sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N338C to reconstruct the assayed variant sequence.


enzyme_display_name: 1,8-cineole synthase

organism: Salvia fruticosa

substrate_name: geranyl diphosphate

source_db: brenda

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

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

data_origin: experimental

enzyme: 1,8-cineole synthase

substrate: geranyl diphosphate

source: brenda


kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N338A to reconstruct the assayed variant sequence.

mutation_type: substitution


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N338I to reconstruct the assayed variant sequence.


substrate_name: (2E)-geranyl diphosphate

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

proof_lines: kcat is 3.18 min(-1) with (2E)-geranyl diphosphate as substrate.

substrate: (2E)-geranyl diphosphate

source: uniprot


organism: Nicotiana suaveolens

sequence_variant_note: Mutation signature F266S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: recombinant mutant F266S, pH and temperature not specified in the publication


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


enzyme_display_name: alpha-humulene synthase

organism: Zingiber zerumbet

proof_lines: pH 7.5, 38°C, recombinant His-tagged enzyme

enzyme: alpha-humulene synthase


organism: Lavandula x intermedia

protein_accession_database: NCBI Protein

sequence_source: NCBI GenBank JN701459.1 CDS translation (protein_id AFL03421.1) cited in PMID 22592779

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

assay_conditions_summary: pH 7


enzyme_display_name: 7-epi-sesquithujene synthase

organism: Zea mays

sequence_source: multiple

proof_lines: 20 mM MgCl2, 0.2 mM MnCl2, 0.2 mM NaWO4, and 0.1 mM NaF, pH not specified in the publication, at 30°C

proof_lines: Increased production of (E)-beta-farnesene the presence of manganese.

source_databases_merged: brenda uniprot

enzyme: 7-epi-sesquithujene synthase


substrate_name: (2E,6E)-farnesyl diphosphate

substrate: (2E,6E)-farnesyl diphosphate


substrate_name: magnesium (in the presence of 10 uM farnesyl diphosphate)

smiles: [Mg]


substrate_name: manganese (in the presence of 10 uM farnesyl diphosphate)

smiles: [Mn]


verification_status: unverified

proof_lines: kcat is 0.33 sec(-1) with (2E)-geranyl diphosphate as substrate.

status: unverified


organism: Piper nigrum

proof_lines: kcat is 0.455 sec(-1) with (2E,6E)-farnesyl diphosphate as substrate.


enzyme_display_name: (+)-T-muurolol synthase

organism: Streptomyces clavuligerus

proof_lines: 30°C, pH not specified in the publication, presence of Mg2+

enzyme: (+)-T-muurolol synthase


organism: Arabidopsis thaliana

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


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

proof_lines: kcat is 0.079 sec(-1) with geranyl diphosphate (GPP) as substrate.

source_databases_merged: brenda skid uniprot


enzyme_display_name: (+)-car-3-ene synthase

organism: Pinus contorta

substrate_name: (3S)-linalyl diphosphate

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

enzyme: (+)-car-3-ene synthase

substrate: (3S)-linalyl diphosphate


organism: Picea sitchensis

substrate_name: Geranyl diphosphate

source_db: oed

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

substrate: Geranyl diphosphate

source: oed


enzyme_display_name: crotonobetainyl-CoA hydratase

organism: Proteus sp. (in: enterobacteria)

substrate_name: crotonyl-CoA

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: crotonyl-CoA low efficiency factor of 10^3

enzyme: crotonobetainyl-CoA hydratase

substrate: crotonyl-CoA


enzyme_display_name: (E)-beta-ocimene synthase

substrate_name: Unknown

km_display: Not reported

proof_lines: kcat is 3.5x10(-2) sec(-1) with (2E)-geranyl diphosphate as substrate (PubMed:20463089). kcat is 4.5x10(-3) sec(-1) with (2E,6E)-farnesyl diphosphate as substrate (PubMed:20463089).

enzyme: (E)-beta-ocimene synthase

substrate: Unknown


proof_lines: kcat is 2.21 sec(-1) with geranyl diphosphate as substrate.


proof_lines: kcat is 0.06 sec(-1) with geranyl diphosphate as substrate.


proof_lines: kcat is less than 0.00001 sec(-1) with geranyl diphosphate as substrate.


sequence_variant_note: Mutation signature F266T could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: recombinant mutant F266T, pH and temperature not specified in the publication


sequence_variant_note: Mutation signature F266V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: recombinant mutant F266V, pH and temperature not specified in the publication


organism: Homo sapiens

substrate_name: 17beta-estradiol (2-hydroxylation)

substrate: 17beta-estradiol (2-hydroxylation)


substrate_name: Geranyl diphosphate; H2O

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

substrate: Geranyl diphosphate; H2O


organism: Salvia officinalis


organism: Danio rerio

substrate_name: prostaglandin H2 (at 23 degrees Celsius)

verification_status: verified

column_label: Table 2 gives zPGIS Km 25 +/- 5 microM; methods state PGH2 initial-rate assay at 23 C.

raw_value_unit_evidence: Km raw_value=25 +/- 5 microM raw_unit=microM

row_label: zPGIS / PGH2 steady-state kinetics

table_label: Official PMC full-text Table 2

status: verified


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N338A to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: kcat normalized_value=0.069 normalized_unit=s^-1; km normalized_value=0.0119 normalized_unit=mM; kcat_over_km normalized_value=5.798319327731092 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 row Sf-CinS1 (N338A): kcat 4.15 min^-1; Km 11.9 uM; printed kcat/Km 0.348 uM^-1 min^-1.

row_label: Sf-CinS1 (N338A)

table_label: Table 2. Volatile Composition of Sf-CinS1, Sp-SabS1, and Their Mutants


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N338C to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: kcat normalized_value=0.052 normalized_unit=s^-1; km normalized_value=0.201 normalized_unit=mM; kcat_over_km normalized_value=0.25870646766169153 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 row Sf-CinS1 (N338C): kcat 3.13 min^-1; Km 201.0 uM; printed kcat/Km 0.016 uM^-1 min^-1.

row_label: Sf-CinS1 (N338C)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N338I to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: kcat normalized_value=0.096 normalized_unit=s^-1; km normalized_value=0.0566 normalized_unit=mM; kcat_over_km normalized_value=1.696113074204947 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 row Sf-CinS1 (N338I): kcat 5.78 min^-1; Km 56.6 uM; printed kcat/Km 0.102 uM^-1 min^-1.

row_label: Sf-CinS1 (N338I)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N338I/A339T to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: kcat normalized_value=0.024 normalized_unit=s^-1; km normalized_value=0.136 normalized_unit=mM; kcat_over_km normalized_value=0.1764705882352941 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 row Sf-CinS1 (N338I/A339T): kcat 1.42 min^-1; Km 135.8 uM; printed kcat/Km 0.011 uM^-1 min^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N338I/A339T/G447S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N338I/A339T/G447S/I449P/P450T to reconstruct the assayed variant sequence.

column_label: PMID 17557809 Table 2, row Sf-CinS1 (N338I/A339T/SGPTa), columns kcat (min^-1)=0.26, Km (uM)=12.9, kcat/Km (uM^-1 min^-1)=0.020; footnote SGPT denotes G447S/I449P/P450T.

normalized_value_unit_evidence: kcat normalized_value=0.0043 normalized_unit=s^-1; km normalized_value=0.0129 normalized_unit=mM; kcat_over_km normalized_value=0.3333333333333333 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 row Sf-CinS1 (N338I/A339T/SGPTa): kcat 0.26 min^-1; Km 12.9 uM; printed kcat/Km 0.020 uM^-1 min^-1; footnote SGPT=G447S/I449P/P450T.

row_label: Sf-CinS1 (N338I/A339T/SGPTa)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N338L to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: kcat normalized_value=0.009 normalized_unit=s^-1; km normalized_value=0.0265 normalized_unit=mM; kcat_over_km normalized_value=0.33962264150943394 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 row Sf-CinS1 (N338L): kcat 0.54 min^-1; Km 26.5 uM; printed kcat/Km 0.020 uM^-1 min^-1.

row_label: Sf-CinS1 (N338L)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N338S to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: kcat normalized_value=0.022 normalized_unit=s^-1; km normalized_value=0.0144 normalized_unit=mM; kcat_over_km normalized_value=1.5277777777777777 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 row Sf-CinS1 (N338S): kcat 1.30 min^-1; Km 14.4 uM; printed kcat/Km 0.090 uM^-1 min^-1.

row_label: Sf-CinS1 (N338S)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N338V to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: kcat normalized_value=0.012 normalized_unit=s^-1; km normalized_value=0.055 normalized_unit=mM; kcat_over_km normalized_value=0.2181818181818182 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 row Sf-CinS1 (N338V): kcat 0.73 min^-1; Km 55.1 uM; printed kcat/Km 0.013 uM^-1 min^-1.

row_label: Sf-CinS1 (N338V)


verification_status: corrected

column_label: Table 2; row Sf-CinS1 (wild type); column kcat: raw 3.18 min^-1; normalized 0.053 s^-1; column Km: raw 65.4 uM; normalized 0.0654 mM; column kcat/Km: raw 0.049 uM^-1 min^-1; normalized 0.8166666666666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Sf-CinS1 (wild type) gives kcat 3.18 min^-1; Km 65.4 uM; kcat/Km 0.049 uM^-1 min^-1.

row_label: Sf-CinS1 (wild type)

table_label: PMID 17557809, Table 2: Volatile Composition of Sf-CinS1, Sp-SabS1, and Their Mutants

status: corrected


enzyme_display_name: short-chain-enoyl-CoA hydratase

organism: Metallosphaera sedula

assay_conditions_summary: pH 8; 343.15 K; cofactor CoA

enzyme: short-chain-enoyl-CoA hydratase


enzyme_display_name: (-)-limonene synthase TPS1, chloroplastic

organism: Cannabis sativa

substrate_name: Geranyl pyrophosphate

substrate: Geranyl pyrophosphate


smiles: CCCCCC(C=CC=CCC=CCC=CCCCC(=O)[O-])OO

column_label: Abstract reports approximately 60 microM 15-HPETE for PGIS.

raw_value_unit_evidence: Km raw_value=approximately 60 microM raw_unit=microM

row_label: human prostacyclin synthase PGIS / 15-HPETE

table_label: PubMed XML abstract PMID 17459323


organism: Sus scrofa

substrate_name: prostaglandin H2

proof_lines:
porcine thromboxane synthase
Km value
thromboxane-A synthase EC 5.3.99.5

substrate: prostaglandin H2


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


enzyme_display_name: tetracenomycin F2 cyclase

organism: Streptomyces glaucescens

substrate_name: tetracenomycin F2

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

assay_conditions_summary: pH 8

column_label: Abstract states under pH >= 8.0 the enzyme catalyzes cyclization of Tcm F2 to Tcm F1 and has a Km of 121 +/- 18.2 microM.

raw_value_unit_evidence: Km raw_value=121 +/- 18.2 raw_unit=microM

row_label: Streptomyces glaucescens Tcm F2 cyclase with Tcm F2

table_label: PubMed abstract PMID 8218177

enzyme: tetracenomycin F2 cyclase

substrate: tetracenomycin F2


enzyme_display_name: terpinolene synthase

substrate_name: neryl diphosphate

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

enzyme: terpinolene synthase

substrate: neryl diphosphate


substrate_name: (3R)-linalyl diphosphate

substrate: (3R)-linalyl diphosphate


enzyme_display_name: gamma-terpinene synthase

substrate_name: geranyl diphosphate

enzyme: gamma-terpinene synthase


organism: Lavandula angustifolia


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

proof_lines: mutant A595G/F596L/L599F, 30°C, pH not specified in the publication


proof_lines: mutant F596L, 30°C, pH not specified in the publication


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


proof_lines: mutant L596F, 30°C, pH not specified in the publication


organism: Citrus x limon


column_label: Preserved note quotes PMID 9873013: Km of 20 uM PGH2 and Vmax of 12 umol of TXA2/min/mg; PMID 22735388 also reports wild-type value 32 uM PGH2 for the same enzyme/substrate context.

raw_value_unit_evidence: Km raw_value=20 raw_unit=uM

row_label: human thromboxane synthase / prostaglandin H2

table_label: Preserved PMID 9873013 kinetic statement from current verified_catlog note


organism: Nicotiana suaveolens

substrate_name: (2E)-geranyl diphosphate

proof_lines: kcat is 0.33 sec(-1) with (2E)-geranyl diphosphate as substrate.


enzyme_display_name: (+)-camphene synthase

organism: Artemisia annua

enzyme: (+)-camphene synthase


enzyme_display_name: (-)-camphene synthase

enzyme: (-)-camphene synthase


organism: Hedychium coronarium

proof_lines: kcat is 0.057 sec(-1) with (2E)-geranyl diphosphate as substrate.


enzyme_display_name: (+)-sabinene synthase

proof_lines: kcat is 0.89 sec(-1) with geranyl diphosphate as substrate.

enzyme: (+)-sabinene synthase


organism: Camellia sinensis var. sinensis

proof_lines:
pH 7.5, 30°C
pH 7.5, 30°C, recombinant enzyme
at pH 7.5 and 30°C


organism: Origanum vulgare


enzyme_display_name: alpha-terpinene synthase

enzyme: alpha-terpinene synthase


column_label: Official Springer Table 2 page, Biochemical characterization of OvTPS2 of cultivar d06-01

row_label: GPP row

table_label: Official Springer Table 2 Biochemical characterization of OvTPS2


substrate_name: manganese (in the presence of 10 uM geranyl diphosphate)

row_label: Mn2+ row


substrate_name: magnesium (in the presence of 10 uM geranyl diphosphate)

row_label: Mg2+ row


substrate_name: geranyl diphosphate (in the presence of 0.5 mM manganese)


substrate: manganese (in the presence of 10 uM geranyl diphosphate)


substrate: magnesium (in the presence of 10 uM geranyl diphosphate)


organism: Zea mays

substrate_name: farnesyl diphosphate

proof_lines: multiple products from a single prenyl diphosphate substrate

substrate: farnesyl diphosphate


substrate: geranyl diphosphate


substrate_name: magnesium (in the presence of 10 uM farnesyl diphosphate)

proof_lines:
presence of a Mg(2+) cofactor
reprotonation is dependent on the pH
TPS6 and TPS11


substrate_name: manganese (in the presence of 10 uM farnesyl diphosphate)


enzyme_display_name: (+)-alpha-pinene synthase TPS2, chloroplastic


enzyme: (-)-limonene synthase TPS1, chloroplastic


enzyme: (+)-alpha-pinene synthase TPS2, chloroplastic


enzyme_display_name: cis-L-3-hydroxyproline dehydratase

organism: Agrobacterium tumefaciens

enzyme: cis-L-3-hydroxyproline dehydratase


organism: Oceanobacillus iheyensis

substrate_name: galactarate

substrate: galactarate


organism: Saccharopolyspora spinosa

proof_lines:
SpnQ steady-state kinetics
kcat 2.6 min^-1
Km 49 uM


enzyme_display_name: L-talarate dehydratase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: L-talarate

enzyme: L-talarate dehydratase

substrate: L-talarate


enzyme_display_name: (-)-alpha-terpineol synthase

organism: Salvia fruticosa

proof_lines: kcat is 3.18 min(-1) with (2E)-geranyl diphosphate as substrate.

enzyme: (-)-alpha-terpineol synthase

substrate: (2E)-geranyl diphosphate


enzyme_display_name: (-)-alpha-pinene synthase

organism: Salvia officinalis

enzyme: (-)-alpha-pinene synthase


enzyme_display_name: (-)-beta-pinene synthase

organism: Gossypium hirsutum

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

enzyme: (-)-beta-pinene synthase


substrate_name: (RS)-alpha-terpinyl diphosphate

proof_lines:
pH 6.8, 31°C
pH 6.8, 31°C, presence of diphosphate

substrate: (RS)-alpha-terpinyl diphosphate


enzyme_display_name: (+)-beta-pinene synthase

enzyme: (+)-beta-pinene synthase


enzyme_display_name: (+)-alpha-pinene synthase

enzyme: (+)-alpha-pinene synthase


enzyme_display_name: beta-sesquiphellandrene synthase

organism: Persicaria minor

substrate_name: (2E,6E)-farnesyl diphosphate

mutation_type: deletion

proof_lines: pH 8.0, 30°C, recombinant enzyme mutant PmSTS_DELTA124

enzyme: beta-sesquiphellandrene synthase

substrate: (2E,6E)-farnesyl diphosphate


enzyme_display_name: 2-deoxy-scyllo-inosose synthase

organism: Streptoalloteichus hindustanus

substrate_name: D-glucose 6-phosphate

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

proof_lines: pH not specified in the publication, 46°C

enzyme: 2-deoxy-scyllo-inosose synthase

substrate: D-glucose 6-phosphate


column_label: Wiley full article kinetic paragraph assigns Cl(-)betaPINS Km as 3.1 uM for geranyl diphosphate; this normalizes to 0.0031 mM and matches the expected 0.0031 mM.

raw_value_unit_evidence: Km raw_value=3.1 raw_unit=uM

row_label: Cl(-)betaPINS / geranyl diphosphate

table_label: Kinetic characterization paragraph


organism: Rickettsia endosymbiont of Ixodes scapularis


organism: Niallia circulans

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K141Q with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

proof_lines: below, pH 7.7, 37°C, recombinant mutant K141Q

proof_lines: above, pH 7.7, 37°C, recombinant mutant K141Q


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E243Q to reconstruct the assayed variant sequence.


proof_lines: pH 7.7, 37°C, recombinant wild-type enzyme

proof_lines: pH 7.7, 35°C, recombinant wild-type enzyme, BtrC + BtrC2


proof_lines: kcat is 0.088 sec(-1) with (2E)-geranyl diphosphate as substrate.


organism: Bacillus circulans

substrate_name: D-Glucose 6-phosphate

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

ki_unit: mM

proof_lines:
pH 7.7, 46°C
pH 7.7, 35°C, native enzyme
pH 7.7, 28°C

source_databases_merged: sabio_rk brenda skid uniprot

substrate: D-Glucose 6-phosphate


organism: Nicotiana suaveolens

proof_lines: kcat is 0.33 sec(-1) with (2E)-geranyl diphosphate as substrate.


organism: Arabidopsis thaliana

proof_lines: The formation of monoterpene products from geranyl diphosphate (GPP) is unlikely, as the protein is not expected to be present in plastids, where GPP is thought to be produced.


organism: Pseudomonas aeruginosa

proof_lines: cis- and trans-3-hydroxy-L-proline dehydratases


enzyme_display_name: 2-methylisoborneol synthase

organism: Pseudanabaena limnetica

substrate_name: (E)-2-methylgeranyl diphosphate

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

enzyme: 2-methylisoborneol synthase

substrate: (E)-2-methylgeranyl diphosphate


organism: Streptomyces coelicolor

substrate_name: Geranyl diphosphate; H2O

substrate: Geranyl diphosphate; H2O


proof_lines:
pH 5.8, 31°C
pH 5.8, 31°C, presence of diphosphate


organism: Hedychium coronarium

substrate_name: Unknown

substrate: Unknown


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


enzyme_display_name: guluronate-specific alginate lyase

organism: Flammeovirga sp. NJ-04

substrate_name: alginate

enzyme: guluronate-specific alginate lyase

substrate: alginate


substrate_name: 2-methylneryl diphosphate

substrate: 2-methylneryl diphosphate


enzyme_display_name: 2-methylisocitrate dehydratase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: isocitrate

enzyme: 2-methylisocitrate dehydratase

substrate: isocitrate


organism: Wenyingzhuangia fucanilytica


organism: Escherichia coli


enzyme_display_name: 1,8-cineole synthase

organism: Salvia officinalis

substrate_name: geranyl diphosphate

enzyme: 1,8-cineole synthase


substrate_name: (3R)-linalyl diphosphate

substrate: (3R)-linalyl diphosphate


enzyme_display_name: chondroitin-sulfate-ABC exolyase

organism: Proteus vulgaris

substrate_name: dermatan sulfate

column_label: Table 2 row Dermatan sulfate reports Km 19.2 ± 2.9 μM for chondroitinase ABC II.

raw_value_unit_evidence: Km raw_value=19.2 ± 2.9 raw_unit=μM; table also reports kcat=1150 ± 26 min^-1 and kcat/Km=60 μM^-1 min^-1

row_label: Dermatan sulfate

table_label: PMC2613618 Table 2

enzyme: chondroitin-sulfate-ABC exolyase

substrate: dermatan sulfate


enzyme_display_name: 5-phosphooxy-L-lysine phospho-lyase

organism: Rattus norvegicus

smiles: C(CC(C(=O)O)NO)C(CN)P(=O)(O)O

enzyme: 5-phosphooxy-L-lysine phospho-lyase


enzyme_display_name: mannuronate-specific alginate lyase

enzyme: mannuronate-specific alginate lyase


organism: Paenarthrobacter aurescens

substrate_name: inulin

substrate: inulin


organism: Isoptericola halotolerans

column_label: Table 1 lists Sodium Alginate with Km 5.6 mM, kcat 45.92 s^-1, and kcat/Km 8.20 s^-1 mM^-1.

normalized_value_unit_evidence: kcat normalized_value=45.92 normalized_unit=s^-1; Km normalized_value=5.6 normalized_unit=mM; kcat/Km normalized_value=8.20 normalized_unit=s^-1 mM^-1; exported computed ratio from 45.9/5.6=8.196428571428571

raw_value_unit_evidence: kcat raw_value=45.92 raw_unit=s^-1; Km raw_value=5.6 raw_unit=mM; kcat/Km raw_value=8.20 raw_unit=s^-1 mM^-1

row_label: Sodium Alginate column

table_label: Table 1, kinetic parameters of AlyA toward sodium alginate, PolyG, and PolyM


organism: Mus musculus


enzyme_display_name: valerena-4,7(11)-diene synthase

organism: Valeriana officinalis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T310M to reconstruct the assayed variant sequence.

proof_lines: mutant T310M, 37°C, pH not specified in the publication

enzyme: valerena-4,7(11)-diene synthase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y535F to reconstruct the assayed variant sequence.

proof_lines: mutant Y535F, 37°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T310A to reconstruct the assayed variant sequence.

proof_lines: mutant T310A, 37°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N455S to reconstruct the assayed variant sequence.

proof_lines: mutant N455S, 37°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T310A/N455S to reconstruct the assayed variant sequence.

proof_lines: mutant T310A/N455S, 37°C, pH not specified in the publication


assay_conditions_summary: 310.15 K; buffer GraphPad. The article states no

column_label: Results text, printed page 3875, the C452A paragraph: the sentence names the mutant form 'the C452A mutant' with KM '20.7 μM' and kcat '0.038 s−1', and it names the wild type comparator 'VDS' with KM '20.1 μM' and kcat '0.018 s−1'. It points at Table 2, whose body is an image in the PDF and whose kcat/KM column was not read.

normalized_value_unit_evidence: km: printed cell 20.1 μM; 1 μM is 0.001 mM, so 20.1 / 1000 = 0.0201 mM; the exported value is 0.0201 mM. kcat: printed cell 0.018 s−1; the value is already in s^-1, so no unit conversion applies; the exported value is 0.018 s^(-1). kcat_over_km: this article prints no readable efficiency value for this measurement, so the exported ratio is the full-precision quotient of the two printed cells above, 0.018 / 0.0201 = 0.8955223880597014 s^-1 mM^-1, which is the exported value.

raw_value_unit_evidence: Results text, printed page 3875: the sentence that restates the Table 2 kinetic parameters prints KM 20.1 μM and kcat 0.018 s−1 for wild type VDS. The Table 2 kcat/KM column was not read, because that table body is an embedded image in the PDF.

row_label: Wild type VDS, the Table 2 wild type kinetic parameters as restated in the Results text on printed page 3875

table_label: Table 2: Steady-State Kinetic Parameters and In Vitro Product Distributions (percent) of WT and Mutant VDS Enzymes (Biochemistry 2021, 60 (51), 3868-3878). The table body is an image in the PDF, so the two cells used here are the ones the Results text restates.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N455A to reconstruct the assayed variant sequence.

proof_lines: mutant N455A, 37°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:J9R5V4 and applied mutation signature C452A to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: km: printed cell 20.7 μM; 1 μM is 0.001 mM, so 20.7 / 1000 = 0.0207 mM; the exported value is 0.0207 mM. kcat: printed cell 0.038 s−1; the value is already in s^-1, so no unit conversion applies; the exported value is 0.038 s^(-1). kcat_over_km: this article prints no readable efficiency value for this measurement, so the exported ratio is the full-precision quotient of the two printed cells above, 0.038 / 0.0207 = 1.8357487922705313 s^-1 mM^-1, which is the exported value.

raw_value_unit_evidence: Results text, printed page 3875: the sentence that restates the Table 2 kinetic parameters prints KM 20.7 μM and kcat 0.038 s−1 for C452A. The Table 2 kcat/KM column was not read, because that table body is an embedded image in the PDF.

row_label: C452A mutant, the Table 2 C452A kinetic parameters as restated in the Results text on printed page 3875


enzyme_display_name: (+)-epi-alpha-bisabolol synthase

organism: Phyla dulcis

proof_lines: kcat is 0.04 sec(-1) for (2E,6E)-farnesyl diphosphate.

enzyme: (+)-epi-alpha-bisabolol synthase


enzyme_display_name: sclareol synthase

organism: Salvia sclarea

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N431I to reconstruct the assayed variant sequence.

proof_lines: recombinant enzyme mutant N431I, pH 7.2, 30°C

enzyme: sclareol synthase


sequence_variant_note: Mutation signature N431Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: recombinant enzyme mutant N431Q, pH 7.2, 30°C


proof_lines: recombinant wild-type enzyme, pH 7.2, 30°C


proof_lines: kcat is 0.013 sec(-1) with farnesyl diphosphate as substrate.


organism: Pinus taeda

proof_lines: pH and temperature not specified in the publication

substrate: geranyl diphosphate


organism: Streptomyces fradiae

proof_lines: at C-terminus 39 aa trimmed from the original NeoC, pH 7.7, 28°C


organism: Homo sapiens

substrate_name: H2O; 5-Phosphonooxy-L-lysine

substrate: H2O; 5-Phosphonooxy-L-lysine


organism: Abies grandis

column_label: PMID 1731633 abstract/main text, geranyl pyrophosphate substrate, Km = 6 uM.

raw_value_unit_evidence: Abstract and main text report a Km value of 6 uM for geranyl pyrophosphate.

row_label: wound-inducible pinene cyclase / geranyl pyrophosphate

table_label: Abstract and main text kinetics prose


enzyme_display_name: Delta(6)-protoilludene synthase

organism: Stereum hirsutum (strain FP-91666)

enzyme: Delta(6)-protoilludene synthase


proof_lines: divalent metal-ion Michaelis-Menten conditions


substrate_name: farnesyl diphosphate (FPP)

column_label: PMC3866635 Table 1, row Stehi1|73029, Km [M] column reports (1.52 +/- 0.2) x 10^-6 M; this normalizes to 0.00152 mM.

row_label: Table 1 row: Stehi1|73029

table_label: PMC3866635 Table 1: Kinetic parameters determined for Stehi1|25180, Stehi1|64702 and Stehi1|73029

substrate: farnesyl diphosphate (FPP)


column_label: PMC3866635 Table 1, row Stehi1|64702, Km [M] column reports (1.91 +/- 0.3) x 10^-6 M; this normalizes to 0.00191 mM.

row_label: Table 1 row: Stehi1|64702


column_label: PMC3866635 Table 1, row Stehi1|25180, Km [M] column reports (5.02 +/- 0.9) x 10^-6 M; this normalizes to 0.00502 mM.

row_label: Table 1 row: Stehi1|25180


proof_lines: SsSS N431I kcat/KM


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N431Q to reconstruct the assayed variant sequence.

proof_lines: SsSS N431Q kcat/KM


proof_lines:
SsSS
8alpha-hydroxy-copalyl diphosphate
(13R)-sclareol


organism: Microbulbifer sp. 6532A

proof_lines:
at pH 8.0 and 50°C
pH 7.0, 45°C


enzyme_display_name: threonine synthase

organism: Escherichia coli (strain K12)

substrate_name: O-phospho-L-homoserine

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

column_label: Abstract states threonine synthase catalyzes L-threonine formation from L-homoserine phosphate (HSerP; Km = 0.5 mM).

raw_value_unit_evidence: Km raw_value=0.5 raw_unit=mM

row_label: Escherichia coli threonine synthase with L-homoserine phosphate

table_label: PubMed abstract PMID 7907888

enzyme: threonine synthase

substrate: O-phospho-L-homoserine


organism: Pseudoalteromonas sp.

assay_conditions_summary: pH 7; buffer 50 mM phosphate

column_label: PDF p.1117 states the Km value of AlyPI for sodium alginate was 2.36 mmol/L (sugar residues).

row_label: AlyPI / sodium alginate substrate

table_label: Canadian Journal of Microbiology PDF p.1117 Results prose


organism: Methanosarcina acetivorans C2A

assay_conditions_summary: pH 8; cofactor ATP

column_label: PDF p.473 states MA1610 produced L-threonine/phosphate with specific TS activity 1.6 units/mg (68 min^-1); no 4080 s^-1 kcat cell is present for O-phospho-L-homoserine.

raw_value_unit_evidence: Specific TS activity 1.6 units/mg, corresponding to 68 min^-1; target source row records kcat 4080 s^-1.

row_label: MA1610 protein catalysing phosphohomoserine to threonine

table_label: Biochem. J. PDF p.473 Results / Figure 4-associated TS activity prose


organism: Methanocaldococcus jannaschii

substrate_name: D-glyceraldehyde 3-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K155R to reconstruct the assayed variant sequence.

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

substrate: D-glyceraldehyde 3-phosphate


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


organism: Streptomyces sp.

substrate_name: geranylgeranyl diphosphate

substrate: geranylgeranyl diphosphate


enzyme_display_name: demethyl-4-deoxygadusol synthase

organism: Trichormus variabilis

substrate_name: D-sedoheptulose 7-phosphate

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

enzyme: demethyl-4-deoxygadusol synthase

substrate: D-sedoheptulose 7-phosphate


enzyme_display_name: 2-epi-valiolone synthase

organism: Stigmatella aurantiaca

enzyme: 2-epi-valiolone synthase


enzyme_display_name: (-)-spiroviolene synthase

organism: Streptomyces violens

proof_lines: reconstructed ancient synthase SvS-A2, 11.7°C, pH 7.4

proof_lines: reconstructed ancient synthase SvS-A2, 20.4°C, pH 7.4

proof_lines: reconstructed ancient synthase SvS-A2, 25°C, pH 7.4

enzyme: (-)-spiroviolene synthase


organism: Nostoc punctiforme (strain ATCC 29133 / PCC 73102)

substrate_name: sedoheptulose 7-phosphate

substrate: sedoheptulose 7-phosphate


organism: Mycobacterium tuberculosis

source_db: skid

source_databases_merged: skid uniprot

source: skid


enzyme_display_name: alpha-humulene synthase

organism: Arabidopsis thaliana

substrate_name: farnesyl diphosphate

enzyme: alpha-humulene synthase

substrate: farnesyl diphosphate


substrate_name: D-glyceraldehyde

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

substrate: D-glyceraldehyde


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

substrate_name: Unknown

substrate: Unknown


proof_lines:
wild-type, 11.7°C, pH 7.4
wild-type, 13.7°C, pH 7.4
wild-type, 17.9°C, pH 7.4


enzyme_display_name: dolabella-3,7-dien-18-ol synthase

proof_lines: kcat is 0.00083 sec(-1) with geranylgeranyl diphosphate as substrate.

enzyme: dolabella-3,7-dien-18-ol synthase


enzyme_display_name: dolathalia-3,7,11-triene synthase

enzyme: dolathalia-3,7,11-triene synthase


enzyme_display_name: 5-hydroxy-alpha-gurjunene synthase

organism: Marchantia polymorpha

substrate_name: (2E,6E)-farnesyl diphosphate

proof_lines: kcat is 0.058 sec(-1) with (2E,6E)-farnesyl diphosphate as substrate.

enzyme: 5-hydroxy-alpha-gurjunene synthase

substrate: (2E,6E)-farnesyl diphosphate


substrate_name: Geranyl diphosphate

substrate: Geranyl diphosphate


organism: Humulus lupulus

proof_lines: HlSTS1 humulene caryophyllene


organism: Artemisia annua

column_label: Table 1; row AaTPS6; column K_m (uM) cell 17.70; column K_cat (s^-1) cell 4.46; column K_cat/K_m (s^-1 M^-1) cell 2.52 x 10^5. Column headers as printed: (enzyme) | K_m (μM) | K_cat (s^-1) | K_cat/K_m (s^-1 •M^-1)

normalized_value_unit_evidence: K_m 17.70 uM = 17.70/1000 = 0.0177 mM. K_cat 4.46 s^-1 = 4.46 s^-1 (already the canonical kcat unit). kcat/Km taken as this same row's K_cat divided by its K_m: 4.46 / 0.0177 = 251.9774011299435 s^-1 mM^-1. The table's own efficiency column prints 2.52 x 10^5 s^-1 M^-1 = 252 s^-1 mM^-1, which is this quotient at the precision the table prints.

raw_value_unit_evidence: Table 1. Kinetic parameters of AaTPS2, AaTPS5, and AaTPS6 proteins. Row AaTPS6: column K_m (uM) cell 17.70; column K_cat (s^-1) cell 4.46; column K_cat/K_m (s^-1 M^-1) cell 2.52 x 10^5.


enzyme_display_name: (-)-drimenol synthase

organism: Aquimarina spongiae

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

enzyme: (-)-drimenol synthase


enzyme_display_name: 1,8-cineole synthase

organism: Streptomyces clavuligerus

proof_lines:
1,8-cineole synthase
geranyl diphosphate
Streptomyces clavuligerus

enzyme: 1,8-cineole synthase


enzyme_display_name: (-)-5-epieremophilene synthase

organism: Salvia miltiorrhiza

enzyme: (-)-5-epieremophilene synthase


organism: Valeriana officinalis

proof_lines: kcat is 0.025 sec(-1) with (2E,6E)-farnesyl diphosphate as substrate.


enzyme_display_name: rhizathalene A synthase

proof_lines: at 30°C, pH not specified in the publication

enzyme: rhizathalene A synthase


substrate_name: trans,trans-Farnesyl diphosphate

proof_lines: kcat is 2.09 sec(-1) with farnesyl diphosphate as substrate.

substrate: trans,trans-Farnesyl diphosphate


proof_lines: kcat is 2.07 sec(-1) with farnesyl diphosphate as substrate.


proof_lines: kcat is 1.53 sec(-1) with farnesyl diphosphate as substrate.


enzyme_display_name: (E)-beta-ocimene synthase

organism: Melampsora lini

column_label: The full-text kinetic paragraph states that the apparent Km values of MliILTPS2 and MliILTPS3 using FDP were 1.9 +/- 0.3 uM and 1.6 +/- 0.2 uM, respectively; the selected row is the MliILTPS2/FDP entry.

raw_value_unit_evidence: Km raw_value=1.9 +/- 0.3 raw_unit=uM

row_label: MliILTPS2 recombinant enzyme / FDP substrate

table_label: Scientific Reports PMID 32913319 Results paragraph: ILTPS genes encode active terpene synthases

enzyme: (E)-beta-ocimene synthase


organism: Actinosynnema mirum

assay_conditions_summary: pH 7; cofactor NAD+

normalized_value_unit_evidence: Km normalized_value=0.0599 normalized_unit=mM; kcat normalized_value=0.033 normalized_unit=s^(-1); kcat/Km normalized_value=0.55 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Km raw_value=59.9 microM raw_unit=microM raw_cell=59.9 +/- 13.4; kcat raw_value=2.0 min^-1 raw_unit=min^-1 raw_cell=2.0 +/- 0.1; kcat/Km raw_value=0.033 microM^-1 min^-1 raw_unit=microM^-1 min^-1 raw_cell=0.033 +/- 0.004

table_label: Table 1. Apparent kinetic values for ValA Amir_2000 Staur_3140 Npun_5600 and Ava_3858


enzyme_display_name: cembrene A synthase

organism: Streptomyces sp.

enzyme: cembrene A synthase


enzyme_display_name: alpha-selinene synthase

organism: Stereum hirsutum (strain FP-91666)

enzyme: alpha-selinene synthase


enzyme_display_name: (+)-sabinene synthase

organism: Picea sitchensis

enzyme: (+)-sabinene synthase


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


column_label: Supplementary Table 2; row Stehi64702; Metal (1 mM) Mg2+; Km (M) column = (22.3 +/- 3.6) x 10^-6 M

normalized_value_unit_evidence: Km=0.0223 mM after converting (22.3 +/- 3.6) x 10^-6 M to mM

raw_value_unit_evidence: Supplementary Table 2 Stehi64702 Mg2+ Km (M) = (22.3 +/- 3.6) x 10^-6 M

row_label: P9WEW1 / Stehi64702 / Mg2+

table_label: Supplementary Table 2 / Kinetic parameters determined for delta6-protoilludene synthases with divalent metal ions


column_label: Supplementary Table 2; row Stehi64702; Metal (1 mM) Mn2+; Km (M) column = (4.9 +/- 0.3) x 10^-6 M

normalized_value_unit_evidence: Km=0.0049 mM after converting (4.9 +/- 0.3) x 10^-6 M to mM

raw_value_unit_evidence: Supplementary Table 2 Stehi64702 Mn2+ Km (M) = (4.9 +/- 0.3) x 10^-6 M

row_label: P9WEW1 / Stehi64702 / Mn2+


column_label: Supplementary Table 2; row Stehi64702; Metal (1 mM) Ca2+; Km (M) column = (2.9 +/- 0.2) x 10^-6 M

normalized_value_unit_evidence: Km=0.0029 mM after converting (2.9 +/- 0.2) x 10^-6 M to mM

raw_value_unit_evidence: Supplementary Table 2 Stehi64702 Ca2+ Km (M) = (2.9 +/- 0.2) x 10^-6 M

row_label: P9WEW1 / Stehi64702 / Ca2+


column_label: Supplementary Table 2; row Stehi64702; Metal (1 mM) Ni2+; Km (M) column = (24.4 +/- 1.0) x 10^-6 M

normalized_value_unit_evidence: Km=0.0244 mM after converting (24.4 +/- 1.0) x 10^-6 M to mM

raw_value_unit_evidence: Supplementary Table 2 Stehi64702 Ni2+ Km (M) = (24.4 +/- 1.0) x 10^-6 M

row_label: P9WEW1 / Stehi64702 / Ni2+


column_label: Supplementary Table 2; row Stehi64702; Metal (1 mM) Co2+; Km (M) column = (23.8 +/- 0.9) x 10^-6 M

normalized_value_unit_evidence: Km=0.0238 mM after converting (23.8 +/- 0.9) x 10^-6 M to mM

raw_value_unit_evidence: Supplementary Table 2 Stehi64702 Co2+ Km (M) = (23.8 +/- 0.9) x 10^-6 M

row_label: P9WEW1 / Stehi64702 / Co2+


column_label: Supplementary Table 2; row Stehi73029; Metal (1 mM) Mg2+; Km (M) column = (33.5 +/- 4.4) x 10^-6 M

normalized_value_unit_evidence: Km=0.0335 mM after converting (33.5 +/- 4.4) x 10^-6 M to mM

raw_value_unit_evidence: Supplementary Table 2 Stehi73029 Mg2+ Km (M) = (33.5 +/- 4.4) x 10^-6 M

row_label: P9WEW2 / Stehi73029 / Mg2+


column_label: Supplementary Table 2; row Stehi73029; Metal (1 mM) Mn2+; Km (M) column = (8.5 +/- 0.3) x 10^-6 M

normalized_value_unit_evidence: Km=0.0085 mM after converting (8.5 +/- 0.3) x 10^-6 M to mM

raw_value_unit_evidence: Supplementary Table 2 Stehi73029 Mn2+ Km (M) = (8.5 +/- 0.3) x 10^-6 M

row_label: P9WEW2 / Stehi73029 / Mn2+


column_label: Supplementary Table 2; row Stehi73029; Metal (1 mM) Ca2+; Km (M) column = (12.9 +/- 0.4) x 10^-6 M

normalized_value_unit_evidence: Km=0.0129 mM after converting (12.9 +/- 0.4) x 10^-6 M to mM

raw_value_unit_evidence: Supplementary Table 2 Stehi73029 Ca2+ Km (M) = (12.9 +/- 0.4) x 10^-6 M

row_label: P9WEW2 / Stehi73029 / Ca2+


column_label: Supplementary Table 2; row Stehi73029; Metal (1 mM) Ni2+; Km (M) column = (16.0 +/- 0.8) x 10^-6 M

normalized_value_unit_evidence: Km=0.016 mM after converting (16.0 +/- 0.8) x 10^-6 M to mM

raw_value_unit_evidence: Supplementary Table 2 Stehi73029 Ni2+ Km (M) = (16.0 +/- 0.8) x 10^-6 M

row_label: P9WEW2 / Stehi73029 / Ni2+


column_label: Supplementary Table 2; row Stehi73029; Metal (1 mM) Co2+; Km (M) column = (30.3 +/- 1.7) x 10^-6 M

normalized_value_unit_evidence: Km=0.0303 mM after converting (30.3 +/- 1.7) x 10^-6 M to mM

raw_value_unit_evidence: Supplementary Table 2 Stehi73029 Co2+ Km (M) = (30.3 +/- 1.7) x 10^-6 M

row_label: P9WEW2 / Stehi73029 / Co2+


enzyme_display_name: 2-deoxy-scyllo-inosose synthase

organism: Niallia circulans

substrate_name: D-glucose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E243Q to reconstruct the assayed variant sequence.

enzyme: 2-deoxy-scyllo-inosose synthase

substrate: D-glucose 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K141Q with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


enzyme_display_name: tau-cadinol synthase

organism: Zea mays

proof_lines: kcat is 0.00136 sec(-1) with (2E,6E)-farnesyl diphosphate as substrate.

enzyme: tau-cadinol synthase


organism: Salvia officinalis

proof_lines:
Salvia officinalis
(+)-sabinene synthase
geranyl diphosphate


enzyme_display_name: gamma-terpinene synthase

organism: Citrus limon

substrate_name: geranyl diphosphate

column_label: Wiley full article kinetic paragraph assigns ClgammaTS Km as 2.7 uM for geranyl diphosphate; this normalizes to 0.0027 mM and matches the expected 0.0027 mM.

raw_value_unit_evidence: Km raw_value=2.7 raw_unit=uM

row_label: ClgammaTS / geranyl diphosphate

enzyme: gamma-terpinene synthase


organism: Thymus vulgaris

column_label: Abstract reports Km value for geranyl pyrophosphate was 2.6 microM.

raw_value_unit_evidence: Km raw_value=2.6 microM raw_unit=microM

row_label: Thymus vulgaris gamma-terpinene synthase / geranyl pyrophosphate

table_label: PubMed XML abstract PMID 1897973


enzyme_display_name: (Z)-beta-ocimene synthase

organism: Lilium orientalis

enzyme: (Z)-beta-ocimene synthase


enzyme_display_name: (+)-camphene synthase

column_label: Table 1; row AaTPS5; column K_m (uM) cell 19.74; column K_cat (s^-1) cell 1.49; column K_cat/K_m (s^-1 M^-1) cell 7.66 x 10^4. Column headers as printed: (enzyme) | K_m (μM) | K_cat (s^-1) | K_cat/K_m (s^-1 •M^-1)

normalized_value_unit_evidence: K_m 19.74 uM = 19.74/1000 = 0.01974 mM. K_cat 1.49 s^-1 = 1.49 s^-1 (already the canonical kcat unit). kcat/Km taken as this same row's K_cat divided by its K_m: 1.49 / 0.01974 = 75.48125633232016 s^-1 mM^-1. The table's own efficiency column prints 7.66 x 10^4 s^-1 M^-1 = 76.6 s^-1 mM^-1, which does NOT reproduce the quotient of the same row's printed K_m and K_cat (75.48 s^-1 mM^-1) at three significant figures; the paper's efficiency column is internally inconsistent with its own K_m/K_cat cells for this row. The value recorded here is the quotient of the two cells actually printed for this row, not the paper's separately printed efficiency figure.

raw_value_unit_evidence: Table 1. Kinetic parameters of AaTPS2, AaTPS5, and AaTPS6 proteins. Row AaTPS5: column K_m (uM) cell 19.74; column K_cat (s^-1) cell 1.49; column K_cat/K_m (s^-1 M^-1) cell 7.66 x 10^4.

enzyme: (+)-camphene synthase


enzyme_display_name: (+)-delta-cadinol synthase

organism: Coniophora puteana

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

proof_lines: mutant S314N of isoform Copu9, at pH 7.5 and 25°C

enzyme: (+)-delta-cadinol synthase


proof_lines: mutant N228A of isoform Copu9, at pH 7.5 and 25°C


proof_lines: mutant C76V of isoform Copu9, at pH 7.5 and 25°C


proof_lines: wild type isoform Copu9, at pH 7.5 and 25°C


proof_lines: mutant G194A of isoform Copu9, at pH 7.5 and 25°C


proof_lines: mutant P197C of isoform Copu9, at pH 7.5 and 25°C


proof_lines: mutant T192N of isoform Copu9, at pH 7.5 and 25°C


proof_lines: mutant C195V of isoform Copu9, at pH 7.5 and 25°C


proof_lines: mutant T73C of isoform Copu9, at pH 7.5 and 25°C


enzyme_display_name: (+)-2-epi-prezizaene synthase

organism: Nicotiana tabacum

substrate_name: (2Z,6E)-farnesyl diphosphate

proof_lines: kcat is 2.5 min(-1) with (2E,6E)-farnesyl diphosphate as substrate (PubMed:20175559, PubMed:20201526). kcat is 5.71 min(-1) with (2Z,6E)-farnesyl diphosphate as substrate (PubMed:20175559, PubMed:20201526). kcat is 0.032 sec(-1) with farnes

enzyme: (+)-2-epi-prezizaene synthase

substrate: (2Z,6E)-farnesyl diphosphate


enzyme_display_name: (-)-alpha-cedrene synthase

enzyme: (-)-alpha-cedrene synthase


enzyme_display_name: (-)-cyatha-3,12-diene synthase

organism: Hericium erinaceus

enzyme: (-)-cyatha-3,12-diene synthase


substrate_name: anilinogeranyl diphosphate

substrate: anilinogeranyl diphosphate


enzyme_display_name: 2-deoxy-4-epi-scyllo-inosose synthase

organism: Sporocytophaga myxococcoides

substrate_name: D-mannose 6-phosphate

enzyme: 2-deoxy-4-epi-scyllo-inosose synthase

substrate: D-mannose 6-phosphate


enzyme_display_name: (+)-sativene synthase

organism: Coprinopsis cinerea

proof_lines: wild-type enzyme, and mutants H235P and N239L, pH 8.0, 30?

enzyme: (+)-sativene synthase


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

proof_lines: Cop6 loop graft mutant Cop6L4, pH 8.0, 30?


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K233I to reconstruct the assayed variant sequence.


enzyme_display_name: beta-cubebene synthase

organism: Magnolia grandiflora

proof_lines: kcat is 0.35 x 10(-3) sec(-1) for farnesyl diphosphate.

enzyme: beta-cubebene synthase


enzyme_display_name: neoabietadiene synthase

organism: Abies grandis

substrate_name: (+)-copalyl diphosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R356A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R356A, pH and temperature not specified in the publication

enzyme: neoabietadiene synthase

substrate: (+)-copalyl diphosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N451A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N451A, pH and temperature not specified in the publication


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


enzyme_display_name: beta-copaene synthase

organism: Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)

substrate_name: cis-trans-farnesyl diophosphate

enzyme: beta-copaene synthase

substrate: cis-trans-farnesyl diophosphate


substrate_name: CPP (in presence of magnesium)

substrate: CPP (in presence of magnesium)


enzyme_display_name: (-)-camphene synthase

organism: Artemisia annua

table_label: Table 1. Kinetic parameters of AaTPS2, AaTPS5, and AaTPS6 proteins.

enzyme: (-)-camphene synthase

substrate: geranyl diphosphate


enzyme_display_name: 6-pyruvoyltetrahydropterin synthase

organism: Drosophila melanogaster

enzyme: 6-pyruvoyltetrahydropterin synthase


enzyme_display_name: 2-methylisoborneol synthase

organism: Streptomyces coelicolor

enzyme: 2-methylisoborneol synthase


enzyme_display_name: alpha-copaene synthase

organism: Piper nigrum

proof_lines: kcat is 0.185 sec(-1) with (2E,6E)-farnesyl diphosphate as substrate.

enzyme: alpha-copaene synthase


enzyme_display_name: UniProt Q9X9I8

organism: Yersinia enterocolitica

substrate_name: isochorismate

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q9X9I8

substrate: isochorismate


enzyme_display_name: (+)-alpha-pinene synthase

organism: Pinus taeda

proof_lines: Pinus taeda alpha-pinene synthase identity

proof_lines: functional expression of antipodal pinene synthases

enzyme: (+)-alpha-pinene synthase


organism: Lavandula angustifolia


organism: Salvia officinalis


enzyme_display_name: isochorismate lyase

proof_lines: mutant T348A, 25°C, pH not specified in the publication

enzyme: isochorismate lyase


proof_lines: mutant E281D/T348A, 25°C, pH not specified in the publication


proof_lines: mutant E281D, 25°C, pH not specified in the publication


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


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

proof_lines: pH and temperature not specified in the publication


organism: Pseudomonas aeruginosa

sequence_variant_note: Mutation signature D310E/A375T references residue 310, which is outside the resolved sequence length.

proof_lines: mutant D310E/A375T, 25°C, pH not specified in the publication


sequence_variant_note: Mutation signature A375T references residue 375, which is outside the resolved sequence length.

proof_lines: mutant A375T, 25°C, pH not specified in the publication


sequence_variant_note: Mutation signature D310E references residue 310, which is outside the resolved sequence length.

proof_lines: mutant D310E, 25°C, pH not specified in the publication


substrate_name: (3R)-linalyl diphosphate

proof_lines:
pH 6.5, 30°C
sage pinene cyclase chemistry
linalyl pyrophosphate

substrate: (3R)-linalyl diphosphate


proof_lines: pH 7.5, 22°C, promiscuous mutant enzyme M4


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: isochorismate (for isochorismate pyruvate lyase activity at pH 8 and 37 degrees Celsius)

proof_lines: kcat is 2.6 min(-1) for isochorismate pyruvate lyase activity (at pH 8 and 37 degrees Celsius). kcat is 2.8 min(-1) for salicylate synthase activity (at pH 8 and 37 degrees Celsius). kcat is 3.1 min(-1) for isochorismate synthase activity (


substrate_name: chorismate (for chorismate mutase activity without magnesium at pH 7.5 and 37 degrees Celsius)


enzyme_display_name: tuliposide A-converting enzyme

organism: Tulipa gesneriana

substrate_name: 6-tuliposide A

proof_lines: kcat is 2800 sec(-1) with 6-tuliposide A as substrate. kcat is 510 sec(-1) with 6-tuliposide B as substrate.

enzyme: tuliposide A-converting enzyme

substrate: 6-tuliposide A


substrate_name: 6-tuliposide B

substrate: 6-tuliposide B


proof_lines: kcat is 2400 sec(-1) with 6-tuliposide A as substrate. kcat is 480 sec(-1) with 6-tuliposide B as substrate.


substrate_name: (2E,6E)-farnesyl diphosphate

proof_lines: wild-type enzyme, and mutants H235P and N239L, pH 8.0, 30°C


proof_lines: Cop6 loop graft mutant Cop6L4, pH 8.0, 30°C


enzyme_display_name: tuliposide B-converting enzyme

proof_lines: isoform 2, pH and temperature not specified in the publication

enzyme: tuliposide B-converting enzyme


proof_lines: isoform 3, pH and temperature not specified in the publication


proof_lines: substrate 2-2H-isochorismate, pH 7.5, 30°C


enzyme_display_name: (+)-2-epi-prezizaene synthase

organism: Nicotiana tabacum

proof_lines: kcat is 2.5 min(-1) with (2E,6E)-farnesyl diphosphate as substrate (PubMed:20175559, PubMed:20201526). kcat is 5.71 min(-1) with (2Z,6E)-farnesyl diphosphate as substrate (PubMed:20175559, PubMed:20201526). kcat is 0.032 sec(-1) with farnes

enzyme: (+)-2-epi-prezizaene synthase


organism: Hericium erinaceum

substrate_name: Geranylgeranyl diphosphate

source_databases_merged: sabio_rk brenda uniprot

substrate: Geranylgeranyl diphosphate


proof_lines: in 50 mM HEPES, pH 7.2, 100 mM KCl, 7.5 mM MgCl2, 0.02 mM MnCl2, at 30°C


proof_lines: kcat is 1700 sec(-1) with 6-tuliposide A as substrate. kcat is 500 sec(-1) with 6-tuliposide B as substrate.


enzyme_display_name: DNA-(apurinic or apyrimidinic site) lyase

organism: Escherichia coli

proof_lines:
mutant deltaQLY, Nei placed opposite G
mutant QLY/AAA, Nei placed opposite G
mutant QLY/AAA, Nei placed opposite A


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature Q261A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines:
mutant Q261A, Nei placed opposite C
mutant Q261A, Nei placed opposite G
mutant Q261A, Nei placed opposite A

enzyme: DNA-(apurinic or apyrimidinic site) lyase


proof_lines:
wild-type, Nei placed opposite A
wild-type, Nei placed opposite T
wild-type, Nei placed opposite C


substrate_name: AP-DNA

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature R37A with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: mutant R37A in rAP-containing oligonucleotide cleavage assay

substrate: AP-DNA


organism: Homo sapiens

substrate_name: oligomer with G/U pair

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature D308A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

proof_lines:
D283/D308A mutant, pH 7.5
D308A mutant, pH 7.5

substrate: oligomer with G/U pair


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature D283A with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


substrate_name: 43-mer oligonucleotide containing apurinic/apyrimidinic sites

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N226A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N229A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

substrate: 43-mer oligonucleotide containing apurinic/apyrimidinic sites


substrate_name: DNA containing an abasic site

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y171A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, mutant enzyme Y171A, high salt concentration (150 mM NaCl)

proof_lines: pH 7.5, mutant enzyme Y171A, low salt concentration (82 mM NaCl)

substrate: DNA containing an abasic site


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y171F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, mutant enzyme Y171F, low salt concentration (82 mM NaCl)


substrate_name: THF-containing oligonucleotide

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D70A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

proof_lines: APE1 mutant D70A, AP endonuclease activity

proof_lines: Ape mutant D70A, 3'-phosphodiesterase activity

proof_lines: APE1 mutant D70A, 3'-phosphodiesterase activity

substrate: THF-containing oligonucleotide


substrate_name: synthetic oligonucleotide

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R274Q with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

substrate: synthetic oligonucleotide


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M270T with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


substrate_name: DNA with an intact AP site

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

proof_lines: kcat is 0.075 sec(-1) for 5'-deoxyribose-phosphate lyase activity (at pH 7.0 and 37 degrees Celsius) (PubMed:9614142). kcat is 0.004 sec(-1) for AP lyase activity (at pH 7.0 and 37 degrees Celsius) (PubMed:9614142).

substrate: DNA with an intact AP site


substrate_name: DNA containing dihydrouracil

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K212R to reconstruct the assayed variant sequence.

substrate: DNA containing dihydrouracil


substrate_name: Isochorismate; 2-Oxoglutarate

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

substrate: Isochorismate; 2-Oxoglutarate


substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication, inhibition of salicylate synthase activity

proof_lines: kcat is 1.01 sec(-1) for lyase activity (at pH 7.5 and 22 degrees Celsius). kcat is 23.5 sec(-1) for chorismate mutase activity (at pH 7.5 and 22 degrees Celsius). kcat is 106 min(-1) for lyase activity (at pH 7 and 30 degrees Celsius). kca

substrate: Unknown


substrate_name: 1,6-tuliposide D

substrate: 1,6-tuliposide D


substrate_name: 7,8-Dihydroneopterin 3'-triphosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S19A to reconstruct the assayed variant sequence.

proof_lines:
PTPS-S19A
6-pyruvoyltetrahydropterin synthase
7,8-dihydroneopterin 3'-triphosphate

substrate: 7,8-Dihydroneopterin 3'-triphosphate


substrate_name: DNA containing 5-hydroxycytosine

substrate: DNA containing 5-hydroxycytosine


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: dihydrouracil containing duplex oligonucleotides (N-glycosylase activity)

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


substrate: dihydrouracil containing duplex oligonucleotides (N-glycosylase activity)


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

substrate_name: 5-hydroxy-6-hydrothymine containing duplex oligonucleotides (N-glycosylase activity)


organism: Coprinopsis cinerea

substrate_name: (2E,6E)-farnesyl diphosphate

proof_lines: wild-type enzyme, and mutants H235P and N239L, pH 8.0, 30°C

substrate: (2E,6E)-farnesyl diphosphate


proof_lines: Cop6 loop graft mutant Cop6L4, pH 8.0, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K233I to reconstruct the assayed variant sequence.


substrate_name: 6-tuliposide A

substrate: 6-tuliposide A


substrate_name: 6-tuliposide B

substrate: 6-tuliposide B


substrate_name: tuliposide F

substrate: tuliposide F


organism: Arabidopsis thaliana

column_label: The ACS full article Table 1 row 8-OH-Gua reports KM (nM) under air as 2287 +/- 242; this normalizes to 0.002287 mM and matches the expected 0.00229 mM within rounding.

raw_value_unit_evidence: Km raw_value=2287 +/- 242 raw_unit=nM

table_label: Table 1: Kinetic Constants for Excision of 8-OH-Gua and FapyGua by AtOgg1 from DNA gamma-Irradiated under Air or N2O


column_label: The ACS full article Table 1 row FapyGua reports KM (nM) under air as 3600 +/- 824; this normalizes to 0.0036 mM and matches the expected 0.0036000000000000003 mM.

raw_value_unit_evidence: Km raw_value=3600 +/- 824 raw_unit=nM

row_label: FapyGua


substrate_name: isochorismate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I87T to reconstruct the assayed variant sequence.

substrate: isochorismate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K42A to reconstruct the assayed variant sequence.

proof_lines: mutant K42A, presence of ethylamine, pH 8.0, 20°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K42H to reconstruct the assayed variant sequence.

proof_lines:
mutant K42H, pH 7.5, 25°C
mutant K42H, pH 5.0, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K42E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A43P to reconstruct the assayed variant sequence.


enzyme_display_name: 2-deoxy-scyllo-inosose synthase

organism: Bacillus circulans

substrate_name: NAD+

assay_conditions_summary: pH 7.7; 319.15 K; cofactor NAD+

enzyme: 2-deoxy-scyllo-inosose synthase

substrate: NAD+


column_label: Table 2 Kinetic parameters of the recombinant TgTCEs for 6-PosA/B and PosD/F; TgTCEA1 block; substrate row 'PosD [d]'; column 'Km (mM)' = 2.0 +/- 0.090; column 'kcat (s^-1)' = 3300 +/- 61; column 'kcat/Km (s^-1/mM)' = 1700; column 'Relative efficiency (%)' as printed for that row.

normalized_value_unit_evidence: Km: paper cell 2.0 +/- 0.090 mM; no conversion needed, 2.0 mM = catalog km 2.0 mM. kcat: paper cell 3300 +/- 61 s^-1; no conversion needed, 3300.0 s^-1 = catalog kcat 3300.0 s^-1. kcat/Km: the catalog value 1650.0 s^-1 mM^-1 is the exact quotient 3300.0 / 2.0 of this row's own printed cells; the printed kcat/Km cell of the same row is the two-significant-figure value 1700 s^-1/mM and is not the stored number.

raw_value_unit_evidence: Table 2, TgTCEA1 block, substrate row `PosD [d]`: Km = 2.0 +/- 0.090 mM; kcat = 3300 +/- 61 s^-1; printed kcat/Km = 1700 s^-1/mM.

row_label: Table 2, TgTCEA1 block, substrate row 'PosD [d]'


column_label: Table 2 Kinetic parameters of the recombinant TgTCEs for 6-PosA/B and PosD/F; TgTCEA1 block; substrate row 'PosF [d]'; column 'Km (mM)' = 3.2 +/- 0.15; column 'kcat (s^-1)' = 780 +/- 26; column 'kcat/Km (s^-1/mM)' = 240; column 'Relative efficiency (%)' as printed for that row.

normalized_value_unit_evidence: Km: paper cell 3.2 +/- 0.15 mM; no conversion needed, 3.2 mM = catalog km 3.2 mM. kcat: paper cell 780 +/- 26 s^-1; no conversion needed, 780.0 s^-1 = catalog kcat 780.0 s^-1. kcat/Km: the catalog value 243.75 s^-1 mM^-1 is the exact quotient 780.0 / 3.2 of this row's own printed cells; the printed kcat/Km cell of the same row is the two-significant-figure value 240 s^-1/mM and is not the stored number.

raw_value_unit_evidence: Table 2, TgTCEA1 block, substrate row `PosF [d]`: Km = 3.2 +/- 0.15 mM; kcat = 780 +/- 26 s^-1; printed kcat/Km = 240 s^-1/mM.

row_label: Table 2, TgTCEA1 block, substrate row 'PosF [d]'


proof_lines:
6-tuliposide A
tuliposide A-converting enzyme
Tulipa gesneriana


proof_lines:
6-tuliposide B
tuliposide-converting enzyme
Tulipa gesneriana


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K42C with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

proof_lines: mutant K42C, treatment with bromoethanol, pH 8.0, 20°C

proof_lines: mutant K42C, treatment with bromoethylamine, pH 8.0, 20°C


sequence_variant_note: Mutation signature C7A/K42C could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant C7A/K42C, treatment with bromoethanol, pH 8.0, 20°C

proof_lines: mutant C7A/K42C, treatment with bromoethylamine, pH 8.0, 20°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C7A to reconstruct the assayed variant sequence.


organism: Micromonospora echinospora

substrate_name: D-glucose 6-phosphate

substrate: D-glucose 6-phosphate


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -12, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature Q91N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Streptomyces tenjimariensis

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


organism: Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)

substrate_name: all-trans-farnesyl diphosphate

substrate: all-trans-farnesyl diphosphate


organism: Niallia circulans

substrate_name: NAD(+) (at pH 7.7 and 46 degrees Celsius)

assay_conditions_summary: cofactor NAD+

column_label: Abstract reports Km for D-glucose-6-phosphate was 9.0 x 10(-4) M and that for NAD+ 1.7 x 10(-4) M.

raw_value_unit_evidence: Km raw_value=1.7 x 10(-4) M raw_unit=M

row_label: Bacillus circulans 2-deoxy-scyllo-inosose synthase / NAD+

table_label: PubMed XML abstract PMID 10344560


organism: Abies grandis

substrate_name: GGPP (in presence of magnesium)

column_label: PMID 11112547 page 15598, Results prose beside Figure 4; substrate GGPP; metric Km.

raw_value_unit_evidence: Fitting the kinetic data for GGPP yielded Km = 3 plus/minus 0.8 uM, Ki = 5 plus/minus 2 uM, and kcat = 0.75 plus/minus 0.15 s^-1.

row_label: Recombinant abietadiene synthase / GGPP

table_label: Results prose with Figure 4 steady-state kinetic plots

substrate: GGPP (in presence of magnesium)


column_label: Table 1 row Cop4, (E,E)-FPP Km column reports 11+/-3 uM.

raw_value_unit_evidence: Km raw_value=11+/-3 raw_unit=uM

row_label: Cop4 / (E,E)-FPP

table_label: PMC2873112 Table 1, kinetic constants of Cop4 and Cop6


substrate_name: farnesyl diphosphate

substrate: farnesyl diphosphate


proof_lines: isoform TCEA-b1, pH not specified in the publication, temperature not specified in the publication

proof_lines: kcat is 1400 sec(-1) with 6-tuliposide A as substrate. kcat is 610 sec(-1) with 6-tuliposide B as substrate.


proof_lines: kcat is 3200 sec(-1) with 6-tuliposide A as substrate. kcat is 720 sec(-1) with 6-tuliposide B as substrate.


organism: Phyla dulcis

proof_lines:
(+)-epi-alpha-bisabolol synthase
Km 4.8 uM
kcat 0.04 s^-1


enzyme_display_name: Delta(6)-protoilludene synthase

organism: Armillaria gallica

substrate_name: trans,trans-Farnesyl diphosphate

assay_conditions_summary: pH 7.2; buffer tritium-labeled farnesyl diphosphate in MOPS/MgCl2/2-mercaptoethanol

column_label: PMC full-text Enzymatic Characterization section reports Km for farnesyl diphosphate as 0.53 uM, normalized to 0.00053 mM.

normalized_value_unit_evidence: Km normalized_value=0.00053 normalized_unit=mM from 0.53 uM.

raw_value_unit_evidence: PMC full-text prose: experiments revealed a Km for farnesyl diphosphate of 0.53 uM.

row_label: A. gallica protoilludene synthase farnesyl diphosphate Km sentence

table_label: Enzymatic Characterization prose

enzyme: Delta(6)-protoilludene synthase

substrate: trans,trans-Farnesyl diphosphate


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

substrate_name: chorismate (at pH 7.5 and 22 degrees Celsius)


enzyme_display_name: myrcene synthase

organism: Artemisia annua

substrate_name: geranyl diphosphate

column_label: Table 1; row AaTPS2; column K_m (uM) cell 8.25; column K_cat (s^-1) cell 0.52; column K_cat/K_m (s^-1 M^-1) cell 6.31 x 10^4. Column headers as printed: (enzyme) | K_m (μM) | K_cat (s^-1) | K_cat/K_m (s^-1 •M^-1)

normalized_value_unit_evidence: K_m 8.25 uM = 8.25/1000 = 0.00825 mM. K_cat 0.52 s^-1 = 0.52 s^-1 (already the canonical kcat unit). kcat/Km taken as this same row's K_cat divided by its K_m: 0.52 / 0.00825 = 63.03030303030303 s^-1 mM^-1. The table's own efficiency column prints 6.31 x 10^4 s^-1 M^-1 = 63.1 s^-1 mM^-1, which does NOT reproduce the quotient of the same row's printed K_m and K_cat (63.03 s^-1 mM^-1) at three significant figures; the paper's efficiency column is internally inconsistent with its own K_m/K_cat cells for this row. The value recorded here is the quotient of the two cells actually printed for this row, not the paper's separately printed efficiency figure.

raw_value_unit_evidence: Table 1. Kinetic parameters of AaTPS2, AaTPS5, and AaTPS6 proteins. Row AaTPS2: column K_m (uM) cell 8.25; column K_cat (s^-1) cell 0.52; column K_cat/K_m (s^-1 M^-1) cell 6.31 x 10^4.

enzyme: myrcene synthase

substrate: geranyl diphosphate


enzyme_display_name: 5-phosphooxy-L-lysine phospho-lyase

substrate_name: 5-phosphohydroxy-L-lysine (at 30 degrees Celsius)

column_label: Results report a Km for 5P Hyl of 16.9 +/- 4.5 uM and Vmax 256 +/- 15 nmol min^-1 mg^-1 protein.

raw_value_unit_evidence: Km raw_value=16.9 +/- 4.5 raw_unit=uM

row_label: AGXT2L2 with 5P Hyl

table_label: PMC3293546 Figure 4B / 5PHyl-phospholyase Results prose

enzyme: 5-phosphooxy-L-lysine phospho-lyase


organism: Humulus lupulus

column_label: Results prose reports purified His-tagged recombinant HlMTS2 had Km for geranyl pyrophosphate of 7.65 +/- 2.40 uM (n=3).

raw_value_unit_evidence: Km raw_value=7.65 +/- 2.40 uM raw_unit=uM

row_label: Purified His-tagged recombinant HlMTS2 / geranyl pyrophosphate

table_label: PMC2577278 Results prose, Functional Identification of Hop Monoterpene Synthases


organism: Quercus ilex

column_label: Table 2 reports mean Michaelis constant Km for myrcene formation from GDP = 84 +/- 14 uM.

raw_value_unit_evidence: Km raw_value=84 +/- 14 uM raw_unit=microM

row_label: Mean Michaelis constant for myrcene formation from GDP

table_label: Wiley full text Table 2: Biochemical properties of purified MyrS


enzyme_display_name: 2-epi-valiolone synthase

organism: Actinosynnema mirum

substrate_name: D-sedoheptulose 7-phosphate

assay_conditions_summary: pH 7; 301.15 K; cofactor NAD+

raw_value_unit_evidence: Km raw_value=59.9 microM raw_unit=microM raw_cell=59.9 +/- 13.4; kcat raw_value=2.0 min^-1 raw_unit=min^-1 raw_cell=2.0 +/- 0.1; kcat/Km raw_value=0.033 microM^-1 min^-1 raw_unit=microM^-1 min^-1 raw_cell=0.033 +/- 0.004

enzyme: 2-epi-valiolone synthase

substrate: D-sedoheptulose 7-phosphate


enzyme_display_name: (4S)-limonene synthase

organism: Mentha spicata

substrate_name: Geranyl diphosphate

enzyme: (4S)-limonene synthase

substrate: Geranyl diphosphate


enzyme_display_name: taxadiene synthase

organism: Taxus canadensis

substrate_name: geranylgeranyl diphosphate

enzyme: taxadiene synthase

substrate: geranylgeranyl diphosphate


organism: Stigmatella aurantiaca

normalized_value_unit_evidence: Normalized values: Km=0.0386 mM; catalog-precision kcat=0.062 s^-1 from 3.7 min^-1; independently printed kcat/Km=1.6 s^-1 mM^-1; current quotient-derived kcat/Km=1.6062176165803108 s^-1 mM^-1.

table_label: Table 1. Apparent kinetic values for ValA, Amir_2000, Staur_3140, Npun_5600, and Ava_3858


enzyme_display_name: germacrene-A synthase

substrate_name: (2E,6E)-farnesyl diphosphate

proof_lines:
Humulus lupulus
hop sesquiterpene synthase
germacrene A

enzyme: germacrene-A synthase


enzyme_display_name: demethyl-4-deoxygadusol synthase

organism: Trichormus variabilis

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

normalized_value_unit_evidence: Km normalized_value=0.0216 normalized_unit=mM; kcat normalized_value=0.0533 normalized_unit=s^(-1); kcat/Km normalized_value=2.4667 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Km raw_value=21.6 microM raw_unit=microM raw_cell=21.6 +/- 2.8; kcat raw_value=3.2 min^-1 raw_unit=min^-1 raw_cell=3.2 +/- 0.3; kcat/Km raw_value=0.148 microM^-1 min^-1 raw_unit=microM^-1 min^-1 raw_cell=0.148 +/- 0.005

enzyme: demethyl-4-deoxygadusol synthase


enzyme_display_name: germacradienol synthase

organism: Streptomyces coelicolor

enzyme: germacradienol synthase


enzyme_display_name: ethanolamine-phosphate phospho-lyase

organism: Homo sapiens

substrate_name: phosphoethanolamine (at pH 7.4)

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

proof_lines:
AGXT2L1
phosphoethanolamine phospho-lyase
phosphoethanolamine

enzyme: ethanolamine-phosphate phospho-lyase

substrate: phosphoethanolamine (at pH 7.4)


enzyme_display_name: amorpha-4,11-diene synthase

substrate_name: magnesium ions

column_label: Official PubMed XML abstract reports Mg2+ Km = 70 uM, respectively ordered after farnesyl diphosphate.

normalized_value_unit_evidence: Km normalized_value=0.07 normalized_unit=mM for Mg2+

raw_value_unit_evidence: Km raw_value=70 raw_unit=uM for Mg2+

row_label: Recombinant amorpha-4,11-diene synthase

table_label: Official PubMed XML abstract kinetic prose

enzyme: amorpha-4,11-diene synthase

substrate: magnesium ions


substrate_name: farnesyl diphosphate (at 30 degrees Celsius)

column_label: Abstract reports amorpha-4,11-diene synthase has a K(m) of 0.6 microM.

raw_value_unit_evidence: Km raw_value=0.6 microM raw_unit=microM

row_label: Artemisia annua amorpha-4,11-diene synthase / farnesyl diphosphate

table_label: PubMed XML abstract PMID 10626375


enzyme_display_name: S-linalool synthase

organism: Clarkia breweri

column_label: Abstract states S-linalool synthase has a Km of 0.9 microM for geranyl pyrophosphate and shows an optimal pH of 7.4.

raw_value_unit_evidence: Km raw_value=0.9 raw_unit=microM

row_label: Clarkia breweri S-linalool synthase with geranyl pyrophosphate

table_label: PubMed abstract PMID 7864636

enzyme: S-linalool synthase


enzyme_display_name: isoprene synthase

organism: Populus alba

substrate_name: dimethylallyl diphosphate

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

column_label: Full text section 3.4 states that recombinant PaIspS produced isoprene from DMAPP and that the apparent K_m value of recombinant PaIspS for DMAPP was determined as 8.7 mM.

raw_value_unit_evidence: Km raw_value=8.7 raw_unit=mM

row_label: recombinant PaIspS / DMAPP

table_label: Wiley full text PMID 15848197 section 3.4 PaIspS enzymatic characterization

enzyme: isoprene synthase

substrate: dimethylallyl diphosphate


organism: Populus tremuloides


enzyme_display_name: R-linalool synthase

substrate_name: magnesium

column_label: Abstract reports QH1-linalool synthase displays a K(m) value of 64 microM for geranyl diphosphate and a K(m) value of 4.6 mM for Mg(+2).

raw_value_unit_evidence: Km raw_value=4.6 mM raw_unit=mM

row_label: Artemisia annua QH1-linalool synthase / Mg(+2)

table_label: PubMed XML abstract PMID 10562427

enzyme: R-linalool synthase

substrate: magnesium


organism: Pueraria montana

substrate_name: Dimethylallyl diphosphate

substrate: Dimethylallyl diphosphate


enzyme_display_name: ent-sandaracopimaradiene synthase

organism: Oryza sativa subsp. japonica

substrate_name: 9alpha-copalyl diphosphate

proof_lines:
OsKSL10
9alpha-copalyl diphosphate
syn-copalyl diphosphate

enzyme: ent-sandaracopimaradiene synthase

substrate: 9alpha-copalyl diphosphate


enzyme_display_name: methylglyoxal synthase

substrate_name: D-glyceraldehyde 3-phosphate (at pH 7.4 and 25 degrees Celsius)

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +3, so it is treated as a source-provided variant sequence.

proof_lines: human triosephosphate isomerase deficiency

enzyme: methylglyoxal synthase


enzyme_display_name: epi-isozizaene synthase

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

proof_lines:
pH 6.5, 30°C
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=6.5

enzyme: epi-isozizaene synthase

substrate: (2E,6E)-farnesyl diphosphate


organism: Mentha aquatica var. citrata


enzyme_display_name: ent-pimara-9(11),15-diene synthase

organism: Streptomyces sp.

substrate_name: ent-copalyl diphosphate

column_label: PMID 17148547 Table 1, PMD synthase row, ent-CDP substrate: Km = 2.6 +/- 0.2 uM and kcat = 1.4 x 10^-3 s^-1; no metric-labeled kcat/Km cell.

raw_value_unit_evidence: Table 1 reports Km = 2.6 +/- 0.2 uM and kcat = 1.4 x 10^-3 s^-1 for PMD synthase with ent-CDP; no kcat/Km value is printed.

row_label: PMD synthase / ent-CDP

table_label: Table 1. Kinetic properties of ent-CDP synthase and PMD synthase

enzyme: ent-pimara-9(11),15-diene synthase

substrate: ent-copalyl diphosphate


enzyme_display_name: alpha-bisabolene synthase

organism: Abies grandis

enzyme: alpha-bisabolene synthase


enzyme_display_name: epi-cedrol synthase

organism: Artemisia annua

substrate_name: magnesium (at pH 7.0)

enzyme: epi-cedrol synthase

substrate: magnesium (at pH 7.0)


organism: Thermus sp.

substrate_name: dihydroxyacetone phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R97E to reconstruct the assayed variant sequence.

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

proof_lines:
Thermus sp.
methylglyoxal synthase
dihydroxyacetone phosphate

substrate: dihydroxyacetone phosphate


enzyme_display_name: 3-dehydroquinate synthase

organism: Escherichia coli

enzyme: 3-dehydroquinate synthase


enzyme_display_name: UniProt Q9LCC6

organism: Bacillus sp. (in: Bacteria)

substrate_name: fumarate

enzyme: UniProt Q9LCC6

substrate: fumarate


enzyme_display_name: UniProt Q6KC22

organism: Anaerotignum propionicum

substrate_name: beta-alanyl-CoA

enzyme: UniProt Q6KC22

substrate: beta-alanyl-CoA


substrate_name: acryloyl-CoA

substrate: acryloyl-CoA


smiles: N


organism: Neurospora crassa

assay_conditions_summary: buffer a phosphate-free


enzyme_display_name: beta-farnesene synthase

enzyme: beta-farnesene synthase


enzyme_display_name: alpha-farnesene synthase

organism: Melampsora lini

substrate_name: farnesyl diphosphate

column_label: The full-text kinetic paragraph states that the apparent Km values of MliILTPS2 and MliILTPS3 using FDP were 1.9 +/- 0.3 uM and 1.6 +/- 0.2 uM, respectively; the selected row is the MliILTPS2/FDP entry.

raw_value_unit_evidence: Km raw_value=1.9 +/- 0.3 raw_unit=uM

row_label: MliILTPS2 recombinant enzyme / FDP substrate

table_label: Scientific Reports PMID 32913319 Results paragraph: ILTPS genes encode active terpene synthases

enzyme: alpha-farnesene synthase

substrate: farnesyl diphosphate


enzyme_display_name: (3S,6E)-nerolidol synthase

organism: Zea mays

proof_lines:
(E)-nerolidol synthase
farnesyl diphosphate
(3S)-(E)-nerolidol

enzyme: (3S,6E)-nerolidol synthase


enzyme_display_name: beta-alanyl-CoA ammonia-lyase

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

assay_conditions_summary: pH 7; cofactor CoA

enzyme: beta-alanyl-CoA ammonia-lyase


enzyme_display_name: aspartate ammonia-lyase

organism: Bacterium cadaveris

substrate_name: L-aspartate

proof_lines:
Tris buffer, pH 7.0
phosphate buffer, pH 7.0
phosphate buffer, pH 6.8

enzyme: aspartate ammonia-lyase

substrate: L-aspartate


organism: Clostridium cylindrosporum


substrate_name: (-)-formiminotetrahydrofolate

substrate: (-)-formiminotetrahydrofolate


enzyme_display_name: histidine ammonia-lyase

organism: Achromobacter liquidum

substrate_name: L-histidine

enzyme: histidine ammonia-lyase

substrate: L-histidine


organism: Ligilactobacillus murinus


enzyme_display_name: (3R,6E)-nerolidol synthase

organism: Tripterygium wilfordii

substrate_name: (2E,6E)-farnesyl diphosphate

normalized_value_unit_evidence: Km normalized_value=0.0127 normalized_unit=mM; Kcat normalized_value=0.371 normalized_unit=s^-1; Kcat/Km paper rounded normalized_value=29.0 normalized_unit=s^-1*mM^-1; exported central ratio 0.371/0.0127=29.212598425196852 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=12.700 +/- 1.900 raw_unit=uM; Kcat raw_value=0.371 +/- 0.011 raw_unit=s^-1; Kcat/Km raw_value=0.029 +/- 0.006 raw_unit=s^-1/uM

row_label: TwNES / (E,E)-FPP row

table_label: Figure 5, kinetic analysis table for purified recombinant NES and GES1 proteins

enzyme: (3R,6E)-nerolidol synthase


organism: Bacillus sp. (in: firmicutes)

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S319A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature P322A to reconstruct the assayed variant sequence.


enzyme_display_name: beta-copaene synthase

organism: Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)

substrate_name: all-trans-farnesyl diphosphate

enzyme: beta-copaene synthase

substrate: all-trans-farnesyl diphosphate


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

proof_lines: kcat is 4.908 sec(-1) with L-aspartate as substrate. kcat is 8.002 sec(-1) with L-phenylalanine as substrate. kcat is 13.64 sec(-1) with fumarate as substrate.


substrate_name: L-phenylalanine

substrate: L-phenylalanine


organism: Bacillus sp

substrate_name: NH(3) (for the recombinant His6-tagged enzyme)

proof_lines: kcat is 40 sec(-1) with L-aspartate as substrate (for the recombinant His6-tagged enzyme) (PubMed:18844200). kcat is 89 sec(-1) with NH(3) as substrate (for the recombinant His6-tagged enzyme) (PubMed:18844200).


organism: Bacillus sp. YM55-1

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T141A to reconstruct the assayed variant sequence.


substrate_name: L-Aspartate

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8.5
kcat is 40.6 min(-1).

source_databases_merged: sabio_rk skid uniprot

substrate: L-Aspartate


enzyme_display_name: methylaspartate ammonia-lyase

organism: Clostridium tetanomorphum

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

assay_conditions_summary: pH 9

proof_lines:
pH 9.0, 30°C
recombinant 3-methylaspartase
pH 9.7

enzyme: methylaspartate ammonia-lyase


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

proof_lines: kcat is 61 sec(-1) for amination of mesaconate (with 20 mM of MgCl(2) at pH 9 and at 30 degrees Celsius). kcat is 89 sec(-1) for deamination of L-threo-beta-methylaspartate (with 20 mM of MgCl(2) at pH 9 and at 30 degrees Celsius).


organism: Fusobacterium varium


enzyme_display_name: thebaine synthase

organism: Papaver somniferum

substrate_name: Unknown

enzyme: thebaine synthase

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M321A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I320A with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N142Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N326Q with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


organism: Pseudomonas putida

proof_lines: kcat is 1.5 sec(-1) with L-histidine as substrate.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T141K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S140A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N326A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


organism: Escherichia coli (strain K12)


organism: Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)

proof_lines: kcat is 16 sec(-1) for aminase activity with mesaconate (at pH 9 and 30 degrees Celsius). kcat is 16 sec(-1) for deaminase activity with L-threo-beta-methylaspartate (at pH 9 and 30 degrees Celsius). kcat is 78 sec(-1) for deaminase activit


substrate_name: mesaconate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C361A to reconstruct the assayed variant sequence.

column_label: PDF text lines 151-175 and rendered page 3 contain Table 1; row C361A; columns kcat, Km for 1, and kcat/Km.

raw_value_unit_evidence: Table 1 C361A row reports kcat 27.5 s^-1, Km 2.9 mM, and kcat/Km 9.5 x 10^3 M^-1 s^-1.

table_label: Table 1. Apparent kinetic parameters for the amination of mesaconate (1) catalyzed by wild-type or mutant MAL

substrate: mesaconate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F170A to reconstruct the assayed variant sequence.

column_label: PDF text lines 151-175 and rendered page 3 contain Table 1; row F170A; columns kcat, Km for 1, and kcat/Km.

raw_value_unit_evidence: Table 1 F170A row reports kcat 10 s^-1, Km 0.9 mM, and kcat/Km 1.1 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L384A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q172A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q73A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

column_label: PDF text lines 151-175 and rendered page 3 contain Table 1; row Q73A; columns kcat, Km for 1, and kcat/Km.

raw_value_unit_evidence: Table 1 Q73A row reports kcat 0.7 s^-1, Km 0.2 mM, and kcat/Km 3.5 x 10^3 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T360A to reconstruct the assayed variant sequence.

column_label: PDF text lines 151-175 and rendered page 3 contain Table 1; row T360A; columns kcat, Km for 1, and kcat/Km.

normalized_value_unit_evidence: kcat 0.6 s^-1; Km 15 mM; kcat/Km 0.04 s^-1 mM^-1 after dividing 40 M^-1 s^-1 by 1000.

raw_value_unit_evidence: Table 1 T360A row reports kcat 0.6 s^-1, Km 15 mM, and kcat/Km 40 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T360S to reconstruct the assayed variant sequence.

column_label: PDF text lines 151-175 and rendered page 3 contain Table 1; row T360S; columns kcat, Km for 1, and kcat/Km.

raw_value_unit_evidence: Table 1 T360S row reports kcat 35 s^-1, Km 1.4 mM, and kcat/Km 2.5 x 10^4 M^-1 s^-1.


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

column_label: PDF text lines 151-175 and rendered page 3 contain Table 1; row MAL; columns kcat, Km for 1, and kcat/Km.

raw_value_unit_evidence: Table 1 MAL row reports kcat 61 s^-1, Km 0.7 mM, and kcat/Km 8.7 x 10^4 M^-1 s^-1.

row_label: MAL


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y356A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


substrate_name: L-threo-beta-methylaspartate (with 4 mM of KCl at pH 9.76 and at 25 degrees Celsius)


organism: Cavia porcellus


organism: Homo sapiens

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


substrate_name: L-threo-3-methylaspartic acid

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q329A to reconstruct the assayed variant sequence.

substrate: L-threo-3-methylaspartic acid


substrate_name: mesaconic acid

substrate: mesaconic acid


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature H194A to reconstruct the assayed variant sequence.


proof_lines:
wild-type
pH 9, 30°C, wild-type


organism: Bacillus sp. (in: Bacteria)

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P322A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S319A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature T360A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q73A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y356A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature F170A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature L384A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q172A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C361A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +7, so it is treated as a source-provided variant sequence.


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C273A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +1, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C389A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -14, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H123L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K326R with inferred residue-numbering offset +1 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.


enzyme_display_name: chorismate synthase

organism: Capnoides sempervirens

proof_lines:
chorismate synthase
shikimate pathway
reduced FMN

enzyme: chorismate synthase


organism: Neurospora crassa


organism: Pseudomonas aeruginosa

substrate_name: fumarate


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


organism: Staphylococcus aureus

substrate_name: EPSP

proof_lines:
chorismate synthase
aroC
Staphylococcus aureus

substrate: EPSP


substrate_name: mesaconate (at pH 9 and 30 degrees Celsius)


organism: Lavandula angustifolia

substrate_name: geranyl diphosphate

column_label: Full-text prose reports Km 6.55 +/- 1.01 uM, kcat 1.7 x 10^-2 s^-1, and catalytic efficiency (kcat/Km) 2.83 x 10^-3 uM^-1*s^-1 for La beta-PHLS with GPP

normalized_value_unit_evidence: explicit paper kcat/Km normalized_value=2.83 normalized_unit=s^-1*mM^-1 does not match expected 2.595419847328244

raw_value_unit_evidence: Km raw_value=6.55 +/- 1.01 raw_unit=uM; kcat raw_value=1.7 x 10^-2 raw_unit=s^-1; catalytic_efficiency raw_value=2.83 x 10^-3 raw_unit=uM^-1*s^-1

row_label: La beta-PHLS / GPP kinetic constants

table_label: PMID 21165645 Springer full-text biochemical characterization prose

substrate: geranyl diphosphate


proof_lines:
pH 9.2 and pH 7.0, epidermal enzyme
pH 9.2, liver enzyme
pH 7.0, liver enzyme


enzyme_display_name: gamma-humulene synthase

organism: Abies grandis

substrate_name: trans,trans-Farnesyl diphosphate

proof_lines:
gamma-humulene synthase
trans,trans-Farnesyl diphosphate
Abies grandis

enzyme: gamma-humulene synthase

substrate: trans,trans-Farnesyl diphosphate


enzyme_display_name: (-)-beta-caryophyllene synthase

organism: Artemisia annua

proof_lines:
Artemisia annua
beta-caryophyllene synthase
farnesyl diphosphate

enzyme: (-)-beta-caryophyllene synthase

substrate: (2E,6E)-farnesyl diphosphate


enzyme_display_name: (S)-beta-bisabolene synthase

organism: Santalum album

enzyme: (S)-beta-bisabolene synthase


organism: Vitis vinifera

column_label: Section 2.1 prose; segment purified recombinant VvGwECar2 enzyme assay with FPP; metric labels Km, kcat, and efficiency (kcat/Km).

normalized_value_unit_evidence: kcat normalized_value=0.19 normalized_unit=s^-1 | km normalized_value=0.0314 normalized_unit=mM | kcat_over_km normalized_value=6.1 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Section 2.1 prose: Km = 31.4 microM; kcat = 0.19 s^-1; efficiency kcat/Km = 6.1 mM^-1 s^-1.

row_label: Purified recombinant VvGwECar2 enzyme assay with farnesyl pyrophosphate (FPP)

table_label: Section 2.1. Bacterial VvGwECar2 expression and characterization


organism: Arabidopsis thaliana

substrate_name: farnesyl diphosphate

column_label: Full text states that At5g44630 and At5g23960 TPS enzymes showed apparent K_m values of 1.2 and 2.1 uM, respectively, for FPP; the second value maps to At5g23960.

raw_value_unit_evidence: Km raw_value=2.1 raw_unit=uM

row_label: At5g23960 TPS / FPP

table_label: Wiley free full text PMID 15918888 TPS enzymatic properties prose


enzyme_display_name: alpha-bisabolene synthase

organism: Ginkgo biloba

substrate_name: (2E,6E)-farnesyl diphosphate

enzyme: alpha-bisabolene synthase


enzyme_display_name: patchoulol synthase

organism: Pogostemon cablin

enzyme: patchoulol synthase


substrate_name: (2Z,6E)-farnesyl diphosphate

substrate: (2Z,6E)-farnesyl diphosphate


enzyme_display_name: trichodiene synthase

organism: Fusarium sporotrichioides

proof_lines:
trichodiene synthetase
Fusarium sporotrichioides
farnesyl pyrophosphate

enzyme: trichodiene synthase

substrate: farnesyl diphosphate


enzyme_display_name: (E,E)-germacrene B synthase

proof_lines:
Abies grandis
sesquiterpene synthase
farnesyl diphosphate

enzyme: (E,E)-germacrene B synthase


enzyme_display_name: pentalenene synthase

organism: Streptomyces exfoliatus

proof_lines: pentalenene synthase from Streptomyces exfoliatus UC5319

enzyme: pentalenene synthase


enzyme_display_name: presilphiperfolanol synthase

organism: Botrytis cinerea

enzyme: presilphiperfolanol synthase


enzyme_display_name: (-)-germacrene D synthase

organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)

substrate_name: FPP

enzyme: (-)-germacrene D synthase

substrate: FPP


enzyme_display_name: (+)-germacrene D synthase

organism: Actinidia deliciosa

enzyme: (+)-germacrene D synthase


enzyme_display_name: valencene synthase

organism: Callitropsis nootkatensis

enzyme: valencene synthase


organism: Zingiber officinale

substrate_name: (2E,6E)-farnesyl diphosphate (in presence of magnesium)

column_label: Abstract reports Km- and kcat-values are 0.88 microM and 3.34 x 10(-3) s(-1), respectively.

raw_value_unit_evidence: Km raw_value=0.88 microM raw_unit=microM

row_label: Recombinant (+)-germacrene D synthase / FPP

table_label: PubMed XML abstract PMID 16839518


enzyme_display_name: exo-alpha-bergamotene synthase

enzyme: exo-alpha-bergamotene synthase


enzyme_display_name: (+)-delta-selinene synthase

enzyme: (+)-delta-selinene synthase


normalized_value_unit_evidence: Km: printed Results value 1.4 uM (apparent, +/- 0.3); 1.4 / 1000 = 0.0014 mM; the exported value is 0.0014 mM, an exact match. kcat: printed Results value 0.34 s^-1 for SaSSy; already in s^(-1), no conversion is applied (this paper prints no min^-1 kinetic value); the exported value is 0.34 s^(-1), an exact match. kcat/Km: the paper prints no kcat/Km value, so nothing is converted; the exported 242.8571428571429 s^(-1)*mM^(-1) is carried unchanged and typed as the full-precision quotient 0.34 / 0.0014 of this row's own two confirmed components.

raw_value_unit_evidence: Results prose, journal page 17449 (PDF page 5). Km sentence, decoded from the 300 dpi render: 'Each santalene synthase had an apparent Km of 1.4 (+/- 0.3) uM, indicating a biologically relevant, high affinity for (E,E)-FPP.' kcat sentence, decoded: 'Catalytic turnover rates were similar for all three enzymes, with a kcat for SaSSy of 0.34 s^-1, 0.91 s^-1 for SauSSy, and 2.6 s^-1 for SpiSSy.' For SaSSy, the Santalum album santalene synthase, that pair reads Km = 1.4 uM and kcat = 0.34 s^-1. The paper prints no kcat/Km value for this or any other enzyme.

row_label: SaSSy | Santalum album santalene synthase | (E,E)-FPP


organism: Santalum austrocaledonicum

normalized_value_unit_evidence: Km: printed Results value 1.4 uM (apparent, +/- 0.3); 1.4 / 1000 = 0.0014 mM; the exported value is 0.0014 mM, an exact match. kcat: printed Results value 0.91 s^-1 for SauSSy; already in s^(-1), no conversion is applied (this paper prints no min^-1 kinetic value); the exported value is 0.91 s^(-1), an exact match. kcat/Km: the paper prints no kcat/Km value, so nothing is converted; the exported 650.0 s^(-1)*mM^(-1) is carried unchanged and typed as the full-precision quotient 0.91 / 0.0014 of this row's own two confirmed components.

raw_value_unit_evidence: Results prose, journal page 17449 (PDF page 5). Km sentence, decoded from the 300 dpi render: 'Each santalene synthase had an apparent Km of 1.4 (+/- 0.3) uM, indicating a biologically relevant, high affinity for (E,E)-FPP.' kcat sentence, decoded: 'Catalytic turnover rates were similar for all three enzymes, with a kcat for SaSSy of 0.34 s^-1, 0.91 s^-1 for SauSSy, and 2.6 s^-1 for SpiSSy.' For SauSSy, the Santalum austrocaledonicum santalene synthase, that pair reads Km = 1.4 uM and kcat = 0.91 s^-1. The paper prints no kcat/Km value for this or any other enzyme.

row_label: SauSSy | Santalum austrocaledonicum santalene synthase | (E,E)-FPP