; absolute kcat/KM is locked from the same-row kcat and KM cells, not from the relative column.

normalized_value_unit_evidence: KM 0.206 mM; kcat 0.0115 s^-1; absolute kcat/KM 0.055825242718446605 s^-1 mM^-1 locked from same-row kcat and KM cells.

raw_value_unit_evidence: Table 2 row WT/3: KM 206 +/- 49 uM; kcat 0.69 +/- 0.05 min^-1; printed relative kcat/KM 1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y293I to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetics of NcsB1 and mutant constructs; row_label: Tyr293Ile/3; columns KM (uM), kcat (min^-1), and printed relative kcat/KM; absolute kcat/KM is locked from the same-row kcat and KM cells, not from the relative column.

raw_value_unit_evidence: Table 2 row Tyr293Ile/3: KM 649 +/- 9 uM; kcat 0.76 +/- 0.04 min^-1; printed relative kcat/KM 0.35.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R11A to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetics of NcsB1 and mutant constructs; row_label: Arg11Ala/3; columns KM (uM), kcat (min^-1), and printed relative kcat/KM; absolute kcat/KM is locked from the same-row kcat and KM cells, not from the relative column.

raw_value_unit_evidence: Table 2 row Arg11Ala/3: KM 419 +/- 61 uM; kcat 1.24 +/- 0.06 min^-1; printed relative kcat/KM 0.88.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R11K to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetics of NcsB1 and mutant constructs; row_label: Arg11Lys/3; columns KM (uM), kcat (min^-1), and printed relative kcat/KM; absolute kcat/KM is locked from the same-row kcat and KM cells, not from the relative column.

raw_value_unit_evidence: Table 2 row Arg11Lys/3: KM 319 +/- 40 uM; kcat 1.18 +/- 0.05 min^-1; printed relative kcat/KM 1.10.


enzyme_display_name: Pavine N-methyltransferase

organism: Thalictrum flavum subsp. glaucum

substrate_name: (+-)-pavine

proof_lines: kcat is 0.00005 sec(-1) with (+-)-pavine as substrate (PubMed:19624470). kcat is 0.00079 sec(-1) with (R,S)-tetrahydropapaverine as substrate (PubMed:27573242).

enzyme: Pavine N-methyltransferase

substrate: (+-)-pavine


enzyme_display_name: pavine N-methyltransferase

substrate_name: (S)-tetrahydropapaverine

enzyme: pavine N-methyltransferase

substrate: (S)-tetrahydropapaverine


organism: Streptomyces sahachiroi


column_label: Primary Results prose explicitly pairs compound 3, saturated SAM, and Km 145 +/- 14 uM; Figure 3D I is the corresponding kinetic plot.

normalized_value_unit_evidence: Km=0.145 mM after exact conversion of 145 uM.

raw_value_unit_evidence: The paper reports Km 145 +/- 14 uM for compound 3 with saturated SAM.

row_label: AziB2 O-methylation with 3-hydroxy-5-methyl-NPA (compound 3) varied and SAM saturated

table_label: Results kinetic prose and Figure 3D I, PDF pages 4-5 / journal pages 1074-1075


organism: Streptomyces wedmorensis

substrate_name: HEP-CMP

substrate: HEP-CMP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R202L to reconstruct the assayed variant sequence.


substrate_name: 6-hydroxytryprostatin B

substrate: 6-hydroxytryprostatin B


column_label: Table 2; row FtmD / SAM; column Km (uM).

normalized_value_unit_evidence: Km paper=0.011 mM

raw_value_unit_evidence: Table 2 row FtmD / SAM: Km 11 +/- 3 uM; kcat 28 +/- 2 s^-1; kcat/Km 2.5 uM^-1 s^-1.

row_label: FtmD SAM

table_label: Table 2. Kinetic Constants for FtmD and FtmD R202L


column_label: Table 2; row FtmD / substrate 4; column Km (uM).

normalized_value_unit_evidence: Km paper=0.021 mM

raw_value_unit_evidence: Table 2 row FtmD / substrate 4: Km 21 +/- 2 uM; kcat 27 +/- 1 s^-1; kcat/Km 1.3 uM^-1 s^-1.

row_label: FtmD substrate 4


enzyme_display_name: juvenile hormone-III synthase

organism: Aedes aegypti

substrate_name: (trans/cis/cis)-juvenile hormone I acid

enzyme: juvenile hormone-III synthase

substrate: (trans/cis/cis)-juvenile hormone I acid


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


organism: Pseudomonas aeruginosa

proof_lines: presence of hydroxylase PhzS, pH 7.8, 22°C


organism: Bombyx mori

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q767F1 and applied mutation signature F147A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic parameters of the wild-type JHAMT1 and its mutants toward farnesoic acid. The printed column heads of the table are, in order, Enzyme, Km (uM), kcat (min^-1) and kcat/Km (mM^-1 min^-1). The enzyme form used here is the row labelled F147A, which is the JHAMT1-F147A form; within that row the Km column prints 20.42, the kcat column prints 0.02 and the kcat/Km column prints 1.08.

raw_value_unit_evidence: Table 3, JHAMT1-F147A enzyme row, substrate farnesoic acid: Km = 20.42 uM in the column headed Km (uM); kcat = 0.02 min^-1 in the column headed kcat (min^-1); printed kcat/Km = 1.08 mM^-1 min^-1 in the column headed kcat/Km (mM^-1 min^-1). The printed column heads of Table 3 carry those three units for every enzyme row of the table.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q767F1 and applied mutation signature I219A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic parameters of the wild-type JHAMT1 and its mutants toward farnesoic acid. The printed column heads of the table are, in order, Enzyme, Km (uM), kcat (min^-1) and kcat/Km (mM^-1 min^-1). The enzyme form used here is the row labelled I219A, which is the JHAMT1-I219A form; within that row the Km column prints 40.23, the kcat column prints 0.09 and the kcat/Km column prints 2.30.

raw_value_unit_evidence: Table 3, JHAMT1-I219A enzyme row, substrate farnesoic acid: Km = 40.23 uM in the column headed Km (uM); kcat = 0.09 min^-1 in the column headed kcat (min^-1); printed kcat/Km = 2.30 mM^-1 min^-1 in the column headed kcat/Km (mM^-1 min^-1). The printed column heads of Table 3 carry those three units for every enzyme row of the table.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q767F1 and applied mutation signature Y150A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic parameters of the wild-type JHAMT1 and its mutants toward farnesoic acid. The printed column heads of the table are, in order, Enzyme, Km (uM), kcat (min^-1) and kcat/Km (mM^-1 min^-1). The enzyme form used here is the row labelled Y150A, which is the JHAMT1-Y150A form; within that row the Km column prints 23.82, the kcat column prints 0.11 and the kcat/Km column prints 4.39.

raw_value_unit_evidence: Table 3, JHAMT1-Y150A enzyme row, substrate farnesoic acid: Km = 23.82 uM in the column headed Km (uM); kcat = 0.11 min^-1 in the column headed kcat (min^-1); printed kcat/Km = 4.39 mM^-1 min^-1 in the column headed kcat/Km (mM^-1 min^-1). The printed column heads of Table 3 carry those three units for every enzyme row of the table.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q767F1 and applied mutation signature W115A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic parameters of the wild-type JHAMT1 and its mutants toward farnesoic acid. The printed column heads of the table are, in order, Enzyme, Km (uM), kcat (min^-1) and kcat/Km (mM^-1 min^-1). The enzyme form used here is the row labelled W115A, which is the JHAMT1-W115A form; within that row the Km column prints 73.32, the kcat column prints 0.13 and the kcat/Km column prints 1.83.

normalized_value_unit_evidence: Km: printed Table 3 cell 73.32 uM; 1 uM is 1/1000 mM, so 73.32 / 1000 = 0.07332 mM; the exported value is 0.07332 mM. kcat: printed Table 3 cell 0.13 min^-1; the printed turnover column is per MINUTE, so 0.13 / 60 = 0.0021666666666666666 s^-1; the exported value is 0.0022 s^(-1). kcat/Km: printed Table 3 cell 1.83 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 1.83 / 60 = 0.0305 s^-1 mM^-1; the exported value is 0.030005455537370433 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, JHAMT1-W115A enzyme row, substrate farnesoic acid: Km = 73.32 uM in the column headed Km (uM); kcat = 0.13 min^-1 in the column headed kcat (min^-1); printed kcat/Km = 1.83 mM^-1 min^-1 in the column headed kcat/Km (mM^-1 min^-1). The printed column heads of Table 3 carry those three units for every enzyme row of the table.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q767F1 and applied mutation signature I170A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic parameters of the wild-type JHAMT1 and its mutants toward farnesoic acid. The printed column heads of the table are, in order, Enzyme, Km (uM), kcat (min^-1) and kcat/Km (mM^-1 min^-1). The enzyme form used here is the row labelled I170A, which is the JHAMT1-I170A form; within that row the Km column prints 45.01, the kcat column prints 0.18 and the kcat/Km column prints 4.02.

normalized_value_unit_evidence: Km: printed Table 3 cell 45.01 uM; 1 uM is 1/1000 mM, so 45.01 / 1000 = 0.04501 mM; the exported value is 0.04501 mM. kcat: printed Table 3 cell 0.18 min^-1; the printed turnover column is per MINUTE, so 0.18 / 60 = 0.003 s^-1; the exported value is 0.003 s^(-1). kcat/Km: printed Table 3 cell 4.02 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 4.02 / 60 = 0.06699999999999999 s^-1 mM^-1; the exported value is 0.06665185514330149 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, JHAMT1-I170A enzyme row, substrate farnesoic acid: Km = 45.01 uM in the column headed Km (uM); kcat = 0.18 min^-1 in the column headed kcat (min^-1); printed kcat/Km = 4.02 mM^-1 min^-1 in the column headed kcat/Km (mM^-1 min^-1). The printed column heads of Table 3 carry those three units for every enzyme row of the table.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q767F1 and applied mutation signature P221A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic parameters of the wild-type JHAMT1 and its mutants toward farnesoic acid. The printed column heads of the table are, in order, Enzyme, Km (uM), kcat (min^-1) and kcat/Km (mM^-1 min^-1). The enzyme form used here is the row labelled P221A, which is the JHAMT1-P221A form; within that row the Km column prints 50.32, the kcat column prints 0.41 and the kcat/Km column prints 8.08.

raw_value_unit_evidence: Table 3, JHAMT1-P221A enzyme row, substrate farnesoic acid: Km = 50.32 uM in the column headed Km (uM); kcat = 0.41 min^-1 in the column headed kcat (min^-1); printed kcat/Km = 8.08 mM^-1 min^-1 in the column headed kcat/Km (mM^-1 min^-1). The printed column heads of Table 3 carry those three units for every enzyme row of the table.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q767F1 and applied mutation signature F222A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic parameters of the wild-type JHAMT1 and its mutants toward farnesoic acid. The printed column heads of the table are, in order, Enzyme, Km (uM), kcat (min^-1) and kcat/Km (mM^-1 min^-1). The enzyme form used here is the row labelled F222A, which is the JHAMT1-F222A form; within that row the Km column prints 40.42, the kcat column prints 0.46 and the kcat/Km column prints 11.41.

raw_value_unit_evidence: Table 3, JHAMT1-F222A enzyme row, substrate farnesoic acid: Km = 40.42 uM in the column headed Km (uM); kcat = 0.46 min^-1 in the column headed kcat (min^-1); printed kcat/Km = 11.41 mM^-1 min^-1 in the column headed kcat/Km (mM^-1 min^-1). The printed column heads of Table 3 carry those three units for every enzyme row of the table.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q767F1 and applied mutation signature I146A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic parameters of the wild-type JHAMT1 and its mutants toward farnesoic acid. The printed column heads of the table are, in order, Enzyme, Km (uM), kcat (min^-1) and kcat/Km (mM^-1 min^-1). The enzyme form used here is the row labelled I146A, which is the JHAMT1-I146A form; within that row the Km column prints 67.83, the kcat column prints 0.50 and the kcat/Km column prints 7.33.

raw_value_unit_evidence: Table 3, JHAMT1-I146A enzyme row, substrate farnesoic acid: Km = 67.83 uM in the column headed Km (uM); kcat = 0.50 min^-1 in the column headed kcat (min^-1); printed kcat/Km = 7.33 mM^-1 min^-1 in the column headed kcat/Km (mM^-1 min^-1). The printed column heads of Table 3 carry those three units for every enzyme row of the table.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q767F1 and applied mutation signature T144A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic parameters of the wild-type JHAMT1 and its mutants toward farnesoic acid. The printed column heads of the table are, in order, Enzyme, Km (uM), kcat (min^-1) and kcat/Km (mM^-1 min^-1). The enzyme form used here is the row labelled T144A, which is the JHAMT1-T144A form; within that row the Km column prints 40.42, the kcat column prints 0.78 and the kcat/Km column prints 19.33.

raw_value_unit_evidence: Table 3, JHAMT1-T144A enzyme row, substrate farnesoic acid: Km = 40.42 uM in the column headed Km (uM); kcat = 0.78 min^-1 in the column headed kcat (min^-1); printed kcat/Km = 19.33 mM^-1 min^-1 in the column headed kcat/Km (mM^-1 min^-1). The printed column heads of Table 3 carry those three units for every enzyme row of the table.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q767F1 and applied mutation signature F169A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic parameters of the wild-type JHAMT1 and its mutants toward farnesoic acid. The printed column heads of the table are, in order, Enzyme, Km (uM), kcat (min^-1) and kcat/Km (mM^-1 min^-1). The enzyme form used here is the row labelled F169A, which is the JHAMT1-F169A form; within that row the Km column prints 112.60, the kcat column prints 0.84 and the kcat/Km column prints 7.45.

raw_value_unit_evidence: Table 3, JHAMT1-F169A enzyme row, substrate farnesoic acid: Km = 112.60 uM in the column headed Km (uM); kcat = 0.84 min^-1 in the column headed kcat (min^-1); printed kcat/Km = 7.45 mM^-1 min^-1 in the column headed kcat/Km (mM^-1 min^-1). The printed column heads of Table 3 carry those three units for every enzyme row of the table.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q767F1 and applied mutation signature V166A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic parameters of the wild-type JHAMT1 and its mutants toward farnesoic acid. The printed column heads of the table are, in order, Enzyme, Km (uM), kcat (min^-1) and kcat/Km (mM^-1 min^-1). The enzyme form used here is the row labelled V166A, which is the JHAMT1-V166A form; within that row the Km column prints 291.60, the kcat column prints 1.07 and the kcat/Km column prints 3.66.

normalized_value_unit_evidence: Km: printed Table 3 cell 291.60 uM; 1 uM is 1/1000 mM, so 291.60 / 1000 = 0.2916 mM; the exported value is 0.2916 mM. kcat: printed Table 3 cell 1.07 min^-1; the printed turnover column is per MINUTE, so 1.07 / 60 = 0.017833333333333333 s^-1; the exported value is 0.01783 s^(-1). kcat/Km: printed Table 3 cell 3.66 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 3.66 / 60 = 0.061 s^-1 mM^-1; the exported value is 0.061145404663923174 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, JHAMT1-V166A enzyme row, substrate farnesoic acid: Km = 291.60 uM in the column headed Km (uM); kcat = 1.07 min^-1 in the column headed kcat (min^-1); printed kcat/Km = 3.66 mM^-1 min^-1 in the column headed kcat/Km (mM^-1 min^-1). The printed column heads of Table 3 carry those three units for every enzyme row of the table.


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

column_label: Table 3: Kinetic parameters of the wild-type JHAMT1 and its mutants toward farnesoic acid. The printed column heads of the table are, in order, Enzyme, Km (uM), kcat (min^-1) and kcat/Km (mM^-1 min^-1). The enzyme form used here is the row labelled JHAMT1-WT, which is the JHAMT1-WT form; within that row the Km column prints 11.05, the kcat column prints 1.14 and the kcat/Km column prints 102.89.

normalized_value_unit_evidence: Km: printed Table 3 cell 11.05 uM; 1 uM is 1/1000 mM, so 11.05 / 1000 = 0.01105 mM; the exported value is 0.01105 mM. kcat: printed Table 3 cell 1.14 min^-1; the printed turnover column is per MINUTE, so 1.14 / 60 = 0.019 s^-1; the exported value is 0.019 s^(-1). kcat/Km: printed Table 3 cell 102.89 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 102.89 / 60 = 1.7148333333333332 s^-1 mM^-1; the exported value is 1.7194570135746605 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, JHAMT1-WT enzyme row, substrate farnesoic acid: Km = 11.05 uM in the column headed Km (uM); kcat = 1.14 min^-1 in the column headed kcat (min^-1); printed kcat/Km = 102.89 mM^-1 min^-1 in the column headed kcat/Km (mM^-1 min^-1). The printed column heads of Table 3 carry those three units for every enzyme row of the table.


organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)

proof_lines: kcat is 8.2 sec(-1) with 6-hydroxytryprostatin B as substrate. kcat is 6.9 sec(-1) with S-adenosyl-L-methionine as substrate.


substrate_name: farnesoic acid

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

proof_lines: kcat is 0.004 sec(-1) with farnesoic acid as substrate.

substrate: farnesoic acid


organism: Diaphorina citri

substrate_name: (2E,6Z)-10cis-juvenile hormone I acid

sequence_source: GenBank protein AIG94926.1 translated from KM212828.1

substrate: (2E,6Z)-10cis-juvenile hormone I acid


protein_accession_database: NCBI Protein


enzyme_display_name: (R,S)-reticuline 7-O-methyltransferase

organism: Unknown

substrate_name: Unknown

source_db: unknown

source_license: see source

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

enzyme: (R,S)-reticuline 7-O-methyltransferase

substrate: Unknown

source: unknown


organism: Homo sapiens

substrate_name: SPKRIAKRRSPPADA

proof_lines: recombinant NRMT2, pH and temperature not specified in the publication

substrate: SPKRIAKRRSPPADA


organism: Thalictrum flavum

substrate_name: Pavine

substrate: Pavine


substrate_name: S-Adenosyl-L-methionine; Pavine

ki_unit: mM

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

substrate: S-Adenosyl-L-methionine; Pavine


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

proof_lines: kcat is 0.69 min(-1) with 2,7-dihydroxy-5-methyl-1-naphthoate as substrate. kcat is 0.27 min(-1) with 3,5-dihydroxy-2-naphthoate as substrate. kcat is 0.030 min(-1) with 3,7-dihydroxy-2-naphthoate as substrate. kcat is 0.0080 min(-1) 1,4-di


proof_lines: at 28°C, pH not specified in the publication


substrate_name: 1,4-dihydroxy-2-naphthoic acid

column_label: Table 1; acid 15; product 18; Km and kcat columns; relative kcat/Km column is not an absolute unit column.

source_databases_merged: brenda skid

substrate: 1,4-dihydroxy-2-naphthoic acid


column_label: Table 1; acid 8; product 9; Km and kcat columns; relative kcat/Km column is not an absolute unit column.

raw_value_unit_evidence: Table 1 acid 8/product 9: Km=206 +/- 49 uM; kcat=0.69 +/- 0.05 min^-1; relative kcat/Km=1.


column_label: Table 1; acid 13; product 16; Km and kcat columns; relative kcat/Km column is not an absolute unit column.

raw_value_unit_evidence: Table 1 acid 13/product 16: Km=352 +/- 71 uM; kcat=0.27 +/- 0.02 min^-1; relative kcat/Km=0.23.

row_label: acid 13 / product 16


column_label: Table 1; acid 14; product 17; Km and kcat columns; relative kcat/Km column is not an absolute unit column.

raw_value_unit_evidence: Table 1 acid 14/product 17: Km=66 +/- 12 uM; kcat=0.030 +/- 0.002 min^-1; relative kcat/Km=0.14.

row_label: acid 14 / product 17


organism: Aspergillus fumigatus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R202L to reconstruct the assayed variant sequence.


column_label: Table 2; row FtmD / substrate 4; columns Km (uM), kcat (s^-1), kcat/Km (uM^-1 s^-1).

normalized_value_unit_evidence: kcat paper=27 s^-1; Km paper=0.021 mM; kcat/Km paper=1300 s^-1 mM^-1


column_label: Table 2; row FtmD / SAM; columns Km (uM), kcat (s^-1), kcat/Km (uM^-1 s^-1).

normalized_value_unit_evidence: kcat paper=28 s^-1; Km paper=0.011 mM; kcat/Km paper=2500 s^-1 mM^-1

raw_value_unit_evidence: Table 2 row FtmD / SAM: Km 11 +/- 3 uM; kcat 28 +/- 2 s^-1; kcat/Km 2.5 uM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R11A to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetics of NcsB1 and mutant constructs; row_label: Arg11Ala/3; columns KM (uM), kcat (min^-1), and printed relative kcat/KM; absolute kcat/KM is locked from the same-row kcat and KM cells, not from the relative column.

raw_value_unit_evidence: Table 2 row Arg11Ala/3: KM 419 +/- 61 uM; kcat 1.24 +/- 0.06 min^-1; printed relative kcat/KM 0.88.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R11K to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetics of NcsB1 and mutant constructs; row_label: Arg11Lys/3; columns KM (uM), kcat (min^-1), and printed relative kcat/KM; absolute kcat/KM is locked from the same-row kcat and KM cells, not from the relative column.

raw_value_unit_evidence: Table 2 row Arg11Lys/3: KM 319 +/- 40 uM; kcat 1.18 +/- 0.05 min^-1; printed relative kcat/KM 1.10.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R11W to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetics of NcsB1 and mutant constructs; row_label: Arg11Trp/3; columns KM (uM), kcat (min^-1), and printed relative kcat/KM; absolute kcat/KM is locked from the same-row kcat and KM cells, not from the relative column.

raw_value_unit_evidence: Table 2 row Arg11Trp/3: KM 400 +/- 68 uM; kcat 0.60 +/- 0.03 min^-1; printed relative kcat/KM 0.45.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y293I to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetics of NcsB1 and mutant constructs; row_label: Tyr293Ile/3; columns KM (uM), kcat (min^-1), and printed relative kcat/KM; absolute kcat/KM is locked from the same-row kcat and KM cells, not from the relative column.

raw_value_unit_evidence: Table 2 row Tyr293Ile/3: KM 649 +/- 9 uM; kcat 0.76 +/- 0.04 min^-1; printed relative kcat/KM 0.35.


enzyme_display_name: methanethiol S-methyltransferase

organism: Marinobacter litoralis

proof_lines: with methanethiol as cosubstrate, at pH 9.0 and 45°C

enzyme: methanethiol S-methyltransferase


substrate_name: methanethiol

smiles: CS

substrate: methanethiol


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

proof_lines: with H2S as cosubstrate, at pH 9.0 and 45°C


smiles: S


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


substrate_name: (cis/trans/cis)-juvenile hormone I acid

substrate: (cis/trans/cis)-juvenile hormone I acid


substrate_name: (cis/trans/trans)-juvenile hormone I acid


substrate_name: homofarnesoate

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

proof_lines:
AeaJHAMT
JHA III
JHA analogues

substrate: homofarnesoate


substrate_name: juvenile hormone III acid

substrate: juvenile hormone III acid


enzyme_display_name: norbelladine O-methyltransferase

organism: Lycoris aurea

substrate_name: caffeic acid

enzyme: norbelladine O-methyltransferase

substrate: caffeic acid


organism: Drosophila melanogaster

substrate_name: palmitate

smiles: CCCCCCCCCCCCCCCC(=O)O

proof_lines: juvenile hormone acid O-methyltransferase

substrate: palmitate


substrate_name: laurate

smiles: CCCCCCCCCCCC(=O)[O-]

substrate: laurate


enzyme_display_name: reticuline N-methyltransferase

organism: Papaver somniferum

substrate_name: (S)-N-methylcoclaurine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G204E with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines:
pH 8.0, 37°C, mutant enzyme G204E
mutant G204E, pH 8.0, 30°C

enzyme: reticuline N-methyltransferase

substrate: (S)-N-methylcoclaurine


proof_lines:
wild-type, pH 8.0, 30°C
pH 8.0, 37°C, wild-type enzyme


substrate_name: juvenile hormone I acid bisepoxide

substrate: juvenile hormone I acid bisepoxide


substrate_name: juvenile hormone III acid bisepoxide

substrate: juvenile hormone III acid bisepoxide


substrate_name: (2E,6Z)-10cis-juvenile hormone I acid


substrate_name: (2Z,6E)-10cis-juvenile hormone I acid

substrate: (2Z,6E)-10cis-juvenile hormone I acid


proof_lines: kcat is 7.7 min(-1) for juvenile hormone III acid. kcat is 10.1 min(-1) for farnesoate. kcat is 0.103 min(-1) for laureate acid. kcat is 0.041 min(-1) for palmitate acid.


enzyme_display_name: Norbelladine 4'-O-methyltransferase

organism: Narcissus aff. pseudonarcissus MK-2014

substrate_name: norbelladine

column_label: Table 1 'Table 1: Kinetic parameters of Narcissus norbelladine 4'-O-methyltransferase'; row norbelladine; km cells.

normalized_value_unit_evidence: Table 1 row norbelladine normalized: Km 0.0016 mM.

raw_value_unit_evidence: Table 1 row norbelladine: Km 1.6 uM.

row_label: norbelladine

enzyme: Norbelladine 4'-O-methyltransferase

substrate: norbelladine


substrate_name: S-adenosyl-L-methionine

column_label: Table 1 'Table 1: Kinetic parameters of Narcissus norbelladine 4'-O-methyltransferase'; row AdoMet; km cells.

normalized_value_unit_evidence: Table 1 row AdoMet normalized: Km 0.0285 mM.

raw_value_unit_evidence: Table 1 row AdoMet: Km 28.5 uM.

row_label: AdoMet

substrate: S-adenosyl-L-methionine


substrate_name: N-methylnorbelladine

column_label: Table 1 'Table 1: Kinetic parameters of Narcissus norbelladine 4'-O-methyltransferase'; row N-methylnorbelladine; km cells.

normalized_value_unit_evidence: Table 1 row N-methylnorbelladine normalized: Km 0.0019 mM.

raw_value_unit_evidence: Table 1 row N-methylnorbelladine: Km 1.9 uM.

row_label: N-methylnorbelladine

substrate: N-methylnorbelladine


substrate_name: dopamine

column_label: Table 1 'Table 1: Kinetic parameters of Narcissus norbelladine 4'-O-methyltransferase'; row dopamine; km cells.

normalized_value_unit_evidence: Table 1 row dopamine normalized: Km 0.0073 mM.

raw_value_unit_evidence: Table 1 row dopamine: Km 7.3 uM.

row_label: dopamine

substrate: dopamine


enzyme_display_name: Xanthohumol 4-O-methyltransferase

organism: Humulus lupulus

substrate_name: Unknown

enzyme: Xanthohumol 4-O-methyltransferase

substrate: Unknown


enzyme_display_name: 3-aminomethylindole N-methyltransferase

organism: Hordeum vulgare subsp. vulgare

enzyme: 3-aminomethylindole N-methyltransferase


substrate_name: (S)-reticuline

proof_lines: kcat is 0.028 sec(-1) with (S)-reticuline as substrate. kcat is 0.053 sec(-1) with (R)-reticuline as substrate. kcat is 0.047 sec(-1) with S-adenosyl-L-methionine as substrate.

substrate: (S)-reticuline


column_label: Table 2; Table 2 row AdoMet; columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Table 2 row AdoMet reports Km 168 +/- 8 uM, Vmax 66.5 +/- 1.4 pmol min^-1 ug^-1 protein, kcat 0.047 s^-1, and kcat/Km 280 s^-1 M^-1.

row_label: Table 2 row AdoMet

table_label: PMID 27634038, Table 2: Michaelis-Menten enzyme kinetic parameters for RNMT with respect to (S)-reticuline, (R)-reticuline, and AdoMet


organism: Narcissus papyraceus

proof_lines: in the presence of Mg2+, at pH 9.0 and 37°C


enzyme_display_name: flavonoid 3',5'-methyltransferase

organism: Vitis vinifera

substrate_name: Cyanidin 3-O-glucoside

enzyme: flavonoid 3',5'-methyltransferase

substrate: Cyanidin 3-O-glucoside


substrate_name: Quercetin 3-O-glucoside

substrate: Quercetin 3-O-glucoside


substrate_name: desmethylxanthohumol

substrate: desmethylxanthohumol


substrate_name: chalconaringenin

substrate: chalconaringenin


substrate_name: xanthohumol

substrate: xanthohumol


substrate_name: resveratrol

substrate: resveratrol


proof_lines: in the presence of Zn2+, vanillin as product, at pH 9.0 and 37°C

proof_lines: in the presence of Ni2+, isovanillin as product, at pH 9.0 and 37°C


enzyme_display_name: Reticuline N-methyltransferase

enzyme: Reticuline N-methyltransferase


substrate_name: (S)-Coclaurine

proof_lines:
mutant G204E, pH 8.0, 30°C
pH 8.0, 37°C, mutant enzyme G204E

substrate: (S)-Coclaurine


proof_lines:
pH 8.0, 37°C, wild-type enzyme
wild-type, pH 8.0, 30°C


column_label: Table 1 'Table 1: Kinetic parameters of Narcissus norbelladine 4'-O-methyltransferase'; row dopamine; kcat, kcat_over_km, km cells.

raw_value_unit_evidence: Table 1 row dopamine: Km 7.3 uM; kcat 3.6 1/min; kcat/Km 0.5 1/uM*min.


column_label: Table 1 'Table 1: Kinetic parameters of Narcissus norbelladine 4'-O-methyltransferase'; row N-methylnorbelladine; kcat, kcat_over_km, km cells.

raw_value_unit_evidence: Table 1 row N-methylnorbelladine: Km 1.9 uM; kcat 2.6 1/min; kcat/Km 1.3 1/uM*min.


column_label: Table 1 'Table 1: Kinetic parameters of Narcissus norbelladine 4'-O-methyltransferase'; row norbelladine; kcat, kcat_over_km, km cells.

raw_value_unit_evidence: Table 1 row norbelladine: Km 1.6 uM; kcat 1.3 1/min; kcat/Km 0.8 1/uM*min.


column_label: Table 1 'Table 1: Kinetic parameters of Narcissus norbelladine 4'-O-methyltransferase'; row AdoMet; kcat, kcat_over_km, km cells.

raw_value_unit_evidence: Table 1 row AdoMet: Km 28.5 uM; kcat 4.5 1/min; kcat/Km 0.16 1/uM*min.


organism: Pseudomonas deceptionensis


substrate_name: methanethiol

column_label: Table 1 columns Km (mM), kcat (s^-1), kcat/Km (M^-1 s^-1); row MeSH.

row_label: PdMddA / MeSH (methanethiol)

table_label: Table 1: Kinetic parameters of PdMddA with different substrates

substrate: methanethiol


substrate_name: dithiothreitol

smiles: C(C(C(CS)O)O)S

column_label: Table 1 columns Km (mM), kcat (s^-1), kcat/Km (M^-1 s^-1); row DTT.

row_label: PdMddA / DTT

substrate: dithiothreitol


enzyme_display_name: xanthohumol 4-O-methyltransferase

column_label: Table 3 row OMT2 Resveratrol under Km Substrate column: 19 +/- 1 uM.

row_label: OMT2 / Resveratrol

table_label: Table 3

enzyme: xanthohumol 4-O-methyltransferase


column_label: Table 3 row OMT2 Desmethylxanthohumol under Km Substrate column: 23 +/- 6 uM.

row_label: OMT2 / Desmethylxanthohumol


column_label: Table 3 row OMT2 Xanthohumol under Km Substrate column: 31 +/- 3 uM.

row_label: OMT2 / Xanthohumol


column_label: Table 3 row OMT2 SAM under Km Substrate column: 34 +/- 3 uM; footnote c says determined with xanthohumol as cosubstrate.

raw_value_unit_evidence: Km 34 +/- 3 uM; footnote c determined with xanthohumol as cosubstrate.

row_label: OMT2 / SAM


column_label: Table 3 row OMT2 Chalconaringenin under Km Substrate column: 237 +/- 19 uM.

row_label: OMT2 / Chalconaringenin


substrate_name: (R)-reticuline

column_label: Table 2; Table 2 row (R)-Reticuline; columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Table 2 row (R)-Reticuline reports Km 85 +/- 11 uM, Vmax 74.8 +/- 3.6 pmol min^-1 ug^-1 protein, kcat 0.053 s^-1, and kcat/Km 618 s^-1 M^-1.

row_label: Table 2 row (R)-Reticuline

substrate: (R)-reticuline


column_label: Table 2; Table 2 row (S)-Reticuline; columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Table 2 row (S)-Reticuline reports Km 42 +/- 3 uM, Vmax 39.6 +/- 0.9 pmol min^-1 ug^-1 protein, kcat 0.028 s^-1, and kcat/Km 655 s^-1 M^-1.

row_label: Table 2 row (S)-Reticuline


enzyme_display_name: UniProt Q9NR48

enzyme: UniProt Q9NR48


enzyme_display_name: Botryococcene C-methyltransferase

organism: Botryococcus braunii

substrate_name: botryococcene

enzyme: Botryococcene C-methyltransferase

substrate: botryococcene


enzyme_display_name: Flavone 3'-O-methyltransferase 1

organism: Arabidopsis thaliana

substrate_name: N-acetylserotonin (at pH 7.8 and 37 degrees Celsius)

enzyme: Flavone 3'-O-methyltransferase 1


organism: Diaphorina citri

substrate_name: farnesoic acid

substrate: farnesoic acid


substrate_name: homofarnesoic acid

substrate: homofarnesoic acid


enzyme_display_name: Bergaptol O-methyltransferase

organism: Glehnia littoralis

substrate_name: bergaptol

enzyme: Bergaptol O-methyltransferase

substrate: bergaptol


substrate_name: quercetin

substrate: quercetin


enzyme_display_name: UniProt P51580

organism: Homo sapiens

enzyme: UniProt P51580


organism: Lycoris radiata

column_label: PDF pages 8-9, Table 1, 3,4-Dihydroxybenzaldehyde substrate / Vanillin product column: Km, kcat, kcat/Km

row_label: 3,4-Dihydroxybenzaldehyde -> Vanillin

table_label: PMID 31494163 Table 1. Kinetic parameters for LrOMT-catalyzed O-methylation


substrate_name: caffeic acid

column_label: PDF pages 8-9, Table 1, Caffeic acid substrate / Ferulic acid product column: Km, kcat, kcat/Km

row_label: Caffeic acid -> Ferulic acid

substrate: caffeic acid


substrate_name: norbelladine

substrate: norbelladine


substrate_name: serotonin

substrate: serotonin


enzyme_display_name: Indolethylamine N-methyltransferase

substrate_name: tryptamine

column_label: Abstract reports the recombinant enzyme catalyzed methylation of tryptamine with an apparent K(m) value of 2.9 mM.

raw_value_unit_evidence: Km raw_value=2.9 mM raw_unit=mM

row_label: Human recombinant indolethylamine N-methyltransferase / tryptamine

table_label: PubMed XML abstract PMID 10552930

enzyme: Indolethylamine N-methyltransferase

substrate: tryptamine


enzyme_display_name: demethylphylloquinol methyltransferase

substrate_name: menadione

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

proof_lines:
NDC1
demethylphylloquinone
vitamin K1

enzyme: demethylphylloquinol methyltransferase

substrate: menadione


enzyme_display_name: tabersonine 16-O-methyltransferase

organism: Catharanthus roseus

substrate_name: S-adenosyl-L-methionine

enzyme: tabersonine 16-O-methyltransferase

substrate: S-adenosyl-L-methionine


enzyme_display_name: nicotinate methyltransferase

organism: Glycine max

enzyme: nicotinate methyltransferase


substrate_name: nicotinate

substrate: nicotinate


substrate_name: Unknown

substrate: Unknown


proof_lines:
at pH 7.5 and 28°C
pH 7.0, 23°C


enzyme_display_name: sialate 8-O-methyltransferase

organism: Asterias rubens

proof_lines: pH 8.0, 25°C, with N-acetylneuraminyl alpha2,3-lactose

enzyme: sialate 8-O-methyltransferase


substrate_name: N-acetylneuraminyl alpha2,3-lactose

substrate: N-acetylneuraminyl alpha2,3-lactose


substrate_name: N-acetylneuraminic acid

substrate: N-acetylneuraminic acid


enzyme_display_name: resveratrol 4'-O-methyltransferase

organism: Acorus calamus

substrate_name: resveratrol

enzyme: resveratrol 4'-O-methyltransferase

substrate: resveratrol


substrate_name: isorhapontigenin

substrate: isorhapontigenin


organism: Methanocaldococcus jannaschii

proof_lines: pH and temperature not specified in the publication


organism: Methanococcus maripaludis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y51F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y51F, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T6V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T6V, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S233A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S233A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S175A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S175A, pH and temperature not specified in the publication


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


enzyme_display_name: thymidylate synthase (FAD)

organism: Helicobacter pylori

substrate_name: dUMP

enzyme: thymidylate synthase (FAD)

substrate: dUMP


enzyme_display_name: 24-methylenesterol C-methyltransferase

enzyme: 24-methylenesterol C-methyltransferase


substrate_name: Zymosterol

substrate: Zymosterol


substrate_name: Cycloartenol

substrate: Cycloartenol


substrate_name: obtusifoliol

substrate: obtusifoliol


substrate_name: lanosterol

substrate: lanosterol


enzyme_display_name: glycine hydroxymethyltransferase

organism: Psychromonas ingrahamii

substrate_name: L-serine

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

proof_lines:
pH 7.2, 20°C
Raw SKiD Env: Temp=20°C, pH=7.2

enzyme: glycine hydroxymethyltransferase

substrate: L-serine


enzyme_display_name: UniProt P07511

organism: Oryctolagus cuniculus

substrate_name: tetrahydrofolate

enzyme: UniProt P07511

substrate: tetrahydrofolate


enzyme_display_name: UniProt Q7SIB6

organism: Geobacillus stearothermophilus

enzyme: UniProt Q7SIB6


enzyme_display_name: caffeate O-methyltransferase

enzyme: caffeate O-methyltransferase


substrate_name: Protocatechuic aldehyde

substrate: Protocatechuic aldehyde


substrate_name: 5-hydroxyferulic acid

substrate: 5-hydroxyferulic acid


substrate_name: 3,4,5-trihydroxycinnamic acid

substrate: 3,4,5-trihydroxycinnamic acid


substrate_name: caffeic acid

substrate: caffeic acid


enzyme_display_name: trans-aconitate 2-methyltransferase

organism: Escherichia coli

substrate_name: trans-aconitate

enzyme: trans-aconitate 2-methyltransferase

substrate: trans-aconitate


substrate_name: DL-isocitrate

substrate: DL-isocitrate


substrate_name: citrate

substrate: citrate


organism: Neomoorella thermoacetica

substrate_name: [methyl-Co(III) corrinoid Fe-S protein]

proof_lines: kcat below 0.02 s(-1), in 1 mM Tris-HCl (pH 7.6), at 25°C

substrate: [methyl-Co(III) corrinoid Fe-S protein]


substrate_name: hydroxocobalamin

substrate: hydroxocobalamin


proof_lines: using hydroxocobalamin as cosubstrate, in 1 mM Tris-HCl (pH 7.6), at 25°C

proof_lines: using [Co(I) corrinoid Fe-S protein] as cosubstrate, in 1 mM Tris-HCl (pH 7.6), at 25°C


substrate_name: methylcobalamin

substrate: methylcobalamin


proof_lines: Km above 0.2 mM, using [Co(I) corrinoid Fe-S protein] as cosubstrate, in 1 mM Tris-HCl (pH 7.6), at 25°C


organism: Mycobacterium tuberculosis

substrate_name: dUMP

substrate: dUMP


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: trans-aconitate 3-methyltransferase

organism: Saccharomyces cerevisiae

enzyme: trans-aconitate 3-methyltransferase


substrate_name: isopropylmaleate

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

substrate: isopropylmaleate


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


enzyme_display_name: norbelladine O-methyltransferase

organism: Narcissus aff. pseudonarcissus MK-2014

substrate_name: norbelladine

enzyme: norbelladine O-methyltransferase

substrate: norbelladine


substrate_name: N-methylnorbelladine

substrate: N-methylnorbelladine


substrate_name: dopamine

substrate: dopamine


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


substrate_name: [Co(I) corrinoid Fe-S protein]

proof_lines: mutant enzyme N199A, in 0.1 M potassium succinate, pH 5.0, 60 mM NaCl, at 25°C

substrate: [Co(I) corrinoid Fe-S protein]


proof_lines: wild type enzyme, in 0.1 M potassium succinate, pH 5.0, 60 mM NaCl, at 25°C


organism: Sorghum bicolor


enzyme_display_name: UniProt P31939

organism: Homo sapiens

substrate_name: (6R,6S)-10-formyltetrahydrofolic acid

enzyme: UniProt P31939

substrate: (6R,6S)-10-formyltetrahydrofolic acid


enzyme_display_name: 2-methylserine hydroxymethyltransferase

organism: Paracoccus sp

substrate_name: alpha-methyl-L-serine

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

enzyme: 2-methylserine hydroxymethyltransferase

substrate: alpha-methyl-L-serine


substrate_name: tetrahydrofolate

substrate: tetrahydrofolate


substrate_name: uracil1498 in 16S rRNA

proof_lines: pH 7.0, 37°C, the Km-value for 16S rRNA is measured as a Km for the physiological substrate, 30S ribosomal subunit

substrate: uracil1498 in 16S rRNA


organism: Bacillus cereus

proof_lines: pH 7, 37°C, cosubstrate malonyl-[acyl-carrier protein]


substrate_name: malonyl-[acyl-carrier protein]

substrate: malonyl-[acyl-carrier protein]


enzyme_display_name: aspartate carbamoyltransferase

substrate_name: L-asparagine

enzyme: aspartate carbamoyltransferase

substrate: L-asparagine


assay_conditions_summary: pH 8; 295.15 K; cofactor NADPH

proof_lines: in 50 mM Tris-HCl pH 8.0, 10 mM MgCl2, 2 mM NADPH, 0.5 mM FAD, at 22°C


enzyme_display_name: thiopurine S-methyltransferase

organism: Mus musculus

enzyme: thiopurine S-methyltransferase


substrate_name: N-acetyl-S-farnesyl-L-cysteine

proof_lines:
at pH 7.5 and 25°C
apparent value, at pH 7.5 and 30°C

substrate: N-acetyl-S-farnesyl-L-cysteine


organism: Nicotiana tabacum

substrate_name: 24-methylene lophenol

substrate: 24-methylene lophenol


substrate_name: Cycloartenol

substrate: Cycloartenol


enzyme_display_name: gibberellin 3beta-dioxygenase

organism: Cucurbita maxima

substrate_name: gibberellin a15

enzyme: gibberellin 3beta-dioxygenase

substrate: gibberellin a15


organism: Equus caballus

substrate_name: vitamin K1 2,3-epoxide

substrate: vitamin K1 2,3-epoxide


enzyme_display_name: UniProt Q837U7

organism: Enterococcus faecalis

substrate_name: L-ornithine

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

enzyme: UniProt Q837U7

substrate: L-ornithine


enzyme_display_name: UniProt P84010

organism: Ovis aries

proof_lines:
Raw SKiD Env: Temp=37°C, pH=9
Raw SKiD Env: Temp=37°C, pH=8.2

enzyme: UniProt P84010


enzyme_display_name: UniProt P00480

substrate_name: Carbamoyl phosphate

enzyme: UniProt P00480

substrate: Carbamoyl phosphate


enzyme_display_name: formate dehydrogenase-N

substrate_name: formate

enzyme: formate dehydrogenase-N

substrate: formate


substrate_name: uracil1939 in 23S rRNA

proof_lines: the enzymatic activity of RumA is measured for a 12-mer 5' RNA segment (1932?1943) lacking the 3' hairpin

proof_lines: pH 7.5, 37°C, uracil1939 in 40-nucleotide 23 S rRNA fragment (nucleotide 1930?1969)

proof_lines: the enzymatic activity of RumA is measured for a 37-mer RNA (1932?1968) segment lacking the 3' hairpin

substrate: uracil1939 in 23S rRNA


substrate_name: homocysteine

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

substrate: homocysteine


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


enzyme_display_name: ribonucleoside-diphosphate reductase

substrate_name: CDP

proof_lines: activity of subunit B1 assayed in the presence of an excess of subunit B2

proof_lines: activity of subunit B2 assayed in the presence of an excess of subunit B1

enzyme: ribonucleoside-diphosphate reductase

substrate: CDP


enzyme_display_name: DNA oxidative demethylase

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

enzyme: DNA oxidative demethylase


enzyme_display_name: taurine dioxygenase

substrate_name: palmitoyl[zDHHC6 protein]

proof_lines:
commercially available substrate
deuterated substrate

enzyme: taurine dioxygenase

substrate: palmitoyl[zDHHC6 protein]


enzyme_display_name: UniProt P34736

organism: Scheffersomyces stipitis

substrate_name: D-xylulose 5-phosphate

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

enzyme: UniProt P34736

substrate: D-xylulose 5-phosphate


substrate_name: sedoheptulose 7-phosphate

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

substrate: sedoheptulose 7-phosphate


substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


enzyme_display_name: UniProt Q8MPM3

organism: Leishmania mexicana

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

enzyme: UniProt Q8MPM3


enzyme_display_name: UniProt A0A0I9QGZ2

organism: Geobacillus stearothermophilus

substrate_name: L-glyceraldehyde

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

enzyme: UniProt A0A0I9QGZ2

substrate: L-glyceraldehyde


substrate_name: L-lactaldehyde

smiles: CC(C=O)O

substrate: L-lactaldehyde


proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=50°C, pH=7.5


substrate_name: L-erythrulose

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

proof_lines:
Raw SKiD Env: Temp=50°C, pH=7.5
Raw SKiD Env: Temp=25°C, pH=7.5

substrate: L-erythrulose


enzyme_display_name: UniProt P23254

enzyme: UniProt P23254


substrate_name: Hydroxypyruvate

substrate: Hydroxypyruvate


substrate_name: glyceraldehyde 3-phosphate

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

substrate: glyceraldehyde 3-phosphate


enzyme_display_name: UniProt P29401

substrate_name: D-ribose 5-phosphate

enzyme: UniProt P29401

substrate: D-ribose 5-phosphate


enzyme_display_name: UniProt P9WG25

enzyme: UniProt P9WG25


substrate_name: fructose 6-phosphate

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

substrate: fructose 6-phosphate


substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


enzyme_display_name: Transketolase

substrate_name: D-ribose 5-phosphate (at 25 degrees Celsius)

enzyme: Transketolase


enzyme_display_name: transaldolase

organism: Dictyostelium discoideum

enzyme: transaldolase


substrate_name: D-erythrose 4-phosphate

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

substrate: D-erythrose 4-phosphate


enzyme_display_name: UniProt Q9HKI3

organism: Thermoplasma acidophilum

enzyme: UniProt Q9HKI3


organism: Escherichia coli

substrate_name: nucleoside32 in EctRNAGln1(UUG)

proof_lines: pH 9.0, 37°C, recombinant wild-type enzyme

substrate: nucleoside32 in EctRNAGln1(UUG)


substrate_name: glutaredoxin

substrate: glutaredoxin


enzyme_display_name: alkanesulfonate monooxygenase

substrate_name: octanesulfonate

enzyme: alkanesulfonate monooxygenase

substrate: octanesulfonate


enzyme_display_name: superoxide dismutase

substrate_name: Unknown

enzyme: superoxide dismutase

substrate: Unknown


enzyme_display_name: mercury(II) reductase

enzyme: mercury(II) reductase


organism: Herpes simplex virus

proof_lines:
derived from slope
derived from intercept


smiles: O=O


substrate_name: vitamin K1 2,3-epoxide

substrate: vitamin K1 2,3-epoxide


enzyme_display_name: nitric-oxide synthase (NADPH)

substrate_name: L-arginine

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

proof_lines: in presence of tetrahydrobiopterin and L-arginine

enzyme: nitric-oxide synthase (NADPH)

substrate: L-arginine


enzyme_display_name: phytanoyl-CoA dioxygenase

enzyme: phytanoyl-CoA dioxygenase


enzyme_display_name: cuproxidase

substrate_name: Cu+

assay_conditions_summary: pH 5

proof_lines: pH 5.0, temperature not specified in the publication

enzyme: cuproxidase

substrate: Cu+


enzyme_display_name: indoleamine 2,3-dioxygenase

substrate_name: tryptamine

enzyme: indoleamine 2,3-dioxygenase

substrate: tryptamine


enzyme_display_name: transketolase

organism: Saccharomyces cerevisiae

enzyme: transketolase


substrate_name: D-xylulose 5-phosphate

substrate: D-xylulose 5-phosphate


enzyme_display_name: ferroxidase

organism: Homo sapiens

substrate_name: Ferrous ammonium sulfate

enzyme: ferroxidase

substrate: Ferrous ammonium sulfate


enzyme_display_name: sterol 14alpha-demethylase

substrate_name: lanosterol

enzyme: sterol 14alpha-demethylase

substrate: lanosterol


organism: Gallus sp.

substrate_name: N,N'-dimethyl-p-phenylenediamine

substrate: N,N'-dimethyl-p-phenylenediamine


enzyme_display_name: arachidonate 12-lipoxygenase

substrate_name: arachidonic acid

smiles: CCCCCC=CCC=CCC=CCC=CCCCC(=O)O

proof_lines: cytosolic hp-12LOX, pH 7.4, recombinant wild-type enzyme

proof_lines: membrane hp-12LOX, pH 7.4, recombinant wild-type enzyme

enzyme: arachidonate 12-lipoxygenase

substrate: arachidonic acid


enzyme_display_name: arachidonate 15-lipoxygenase

substrate_name: linoleic acid

smiles: CCCCCC=CCC=CCCCCCCCC(=O)O

proof_lines:
recombinant enzyme
pH 7.5, 20°C
pH 7.5, 30°C

enzyme: arachidonate 15-lipoxygenase

substrate: linoleic acid


enzyme_display_name: UniProt P77488

enzyme: UniProt P77488


substrate_name: pyruvate

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=37°C, pH=8

substrate: pyruvate


substrate_name: D-glyceraldehyde 3-phosphate

substrate: D-glyceraldehyde 3-phosphate


substrate_name: D-glyceraldehyde

substrate: D-glyceraldehyde


enzyme_display_name: UniProt P23970

organism: Bacillus subtilis

enzyme: UniProt P23970


enzyme_display_name: mRNA N6-methyladenine demethylase

substrate_name: N3-methylthymine in single-stranded DNA

proof_lines: pH and temperature not specified in the publication

enzyme: mRNA N6-methyladenine demethylase

substrate: N3-methylthymine in single-stranded DNA


enzyme_display_name: ribonucleoside-diphosphate reductase

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

enzyme: ribonucleoside-diphosphate reductase


substrate_name: linoleate

smiles: CCCCCC=CCC=CCCCCCCCC(=O)[O-]

proof_lines: fully deuterated, in the presence of 13-(S)-hydroxyoctadecadienoic acid

substrate: linoleate


enzyme_display_name: thymidylate synthase (FAD)

organism: Helicobacter pylori

enzyme: thymidylate synthase (FAD)


substrate_name: L-tryptophan

substrate: L-tryptophan


substrate_name: o-Dianisidine

substrate: o-Dianisidine


substrate_name: Unknown

proof_lines: enzyme hVKOR, microsomal hVKOR not subjected to detergent solubilization, endoplasmic reticulum-enriched microsomes, in presence of glutahione with substrate KO, pH and temperature not specified in the publication

substrate: Unknown


enzyme_display_name: UniProt Q5FAK7

organism: Pseudomonas aeruginosa

substrate_name: acetyl-CoA

enzyme: UniProt Q5FAK7

substrate: acetyl-CoA


enzyme_display_name: UniProt Q8N159

enzyme: UniProt Q8N159


substrate_name: L-glutamate

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

substrate: L-glutamate


enzyme_display_name: Arginine biosynthesis bifunctional protein ArgJ, chloroplastic

organism: Citrullus lanatus

substrate_name: N(2)-acetyl-L-ornithine (at pH 7.0)

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

substrate: N(2)-acetyl-L-ornithine (at pH 7.0)


substrate_name: L-glutamate (at pH 7.0)

enzyme: Arginine biosynthesis bifunctional protein ArgJ, chloroplastic

substrate: L-glutamate (at pH 7.0)


enzyme_display_name: UniProt Q17427

organism: Caenorhabditis elegans

substrate_name: D-glucosamine 6-phosphate

enzyme: UniProt Q17427

substrate: D-glucosamine 6-phosphate


enzyme_display_name: UniProt Q5CPU3

organism: Cryptosporidium parvum

enzyme: UniProt Q5CPU3


enzyme_display_name: UniProt Q96EK6

substrate_name: propionyl-CoA

enzyme: UniProt Q96EK6

substrate: propionyl-CoA


enzyme_display_name: UniProt O86309

organism: Mycolicibacterium smegmatis

enzyme: UniProt O86309


substrate_name: hydralazine

substrate: hydralazine


enzyme_display_name: UniProt P18440

enzyme: UniProt P18440


substrate_name: 5-aminosalicylic acid

substrate: 5-aminosalicylic acid


enzyme_display_name: UniProt Q5YYQ3

organism: Nocardia farcinica

substrate_name: isoniazid

enzyme: UniProt Q5YYQ3

substrate: isoniazid


substrate_name: hypoxia-inducible factor2alpha C-terminal oxygen-dependent degradation domain-L-proline


enzyme_display_name: ferroxidase

substrate_name: N,N'-dimethyl-p-phenylenediamine

enzyme: ferroxidase

substrate: N,N'-dimethyl-p-phenylenediamine


enzyme_display_name: nitric-oxide synthase (NADPH)

proof_lines: irreversible inactivation of endothelial isoform after preincubation

proof_lines: at lower concentration than the Ki value agmatine leads to time-, concentration-, NADPH- and calmodulin-dependent inhibition of the neuronal enzyme in presence of calmodulin

enzyme: nitric-oxide synthase (NADPH)


assay_conditions_summary: pH 7; 303.15 K; buffer pH 7

proof_lines:
pH 7.0, 30°C, 0.2 M phosphate buffer
pH 7.0, 30°C, 0.2 M acetate buffer
pH 5.2, 30°C, 0.0133 M phosphate buffer


enzyme_display_name: phytanoyl-CoA dioxygenase

enzyme: phytanoyl-CoA dioxygenase


enzyme_display_name: FAD-dependent urate hydroxylase

organism: Klebsiella pneumoniae

substrate_name: Urate

assay_conditions_summary: pH 8; cofactor NADH

proof_lines:
pH 8.0, 1.5 mM NADH as cosubstrate
pH 8.0, cosubstrate 1.5 mM NADH

enzyme: FAD-dependent urate hydroxylase

substrate: Urate


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


enzyme_display_name: trimethylamine monooxygenase

substrate_name: N,N,N-trimethylamine

smiles: CN(C)C

proof_lines: the Km for isoform FMO3 determined in human liver microsomes ranges from 0.013.to 0.0548 mM, at pH 7.4 and 22°C

proof_lines: recombinant isoform FMO3, at pH 7.4 and 22°C

enzyme: trimethylamine monooxygenase

substrate: N,N,N-trimethylamine


enzyme_display_name: UniProt P47934

organism: Mus musculus

substrate_name: hexanoyl-CoA

enzyme: UniProt P47934

substrate: hexanoyl-CoA


enzyme_display_name: UniProt P43155

substrate_name: L-carnitine

enzyme: UniProt P43155

substrate: L-carnitine


substrate_name: carnitine

substrate: carnitine


substrate_name: CoA

substrate: CoA


enzyme_display_name: acetyl-CoA C-acetyltransferase

organism: Bacopa monnieri

substrate_name: acetoacetyl-CoA

enzyme: acetyl-CoA C-acetyltransferase

substrate: acetoacetyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


enzyme_display_name: UniProt P76461

enzyme: UniProt P76461


enzyme_display_name: Acetyl-CoA acetyltransferase erg10B, cytosolic

organism: Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10)

substrate_name: acetoacetyl-CoA (in law salt conditions)


enzyme_display_name: UniProt Q2KIR7

organism: Bos taurus

substrate_name: glycine

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

enzyme: UniProt Q2KIR7

substrate: glycine


substrate_name: benzoyl-CoA

substrate: benzoyl-CoA


enzyme_display_name: ent-kaurene monooxygenase

organism: Malus sp.

substrate_name: Unknown

enzyme: ent-kaurene monooxygenase

substrate: Unknown


enzyme_display_name: coenzyme F420 hydrogenase

organism: Methanosarcina barkeri

smiles: [HH]

proof_lines: 37°C, pH 7.2, cosubstrate: oxidized coenzyme F420

proof_lines: 37°C, pH 7.2, cosubstrate: oxidized methyl viologen

enzyme: coenzyme F420 hydrogenase


substrate_name: oxidized coenzyme F420

substrate: oxidized coenzyme F420


organism: Methanothermobacter thermautotrophicus


enzyme_display_name: ribonucleoside-diphosphate reductase

substrate_name: CDP

assay_conditions_summary: cofactor ATP

proof_lines: CDP reduction in the absence of allosteric effectors

proof_lines: CDP reduction in the presence of 1 mM ATP

proof_lines: CDP reduction in the presence of 0.2 mM ATP

enzyme: ribonucleoside-diphosphate reductase

substrate: CDP


enzyme_display_name: gibberellin 2beta-dioxygenase

organism: Lathyrus oleraceus

substrate_name: gibberellin 20

proof_lines: in 100 mM Tris-HCl pH 7.9 containing 4 mM ascorbate, 4 mM DTT, 4 mM 2-oxoglutarate, 0.5 mM FeSO4, 2 mg/ml bovine serum albumin and 1 mg/ml catalase

enzyme: gibberellin 2beta-dioxygenase

substrate: gibberellin 20


substrate_name: Ngamma-hydroxy-L-arginine

proof_lines:
nonlinear regression analysis
Eadie-Hofstee graph
25°C, with tetrahydrobiopterin

substrate: Ngamma-hydroxy-L-arginine


enzyme_display_name: cysteine dioxygenase

substrate_name: L-cysteine

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

proof_lines: presence of 0.1 mol Fe2+, absence of EDTA. Cysteine sulfinic acid content is determined by ion-paired reverse-phase chromatopraphy using UV detection at 215 nm.

enzyme: cysteine dioxygenase

substrate: L-cysteine


enzyme_display_name: thiopurine S-methyltransferase

enzyme: thiopurine S-methyltransferase


enzyme_display_name: UniProt P35610

organism: Homo sapiens

substrate_name: pregnenolone

enzyme: UniProt P35610

substrate: pregnenolone


substrate_name: vitamin K1 2,3-epoxide

substrate: vitamin K1 2,3-epoxide


enzyme_display_name: cytochrome-c3 hydrogenase

organism: Nitratidesulfovibrio vulgaris

substrate_name: [Fe] hydrogenase-cytochrome Hmc complex

proof_lines:
pH 7.0, electron transfer kinetics
25°C, pH 7.0

enzyme: cytochrome-c3 hydrogenase

substrate: [Fe] hydrogenase-cytochrome Hmc complex


enzyme_display_name: catechol 1,2-dioxygenase

organism: Nocardia sp.

substrate_name: catechol

proof_lines:
immobilized enzyme
free enzyme

enzyme: catechol 1,2-dioxygenase

substrate: catechol


substrate_name: GDP

substrate: GDP


enzyme_display_name: UniProt Q401L4

organism: Entamoeba histolytica

substrate_name: L-serine

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

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=-----, pH=8

enzyme: UniProt Q401L4

substrate: L-serine


enzyme_display_name: UniProt P43886

organism: Haemophilus influenzae

enzyme: UniProt P43886


enzyme_display_name: UniProt P9WPZ3

organism: Mycobacterium tuberculosis

enzyme: UniProt P9WPZ3


enzyme_display_name: chlorite O2-lyase

organism: Nitrospira defluvii

substrate_name: Chlorite

smiles: [O-]Cl=O

enzyme: chlorite O2-lyase

substrate: Chlorite


enzyme_display_name: ferroxidase

organism: Ovis aries

enzyme: ferroxidase


proof_lines: pH 7.0, 30°C, recombinant wild-type enzyme


enzyme_display_name: nitric-oxide synthase (NADPH)

substrate_name: L-arginine

proof_lines:
detrusor
urethra
pH 7.4, 30°C

enzyme: nitric-oxide synthase (NADPH)

substrate: L-arginine


enzyme_display_name: UniProt P9WNG5

substrate_name: malonyl-CoA

enzyme: UniProt P9WNG5

substrate: malonyl-CoA


organism: Cavia porcellus

substrate_name: acetyl-CoA

substrate: acetyl-CoA


enzyme_display_name: caffeate O-methyltransferase

organism: Populus trichocarpa

proof_lines: isoform COMT2, in 50 mM Tris-HCl, pH 7.5, at 30°C

enzyme: caffeate O-methyltransferase


organism: Oryza sativa


organism: Pseudomonas aeruginosa

proof_lines:
pH 7.5, 25°C
pH 7.5, 25°C, in presence of ascorbate


enzyme_display_name: mercury(II) reductase

substrate_name: NADPH

assay_conditions_summary: pH 7.3; 298.15 K; cofactor NADPH

proof_lines:
in presence of 1 mM cysteine
25°C, pH 7.3

enzyme: mercury(II) reductase

substrate: NADPH


enzyme_display_name: protocatechuate 3,4-dioxygenase

substrate_name: Unknown

enzyme: protocatechuate 3,4-dioxygenase

substrate: Unknown


enzyme_display_name: nitrite reductase (NO-forming)

substrate_name: ferricytochrome c551

proof_lines: recombinant Y10F mutant enzyme, at pH 6.2 and 27°C

enzyme: nitrite reductase (NO-forming)

substrate: ferricytochrome c551


organism: Pseudomonas chlororaphis

substrate_name: nitrite

proof_lines:
pH 7.0, electron donor azurin
pH 7.0, electron donor benzyl viologen

substrate: nitrite


enzyme_display_name: homogentisate 1,2-dioxygenase

organism: Pseudomonas fluorescens

substrate_name: homogentisate

assay_conditions_summary: pH 6

enzyme: homogentisate 1,2-dioxygenase

substrate: homogentisate


enzyme_display_name: UniProt Q9H7Z6

enzyme: UniProt Q9H7Z6


enzyme_display_name: UniProt Q93UV0

organism: Sphingomonas paucimobilis

substrate_name: caproyl-CoA

enzyme: UniProt Q93UV0

substrate: caproyl-CoA


organism: Pseudomonas putida


enzyme_display_name: benzoate 1,2-dioxygenase

substrate_name: benzoate

assay_conditions_summary: pH 6.8; cofactor NADH

proof_lines: at pH 6.8 temperature not specified in the publication

proof_lines: in the presence of saturating amounts of NADH-cytochrome c reductase

enzyme: benzoate 1,2-dioxygenase

substrate: benzoate


proof_lines: multi-walled carbon nanotube-immobilized enzyme, at pH 10.0 and 60°C


enzyme_display_name: 2-oxoadipate dioxygenase/decarboxylase

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

enzyme: 2-oxoadipate dioxygenase/decarboxylase


proof_lines:
6°C, pH 7.3
in presence of 1 mM cysteine
1 mM cysteine, 25°C, pH 7.3


organism: Pseudomonas sp.

substrate_name: L-glutamate

assay_conditions_summary: cofactor FMN

proof_lines:
5-deazaFMN reconstituted enzyme
FMN reconstituted enzyme

substrate: L-glutamate


substrate_name: ammonia

smiles: N

substrate: ammonia


substrate_name: Hg

smiles: [Hg]

substrate: Hg


enzyme_display_name: trans-cinnamate 4-monooxygenase

organism: Pyrus x bretschneideri

substrate_name: trans-cinnamate

enzyme: trans-cinnamate 4-monooxygenase

substrate: trans-cinnamate


enzyme_display_name: UniProt K9MUA0

organism: Malus domestica

enzyme: UniProt K9MUA0


proof_lines:
at pH 7.0
at pH 8.4


enzyme_display_name: gentisate 1,2-dioxygenase

organism: Ralstonia solanacearum

enzyme: gentisate 1,2-dioxygenase


enzyme_display_name: cysteine dioxygenase

organism: Rattus norvegicus

substrate_name: L-cysteine

assay_conditions_summary: pH 6.1; 310.15 K; buffer the presence of 62.5 mM Mes

proof_lines: assay standart conditions are: the enzyme is incubated at 37°C in the presence of 62.5 mM Mes buffer (pH 6.1), 0.3 mM ferrous sulfate, 0.0125 mM bathocuproine disulfonate and 1.2 mM cysteine

enzyme: cysteine dioxygenase

substrate: L-cysteine


organism: Homo sapiens

substrate_name: beta-D-glucosamine

substrate: beta-D-glucosamine


enzyme_display_name: UniProt Q51405

substrate_name: neomycin E

enzyme: UniProt Q51405

substrate: neomycin E


substrate_name: kanamycin B

substrate: kanamycin B


substrate_name: neomycin

substrate: neomycin


substrate_name: sisomycin

substrate: sisomycin


substrate_name: kanamycin A

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.6
Raw SKiD Env: Temp=25°C, pH=6.6

substrate: kanamycin A


substrate_name: ribostamycin

substrate: ribostamycin


substrate_name: tobramycin

substrate: tobramycin


enzyme_display_name: UniProt Q44057

organism: Acinetobacter haemolyticus

substrate_name: arbekacin

enzyme: UniProt Q44057

substrate: arbekacin


substrate_name: dibekacin

substrate: dibekacin


substrate_name: sisomicin

substrate: sisomicin


substrate_name: butirosin A

substrate: butirosin A


substrate_name: gentamicin

substrate: gentamicin


substrate_name: tobramicin

substrate: tobramicin


substrate_name: neomycin C

substrate: neomycin C


substrate_name: amikacin

substrate: amikacin


substrate_name: isepamicin

substrate: isepamicin


enzyme_display_name: UniProt Q43899

organism: Acinetobacter baumannii

enzyme: UniProt Q43899


enzyme_display_name: UniProt P19096

organism: Mus musculus

substrate_name: crotonyl-CoA

enzyme: UniProt P19096

substrate: crotonyl-CoA


substrate_name: phenylacetyl-CoA

substrate: phenylacetyl-CoA


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


substrate_name: methylmalonyl-CoA

substrate: methylmalonyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


substrate_name: succinyl-CoA

substrate: succinyl-CoA


substrate_name: octanoyl-CoA

substrate: octanoyl-CoA


substrate_name: L-cysteine

proof_lines: 20% cross-linked wild-type enzyme, pH 9.1, temperature not specified in the publication

proof_lines: 60% cross-linked wild-type enzyme, pH 7.7, temperature not specified in the publication

proof_lines: not cross-linked wild-type enzyme, pH 7.7, temperature not specified in the publication

substrate: L-cysteine


enzyme_display_name: aminoglycoside 6'-N-acetyltransferase

organism: Enterococcus faecium

enzyme: aminoglycoside 6'-N-acetyltransferase


substrate_name: neomycin

substrate: neomycin


substrate_name: kanamycin A

substrate: kanamycin A


substrate_name: neamine

substrate: neamine


substrate_name: acetyl-CoA

assay_conditions_summary: pH 6; 310.15 K; cofactor CoA

substrate: acetyl-CoA


substrate_name: tobramycin

substrate: tobramycin


proof_lines:
pH 6.0, 37°C, wild-type enzyme
wild-type enzyme


substrate_name: ribostamycin

substrate: ribostamycin


substrate_name: kanamycin B

substrate: kanamycin B


substrate_name: amikacin

substrate: amikacin


substrate_name: neomycin C

substrate: neomycin C


substrate_name: propionyl-CoA

substrate: propionyl-CoA


substrate_name: sisomicin

substrate: sisomicin


substrate_name: gentamicin B

substrate: gentamicin B


substrate_name: butirosin

substrate: butirosin


substrate_name: netilmicin

substrate: netilmicin


substrate_name: dibekacin

substrate: dibekacin


enzyme_display_name: alcohol O-acetyltransferase

organism: Fragaria x ananassa

substrate_name: eugenol

enzyme: alcohol O-acetyltransferase

substrate: eugenol


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: hexanoyl-CoA

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

proof_lines: cosubstrate cinnamyl alcohol, pH 7.5, 30°C

substrate: hexanoyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


organism: Streptomyces noursei


substrate_name: neomycin B

substrate: neomycin B


substrate_name: kanamycin A

substrate: kanamycin A


substrate_name: n-propionyl-CoA

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

substrate: n-propionyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: lividomycin A

substrate: lividomycin A


substrate_name: n-butyryl-CoA

substrate: n-butyryl-CoA


substrate_name: malonyl-CoA

substrate: malonyl-CoA


substrate_name: ribostamycin

substrate: ribostamycin


substrate_name: neamine

substrate: neamine


substrate_name: neomycin C

substrate: neomycin C


organism: Petunia x hybrida

substrate_name: coniferyl alcohol

assay_conditions_summary: pH 7.5; 293.15 K; cofactor CoA

proof_lines: recombinant protein with acetyl-CoA, pH 6.0, 20°C

proof_lines: apparent KM value of recombinant protein with acetyl-CoA, pH 7.5, 20°C

substrate: coniferyl alcohol


substrate_name: benzyl alcohol

proof_lines: recombinant protein with acetyl-CoA, pH 7.5, 20°C

substrate: benzyl alcohol


proof_lines: recombinant protein with 2-phenylethanol, pH 7.5, 20°C

proof_lines: recombinant protein with benzyl alcohol, pH 7.5, 20°C

proof_lines: recombinant protein with coniferyl alcohol, pH 7.5, 20°C


substrate_name: alpha-D-glucosamine

substrate: alpha-D-glucosamine


assay_conditions_summary: cofactor CoA


organism: uncultured bacterium

substrate_name: kanamycin

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

column_label: Table 1 columns enzyme=meta-AAC0020, substrate=kanamycin; kinetic parameter rows K0.5 (uM), kcat (s^-1), kcat/K0.5 (M^-1 s^-1, x10^4), and H.

normalized_value_unit_evidence: kcat 0.207 s^-1; K0.5 0.3464 mM (not paper-labeled Km); kcat/K0.5 0.6 s^-1 mM^-1. Expected row has Km 0.346 mM and kcat_over_km 0.598266 s^-1 mM^-1, but the primary metric labels are K0.5 and kcat/K0.5.

row_label: meta-AAC0020; substrate column kanamycin

table_label: Table 1. Steady State Kinetic Parameters for the Wild-Type meta-AAC Proteins and AAC(3)-Ib

substrate: kanamycin


substrate_name: tobramycin

proof_lines:
wild-type enzyme
pH 6.0, 37°C, wild-type enzyme

substrate: tobramycin


substrate_name: gentamicin C

substrate: gentamicin C


organism: Rosa hybrid cultivar


proof_lines:
cosubstrate: benzyl alcohol
cosubstrate: geraniol
cosubstrate: phenylethanol


substrate_name: geraniol

smiles: CC(=CCCC(=CCO)C)C

substrate: geraniol


substrate_name: phenyl ethanol

substrate: phenyl ethanol


organism: Musa x paradisiaca


substrate_name: Isoamylalcohol

smiles: CC(C)CCO

substrate: Isoamylalcohol


organism: Mycobacterium tuberculosis

substrate_name: amikacin

substrate: amikacin


organism: Cymbopogon martini

smiles: CCC=CCCO


substrate_name: (-)-beta-citronellol

smiles: CC(CCC=C(C)C)CCO

substrate: (-)-beta-citronellol


substrate_name: Heptanol

smiles: CCCCCCCO

substrate: Heptanol


substrate_name: Octanol

smiles: CCCCCCCCO

substrate: Octanol


substrate_name: Nonanol

smiles: CCCCCCCCCO

substrate: Nonanol


organism: Hanseniaspora valbyensis

substrate_name: 2-phenylethyl alcohol

substrate: 2-phenylethyl alcohol


substrate_name: isoamyl alcohol

substrate: isoamyl alcohol


substrate_name: Unknown

proof_lines:
versus acetyl-CoA
versus N-acetyl-alpha-D-glucosamine
versus glusosamine, no detergents added

substrate: Unknown


enzyme_display_name: aminoglycoside 3-N-acetyltransferase

organism: Corynebacterium striatum

substrate_name: dibekacin

proof_lines: recombinant His-tagged enzyme, pH 6.0, 37°C

enzyme: aminoglycoside 3-N-acetyltransferase

substrate: dibekacin


substrate_name: kanamycin B

substrate: kanamycin B


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: ethanol

smiles: CCO

substrate: ethanol


substrate_name: Propanol

smiles: CCCO

substrate: Propanol


substrate_name: methanol

smiles: CO

substrate: methanol


substrate_name: butanol

smiles: CCCCO

substrate: butanol


substrate_name: benzyl alcohol

substrate: benzyl alcohol


substrate_name: geraniol

substrate: geraniol


proof_lines:
cosubstrate heptanol, pH 7.5, 30°C
cosubstrate eugenol, pH 7.5, 30°C
cosubstrate octanol, pH 7.5, 30°C


substrate_name: Pentanol

smiles: CCCCCO

substrate: Pentanol


substrate_name: Hexanol

smiles: CCCCCCO

substrate: Hexanol


substrate_name: sisomicin

column_label: Table 1 columns enzyme=meta-AAC0020, substrate=sisomicin; kinetic parameter rows K0.5 (uM), kcat (s^-1), kcat/K0.5 (M^-1 s^-1, x10^4), and H.

normalized_value_unit_evidence: kcat 2.42 s^-1; K0.5 0.038 mM (not paper-labeled Km); kcat/K0.5 64 s^-1 mM^-1. Expected row has Km 0.038 mM and kcat_over_km 63.6842 s^-1 mM^-1, but the primary metric labels are K0.5 and kcat/K0.5.

row_label: meta-AAC0020; substrate column sisomicin

substrate: sisomicin


substrate_name: tobramycin

column_label: Table 1 columns enzyme=meta-AAC0020, substrate=tobramycin; kinetic parameter rows K0.5 (uM), kcat (s^-1), kcat/K0.5 (M^-1 s^-1, x10^4), and H.

normalized_value_unit_evidence: kcat 1.2 s^-1; K0.5 0.028 mM (not paper-labeled Km); kcat/K0.5 43 s^-1 mM^-1. Expected row has Km 0.028 mM and kcat_over_km 42.8571 s^-1 mM^-1, but the primary metric labels are K0.5 and kcat/K0.5.

row_label: meta-AAC0020; substrate column tobramycin

substrate: tobramycin


substrate_name: gentamycin

column_label: Table 1 columns enzyme=meta-AAC0020, substrate=gentamicin; kinetic parameter rows K0.5 (uM), kcat (s^-1), kcat/K0.5 (M^-1 s^-1, x10^4), and H.

normalized_value_unit_evidence: kcat 1.17 s^-1; K0.5 0.022 mM (not paper-labeled Km); kcat/K0.5 52 s^-1 mM^-1. Expected row has Km 0.022 mM and kcat_over_km 53.1818 s^-1 mM^-1, but the primary metric labels are K0.5 and kcat/K0.5.

row_label: meta-AAC0020; substrate column gentamicin

substrate: gentamycin


substrate_name: kanamycin

substrate: kanamycin


column_label: Table 1 columns enzyme=meta-AAC0020, substrate=acetyl-CoA; kinetic parameter rows K0.5 (uM), kcat (s^-1), kcat/K0.5 (M^-1 s^-1, x10^4), and H.

normalized_value_unit_evidence: kcat 1.51 s^-1; K0.5 0.021 mM (not paper-labeled Km); kcat/K0.5 69 s^-1 mM^-1. Expected row has Km 0.021 mM and kcat_over_km 71.9048 s^-1 mM^-1, but the primary metric labels are K0.5 and kcat/K0.5.

row_label: meta-AAC0020; substrate column acetyl-CoA


organism: Mycobacteroides abscessus

assay_conditions_summary: 298.15 K; cofactor CoA

proof_lines: 25°C, pH not specified in the publication


organism: Rattus norvegicus

substrate_name: dolichol

substrate: dolichol


substrate_name: poly-L-Lys

proof_lines:
pH 7.5, 37°C
competitive inhibition

substrate: poly-L-Lys


organism: Staphylococcus aureus

substrate_name: Unknown

proof_lines: pH 6.9, 37°C, inhibition of the reaction with neamine

substrate: Unknown


enzyme_display_name: UniProt A0QY29

organism: Mycolicibacterium smegmatis

substrate_name: propionyl-CoA

enzyme: UniProt A0QY29

substrate: propionyl-CoA


substrate_name: octopamine

substrate: octopamine


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: histamine

substrate: histamine


enzyme_display_name: UniProt P9WFK7

enzyme: UniProt P9WFK7


organism: Sus scrofa


enzyme_display_name: fatty-acid synthase system

enzyme: fatty-acid synthase system


enzyme_display_name: Maltose O-acetyltransferase

organism: Escherichia coli (strain K12)

substrate_name: maltotriose

proof_lines: Acetylates glucose, maltose, mannose, galactose, and fructose with a decreasing relative rate of 1, 0.55, 0.20, 0.07, 0.04.

enzyme: Maltose O-acetyltransferase

substrate: maltotriose


substrate_name: Acetyl-CoA; L-cysteine-S-conjugate

substrate: Acetyl-CoA; L-cysteine-S-conjugate


organism: Escherichia coli

substrate_name: Ciprofloxacin

substrate: Ciprofloxacin


substrate_name: Norfloxacin

substrate: Norfloxacin


substrate_name: kanamycin B

substrate: kanamycin B


substrate_name: neomycin B

substrate: neomycin B


enzyme_display_name: UniProt Q9GPZ4

organism: Leishmania major

substrate_name: myristoyl-CoA

enzyme: UniProt Q9GPZ4

substrate: myristoyl-CoA


enzyme_display_name: UniProt Q9UVX3

organism: Aspergillus fumigatus

substrate_name: myristoleoyl-CoA

enzyme: UniProt Q9UVX3

substrate: myristoleoyl-CoA


enzyme_display_name: quinate O-hydroxycinnamoyltransferase

organism: Solanum lycopersicum

substrate_name: coumaroyl-CoA

enzyme: quinate O-hydroxycinnamoyltransferase

substrate: coumaroyl-CoA


substrate_name: caffeoyl-CoA

substrate: caffeoyl-CoA


substrate_name: chlorogenic acid

substrate: chlorogenic acid


substrate_name: CoA

substrate: CoA


substrate_name: glucose

substrate: glucose


substrate_name: maltose

substrate: maltose


enzyme_display_name: fatty-acid synthase

substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n Malonyl-CoA; 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n NADPH; Acetyl-CoA; H+

assay_conditions_summary: cofactor NADPH

enzyme: fatty-acid synthase


organism: Homo sapiens


organism: Acinetobacter baumannii

substrate_name: 2'-N-ethyl netilmicin

substrate: 2'-N-ethyl netilmicin


organism: Saccharomyces cerevisiae

substrate_name: Acetyl-CoA; 3-Methylbutanol

substrate: Acetyl-CoA; 3-Methylbutanol


organism: Gallus gallus

substrate_name: Acetyl-CoA; H+; 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n NADPH; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n Malonyl-CoA


substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n Malonyl-CoA; Acetyl-CoA; 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n NADPH


organism: Anthoceros agrestis

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA

proof_lines: cosubstrate shikimate, Hanes-Woolf plot, pH 7.0, 30°C

proof_lines: cosubstrate shikimate, Michaelis-Menten plot, pH 7.0, 30°C

proof_lines: cosubstrate 3-hydroxyanthranilate, Michaelis-Menten plot, pH 9.0, 30°C


proof_lines: cosubstrate 2,3-dihydroxybenzoate, Hanes-Woolf plot, pH 7.0, 30°C


substrate_name: shikimate

proof_lines: cosubstrate 4-coumaroyl-CoA, Michaelis-Menten plot, pH 7.0, 30°C

proof_lines: cosubstrate 4-coumaroyl-CoA, Hanes-Woolf plot, pH 7.0, 30°C

proof_lines: cosubstrate caffeoyl-CoA, Michaelis-Menten plot, pH 7.0, 30°C

substrate: shikimate


assay_conditions_summary: pH 9; 303.15 K; cofactor CoA

proof_lines: cosubstrate 4-coumaroyl-CoA, Michaelis-Menten plot, pH 9.0, 30°C

proof_lines: cosubstrate 4-coumaroyl-CoA, Hanes-Woolf plot, pH 9.0, 30°C

proof_lines: cosubstrate caffeoyl-CoA, Michaelis-Menten plot, pH 9.0, 30°C


proof_lines: cosubstrate caffeoyl-CoA, Hanes-Woolf plot, pH 7.0, 30°C


organism: Malus sylvestris


substrate_name: feruloyl-CoA

substrate: feruloyl-CoA


substrate_name: quinate

substrate: quinate


substrate_name: Acetyl-CoA; beta-D-Glucosamine

assay_conditions_summary: pH 6.5; 310.15 K; cofactor CoA

proof_lines: substrate 1-[4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-propionyl-glycylamino]-beta-D-glucosamine, pH 6.5, 37°C

substrate: Acetyl-CoA; beta-D-Glucosamine


substrate_name: Unknown

substrate: Unknown


organism: Columba sp.

substrate_name: H+; Acetyl-CoA; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n Malonyl-CoA; 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n NADPH


organism: Fragaria x ananassa

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row 2-Phenyl ethanol; columns Km (mM), Kcat, Kcat/Km; cells 4.32, 49.6, 11.4

raw_value_unit_evidence: 2-Phenyl ethanol: Km=4.32 mM; kcat=49.6 s^-1; kcat/Km=11.4 s^-1 mM^-1

row_label: 2-Phenyl ethanol


substrate_name: acetyl-CoA

column_label: Table 3. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols in combination with acetyl-CoA at variable concentrations; row Cinnamyl alcohol; columns Km (uM), Kcat, Kcat/Km; cells 77, 3890, 50.53

raw_value_unit_evidence: Cinnamyl alcohol co-substrate / acetyl-CoA varied: Km=77 uM; kcat=3890 s^-1; kcat/Km=50.53 s^-1 uM^-1

substrate: acetyl-CoA