sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UR08 and applied mutation signature N299A/S303A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters for ATAS mutants), body row 'N299A/S303A'; column 'kcat (s-1)' = 0.0058; column 'KM (uM)' = 0.41; column 'kcat/KM (M-1s-1)' = 1.4 x 10^4. The value printed after the plus/minus sign beside the kcat and KM cells of this line is the printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.0058 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.0058 s^(-1). KM: printed Table 2 cell 0.41 in a column headed KM (uM); 1 uM is 0.001 mM, so 0.41 / 1000 = 0.00041 mM. kcat/KM: printed Table 2 cell 1.4 x 10^4 in a column headed kcat/KM (M-1s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.4 x 10^4 / 1000 = 14.0 s^(-1)*mM^(-1). The exported values are kcat 0.0058 s^(-1), Km 0.00041 mM and kcat_over_km 14.146341463414634 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'N299A/S303A': kcat = 0.0058 in a column headed kcat (s-1); KM = 0.41 in a column headed KM (uM); printed kcat/KM = 1.4 x 10^4 in a column headed kcat/KM (M-1s-1).

row_label: Table 2, row N299A/S303A


enzyme_display_name: aristolochene synthase

organism: Aspergillus terreus

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

source_db: oed

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q151E with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

mutation_type: substitution

data_origin: experimental

enzyme: aristolochene synthase

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

status: unverified

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q151H with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UR08 and applied mutation signature S303A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; buffer triplicate on a 100-uL scale in assay

column_label: Table 2 (Steady-state kinetic parameters for ATAS mutants), body row 'S303A'; column 'kcat (s-1)' = 0.045; column 'KM (uM)' = 0.12; column 'kcat/KM (M-1s-1)' = 3.7 x 10^5. The value printed after the plus/minus sign beside the kcat and KM cells of this line is the printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.045 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.045 s^(-1). KM: printed Table 2 cell 0.12 in a column headed KM (uM); 1 uM is 0.001 mM, so 0.12 / 1000 = 0.00012 mM. kcat/KM: printed Table 2 cell 3.7 x 10^5 in a column headed kcat/KM (M-1s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.7 x 10^5 / 1000 = 370.0 s^(-1)*mM^(-1). The exported values are kcat 0.045 s^(-1), Km 0.00012 mM and kcat_over_km 375.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'S303A': kcat = 0.045 in a column headed kcat (s-1); KM = 0.12 in a column headed KM (uM); printed kcat/KM = 3.7 x 10^5 in a column headed kcat/KM (M-1s-1).

row_label: Table 2, row S303A

table_label: Table 2: Steady-state kinetic parameters for ATAS mutants (Biochemistry 2016, 55(20):2864-2874). Printed column heads: Mutant; kcat (s-1); KM (uM); kcat/KM (M-1s-1).

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UR08 and applied mutation signature S303D with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters for ATAS mutants), body row 'S303D'; column 'kcat (s-1)' = 0.00041; column 'KM (uM)' = 0.36; column 'kcat/KM (M-1s-1)' = 1.1 x 10^3. The value printed after the plus/minus sign beside the kcat and KM cells of this line is the printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.00041 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.00041 s^(-1). KM: printed Table 2 cell 0.36 in a column headed KM (uM); 1 uM is 0.001 mM, so 0.36 / 1000 = 0.00036 mM. kcat/KM: printed Table 2 cell 1.1 x 10^3 in a column headed kcat/KM (M-1s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^3 / 1000 = 1.1 s^(-1)*mM^(-1). The exported values are kcat 0.00041 s^(-1), Km 0.00036 mM and kcat_over_km 1.1388888888888888 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'S303D': kcat = 0.00041 in a column headed kcat (s-1); KM = 0.36 in a column headed KM (uM); printed kcat/KM = 1.1 x 10^3 in a column headed kcat/KM (M-1s-1).

row_label: Table 2, row S303D


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UR08 and applied mutation signature S303H with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters for ATAS mutants), body row 'S303H'; column 'kcat (s-1)' = 0.0013; column 'KM (uM)' = 0.061; column 'kcat/KM (M-1s-1)' = 2.1 x 10^4. The value printed after the plus/minus sign beside the kcat and KM cells of this line is the printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.0013 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.0013 s^(-1). KM: printed Table 2 cell 0.061 in a column headed KM (uM); 1 uM is 0.001 mM, so 0.061 / 1000 = 0.000061 mM. kcat/KM: printed Table 2 cell 2.1 x 10^4 in a column headed kcat/KM (M-1s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.1 x 10^4 / 1000 = 21.0 s^(-1)*mM^(-1). The exported values are kcat 0.0013 s^(-1), Km 0.000061 mM and kcat_over_km 21.311475409836063 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'S303H': kcat = 0.0013 in a column headed kcat (s-1); KM = 0.061 in a column headed KM (uM); printed kcat/KM = 2.1 x 10^4 in a column headed kcat/KM (M-1s-1).

row_label: Table 2, row S303H


verification_status: verified

mutation_signature: Unknown

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

column_label: PMC4879067 Table 2 row wild-type columns kcat, KM, and kcat/KM report 0.027 +/- 0.003 s^-1, 0.099 +/- 0.05 uM, and 2.7 x 10^5 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=0.027 s^-1; Km normalized_value=0.000099 mM; kcat/Km normalized_value=270 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 reports wild-type kcat raw_value=0.027 s^-1, KM raw_value=0.099 uM, kcat/KM raw_value=2.7 x 10^5 M^-1 s^-1.

row_label: wild-type ATAS / farnesyl diphosphate

table_label: PMC4879067 Table 2

status: verified


enzyme_display_name: 6-pyruvoyltetrahydropterin synthase

organism: Homo sapiens

substrate_name: 7,8-Dihydroneopterin 3'-triphosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P87L to reconstruct the assayed variant sequence.

enzyme: 6-pyruvoyltetrahydropterin synthase

substrate: 7,8-Dihydroneopterin 3'-triphosphate


kcat_over_km_origin: calculated


enzyme_display_name: 3-dehydroquinate synthase

organism: Escherichia coli

proof_lines:
dehydroquinate synthase
fluorinated substrates
Escherichia coli

enzyme: 3-dehydroquinate synthase


organism: Penicillium roqueforti

source_db: brenda

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y92C to reconstruct the assayed variant sequence.

proof_lines: mutant Y92C, pH 7.5, temperature not specified in the publication

source: brenda


substrate_name: trans,trans-farnesyl diphosphate

sequence_variant_note: Mutation signature Y92A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant Y92A, pH 7.5, temperature not specified in the publication

substrate: trans,trans-farnesyl diphosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q151H with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q151E with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9UR08 and applied mutation signature N299A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters for ATAS mutants), body row 'N299A'; column 'kcat (s-1)' = 0.012; column 'KM (uM)' = 0.41; column 'kcat/KM (M-1s-1)' = 2.9 x 10^4. The value printed after the plus/minus sign beside the kcat and KM cells of this line is the printed uncertainty and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.012 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.012 s^(-1). KM: printed Table 2 cell 0.41 in a column headed KM (uM); 1 uM is 0.001 mM, so 0.41 / 1000 = 0.00041 mM. kcat/KM: printed Table 2 cell 2.9 x 10^4 in a column headed kcat/KM (M-1s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.9 x 10^4 / 1000 = 29.0 s^(-1)*mM^(-1). The exported values are kcat 0.012 s^(-1), Km 0.00041 mM and kcat_over_km 29.26829268292683 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'N299A': kcat = 0.012 in a column headed kcat (s-1); KM = 0.41 in a column headed KM (uM); printed kcat/KM = 2.9 x 10^4 in a column headed kcat/KM (M-1s-1).

row_label: Table 2, row N299A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E227D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8


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


enzyme_display_name: ectoine synthase

organism: Sphingopyxis alaskensis

column_label: PLOS PDF page 11 lines 566-580; section label Kinetic parameters of EctC for N-gamma-ADABA and N-alpha-ADABA; N-alpha-ADABA prose; metric labels apparent Km, kcat, and catalytic efficiency kcat/Km.

raw_value_unit_evidence: Prose reports N-alpha-ADABA Km 25.4 +/- 2.9 mM; kcat 0.6 s^-1; catalytic efficiency 0.02 mM^-1 s^-1.

row_label: N-alpha-ADABA / isomer substrate

table_label: Results prose: Kinetic parameters of EctC for N-gamma-ADABA and N-alpha-ADABA

enzyme: ectoine synthase


enzyme_display_name: (-)-limonene synthase TPS1, chloroplastic

organism: Cannabis sativa

substrate_name: Geranyl pyrophosphate

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

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

substrate: Geranyl pyrophosphate

source: uniprot


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


enzyme: (-)-limonene synthase TPS1, chloroplastic


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


enzyme_display_name: Ent-kaur-16-ene synthase, chloroplastic

organism: Cucurbita maxima

substrate_name: copalyl diphosphate

enzyme: Ent-kaur-16-ene synthase, chloroplastic

substrate: copalyl diphosphate


substrate_name: farnesyl diphosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature F112A to reconstruct the assayed variant sequence.

proof_lines:
mutant F112A-178A
mutant F112A

substrate: farnesyl diphosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature F178I with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature F178V with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature F178C with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature F178Y with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature F178W with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E366A to reconstruct the assayed variant sequence.

proof_lines: E366A variant had a kcat/Km value 100 times lower


proof_lines: wild type and noncomplementing E366A and D510A variants


enzyme_display_name: carotenoid 1,2-hydratase

organism: Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)

substrate_name: lycopene (at pH 8 and at 28 degrees Celsius)

enzyme: carotenoid 1,2-hydratase


substrate_name: neurosporene (at pH 8 and at 28 degrees Celsius)

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


organism: Helicobacter pylori

substrate_name: UDP-N-acetyl-D-glucosamine

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

sequence_source: multiple

proof_lines:
FlaA1
Helicobacter pylori
UDP-GlcNAc

substrate: UDP-N-acetyl-D-glucosamine


enzyme_display_name: ent-kaurene synthase

organism: Marah macrocarpa

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

enzyme: ent-kaurene synthase


enzyme_display_name: (4S)-limonene synthase

organism: Mentha sp.

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

enzyme: (4S)-limonene synthase

substrate: Unknown


organism: Ricciocarpos natans

substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


substrate_name: neryl diphosphate

substrate: neryl diphosphate


substrate_name: (3R)-linalyl diphosphate

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

substrate: (3R)-linalyl diphosphate


enzyme_display_name: abieta-7,13-diene synthase

organism: Abies grandis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E589A to reconstruct the assayed variant sequence.

enzyme: abieta-7,13-diene synthase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E778A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T617A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E773A/E778A 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.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N765A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R762A/E699A/D621A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T848A/Y841F with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E589A/R584A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R586A/T769A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S721A to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation context was captured, but conflicting substitutions targeted the same residue position.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D404N/R411A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W358A/D361A/D404A/D405E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D402E/D405E/R454A/E499A/Y520A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D405N/R365A with inferred residue-numbering offset +25 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K86A/R87A with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D96A to reconstruct the assayed variant sequence.


organism: Fusarium verticillioides

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


enzyme_display_name: myrcene synthase

organism: Salvia fruticosa

substrate_name: (2E)-geranyl diphosphate

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

enzyme: myrcene synthase

substrate: (2E)-geranyl diphosphate


enzyme_display_name: taxadiene synthase

organism: Taxus canadensis

enzyme: taxadiene synthase


organism: Hedychium coronarium

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


organism: Arabidopsis thaliana

substrate_name: ent-copalyl diphosphate

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

substrate: ent-copalyl diphosphate


enzyme_display_name: (R)-limonene synthase

organism: Citrus sinensis

substrate_name: Geranyl diphosphate

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

proof_lines: at pH 8.0, temperature not specified in the publication

proof_lines: kcat is 0.186 sec(-1) for geranyl diphosphate in presence of manganese. kcat is 0.118 sec(-1) for geranyl diphosphate in presence of magnesium. kcat is 0.43 sec(-1) for neryl diphosphate.

source_databases_merged: sabio_rk brenda skid uniprot

enzyme: (R)-limonene synthase

substrate: Geranyl diphosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D404A to reconstruct the assayed variant sequence.


enzyme_display_name: pentalenene synthase

organism: Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)

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

enzyme: pentalenene synthase


organism: Taxus brevifolia

substrate_name: Geranylgeranyl diphosphate

proof_lines:
M1 preprotein
thioredoxin fusion
M93

substrate: Geranylgeranyl diphosphate


substrate_name: 2-Fluoroneryl diphosphate

proof_lines: pH and temperature not specified in the publication

source_databases_merged: sabio_rk brenda uniprot

substrate: 2-Fluoroneryl diphosphate


organism: Lavandula angustifolia

mutation_signature: truncated protein LaLIMS_RR / truncated protein

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

mutation_type: truncation


assay_conditions_summary: pH 7

proof_lines: kcat is 0.012 sec(-1) with geranyl diphosphate as substrate.

source_databases_merged: brenda uniprot


enzyme_display_name: germacrene-A synthase

organism: Ixeridium dentatum

substrate_name: 2-trans,6-trans-farnesyl diphosphate

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

enzyme: germacrene-A synthase

substrate: 2-trans,6-trans-farnesyl diphosphate


proof_lines: pH 7.0, 25°C, recombinant mutant T433A/A435T


proof_lines: pH 7.0, 25°C, recombinant wild-type enzyme


enzyme_display_name: S-linalool synthase

organism: Actinidia arguta

enzyme: S-linalool synthase


proof_lines: cofactor Mn2+, substrate 0.05 mM geranyl diphosphate


proof_lines: cofactor Mg2+, substrate 0.05 mM geranyl diphosphate


organism: Zea mays


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

smiles: [Mn]


enzyme_display_name: germacradienol synthase

organism: Streptomyces avermitilis

enzyme: germacradienol synthase


organism: Cereus peruvianus


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

smiles: [Mg]


organism: Mentha spicata

substrate_name: 3S-Linalyl diphosphate

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

substrate: 3S-Linalyl diphosphate


enzyme_display_name: amorpha-4,11-diene synthase

organism: Penicillium roqueforti

proof_lines: in presence of 0.25 mM inorganic disphosphate, pH and temperature not specified in the publication

enzyme: amorpha-4,11-diene synthase


organism: Camellia sinensis var. sinensis

proof_lines:
pH 7.5, 37°C, cultivar Lingtoudancong
pH 7.5, 37°C, cultivar Jinxuan


enzyme_display_name: R-linalool synthase

proof_lines:
pH 7.5, 37°C, cultivar Jinxuan
pH 7.5, 37°C, cultivar Lingtoudancong

enzyme: R-linalool synthase


organism: Cyclocybe aegerita

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


enzyme_display_name: isoprene synthase

organism: Bauhinia variegata

substrate_name: dimethylallyl diphosphate

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

proof_lines: pH 8.5, temperature not specified in the publication

enzyme: isoprene synthase

substrate: dimethylallyl diphosphate


organism: Nostoc sp.

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

proof_lines: determined by incubating purified enzyme with various concentrations of 1 to 100 microM 2-trans,6-trans-farnesyl diphosphate

proof_lines: in 10 mM Tris-HCl, 10 mM MgCl2, 1 mM mercaptoethanol


enzyme_display_name: (+)-delta-cadinene synthase

organism: Piper nigrum

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

enzyme: (+)-delta-cadinene synthase

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


organism: Actinidia polygama

assay_conditions_summary: pH 7.5; buffer Bis-Tris propane

column_label: Table 1; row ApLS1 / GPP; columns Km (uM) raw 2.6 +/- 0.1 uM, Vmax (pkat mg^-1) raw 214 +/- 2, Kcat (s^-1) raw 0.014 +/- 0.0001 s^-1, Kcat/Km (s^-1 mM^-1) raw 5.6 +/- 0.1 s^-1 mM^-1. The Kcat/Km cell is the mismatching column.

normalized_value_unit_evidence: Km 2.6 uM = 2.6/1000 = 0.0026 mM. kcat 0.014 s^-1 = 0.014 s^-1 (already canonical, no conversion). kcat/Km 5.6 s^-1 mM^-1 = 5.6 s^-1 mM^-1 (printed by the paper, not derived). The catalog value 5.384615384615385 is 0.014/0.0026, i.e. the ratio recomputed from the paper's rounded kcat and Km; it disagrees with the paper's own printed 5.6 +/- 0.1 s^-1 mM^-1 and falls outside the printed 5.5-5.7 SE band.

row_label: ApLS1 / GPP

table_label: Table 1. Kinetic properties of recombinant AaLS1 and ApLS1 enzymes


organism: Artemisia annua

proof_lines: AaTPS2 produced a single product, beta-myrcene

proof_lines: GPP substrate and divalent-metal-dependent relative activity


column_label: Table 1 row ApLS1/GPP + Mn2+ column Km (uM); cofactor row includes Vmax 22%.

row_label: ApLS1 / GPP + Mn2+


organism: Solidago canadensis

proof_lines:
(+)-(10R)-germacrene A synthase
Solidago canadensis
farnesyl diphosphate


organism: Citrus x limon

proof_lines:
Citrus x limon
(R)-limonene synthase
geranyl diphosphate


organism: Coleus amboinicus

proof_lines:
PamTps1
Plectranthus amboinicus
GPP


organism: Agrocybe pediades

proof_lines:
Ap.LS
geranyl diphosphate
100% linalool


organism: Santalum album

proof_lines:
recombinant enzyme
geranyl diphosphate
pH 7.4


column_label: Table 1 row ApLS1/GPP + Mg2+ column Km (uM); cofactor row includes Vmax 100%.

row_label: ApLS1 / GPP + Mg2+


organism: Barnadesia spinosa


organism: Ixeridium dentatum


organism: Robinia pseudoacacia


organism: Calophyllum inophyllum


organism: Campylopus introflexus


organism: Ipomoea batatas


organism: Salix discolor


organism: Metrosideros polymorpha


organism: Syzygium cumini


organism: Syzygium samarangense


organism: Mangifera indica


organism: Garcinia subelliptica


organism: Artemisia annua

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T296I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T296V to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme T296V, at pH 7.2 and 30°C
mutant enzyme T296V, at pH 7.0 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T296A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T296S to reconstruct the assayed variant sequence.


organism: Nicotiana suaveolens

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


organism: Clarkia breweri


organism: Citrus sinensis

substrate_name: 2-Fluorogeranyl diphosphate

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

proof_lines: pH and temperature not specified in the publication

substrate: 2-Fluorogeranyl diphosphate


organism: Hedychium coronarium

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


enzyme_display_name: ent-sandaracopimaradiene synthase

organism: Oryza sativa

proof_lines: 22°C, pH not specified in the publication

enzyme: ent-sandaracopimaradiene synthase


organism: Cichorium intybus


organism: Zea mays


substrate_name: farnesyl diphosphate


substrate_name: magnesium

substrate: magnesium


substrate_name: manganese

substrate: manganese


substrate_name: geranyl diphosphate

column_label: Biochemical Characterization section, prose sentence giving Km values with GPP and FPP.

raw_value_unit_evidence: The K_m values with GPP and FPP were 1.1 and 1.0 uM, respectively.

row_label: GPP Km prose sentence

table_label: Biochemical Characterization section: TPS1 kinetic prose values


row_label: FPP Km prose sentence

substrate: farnesyl diphosphate


column_label: Biochemical Characterization section, prose sentence giving Km values for Mg2+ and Mn2+.

raw_value_unit_evidence: The K_m values were 470 and 26 uM for Mg2+ and Mn2+, respectively.

row_label: Mg2+ Km prose sentence


row_label: Mn2+ Km prose sentence


organism: Streptomyces coelicolor

substrate_name: trans,trans-Farnesyl diphosphate; H2O

substrate: trans,trans-Farnesyl diphosphate; H2O


substrate_name: manganese ions

substrate: manganese ions


substrate_name: H2O; Geranyl diphosphate

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

substrate: H2O; Geranyl diphosphate


column_label: Table I row Maize NADHX gives Km 0.86 microM, Kcat 0.30 s^-1, and Kcat/Km 358 mM^-1 s^-1.

row_label: Maize / NADHX

table_label: Table I. Kinetic properties of Arabidopsis and maize NADHX and NADPHX dehydratases.


column_label: Table I row Maize NADPHX gives Km 0.89 microM, Kcat 0.38 s^-1, and Kcat/Km 524 mM^-1 s^-1.

row_label: Maize / NADPHX


organism: Escherichia coli (strain K12)

substrate_name: (S)-NADPHX

assay_conditions_summary: cofactor ADP

proof_lines: YjeF NADPHX ADP

substrate: (S)-NADPHX


substrate_name: ADP

assay_conditions_summary: cofactor ATP

substrate: ADP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T296A 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.


organism: Arabidopsis thaliana

assay_conditions_summary: pH 8; 295.15 K; cofactor NADPH

row_label: Arabidopsis / NADHX

table_label: Table I


sequence_variant_note: Mutation signature T296I could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


substrate_name: farnesyl diphosphate (at pH 7.5)

proof_lines: TPS2 (E)-nerolidol linalool

substrate: farnesyl diphosphate (at pH 7.5)


substrate_name: geranylgeranyl diphosphate (at pH 7.5)

proof_lines: TPS2 (E,E)-geranyllinalool linalool

substrate: geranylgeranyl diphosphate (at pH 7.5)


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


substrate_name: geranyl diphosphate (at pH 7.5)

proof_lines: TPS2 linalool (E)-nerolidol

substrate: geranyl diphosphate (at pH 7.5)


substrate: geranyl diphosphate


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

proof_lines:
abstract
Mg(2+) cofactor
TPS6


proof_lines:
Figure 3
GPP
FPP


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


row_label: Arabidopsis / NADPHX


sequence_variant_note: Mutation signature T296V could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T399S to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature T399S/T447S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme T399S/T447S, at pH 7.0 and 30°C


enzyme_display_name: epi-isozizaene synthase

organism: Streptomyces avermitilis

enzyme: epi-isozizaene synthase


enzyme_display_name: gluconate/galactonate dehydratase

organism: Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)

substrate_name: galactonate (at 60 degrees Celsius and pH 6.2)

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

assay_conditions_summary: pH 6.2; 333.15 K; buffer 50 mM sodium phosphate

column_label: Results prose; row GAD / galactonate; metric Km.

normalized_value_unit_evidence: Km=2 mM directly from results prose.

raw_value_unit_evidence: PMC2812977 results prose reports a Km for galactonate of 2 mM.

row_label: GAD / galactonate

table_label: Results prose, gluconate dehydratase characterization

enzyme: gluconate/galactonate dehydratase


substrate_name: gluconate (at 60 degrees Celsius and pH 6.2)

column_label: Results prose; row GAD / gluconate; metric Km.

normalized_value_unit_evidence: Km=2.5 mM directly from results prose.

raw_value_unit_evidence: PMC2812977 results prose reports gluconate dehydratase Km for gluconate as 2.5 mM.

row_label: GAD / gluconate


organism: Methanosarcina barkeri (strain Fusaro / DSM 804)

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

column_label: The abstract reports Km values of 0.1 mM for formaldehyde and 30 microM for H4MPT.

raw_value_unit_evidence: Km raw_value=30 microM raw_unit=microM

row_label: Prose segment: H4MPT Km

table_label: PubMed PMID 16075199 abstract


substrate_name: formaldehyde

smiles: C=O

raw_value_unit_evidence: Km raw_value=0.1 mM raw_unit=mM

row_label: Prose segment: formaldehyde Km

substrate: formaldehyde


enzyme_display_name: elisabethatriene synthase

organism: Antillogorgia elisabethae

enzyme: elisabethatriene synthase


substrate_name: farnesyl diphosphate


substrate_name: geranylgeranyl diphosphate

substrate: geranylgeranyl diphosphate


substrate_name: (2E)-geranyl diphosphate

substrate: (2E)-geranyl diphosphate


enzyme_display_name: alpha-bisabolene synthase

organism: Ginkgo biloba

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

proof_lines: pH 7.5, 22°C, recombinant His-tagged enzyme

enzyme: alpha-bisabolene synthase

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


enzyme_display_name: fusicocca-2,10(14)-diene synthase

organism: Diaporthe amygdali

enzyme: fusicocca-2,10(14)-diene synthase


substrate_name: geranyl diphosphate


enzyme_display_name: epi-cedrol synthase

organism: Artemisia annua

proof_lines:
pH 8.5, 30°C, recombinant enzyme ECS
pH 7.0, 25°C, recombinant enzyme
pH 9.0, 25°C, recombinant enzyme

enzyme: epi-cedrol synthase


substrate_name: isopentenyl diphosphate

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

proof_lines: pH 8.5, 30°C, recombinant enzyme ECS combined with recombinant FPPS, both as individual enzymes

proof_lines: pH 8.5, 30°C, recombinant fusion enzyme FPPS-ECS

substrate: isopentenyl diphosphate


substrate_name: dimethylallyl diphosphate

substrate: dimethylallyl diphosphate


enzyme_display_name: terpentetriene synthase

organism: Kitasatospora griseola

substrate_name: TDP

enzyme: terpentetriene synthase

substrate: TDP


substrate_name: trans,trans-Farnesyl diphosphate; Isopentenyl diphosphate


organism: Santalum album

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


organism: Abies grandis

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

proof_lines: in 25 mM Tris, 15 mM MgCl2, pH 7.5, at 30°C

source_databases_merged: brenda skid uniprot


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

organism: Streptomyces sp. (strain KO-3988)

substrate_name: ent-CDP

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

substrate: ent-CDP


organism: Hedychium coronarium

substrate_name: Unknown

substrate: Unknown


proof_lines: pH 8.2, 30°C, recombinant N-terminal domain


enzyme_display_name: crotonobetainyl-CoA hydratase

substrate_name: crotonobetainyl-CoA

assay_conditions_summary: pH 7.5; cofactor CoA

column_label: Printed page 11143, Results paragraph under Enzymatic Function of CaiD, states the Km value of CaiD for crotonobetainyl-CoA was 12 uM.

raw_value_unit_evidence: Km raw_value=12 raw_unit=uM

row_label: crotonobetainyl-CoA

table_label: Prose - Results, Enzymatic Function of CaiD

enzyme: crotonobetainyl-CoA hydratase

substrate: crotonobetainyl-CoA


substrate_name: crotonyl-CoA

column_label: Printed page 11143, Results paragraph under Enzymatic Function of CaiD, states the Km value of CaiD for crotonyl-CoA was 38 uM.

raw_value_unit_evidence: Km raw_value=38 raw_unit=uM

row_label: crotonyl-CoA

substrate: crotonyl-CoA


source_db: skid

column_label: Table 1 columns under Full-length PaFS are substrate, kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1), h; GPP row cells are 0.036 +/- 0.007, 9.2 +/- 2.6, 3.9 x 10^3, 1.0.

normalized_value_unit_evidence: Km 9.2 uM = 0.0092 mM; kcat 0.036 s^-1; printed kcat/Km 3.9 x 10^3 M^-1 s^-1 = 3.9 s^-1 mM^-1; expected computed ratio 3.913043478260869 s^-1 mM^-1 is within table precision/rounding.

row_label: Full-length PaFS / GPP

table_label: Table 1, Catalytic activity of PaFS constructs

source_databases_merged: skid uniprot

source: skid


column_label: Table 1 columns under Full-length PaFS are substrate, kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1), h; FPP row cells are 0.027 +/- 0.001, 0.14 +/- 0.02, 1.9 x 10^5, 3.0.

normalized_value_unit_evidence: Km 0.14 uM = 0.00014 mM; kcat 0.027 s^-1; printed kcat/Km 1.9 x 10^5 M^-1 s^-1 = 190.0 s^-1 mM^-1; expected computed ratio 192.85714285714286 s^-1 mM^-1 is within table precision/rounding.

row_label: Full-length PaFS / FPP


column_label: Table 1 columns under Full-length PaFS are substrate, kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1), h; GGPP row cells are 0.021 +/- 0.002, 0.63 +/- 0.03, 3.3 x 10^4, 2.2.

normalized_value_unit_evidence: Km 0.63 uM = 0.00063 mM; kcat 0.021 s^-1; printed kcat/Km 3.3 x 10^4 M^-1 s^-1 = 33.0 s^-1 mM^-1; expected computed ratio 33.333333333333336 s^-1 mM^-1 is within table precision/rounding.

row_label: Full-length PaFS / GGPP


enzyme_display_name: short-chain-enoyl-CoA hydratase

organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)

assay_conditions_summary: cofactor CoA

enzyme: short-chain-enoyl-CoA hydratase


substrate_name: hexenoyl-CoA

substrate: hexenoyl-CoA


organism: Homo sapiens

substrate_name: 17beta-estradiol (2-hydroxylation)

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

substrate: 17beta-estradiol (2-hydroxylation)


substrate_name: estrone (2-hydroxylation)

substrate: estrone (2-hydroxylation)


enzyme_display_name: (2S)-3-sulfopropanediol dehydratase

organism: Klebsiella oxytoca

assay_conditions_summary: pH 7.5; cofactor NADH

column_label: Results section, kinetics sentences of the paper (Proc Natl Acad Sci U S A 2020, 117(27):15599-15608); this paper prints its kinetic constants in the running text of the Results section and carries no numbered table of kinetic constants. Results, HpfG kinetics sentence, DHPS dehydration measurement; printed kcat 130 s^-1; printed Km 5.0 mM; printed kcat/Km 26 mM^-1 s^-1. captured primary segment: HpfG (DHPS dehydration) | kcat 130 ± 4 s^-1 | Km 5.0 ± 0.6 mM | kcat/Km 26 ± 3 mM^-1 s^-1

normalized_value_unit_evidence: kcat: printed value 130 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 130.0 s^(-1); the exported value is 130.0 s^(-1). Km: printed value 5.0 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 5.0 mM; the exported value is 5.0 mM. kcat/Km: printed value 26 mM^-1 s^-1; the printed unit is already the export unit, so no unit conversion applies and the paper value is 26.0 s^(-1)*mM^(-1); the exported value is 26.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Results, HpfG kinetics sentence, DHPS dehydration measurement: kcat = 130 s^-1; Km = 5.0 mM; printed kcat/Km = 26 mM^-1 s^-1.

enzyme: (2S)-3-sulfopropanediol dehydratase


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

row_label: Results, HpfG kinetics sentence, DHPS dehydration measurement

table_label: Results section, kinetics sentences of the paper (Proc Natl Acad Sci U S A 2020, 117(27):15599-15608); this paper prints its kinetic constants in the running text of the Results section and carries no numbered table of kinetic constants


enzyme_display_name: alpha-farnesene synthase

organism: Actinidia deliciosa

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

enzyme: alpha-farnesene synthase


enzyme_display_name: chondroitin-sulfate-ABC endolyase

organism: Proteus vulgaris

substrate_name: dermatan sulfate

proof_lines: Independent QA found that the related dermatan sulfate values in PMID 15691229 do not verify this mixed exported tuple.

enzyme: chondroitin-sulfate-ABC endolyase

substrate: dermatan sulfate


substrate_name: all-trans retinol

assay_conditions_summary: pH 7.5; 310.15 K; buffer CYP isoforms (0.025 nmol) in potassium phosphate

column_label: Table 3 row CYP 1A2, column Apparent Km μM reports 9 for all-trans-retinol oxidation to all-trans-retinal.

raw_value_unit_evidence: Km raw_value=9 raw_unit=microM

row_label: CYP 1A2

table_label: ScienceDirect full-text Table 3

substrate: all-trans retinol


column_label: Table 3 row CYP 1A1, column Apparent Km μM reports 8 for all-trans-retinol oxidation to all-trans-retinal.

raw_value_unit_evidence: Km raw_value=8 raw_unit=microM

row_label: CYP 1A1


enzyme_display_name: beta-farnesene synthase

organism: Mentha x piperita

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

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

enzyme: beta-farnesene synthase

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


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

organism: Fragaria x ananassa

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


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

organism: Tripterygium wilfordii

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


enzyme_display_name: guluronate-specific alginate lyase

organism: Isoptericola halotolerans

substrate_name: alginate

enzyme: guluronate-specific alginate lyase

substrate: alginate


organism: Actinidia chinensis

column_label: Table 3 columns KM (uM), kcat (s^-1), kcat/KM (s^-1 mM^-1), and Vrel (%); row GDP (Mg2+).

normalized_value_unit_evidence: KM 1.89 uM = 0.00189 mM, rounds to expected 0.0019 mM; kcat 0.13 s^-1 matches; table kcat/KM 69 s^-1 mM^-1 is consistent with expected 68.42105263157895 computed from rounded expected kcat/Km operands.

row_label: GDP (Mg2+)

table_label: Table 3: Kinetic profiles of recombinant AcNES1 protein

substrate: geranyl diphosphate


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

column_label: Table 3 columns KM (uM), kcat (s^-1), kcat/KM (s^-1 mM^-1), and Vrel (%); row FDP (Mg2+).

normalized_value_unit_evidence: KM 0.80 uM = 0.00080 mM; kcat 0.24 s^-1 matches; kcat/KM 300 s^-1 mM^-1 matches expected 300.0.

row_label: FDP (Mg2+)


enzyme_display_name: epi-isozizaene synthase

organism: Streptomyces coelicolor

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F96A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

enzyme: epi-isozizaene synthase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F198A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F203F with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


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

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


substrate_name: (2E)-geranyl diphosphate

substrate: (2E)-geranyl diphosphate


organism: Arabidopsis thaliana

substrate_name: farnesyl diphosphate

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.

substrate: farnesyl diphosphate


substrate_name: geranyl diphosphate


organism: Malus domestica

substrate_name: trans,trans-Farnesyl diphosphate

proof_lines: activity enhanced 5-fold on addition of 30-50 mM potassium.

substrate: trans,trans-Farnesyl diphosphate


organism: Lavandula angustifolia

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

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: kcat normalized_value=0.017 normalized_unit=s^-1 matches; Km normalized_value=0.00655 normalized_unit=mM; 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


organism: Fragaria ananassa

substrate_name: H2O; trans,trans-Farnesyl diphosphate

substrate: H2O; trans,trans-Farnesyl diphosphate


organism: Zea mays


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).


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D484A with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines:
mutant D484A
pH 7.5, 30°C, mutant enzyme D484A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S487A to reconstruct the assayed variant sequence.

proof_lines:
mutant S487A
pH 7.5, 30°C, mutant enzyme S487A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S488A to reconstruct the assayed variant sequence.

proof_lines:
mutant S488A
pH 7.5, 30°C, mutant enzyme S488A


organism: Hedychium coronarium


organism: Coleus amboinicus

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


organism: Mentha piperita


substrate_name: magnesium

substrate: magnesium


substrate_name: Manganese

substrate: Manganese


organism: Santalum album


column_label: Biochemical Characterization section, prose sentence giving Km values with GPP and FPP.

row_label: GPP Km prose sentence


row_label: FPP Km prose sentence


column_label: Biochemical Characterization section, prose sentence giving Km values for Mg2+ and Mn2+.

row_label: Mg2+ Km prose sentence


substrate_name: manganese

row_label: Mn2+ Km prose sentence

substrate: manganese


enzyme_display_name: sabinene-hydrate synthase

organism: Thymus vulgaris

enzyme: sabinene-hydrate synthase


enzyme_display_name: threonine synthase

substrate_name: O-Phospho-L-homoserine

enzyme: threonine synthase

substrate: O-Phospho-L-homoserine


substrate_name: O-phospho-L-homoserine (in presence of 100 uM S-adenosyl-L-methionine)

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


enzyme_display_name: methylglyoxal synthase

organism: Thermus sp.

substrate_name: dihydroxyacetone phosphate

sequence_variant_note: Resolved canonical sequence from hash_bound_local_uniprot_accession:B3VH91 and applied mutation signature D10N to reconstruct the assayed variant sequence.

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

column_label: Official PMC full text Table 1 lists the TMGS D10N row with Km (mM)=0.75 +/- 0.03, kcat (s^-1)=0.41 +/- 0.02, and kcat/Km=0.544.

normalized_value_unit_evidence: Km normalized_value=0.75 normalized_unit=mM; kcat normalized_value=0.41 normalized_unit=s^-1; kcat/Km normalized_value=0.544 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 row TMGS D10N reports Km raw_value=0.75 +/- 0.03 raw_unit=mM, kcat raw_value=0.41 +/- 0.02 raw_unit=s^-1, and kcat/Km raw_value=0.544.

row_label: TMGS D10N

table_label: PMC4133812 Table 1

enzyme: methylglyoxal synthase

substrate: dihydroxyacetone phosphate


enzyme_display_name: germacrene-A synthase

organism: Cichorium intybus

substrate_name: 2-trans,6-trans-farnesyl diphosphate

enzyme: germacrene-A synthase

substrate: 2-trans,6-trans-farnesyl diphosphate


organism: Kitasatospora griseola

substrate_name: terpentedienyl diphosphate

substrate: terpentedienyl diphosphate


substrate_name: GGDP

substrate: GGDP


enzyme_display_name: abieta-7,13-diene synthase

organism: Abies grandis

substrate_name: copalyl diphosphate

proof_lines:
Abies grandis
abietadiene synthase
copalyl diphosphate

enzyme: abieta-7,13-diene synthase

substrate: copalyl diphosphate


substrate_name: GGPP (in presence of magnesium)

proof_lines:
geranylgeranyl diphosphate
(+)-copalyl diphosphate
Abies grandis

substrate: GGPP (in presence of magnesium)


enzyme_display_name: 3-dehydroquinate synthase

organism: Aspergillus nidulans

proof_lines:
Aspergillus nidulans
dehydroquinate synthase
DAHP

enzyme: 3-dehydroquinate synthase


enzyme_display_name: (-)-beta-caryophyllene synthase

organism: Gossypium hirsutum

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

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

enzyme: (-)-beta-caryophyllene synthase


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S485A to reconstruct the assayed variant sequence.

proof_lines:
mutant S485A
pH 7.5, 30°C, mutant enzyme S485A


proof_lines:
mutant S487A, 50 mM KCl, 10 mM MgCl2
pH 7.5, 30°C, mutant enzyme S487A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D484A to reconstruct the assayed variant sequence.

proof_lines:
mutant D484A, 50 mM KCl, 10 mM MgCl2
pH 7.5, 30°C, mutant enzyme D484A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S487K to reconstruct the assayed variant sequence.

proof_lines: without K+, sesquiterpene synthase activity in mutant S487K is independent of K+


proof_lines:
mutant S488A, 50 mM KCl, 10 mM MgCl2
pH 7.5, 30°C, mutant enzyme S488A


proof_lines:
wild-type MdAFS, 50 mM KCl, 10 mM MgCl2
pH 7.5, 30°C, wild-type enzyme


proof_lines:
mutant S485A, 50 mM KCl, 10 mM MgCl2
pH 7.5, 30°C, mutant enzyme S485A


column_label: Results prose linked to Figure 7B; row FaNES1 / FPP; metric Km.

normalized_value_unit_evidence: Km=0.0081 mM converted from 8.1 uM.

raw_value_unit_evidence: PMC527202 results prose reports the Km for FPP as 8.1 uM.

row_label: FaNES1 / FPP

table_label: Results prose / Figure 7B kinetic analysis


organism: Ocimum kilimandscharicum

proof_lines: pH not specified in the publication, 30°C, recombinant His-tagged enzyme


enzyme_display_name: (S)-beta-bisabolene synthase

proof_lines: pH 7.4, 30°C, recombinant His6-tagged enzyme

enzyme: (S)-beta-bisabolene synthase


enzyme_display_name: mannuronate-specific alginate lyase

organism: Vibrio sp. NJ-04

substrate_name: alginate

enzyme: mannuronate-specific alginate lyase

substrate: alginate


organism: Helianthus annuus

substrate_name: farnesyl diphosphate


organism: Artemisia annua

proof_lines: about, recombinant wild-type enzyme, or mutants ECPSY312F, ECPSV344D, and ECPSV21A, pH 7.5, 25°C


proof_lines: about, recombinant mutant ECPSE353D, pH 7.5, 25°C


substrate_name: farnesyl diphosphate (in the presence of 10 mM magnesium and 1 mM manganese)

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


substrate_name: geranyl diphosphate (in the presence of 10 mM magnesium and 1 mM manganese)


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


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


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


substrate_name: (2E)-geranyl diphosphate


substrate: farnesyl diphosphate (in the presence of 10 mM magnesium and 1 mM manganese)


substrate: geranyl diphosphate (in the presence of 10 mM magnesium and 1 mM manganese)


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


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


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


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: Bifunctional albaflavenone monooxygenase/terpene synthase

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

substrate_name: FPP (in the presence of magnesium ions at 30 degrees Celsius and at pH 5.5)

proof_lines: kcat is 0.019 sec(-1) with farnesyl diphosphate (FPP) as substrate (in the presence of magnesium ions at 30 degrees Celsius and at pH 5.5).


organism: Streptomyces coelicolor

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


enzyme_display_name: alpha-farnesene synthase

organism: Arabidopsis thaliana

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).

substrate: (2E)-geranyl diphosphate


organism: Piper nigrum

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


organism: Zea mays

proof_lines: kcat is 0.00191 sec(-1) with farnesyl diphosphate (in the presence of MgCl(2)). kcat is 0.0013 sec(-1) with farnesyl diphosphate (in the presence of MnCl(2)).


enzyme_display_name: (+)-epicubenol synthase

organism: Streptomyces griseus

protein_accession_database: NCBI Protein

sequence_source: GenBank accession BAG22894.1

column_label: Abstract reports Km 254 +/- 7.1 nM, kcat 0.026 +/- 0.001 s^-1, and kcat/Km 0.10 s^-1 uM^-1 for recombinant GecA.

normalized_value_unit_evidence: kcat normalized_value=0.026 normalized_unit=s^-1; Km normalized_value=0.000254 normalized_unit=mM; kcat/Km normalized_value=100 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=0.026 +/- 0.001 raw_unit=s^-1; Km raw_value=254 +/- 7.1 raw_unit=nM; kcat/Km raw_value=0.10 raw_unit=s^-1 uM^-1

row_label: GecA/SGR6065 conversion of farnesyl diphosphate to (+)-epicubenol

table_label: PubMed XML abstract PMID 22872183

enzyme: (+)-epicubenol synthase


enzyme_display_name: beta-selinene cyclase

organism: Citrus x microcarpa

enzyme: beta-selinene cyclase


enzyme_display_name: (-)-germacrene D synthase

organism: Solidago canadensis

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

enzyme: (-)-germacrene D synthase


organism: Coprinopsis cinerea


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.

substrate: farnesyl diphosphate


substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


enzyme_display_name: (+)-germacrene D synthase

organism: Actinidia deliciosa

enzyme: (+)-germacrene D synthase


enzyme_display_name: alpha-gurjunene synthase

enzyme: alpha-gurjunene synthase


enzyme_display_name: valencene synthase

organism: Callitropsis nootkatensis

enzyme: valencene synthase


enzyme_display_name: (+)-alpha-barbatene synthase

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

enzyme: (+)-alpha-barbatene synthase


enzyme_display_name: cis-muuroladiene synthase

organism: Mentha x piperita

enzyme: cis-muuroladiene synthase


enzyme_display_name: 5-epiaristolochene 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: 5-epiaristolochene synthase


organism: Marchantia polymorpha

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


substrate_name: anilinogeranyl diphosphate

substrate: anilinogeranyl diphosphate


enzyme_display_name: presilphiperfolanol synthase

organism: Botrytis cinerea

proof_lines: recombinant enzyme, in 50 mM PIPES, 10 mM MgCl2, 100 mM NaCl, pH 7.0, at 30°C

enzyme: presilphiperfolanol synthase


substrate_name: trans,trans-Farnesyl diphosphate; H2O

substrate: trans,trans-Farnesyl diphosphate; H2O


enzyme_display_name: alpha-santalene synthase

organism: Clausena lansium

proof_lines: recombinant His-tagged enzyme, pH 7.4, 37°C

proof_lines: recombinant enzyme, pH 7.4, 25°C, coupled assay with IPP1 activity

enzyme: alpha-santalene synthase


enzyme_display_name: exo-alpha-bergamotene synthase

enzyme: exo-alpha-bergamotene synthase


organism: Valeriana officinalis

proof_lines: kcat is 0.01 sec(-1) with farnesyl diphosphate as substrate.


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

substrate_name: geranylgeranyl diphosphate (at pH 7.5)

column_label: Exact metric-labeled prose evidence maps the third value in the GDP/FDP/GGDP sequence to GGDP: Km for GGDP = 25 uM, normalized to 0.025 mM.

normalized_value_unit_evidence: Km normalized_value=0.025 normalized_unit=mM from raw 25 uM.

raw_value_unit_evidence: Results prose states Km values for reactions with GDP, FDP, and GGDP were 16.9 uM (+/-6.1 uM), 18 uM (+/-7.8 uM), and 25 uM (+/-12.6 uM), respectively.

row_label: TPS2 reaction with GGDP

table_label: PMC5134970 Results and Figure 4

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

substrate: geranylgeranyl diphosphate (at pH 7.5)


substrate_name: geranyl diphosphate (at pH 7.5)

column_label: Exact metric-labeled prose evidence maps the first value in the GDP/FDP/GGDP sequence to GDP: Km for GDP = 16.9 uM, normalized to 0.0169 mM.

normalized_value_unit_evidence: Km normalized_value=0.0169 normalized_unit=mM from raw 16.9 uM.

row_label: TPS2 reaction with GDP

substrate: geranyl diphosphate (at pH 7.5)


enzyme_display_name: beta-chamigrene synthase

enzyme: beta-chamigrene synthase


enzyme_display_name: 2-methylfumaryl-CoA hydratase

organism: Haloarcula hispanica

assay_conditions_summary: pH 7.8; cofactor CoA

enzyme: 2-methylfumaryl-CoA hydratase


substrate_name: (S)-citramalyl-CoA

column_label: PMC5592240 Table 4 reports (S)-Citramalyl-CoA Km = 2.6 +/- 0.3 mM; this matches the current row value.

raw_value_unit_evidence: Km raw_value=2.6 +/- 0.3 mM raw_unit=mM

row_label: Row: (S)-Citramalyl-CoA

table_label: PMC5592240 Table 4

substrate: (S)-citramalyl-CoA


enzyme_display_name: mannuronate-specific alginate lyase

organism: Saccharophagus degradans

substrate_name: sodium alginate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H202L with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

proof_lines:
Alg17c H202L
Table 2
steady-state kinetics

substrate: sodium alginate


sequence_variant_note: Mutation signature Q149A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
Alg17c Q149A
Table 2
steady-state kinetics


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R260A to reconstruct the assayed variant sequence.

proof_lines:
Alg17c R260A
Table 2
steady-state kinetics


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R438A to reconstruct the assayed variant sequence.

proof_lines:
Alg17c R438A
Table 2
steady-state kinetics


row_label: Wild type

table_label: Table 2. Steady-state kinetic parameters for wild-type and mutant Alg17c enzymes


enzyme_display_name: enoyl-CoA hydratase 2

organism: Aeromonas caviae

substrate_name: crotonyl-CoA

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

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: trans-2-enoyl-CoA substrates with four to six carbon atoms

enzyme: enoyl-CoA hydratase 2

substrate: crotonyl-CoA


organism: Homo sapiens


enzyme_display_name: 3-dehydroshikimate dehydratase

organism: Bacillus anthracis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K200R to reconstruct the assayed variant sequence.

proof_lines:
Bacillus anthracis AsbF
3-dehydroshikimate dehydratase
dehydration reaction family

enzyme: 3-dehydroshikimate dehydratase


sequence_variant_note: Mutation signature Y70A/Y217A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: cyclohexyl-isocyanide hydratase

organism: Pseudomonas fluorescens

substrate_name: 2-naphthyl isocyanide

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T102S with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

enzyme: cyclohexyl-isocyanide hydratase

substrate: 2-naphthyl isocyanide


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T102V with inferred residue-numbering offset -4 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: oligo-alginate lyase

organism: Stenotrophomonas maltophilia

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H208F to reconstruct the assayed variant sequence.

smiles: N#N

proof_lines:
Stenotrophomonas maltophilia
Smlt2602
alginate

enzyme: oligo-alginate lyase


enzyme_display_name: 2-hydroxyisoflavanone dehydratase

organism: Glycine max

column_label: Table label: PMC1065389 Table 2 - kinetic parameters of G. echinata HIDM and soybean HIDH. Row: 2,5,7,4'-Tetrahydroxyisoflavanone -> Genistein. Enzyme column group: Soybean HIDH. Columns read: Km (uM) cell 170, kcat (s^-1) cell 18.1, kcat/Km (s^-1 mM^-1) cell 106. metric: kcat; raw value: 18.1; raw unit: s^-1; normalized value: 18.1 s^(-1); metric: Km; raw value: 170; raw unit: uM; normalized value: 0.17 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 106.47058823529412 s^-1 mM^-1; assay condition: 2-hydroxyisoflavanone dehydratase kinetic parameters; Table 2 reports Km in uM, kcat in s^-1, and kcat/Km in s^-1 mM^-1 for G. echinata HIDM and soybean HIDH.

normalized_value_unit_evidence: Soybean HIDH columns of Table 2 row 2,5,7,4'-Tetrahydroxyisoflavanone -> Genistein: kcat 18.1 s^-1 = 18.1 s^(-1); Km 170 uM = 0.17 mM (1 uM = 0.001 mM); kcat/Km 106.47058823529412 s^-1 mM^-1 derived as the quotient of this row's own kcat and Km cells (18.1 s^-1 divided by 0.17 mM). Table 2 also prints a rounded kcat/Km cell for this row, 106 s^-1 mM^-1; the quotient 106.47058823529412 rounds to 106 at the printed cell's own integer precision, so the two agree and the disagreement is printed precision only. In the table extract asset the micro sign renders as μ and the paper's small-caps M renders as lowercase m, so the unit cell μm is the paper's uM and s−1mm−1 / s−1 mm−1 is the paper's s^-1 mM^-1; the superscript minus one renders as −1 and the prime in substrate names renders as ′.

raw_value_unit_evidence: PMC1065389 Table 2 - kinetic parameters of G. echinata HIDM and soybean HIDH | header rows of Table 2 in the table extract asset: Substrate Product G. echinata HIDM Soybean HIDH | Km kcat kcat/Km Km kcat kcat/Km | μm s−1 s−1mm−1 μm s−1 s−1 mm−1 | data row: 2,5,7,4′-Tetrahydroxyisoflavanone Genistein 304 0.19 0.62 170 18.1 106 | Soybean HIDH cells read: Km = 170 uM; kcat = 18.1 s^-1; kcat/Km = 106 s^-1 mM^-1; the first Km/kcat/kcat-over-Km column triple belongs to G. echinata HIDM and the second to Soybean HIDH, per the Table 2 header row.

row_label: Soybean HIDH / 2,5,7,4'-Tetrahydroxyisoflavanone -> Genistein

enzyme: 2-hydroxyisoflavanone dehydratase


enzyme_display_name: 3-dehydroquinate synthase

organism: Pyrococcus furiosus

enzyme: 3-dehydroquinate synthase


enzyme_display_name: aldos-2-ulose dehydratase

organism: Phanerodontia chrysosporium

substrate_name: glucosone

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

proof_lines:
glucosone
4.9 mM
7.4 mM

enzyme: aldos-2-ulose dehydratase

substrate: glucosone


substrate_name: ascopyrone M

proof_lines:
ascopyrone M
APM
AF

substrate: ascopyrone M


substrate_name: xylosone

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

proof_lines:
xylosone
113 mM

substrate: xylosone


organism: Glycyrrhiza echinata

column_label: Table label: PMC1065389 Table 2 - kinetic parameters of G. echinata HIDM and soybean HIDH. Row: 2,5,7,4'-Tetrahydroxyisoflavanone -> Genistein. Enzyme column group: G. echinata HIDM. Columns read: Km (uM) cell 304, kcat (s^-1) cell 0.19, kcat/Km (s^-1 mM^-1) cell 0.62. metric: kcat; raw value: 0.19; raw unit: s^-1; normalized value: 0.19 s^(-1); metric: Km; raw value: 304; raw unit: uM; normalized value: 0.304 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 0.625 s^-1 mM^-1; assay condition: 2-hydroxyisoflavanone dehydratase kinetic parameters; Table 2 reports Km in uM, kcat in s^-1, and kcat/Km in s^-1 mM^-1 for G. echinata HIDM and soybean HIDH.

normalized_value_unit_evidence: G. echinata HIDM columns of Table 2 row 2,5,7,4'-Tetrahydroxyisoflavanone -> Genistein: kcat 0.19 s^-1 = 0.19 s^(-1); Km 304 uM = 0.304 mM (1 uM = 0.001 mM); kcat/Km 0.625 s^-1 mM^-1 derived as the quotient of this row's own kcat and Km cells (0.19 s^-1 divided by 0.304 mM). Table 2 also prints a rounded kcat/Km cell for this row, 0.62 s^-1 mM^-1; the quotient is exactly 0.625 (0.19 divided by 0.304 equals 190/304 = 0.625), and 0.625 rounds to 0.62 at the printed cell's own two-decimal precision under the repository's round-half-even convention, so the two agree and the disagreement is printed precision only. In the table extract asset the micro sign renders as μ and the paper's small-caps M renders as lowercase m, so the unit cell μm is the paper's uM and s−1mm−1 / s−1 mm−1 is the paper's s^-1 mM^-1; the superscript minus one renders as −1 and the prime in substrate names renders as ′.

raw_value_unit_evidence: PMC1065389 Table 2 - kinetic parameters of G. echinata HIDM and soybean HIDH | header rows of Table 2 in the table extract asset: Substrate Product G. echinata HIDM Soybean HIDH | Km kcat kcat/Km Km kcat kcat/Km | μm s−1 s−1mm−1 μm s−1 s−1 mm−1 | data row: 2,5,7,4′-Tetrahydroxyisoflavanone Genistein 304 0.19 0.62 170 18.1 106 | G. echinata HIDM cells read: Km = 304 uM; kcat = 0.19 s^-1; kcat/Km = 0.62 s^-1 mM^-1; the first Km/kcat/kcat-over-Km column triple belongs to G. echinata HIDM and the second to Soybean HIDH, per the Table 2 header row.

row_label: G. echinata HIDM / 2,5,7,4'-Tetrahydroxyisoflavanone -> Genistein


proof_lines: 4'-hydroxylated and 4'-methoxylated 2-hydroxyisoflavanones


column_label: Table label: PMC1065389 Table 2 - kinetic parameters of G. echinata HIDM and soybean HIDH. Row: 2,7-Dihydroxy-4'-methoxyisoflavanone -> Formononetin. Enzyme column group: G. echinata HIDM. Columns read: Km (uM) cell 58, kcat (s^-1) cell 9.8, kcat/Km (s^-1 mM^-1) cell 170. metric: kcat; raw value: 9.8; raw unit: s^-1; normalized value: 9.8 s^(-1); metric: Km; raw value: 58; raw unit: uM; normalized value: 0.058 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 168.9655172413793 s^-1 mM^-1; assay condition: 2-hydroxyisoflavanone dehydratase kinetic parameters; Table 2 reports Km in uM, kcat in s^-1, and kcat/Km in s^-1 mM^-1 for G. echinata HIDM and soybean HIDH.

normalized_value_unit_evidence: G. echinata HIDM columns of Table 2 row 2,7-Dihydroxy-4'-methoxyisoflavanone -> Formononetin: kcat 9.8 s^-1 = 9.8 s^(-1); Km 58 uM = 0.058 mM (1 uM = 0.001 mM); kcat/Km 168.9655172413793 s^-1 mM^-1 derived as the quotient of this row's own kcat and Km cells (9.8 s^-1 divided by 0.058 mM). Table 2 also prints a rounded kcat/Km cell for this row, 170 s^-1 mM^-1; the kcat/Km column of Table 2 is printed to two significant figures (its other cells read 46, 47, 0.56, 0.62 and 106), the trailing zero of 170 is not a significant digit under that column style, and the quotient 168.9655172413793 rounds to 170 at that two-significant-figure printed precision, so the two agree and the disagreement is printed precision only. In the table extract asset the micro sign renders as μ and the paper's small-caps M renders as lowercase m, so the unit cell μm is the paper's uM and s−1mm−1 / s−1 mm−1 is the paper's s^-1 mM^-1; the superscript minus one renders as −1 and the prime in substrate names renders as ′.

raw_value_unit_evidence: PMC1065389 Table 2 - kinetic parameters of G. echinata HIDM and soybean HIDH | header rows of Table 2 in the table extract asset: Substrate Product G. echinata HIDM Soybean HIDH | Km kcat kcat/Km Km kcat kcat/Km | μm s−1 s−1mm−1 μm s−1 s−1 mm−1 | data row: 2,7-Dihydroxy-4′-methoxyisoflavanone Formononetin 58 9.8 170 29 1.6 46 | G. echinata HIDM cells read: Km = 58 uM; kcat = 9.8 s^-1; kcat/Km = 170 s^-1 mM^-1; the first Km/kcat/kcat-over-Km column triple belongs to G. echinata HIDM and the second to Soybean HIDH, per the Table 2 header row.

row_label: G. echinata HIDM / 2,7-Dihydroxy-4'-methoxyisoflavanone -> Formononetin


enzyme_display_name: 3-hydroxypropionyl-CoA dehydratase

organism: Metallosphaera sedula

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

column_label: Table 3. Molecular and catalytic properties of recombinant acryloyl-CoA reductase from S. tokodaii and 3-hydroxypropionyl-CoA dehydratase from M. sedula.; row M. sedula 3-hydroxypropionyl-CoA dehydratase / 3-Hydroxypropionyl-CoA apparent Km and Vmax; column Turnover (s^-1); metric kcat; normalized value 96 s^-1 | Table 3. Molecular and catalytic properties of recombinant acryloyl-CoA reductase from S. tokodaii and 3-hydroxypropionyl-CoA dehydratase from M. sedula.; row M. sedula 3-hydroxypropionyl-CoA dehydratase / 3-Hydroxypropionyl-CoA apparent Km and Vmax; column Apparent Km (uM); Turnover (s^-1); adjacent prose Vmax; metric km; normalized value 0.06 mM | Table 3. Molecular and catalytic properties of recombinant acryloyl-CoA reductase from S. tokodaii and 3-hydroxypropionyl-CoA dehydratase from M. sedula.; row M. sedula 3-hydroxypropionyl-CoA dehydratase / 3-Hydroxypropionyl-CoA apparent Km and Vmax; column Computed from exact turnover and Km cells; metric kcat_over_km; normalized value 1600.0 s^-1*mM^-1 | Table 3. Molecular and catalytic properties of recombinant acryloyl-CoA reductase from S. tokodaii and 3-hydroxypropionyl-CoA dehydratase from M. sedula.; row M. sedula 3-hydroxypropionyl-CoA dehydratase / 3-Hydroxypropionyl-CoA apparent Km and Vmax; column Apparent Km (uM); Turnover (s^-1); adjacent prose Vmax; metric vmax; normalized value 0.0031 mol*s^-1*g^-1

normalized_value_unit_evidence: kcat normalized_value=96 normalized_unit=s^-1; km normalized_value=0.06 normalized_unit=mM; kcat_over_km normalized_value=1600.0 normalized_unit=s^-1*mM^-1; vmax normalized_value=0.0031 normalized_unit=mol*s^-1*g^-1

raw_value_unit_evidence: kcat raw_value=96 raw_unit=s^-1; km raw_value=0.06 raw_unit=mM; kcat_over_km raw_value=96/0.06 raw_unit=s^-1*mM^-1; computed from explicit turnover and apparent Km cells; vmax raw_value=186 raw_unit=umol*min^-1*mg^-1; converted to mol*s^-1*g^-1 for export comparison

enzyme: 3-hydroxypropionyl-CoA dehydratase


assay_conditions_summary: pH 8.6; 338.15 K; cofactor CoA

column_label: Table 3. Molecular and catalytic properties of recombinant acryloyl-CoA reductase from S. tokodaii and 3-hydroxypropionyl-CoA dehydratase from M. sedula.; row M. sedula 3-hydroxypropionyl-CoA dehydratase / 3-Hydroxypropionyl-CoA apparent Km; column Turnover (s^-1); metric kcat; normalized value 96 s^-1 | Table 3. Molecular and catalytic properties of recombinant acryloyl-CoA reductase from S. tokodaii and 3-hydroxypropionyl-CoA dehydratase from M. sedula.; row M. sedula 3-hydroxypropionyl-CoA dehydratase / 3-Hydroxypropionyl-CoA apparent Km; column Apparent Km (uM); Turnover (s^-1); metric km; normalized value 0.06 mM | Table 3. Molecular and catalytic properties of recombinant acryloyl-CoA reductase from S. tokodaii and 3-hydroxypropionyl-CoA dehydratase from M. sedula.; row M. sedula 3-hydroxypropionyl-CoA dehydratase / 3-Hydroxypropionyl-CoA apparent Km; column Computed from exact turnover and Km cells; metric kcat_over_km; normalized value 1600.0 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=96 normalized_unit=s^-1; km normalized_value=0.06 normalized_unit=mM; kcat_over_km normalized_value=1600.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=96 raw_unit=s^-1; km raw_value=0.06 raw_unit=mM; kcat_over_km raw_value=96/0.06 raw_unit=s^-1*mM^-1; computed from explicit turnover and apparent Km cells


enzyme_display_name: colneleate synthase

organism: Solanum lycopersicum

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

enzyme: colneleate synthase


organism: Solanum tuberosum

smiles: CCCCCC=CC=CC(CCCCCCCC(=O)[O-])OO


enzyme_display_name: (+)-delta-cadinene synthase

organism: Gossypium arboreum

substrate_name: 2-trans,6-trans-farnesyl diphosphate

proof_lines:
CAD1-A
Gossypium arboreum
farnesyl diphosphate

enzyme: (+)-delta-cadinene synthase

substrate: 2-trans,6-trans-farnesyl diphosphate


enzyme_display_name: 6-pyruvoyltetrahydropterin synthase

substrate_name: 7,8-Dihydroneopterin 3'-triphosphate

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7.4

source_databases_merged: sabio_rk skid uniprot

enzyme: 6-pyruvoyltetrahydropterin synthase

substrate: 7,8-Dihydroneopterin 3'-triphosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R16C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R25Q to reconstruct the assayed variant sequence.


enzyme_display_name: methylglyoxal synthase

organism: Escherichia coli

substrate_name: glycerone phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H98N to reconstruct the assayed variant sequence.

enzyme: methylglyoxal synthase

substrate: glycerone phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H98Q to reconstruct the assayed variant sequence.


organism: Actinidia chinensis


enzyme_display_name: bile-acid 7alpha-dehydratase

organism: [Clostridium] hylemonae

assay_conditions_summary: pH 7.3; 298.15 K; cofactor CoA

column_label: Table 3 row BaiE_15053, substrate column 3-oxo-Delta4-CDCA, metric rows kcat (sec^-1), KM (microM), and kcat/KM (microM^-1 sec^-1), raw cells 18.6(0.6), 21.0 (2.0), and 0.9, normalized to 18.6 s^(-1), 0.021 mM, and 900 s^(-1)*mM^(-1)

normalized_value_unit_evidence: kcat normalized_value=18.6 normalized_unit=s^(-1); KM normalized_value=0.021 normalized_unit=mM; kcat/KM normalized_value=900 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: kcat raw_value=18.6 sec^-1 raw_unit=sec^-1 raw_cell=18.6(0.6); KM raw_value=21.0 microM raw_unit=microM raw_cell=21.0 (2.0); kcat/KM raw_value=0.9 microM^-1 sec^-1 raw_unit=microM^-1 sec^-1 raw_cell=0.9

row_label: BaiE_15053 / 3-oxo-Delta4-CDCA

table_label: Table 3. Homolog kinetic parameters

enzyme: bile-acid 7alpha-dehydratase


column_label: Table 3 row BaiE_15053, substrate column 3-oxo-Delta4-CDC-CoA, metric rows kcat (sec^-1), KM (microM), and kcat/KM (microM^-1 sec^-1), raw cells 12.6 (0.6), 11.4 (1.9), and 1.1, normalized to 12.6 s^(-1), 0.0114 mM, and 1100 s^(-1)*mM^(-1)

normalized_value_unit_evidence: kcat normalized_value=12.6 normalized_unit=s^(-1); KM normalized_value=0.0114 normalized_unit=mM; kcat/KM normalized_value=1100 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: kcat raw_value=12.6 sec^-1 raw_unit=sec^-1 raw_cell=12.6 (0.6); KM raw_value=11.4 microM raw_unit=microM raw_cell=11.4 (1.9); kcat/KM raw_value=1.1 microM^-1 sec^-1 raw_unit=microM^-1 sec^-1 raw_cell=1.1

row_label: BaiE_15053 / 3-oxo-Delta4-CDC-CoA


enzyme_display_name: ectoine synthase

organism: Sphingopyxis alaskensis

proof_lines:
N-α-ADABA
K_m 25.4 ± 2.9 mM
k_cat 0.6 s^-1

enzyme: ectoine synthase


organism: Peptacetobacter hiranonis


enzyme_display_name: o-succinylbenzoate synthase

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +2, so it is treated as a source-provided variant sequence.

enzyme: o-succinylbenzoate synthase


enzyme_display_name: carotenoid 1,2-hydratase

organism: Rubrivivax gelatinosus

substrate_name: spheroidene

enzyme: carotenoid 1,2-hydratase

substrate: spheroidene


substrate_name: Neurosporene

substrate: Neurosporene


enzyme_display_name: abieta-7,13-diene synthase

organism: Abies grandis

substrate_name: CPP (in presence of magnesium)

proof_lines:
Abies grandis
geranylgeranyl diphosphate
(+)-copalyl diphosphate

enzyme: abieta-7,13-diene synthase

substrate: CPP (in presence of magnesium)


enzyme_display_name: S-linalool synthase

organism: Clarkia breweri

enzyme: S-linalool synthase


enzyme_display_name: isoprene synthase

organism: Populus tremula x Populus tremuloides

substrate_name: dimethylallyl diphosphate

proof_lines: Km of 3.8 miromol/qm are estimated from the Lineweaver-Burks plot

proof_lines: separate BRENDA 0.26 mM conversion entry not used as this row value

enzyme: isoprene synthase

substrate: dimethylallyl diphosphate


enzyme_display_name: gluconate/galactonate dehydratase

organism: Saccharolobus solfataricus

substrate_name: D-galactonate

enzyme: gluconate/galactonate dehydratase

substrate: D-galactonate


substrate_name: D-Gluconate

substrate: D-Gluconate


enzyme_display_name: R-linalool synthase

organism: Lavandula angustifolia

substrate_name: geranyl diphosphate

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

proof_lines: Lavandula angustifolia bergamotene synthase / linalool synthase context

proof_lines: kcat is 0.039 sec(-1) with geranyl diphosphate as substrate

enzyme: R-linalool synthase

substrate: geranyl diphosphate


organism: Thermus sp.

substrate_name: dihydroxyacetone phosphate

proof_lines:
Thermus sp. GH5
methylglyoxal synthase
dihydroxyacetone phosphate

substrate: dihydroxyacetone phosphate


organism: Aspergillus nidulans

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

proof_lines:
Aspergillus nidulans
dehydroquinate synthase
NAD+

substrate: NAD+


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

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

proof_lines:
AcNES1
FDP
Km 0.80 μM

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

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


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

proof_lines:
AcNES1
GDP
Km 1.89 μM


organism: Fragaria ananassa

column_label: Results prose linked to Figure 7B; row FaNES1 / GPP; metric Km.

normalized_value_unit_evidence: Km=0.029 mM converted from 29.0 uM.

raw_value_unit_evidence: PMC527202 results prose reports the Km for GPP as 29.0 uM.

row_label: FaNES1 / GPP


enzyme_display_name: (S)-beta-bisabolene synthase

organism: Zea mays

substrate_name: farnesyl diphosphate

assay_conditions_summary: pH 7; buffer 100 uL assay

column_label: Table 1; row label: TPS6-B73; column label: FPP / Km column; raw value 2.1 uM; normalized value 0.0021 mM.

normalized_value_unit_evidence: Km=0.0021 mM after converting 2.1 uM from Table 1.

raw_value_unit_evidence: Table 1; TPS6-B73; FPP / Km column = 2.1 uM (footnote a).

row_label: TPS6-B73 table row / FPP / Km column

table_label: Table 1. Kinetic constants for TPS6-B73 heterologously expressed in E. coli

enzyme: (S)-beta-bisabolene synthase

substrate: farnesyl diphosphate


column_label: Table 1; row label: TPS6-B73; column label: GPP / Km column; raw value 1.1 uM; normalized value 0.0011 mM.

normalized_value_unit_evidence: Km=0.0011 mM after converting 1.1 uM from Table 1.

raw_value_unit_evidence: Table 1; TPS6-B73; GPP / Km column = 1.1 uM (footnote a).

row_label: TPS6-B73 table row / GPP / Km column


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

smiles: [Mg]

assay_conditions_summary: pH 7; buffer assay

column_label: Table 1; row label: TPS6-B73; column label: Mg2+ / Km column; raw value 130.7 uM; normalized value 0.1307 mM.

normalized_value_unit_evidence: Km=0.1307 mM after converting 130.7 uM from Table 1.

raw_value_unit_evidence: Table 1; TPS6-B73; Mg2+ / Km column = 130.7 uM (footnote b).

row_label: TPS6-B73 table row / Mg2+ / Km column


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

smiles: [Mn]

column_label: Table 1; row label: TPS6-B73; column label: Mn2+ / Km column; raw value 23.4 uM; normalized value 0.0234 mM.

normalized_value_unit_evidence: Km=0.0234 mM after converting 23.4 uM from Table 1.

raw_value_unit_evidence: Table 1; TPS6-B73; Mn2+ / Km column = 23.4 uM (footnote b).

row_label: TPS6-B73 table row / Mn2+ / Km column


enzyme_display_name: exo-alpha-bergamotene synthase

organism: Santalum spicatum

proof_lines: recombinant enzyme, pH 7.4, 25°C, coupled assay with IPP1 activity

enzyme: exo-alpha-bergamotene synthase


organism: Santalum austrocaledonicum

assay_conditions_summary: pH 8

proof_lines: kcat is 0.91 sec(-1) with (2E,6E)-farnesyl diphosphate as substrate.


organism: Santalum album


enzyme_display_name: zingiberene synthase

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.

enzyme: zingiberene synthase


enzyme_display_name: beta-santalene synthase

enzyme: beta-santalene synthase


enzyme_display_name: thujopsene synthase

enzyme: thujopsene synthase


enzyme_display_name: alpha-santalene synthase

proof_lines: recombinant His-tagged enzyme, pH 7.4, 37°C

enzyme: alpha-santalene synthase


organism: Hedychium coronarium

substrate_name: Unknown

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

substrate: Unknown


substrate_name: (2E)-geranyl diphosphate

substrate: (2E)-geranyl diphosphate


enzyme_display_name: trichodiene synthase

organism: Fusarium sporotrichioides

assay_conditions_summary: buffer Mn2+

proof_lines:
divalent cation requirement
Mg2+ substitution by Mn2+
kcat/Km changes in Mn2+ buffer

enzyme: trichodiene synthase


enzyme_display_name: (+)-beta-caryophyllene synthase

organism: Ocimum kilimandscharicum

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

proof_lines: pH not specified in the publication, 30°C, recombinant His-tagged enzyme

enzyme: (+)-beta-caryophyllene synthase


enzyme_display_name: cis-muuroladiene synthase

organism: Mentha piperita

substrate_name: trans,trans-Farnesyl diphosphate

enzyme: cis-muuroladiene synthase

substrate: trans,trans-Farnesyl diphosphate


organism: Piper nigrum


organism: Solanum lycopersicum

substrate_name: neryl diphosphate

substrate: neryl diphosphate


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


organism: Vitis vinifera


enzyme_display_name: alpha-guaiene synthase

organism: Aquilaria crassna

proof_lines: kcat is 4.99 x 10(-3) sec(-1) for farnesyl diphosphate.

enzyme: alpha-guaiene synthase


proof_lines: kcat is 7.34 x 10(-3) sec(-1) for farnesyl diphosphate.


proof_lines: kcat is 9.72 x 10(-5) sec(-1) for farnesyl diphosphate.


organism: Lavandula angustifolia

proof_lines: kcat is 0.033 sec(-1) with (2E,6E)-farnesyl diphosphate as substrate. kcat is 0.00026 sec(-1) with geranyl diphosphate as substrate.


enzyme_display_name: cubebol synthase

organism: Coprinopsis cinerea

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

enzyme: cubebol synthase


substrate_name: trans,trans-Farnesyl diphosphate; H2O

substrate: trans,trans-Farnesyl diphosphate; H2O


enzyme_display_name: cyclohexyl-isocyanide hydratase

organism: Pseudomonas putida

substrate_name: cyclohexyl isocyanide

column_label: Abstract reports the apparent Km value for cyclohexyl isocyanide was 16.2 mM.

raw_value_unit_evidence: Km raw_value=16.2 mM raw_unit=mM

row_label: Pseudomonas putida isonitrile hydratase / cyclohexyl isocyanide

table_label: PubMed XML abstract PMID 11306561

enzyme: cyclohexyl-isocyanide hydratase

substrate: cyclohexyl isocyanide


organism: Thauera aromatica


enzyme_display_name: 5-epi-alpha-selinene synthase

organism: Nostoc sp.

proof_lines: in 10 mM Tris-HCl, 10 mM MgCl2, 1 mM beta-mercaptoethanol, pH 8.0, at 30°C

proof_lines: kcat is 0.044 sec(-1) with FPP as substrate (at pH 8).

enzyme: 5-epi-alpha-selinene synthase


enzyme_display_name: bile-acid 7alpha-dehydratase

organism: Clostridium scindens

enzyme: bile-acid 7alpha-dehydratase


organism: Bacillus subtilis (strain 168)

substrate_name: S-methyl-5-thio-D-ribulose 1-phosphate (at 25 degrees Celsius)

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

column_label: Abstract reports K(m) of the enzyme was 8.9 microM at 25 degrees C.

raw_value_unit_evidence: Km raw_value=8.9 microM raw_unit=microM

row_label: Bacillus subtilis MTRu-1-P dehydratase / MTRu-1-P

table_label: PubMed XML abstract PMID 18391471


enzyme_display_name: acetylene hydratase

organism: Syntrophotalea acetylenica

substrate_name: Acetylene

smiles: C#C

assay_conditions_summary: pH 7; cofactor NADH

column_label: PMC XML abstract metric sentence gives Km for acetylene as 14 microM

normalized_value_unit_evidence: PMC XML abstract Km normalized_value=0.014 normalized_unit=mM

raw_value_unit_evidence: PMC XML abstract: The Km for acetylene as assayed in a coupled photometric test with yeast alcohol dehydrogenase and NADH was 14 microM

row_label: acetylene hydratase activity paragraph

table_label: PMC XML abstract

enzyme: acetylene hydratase

substrate: Acetylene


enzyme_display_name: (-)-alpha-cuprenene synthase

proof_lines: wild type enzyme, in 50 mM Tris-HCl, 10 mM MgCl2 (pH 8.0), at 30°C

enzyme: (-)-alpha-cuprenene synthase


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

proof_lines: mutant enzyme C236A, in 50 mM Tris-HCl, 10 mM MgCl2 (pH 8.0), at 30°C


proof_lines: mutant enzyme E237L, in 50 mM Tris-HCl, 10 mM MgCl2 (pH 8.0), at 30°C


proof_lines: mutant enzyme N240L, in 50 mM Tris-HCl, 10 mM MgCl2 (pH 8.0), at 30°C


enzyme_display_name: o-succinylbenzoate synthase

organism: Bacillus subtilis

proof_lines:
Bacillus subtilis
o-succinylbenzoate synthase
menaquinone biosynthesis

enzyme: o-succinylbenzoate synthase


organism: Escherichia coli

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


organism: Streptomyces griseus

proof_lines: at pH 7.5 and 30°C in the presence of 5 mM MgCl2

proof_lines: kcat is 0.025 sec(-1) for (+)-caryolan-1-ol formation (at pH 7.5 and 30 degrees Celsius).


enzyme_display_name: germacrene C synthase

organism: Valeriana officinalis

proof_lines: kcat is 0.01 sec(-1) with farnesyl diphosphate as substrate.

enzyme: germacrene C synthase


enzyme_display_name: avermitilol synthase

organism: Streptomyces avermitilis

proof_lines: pH and temperature not specified in the publication

enzyme: avermitilol synthase


enzyme_display_name: (-)-delta-cadinene synthase

organism: Streptomyces clavuligerus

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

enzyme: (-)-delta-cadinene synthase


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


enzyme_display_name: labdatriene synthase

organism: Oryza sativa

substrate_name: syn-copalyl diphosphate

proof_lines: 22°C, pH not specified in the publication

enzyme: labdatriene synthase

substrate: syn-copalyl diphosphate


enzyme_display_name: carotenoid 1,2-hydratase

organism: Rubrivivax gelatinosus

substrate_name: lycopene

enzyme: carotenoid 1,2-hydratase

substrate: lycopene


enzyme_display_name: 4-hydroxybutanoyl-CoA dehydratase

organism: Clostridium aminobutyricum

assay_conditions_summary: pH 9; cofactor CoA

column_label: Abstract states the dehydratase catalyses reversible conversion of 4-hydroxybutyryl-CoA (Km = 50 microM) to crotonyl-CoA.

raw_value_unit_evidence: Km raw_value=50 raw_unit=microM

table_label: PubMed abstract PMID 8344309

enzyme: 4-hydroxybutanoyl-CoA dehydratase


enzyme_display_name: delta-guaiene synthase

organism: Aquilaria crassna

proof_lines: kcat is 7.34 x 10(-3) sec(-1) for farnesyl diphosphate.

enzyme: delta-guaiene synthase


proof_lines: kcat is 9.72 x 10(-5) sec(-1) for farnesyl diphosphate.


proof_lines: kcat is 4.99 x 10(-3) sec(-1) for farnesyl diphosphate.


organism: Thiocapsa roseopersicina


enzyme_display_name: 3-dehydroshikimate dehydratase

organism: Neurospora crassa

proof_lines: Neurospora crassa 3-dehydroshikimate dehydratase

enzyme: 3-dehydroshikimate dehydratase


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Metallosphaera sedula

assay_conditions_summary: pH 8; 343.15 K; cofactor CoA


enzyme_display_name: tetrahymanol synthase

organism: Tetrahymena thermophila

substrate_name: squalene

assay_conditions_summary: pH 7

enzyme: tetrahymanol synthase

substrate: squalene


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.


substrate_name: geranyl diphosphate


enzyme_display_name: L-galactonate dehydratase

organism: Trichoderma reesei

substrate_name: L-galactonate

enzyme: L-galactonate dehydratase

substrate: L-galactonate


enzyme_display_name: 2-methylfumaryl-CoA hydratase

organism: Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM B-1755)

substrate_name: mesaconyl-CoA

column_label: PDF Table 4 row Mesaconyl-C1-CoA / mesaconyl-CoA; Km column reports Km 1.0 +/- 0.1 mM, matching the exported Km-only record.

row_label: Mesaconyl-C1-CoA / mesaconyl-CoA

table_label: Table 4. Catalytic properties of recombinant Mch from H. hispanica

enzyme: 2-methylfumaryl-CoA hydratase

substrate: mesaconyl-CoA


enzyme_display_name: versicolorin B synthase

organism: Aspergillus parasiticus

substrate_name: versiconal

enzyme: versicolorin B synthase

substrate: versiconal


enzyme_display_name: (-)-sabinene synthase

organism: Picea sitchensis

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

enzyme: (-)-sabinene synthase

substrate: geranyl diphosphate


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


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


enzyme_display_name: alpha-humulene synthase

organism: Gossypium hirsutum

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

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

enzyme: alpha-humulene synthase


organism: Methylorubrum extorquens

proof_lines:
30°C, pH 8.0
Raw SKiD Env: Temp=30°C, pH=8

source_databases_merged: brenda skid


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


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

organism: Lavandula x intermedia

proof_lines: recombinant His-tagged enzyme, pH 7.2, temperature not specified in the publication

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


organism: Conocephalum conicum


enzyme_display_name: 1,8-cineole synthase

organism: Artemisia annua

enzyme: 1,8-cineole synthase


enzyme_display_name: pterocarpan synthase

organism: Glycyrrhiza echinata

enzyme: pterocarpan synthase


enzyme_display_name: gamma-curcumene synthase

organism: Zea mays

substrate_name: farnesyl diphosphate (in the presence of 10 mM magnesium and 1 mM manganese)

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

enzyme: gamma-curcumene synthase


substrate_name: geranyl diphosphate (in the presence of 10 mM magnesium and 1 mM manganese)


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


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


enzyme_display_name: (E)-beta-ocimene synthase

substrate_name: (2E)-geranyl diphosphate

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


organism: Salvia fruticosa

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


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


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


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


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


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N338C 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.


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


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


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


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


organism: Zingiber zerumbet

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


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.


enzyme_display_name: 7-epi-sesquithujene synthase

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

enzyme: 7-epi-sesquithujene synthase


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


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


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


organism: Piper nigrum

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

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


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


organism: Pinus contorta

substrate_name: (3S)-linalyl diphosphate

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

substrate: (3S)-linalyl diphosphate


substrate_name: Geranyl diphosphate

substrate: Geranyl diphosphate


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


substrate_name: Unknown

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

substrate: Geranyl diphosphate; H2O


organism: Salvia officinalis


organism: Danio rerio

substrate_name: prostaglandin H2 (at 23 degrees Celsius)

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


substrate_name: geranyl diphosphate

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)