substrate_name: isovaleryl-CoA

column_label: Table 1 row Isovaleryl-CoA, Triketide pyrone Km column: 99.1 uM.

raw_value_unit_evidence: Table 1 row Isovaleryl-CoA under Triketide pyrone: Km 99.1 uM.

row_label: Isovaleryl-CoA / Triketide pyrone

substrate: isovaleryl-CoA


enzyme_display_name: 3,5,7-trioxododecanoyl-CoA synthase

organism: Cannabis sativa

substrate_name: octanoyl-CoA

source_db: uniprot

verification_status: verified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: cofactor CoA

column_label: Table 1 row Octanoyl-CoA, Triketide pyrone Km column: 81.7 uM.

raw_value_unit_evidence: Table 1 row Octanoyl-CoA under Triketide pyrone: Km 81.7 uM.

row_label: Octanoyl-CoA / Triketide pyrone

table_label: Table 1

data_origin: experimental

enzyme: 3,5,7-trioxododecanoyl-CoA synthase

substrate: octanoyl-CoA

status: verified

source: uniprot


enzyme_display_name: 4-hydroxycoumarin synthase

organism: Sorbus aucuparia

source_db: brenda

verification_status: corrected

assay_conditions_summary: pH 6.5; buffer and no single assay pH numeral; cofactor CoA

column_label: Table 2: Steady-state kinetic parameters for BIS isoenzymes from S. aucuparia cell cultures with benzoyl-CoA and salicoyl-CoA as starter substrates (Plant Mol Biol 2010, 72:17-25); isoenzyme row 'BIS2'; group head 'salicoyl-CoA'; column 'kcat (min^-1)' = 1.76; column 'Km (uM)' = 2.3; column 'kcat/Km (M^-1 s^-1)' = 12,716; the same printed line also carries the benzoyl-CoA group (three cells) and the Malonyl-CoA group head with one cell, column 'Km (uM)' = 10.0.

raw_value_unit_evidence: Table 2, isoenzyme row 'BIS2', salicoyl-CoA group: kcat = 1.76 min^-1; Km = 2.3 uM; printed kcat/Km = 12,716 M^-1 s^-1.

row_label: Table 2, isoenzyme row 'BIS2', salicoyl-CoA starter-substrate block (the three columns headed kcat (min^-1), Km (uM) and kcat/Km (M^-1 s^-1) under the salicoyl-CoA group head)

source_databases_merged: brenda uniprot

enzyme: 4-hydroxycoumarin synthase

status: corrected

source: brenda


column_label: Table 2: Steady-state kinetic parameters for BIS isoenzymes from S. aucuparia cell cultures with benzoyl-CoA and salicoyl-CoA as starter substrates (Plant Mol Biol 2010, 72:17-25); isoenzyme row 'BIS3'; group head 'salicoyl-CoA'; column 'kcat (min^-1)' = 2.22; column 'Km (uM)' = 3.2; column 'kcat/Km (M^-1 s^-1)' = 11,486; the same printed line also carries the benzoyl-CoA group (three cells) and the Malonyl-CoA group head with one cell, column 'Km (uM)' = 10.1.

raw_value_unit_evidence: Table 2, isoenzyme row 'BIS3', salicoyl-CoA group: kcat = 2.22 min^-1; Km = 3.2 uM; printed kcat/Km = 11,486 M^-1 s^-1.

row_label: Table 2, isoenzyme row 'BIS3', salicoyl-CoA starter-substrate block (the three columns headed kcat (min^-1), Km (uM) and kcat/Km (M^-1 s^-1) under the salicoyl-CoA group head)


substrate_name: malonyl-CoA

verification_status: unverified

assay_conditions_summary: pH 6.5; cofactor CoA

proof_lines: kcat is 0.89 min(-1) with benzoyl-CoA as substrate. kcat is 1.76 min(-1) with salicoyl-CoA as substrate.

substrate: malonyl-CoA

status: unverified


proof_lines: kcat is 1.02 min(-1) with benzoyl-CoA as substrate. kcat is 2.22 min(-1) with salicoyl-CoA as substrate.


enzyme_display_name: 4-hydroxycoumarin synthase 2

substrate_name: benzoyl-CoA

enzyme: 4-hydroxycoumarin synthase 2

substrate: benzoyl-CoA


enzyme_display_name: 4-hydroxycoumarin synthase 1

enzyme: 4-hydroxycoumarin synthase 1


enzyme_display_name: benzalacetone synthase

organism: Rheum palmatum

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

column_label: Table I BAS WT row, malonyl-CoA columns kcat, Km, and kcat/Km: 1780 +/- 59 x10^-3 min^-1; 23.3 +/- 2.2 uM; 1273 s^-1 M^-1.

raw_value_unit_evidence: BAS WT malonyl-CoA row: kcat 1780 +/- 59 x10^-3 min^-1; Km 23.3 +/- 2.2 uM; independently printed kcat/Km 1273 s^-1 M^-1.

row_label: BAS WT

table_label: Table I. Steady state kinetic parameters for enzyme reactions

enzyme: benzalacetone synthase


organism: Escherichia coli

source_db: oed

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D232A to reconstruct the assayed variant sequence.

mutation_type: substitution

column_label: PMCID PMC2435086 Table 4; row D232A; columns kcat (s^-1) and KM, UDP-3-O-(R-3-OHC14)-GlcN (uM); kcat/Km is same-row computed after converting Km to mM.

table_label: Table 4. Steady-State Kinetic Parameters for Selected EcLpxD Mutants

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F41A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row F41A; columns kcat (s^-1) and KM, UDP-3-O-(R-3-OHC14)-GlcN (uM); kcat/Km is same-row computed after converting Km to mM.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H239A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row H239A; columns kcat (s^-1) and KM, UDP-3-O-(R-3-OHC14)-GlcN (uM); kcat/Km is same-row computed after converting Km to mM.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H276A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row H276A; columns kcat (s^-1) and KM, UDP-3-O-(R-3-OHC14)-GlcN (uM); kcat/Km is same-row computed after converting Km to mM.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K194A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row K194A; columns kcat (s^-1) and KM, UDP-3-O-(R-3-OHC14)-GlcN (uM); kcat/Km is same-row computed after converting Km to mM.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K46A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row K46A; columns kcat (s^-1) and KM, UDP-3-O-(R-3-OHC14)-GlcN (uM); kcat/Km is same-row computed after converting Km to mM.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N233A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row N233A; columns kcat (s^-1) and KM, UDP-3-O-(R-3-OHC14)-GlcN (uM); kcat/Km is same-row computed after converting Km to mM.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q236A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row Q236A; columns kcat (s^-1) and KM, UDP-3-O-(R-3-OHC14)-GlcN (uM); kcat/Km is same-row computed after converting Km to mM.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R293A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2435086 Table 4; row R293A; columns kcat (s^-1) and KM, UDP-3-O-(R-3-OHC14)-GlcN (uM); kcat/Km is same-row computed after converting Km to mM.


column_label: PMCID PMC2435086 Table 4; row Wild type; columns kcat (s^-1) and KM, UDP-3-O-(R-3-OHC14)-GlcN (uM); kcat/Km is same-row computed after converting Km to mM.

raw_value_unit_evidence: Table 4 row Wild type: kcat 23+/-1 s^-1; KM, UDP-3-O-(R-3-OHC14)-GlcN 2.5+/-0.3 uM.

row_label: Wild type


kcat_over_km_origin: calculated

assay_conditions_summary: pH 8; cofactor CoA

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


enzyme_display_name: UniProt Q94FV7

source_db: skid

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

sequence_source: multiple

proof_lines: kcat is 1.79 min(-1) with 4-coumaroyl-CoA as substrate (at pH 8 and 30 degrees Celsius).

source_databases_merged: skid uniprot

enzyme: UniProt Q94FV7

source: skid


substrate_name: N-methylanthraniloyl-CoA

proof_lines: pH 8.0, temperature not specified in the publication

source_databases_merged: brenda skid

substrate: N-methylanthraniloyl-CoA


substrate_name: D-phenylalanyl-CoA

substrate: D-phenylalanyl-CoA


substrate_name: Hexanoyl-CoA; Malonyl-CoA

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

substrate: Hexanoyl-CoA; Malonyl-CoA


substrate_name: Malonyl-CoA; 2-Hydroxybenzoyl-CoA

assay_conditions_summary: buffer and no single assay pH numeral; cofactor CoA

table_label: Table 2: Steady-state kinetic parameters for BIS isoenzymes from S. aucuparia cell cultures with benzoyl-CoA and salicoyl-CoA as starter substrates (Plant Mol Biol 2010, 72:17-25)

substrate: Malonyl-CoA; 2-Hydroxybenzoyl-CoA


substrate_name: 2-Hydroxybenzoyl-CoA; Malonyl-CoA

substrate: 2-Hydroxybenzoyl-CoA; Malonyl-CoA


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


enzyme_display_name: Polyketide synthase 4

organism: Rubus idaeus

substrate_name: p-coumaryl CoA

enzyme: Polyketide synthase 4

substrate: p-coumaryl CoA


substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.4; cofactor CoA

column_label: Table 3. Kinetic parameters; row VioB O7 / SH-CoA table row resolved by adjacent prose as acetyl-CoA variable-substrate assay; column kcat /s; metric kcat; normalized value 21.6 s^-1 | Table 3. Kinetic parameters and adjacent prose; row VioB O7 / acetyl-CoA variable-substrate assay; column Km (uM); metric km; normalized value 0.554 mM | Table 3. Kinetic parameters; row VioB O7 / acetyl-CoA variable-substrate assay; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 38.98916967509025 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=21.6 normalized_unit=s^-1; km normalized_value=0.554 normalized_unit=mM; kcat_over_km normalized_value=38.98916967509025 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=21.6 raw_unit=s^-1; km raw_value=554 raw_unit=uM; kcat_over_km raw_value=21.6/0.554 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km evidence

table_label: Table 3. Kinetic parameters

substrate: acetyl-CoA


column_label: Table 3. Kinetic parameters; row VioB O7 / dTDP-D-Qui4N; column kcat /s; metric kcat; normalized value 155.3 s^-1 | Table 3. Kinetic parameters; row VioB O7 / dTDP-D-Qui4N; column Km (uM); metric km; normalized value 0.142 mM | Table 3. Kinetic parameters; row VioB O7 / dTDP-D-Qui4N; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 1093.6619718309862 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=155.3 normalized_unit=s^-1; km normalized_value=0.142 normalized_unit=mM; kcat_over_km normalized_value=1093.6619718309862 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=155.3 raw_unit=s^-1; km raw_value=142 raw_unit=uM; kcat_over_km raw_value=155.3/0.142 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km cells

row_label: VioB O7 / dTDP-D-Qui4N


organism: Strongylocentrotus purpuratus

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

assay_conditions_summary: pH 8; 296.15 K; cofactor CoA


enzyme_display_name: benzyl alcohol O-benzoyltransferase

organism: Petunia x hybrida

assay_conditions_summary: pH 7.7; 295.15 K; cofactor CoA

column_label: Table I row Phenyl ethanol footnote e columns Km, Kcat, Kcat/Km

row_label: Phenyl ethanol

table_label: Table I

enzyme: benzyl alcohol O-benzoyltransferase


column_label: Table I row Acetyl-CoA columns Km, Kcat, Kcat/Km

row_label: Acetyl-CoA


substrate_name: benzyl alcohol

column_label: Table I row Benzyl alcohol footnote d columns Km, Kcat, Kcat/Km

row_label: Benzyl alcohol

substrate: benzyl alcohol


enzyme_display_name: UniProt Q9Y7D1

organism: Aspergillus terreus

substrate_name: butyryl-CoA

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q9Y7D1

substrate: butyryl-CoA


organism: Streptomyces coelicolor

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y224M with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature Y224L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y224C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y224F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


assay_conditions_summary: pH 7.4; buffer 100 mM Tris-HCl; cofactor CoA

proof_lines: wild type enzyme, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C


assay_conditions_summary: pH 5.5; 303.15 K; cofactor CoA

column_label: Table 1 row Isovaleryl-CoA, Triketide pyrone columns: Km 99.1 uM, kcat 0.585 min^-1, kcat/Km 98.4 s^-1 M^-1.

normalized_value_unit_evidence: Km 0.0991 mM; kcat 0.00975 s^-1; kcat/Km 0.0984 s^-1 mM^-1 from explicit paper column; source kcat and Km are rounded.

raw_value_unit_evidence: Table 1 row Isovaleryl-CoA under Triketide pyrone: Km 99.1 uM; kcat 0.585 min^-1; kcat/Km 98.4 s^-1 M^-1.


substrate_name: Hexanoyl-CoA

substrate: Hexanoyl-CoA


substrate_name: Octanoyl-CoA

column_label: Table 1 row Octanoyl-CoA, Triketide pyrone columns: Km 81.7 uM, kcat 0.525 min^-1, kcat/Km 107 s^-1 M^-1.

normalized_value_unit_evidence: Km 0.0817 mM; kcat 0.00875 s^-1; kcat/Km 0.107 s^-1 mM^-1 from explicit paper column; source values are rounded.

raw_value_unit_evidence: Table 1 row Octanoyl-CoA under Triketide pyrone: Km 81.7 uM; kcat 0.525 min^-1; kcat/Km 107 s^-1 M^-1.

substrate: Octanoyl-CoA


substrate_name: butanoyl-CoA

column_label: Table 1 row Butyryl-CoA, Triketide pyrone columns: Km 88.9 uM, kcat 0.719 min^-1, kcat/Km 134 s^-1 M^-1.

normalized_value_unit_evidence: Km 0.0889 mM; kcat 0.011983333333333334 s^-1; kcat/Km 0.134 s^-1 mM^-1 from explicit paper column; source values are rounded.

raw_value_unit_evidence: Table 1 row Butyryl-CoA under Triketide pyrone: Km 88.9 uM; kcat 0.719 min^-1; kcat/Km 134 s^-1 M^-1.

row_label: Butyryl-CoA / Triketide pyrone

substrate: butanoyl-CoA


enzyme_display_name: UniProt B0VHH0

organism: Candidatus Cloacimonas acidaminovorans

enzyme: UniProt B0VHH0


enzyme_display_name: 2-heptyl-4(1H)-quinolone synthase subunit PqsC

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

substrate_name: octanoyl-CoA (in the presence of PqsB)

substrate: octanoyl-CoA (in the presence of PqsB)


substrate_name: 2-ABA (in the presence of PqsB)

enzyme: 2-heptyl-4(1H)-quinolone synthase subunit PqsC

substrate: 2-ABA (in the presence of PqsB)


enzyme_display_name: methanol O-anthraniloyltransferase

organism: Vitis labrusca

substrate_name: methanol

smiles: CO

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, native enzyme

proof_lines: pH 7.5, 20-22°C, cosubstrate: anthraniloyl-CoA, recombinant enzyme

proof_lines: kcat is 0.045 sec(-1) with benzoyl-CoA as substrate (with native enzyme). kcat is 0.022 sec(-1) with anthraniloyl-CoA as substrate (with native enzyme). kcat is 0.0035 sec(-1) with methanol as substrate (with native enzyme). kcat is 0.045 s

enzyme: methanol O-anthraniloyltransferase

substrate: methanol


substrate_name: anthraniloyl-CoA

proof_lines: pH 7.5, 20-22°C, cosubstrate: methanol, recombinant enzyme

proof_lines: pH 7.5, 20-22°C, cosubstrate: methanol, native enzyme

substrate: anthraniloyl-CoA


enzyme_display_name: Methanol O-anthraniloyltransferase

substrate_name: benzoyl-CoA (with native enzyme, in the presence of benzyl alcohol)

enzyme: Methanol O-anthraniloyltransferase


substrate_name: malonyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C171S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; buffer 100 mM Tris-HCl; cofactor CoA

proof_lines: mutant enzyme C171S, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C

substrate: malonyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C184S with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C184S, in 100 mM Tris-HCl buffer (pH 7.5), at 22°C


enzyme_display_name: 3,5-dihydroxyphenylacetyl-CoA synthase

organism: Amycolatopsis mediterranei

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

assay_conditions_summary: pH 7.5; 297.15 K; cofactor CoA

enzyme: 3,5-dihydroxyphenylacetyl-CoA synthase


enzyme_display_name: spermidine disinapoyl transferase

organism: Arabidopsis thaliana

substrate_name: putrescine

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

smiles: C(CCN)CN

assay_conditions_summary: pH 7.3; 303.15 K; buffer vitro forward-reaction assay in 0.1 M Tris-HCl; cofactor CoA

column_label: Table 1: Kinetics of Recombinant At2g23510 on Different Acyl Donors and Acceptors (Plant Cell 2009, 21(1):318-333); Table 1, Forward reaction, Acyl acceptor row Putrescine; the turnover number 0.3 s^-1 comes from the kcat (s^-1) column of Table 1 and the Michaelis constant 236.9 uM comes from the Km (uM) column of Table 1. Table 1 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 0.3 s^-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 0.3 s^(-1). Km: printed cell 236.9 uM; 1 uM is 0.001 mM, so 236.9 / 1000 = 0.2369 mM; the paper value is 0.2369 mM. kcat/Km: Table 1 prints no kcat/Km cell for this measurement, so the exported 1.2663571127057829 s^(-1)*mM^(-1) is not a printed value; it is the quotient 0.3 / 0.2369 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Forward reaction, Acyl acceptor row Putrescine: kcat = 0.3 s^-1 (printed column the kcat (s^-1) column of Table 1); Km = 236.9 uM (printed column the Km (uM) column of Table 1). Table 1 carries no catalytic-efficiency column, so no kcat/Km value is printed for this measurement.

source_databases_merged: brenda skid uniprot

enzyme: spermidine disinapoyl transferase

substrate: putrescine


substrate_name: sinapoyl-CoA

column_label: Table 1: Kinetics of Recombinant At2g23510 on Different Acyl Donors and Acceptors (Plant Cell 2009, 21(1):318-333); Table 1, Forward reaction, Acyl donor row Sinapoyl-CoA; the turnover number 5.1 s^-1 comes from the kcat (s^-1) column of Table 1 and the Michaelis constant 8.3 uM comes from the Km (uM) column of Table 1. Table 1 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 5.1 s^-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 5.1 s^(-1). Km: printed cell 8.3 uM; 1 uM is 0.001 mM, so 8.3 / 1000 = 0.0083 mM; the paper value is 0.0083 mM. kcat/Km: Table 1 prints no kcat/Km cell for this measurement, so the exported 614.4578313253012 s^(-1)*mM^(-1) is not a printed value; it is the quotient 5.1 / 0.0083 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Forward reaction, Acyl donor row Sinapoyl-CoA: kcat = 5.1 s^-1 (printed column the kcat (s^-1) column of Table 1); Km = 8.3 uM (printed column the Km (uM) column of Table 1). Table 1 carries no catalytic-efficiency column, so no kcat/Km value is printed for this measurement.

substrate: sinapoyl-CoA


substrate_name: spermidine

smiles: C(CCNCCCN)CN

column_label: Table 1: Kinetics of Recombinant At2g23510 on Different Acyl Donors and Acceptors (Plant Cell 2009, 21(1):318-333); Table 1, Forward reaction, Acyl acceptor row Spermidine; the turnover number 5.6 s^-1 comes from the kcat (s^-1) column of Table 1 and the Michaelis constant 37.4 uM comes from the Km (uM) column of Table 1. Table 1 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 5.6 s^-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 5.6 s^(-1). Km: printed cell 37.4 uM; 1 uM is 0.001 mM, so 37.4 / 1000 = 0.0374 mM; the paper value is 0.0374 mM. kcat/Km: Table 1 prints no kcat/Km cell for this measurement, so the exported 149.7326203208556 s^(-1)*mM^(-1) is not a printed value; it is the quotient 5.6 / 0.0374 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Forward reaction, Acyl acceptor row Spermidine: kcat = 5.6 s^-1 (printed column the kcat (s^-1) column of Table 1); Km = 37.4 uM (printed column the Km (uM) column of Table 1). Table 1 carries no catalytic-efficiency column, so no kcat/Km value is printed for this measurement.

substrate: spermidine


assay_conditions_summary: pH 7.3; 303.15 K; buffer 0.1 M Tris-HCl; cofactor CoA

column_label: Table 1: Kinetics of Recombinant At2g23510 on Different Acyl Donors and Acceptors (Plant Cell 2009, 21(1):318-333); Table 1, Reverse reaction, row Disinapoyl spermidine; the turnover number 37.8 s^-1 comes from the kcat (s^-1) column of Table 1 and the Michaelis constant 34.6 uM comes from the Km (uM) column of Table 1. Table 1 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 37.8 s^-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 37.8 s^(-1). Km: printed cell 34.6 uM; 1 uM is 0.001 mM, so 34.6 / 1000 = 0.0346 mM; the paper value is 0.0346 mM. kcat/Km: Table 1 prints no kcat/Km cell for this measurement, so the exported 1092.4855491329479 s^(-1)*mM^(-1) is not a printed value; it is the quotient 37.8 / 0.0346 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Reverse reaction, row Disinapoyl spermidine: kcat = 37.8 s^-1 (printed column the kcat (s^-1) column of Table 1); Km = 34.6 uM (printed column the Km (uM) column of Table 1). Table 1 carries no catalytic-efficiency column, so no kcat/Km value is printed for this measurement.


substrate_name: CoA

column_label: Table 1: Kinetics of Recombinant At2g23510 on Different Acyl Donors and Acceptors (Plant Cell 2009, 21(1):318-333); Table 1, Reverse reaction, row CoA; the turnover number 39.6 s^-1 comes from the kcat (s^-1) column of Table 1 and the Michaelis constant 83.6 uM comes from the Km (uM) column of Table 1. Table 1 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 39.6 s^-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 39.6 s^(-1). Km: printed cell 83.6 uM; 1 uM is 0.001 mM, so 83.6 / 1000 = 0.0836 mM; the paper value is 0.0836 mM. kcat/Km: Table 1 prints no kcat/Km cell for this measurement, so the exported 473.68421052631584 s^(-1)*mM^(-1) is not a printed value; it is the quotient 39.6 / 0.0836 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Reverse reaction, row CoA: kcat = 39.6 s^-1 (printed column the kcat (s^-1) column of Table 1); Km = 83.6 uM (printed column the Km (uM) column of Table 1). Table 1 carries no catalytic-efficiency column, so no kcat/Km value is printed for this measurement.

row_label: Table 1, Reverse reaction, row CoA

substrate: CoA


enzyme_display_name: phloroglucinol synthase

organism: Pseudomonas fluorescens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y256R/A289R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y256R/A289R, pH and temperature not specified in the publication

enzyme: phloroglucinol synthase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K210L/Y256R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K210L/Y256R, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A289R with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A289R, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y256R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y256R, pH and temperature not specified in the publication


enzyme_display_name: spermidine dicoumaroyl transferase

column_label: Table 2: Kinetics of Recombinant At2g25150 on Different Acyl Donors and Acceptors (Plant Cell 2009, 21(1):318-333); Table 2, Acyl acceptor row Spermidine; the turnover number 3.1 s^-1 comes from the kcat (s^-1) column of Table 2 and the Michaelis constant 52.7 uM comes from the Km (uM) column of Table 2. Table 2 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 3.1 s^-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 3.1 s^(-1). Km: printed cell 52.7 uM; 1 uM is 0.001 mM, so 52.7 / 1000 = 0.0527 mM; the paper value is 0.0527 mM. kcat/Km: Table 2 prints no kcat/Km cell for this measurement, so the exported 58.82352941176471 s^(-1)*mM^(-1) is not a printed value; it is the quotient 3.1 / 0.0527 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, Acyl acceptor row Spermidine: kcat = 3.1 s^-1 (printed column the kcat (s^-1) column of Table 2); Km = 52.7 uM (printed column the Km (uM) column of Table 2). Table 2 carries no catalytic-efficiency column, so no kcat/Km value is printed for this measurement.

row_label: Table 2, Acyl acceptor row Spermidine

enzyme: spermidine dicoumaroyl transferase


column_label: Table 2: Kinetics of Recombinant At2g25150 on Different Acyl Donors and Acceptors (Plant Cell 2009, 21(1):318-333); Table 2, Acyl donor row Coumaroyl-CoA; the turnover number 3.4 s^-1 comes from the kcat (s^-1) column of Table 2 and the Michaelis constant 10.6 uM comes from the Km (uM) column of Table 2. Table 2 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed cell 3.4 s^-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 3.4 s^(-1). Km: printed cell 10.6 uM; 1 uM is 0.001 mM, so 10.6 / 1000 = 0.0106 mM; the paper value is 0.0106 mM. kcat/Km: Table 2 prints no kcat/Km cell for this measurement, so the exported 320.75471698113205 s^(-1)*mM^(-1) is not a printed value; it is the quotient 3.4 / 0.0106 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, Acyl donor row Coumaroyl-CoA: kcat = 3.4 s^-1 (printed column the kcat (s^-1) column of Table 2); Km = 10.6 uM (printed column the Km (uM) column of Table 2). Table 2 carries no catalytic-efficiency column, so no kcat/Km value is printed for this measurement.

row_label: Table 2, Acyl donor row Coumaroyl-CoA


organism: Streptomyces griseus

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

proof_lines: in 100 mM Tris-HCl (pH 7.5), 1 mM EDTA, 1 mM 2-mercaptoethanol, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S82G to reconstruct the assayed variant sequence.

column_label: Official PMC HTML Table 2, row S82G, columns Km (S)-KAH, kcat, and kcat/Km ((S)-KAH), HTML lines 1798-1880.

normalized_value_unit_evidence: kcat normalized_value=0.13 normalized_unit=s^-1; km normalized_value=1.181 normalized_unit=mM; kcat_over_km normalized_value=0.1 normalized_unit=s^-1 mM^-1.

table_label: Table 2. Steady-state kinetic analysis of Kce and point mutants


column_label: Official PMC HTML Table 2, row S82G, columns Km AcCoA, kcat, and kcat/Km (AcCoA), HTML lines 1798-1880.

normalized_value_unit_evidence: kcat normalized_value=0.13 normalized_unit=s^-1; km normalized_value=0.046 normalized_unit=mM; kcat_over_km normalized_value=2.8 normalized_unit=s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E143Q to reconstruct the assayed variant sequence.

column_label: Official PMC HTML Table 2, row E143Q, columns Km (S)-KAH, kcat, and kcat/Km ((S)-KAH), HTML lines 1798-1880.

normalized_value_unit_evidence: kcat normalized_value=0.32 normalized_unit=s^-1; km normalized_value=0.442 normalized_unit=mM; kcat_over_km normalized_value=0.7 normalized_unit=s^-1 mM^-1.


column_label: Official PMC HTML Table 2, row E143Q, columns Km AcCoA, kcat, and kcat/Km (AcCoA), HTML lines 1798-1880.

normalized_value_unit_evidence: kcat normalized_value=0.32 normalized_unit=s^-1; km normalized_value=0.012 normalized_unit=mM; kcat_over_km normalized_value=26.7 normalized_unit=s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E143G to reconstruct the assayed variant sequence.

column_label: Official PMC HTML Table 2, row E143G, columns Km (S)-KAH, kcat, and kcat/Km ((S)-KAH), HTML lines 1798-1880.

normalized_value_unit_evidence: kcat normalized_value=0.37 normalized_unit=s^-1; km normalized_value=0.921 normalized_unit=mM; kcat_over_km normalized_value=0.4 normalized_unit=s^-1 mM^-1.


column_label: Official PMC HTML Table 2, row E143G, columns Km AcCoA, kcat, and kcat/Km (AcCoA), HTML lines 1798-1880.

normalized_value_unit_evidence: kcat normalized_value=0.37 normalized_unit=s^-1; km normalized_value=0.024 normalized_unit=mM; kcat_over_km normalized_value=15.4 normalized_unit=s^-1 mM^-1.


column_label: Official PMC HTML Table 2, row Wild type, columns Km (S)-KAH, kcat, and kcat/Km ((S)-KAH), HTML lines 1798-1880.

normalized_value_unit_evidence: kcat normalized_value=2.69 normalized_unit=s^-1; km normalized_value=0.208 normalized_unit=mM; kcat_over_km normalized_value=12.9 normalized_unit=s^-1 mM^-1.


column_label: Official PMC HTML Table 2, row Wild type, columns Km AcCoA, kcat, and kcat/Km (AcCoA), HTML lines 1798-1880.

normalized_value_unit_evidence: kcat normalized_value=2.69 normalized_unit=s^-1; km normalized_value=0.012 normalized_unit=mM; kcat_over_km normalized_value=224.2 normalized_unit=s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y224L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA


substrate_name: hexanoyl-CoA

substrate: hexanoyl-CoA


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


substrate_name: Methanol; Anthraniloyl-CoA

assay_conditions_summary: cofactor CoA

substrate: Methanol; Anthraniloyl-CoA


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

substrate_name: 5 malonyl-CoA

proof_lines: kcat is 0.48 min(-1) for THN synthase activity with THN as substrate.

substrate: 5 malonyl-CoA


enzyme_display_name: Spermidine sinapoyl-CoA acyltransferase

substrate_name: disinapoyl-spermidine (with CoA as cosubstrate, at 30 degrees Celsius)

proof_lines: kcat is 5.1 sec(-1) with sinapoyl-CoA as substrate (in the presence of spermidine as the acyl acceptor). kcat is 5.6 sec(-1) with spermidine as substrate (in the presence of sinapoyl-CoA as the acyl donor). kcat is 0.3 sec(-1) with putresci

enzyme: Spermidine sinapoyl-CoA acyltransferase


organism: Amycolatopsis orientalis

proof_lines: kcat is 1 min(-1) for transferase activity with malonyl-CoA as substrate.


organism: Amycolatopsis balhimycina

proof_lines: kcat is 0.81 min(-1) for transferase activity with malonyl-CoA as substrate.


enzyme_display_name: (Z)-3-hexen-1-ol acetyltransferase

smiles: CCCCCCCCO

enzyme: (Z)-3-hexen-1-ol acetyltransferase


smiles: CC/C=C\CCO

assay_conditions_summary: pH 7.7; 298.15 K; cofactor CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


enzyme_display_name: 3-keto-5-aminohexanoate cleavage enzyme

organism: Cloacimonas acidaminovorans (strain Evry)

substrate_name: KAH

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

column_label: Official PMC HTML Table 2, row Wild type, column Km (S)-KAH, HTML lines 1798-1880.

raw_value_unit_evidence: Table 2 row Wild type, Km (S)-KAH column = 0.208 +/- 0.032 mM.

enzyme: 3-keto-5-aminohexanoate cleavage enzyme

substrate: KAH


substrate_name: acetoacetate

proof_lines: kcat is 2.69 sec(-1) for 3-keto-5-aminohexanoate cleavage.

substrate: acetoacetate


enzyme_display_name: Phloroglucinol synthase

organism: Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)

column_label: PMID 15826166 primary JACS prose, purified PhlD enzymology segment, malonyl-CoA Km = 5.6 uM.

raw_value_unit_evidence: Primary prose reports a Km = 5.6 uM for malonyl-CoA and a kcat = 10 min-1 determined for PhlD.

row_label: Purified PhlD / malonyl-CoA

table_label: Primary prose enzymology section in PMID 15826166

enzyme: Phloroglucinol synthase


organism: Salmonella enterica subsp. enterica serovar Typhimurium

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines: cosubstrate: (S)-1-aminoethylphosphonic acid, pH 7.5, 25°C


substrate_name: 4-aminobutylphosphonic acid

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

substrate: 4-aminobutylphosphonic acid


substrate_name: 1-aminobutyl phosphonic acid

substrate: 1-aminobutyl phosphonic acid


substrate_name: (aminomethyl)phosphonate

substrate: (aminomethyl)phosphonate


substrate_name: 2-aminoethyl phosphonic acid

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

substrate: 2-aminoethyl phosphonic acid


substrate_name: (S)-1-aminoethylphosphonic acid

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

substrate: (S)-1-aminoethylphosphonic acid


substrate_name: propionyl-CoA

substrate: propionyl-CoA


substrate_name: 2-aminoethanesulfonic acid

substrate: 2-aminoethanesulfonic acid


substrate_name: 2-aminoethanesulfinic acid

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

substrate: 2-aminoethanesulfinic acid


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

substrate_name: 3-aminopropylphosphonate (in the presence of Ni(2+))

proof_lines: kcat is 13.1 sec(-1) for the acetylation of (S)-1AEP. kcat is 14.7 sec(-1) for the propionylation of (S)-1AEP. kcat is 0.4 sec(-1) for the malonylation of (S)-1AEP. kcat is 7.0 sec(-1) for the acetylation of aminomethylphosphonate. kcat is


organism: Mycobacterium tuberculosis

proof_lines: kcat is 0.12 min(-1) with trehalose-2-sulfate-2'-palmitate as substrate.


organism: Mycobacterium marinum

substrate_name: glycosyl-phenolphthiocerol

substrate: glycosyl-phenolphthiocerol


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: mycoserosate acylated to mas protein

substrate: mycoserosate acylated to mas protein


organism: Papaver somniferum


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


enzyme_display_name: 4-hydroxycoumarin synthase

organism: Sorbus aucuparia

assay_conditions_summary: pH 7; 308.15 K; buffer and no single assay pH numeral; cofactor CoA

column_label: Table 2: Steady-state kinetic parameters for BIS isoenzymes from S. aucuparia cell cultures with benzoyl-CoA and salicoyl-CoA as starter substrates (Plant Mol Biol 2010, 72:17-25); isoenzyme row 'BIS2'; group head 'salicoyl-CoA'; column 'kcat (min^-1)' = 1.76; column 'Km (uM)' = 2.3; column 'kcat/Km (M^-1 s^-1)' = 12,716; the same printed line also carries the benzoyl-CoA group (three cells) and the Malonyl-CoA group head with one cell, column 'Km (uM)' = 10.0.

raw_value_unit_evidence: Table 2, isoenzyme row 'BIS2', salicoyl-CoA group: kcat = 1.76 min^-1; Km = 2.3 uM; printed kcat/Km = 12,716 M^-1 s^-1.

enzyme: 4-hydroxycoumarin synthase


column_label: Table 2: Steady-state kinetic parameters for BIS isoenzymes from S. aucuparia cell cultures with benzoyl-CoA and salicoyl-CoA as starter substrates (Plant Mol Biol 2010, 72:17-25); isoenzyme row 'BIS3'; group head 'salicoyl-CoA'; column 'kcat (min^-1)' = 2.22; column 'Km (uM)' = 3.2; column 'kcat/Km (M^-1 s^-1)' = 11,486; the same printed line also carries the benzoyl-CoA group (three cells) and the Malonyl-CoA group head with one cell, column 'Km (uM)' = 10.1.

raw_value_unit_evidence: Table 2, isoenzyme row 'BIS3', salicoyl-CoA group: kcat = 2.22 min^-1; Km = 3.2 uM; printed kcat/Km = 11,486 M^-1 s^-1.


column_label: Table 2: Steady-state kinetic parameters for BIS isoenzymes from S. aucuparia cell cultures with benzoyl-CoA and salicoyl-CoA as starter substrates (Plant Mol Biol 2010, 72:17-25); isoenzyme row 'BIS1'; group head 'salicoyl-CoA'; column 'kcat (min^-1)' = 0.27; column 'Km (uM)' = 0.8; column 'kcat/Km (M^-1 s^-1)' = 5,625; the same printed line also carries the benzoyl-CoA group (three cells) and the Malonyl-CoA group head with one cell, column 'Km (uM)' = 6.2.

raw_value_unit_evidence: Table 2, isoenzyme row 'BIS1', salicoyl-CoA group: kcat = 0.27 min^-1; Km = 0.8 uM; printed kcat/Km = 5,625 M^-1 s^-1.

row_label: Table 2, isoenzyme row 'BIS1', salicoyl-CoA starter-substrate block (the three columns headed kcat (min^-1), Km (uM) and kcat/Km (M^-1 s^-1) under the salicoyl-CoA group head)


organism: Aneurinibacillus thermoaerophilus

column_label: Main text FdtC kinetic paragraph names dTDP-d-Fucp3N first and gives first Km/kcat values respectively.

normalized_value_unit_evidence: Km 0.0667 mM; kcat 2.3 s^-1; kcat/Km 34.48275862068966 s^-1 mM^-1 derived from paper values

table_label: Main text - FdtC Catalyzes the Transfer of an Acetyl Group to dTDP-d-Fucp3N


assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

column_label: Main text FdtC kinetic paragraph names acetyl-CoA second and gives second Km/kcat values respectively.

normalized_value_unit_evidence: Km 0.061 mM; kcat 3.1 s^-1; kcat/Km 50.81967213114754 s^-1 mM^-1 derived from paper values

row_label: acetyl-CoA


enzyme_display_name: tRNA(Met) cytidine acetyltransferase TmcA

organism: Escherichia coli (strain K12)

substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


substrate_name: GTP

enzyme: tRNA(Met) cytidine acetyltransferase TmcA

substrate: GTP


organism: Vitis labrusca

substrate_name: anthraniloyl-CoA

assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA

substrate: anthraniloyl-CoA


substrate_name: methanol

substrate: methanol


smiles: CCCCCCCCCCC(C)O


substrate_name: lauroyl-CoA

substrate: lauroyl-CoA


organism: Escherichia coli

substrate_name: Acetyl-CoA

column_label: Table 3. Kinetic parameters; row VioB O7 / SH-CoA table row resolved by adjacent prose as acetyl-CoA variable-substrate assay; column kcat /s; metric kcat; normalized value 21.6 s^-1 | Table 3. Kinetic parameters and adjacent prose; row VioB O7 / acetyl-CoA variable-substrate assay; column Km (uM); metric km; normalized value 0.554 mM | Table 3. Kinetic parameters; row VioB O7 / acetyl-CoA variable-substrate assay; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 38.98916967509025 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=21.6 normalized_unit=s^-1; km normalized_value=0.554 normalized_unit=mM; kcat_over_km normalized_value=38.98916967509025 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=21.6 raw_unit=s^-1; km raw_value=554 raw_unit=uM; kcat_over_km raw_value=21.6/0.554 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km evidence

substrate: Acetyl-CoA


column_label: Table 3. Kinetic parameters; row VioB O7 / dTDP-D-Qui4N; column kcat /s; metric kcat; normalized value 155.3 s^-1 | Table 3. Kinetic parameters; row VioB O7 / dTDP-D-Qui4N; column Km (uM); metric km; normalized value 0.142 mM | Table 3. Kinetic parameters; row VioB O7 / dTDP-D-Qui4N; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 1093.6619718309862 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=155.3 normalized_unit=s^-1; km normalized_value=0.142 normalized_unit=mM; kcat_over_km normalized_value=1093.6619718309862 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=155.3 raw_unit=s^-1; km raw_value=142 raw_unit=uM; kcat_over_km raw_value=155.3/0.142 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km cells


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


enzyme_display_name: benzalacetone synthase

organism: Rubus idaeus

substrate_name: malonyl-CoA

assay_conditions_summary: pH 9.5; cofactor CoA

proof_lines:
pH 9.5, 35°C
at pH 9.5 and 50°C
pH 8.0, 30°C

enzyme: benzalacetone synthase

substrate: malonyl-CoA


enzyme_display_name: benzyl alcohol O-benzoyltransferase

substrate_name: benzoyl-CoA

assay_conditions_summary: pH 7.5; 295.15 K; buffer 50 mM Tris-HCl pH 7; cofactor CoA

column_label: Table 2, Benzoyl-CoA (with benzyl alcohol) row, native purified protein N columns: Km 11.80 uM; kcat 0.045 s^-1; specificity 3.81. Footnote: N = native purified protein from mature grape; R = recombinant purified protein from E. coli.

normalized_value_unit_evidence: Paper Km 11.80 uM converts to 0.01180 mM; paper kcat is 0.045 s^-1; the printed specificity value is 3.81 s^-1 mM^-1. The export specificity value is 3.8135593220338984 s^-1 mM^-1 and does not exactly equal the printed value.

raw_value_unit_evidence: Table 2 native-protein columns report benzoyl-CoA Km = 11.80 uM, kcat = 0.045 s^-1, and specificity = 3.81 with benzyl alcohol. The footnote defines N as native purified protein from mature grape.

row_label: Benzoyl-CoA (with benzyl alcohol)

table_label: Primary-paper Table 2: Kinetic parameters of AMAT

enzyme: benzyl alcohol O-benzoyltransferase

substrate: benzoyl-CoA


organism: Rheum palmatum

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

column_label: PMID 12724310/JBC Table I, BAS WT row, 4-Coumaroyl-CoA column group: kcat = 1790 +/- 54 x 10^-3 min^-1, Km = 10.0 +/- 2.1 uM, kcat/Km = 2963 s^-1 M^-1.

raw_value_unit_evidence: Table I reports kcat = 1790 +/- 54 x 10^-3 min^-1, Km = 10.0 +/- 2.1 uM, and kcat/Km = 2963 s^-1 M^-1 for BAS WT with 4-coumaroyl-CoA.

row_label: BAS WT / Benzalacetone / pH optimum 8.0 / 4-Coumaroyl-CoA

table_label: JBC 2003 Table I. Steady state kinetic parameters for enzyme reactions


column_label: PMID 12724310 Table I, BAS WT row, Malonyl-CoA column group: kcat = 1780 +/- 59 x 10^-3 min^-1, Km = 23.3 +/- 2.2 uM, kcat/Km = 1273 s^-1 M^-1.

raw_value_unit_evidence: Table I reports kcat = 1780 +/- 59 x 10^-3 min^-1, Km = 23.3 +/- 2.2 uM, and kcat/Km = 1273 s^-1 M^-1 for BAS WT with malonyl-CoA.

row_label: BAS WT / Benzalacetone / pH optimum 8.0 / malonyl-CoA


organism: Pseudomonas fluorescens

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

column_label: PMID 16931521 abstract and Kinetics/Stability prose, PhlD / malonyl-CoA: kcat = 24 +/- 4 min^-1, Km = 13 +/- 1 uM, kcat/Km = 1883 mM^-1 min^-1.

raw_value_unit_evidence: Paper reports kcat = 24 +/- 4 min^-1, Km = 13 +/- 1 uM, and kcat/Km = 1883 mM^-1 min^-1 for PhlD with malonyl-CoA.

row_label: PhlD / malonyl-CoA

table_label: Abstract and Kinetics/Stability prose


organism: Clarkia breweri

assay_conditions_summary: pH 7.7; 295.15 K; cofactor CoA


organism: Streptomyces coelicolor

assay_conditions_summary: pH 7.5; cofactor CoA

column_label: Page 513, Kinetic parameters for THN formation: recombinant wild-type S. coelicolor THNS kcat 0.48 +/- 0.03 min^-1 and Km 3.58 +/- 0.85 uM for malonyl-CoA-to-THN formation.

row_label: wild-type THNS malonyl-CoA measurement

table_label: page 513, Kinetic parameters for THN formation


substrate_name: acetyl-CoA (in the presence of Ni(2+))

substrate: acetyl-CoA (in the presence of Ni(2+))


substrate_name: propionyl-CoA (in the presence of Ni(2+))


substrate_name: malonyl-CoA (in the presence of Ni(2+))

substrate: malonyl-CoA (in the presence of Ni(2+))


substrate_name: aminomethylphosphonate (in the presence of Ni(2+))


substrate_name: 2-aminoethylphosphonate (in the presence of Ni(2+))


substrate_name: (S)-1-aminoethylphosphonate (in the presence of Ni(2+))


substrate_name: 2-aminoethanesulfonate (in the presence of Ni(2+))


substrate_name: 2-aminoethanesulfinate (in the presence of Ni(2+))


km_display: Not reported


enzyme_display_name: chlorogenate caffeoyltransferase

organism: Solanum lycopersicum

substrate_name: chlorogenic acid

enzyme: chlorogenate caffeoyltransferase

substrate: chlorogenic acid


organism: Ipomoea batatas

substrate_name: chlorogenate

substrate: chlorogenate


enzyme_display_name: 2-amino-4-oxopentanoate thiolase

organism: Pelosinus propionicus

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

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

enzyme: 2-amino-4-oxopentanoate thiolase


organism: Paraburkholderia graminis (strain ATCC 700544 / DSM 17151 / LMG 18924 / NCIMB 13744 / C4D1M)

substrate_name: acetyl-CoA

column_label: Official Nature Chemical Biology Supplementary Information PDF, Supplementary Table 6a, row BKACE_274 / acetylCoA, column KM (uM), raw value 252 +/- 37.

normalized_value_unit_evidence: 252 uM acetylCoA = 0.252 mM, matching exported Km 0.252 mM.

raw_value_unit_evidence: Supplementary Table 6a reports BKACE_274 acetylCoA KM (uM) = 252 +/- 37.

row_label: BKACE_274 (BKACE G1), acetylCoA, footnote q

table_label: Supplementary Table 6a: Enzymatic kinetics assays

substrate: acetyl-CoA


enzyme_display_name: 2-amino-4-ketopentanoate thiolase alpha subunit

organism: Unknown prokaryotic organism

substrate_name: CoA

column_label: Table 1 row AKPT / CoA-SH column Km

row_label: AKPT / CoA-SH

substrate: CoA


substrate_name: AKP

column_label: Table 1 row AKPT / AKP column Km

row_label: AKPT / AKP

enzyme: 2-amino-4-ketopentanoate thiolase alpha subunit

substrate: AKP


enzyme_display_name: 2-amino-4-ketopentanoate thiolase beta subunit


enzyme: 2-amino-4-ketopentanoate thiolase beta subunit


organism: Taxus sp.

proof_lines: with 3'-N-debenzoyltaxol as cosubstrate, at pH 7.5 and 31°C

proof_lines: with N-debenzoyl-2'-deoxytaxol as cosubstrate, at pH 7.5 and 31°C


organism: Taxus cuspidata

substrate_name: baccatin III

proof_lines: pH and temperature not specified in the publication

substrate: baccatin III


organism: Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)

substrate_name: beta-ketoglutarate

column_label: Official Nature Chemical Biology Supplementary Information PDF, Supplementary Table 6a, row BKACE_378 / beta-ketoglutarate, column KM (uM), raw value 1350 +/- 470.

normalized_value_unit_evidence: 1350 uM beta-ketoglutarate = 1.35 mM, matching exported Km 1.35 mM.

raw_value_unit_evidence: Supplementary Table 6a reports BKACE_378 beta-ketoglutarate KM (uM) = 1350 +/- 470.

row_label: BKACE_378 (BKACE G4), beta-ketoglutarate, footnote h

substrate: beta-ketoglutarate


substrate_name: beta-ketohexanoate

proof_lines: kcat is 0.97 sec(-1) with acetyl-CoA as substrate. kcat is 0.03 sec(-1) with beta-keto-5-aminohexanoate as substrate.

substrate: beta-ketohexanoate


organism: Pseudomonas aeruginosa

substrate_name: Malonyl-CoA; Anthraniloyl-CoA

substrate: Malonyl-CoA; Anthraniloyl-CoA


enzyme_display_name: ethanol O-acetyltransferase

organism: Wickerhamomyces anomalus

substrate_name: Ethanol; Acetyl-CoA

enzyme: ethanol O-acetyltransferase

substrate: Ethanol; Acetyl-CoA


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: 1-aminobutyl phosphonic acid

smiles: CCCC(N)P(=O)(O)O

column_label: Table 1 part B; row 1-aminobutyl phosphonic acid; column Km (mM) raw value 12.5; column kcat (s^-1) raw value 1; column kcat/Km (M^-1 s^-1) raw value (8.0 +/- 0.5) x 10^1

normalized_value_unit_evidence: kcat normalized_value=1 normalized_unit=s^-1; Km normalized_value=12.5 normalized_unit=mM; kcat/Km normalized_value=0.08 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1 raw_unit=s^-1; Km raw_value=12.5 raw_unit=mM; kcat/Km raw_value=(8.0 +/- 0.5) x 10^1 raw_unit=M^-1*s^-1

row_label: 1-aminobutyl phosphonic acid / PhnO Table 1 part B

table_label: Table 1. Kinetic parameters for PhnO with various acyl-CoAs and aminoalkylphosphonates

substrate: 1-aminobutyl phosphonic acid


substrate_name: 1-aminopropyl phosphonic acid

smiles: CCC(N)P(=O)(O)O

column_label: Table 1 part B; row 1-aminopropyl phosphonic acid; column Km (mM) raw value 4.1; column kcat (s^-1) raw value 7.4; column kcat/Km (M^-1 s^-1) raw value (1.8 +/- 0.1) x 10^3

normalized_value_unit_evidence: kcat normalized_value=7.4 normalized_unit=s^-1; Km normalized_value=4.1 normalized_unit=mM; kcat/Km normalized_value=1.8 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=7.4 raw_unit=s^-1; Km raw_value=4.1 raw_unit=mM; kcat/Km raw_value=(1.8 +/- 0.1) x 10^3 raw_unit=M^-1*s^-1

row_label: 1-aminopropyl phosphonic acid / PhnO Table 1 part B

substrate: 1-aminopropyl phosphonic acid


substrate_name: 2-aminoethanesulfinic acid

smiles: NCCS(=O)O

column_label: Table 1 part B; row 2-aminoethanesulfinic acid; column Km (mM) raw value 16.4; column kcat (s^-1) raw value 20; column kcat/Km (M^-1 s^-1) raw value (1.2 +/- 0.1) x 10^3

normalized_value_unit_evidence: kcat normalized_value=20 normalized_unit=s^-1; Km normalized_value=16.4 normalized_unit=mM; kcat/Km normalized_value=1.2 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=20 raw_unit=s^-1; Km raw_value=16.4 raw_unit=mM; kcat/Km raw_value=(1.2 +/- 0.1) x 10^3 raw_unit=M^-1*s^-1

row_label: 2-aminoethanesulfinic acid / PhnO Table 1 part B

substrate: 2-aminoethanesulfinic acid


substrate_name: 2-aminoethanesulfonic acid

column_label: Table 1 part B; row 2-aminoethanesulfonic acid; column Km (mM) raw value 18.9; column kcat (s^-1) raw value 14.8; column kcat/Km (M^-1 s^-1) raw value (7.8 +/- 0.3) x 10^2

normalized_value_unit_evidence: kcat normalized_value=14.8 normalized_unit=s^-1; Km normalized_value=18.9 normalized_unit=mM; kcat/Km normalized_value=0.78 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=14.8 raw_unit=s^-1; Km raw_value=18.9 raw_unit=mM; kcat/Km raw_value=(7.8 +/- 0.3) x 10^2 raw_unit=M^-1*s^-1

row_label: 2-aminoethanesulfonic acid / PhnO Table 1 part B

substrate: 2-aminoethanesulfonic acid


substrate_name: 2-aminoethyl phosphonic acid

smiles: NCCP(=O)(O)O

column_label: Table 1. Kinetic parameters for PhnO with various acyl-CoAs and aminoalkylphosphonates; substrate row 2-Aminoethyl phosphonic acid; columns kcat (s^-1), Km (mM), kcat/Km (M^-1 s^-1); cells 9.0 +/- 0.2 s^-1; 1.8 +/- 0.1 mM; (5.0 +/- 0.2) x 10^3 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=9.0 normalized_unit=s^-1; Km normalized_value=1.8 normalized_unit=mM; kcat/Km normalized_value=5.0 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=5.0 s^-1*mM^-1

row_label: PhnO / 2-Aminoethyl phosphonic acid

substrate: 2-aminoethyl phosphonic acid


substrate_name: 3-aminopropyl phosphonic acid

smiles: NCCCP(=O)(O)O

column_label: Table 1 part B; row 3-aminopropyl phosphonic acid; column Km (mM) raw value 4.0; column kcat (s^-1) raw value 5.4; column kcat/Km (M^-1 s^-1) raw value (1.4 +/- 0.1) x 10^3

normalized_value_unit_evidence: kcat normalized_value=5.4 normalized_unit=s^-1; Km normalized_value=4.0 normalized_unit=mM; kcat/Km normalized_value=1.4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=5.4 raw_unit=s^-1; Km raw_value=4.0 raw_unit=mM; kcat/Km raw_value=(1.4 +/- 0.1) x 10^3 raw_unit=M^-1*s^-1

row_label: 3-aminopropyl phosphonic acid / PhnO Table 1 part B

substrate: 3-aminopropyl phosphonic acid


substrate_name: 4-aminobutylphosphonic acid

smiles: NCCCCP(=O)(O)O

column_label: Table 1 part B; row 4-aminobutylphosphonic acid; column Km (mM) raw value 13.0; column kcat (s^-1) raw value 0.5; column kcat/Km (M^-1 s^-1) raw value (3.8 +/- 0.4) x 10^1

normalized_value_unit_evidence: kcat normalized_value=0.5 normalized_unit=s^-1; Km normalized_value=13.0 normalized_unit=mM; kcat/Km normalized_value=0.038 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.5 raw_unit=s^-1; Km raw_value=13.0 raw_unit=mM; kcat/Km raw_value=(3.8 +/- 0.4) x 10^1 raw_unit=M^-1*s^-1

row_label: 4-aminobutylphosphonic acid / PhnO Table 1 part B

substrate: 4-aminobutylphosphonic acid


column_label: Table 1. Kinetic parameters for PhnO with various acyl-CoAs and aminoalkylphosphonates; substrate row Acetyl-CoA; columns kcat (s^-1), Km (mM), kcat/Km (M^-1 s^-1); cells 13.1 +/- 0.1 s^-1; 0.06 +/- 0.01 mM; (2.2 +/- 0.3) x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=13.1 normalized_unit=s^-1; Km normalized_value=0.06 normalized_unit=mM; kcat/Km normalized_value=218.33333333333334 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=220.0 s^-1*mM^-1

row_label: PhnO / Acetyl-CoA


substrate_name: (aminomethyl)phosphonate

column_label: Table 1 part B; row (aminomethyl)phosphonate; column Km (mM) raw value 1.7; column kcat (s^-1) raw value 7.0; column kcat/Km (M^-1 s^-1) raw value (4.1 +/- 0.2) x 10^3

normalized_value_unit_evidence: kcat normalized_value=7.0 normalized_unit=s^-1; Km normalized_value=1.7 normalized_unit=mM; kcat/Km normalized_value=4.1 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=7.0 raw_unit=s^-1; Km raw_value=1.7 raw_unit=mM; kcat/Km raw_value=(4.1 +/- 0.2) x 10^3 raw_unit=M^-1*s^-1

row_label: (aminomethyl)phosphonate / PhnO Table 1 part B

substrate: (aminomethyl)phosphonate


substrate_name: malonyl-CoA

column_label: Table 1 part A; row malonyl-CoA; column Km (mM) raw value 0.05; column kcat (s^-1) raw value 0.4; column kcat/Km (M^-1 s^-1) raw value (8.0 +/- 0.6) x 10^3

normalized_value_unit_evidence: kcat normalized_value=0.4 normalized_unit=s^-1; Km normalized_value=0.05 normalized_unit=mM; kcat/Km normalized_value=8 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.4 raw_unit=s^-1; Km raw_value=0.05 raw_unit=mM; kcat/Km raw_value=(8.0 +/- 0.6) x 10^3 raw_unit=M^-1*s^-1

row_label: malonyl-CoA / PhnO Table 1 part A

substrate: malonyl-CoA


enzyme_display_name: gamma-glutamyltransferase

organism: Penicillium roqueforti

substrate_name: glycylglycine

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

enzyme: gamma-glutamyltransferase

substrate: glycylglycine


enzyme_display_name: UniProt A9YTT0

organism: Bacillus licheniformis

enzyme: UniProt A9YTT0


substrate_name: acetyl-CoA

proof_lines: kcat is 4.70 sec(-1) with acetyl-CoA as substrate. kcat is 4.70 sec(-1) with 3-oxoadipate as substrate. kcat is 1.15 sec(-1) with beta-ketoglutarate as substrate. kcat is 0.20 sec(-1) with beta-ketohexanoate as substrate.

substrate: acetyl-CoA


substrate_name: propionyl-CoA

column_label: Table 1. Kinetic parameters for PhnO with various acyl-CoAs and aminoalkylphosphonates; substrate row Propionyl-CoA; columns kcat (s^-1), Km (mM), kcat/Km (M^-1 s^-1); cells 14.7 +/- 0.7 s^-1; 0.07 +/- 0.01 mM; (2.1 +/- 0.3) x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=14.7 normalized_unit=s^-1; Km normalized_value=0.07 normalized_unit=mM; kcat/Km normalized_value=209.99999999999997 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=210.0 s^-1*mM^-1

row_label: PhnO / Propionyl-CoA

substrate: propionyl-CoA


substrate_name: (S)-1-aminoethylphosphonic acid

column_label: Table 1 part B; row (S)-1-aminoethylphosphonic acid; column Km (mM) raw value 0.17; column kcat (s^-1) raw value 13.3; column kcat/Km (M^-1 s^-1) raw value (7.8 +/- 0.4) x 10^4

normalized_value_unit_evidence: kcat normalized_value=13.3 normalized_unit=s^-1; Km normalized_value=0.17 normalized_unit=mM; kcat/Km normalized_value=78 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=13.3 raw_unit=s^-1; Km raw_value=0.17 raw_unit=mM; kcat/Km raw_value=(7.8 +/- 0.4) x 10^4 raw_unit=M^-1*s^-1

row_label: (S)-1-aminoethylphosphonic acid / PhnO Table 1 part B

substrate: (S)-1-aminoethylphosphonic acid


substrate_name: ethanol

smiles: CCO

substrate: ethanol


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

substrate_name: anthraniloyl-CoA

substrate: anthraniloyl-CoA


enzyme_display_name: aminoglycoside 6'-N-acetyltransferase

organism: Acinetobacter haemolyticus

substrate_name: gentamicin

proof_lines: S 0.5 value, Hill coefficient 2.05, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 2.05, pH 8.0, 37°C

enzyme: aminoglycoside 6'-N-acetyltransferase

substrate: gentamicin


substrate_name: neomycin C

proof_lines: kcat/S 0.5 value, Hill coefficient 1.43, pH 8.0, 37°C

substrate: neomycin C


substrate_name: ribostamycin

proof_lines: kcat/S 0.5 value, Hill coefficient 1.96, pH 8.0, 37°C

substrate: ribostamycin


substrate_name: arbekacin

proof_lines: S 0.5 value, Hill coefficient 2.19, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 2.19, pH 8.0, 37°C

substrate: arbekacin


substrate_name: tobramicin

proof_lines: S 0.5 value, Hill coefficient 1.21, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 1.21, pH 8.0, 37°C

substrate: tobramicin


proof_lines: S 0.5 value, Hill coefficient 2.28, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 2.28, pH 8.0, 37°C


substrate_name: butirosin A

proof_lines: S 0.5 value, Hill coefficient 1.77, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 1.77, pH 8.0, 37°C

substrate: butirosin A


substrate_name: dibekacin

proof_lines: S 0.5 value, Hill coefficient 1.26, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 1.26, pH 8.0, 37°C

substrate: dibekacin


substrate_name: sisomicin

proof_lines: S 0.5 value, Hill coefficient 2.04, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 2.04, pH 8.0, 37°C

substrate: sisomicin


substrate_name: kanamycin B

proof_lines: S 0.5 value, Hill coefficient 1.93, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 1.93, pH 8.0, 37°C

substrate: kanamycin B


substrate_name: amikacin

proof_lines: kcat/S 0.5 value, Hill coefficient 1.55, pH 8.0, 37°C

substrate: amikacin


substrate_name: isepamicin

proof_lines: S 0.5 value, Hill coefficient 1.45, pH 8.0, 37°C

proof_lines: kcat/S 0.5 valuevalue, Hill coefficient 1.45, pH 8.0, 37°C

substrate: isepamicin


enzyme_display_name: aminoglycoside 3-N-acetyltransferase

organism: Escherichia coli

substrate_name: butyryl-CoA

proof_lines: in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C

enzyme: aminoglycoside 3-N-acetyltransferase

substrate: butyryl-CoA


substrate_name: butirosin

substrate: butirosin


substrate_name: malonyl-CoA

substrate: malonyl-CoA


substrate_name: paromomycin

substrate: paromomycin


substrate_name: netilmicin

substrate: netilmicin


substrate_name: propionyl-CoA

substrate: propionyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: apramycin

substrate: apramycin


substrate_name: ribostamycin

substrate: ribostamycin


organism: Stenotrophomonas maltophilia

substrate_name: kanamycin

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

substrate: kanamycin


substrate_name: tobramycin

substrate: tobramycin


substrate_name: neomycin

substrate: neomycin


substrate_name: arbekacin

substrate: arbekacin


proof_lines:
reaction with AAC (6')-Ib' domain
reaction with AAC (6?)-Ib' domain


substrate_name: dibekacin

substrate: dibekacin


substrate_name: gentamicin

substrate: gentamicin


substrate_name: kanamycin A

assay_conditions_summary: pH 6

proof_lines:
reaction with AAC (6')-Ib' domain
pH 6.0
reaction with AAC (6?)-Ib' domain

substrate: kanamycin A


substrate_name: amikacin

substrate: amikacin


substrate_name: Unknown

ki_unit: mM

proof_lines:
versus kanamycin A, K(is)
versus kanamycin A. K(is)
versus acetyl-CoA, K(is)

substrate: Unknown


organism: Homo sapiens

substrate_name: myristoyl-CoA

substrate: myristoyl-CoA


proof_lines:
wild-type, pH 8.0, 30°C
wild-type, pH 7.5, 25°C


enzyme_display_name: 6-deoxyerythronolide-B synthase

organism: Saccharopolyspora erythraea

substrate_name: propanoyl-CoA

assay_conditions_summary: pH 7.2; cofactor CoA

proof_lines: mutant H384A, pH 7.2, temperature not specified in the publication

enzyme: 6-deoxyerythronolide-B synthase

substrate: propanoyl-CoA


proof_lines: mutant Q386E, pH 7.2, temperature not specified in the publication


proof_lines: mutant H457A, pH 7.2, temperature not specified in the publication


proof_lines: mutant N455L, pH 7.2, temperature not specified in the publication


proof_lines: mutant N381A, pH 7.2, temperature not specified in the publication


proof_lines: wild-type, pH 7.2, temperature not specified in the publication


proof_lines: mutant T209A, pH 7.2, temperature not specified in the publication


assay_conditions_summary: pH 6.6; 298.15 K; cofactor CoA

proof_lines: pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET28a

proof_lines: pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET28a

proof_lines: pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector Int-pET19b-pps


proof_lines: pH 6.6, with malonyl-CoA, His-tagged enzyme expressed from vector pET22b

proof_lines: pH 6.6, with n-propionyl-CoA, His-tagged enzyme expressed from vector pET22b

proof_lines: pH 6.6, with acetyl-CoA, His-tagged enzyme expressed from vector pET22b


substrate_name: neomycin B

proof_lines: in 50 mM HEPES, pH 7.5 and 0.1 mM 4,4'-dithiodipyridine, at pH 7.8 and 25°C

substrate: neomycin B


substrate_name: sisomicin

substrate: sisomicin


enzyme_display_name: N6-hydroxylysine N-acetyltransferase

substrate_name: N-Methylhydroxylamine

smiles: CNO

enzyme: N6-hydroxylysine N-acetyltransferase

substrate: N-Methylhydroxylamine


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


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


substrate_name: hydroxylamine

smiles: NO

substrate: hydroxylamine


substrate_name: acetyl-CoA

proof_lines:
+ L-N6-hydroxylysine
+ L-N5-hydroxyornithine
+ 1-amino-5-(hydroxyamino)pentane

substrate: acetyl-CoA


substrate_name: ribostamycin

substrate: ribostamycin


substrate_name: paromomycin

substrate: paromomycin


substrate_name: lividomycin A

substrate: lividomycin A


substrate_name: tobramycin

substrate: tobramycin


substrate_name: kanamycin B

substrate: kanamycin B


organism: Serratia marcescens

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


substrate_name: neomycin

substrate: neomycin


substrate_name: arbekacin

substrate: arbekacin


substrate_name: isepamicin

substrate: isepamicin


substrate_name: dibekacin

substrate: dibekacin


substrate_name: amikacin

substrate: amikacin


substrate_name: netilmicin

substrate: netilmicin


substrate_name: gentamicin

proof_lines:
pH 7.5
full length enzyme, pH 7.5, 25°C
isolated AAC(6') domain, pH 7.5, 25°C

substrate: gentamicin


substrate_name: kanamycin A

proof_lines:
pH 7.5
isolated AAC(6') domain, pH 7.5, 25°C
full length enzyme, pH 7.5, 25°C

substrate: kanamycin A


substrate_name: Unknown

proof_lines:
versus acetyl-CoA, K(is)
versus kanamycin A, K(is)
versus acetyl-CoA, K(ii)

substrate: Unknown


organism: Enterobacter cloacae

substrate_name: gentamicin C1

substrate: gentamicin C1


substrate_name: gentamicin C2

substrate: gentamicin C2


substrate_name: sisomicin

substrate: sisomicin


organism: Aeromonas hydrophila


substrate_name: ribostamycin

substrate: ribostamycin


substrate_name: kanamycin

substrate: kanamycin


enzyme_display_name: UniProt Q16769

substrate_name: Gln-Gln

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

assay_conditions_summary: pH 7

proof_lines:
Raw SKiD Env: Temp=-----, pH=7
Raw SKiD Env: Temp=-----, pH=8
Raw SKiD Env: Temp=-----, pH=7.5

enzyme: UniProt Q16769

substrate: Gln-Gln


enzyme_display_name: UniProt Q9CYK2

organism: Mus musculus

substrate_name: L-Gln-L-Ala

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

enzyme: UniProt Q9CYK2

substrate: L-Gln-L-Ala


substrate_name: L-Gln-L-Glu

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

substrate: L-Gln-L-Glu


substrate_name: L-Gln-Gly

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

substrate: L-Gln-Gly


substrate_name: L-Gln-L-Gln

substrate: L-Gln-L-Gln


organism: uncultured bacterium

proof_lines: K 0.5 value, Hill coefficient 0.62, pH 7.5, 25°C


substrate_name: gentamycin

proof_lines: K 0.5 value, Hill coefficient 3.14, pH 7.5, 25°C

substrate: gentamycin


substrate_name: tobramycin

proof_lines: K 0.5 value, Hill coefficient 2.3, pH 7.5, 25°C

substrate: tobramycin


substrate_name: acetyl-CoA

proof_lines: K 0.5 value, Hill coefficient 1.77, pH 7.5, 25°C

substrate: acetyl-CoA


proof_lines: K 0.5 value, Hill coefficient 4.39, pH 7.5, 25°C


enzyme_display_name: maltose O-acetyltransferase

assay_conditions_summary: pH 5; 323.15 K; cofactor CoA

enzyme: maltose O-acetyltransferase


substrate_name: triethanolamine

smiles: C(CO)N(CCO)CCO

substrate: triethanolamine


substrate_name: D-glucose

substrate: D-glucose


substrate_name: maltose

substrate: maltose


organism: Mycobacterium tuberculosis

substrate_name: palmitoyl-CoA

assay_conditions_summary: pH 6.8; 301.15 K; cofactor CoA

proof_lines: cosubstrate n-octanol, mutant F331H, pH 6.8, 28°C

substrate: palmitoyl-CoA


proof_lines: cosubstrate n-octanol, mutant F331Y, pH 6.8, 28°C


proof_lines: cosubstrate n-octanol, wild-type, pH 6.8, 28°C


proof_lines: cosubstrate n-octanol, mutant F331W, pH 6.8, 28°C


enzyme_display_name: 6-methylsalicylic-acid synthase

organism: Penicillium griseofulvum

substrate_name: malonyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: 6-methylsalicylic-acid synthase

substrate: malonyl-CoA


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


organism: Enterococcus sp.


substrate_name: neamine

substrate: neamine


substrate_name: kanamycin A

substrate: kanamycin A


substrate_name: UDP-N-acetylglucosamine

substrate: UDP-N-acetylglucosamine


substrate_name: diacerein

proof_lines:
transesterification, pH 5, 50°C
acetyl-CoA synthesis, pH 5, 50°C
hydrolysis of diacerein, pH 5, 50°C

substrate: diacerein


substrate_name: puerarin

proof_lines:
acetylation of puerarin, pH 5, 50°C
transesterification, pH 5, 50°C

substrate: puerarin


substrate_name: CoA

substrate: CoA


organism: Pseudomonas aeruginosa

substrate_name: gentamicin

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D170F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; cofactor CoA

column_label: Table 3; row D170F; columns kcat (s^-1), kcat/Km (s^-1 uM^-1), Km (uM).

normalized_value_unit_evidence: Normalized paper values: kcat=3.4 s^-1; kcat/Km=720 s^-1 mM^-1; Km=0.0047 mM. Export values: Km=0.0047 mM; kcat=3.4 s^-1; kcat/Km=723.404 s^-1 mM^-1.

table_label: Table 3

substrate: gentamicin


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D72W to reconstruct the assayed variant sequence.

column_label: Table 3; row D72W; columns kcat (s^-1), kcat/Km (s^-1 uM^-1), Km (uM).

normalized_value_unit_evidence: Normalized paper values: kcat=3.59 s^-1; kcat/Km=190 s^-1 mM^-1; Km=0.019 mM. Export values: Km=0.019 mM; kcat=3.59 s^-1; kcat/Km=188.947 s^-1 mM^-1.


substrate_name: kanamycin

column_label: Table 4. Kinetic parameters for antibiotics; row Kanamycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: kcat paper=4.45 s^-1; km paper=0.007 mM; kcat_over_km paper=630.0 s^-1 mM^-1

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Kanamycin: kcat 4.45 s^-1; Km 7 uM (0.007 mM); kcat/Km 0.63 s^-1 uM^-1 (630.0 s^-1 mM^-1).

row_label: Kanamycin

substrate: kanamycin


substrate_name: ribostamycin

column_label: Table 4. Kinetic parameters for antibiotics; row Ribostamycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: kcat paper=5.38 s^-1; km paper=0.0079 mM; kcat_over_km paper=680.0 s^-1 mM^-1

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Ribostamycin: kcat 5.38 s^-1; Km 7.9 uM (0.0079 mM); kcat/Km 0.68 s^-1 uM^-1 (680.0 s^-1 mM^-1).

row_label: Ribostamycin

substrate: ribostamycin


substrate_name: paromomycin

column_label: Table 4. Kinetic parameters for antibiotics; row Paromomycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: kcat paper=5.52 s^-1; km paper=0.0067 mM; kcat_over_km paper=820.0 s^-1 mM^-1

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Paromomycin: kcat 5.52 s^-1; Km 6.7 uM (0.0067 mM); kcat/Km 0.82 s^-1 uM^-1 (820.0 s^-1 mM^-1).

row_label: Paromomycin

substrate: paromomycin


substrate_name: tobramycin

column_label: Table 4. Kinetic parameters for antibiotics; row Tobramycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: kcat paper=5.68 s^-1; km paper=0.0066 mM; kcat_over_km paper=860.0 s^-1 mM^-1

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Tobramycin: kcat 5.68 s^-1; Km 6.6 uM (0.0066 mM); kcat/Km 0.86 s^-1 uM^-1 (860.0 s^-1 mM^-1).

row_label: Tobramycin

substrate: tobramycin


column_label: Table 3. Enzymatic assay results between AAC(3)-IIIa mutants and gentamicin; row WT; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: kcat paper=6.12 s^-1; km paper=0.0071 mM; kcat_over_km paper=860.0 s^-1 mM^-1

raw_value_unit_evidence: Table 3. Enzymatic assay results between AAC(3)-IIIa mutants and gentamicin, row WT: kcat 6.12 s^-1; Km 7.1 uM (0.0071 mM); kcat/Km 0.86 s^-1 uM^-1 (860.0 s^-1 mM^-1).

row_label: WT


substrate_name: neomicin

assay_conditions_summary: pH 6.5; 295.15 K; cofactor CoA

column_label: Table 4. Kinetic parameters for antibiotics; row Neomicin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: kcat paper=6.15 s^-1; km paper=0.0066 mM

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Neomicin: kcat 6.15 s^-1; Km 6.6 uM (0.0066 mM); kcat/Km 0.93 s^-1 uM^-1 (930.0 s^-1 mM^-1).

row_label: Neomicin

substrate: neomicin


substrate_name: sisomicin

column_label: Table 4. Kinetic parameters for antibiotics; row Sisomicin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: kcat paper=10.48 s^-1; km paper=0.0109 mM; kcat_over_km paper=970.0 s^-1 mM^-1

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Sisomicin: kcat 10.48 s^-1; Km 10.9 uM (0.0109 mM); kcat/Km 0.97 s^-1 uM^-1 (970.0 s^-1 mM^-1).

row_label: Sisomicin

substrate: sisomicin


substrate_name: myristoyl-CoA

mutation_signature: N-terminal truncation mutant

mutation_type: truncation

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines: N-terminal truncation mutant, pH 7.5, 25°C

substrate: myristoyl-CoA


substrate_name: HIV-1 negative regulatory factor

substrate: HIV-1 negative regulatory factor


smiles: CCCCCCCCO


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


substrate_name: 2 palmitoyl-CoA

assay_conditions_summary: pH 6.5; 310.15 K; cofactor CoA

substrate: 2 palmitoyl-CoA


substrate_name: malonyl-CoA

assay_conditions_summary: pH 7.6; 298.15 K; cofactor CoA

substrate: malonyl-CoA


substrate_name: n-propionyl-CoA

substrate: n-propionyl-CoA


substrate_name: acetyl-CoA

proof_lines:
cosubstrate neomycin B, pH 7.6, 25°C
cosubstrate kanamycin A, pH 7.6, 25°C

substrate: acetyl-CoA


enzyme_display_name: arginine N-succinyltransferase

substrate_name: L-ornithine

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

enzyme: arginine N-succinyltransferase

substrate: L-ornithine


substrate_name: L-arginine

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

substrate: L-arginine


substrate_name: Unknown

substrate: Unknown


organism: Arabidopsis thaliana

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA


organism: Archaeoglobus fulgidus


substrate_name: formylmethanofuran

substrate: formylmethanofuran


enzyme_display_name: trihydroxystilbene synthase

organism: Arachis hypogaea

proof_lines: malonyl-CoA decarboxylation, P375G mutant enzyme

enzyme: trihydroxystilbene synthase


substrate_name: p-Coumaroyl-CoA

substrate: p-Coumaroyl-CoA


organism: Streptomyces mobaraensis

substrate_name: hydroxylamine

substrate: hydroxylamine


substrate_name: N-CBZ-Glu-Gly

substrate: N-CBZ-Glu-Gly


organism: Solanum lycopersicum

substrate_name: glutathione

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

substrate: glutathione


organism: Saccharomyces cerevisiae

proof_lines:
wild-type, 37°C
His-tagged wild-type, 37°C


organism: Bos taurus


substrate_name: p60src-derived peptide

substrate: p60src-derived peptide


organism: Escherichia coli

substrate_name: tobramycin

substrate: tobramycin


substrate_name: amikacin

substrate: amikacin


enzyme_display_name: citrate (Si)-synthase

organism: Nitrobacter winogradskyi

substrate_name: oxaloacetate

enzyme: citrate (Si)-synthase

substrate: oxaloacetate


proof_lines: peptide 920 disrupts LpxA interactions with the R-3-hydroxymyristoyl-ACP substrate


substrate_name: UDP-N-acetylglucosamine

substrate: UDP-N-acetylglucosamine


organism: Burkholderia cepacia

substrate_name: succinyl-CoA

substrate: succinyl-CoA


enzyme_display_name: acridone synthase

organism: Citrus x microcarpa

substrate_name: N-methylanthraniloyl-CoA

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: product 1,3-dihydroxy-N-methylacridone, pH 7.0, 30°C

proof_lines: product 4-hydroxy-N-methylquinolone, pH 7.0, 30°C

enzyme: acridone synthase

substrate: N-methylanthraniloyl-CoA


column_label: Table 1 columns Km, kcat, and kcat/Km for row C. microcarpa ACS under 4-Coumaroyl-CoA with product Naringenin.

normalized_value_unit_evidence: Km normalized_value=0.0136 normalized_unit=mM; kcat normalized_value=0.113 normalized_unit=s^-1; kcat/Km explicit_table_normalized_value=8.333 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=13.6 +/- 3.1 raw_unit=uM; kcat raw_value=6.8 +/- 2.2 raw_unit=min^-1; kcat/Km raw_value=500 raw_unit=min^-1 mM^-1

row_label: 4-Coumaroyl-CoA / C. microcarpa ACS / Product Naringenin

table_label: Table 1. Steady-state kinetic parameters of C. microcarpa QNS and ACS


enzyme_display_name: decylcitrate synthase

organism: Talaromyces trachyspermus

substrate_name: lauroyl-CoA

enzyme: decylcitrate synthase

substrate: lauroyl-CoA


enzyme_display_name: decylhomocitrate synthase

enzyme: decylhomocitrate synthase


organism: Yarrowia lipolytica


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: Oxaloacetate; Acetyl-CoA; H2O

substrate: Oxaloacetate; Acetyl-CoA; H2O


enzyme_display_name: citrate (Re)-synthase

organism: Clostridium acidi-urici

substrate_name: (R)-citryl-CoA

enzyme: citrate (Re)-synthase

substrate: (R)-citryl-CoA


substrate_name: (R)-malyl-CoA

substrate: (R)-malyl-CoA


organism: Cyanidioschyzon merolae

assay_conditions_summary: pH 6.5; 321.15 K; cofactor CoA

proof_lines: without any effector, at pH 6.5 and 48°C

proof_lines: in the presence of 5 mM MgCl2, at pH 7.8 and 48°C

proof_lines: without any effector, at pH 7.8 and 48°C


enzyme_display_name: 2-methylcitrate synthase

enzyme: 2-methylcitrate synthase


substrate_name: propionyl-CoA

substrate: propionyl-CoA


substrate_name: butyryl-CoA

substrate: butyryl-CoA


substrate_name: valeryl-CoA

substrate: valeryl-CoA


enzyme_display_name: UniProt Q50I20

organism: Aspergillus fumigatus

substrate_name: CoA

enzyme: UniProt Q50I20

substrate: CoA


substrate_name: H2O; Acetyl-CoA; Oxaloacetate

substrate: H2O; Acetyl-CoA; Oxaloacetate


substrate_name: H2O; Oxaloacetate; Acetyl-CoA

substrate: H2O; Oxaloacetate; Acetyl-CoA


organism: Gallus gallus

substrate_name: Acetyl-CoA; H2O; Oxaloacetate

substrate: Acetyl-CoA; H2O; Oxaloacetate


organism: Rattus norvegicus


substrate_name: Acetyl-CoA; Oxaloacetate; H2O

substrate: Acetyl-CoA; Oxaloacetate; H2O


organism: Sus scrofa

substrate_name: oxaloacetate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H320G with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

substrate: oxaloacetate


substrate_name: Acetyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H264A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; 293.15 K; cofactor CoA

substrate: Acetyl-CoA


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +5, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D362A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F383A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


enzyme_display_name: ATP citrate synthase

assay_conditions_summary: cofactor ATP

enzyme: ATP citrate synthase


substrate_name: ATP

substrate: ATP


substrate_name: citrate

substrate: citrate


substrate_name: N6-etheno-adenosine triphosphate

substrate: N6-etheno-adenosine triphosphate


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

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

column_label: Archives Biochem Biophys 2007 PMID 17570335 Table 1 row Cit1p / Acetyl-CoA reports Km 76 +/- 7 uM, kcat 11.2 +/- 0.4 s^-1, and kcat/Km 150 +/- 10 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.076 mM; kcat normalized_value=11.2 s^-1; kcat/Km normalized_value=150 s^-1*mM^-1; current row stores 147.36842105263156 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=76 +/- 7 raw_unit=uM; kcat raw_value=11.2 +/- 0.4 raw_unit=s^-1; kcat/Km raw_value=150 +/- 10 raw_unit=10^3 M^-1 s^-1

row_label: Cit1p / Acetyl-CoA

table_label: Table 1


column_label: Archives Biochem Biophys 2007 PMID 17570335 Table 1 row Cit3p / Acetyl-CoA reports Km 1200 +/- 200 uM, kcat 11 +/- 1 s^-1, and kcat/Km 9 +/- 2 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=1.2 mM; kcat normalized_value=11 s^-1; kcat/Km normalized_value=9 s^-1*mM^-1; current row stores 9.166666666666668 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=1200 +/- 200 raw_unit=uM; kcat raw_value=11 +/- 1 raw_unit=s^-1; kcat/Km raw_value=9 +/- 2 raw_unit=10^3 M^-1 s^-1

row_label: Cit3p / Acetyl-CoA


substrate_name: Propanoyl-CoA

column_label: Archives Biochem Biophys 2007 PMID 17570335 Table 1 row Cit3p / Propionyl-CoA reports Km 520 +/- 90 uM, kcat 5.4 +/- 0.5 s^-1, and kcat/Km 10 +/- 2 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.52 mM; kcat normalized_value=5.4 s^-1; kcat/Km normalized_value=10 s^-1*mM^-1; current row stores 10.384615384615385 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=520 +/- 90 raw_unit=uM; kcat raw_value=5.4 +/- 0.5 raw_unit=s^-1; kcat/Km raw_value=10 +/- 2 raw_unit=10^3 M^-1 s^-1

row_label: Cit3p / Propionyl-CoA

substrate: Propanoyl-CoA


organism: Eimeria tenella

substrate_name: propanoyl-CoA

substrate: propanoyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


enzyme_display_name: malate synthase

organism: Fomitopsis palustris

substrate_name: Glyoxylate; H2O; Acetyl-CoA

enzyme: malate synthase

substrate: Glyoxylate; H2O; Acetyl-CoA


substrate_name: glyoxalate

substrate: glyoxalate


organism: Teladorsagia circumcincta


organism: Thermus thermophilus


organism: Clostridium kluyveri

assay_conditions_summary: pH 8; cofactor CoA

column_label: Official PMC full text PMID 17400742, Determination of citrate synthase activity and Results prose for purified IPMS2/Re-citrate synthase

raw_value_unit_evidence: oxaloacetate apparent Km = 40 uM in citrate synthesis from oxaloacetate and acetyl-CoA

row_label: Oxaloacetate Km within citrate synthesis reaction using acetyl-CoA and oxaloacetate

table_label: Official PMC full text Results/prose for purified IPMS2/Re-citrate synthase


organism: Dehalococcoides mccartyi


organism: Ogataea angusta


substrate_name: glyoxylate

substrate: glyoxylate


organism: Pinus densiflora


substrate_name: Unknown

proof_lines:
enzyme form MSH
enzyme form MSL

substrate: Unknown


enzyme_display_name: hydroxymethylglutaryl-CoA synthase

organism: Locusta migratoria

enzyme: hydroxymethylglutaryl-CoA synthase


organism: Antarctic bacterium DS2-3R

substrate_name: oxaloacetate (with propionyl-CoA at pH 8 and 23 degrees Celsius)

proof_lines: kcat is 8 sec(-1) for 2-methylcitrate synthase activity with propionyl-CoA as substrate (at pH 8 and 23 degrees Celsius). kcat is 21 sec(-1) for citrate synthase activity with acetyl-CoA as substrate (at pH 8 and 23 degrees Celsius).


substrate_name: propionyl-CoA (at pH 8 and 23 degrees Celsius)


substrate_name: acetyl-CoA (at pH 8 and 23 degrees Celsius)


organism: Aspergillus nidulans


assay_conditions_summary: pH 8


organism: Homo sapiens

proof_lines: mutant A348G, pH 8.0, temperature not specified in the publication


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme G348G


organism: Haloferax volcanii

column_label: Table 1; HvHMGCS row; Km (uM) / Acetyl-CoA, kcat (s^-1), and kcat/Km (s^-1 mM^-1) columns; printed cells 50 +/- 6 uM, 4.6 +/- 0.2 s^-1, and 92 +/- 11 s^-1 mM^-1. Footnote a states values are means and standard errors.

raw_value_unit_evidence: Table 1 reports HvHMGCS acetyl-CoA Km = 50 +/- 6 uM, kcat = 4.6 +/- 0.2 s^-1, and kcat/Km = 92 +/- 11 s^-1 mM^-1.

row_label: HvHMGCS

table_label: Table 1. Kinetic parameters of H. volcanii, E. faecalis, and H. sapiens HMGCS enzymes


substrate_name: acetoacetyl-CoA

column_label: Table 1; HvHMGCS row; Km (uM) / Acetoacetyl-CoA column; printed cell 1.4 +/- 0.1 uM. Footnote a states values are means and standard errors.

raw_value_unit_evidence: Table 1 reports HvHMGCS acetoacetyl-CoA Km = 1.4 +/- 0.1 uM.

substrate: acetoacetyl-CoA


organism: Colwellia maris

assay_conditions_summary: 293.15 K; cofactor CoA

proof_lines:
at 20°C
at 45°C


enzyme_display_name: UniProt Q56063

organism: Salmonella enterica subsp. enterica serovar Typhimurium

proof_lines: kcat is 1.4 sec(-1) for citrate synthase activity with acetyl-CoA as substrate. kcat is 1.87 sec(-1) for citrate synthase activity with acetyl-CoA as substrate (at pH 8 and 30 degrees Celsius). kcat is 7.4 sec(-1) for 2-methylcitrate syntha

enzyme: UniProt Q56063


organism: Helicobacter pylori

substrate_name: H2O; Acetyl-CoA; Glyoxylate

substrate: H2O; Acetyl-CoA; Glyoxylate


enzyme_display_name: Citramalyl-CoA lyase, mitochondrial

substrate_name: (3S)-citramalyl-CoA (for citramalyl-CoA lyase activity)

proof_lines: kcat is 0.12 sec(-1) for malate synthase reaction (PubMed:24334609). kcat is 0.09 sec(-1) for beta-methylmalate synthase reaction (PubMed:24334609). kcat is 0.135 sec(-1) for beta-methylmalate synthase reaction (PubMed:29056341). kcat is 0.

enzyme: Citramalyl-CoA lyase, mitochondrial


substrate_name: propionyl-CoA (for beta-methylmalate synthase)


substrate_name: acetyl-CoA (for malate synthase)

substrate: acetyl-CoA (for malate synthase)


substrate_name: (S)-malyl-CoA (for malyl-CoA thioesterase activity)


organism: Gallus gallus

substrate_name: H2O; Acetoacetyl-CoA; Acetyl-CoA

substrate: H2O; Acetoacetyl-CoA; Acetyl-CoA


organism: Mus musculus


substrate_name: Coenzyme A; ATP; Citrate

substrate: Coenzyme A; ATP; Citrate


enzyme_display_name: Malate synthase G

organism: Escherichia coli (strain K12)

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines: kcat is 48.1 sec(-1) for glyoxylate (at pH 8 and 37 degrees Celsius).

enzyme: Malate synthase G


organism: Euglena gracilis

proof_lines: N-terminal malate synthase-active domain GCE(13-573) of glyoxylate cycle enzyme, at 25°C, pH not specified in the publication


proof_lines: wild type full-length glyoxylate cycle enzyme, at 25°C, pH not specified in the publication


enzyme_display_name: ATP-citrate synthase

organism: Rattus norvegicus

enzyme: ATP-citrate synthase


assay_conditions_summary: cofactor CoA


substrate_name: glyoxylate (with acetyl-CoA as cosubstrate)


substrate_name: oxaloacetate

substrate: oxaloacetate


organism: Saccharolobus solfataricus

proof_lines: pH 8.0, 70°C, native enzyme from xylose-grown cell extract


substrate_name: acetyl-CoA


organism: Enterococcus faecalis

substrate_name: Acetoacetyl-CoA; Acetyl-CoA; H2O

substrate: Acetoacetyl-CoA; Acetyl-CoA; H2O


proof_lines: kcat is 4.6 sec(-1) (at pH 8 and 30 degrees Celsius).


organism: Arthrobacter sp.

substrate_name: Propanoyl-CoA; Oxaloacetate; H2O

substrate: Propanoyl-CoA; Oxaloacetate; H2O


substrate_name: Unknown


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)


substrate_name: glyoxylate

proof_lines: AceB requires a high salt concentration for activity, the optimum being around 3.0 M KCl. Replacement of KCl by NaCl causes a decrease in activity (about 2-fold).


organism: Sus scrofa

substrate_name: Acetyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D375E with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.1; 298.15 K; cofactor CoA

substrate: Acetyl-CoA


sequence_variant_note: Mutation signature H274G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature H274R could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: Citrate synthase, mitochondrial

column_label: PDF page 4, Table III, nonmutant row, Km(OAA) (uM) column = 6.0 +/- 3.7.

raw_value_unit_evidence: Table III row His274,Asp375 (nonmutant): Km(OAA) 6.0 +/- 3.7 uM.

row_label: His274,Asp375 (nonmutant)

table_label: Table III: Kinetic Parameters of Pig Citrate Synthases Expressed in E. coli

enzyme: Citrate synthase, mitochondrial


substrate_name: acetyl-coA

assay_conditions_summary: pH 8.1; cofactor CoA

column_label: PDF page 4, Table III, nonmutant row, Km(AcCoA) (uM) column = 16.3 +/- 1.5.

raw_value_unit_evidence: Table III row His274,Asp375 (nonmutant): Km(AcCoA) 16.3 +/- 1.5 uM.

substrate: acetyl-coA


organism: Escherichia coli

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +6, so it is treated as a source-provided variant sequence.


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


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

column_label: Archives Biochem Biophys 2007 PMID 17570335 Table 1 row Cit1p / Acetyl-CoA reports Km 76 +/- 7 uM.

normalized_value_unit_evidence: Km normalized_value=0.076 mM

raw_value_unit_evidence: Km raw_value=76 +/- 7 raw_unit=uM


enzyme_display_name: Citrate synthase 3, mitochondrial

column_label: Archives Biochem Biophys 2007 PMID 17570335 Table 1 row Cit3p / Acetyl-CoA reports Km 1200 +/- 200 uM.

normalized_value_unit_evidence: Km normalized_value=1.2 mM

raw_value_unit_evidence: Km raw_value=1200 +/- 200 raw_unit=uM

enzyme: Citrate synthase 3, mitochondrial


substrate_name: propionyl-CoA

column_label: Archives Biochem Biophys 2007 PMID 17570335 Table 1 row Cit3p / Propionyl-CoA reports Km 520 +/- 90 uM.

normalized_value_unit_evidence: Km normalized_value=0.52 mM

raw_value_unit_evidence: Km raw_value=520 +/- 90 raw_unit=uM

substrate: propionyl-CoA


substrate_name: Propanoyl-CoA

sequence_variant_note: Mutation signature A361R could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 8; 296.15 K; cofactor CoA

substrate: Propanoyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K313L/A361R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


enzyme_display_name: 2-methylcitrate synthase, mitochondrial

organism: Fusarium solani

enzyme: 2-methylcitrate synthase, mitochondrial


column_label: Table 2 row Km value acetyl-CoA column McsA F. solani = 1.26 mM.

normalized_value_unit_evidence: Km normalized_value=1.26 mM

raw_value_unit_evidence: Km raw_value=1.26 raw_unit=mM

row_label: Km value acetyl-CoA / McsA F. solani

table_label: Table 2

substrate: acetyl-CoA


substrate_name: oxaloacetate (in presence of propionyl-CoA)

column_label: Table 2 row Km value oxaloacetate (propionyl-CoA) column McsA F. solani = 2.58 mM.

normalized_value_unit_evidence: Km normalized_value=2.58 mM

raw_value_unit_evidence: Km raw_value=2.58 raw_unit=mM

row_label: Km value oxaloacetate (propionyl-CoA) / McsA F. solani


enzyme_display_name: UniProt P53396

organism: Homo sapiens

substrate_name: citrate

enzyme: UniProt P53396

substrate: citrate


substrate_name: CoA

substrate: CoA


substrate_name: ATP

substrate: ATP


enzyme_display_name: Name not preserved

organism: Aspergillus fumigatus

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

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

column_label: Table 1 section Oxaloacetate; row KM (uM); mcsA column.

normalized_value_unit_evidence: 4.9 uM normalizes to 0.0049 mM, not exact exported 0.0027 mM.

raw_value_unit_evidence: Table 1 reports mcsA Oxaloacetate KM as 4.9 +/- 0.2 uM.

row_label: Oxaloacetate; KM (uM); mcsA column

table_label: Table 1: Kinetic parameters of hCS, hCSA348G, mcsA and mcsAG352A determined by UV-Vis spectroscopy

enzyme: Name not preserved


column_label: Table 2 columns Parameter and McsA A. fumigatus; row Km Oxaloacetate; expected Km matches the table value.

raw_value_unit_evidence: Table 2 row Km Oxaloacetate reports 2.7 uM in the A. fumigatus McsA column.

row_label: Km Oxaloacetate

table_label: Table 2: Comparison of properties of methylcitrate synthases from A. fumigatus and A. nidulans


column_label: Table 1 section Acetyl-CoA; row KM (uM); mcsA column.

normalized_value_unit_evidence: 5.0 uM normalizes to 0.0050 mM, not exact exported 0.0026 mM.

raw_value_unit_evidence: Table 1 reports mcsA Acetyl-CoA KM as 5.0 +/- 1.3 uM.

row_label: Acetyl-CoA; KM (uM); mcsA column


column_label: Table 2 columns Parameter and McsA A. fumigatus; row Km Acetyl-CoA; expected Km matches the table value.

raw_value_unit_evidence: Table 2 row Km Acetyl-CoA reports 2.6 uM in the A. fumigatus McsA column.

row_label: Km Acetyl-CoA


substrate_name: propanoyl-CoA

column_label: Table 1 section Propionyl-CoA; row KM (uM); mcsA column. The exported substrate spelling propanoyl-CoA is treated as the same acyl-CoA substrate label.

normalized_value_unit_evidence: 4.7 uM normalizes to 0.0047 mM, not exact exported 0.0019 mM.

raw_value_unit_evidence: Table 1 reports mcsA Propionyl-CoA KM as 4.7 +/- 0.3 uM.

row_label: Propionyl-CoA; KM (uM); mcsA column

substrate: propanoyl-CoA


column_label: Table 2 columns Parameter and McsA A. fumigatus; row Km Propionyl-CoA; expected Km matches the table value.

raw_value_unit_evidence: Table 2 row Km Propionyl-CoA reports 1.9 uM in the A. fumigatus McsA column.

row_label: Km Propionyl-CoA


organism: Chlorobaculum tepidum


organism: Gibberella moniliformis


column_label: Table 2 row Km value acetyl-CoA column McsA F. verticillioides = 2.71 mM.

normalized_value_unit_evidence: Km normalized_value=2.71 mM

raw_value_unit_evidence: Km raw_value=2.71 raw_unit=mM

row_label: Km value acetyl-CoA / McsA F. verticillioides


column_label: Table 2 row Km value oxaloacetate (propionyl-CoA) column McsA F. verticillioides = 2.81 mM.

normalized_value_unit_evidence: Km normalized_value=2.81 mM

raw_value_unit_evidence: Km raw_value=2.81 raw_unit=mM

row_label: Km value oxaloacetate (propionyl-CoA) / McsA F. verticillioides

substrate: oxaloacetate (in presence of propionyl-CoA)


organism: Hydrogenobacter thermophilus


enzyme_display_name: 2-isopropylmalate synthase

organism: Neurospora crassa

enzyme: 2-isopropylmalate synthase


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


substrate_name: pyruvate

substrate: pyruvate


enzyme_display_name: UniProt P9WQB3

organism: Mycobacterium tuberculosis

substrate_name: alpha-ketoisovaleric acid

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

enzyme: UniProt P9WQB3

substrate: alpha-ketoisovaleric acid


enzyme_display_name: UniProt Q9JZG1

organism: Neisseria meningitidis

enzyme: UniProt Q9JZG1


substrate_name: alpha-Ketobutyrate

substrate: alpha-Ketobutyrate


substrate_name: alpha-ketoisovalerate

substrate: alpha-ketoisovalerate


enzyme_display_name: citrate synthase (unknown stereospecificity)

organism: Lathyrus oleraceus

substrate_name: oxaloacetate

substrate: oxaloacetate


substrate_name: acetyl-CoA

enzyme: citrate synthase (unknown stereospecificity)


organism: Natronobacterium gregoryi


organism: Natronomonas pharaonis


enzyme_display_name: UniProt A4YGX6

organism: Metallosphaera sedula

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

enzyme: UniProt A4YGX6


enzyme_display_name: UniProt P0ABH7

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

enzyme: UniProt P0ABH7


enzyme_display_name: UniProt P21553

organism: Thermoplasma acidophilum

enzyme: UniProt P21553


enzyme_display_name: UniProt P20115

organism: Arabidopsis thaliana

enzyme: UniProt P20115


organism: Escherichia coli

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.8
Raw SKiD Env: Temp=-----, pH=-----


organism: Yarrowia lipolytica (strain CLIB 122 / E 150)


substrate_name: butyryl-CoA

substrate: butyryl-CoA


substrate_name: valeryl-CoA

substrate: valeryl-CoA


organism: Rattus norvegicus

proof_lines:
ATP:citrate lyase
rat ACL
very similar enzymological properties


enzyme_display_name: UniProt O75390

organism: Homo sapiens

proof_lines:
human citrate synthase
catalyzes the same reaction

enzyme: UniProt O75390


enzyme_display_name: Hydroxymethylglutaryl-CoA synthase

organism: Enterococcus faecalis

enzyme: Hydroxymethylglutaryl-CoA synthase


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


enzyme_display_name: citrate (Re)-synthase

organism: Clostridium kluyveri

column_label: Official PMC full text PMID 17400742, Determination of citrate synthase activity and Results prose for purified IPMS2/Re-citrate synthase

raw_value_unit_evidence: oxaloacetate apparent Km = 40 uM

row_label: Purified IPMS2/Re-citrate synthase; oxaloacetate substrate

enzyme: citrate (Re)-synthase


raw_value_unit_evidence: acetyl-CoA apparent Km = 50 uM

row_label: Purified IPMS2/Re-citrate synthase; acetyl-CoA substrate


enzyme_display_name: homocitrate synthase

organism: Thermus thermophilus

substrate_name: Acetyl-CoA

assay_conditions_summary: pH 7.5; 323.15 K; cofactor CoA

enzyme: homocitrate synthase

substrate: Acetyl-CoA


enzyme_display_name: Citrate (Re)-synthase

organism: Dehalococcoides mccartyi (strain CBDB1)

enzyme: Citrate (Re)-synthase


organism: Syntrophus aciditrophicus


enzyme_display_name: 2-methylcitrate synthase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

column_label: Table 1 Acetyl-CoA column reports Km 265 +/- 30 uM, Kcat 1.87 +/- 0.4 s^-1, and Kcat/Km 7.05 x 10^-3; the HTML row label prints M^-1 s^-1, but the numeric row is consistent with the uM Km row and s^-1*mM^-1 export normalization

normalized_value_unit_evidence: Km normalized_value=0.265 normalized_unit=mM; Kcat normalized_value=1.87 normalized_unit=s^-1; Kcat/Km normalized_value=7.056603773584905 normalized_unit=s^-1*mM^-1 from same-table values, matching printed row after micromolar-denominator normalization

raw_value_unit_evidence: Km raw_value=265 +/- 30 raw_unit=uM; Kcat raw_value=1.87 +/- 0.4 raw_unit=s^-1; Kcat/Km raw_value=7.05 x 10^-3 raw row as printed under Kcat/Km

row_label: Acetyl-CoA column; rows Km, Kcat, and Kcat/Km

table_label: PMID 20970504 Table 1

enzyme: 2-methylcitrate synthase


column_label: Table 1 Propionyl-CoA column reports Km 45 +/- 10 uM, Kcat 8.25 +/- 0.5 s^-1, and Kcat/Km 183 x 10^-3; the HTML row label prints M^-1 s^-1, but the numeric row is consistent with the uM Km row and s^-1*mM^-1 export normalization; propanoyl-CoA and propionyl-CoA are the same acyl-CoA naming variant

normalized_value_unit_evidence: Km normalized_value=0.045 normalized_unit=mM; Kcat normalized_value=8.25 normalized_unit=s^-1; Kcat/Km normalized_value=183.33333333333334 normalized_unit=s^-1*mM^-1 from same-table values, matching printed row rounded after micromolar-denominator normalization

raw_value_unit_evidence: Km raw_value=45 +/- 10 raw_unit=uM; Kcat raw_value=8.25 +/- 0.5 raw_unit=s^-1; Kcat/Km raw_value=183 x 10^-3 raw row as printed under Kcat/Km

row_label: Propionyl-CoA column; rows Km, Kcat, and Kcat/Km


enzyme_display_name: dextrin dextranase

organism: Gluconobacter oxydans

substrate_name: maltoheptaose

enzyme: dextrin dextranase

substrate: maltoheptaose


substrate_name: maltohexaose

substrate: maltohexaose


substrate_name: maltopentaose

substrate: maltopentaose


substrate_name: maltotetraose

substrate: maltotetraose


substrate_name: maltotriose

substrate: maltotriose


enzyme_display_name: UniProt Q1J0W0

organism: Deinococcus geothermalis

proof_lines:
Raw SKiD Env: Temp=45°C, pH=7
Raw SKiD Env: Temp=45°C, pH=5

enzyme: UniProt Q1J0W0


enzyme_display_name: Dextransucrase

organism: Leuconostoc mesenteroides

substrate_name: sucrose

sequence: DSTNTV

wild_type_sequence: DSTNTV

enzyme: Dextransucrase

substrate: sucrose


organism: Escherichia coli (strain K12)


substrate: acetyl-CoA


enzyme_display_name: Malate synthase G

organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)

substrate_name: acetyl-CoA (at pH 7.6 and 30 degrees Celsius)

enzyme: Malate synthase G


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