sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13255 and applied mutation signature Y21G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 1: Summary of Kinetic Parameters for the Methylation of Glycine by the Recombinant Rat GNMT and Its Mutants (J. Am. Chem. Soc. 2016, 138(28):9158-9165), Table 1, data row labelled Y21G in the GNMT column, AdoMet substrate block; column 'kcat (min-1)' = 0.93; column 'Km (uM)' under the AdoMet spanner = 696; column 'kcat/Km (M-1 s-1)' under the AdoMet spanner = 22.3; the same data line prints the glycine spanner pair as 'Km (mM)' = 33.6 and 'kcat/Km (M-1 s-1)' = 0.46.

raw_value_unit_evidence: Table 1, Table 1, data row labelled Y21G in the GNMT column, AdoMet substrate block: printed kcat (min-1) cell 0.93; printed Km (uM) cell 696; printed kcat/Km (M-1 s-1) cell 22.3.


enzyme_display_name: glycine N-methyltransferase

organism: Rattus norvegicus

substrate_name: S-adenosyl-L-methionine

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13255 and applied mutation signature Y21S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

mutation_type: substitution

column_label: Table 1: Summary of Kinetic Parameters for the Methylation of Glycine by the Recombinant Rat GNMT and Its Mutants (J. Am. Chem. Soc. 2016, 138(28):9158-9165), Table 1, data row labelled Y21S in the GNMT column, AdoMet substrate block; column 'kcat (min-1)' = 0.65; column 'Km (uM)' under the AdoMet spanner = 803; column 'kcat/Km (M-1 s-1)' under the AdoMet spanner = 13.6; the same data line prints the glycine spanner pair as 'Km (mM)' = 23.4 and 'kcat/Km (M-1 s-1)' = 0.46.

raw_value_unit_evidence: Table 1, Table 1, data row labelled Y21S in the GNMT column, AdoMet substrate block: printed kcat (min-1) cell 0.65; printed Km (uM) cell 803; printed kcat/Km (M-1 s-1) cell 13.6.

data_origin: experimental

enzyme: glycine N-methyltransferase

substrate: S-adenosyl-L-methionine

status: corrected

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13255 and applied mutation signature Y21T with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 1: Summary of Kinetic Parameters for the Methylation of Glycine by the Recombinant Rat GNMT and Its Mutants (J. Am. Chem. Soc. 2016, 138(28):9158-9165), Table 1, data row labelled Y21T in the GNMT column, AdoMet substrate block; column 'kcat (min-1)' = 0.81; column 'Km (uM)' under the AdoMet spanner = 1136; column 'kcat/Km (M-1 s-1)' under the AdoMet spanner = 11.9; the same data line prints the glycine spanner pair as 'Km (mM)' = 22.9 and 'kcat/Km (M-1 s-1)' = 0.59.

raw_value_unit_evidence: Table 1, Table 1, data row labelled Y21T in the GNMT column, AdoMet substrate block: printed kcat (min-1) cell 0.81; printed Km (uM) cell 1136; printed kcat/Km (M-1 s-1) cell 11.9.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13255 and applied mutation signature Y21V with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 1: Summary of Kinetic Parameters for the Methylation of Glycine by the Recombinant Rat GNMT and Its Mutants (J. Am. Chem. Soc. 2016, 138(28):9158-9165), Table 1, data row labelled Y21V in the GNMT column, AdoMet substrate block; column 'kcat (min-1)' = 0.58; column 'Km (uM)' under the AdoMet spanner = 582; column 'kcat/Km (M-1 s-1)' under the AdoMet spanner = 16.7; the same data line prints the glycine spanner pair as 'Km (mM)' = 38.8 and 'kcat/Km (M-1 s-1)' = 0.25.

raw_value_unit_evidence: Table 1, Table 1, data row labelled Y21V in the GNMT column, AdoMet substrate block: printed kcat (min-1) cell 0.58; printed Km (uM) cell 582; printed kcat/Km (M-1 s-1) cell 16.7.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

source_db: uniprot

verification_status: unverified

kcat_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

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

status: unverified

source: uniprot


smiles: CN(C)CCO


enzyme_display_name: fatty-acid O-methyltransferase

organism: Mycobacterium marinum

substrate_name: 3-hydroxydecanoic acid

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q31A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

smiles: CCCCCCCC(O)CC(=O)O

proof_lines:
MmFAMT
Q31A
3-hydroxydecanoic acid

enzyme: fatty-acid O-methyltransferase

substrate: 3-hydroxydecanoic acid


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q26A/Q31A to reconstruct the assayed variant sequence.

column_label: Table 1; Wild-Type 3-OH-C10 row; KM, kcat, kcat/KM columns.

row_label: Wild-Type 3-OH-C10 row

table_label: Petronikolou and Nair 2015, Chemistry & Biology, Biochemical Studies of Mycobacterial Fatty Acid Methyltransferase; kinetic table evidence


substrate_name: 3-hydroxyoctanoic acid

smiles: CCCCCC(O)CC(=O)O

column_label: Table 1; Wild-Type 3-OH-C8 row; KM, kcat, kcat/KM columns.

row_label: Wild-Type 3-OH-C8 row

substrate: 3-hydroxyoctanoic acid


substrate_name: Decanoic acid

smiles: CCCCCCCCCC(=O)O

column_label: Table 1; Wild-Type C10 row; KM, kcat, kcat/KM columns.

row_label: Wild-Type C10 row

substrate: Decanoic acid


substrate_name: octanoic acid

smiles: CCCCCCCC(=O)O

proof_lines:
MmFAMT
Q31A
octanoic acid

substrate: octanoic acid


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q26A/Q31A/V211L/L212V to reconstruct the assayed variant sequence.

column_label: Table 1; Wild-Type C8 row; KM, kcat, kcat/KM columns.

row_label: Wild-Type C8 row


column_label: Table 1; Wild-Type SAM row; KM, kcat, kcat/KM columns.

row_label: Wild-Type SAM row


organism: Mus musculus

source_db: brenda

verification_status: verified

assay_conditions_summary: pH 9

column_label: PubMed abstract states the apparent Km values for S-adenosyl-L-methionine were 20 and 400-500 microM for conversion of PE to PME, and 5 microM and 40 microM for conversion of PME to PC.

raw_value_unit_evidence: Km raw_value=20 raw_unit=microM

row_label: murine thymocyte phospholipid N-methyltransferase conversion of PE to PME with S-adenosyl-L-methionine

table_label: PubMed abstract PMID 3872629

status: verified

source: brenda


enzyme_display_name: UniProt P13255

source_db: skid

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

sequence_source: multiple

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.2
Raw SKiD Env: Temp=37°C, pH=7.4

source_databases_merged: skid uniprot

enzyme: UniProt P13255

source: skid


substrate_name: Gly

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

substrate: Gly


enzyme_display_name: 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplastic

organism: Arabidopsis thaliana

column_label: Table II row AtMS3, column Km for 5-CH3-H4PteGlu5.

normalized_value_unit_evidence: 17 uM normalizes to 0.017 mM.

raw_value_unit_evidence: Table II reports AtMS3 Km for 5-CH3-H4PteGlu5 as 17 +/- 3 uM.

row_label: AtMS3; Km for 5-CH3-H4PteGlu5

table_label: Table II, Kinetic properties of B12-independent MS isoforms from Arabidopsis


column_label: Table II row AtMS1, column Km for 5-CH3-H4PteGlu5.

normalized_value_unit_evidence: 60 uM normalizes to 0.060 mM.

raw_value_unit_evidence: Table II reports AtMS1 Km for 5-CH3-H4PteGlu5 as 60 +/- 7 uM.

row_label: AtMS1; Km for 5-CH3-H4PteGlu5


substrate_name: phosphatidylethanolamine (PE)

smiles: CC(=O)OCC(COP(=O)(O)OCCN)OC(=O)C

column_label: Abstract reports for the PEMT reactions, the apparent Km values for PE and S-adenosylmethionine were 57 microM and 110 microM, respectively.

raw_value_unit_evidence: Km raw_value=57 microM raw_unit=microM

row_label: Saccharomyces cerevisiae PEMT / phosphatidylethanolamine

table_label: PubMed XML abstract PMID 2198947

substrate: phosphatidylethanolamine (PE)


enzyme_display_name: Glycine N-methyltransferase

enzyme: Glycine N-methyltransferase


substrate_name: glycine

substrate: glycine


organism: Homo sapiens

proof_lines:
human glycine N-methyltransferase
neutral pH kinetics
S-adenosylmethionine


organism: Oryctolagus cuniculus

source_databases_merged: brenda uniprot


substrate_name: S-adenosylmethionine

substrate: S-adenosylmethionine


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


substrate_name: phosphatidylethanolamine

substrate: phosphatidylethanolamine


organism: Phaseolus sp.

substrate_name: homocysteine

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

substrate: homocysteine


substrate_name: S-methylmethionine

substrate: S-methylmethionine


enzyme_display_name: benzoate 4-monooxygenase

organism: Aspergillus niger

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

enzyme: benzoate 4-monooxygenase

substrate: NADPH


substrate_name: benzoate

proof_lines: reconstituted enzyme system consisting of benzoate 4-hydroxylase, cytochrome P450 reductase, NADPH and dilauroylphosphatidylcholine

substrate: benzoate


organism: Saccharomyces cerevisiae


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines: inhibition with respect to S-adenosylmethionine

proof_lines: inhibition with respect to phosphatidylethanolamine

substrate: Unknown


enzyme_display_name: cysteine dioxygenase

organism: Bacillus subtilis

substrate_name: L-cysteine

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

proof_lines: YubC, measurement of cysteine sulfinic acid production is done by high-performance liquid chromatography

enzyme: cysteine dioxygenase

substrate: L-cysteine


substrate_name: phosphatidyl-N-methylethanolamine

substrate: phosphatidyl-N-methylethanolamine


substrate_name: S-adenosyl-L-homocysteine

substrate: S-adenosyl-L-homocysteine


enzyme_display_name: UniProt P04818

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P04818


substrate_name: dUMP

proof_lines:
Raw SKiD Env: Temp=37°C, pH=-----
Raw SKiD Env: Temp=22°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

substrate: dUMP


enzyme_display_name: UniProt P0A884

organism: Escherichia coli

enzyme: UniProt P0A884


enzyme_display_name: UniProt Q834R3

organism: Enterococcus faecalis

enzyme: UniProt Q834R3


organism: Bos taurus

substrate_name: vitamin K1 2,3-epoxide

substrate: vitamin K1 2,3-epoxide


enzyme_display_name: nitric-oxide synthase (NADPH)

substrate_name: Calmodulin

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

enzyme: nitric-oxide synthase (NADPH)

substrate: Calmodulin


enzyme_display_name: xanthine oxidase

enzyme: xanthine oxidase


enzyme_display_name: Indolethylamine N-methyltransferase

substrate_name: dimethyl selenide

smiles: C[Se]C

enzyme: Indolethylamine N-methyltransferase

substrate: dimethyl selenide


substrate_name: dimethyl sulfide

smiles: CSC

substrate: dimethyl sulfide


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


enzyme_display_name: ferroxidase

substrate_name: NADH

assay_conditions_summary: pH 6; 303.15 K; cofactor NADH

proof_lines: pH 6.0, 30°C, presence of triflupromazine

proof_lines: pH 6.0, 30°C, presence of levomepromazine

proof_lines: pH 6.0, 30°C, presence of chlorpromazine

enzyme: ferroxidase

substrate: NADH


enzyme_display_name: peptide-aspartate beta-dioxygenase

substrate_name: first growth factor-like domain-L-aspartate

proof_lines: substrate is of human protein S, 56 kDa protein

proof_lines: substrate is of human protein S with an asparagine replacing the aspartic acid at position 18, 56 kDa protein

proof_lines: substrate is of human protein S, 52 kDa protein

enzyme: peptide-aspartate beta-dioxygenase


enzyme_display_name: ribonucleoside-diphosphate reductase

proof_lines: N-alpha-acetyl heptapeptide, identical to the last seven amino acids of R2 subunit C-terminus from mouse enzyme

enzyme: ribonucleoside-diphosphate reductase


substrate_name: allopurinol

substrate: allopurinol


enzyme_display_name: UniProt Q8SR66

organism: Encephalitozoon cuniculi

substrate_name: GDP

enzyme: UniProt Q8SR66

substrate: GDP


enzyme_display_name: mercury(II) reductase

organism: Bacillus sp. (in: firmicutes)

proof_lines: recombinant catalytic core, 25°C, pH 7.3

proof_lines: recombinant catalytic core, presence of N-terminal sequence NmerA, 25°C, pH 7.3

enzyme: mercury(II) reductase


substrate_name: Ngamma-hydroxy-L-arginine

substrate: Ngamma-hydroxy-L-arginine


substrate_name: dibromoacetonitrile

smiles: C(#N)C(Br)Br

substrate: dibromoacetonitrile


proof_lines: in 50 mM potassium phosphate (pH 7.2), 50 mM Tris-Cl (pH 7.2) containing 0.1 mM MgSO4, 10 mM dithiothreitol and 2 mM L-homocysteine at 37°C


substrate_name: L-homocysteine

substrate: L-homocysteine


substrate_name: S-adenosylmethionine

proof_lines:
at pH 8.5
at pH 10

substrate: S-adenosylmethionine


enzyme_display_name: caffeate O-methyltransferase

organism: Leucaena leucocephala

enzyme: caffeate O-methyltransferase


enzyme_display_name: Caffeic acid 3-O-methyltransferase

organism: Zea mays

substrate_name: tricetin

enzyme: Caffeic acid 3-O-methyltransferase

substrate: tricetin


substrate_name: luteolin

substrate: luteolin


substrate_name: pterin

proof_lines: cell-associated enzyme, determined in intact cell monolayers

substrate: pterin


enzyme_display_name: protocatechuate 3,4-dioxygenase

organism: Buttiauxella sp. S19-1

enzyme: protocatechuate 3,4-dioxygenase


organism: Canis lupus familiaris


enzyme_display_name: sterol 14alpha-demethylase

organism: Candida albicans

substrate_name: lanosterol

proof_lines: pH and temperature not specified in the publication

enzyme: sterol 14alpha-demethylase

substrate: lanosterol


organism: Nicotiana tabacum


substrate_name: esculetin

substrate: esculetin


substrate_name: homocatechol

substrate: homocatechol


substrate_name: 5-hydroxyferulic acid

substrate: 5-hydroxyferulic acid


substrate_name: caffeic acid

substrate: caffeic acid


substrate_name: Hydrocaffeic acid

substrate: Hydrocaffeic acid


substrate_name: Protocatechuic aldehyde

substrate: Protocatechuic aldehyde


substrate_name: catechol

substrate: catechol


substrate_name: chlorogenic acid

substrate: chlorogenic acid


substrate_name: protocatechuic acid

substrate: protocatechuic acid


organism: Vanilla planifolia

substrate_name: 5-hydroxyferulic acid ethyl ester

substrate: 5-hydroxyferulic acid ethyl ester


substrate_name: caffeic acid ethyl ester

substrate: caffeic acid ethyl ester


substrate_name: caffeoyl aldehyde

substrate: caffeoyl aldehyde


organism: Beta vulgaris

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


substrate_name: Unknown

substrate: Unknown


organism: Triticum aestivum


substrate_name: caffeoyl alcohol

substrate: caffeoyl alcohol


substrate_name: 5-hydroxyconiferyl alcohol

substrate: 5-hydroxyconiferyl alcohol


enzyme_display_name: licodione 2'-O-methyltransferase

organism: Glycyrrhiza echinata

enzyme: licodione 2'-O-methyltransferase


substrate_name: licodione

substrate: licodione


organism: Petroselinum crispum


proof_lines: reaction with bergaptol or 5-hydroxyxanthotoxin


substrate_name: bergaptol

substrate: bergaptol


organism: Conioselinum anthriscoides


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


substrate_name: caffeic acid methyl ester

substrate: caffeic acid methyl ester


organism: Bambusa sp.

substrate_name: 5-hydroxyferulic acid

substrate: 5-hydroxyferulic acid


substrate_name: caffeic acid

substrate: caffeic acid


organism: Trigonella foenum-graecum


enzyme_display_name: thiopurine S-methyltransferase

organism: Homo sapiens

proof_lines:
recombinant enzyme, expressed in yeast
isoenzyme II
cell lysate

enzyme: thiopurine S-methyltransferase


proof_lines:
recombinant enzyme, expressed in yeast
isoenzyme II
isoenzyme I


organism: Cyberlindnera jadinii


enzyme_display_name: trimethylamine monooxygenase

substrate_name: Benzydamine

assay_conditions_summary: pH 7.4; 310.15 K; buffer in 0.1 M tricine

proof_lines: in in 0.1 M tricine buffer, pH 7.4, at 37°C

enzyme: trimethylamine monooxygenase

substrate: Benzydamine


substrate_name: myricetin

substrate: myricetin


substrate_name: methyl gallate

substrate: methyl gallate


proof_lines:
cell lysate
isoenzyme II
Molt-F4 cell


organism: Rehmannia glutinosa


organism: Medicago sativa

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N324H/M130L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A162T with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L136Y to reconstruct the assayed variant sequence.


substrate_name: Protocatechuic aldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N131K to reconstruct the assayed variant sequence.

substrate: Protocatechuic aldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N131D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N324Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H183K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F172Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N131E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N131L to reconstruct the assayed variant sequence.


substrate_name: protocatechuic acid

substrate: protocatechuic acid


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M130L with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


organism: Arabidopsis thaliana

substrate_name: quercetin

proof_lines: pH 7.5, temperature not specified in the publication

substrate: quercetin


organism: Lolium arundinaceum

column_label: Table 1 | Kinetic properties of recombinant tall fescue COMT protein; row 5-Hydroxyferulic acid; column Km (microM): 10.89 +/- 1.52 microM; normalized Km=0.01089 mM.

normalized_value_unit_evidence: Km paper=0.01089 mM after exact conversion of 10.89 microM by dividing by 1000.

raw_value_unit_evidence: Table 1 row 5-Hydroxyferulic acid: Km 10.89 +/- 1.52 microM.

row_label: 5-Hydroxyferulic acid


column_label: Table 1 | Kinetic properties of recombinant tall fescue COMT protein; row Caffeoyl aldehyde; column Km (microM): 14.78 +/- 1.44 microM; normalized Km=0.01478 mM.

normalized_value_unit_evidence: Km paper=0.01478 mM after exact conversion of 14.78 microM by dividing by 1000.

raw_value_unit_evidence: Table 1 row Caffeoyl aldehyde: Km 14.78 +/- 1.44 microM.

row_label: Caffeoyl aldehyde


column_label: Table 1 | Kinetic properties of recombinant tall fescue COMT protein; row 5-Hydroxyconiferaldehyde; column Km (microM): 18.52 +/- 2.48 microM; normalized Km=0.01852 mM.

normalized_value_unit_evidence: Km paper=0.01852 mM after exact conversion of 18.52 microM by dividing by 1000.

raw_value_unit_evidence: Table 1 row 5-Hydroxyconiferaldehyde: Km 18.52 +/- 2.48 microM.


column_label: Table 1 | Kinetic properties of recombinant tall fescue COMT protein; row Caffeoyl alcohol; column Km (microM): 27.30 +/- 3.40 microM; normalized Km=0.02730 mM.

normalized_value_unit_evidence: Km paper=0.02730 mM after exact conversion of 27.30 microM by dividing by 1000.

raw_value_unit_evidence: Table 1 row Caffeoyl alcohol: Km 27.30 +/- 3.40 microM.

row_label: Caffeoyl alcohol


column_label: Table 1 | Kinetic properties of recombinant tall fescue COMT protein; row Caffeic acid; column Km (microM): 49.74 +/- 4.88 microM; normalized Km=0.04974 mM.

normalized_value_unit_evidence: Km paper=0.04974 mM after exact conversion of 49.74 microM by dividing by 1000.

raw_value_unit_evidence: Table 1 row Caffeic acid: Km 49.74 +/- 4.88 microM.

row_label: Caffeic acid


column_label: Table 1 | Kinetic properties of recombinant tall fescue COMT protein; row 5-Hydroxyconiferyl alcohol; column Km (microM): 67.77 +/- 4.62 microM; normalized Km=0.06777 mM.

normalized_value_unit_evidence: Km paper=0.06777 mM after exact conversion of 67.77 microM by dividing by 1000.

raw_value_unit_evidence: Table 1 row 5-Hydroxyconiferyl alcohol: Km 67.77 +/- 4.62 microM.

row_label: 5-Hydroxyconiferyl alcohol


proof_lines:
wild type
wild-type enzyme


enzyme_display_name: Flavone 3'-O-methyltransferase 1

organism: Oryza sativa subsp. japonica

substrate_name: 5-hydroxyferulate (at pH 7.5 and 30 degrees Celsius)

proof_lines: Measured at pH 7.5 and 37 degrees Celsius for all experiments.

enzyme: Flavone 3'-O-methyltransferase 1


substrate_name: caffealdehyde (at pH 7.5 and 30 degrees Celsius)


substrate_name: 5-hydroxyconiferaldehyde (at pH 7.5 and 30 degrees Celsius)


substrate_name: caffeyl alcohol (at pH 7.5 and 30 degrees Celsius)


substrate_name: 5-hydroxyconiferyl alcohol (at pH 7.5 and 30 degrees Celsius)


organism: Rattus norvegicus


substrate_name: S-adenosyl-L-methionine


organism: Oryza sativa

proof_lines: when caffeic acid is supplied at a constant concentration of 1 mM


proof_lines: when S-adenosyl-L-methionine is supplied at a constant concentration of 1 mM


column_label: Table 2 columns Substrate and Km (uM); row Quercetin 1; expected Km matches the table value.

raw_value_unit_evidence: Table 2 row Quercetin 1 reports Km = 61.8 uM.

row_label: Quercetin 1

table_label: Table 2: Substrate specificity of purified recombinant protein ROMT-9


substrate_name: luteolin

column_label: Table 2 columns Substrate and Km (uM); row Luteolin 5; expected Km matches the table value.

raw_value_unit_evidence: Table 2 row Luteolin 5 reports Km = 61.9 uM.

row_label: Luteolin 5

substrate: luteolin


substrate_name: eriodictyol

column_label: Table 2 columns Substrate and Km (uM); row Eriodictyol 4; expected Km matches the table value.

raw_value_unit_evidence: Table 2 row Eriodictyol 4 reports Km = 62.0 uM.

row_label: Eriodictyol 4

substrate: eriodictyol


proof_lines:
isozyme I
isozyme II
recombinant enzyme

source_databases_merged: brenda skid


enzyme_display_name: tocopherol C-methyltransferase

organism: Vinca minor

enzyme: tocopherol C-methyltransferase

substrate: S-adenosyl-L-methionine


substrate_name: picrinine

substrate: picrinine


substrate_name: N-acetylserotonin

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

raw_value_unit_evidence: Table 2 Table 2 row WT reports Km 0.74 mM; kcat 2.94 s^-1; kcat/Km 3.99 x 10^3 s^-1 M^-1.

row_label: Table 2 row WT

substrate: N-acetylserotonin


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

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

raw_value_unit_evidence: Table 2 Table 2 row Q310L reports Km 0.36 mM; kcat 4.76 s^-1; kcat/Km 13.11 x 10^3 s^-1 M^-1.

row_label: Table 2 row Q310L


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C296F to reconstruct the assayed variant sequence.

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

raw_value_unit_evidence: Table 2 Table 2 row C296F reports Km 0.58 mM; kcat 5.41 s^-1; kcat/Km 9.37 x 10^3 s^-1 M^-1.

row_label: Table 2 row C296F


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

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

raw_value_unit_evidence: Table 2 Table 2 row V314T reports Km 0.58 mM; kcat 11.32 s^-1; kcat/Km 19.53 x 10^3 s^-1 M^-1.

row_label: Table 2 row V314T


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique 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).

row_label: Table 2 row C296F-Q310L-V314T


enzyme_display_name: UniProt Q944H0

assay_conditions_summary: pH 8

enzyme: UniProt Q944H0


substrate_name: N-methylethanolamine phosphate

smiles: CNCCOP(=O)(O)O

substrate: N-methylethanolamine phosphate


substrate_name: Ethanolamine phosphate

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

substrate: Ethanolamine phosphate


substrate_name: N,N-dimethylethanolamine phosphate

smiles: CN(C)CCOP(=O)(O)O

substrate: N,N-dimethylethanolamine phosphate


enzyme_display_name: UniProt Q9FR44

enzyme: UniProt Q9FR44


enzyme_display_name: caffeoyl-CoA O-methyltransferase

substrate_name: caffeoyl-CoA

enzyme: caffeoyl-CoA O-methyltransferase

substrate: caffeoyl-CoA


organism: Euglena gracilis

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


organism: Streptomyces antibioticus


organism: Capsicum annuum


substrate_name: gamma-tocopherol

substrate: gamma-tocopherol


substrate_name: delta-tocopherol

substrate: delta-tocopherol


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

organism: Coptis japonica

substrate_name: (S)-scoulerine

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

substrate: (S)-scoulerine


organism: Spinacia oleracea


substrate_name: S-adenosyl-L-methionine (at pH 9.4)

proof_lines: kcat is 0.036 min(-1) for m7GpppAm capped mRNA (PubMed:31279659). kcat is 0.34 min(-1) for m7GpppAm dinucleotide (PubMed:31279659). kcat is 1.76 min(-1) for capped mRNA analog (at pH 5.4) (PubMed:33428944). kcat is 1.44 min(-1) for S-adenos

substrate: S-adenosyl-L-methionine (at pH 9.4)


organism: Eschscholzia californica

substrate_name: (S)-canadine

substrate: (S)-canadine


organism: Anopheles gambiae


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


organism: Angelica dahurica

substrate_name: bergaptol

substrate: bergaptol


organism: Chlamydomonas reinhardtii

proof_lines: in 50 mM HEPES (pH 7.5), 5 mM dithiothreitol, temperature not specified in the publication


enzyme_display_name: macrocin O-methyltransferase

organism: Streptomyces fradiae

proof_lines:
lactenocin as substrate
macrocin as substrate

enzyme: macrocin O-methyltransferase


organism: Medicago sativa

column_label: Table 3; 5-Hydroxyconiferaldehyde row; K_m (uM) column; raw K_m value 1.8 uM.

raw_value_unit_evidence: Table 3 reports 5-Hydroxyconiferaldehyde K_m = 1.8 uM.

row_label: 5-Hydroxyconiferaldehyde row; K_m column

table_label: PMID 11169195, Table 3: Kinetic properties of purified recombinant alfalfa COMT


substrate_name: 5-hydroxyconiferyl alcohol

column_label: Table 3; 5-Hydroxyconiferyl alcohol row; K_m (uM) column; raw K_m value 3.8 uM.

raw_value_unit_evidence: Table 3 reports 5-Hydroxyconiferyl alcohol K_m = 3.8 uM.

row_label: 5-Hydroxyconiferyl alcohol row; K_m column

substrate: 5-hydroxyconiferyl alcohol


substrate_name: 5-hydroxyferulic acid

column_label: Table 3; 5-Hydroxyferulic acid row; K_m (uM) column; raw K_m value 6.8 uM.

raw_value_unit_evidence: Table 3 reports 5-Hydroxyferulic acid K_m = 6.8 uM.

row_label: 5-Hydroxyferulic acid row; K_m column

substrate: 5-hydroxyferulic acid


substrate_name: caffeoyl aldehyde

column_label: Table 3; Caffeoyl aldehyde row; K_m (uM) column; raw K_m value 6.9 uM.

raw_value_unit_evidence: Table 3 reports Caffeoyl aldehyde K_m = 6.9 uM.

row_label: Caffeoyl aldehyde row; K_m column

substrate: caffeoyl aldehyde


substrate_name: caffeoyl alcohol

column_label: Table 3; Caffeoyl alcohol row; K_m (uM) column; raw K_m value 11.5 uM.

normalized_value_unit_evidence: 11.5 uM = 0.0115 mM; expected rounded value is 0.012 mM.

raw_value_unit_evidence: Table 3 reports Caffeoyl alcohol K_m = 11.5 uM.

row_label: Caffeoyl alcohol row; K_m column

substrate: caffeoyl alcohol


organism: Catharanthus roseus

proof_lines: kcat is 2.47 sec(-1) for 2,3-dihydrotabersonine. kcat is 5.4 sec(-1) for S-adenosyl-L-methionine.


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Rauvolfia serpentina

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


substrate_name: picrinine

substrate: picrinine


enzyme_display_name: UniProt Q948P7

substrate_name: (RS)-coclaurine

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

enzyme: UniProt Q948P7

substrate: (RS)-coclaurine


substrate_name: heliamine

substrate: heliamine


substrate_name: (S)-N-methylcoclaurine

substrate: (S)-N-methylcoclaurine


enzyme_display_name: jasmonate O-methyltransferase

organism: Brassica rapa subsp. oleifera

enzyme: jasmonate O-methyltransferase


substrate_name: jasmonate

substrate: jasmonate


organism: Argemone platyceras

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


substrate_name: S-adenosylmethionine

proof_lines: with (S)-norlaudanosoline as cosubstrate

substrate: S-adenosylmethionine


substrate_name: (R,S)-norlaudanosoline

substrate: (R,S)-norlaudanosoline


substrate_name: (R,S)-laudanosoline

substrate: (R,S)-laudanosoline


proof_lines:
isozyme II
isozyme I


enzyme_display_name: inositol 4-methyltransferase

organism: Vigna umbellata

enzyme: inositol 4-methyltransferase


substrate_name: myo-inositol

substrate: myo-inositol


organism: Arabidopsis thaliana

substrate_name: [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine


organism: Nicotiana rustica


organism: Mus musculus


organism: Stephania tetrandra

substrate_name: (S)-norcoclaurine

substrate: (S)-norcoclaurine


organism: Pseudomonas denitrificans (nom. rej.)


enzyme_display_name: UniProt Q5UVJ4

organism: Helicobacter pylori

enzyme: UniProt Q5UVJ4


substrate_name: dUMP

substrate: dUMP


organism: Tribolium castaneum

proof_lines: kcat is 3.3 min(-1) for S-adenosyl-L-methionine. kcat is 1.4 min(-1) for biotin-S-farnesyl-L-cysteine (BFC).


organism: Lathyrus oleraceus

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


organism: Carapichea ipecacuanha

substrate_name: N-deacetylisoipecoside

proof_lines: kcat is 11.3x10(-3) sec(-1) with N-deacetylisoipecoside as substrate (PubMed:20061395). kcat is 20.4x10(-3) sec(-1) with 7-O-methyl-N-deacetylisoipecoside as substrate (PubMed:20061395). kcat is 0.28x10(-3) sec(-1) with cephaeline as substr

substrate: N-deacetylisoipecoside


substrate_name: cephaeline

substrate: cephaeline


proof_lines: kcat is 0.34x10(-3) sec(-1) with N-deacetylisoipecoside as substrate (PubMed:20061395). kcat is 3.8x10(-3) sec(-1) with demethylalangiside as substrate (PubMed:20061395). kcat is 2.3x10(-3) sec(-1) with redipecamine as substrate (PubMed:200


substrate_name: demethylalangiside

substrate: demethylalangiside


enzyme_display_name: caffeate O-methyltransferase

organism: Oryza sativa

substrate_name: N-acetylserotonin

enzyme: caffeate O-methyltransferase

substrate: N-acetylserotonin


enzyme_display_name: cycloartenol 24-C-methyltransferase

enzyme: cycloartenol 24-C-methyltransferase


substrate_name: Cycloartenol

substrate: Cycloartenol


substrate_name: fecosterol

substrate: fecosterol


substrate_name: dehydropollinastanol

proof_lines: pH 7.4, 35°C, substrate: 24(28)-methylenelophenol

substrate: dehydropollinastanol


substrate_name: Zymosterol

substrate: Zymosterol


substrate_name: obtusifoliol

substrate: obtusifoliol


proof_lines:
pH 7.5, 35°C
pH 7.4, 35°C, substrate cycloartenol


organism: Populus trichocarpa

proof_lines: isoform COMT1, in 50 mM Tris-HCl, pH 7.5, at 30°C


organism: Papaver somniferum

substrate_name: (R,S)-norcoclaurine

column_label: Row PSOMT2 / (R,S)-Norcoclaurine; column K m Substrate (uM).

normalized_value_unit_evidence: Km 0.01 mM

raw_value_unit_evidence: Table 3. Kinetic parameters of PSOMT1 and PSOMT2 for various substrates and co-substrate (AdoMet), row PSOMT2 / (R,S)-Norcoclaurine: Km substrate 10 uM.

row_label: PSOMT2 / (R,S)-Norcoclaurine

substrate: (R,S)-norcoclaurine


enzyme_display_name: corydaline synthase

organism: Corydalis cava

substrate_name: S-adenosyl-L-methionine

enzyme: corydaline synthase

substrate: S-adenosyl-L-methionine


substrate_name: Berberine

substrate: Berberine


substrate_name: NADPH

substrate: NADPH


substrate_name: Unknown

substrate: Unknown


organism: Prototheca wickerhamii


substrate_name: desmosterol

substrate: desmosterol


substrate_name: lanosterol

substrate: lanosterol


substrate_name: parkeol

substrate: parkeol


enzyme_display_name: myricetin O-methyltransferase

substrate_name: caffeoyl-coenzyme A

assay_conditions_summary: cofactor CoA

proof_lines:
isoform ROMT-17
isoform ROMT-15

enzyme: myricetin O-methyltransferase

substrate: caffeoyl-coenzyme A


substrate_name: luteolin

substrate: luteolin


substrate_name: myricetin

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

substrate: myricetin


substrate_name: tricetin

substrate: tricetin


organism: Glycine max

substrate_name: 24(28)-methylene lophenol

substrate: 24(28)-methylene lophenol


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


substrate_name: Cycloartenol

substrate: Cycloartenol


organism: Chlamydomonas reinhardtii

substrate_name: 24(28)-methylene cycloartenol

substrate: 24(28)-methylene cycloartenol


enzyme_display_name: (iso)eugenol O-methyltransferase

organism: Rosa chinensis

substrate_name: eugenol

enzyme: (iso)eugenol O-methyltransferase

substrate: eugenol


substrate_name: isoeugenol

substrate: isoeugenol


organism: Helianthus annuus


substrate_name: Zymosterol

substrate: Zymosterol


substrate_name: Agnosterol

substrate: Agnosterol


substrate_name: cyclobranol

substrate: cyclobranol


organism: Paracoccidioides brasiliensis

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


organism: Pimpinella anisum


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


assay_conditions_summary: pH 7.5; 308.15 K; buffer phosphate

proof_lines:
pH 7.5, 35°C, recombinant enzyme
pH 7.5, 35°C
at 35°C in phosphate buffer at pH 8.0


organism: Zea mays

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: Flavin-dependent thymidylate synthase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: dUMP

enzyme: Flavin-dependent thymidylate synthase

substrate: dUMP


substrate_name: NADPH

substrate: NADPH


organism: Clarkia breweri

proof_lines:
plant-purified enzyme
recombinant enzyme
Raw SKiD Env: Temp=-----, pH=-----


proof_lines:
recombinant enzyme
plant-purified enzyme
Raw SKiD Env: Temp=-----, pH=-----


substrate_name: sinapyl alcohol

proof_lines: pH 7.5, 30°C, recombinant enzyme mutant MOMT8

proof_lines: pH 7.5, 30°C, recombinant enzyme mutant MOMT9

proof_lines: pH 7.5, 30°C, recombinant enzyme mutant MOMT5

substrate: sinapyl alcohol


substrate_name: coniferyl alcohol

substrate: coniferyl alcohol


enzyme_display_name: tabersonine 16-O-methyltransferase

organism: Catharanthus roseus

enzyme: tabersonine 16-O-methyltransferase


substrate_name: S-adenosyl-L-methionine with (R,S)-norcoclaurine as substrate

proof_lines: kcat is 0.08 sec(-1) with (R,S)-norcoclaurine as substrate. kcat is 0.02 sec(-1) with (R)-norprotosinomenine as substrate. kcat is 0.02 sec(-1) with (S)-norprotosinomenine as substrate. kcat is 0.03 sec(-1) with (R,S)-isoorientaline as subs


enzyme_display_name: thymidylate synthase (FAD)

organism: Thermotoga maritima

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

source_databases_merged: brenda skid uniprot

enzyme: thymidylate synthase (FAD)


organism: Asarum sieboldii

proof_lines: pH and temperature not specified in the publication


organism: Arabidopsis thaliana

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


organism: Homo sapiens


organism: Mus musculus


organism: Rattus norvegicus


organism: Nicotiana sp.

substrate_name: ribulose-1,5-bisphosphate carboxylase

substrate: ribulose-1,5-bisphosphate carboxylase


proof_lines: kcat is 2.47 sec(-1) for 2,3-dihydrotabersonine. kcat is 5.4 sec(-1) for S-adenosyl-L-methionine.


substrate_name: 5-hydroxyconiferyl aldehyde

proof_lines: pH 7.5, temperature not specified in the publication

substrate: 5-hydroxyconiferyl aldehyde


organism: Medicago sativa

proof_lines:
isozyme II
isozyme I


enzyme_display_name: Flavone 3'-O-methyltransferase 1

organism: Oryza sativa subsp. japonica

proof_lines: Measured at pH 7.5 and 37 degrees Celsius for all experiments.

enzyme: Flavone 3'-O-methyltransferase 1


enzyme_display_name: Caffeic acid 3-O-methyltransferase

enzyme: Caffeic acid 3-O-methyltransferase


enzyme_display_name: thioether S-methyltransferase

substrate_name: ethyl vinyl sulfide

smiles: CCSC=C

enzyme: thioether S-methyltransferase

substrate: ethyl vinyl sulfide


organism: Pisum sativum

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:
native enzyme
at pH 7.8 and 30°C
recombinant enzyme

source_databases_merged: sabio_rk brenda skid uniprot


organism: Carapichea ipecacuanha

substrate_name: redipecamine

proof_lines: kcat is 0.34x10(-3) sec(-1) with N-deacetylisoipecoside as substrate (PubMed:20061395). kcat is 3.8x10(-3) sec(-1) with demethylalangiside as substrate (PubMed:20061395). kcat is 2.3x10(-3) sec(-1) with redipecamine as substrate (PubMed:200

substrate: redipecamine


proof_lines: kcat is 11.3x10(-3) sec(-1) with N-deacetylisoipecoside as substrate (PubMed:20061395). kcat is 20.4x10(-3) sec(-1) with 7-O-methyl-N-deacetylisoipecoside as substrate (PubMed:20061395). kcat is 0.28x10(-3) sec(-1) with cephaeline as substr


organism: Papaver somniferum


organism: Paramecium bursaria Chlorella virus 1


proof_lines: kcat is 0.036 min(-1) for m7GpppAm capped mRNA (PubMed:31279659). kcat is 0.34 min(-1) for m7GpppAm dinucleotide (PubMed:31279659). kcat is 1.76 min(-1) for capped mRNA analog (at pH 5.4) (PubMed:33428944). kcat is 1.44 min(-1) for S-adenos


organism: Anopheles gambiae

substrate_name: biotin-S-farnesyl-L-cysteine

substrate: biotin-S-farnesyl-L-cysteine


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Spodoptera frugiperda

proof_lines: with respect to farnesylated and Rce1-proteolyzed K-Ras protein as substrate

proof_lines: with respect to S-adenosyl-L-methionine as substrate


organism: Tribolium castaneum

proof_lines: kcat is 3.3 min(-1) for S-adenosyl-L-methionine. kcat is 1.4 min(-1) for biotin-S-farnesyl-L-cysteine (BFC).


organism: Streptomyces fradiae

proof_lines:
fixed substrate macrocin
fixed substrate S-adenosyl-L-methionine
fixed substrate lactenocin


organism: Lathyrus oleraceus

substrate_name: L-Lys

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

substrate: L-Lys


organism: Clarkia breweri

substrate_name: Caffeate; S-Adenosyl-L-methionine

substrate: Caffeate; S-Adenosyl-L-methionine


organism: Ocimum basilicum


organism: Triticum aestivum


substrate_name: Eugenol; S-Adenosyl-L-methionine

substrate: Eugenol; S-Adenosyl-L-methionine


substrate_name: S-Adenosyl-L-methionine; Chavicol

substrate: S-Adenosyl-L-methionine; Chavicol


organism: Chlamydia trachomatis

substrate_name: 5,10-Methylenetetrahydrofolate; H+; NADPH; dUMP


organism: Thermotoga maritima

substrate_name: H+; 5,10-Methylenetetrahydrofolate; NADPH; dUMP


enzyme_display_name: thiopurine S-methyltransferase

organism: Homo sapiens

substrate_name: S-Adenosyl-L-methionine; Mercaptopurine

enzyme: thiopurine S-methyltransferase

substrate: S-Adenosyl-L-methionine; Mercaptopurine


organism: Mus musculus


enzyme_display_name: Trans-aconitate 3-methyltransferase

substrate_name: trans-aconitate

enzyme: Trans-aconitate 3-methyltransferase

substrate: trans-aconitate


substrate_name: itaconate

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

column_label: Abstract reports itaconate, the decarboxylation product, was recognized poorly with a Km of 44 mM.

raw_value_unit_evidence: Km raw_value=44 mM raw_unit=mM

row_label: Saccharomyces cerevisiae TMT1 trans-aconitate methyltransferase / itaconate

table_label: PubMed XML abstract PMID 11695919

substrate: itaconate


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


substrate_name: Chavicol

column_label: Table 1 row EOMT1 / Chavicol; exported value set does not exactly match the explicit table row/cell values preserved here.

raw_value_unit_evidence: Export has kcat 0.0009 and derived kcat/Km 0.12857142857142856, but Table 1 reports kcat 8.7 x 10^-4 and kcat/Km column 0.13 for EOMT1 / Chavicol.

row_label: EOMT1 / Chavicol

table_label: Table 1. Properties of Basil Phenylpropanoid OMTs

substrate: Chavicol


column_label: Table 1 row CVOMT1 / Chavicol; columns Km for substrate (6 uM) and kcat (8.0 x 10^-4 s^-1); kcat/Km calculated from normalized kcat and Km cells.

normalized_value_unit_evidence: kcat normalized value: 0.0008; normalized unit: s^-1; km normalized value: 0.006; normalized unit: mM; kcat_over_km normalized value: 0.13333333333333333; normalized unit: s^-1 mM^-1

raw_value_unit_evidence: Table 1 CVOMT1 / Chavicol: Km for substrate 6 uM; kcat 8.0 x 10^-4 s^-1; printed kcat/Km column 0.13.

row_label: CVOMT1 / Chavicol


substrate_name: Eugenol

column_label: Table 1 row EOMT1 / Eugenol; exported value set does not exactly match the explicit table row/cell values preserved here.

raw_value_unit_evidence: Export has kcat 0.003 and kcat/Km 1.0, but Table 1 reports kcat 3.1 x 10^-3 and kcat/Km column 1.23 for EOMT1 / Eugenol.

row_label: EOMT1 / Eugenol

substrate: Eugenol


substrate_name: S-Adenosyl-L-methionine

column_label: Table 1 row EOMT1 / SAM Km column in Eugenol assay row; exported value set does not exactly match the explicit table row/cell values preserved here.

raw_value_unit_evidence: Export has kcat 0.003 and kcat/Km 0.6 for SAM, but Table 1 gives kcat 3.1 x 10^-3 and SAM Km 5 uM; derived kcat/SAM-Km is 0.62 s^-1 mM^-1.

substrate: S-Adenosyl-L-methionine


column_label: Table 1 row CVOMT1 with Km for SAM column 5 uM and kcat column 8.0 x 10^-4 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: 0.0008; normalized unit: s^-1; km normalized value: 0.005; normalized unit: mM; kcat_over_km normalized value: 0.16; normalized unit: s^-1 mM^-1

raw_value_unit_evidence: Table 1 CVOMT1 row: Km for SAM 5 uM; substrate Chavicol; kcat 8.0 x 10^-4 s^-1.

row_label: CVOMT1 / SAM Km column in Chavicol assay row


substrate_name: isoeugenol

column_label: Table 1 row EOMT1 / t-Isoeugenol; exported value set does not exactly match the explicit table row/cell values preserved here.

normalized_value_unit_evidence: paper_kcat_s^-1: 0.0013; paper_km_mM: 0.01; paper_kcat_over_km_s^-1_mM^-1: 0.13

raw_value_unit_evidence: Export has kcat 0.001 and kcat/Km 0.1, but Table 1 reports kcat 1.3 x 10^-3 and kcat/Km column 0.13 for EOMT1 / t-Isoeugenol.

row_label: EOMT1 / t-Isoeugenol

substrate: isoeugenol


enzyme_display_name: Chavicol O-methyltransferase

substrate_name: chavicol

column_label: Table 1 row CVOMT1 / Chavicol; column Km for substrate (6 uM).

normalized_value_unit_evidence: km normalized value: 0.006; normalized unit: mM

raw_value_unit_evidence: Table 1 CVOMT1 / Chavicol: Km for substrate 6 uM.

enzyme: Chavicol O-methyltransferase

substrate: chavicol


enzyme_display_name: Eugenol O-methyltransferase

column_label: Table 1 row EOMT1 / Chavicol; column Km for substrate (7 uM).

normalized_value_unit_evidence: km normalized value: 0.007; normalized unit: mM

raw_value_unit_evidence: Table 1 EOMT1 / Chavicol: Km for substrate 7 uM.

enzyme: Eugenol O-methyltransferase


organism: Ammi majus

substrate_name: caffeate

proof_lines:
AmCOMT
BMT
5-hydroxyferulic acid

substrate: caffeate


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


substrate_name: 5-hydroxyferulic acid

substrate: 5-hydroxyferulic acid


substrate_name: caffeic acid methyl ester

substrate: caffeic acid methyl ester


substrate_name: caffeoyl coenzyme A

substrate: caffeoyl coenzyme A


substrate_name: esculetin

substrate: esculetin


substrate_name: daphnetin

substrate: daphnetin


enzyme_display_name: UniProt F6KV61

organism: Methanohalophilus portucalensis

enzyme: UniProt F6KV61


organism: Papaver somniferum

substrate_name: (R)-Norprotosinomenine

column_label: Row PSOMT2 / (R)-Norprotosinomenine; columns K m Substrate (uM), k cat Substrate (sec^-1), and k cat/Km Substrate (sec^-1 mM^-1).

raw_value_unit_evidence: Table 3. Kinetic parameters of PSOMT1 and PSOMT2 for various substrates and co-substrate (AdoMet), row PSOMT2 / (R)-Norprotosinomenine: Km substrate 5 uM; kcat substrate 0.02 sec^-1; kcat/Km substrate 4.1 sec^-1 mM^-1.

row_label: PSOMT2 / (R)-Norprotosinomenine

substrate: (R)-Norprotosinomenine


substrate_name: (R,S)-Norcoclaurine

column_label: Row PSOMT2 / (R,S)-Norcoclaurine; columns K m Substrate (uM), k cat Substrate (sec^-1), and k cat/Km Substrate (sec^-1 mM^-1).

raw_value_unit_evidence: Table 3. Kinetic parameters of PSOMT1 and PSOMT2 for various substrates and co-substrate (AdoMet), row PSOMT2 / (R,S)-Norcoclaurine: Km substrate 10 uM; kcat substrate 0.08 sec^-1; kcat/Km substrate 7.4 sec^-1 mM^-1.

substrate: (R,S)-Norcoclaurine


substrate_name: (S)-Norprotosinomenine

column_label: Row PSOMT2 / (S)-Norprotosinomenine; columns K m Substrate (uM), k cat Substrate (sec^-1), and k cat/Km Substrate (sec^-1 mM^-1).

raw_value_unit_evidence: Table 3. Kinetic parameters of PSOMT1 and PSOMT2 for various substrates and co-substrate (AdoMet), row PSOMT2 / (S)-Norprotosinomenine: Km substrate 5 uM; kcat substrate 0.02 sec^-1; kcat/Km substrate 4 sec^-1 mM^-1.

row_label: PSOMT2 / (S)-Norprotosinomenine

substrate: (S)-Norprotosinomenine


organism: Arabidopsis thaliana

substrate_name: N-acetylserotonin

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C296F with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

substrate: N-acetylserotonin


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).


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


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


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


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


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


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

enzyme: tocopherol C-methyltransferase

substrate: delta-tocopherol


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

enzyme: tricin synthase

substrate: tricetin


substrate_name: luteolin

substrate: luteolin


organism: Coptis japonica


enzyme_display_name: cycloartenol 24-C-methyltransferase

organism: Glycine max

substrate_name: S-Adenosyl-L-methionine; Cycloartenol

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

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

substrate_name: Isoeugenol; S-Adenosyl-L-methionine

enzyme: (iso)eugenol O-methyltransferase

substrate: Isoeugenol; S-Adenosyl-L-methionine


substrate_name: dimethyl selenide

substrate: dimethyl selenide


substrate_name: Dimethyl sulfide

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


substrate_name: S-adenosyl-L-methionine

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: 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


substrate_name: norcoclaurine

substrate: norcoclaurine


enzyme_display_name: thymidylate synthase (FAD)

organism: Paramecium bursaria Chlorella virus-1

substrate_name: dUMP

enzyme: thymidylate synthase (FAD)

substrate: dUMP


proof_lines:
5,10-methylenetetrahydrofolate
ThyX
methylene group


organism: Medicago sativa

substrate_name: isoliquiritigenin

substrate: isoliquiritigenin


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

enzyme: tRNA (cytosine38-C5)-methyltransferase

substrate: cytosine38 in Q34tRNAAsp


enzyme_display_name: UniProt P51580

organism: Homo sapiens

enzyme: UniProt P51580


enzyme_display_name: Ribosomal RNA small subunit methyltransferase E

substrate_name: 16S rRNA within 30S ribosomal subunits

substrate: 16S rRNA within 30S ribosomal subunits


organism: Lathyrus oleraceus


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

enzyme: UniProt Q9BV86


enzyme_display_name: UniProt O55060

organism: Mus musculus

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


organism: Thermotoga maritima

substrate_name: NADPH

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

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

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


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


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


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

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

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.


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

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.

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.


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

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

column_label: Table 2 (Michaelis Menten and kinetic constants for DcFA-o-MT), substrate row 'JHA I (2E, 6Z, 10cis)'; column 'Km (uM)' = 4.58; column 'Vmax (pmol/min)' = 0.05; column 'kcat (s^-1 x 10^-3)' = 0.003; column 'kcat/Km (s^-1 M^-1)' = 0.66.

normalized_value_unit_evidence: Km: printed Table 2 cell 4.58 uM; 4.58 / 1000 = 0.00458 mM; the exported value is 0.00458 mM. kcat: printed Table 2 cell 0.003 in the column headed kcat (s^-1 x 10^-3), so 0.003 x 10^-3 = 0.000003 s^-1 and no further unit conversion applies; the exported value is 0.000003 s^(-1). kcat/Km: printed Table 2 cell 0.66 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.66 / 1000 = 0.00066 s^-1 mM^-1. Closure disclosure: the exact quotient of the two printed component cells is 0.000003 / 0.00458 = 0.0006550218340611354 s^-1 mM^-1, which is the exported efficiency, and rounding that exact quotient to the two decimal places the paper prints gives 0.66 s^-1 M^-1, the printed cell, so every exported metric closes and none changes.

raw_value_unit_evidence: Table 2, substrate row 'JHA I (2E, 6Z, 10cis)': Km = 4.58 uM; Vmax = 0.05 pmol/min; kcat = 0.003 x 10^-3 s^-1; printed kcat/Km = 0.66 s^-1 M^-1.

row_label: Table 2, substrate row JHA I (2E, 6Z, 10cis)

table_label: Table 2: Michaelis Menten and kinetic constants for DcFA-o-MT (FEBS Open Bio 5 (2015) 264-275)


column_label: Table 2 (Michaelis Menten and kinetic constants for DcFA-o-MT), substrate row 'JHA III (2E, 6E, 10cis)'; column 'Km (uM)' = 2.53; column 'Vmax (pmol/min)' = 0.28; column 'kcat (s^-1 x 10^-3)' = 0.013; column 'kcat/Km (s^-1 M^-1)' = 5.14.

normalized_value_unit_evidence: Km: printed Table 2 cell 2.53 uM; 2.53 / 1000 = 0.00253 mM; the exported value is 0.00253 mM. kcat: printed Table 2 cell 0.013 in the column headed kcat (s^-1 x 10^-3), so 0.013 x 10^-3 = 0.000013 s^-1 and no further unit conversion applies; the exported value is 0.000013 s^(-1). kcat/Km: printed Table 2 cell 5.14 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.14 / 1000 = 0.00514 s^-1 mM^-1. Closure disclosure: the exact quotient of the two printed component cells is 0.000013 / 0.00253 = 0.005138339920948616 s^-1 mM^-1, which is the exported efficiency, and rounding that exact quotient to the two decimal places the paper prints gives 5.14 s^-1 M^-1, the printed cell, so every exported metric closes and none changes.

raw_value_unit_evidence: Table 2, substrate row 'JHA III (2E, 6E, 10cis)': Km = 2.53 uM; Vmax = 0.28 pmol/min; kcat = 0.013 x 10^-3 s^-1; printed kcat/Km = 5.14 s^-1 M^-1.

row_label: Table 2, substrate row JHA III (2E, 6E, 10cis)


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