organism: Nicotiana tabacum

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O24146 and applied mutation signature T193A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

column_label: Table 3: Kinetic Parameters for Nt4CL2 Variants against 4-Coumaric Acid (Structure 2015, volume 23, issue 11, pages 2032-2042); printed column heads KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 3, variant row T193A; column KM (uM) = 2.9; column kcat (s^-1) = 0.996; column kcat/KM (M^-1 s^-1) = 3.434 x 10^5. captured primary segment: T193A | 4-Coumaric Acid | Km 2.9 uM | kcat 0.996 s^-1 | kcat/Km 3.434 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 3 cell 2.9 uM; 2.9 / 1000 = 0.0029 mM. kcat: printed Table 3 cell 0.996 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 0.996 s^(-1). kcat/Km: printed Table 3 cell 3.434 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell becomes 343.4 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.996 / 0.0029 = 343.448275862069 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, variant row T193A: KM = 2.9 uM; kcat = 0.996 s^-1; printed kcat/KM = 3.434 x 10^5 M^-1 s^-1.

row_label: Table 3, variant row T193A


enzyme_display_name: 4-coumarate--CoA ligase

substrate_name: sinapinate

source_db: skid

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

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

km_unit: mM

sequence_source: multiple

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

proof_lines: kcat is 3.978 sec(-1) with (E)-4-coumarate as substrate (PubMed:26412334). kcat is 2.652 sec(-1) with (E)-caffeate as substrate (PubMed:26412334). kcat is 3.576 sec(-1) with (E)-ferulate as substrate (PubMed:26412334). kcat is 0.018 sec(-1)

data_origin: experimental

source_databases_merged: skid uniprot

enzyme: 4-coumarate--CoA ligase

substrate: sinapinate

source: skid


substrate_name: caffeate

verification_status: verified

column_label: Table 2: Steady-State Kinetic Parameters for Nt4CL2 against Hydroxycinnamates (Structure 2015, volume 23, issue 11, pages 2032-2042); printed column heads KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, substrate row Caffeic Acid; column KM (uM) = 1.0; column kcat (s^-1) = 2.652; column kcat/KM (M^-1 s^-1) = 2.652 x 10^6. captured primary segment: Nt4CL2 | Caffeic Acid | Km 1.0 uM | kcat 2.652 s^-1 | kcat/Km 2.652 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 1.0 uM; 1.0 / 1000 = 0.001 mM. kcat: printed Table 2 cell 2.652 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 2.652 s^(-1). kcat/Km: printed Table 2 cell 2.652 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell becomes 2652.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 2.652 / 0.001 = 2652.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate row Caffeic Acid: KM = 1.0 uM; kcat = 2.652 s^-1; printed kcat/KM = 2.652 x 10^6 M^-1 s^-1.

row_label: Table 2, substrate row Caffeic Acid

substrate: caffeate

status: verified


substrate_name: ferulate

column_label: Table 2: Steady-State Kinetic Parameters for Nt4CL2 against Hydroxycinnamates (Structure 2015, volume 23, issue 11, pages 2032-2042); printed column heads KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, substrate row Ferulic Acid; column KM (uM) = 2.9; column kcat (s^-1) = 3.576; column kcat/KM (M^-1 s^-1) = 1.233 x 10^6. captured primary segment: Nt4CL2 | Ferulic Acid | Km 2.9 uM | kcat 3.576 s^-1 | kcat/Km 1.233 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 2.9 uM; 2.9 / 1000 = 0.0029 mM. kcat: printed Table 2 cell 3.576 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 3.576 s^(-1). kcat/Km: printed Table 2 cell 1.233 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell becomes 1233.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.576 / 0.0029 = 1233.103448275862 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate row Ferulic Acid: KM = 2.9 uM; kcat = 3.576 s^-1; printed kcat/KM = 1.233 x 10^6 M^-1 s^-1.

row_label: Table 2, substrate row Ferulic Acid

substrate: ferulate


organism: Anthoceros agrestis

substrate_name: isoferulate

source_db: brenda

kcat_over_km_origin: calculated

source_license: CC BY 4.0

proof_lines:
isoform 4CL_1, at pH 7.0 and 40°C
isoform 4CL_2, at pH 7.0 and 40°C

substrate: isoferulate

source: brenda


substrate_name: CoA

assay_conditions_summary: pH 7; 313.15 K; cofactor CoA

substrate: CoA


substrate_name: cinnamate

verification_status: corrected

assay_conditions_summary: pH 7; cofactor ATP

column_label: Table 1 Kinetic data for Aa4CL_1 (a) and Aa4CL_2 (b). Table 1 panel (b), substrate row 'Cinnamic acid', enzyme column Aa4CL_2; column 'Km (uM)' = 216.7; column 'Kcat (1/s)' = 1.8; column 'kcat/Km (1/s mM)' = 8.1.

normalized_value_unit_evidence: Km: printed cell 216.7 uM; 216.7 / 1000 = 0.2167 mM; the exported value is 0.2167 mM. kcat: printed cell 1.8 in the column headed 'Kcat (1/s)'; 1/s is s^(-1), no conversion; the exported value is 1.8 s^(-1). kcat/Km: printed cell 8.1 in the column headed 'kcat/Km (1/s mM)'; 1/s mM is s^(-1)*mM^(-1), no conversion; the exported value is 8.306414397784955 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1 panel (b), substrate row 'Cinnamic acid', enzyme column Aa4CL_2: Km = 216.7 uM; Kcat = 1.8 1/s; printed kcat/Km = 8.1 1/s mM.

substrate: cinnamate

status: corrected


substrate_name: ATP

assay_conditions_summary: pH 7; 313.15 K; cofactor ATP

substrate: ATP


organism: Plagiochasma appendiculatum


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M247Y/A251S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M247Y/A251S, at pH 7.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M247Y to reconstruct the assayed variant sequence.

mutation_type: substitution


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A251S to reconstruct the assayed variant sequence.


organism: Oryza sativa subsp. japonica

substrate_name: Unknown

source_db: uniprot

kcat_display: Not reported

km_display: Not reported

kcat_over_km_display: Not reported

proof_lines: kcat is 0.37 min(-1) with cinnamate as substrate (PubMed:21807887). kcat is 0.49 min(-1) with 4-coumarate as substrate (PubMed:21807887). kcat is 0.52 min(-1) with caffeate as substrate (PubMed:21807887). kcat is 0.41 min(-1) with ferulate

substrate: Unknown

source: uniprot


proof_lines: kcat is 1.02 min(-1) with cinnamate as substrate (PubMed:21807887). kcat is 2.88 min(-1) with 4-coumarate as substrate (PubMed:21807887). kcat is 0.84 min(-1) with caffeate as substrate (PubMed:21807887). kcat is 2.04 min(-1) with ferulate


proof_lines: kcat is 10.92 min(-1) with cinnamate as substrate (PubMed:21807887). kcat is 17.1 min(-1) with 4-coumarate as substrate (PubMed:21807887). kcat is 15.3 min(-1) with caffeate as substrate (PubMed:21807887). kcat is 17.94 min(-1) with ferulat


proof_lines: kcat is 1.28 min(-1) with cinnamate as substrate (PubMed:21807887). kcat is 2.82 min(-1) with 4-coumarate as substrate (PubMed:21807887). kcat is 2.16 min(-1) with caffeate as substrate (PubMed:21807887). kcat is 1.92 min(-1) with ferulate


proof_lines: kcat is 1.13 min(-1) with cinnamate as substrate (PubMed:21807887). kcat is 2.37 min(-1) with 4-coumarate as substrate (PubMed:21807887). kcat is 2.67 min(-1) with caffeate as substrate (PubMed:21807887). kcat is 2.31 min(-1) with ferulate


organism: Petunia hybrida

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 0.847 sec(-1) with trans-cinnamic acid as substrate (PubMed:22649270). kcat is 1.488 sec(-1) with 4-coumaric acid as substrate (PubMed:22649270). kcat is 3.645 sec(-1) with caffeic acid as substrate (PubMed:22649270). kcat is 2.39 s


organism: Arabidopsis thaliana

substrate_name: adenosine 5'-tetraphosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M293P/K320L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: reverse reaction, M293P/K320L mutant enzyme, pH 7.0, 30°C

substrate: adenosine 5'-tetraphosphate


organism: Glycine max


enzyme_display_name: acetate--CoA ligase (ADP-forming)

organism: Entamoeba histolytica

substrate_name: phosphate

assay_conditions_summary: pH 7.3; cofactor ATP

proof_lines: with propionyl-CoA as cosubstrate, at pH 7.3 and 37°C

proof_lines: with acetyl-CoA as cosubstrate, at pH 7.3 and 37°C

enzyme: acetate--CoA ligase (ADP-forming)

substrate: phosphate


substrate_name: ADP

substrate: ADP


substrate_name: GDP

assay_conditions_summary: pH 7.3; 310.15 K; cofactor CoA

column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetate-forming direction, acetyl-CoA as acyl substrate, varied-substrate row 'GDP'; column 'Km (mM)' = 1.9 ± 0.14; column 'kcat (s^-1)' = 170 ± 5.2; column 'kcat/Km (s^-1 mM^-1)' = 90 ± 8.3. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.9 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 1.9 mM; the exported value is 1.9 mM. kcat: printed Table 1 cell 170 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 170.0 s^(-1); the exported value is 170.0 s^(-1). kcat/Km: printed Table 1 cell 90 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 90.0 s^(-1)*mM^(-1); the exported value is 89.47368421052632 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, acetate-forming direction, acetyl-CoA as acyl substrate, varied substrate GDP: Km = 1.9 ± 0.14 mM; kcat = 170 ± 5.2 s^-1; printed kcat/Km = 90 ± 8.3 s^-1 mM^-1.

table_label: Table 1: Apparent kinetic parameters for EhACD in each direction of the reaction (Eukaryotic Cell 2014, volume 13, number 12, page 1533)

substrate: GDP


substrate_name: GTP

column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetyl-CoA-forming direction, acetate as acyl substrate, varied-substrate row 'GTP'; column 'Km (mM)' = 10 ± 0.1; column 'kcat (s^-1)' = 180 ± 1.6; column 'kcat/Km (s^-1 mM^-1)' = 18 ± 0.1. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 10 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 10.0 mM; the exported value is 10.0 mM. kcat: printed Table 1 cell 180 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 180.0 s^(-1); the exported value is 180.0 s^(-1). kcat/Km: printed Table 1 cell 18 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 18.0 s^(-1)*mM^(-1); the exported value is 18.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, acetyl-CoA-forming direction, acetate as acyl substrate, varied substrate GTP: Km = 10 ± 0.1 mM; kcat = 180 ± 1.6 s^-1; printed kcat/Km = 18 ± 0.1 s^-1 mM^-1.

substrate: GTP


substrate_name: acetyl-CoA

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

proof_lines:
pH 7.0, 37°C, recombinant enzyme
at pH 6.0 and 37°C
at pH 7.0 and 37°C

substrate: acetyl-CoA


substrate_name: acetate

proof_lines:
at pH 6.0 and 37°C
pH 6.0, 37°C, recombinant enzyme
at pH 7.0 and 37°C

substrate: acetate


assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP

proof_lines: with propionate as cosubstrate, at pH 7.3 and 37°C

proof_lines: with acetate as cosubstrate, at pH 7.3 and 37°C


proof_lines:
M293P/K320L mutant enzyme
M293P/K320L mutant enzyme, pH 7.0, 30°C


proof_lines: kcat is 0.472 sec(-1) with trans-cinnamic acid as substrate (PubMed:22649270). kcat is 0.248 sec(-1) with 4-coumaric acid as substrate (PubMed:22649270). kcat is 0.238 sec(-1) with caffeic acid as substrate (PubMed:22649270). kcat is 0.458


enzyme_display_name: cholate--CoA ligase

organism: Homo sapiens

enzyme: cholate--CoA ligase


enzyme_display_name: oxalate--CoA ligase

enzyme: oxalate--CoA ligase


enzyme_display_name: 6-carboxyhexanoate--CoA ligase

organism: Bacillus subtilis

substrate_name: Octanoate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y211F to reconstruct the assayed variant sequence.

smiles: CCCCCCCC(=O)[O-]

proof_lines: mutant Y211F, pH and temperature not specified in the publication

enzyme: 6-carboxyhexanoate--CoA ligase

substrate: Octanoate


substrate_name: Heptanoate

smiles: CCCCCCC(=O)[O-]

substrate: Heptanoate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


enzyme_display_name: malate--CoA ligase

organism: Sus scrofa

enzyme: malate--CoA ligase


substrate_name: tetradecanoate

smiles: CCCCCCCCCCCCCC(=O)[O-]

proof_lines: kcat is 0.43 sec(-1) with tetradecanoate as substrate (PubMed:18267944). kcat is 0.7 sec(-1) with trans-cinnamate as substrate (PubMed:24838974). kcat is 2.1 sec(-1) with p-coumarate as substrate (PubMed:24838974). kcat is 3.6 sec(-1) with

substrate: tetradecanoate


substrate_name: propionyl-CoA

assay_conditions_summary: pH 7.3; 310.15 K; cofactor ADP

column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetate-forming direction, propionyl-CoA as acyl substrate, varied-substrate row 'Propionyl-CoA'; column 'Km (mM)' = 0.032 ± 0.002; column 'kcat (s^-1)' = 21 ± 0.6; column 'kcat/Km (s^-1 mM^-1)' = 650 ± 63. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.032 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.032 mM; the exported value is 0.032 mM. kcat: printed Table 1 cell 21 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 21.0 s^(-1); the exported value is 21.0 s^(-1). kcat/Km: printed Table 1 cell 650 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 650.0 s^(-1)*mM^(-1); the exported value is 656.25 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, acetate-forming direction, propionyl-CoA as acyl substrate, varied substrate Propionyl-CoA: Km = 0.032 ± 0.002 mM; kcat = 21 ± 0.6 s^-1; printed kcat/Km = 650 ± 63 s^-1 mM^-1.

substrate: propionyl-CoA


substrate_name: propionate

column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetyl-CoA-forming direction, propionate as acyl substrate, varied-substrate row 'Propionate'; column 'Km (mM)' = 29 ± 1.4; column 'kcat (s^-1)' = 190 ± 1.5; column 'kcat/Km (s^-1 mM^-1)' = 6.3 ± 0.3. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 29 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 29.0 mM; the exported value is 29.0 mM. kcat: printed Table 1 cell 190 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 190.0 s^(-1); the exported value is 190.0 s^(-1). kcat/Km: printed Table 1 cell 6.3 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 6.3 s^(-1)*mM^(-1); the exported value is 6.551724137931035 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, acetyl-CoA-forming direction, propionate as acyl substrate, varied substrate Propionate: Km = 29 ± 1.4 mM; kcat = 190 ± 1.5 s^-1; printed kcat/Km = 6.3 ± 0.3 s^-1 mM^-1.

substrate: propionate


source_db: oed

smiles: CC(=O)O

column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetyl-CoA-forming direction, acetate as acyl substrate, varied-substrate row 'Acetate'; column 'Km (mM)' = 14 ± 0.6; column 'kcat (s^-1)' = 240 ± 2.7; column 'kcat/Km (s^-1 mM^-1)' = 16 ± 0.5. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 14 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 14.0 mM; the exported value is 14.0 mM. kcat: printed Table 1 cell 240 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 240.0 s^(-1); the exported value is 240.0 s^(-1). kcat/Km: printed Table 1 cell 16 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 16.0 s^(-1)*mM^(-1); the exported value is 17.142857142857142 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, acetyl-CoA-forming direction, acetate as acyl substrate, varied substrate Acetate: Km = 14 ± 0.6 mM; kcat = 240 ± 2.7 s^-1; printed kcat/Km = 16 ± 0.5 s^-1 mM^-1.

source: oed


column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetate-forming direction, acetyl-CoA as acyl substrate, varied-substrate row 'Acetyl-CoA'; column 'Km (mM)' = 0.04 ± 0.001; column 'kcat (s^-1)' = 110 ± 1.6; column 'kcat/Km (s^-1 mM^-1)' = 2,600 ± 370. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.04 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.04 mM; the exported value is 0.04 mM. kcat: printed Table 1 cell 110 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 110.0 s^(-1); the exported value is 110.0 s^(-1). kcat/Km: printed Table 1 cell 2,600 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 2600.0 s^(-1)*mM^(-1); the exported value is 2750.0 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, acetate-forming direction, acetyl-CoA as acyl substrate, varied substrate Acetyl-CoA: Km = 0.04 ± 0.001 mM; kcat = 110 ± 1.6 s^-1; printed kcat/Km = 2,600 ± 370 s^-1 mM^-1.


column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetate-forming direction, acetyl-CoA as acyl substrate, varied-substrate row 'ADP'; column 'Km (mM)' = 1.6 ± 0.15; column 'kcat (s^-1)' = 140 ± 1.2; column 'kcat/Km (s^-1 mM^-1)' = 89 ± 7.9. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.6 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 1.6 mM; the exported value is 1.6 mM. kcat: printed Table 1 cell 140 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 140.0 s^(-1); the exported value is 140.0 s^(-1). kcat/Km: printed Table 1 cell 89 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 89.0 s^(-1)*mM^(-1); the exported value is 87.5 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, acetate-forming direction, acetyl-CoA as acyl substrate, varied substrate ADP: Km = 1.6 ± 0.15 mM; kcat = 140 ± 1.2 s^-1; printed kcat/Km = 89 ± 7.9 s^-1 mM^-1.


column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetyl-CoA-forming direction, acetate as acyl substrate, varied-substrate row 'ATP'; column 'Km (mM)' = 12 ± 0.4; column 'kcat (s^-1)' = 320 ± 4.4; column 'kcat/Km (s^-1 mM^-1)' = 27 ± 0.7. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 12 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 12.0 mM; the exported value is 12.0 mM. kcat: printed Table 1 cell 320 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 320.0 s^(-1); the exported value is 320.0 s^(-1). kcat/Km: printed Table 1 cell 27 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 27.0 s^(-1)*mM^(-1); the exported value is 26.666666666666668 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, acetyl-CoA-forming direction, acetate as acyl substrate, varied substrate ATP: Km = 12 ± 0.4 mM; kcat = 320 ± 4.4 s^-1; printed kcat/Km = 27 ± 0.7 s^-1 mM^-1.


row_label: Table 1, acetate-forming direction, acetyl-CoA as acyl substrate, varied substrate GDP


column_label: TABLE 1. Apparent kinetic parameters for EhACD in each direction of the reaction. TABLE 1, Acetyl-CoA-forming direction, varied substrate GTP; column 'Km (mM)' = 10; column 'kcat (s^-1)' = 180; column 'kcat/Km (s^-1 mM^-1)' = 18.

normalized_value_unit_evidence: Km: printed cell 10 mM converts to 10.0 mM; the exported value is 10.0 mM. kcat: printed cell 180 s^-1 converts to 180.0 s^(-1); the exported value is 180.0 s^(-1). kcat/Km: printed cell 18 s^-1 mM^-1 converts to 18.0 s^(-1)*mM^(-1); the exported value is 18.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 1. Apparent kinetic parameters for EhACD in each direction of the reaction. TABLE 1, Acetyl-CoA-forming direction, varied substrate GTP: Km = 10 mM; kcat = 180 s^-1; printed kcat/Km = 18 s^-1 mM^-1.


smiles: O=P(O)(O)O

column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetate-forming direction, acetyl-CoA as acyl substrate, varied-substrate row 'Phosphate'; column 'Km (mM)' = 1.8 ± 0.18; column 'kcat (s^-1)' = 120 ± 7.8; column 'kcat/Km (s^-1 mM^-1)' = 65 ± 2.3. Table 1 prints no further kinetic column.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.8 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 1.8 mM; the exported value is 1.8 mM. kcat: printed Table 1 cell 120 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 120.0 s^(-1); the exported value is 120.0 s^(-1). kcat/Km: printed Table 1 cell 65 s^-1 mM^-1; the printed unit s^-1 mM^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 65.0 s^(-1)*mM^(-1); the exported value is 66.66666666666667 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, acetate-forming direction, acetyl-CoA as acyl substrate, varied substrate Phosphate: Km = 1.8 ± 0.18 mM; kcat = 120 ± 7.8 s^-1; printed kcat/Km = 65 ± 2.3 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from ncbi_protein_accession:AAB18638.1 and applied mutation signature H237A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Parameters for Nt4CL2 Variants against 4-Coumaric Acid; row H237A / 4-coumaric acid; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); H237A / 4-coumaric acid: kcat 1.98 +/- 0.078 s^-1; Km 143.4 +/- 17.8 uM; kcat/Km (1.381 +/- 0.054) x 10^4 M^-1 s^-1. Normalized directly by unit conversion to kcat=1.98 s^-1; Km=0.1434 mM; kcat/Km=13.81 s^-1*mM^-1.

row_label: H237A / 4-coumaric acid


sequence_variant_note: Resolved canonical sequence from ncbi_protein_accession:AAB18638.1 and applied mutation signature K197A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Parameters for Nt4CL2 Variants against 4-Coumaric Acid; row K197A / 4-coumaric acid; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); K197A / 4-coumaric acid: kcat 7.11 +/- 0.252 s^-1; Km 13.9 +/- 1.8 uM; kcat/Km (5.115 +/- 0.181) x 10^5 M^-1 s^-1. Normalized directly by unit conversion to kcat=7.11 s^-1; Km=0.0139 mM; kcat/Km=511.5 s^-1*mM^-1.

row_label: K197A / 4-coumaric acid


sequence_variant_note: Resolved canonical sequence from ncbi_protein_accession:AAB18638.1 and applied mutation signature K443A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic parameters of Nt4CL2 mutants; row K443A / 4-coumarate; Km, kcat, and kcat/Km columns.

raw_value_unit_evidence: Table 3. Kinetic parameters of Nt4CL2 mutants, row K443A / 4-coumarate: Km 0.9 +/- 0.2 uM; kcat 1.470 +/- 0.096 s^-1; kcat/Km (1.633 +/- 0.107) x 10^6 M^-1 s^-1.

row_label: K443A / 4-coumarate


verification_status: unverified

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M344A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

status: unverified


sequence_variant_note: Resolved canonical sequence from ncbi_protein_accession:AAB18638.1 and applied mutation signature R435A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic parameters of Nt4CL2 mutants; row R435A / 4-coumarate; Km, kcat, and kcat/Km columns.

row_label: R435A / 4-coumarate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T193A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Parameters for Nt4CL2 Variants against 4-Coumaric Acid; row T193A / 4-coumaric acid; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); T193A / 4-coumaric acid: kcat 0.996 +/- 0.036 s^-1; Km 2.9 +/- 0.3 uM; kcat/Km (3.434 +/- 0.124) x 10^5 M^-1 s^-1. Normalized directly by unit conversion to kcat=0.996 s^-1; Km=0.0029 mM; kcat/Km=343.4 s^-1*mM^-1.

row_label: T193A / 4-coumaric acid


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T336A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Parameters for Nt4CL2 Variants against 4-Coumaric Acid; row T336A / 4-coumaric acid; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); T336A / 4-coumaric acid: kcat 0.282 +/- 0.012 s^-1; Km 5.1 +/- 1.0 uM; kcat/Km (5.529 +/- 0.235) x 10^4 M^-1 s^-1. Normalized directly by unit conversion to kcat=0.282 s^-1; Km=0.0051 mM; kcat/Km=55.29 s^-1*mM^-1.

row_label: T336A / 4-coumaric acid


column_label: Table 2. Kinetic parameters of Nt4CL2; row Nt4CL2 wild type / 4-coumarate; Km, kcat, and kcat/Km columns.

raw_value_unit_evidence: Table 2. Kinetic parameters of Nt4CL2, row Nt4CL2 wild type / 4-coumarate: Km 1.5 +/- 0.4 uM; kcat 3.978 +/- 0.252 s^-1; kcat/Km (2.652 +/- 0.168) x 10^6 M^-1 s^-1.

row_label: Nt4CL2 wild type / 4-coumarate

table_label: Table 2. Kinetic parameters of Nt4CL2


sequence_variant_note: Resolved canonical sequence from ncbi_protein_accession:AAB18638.1 and applied mutation signature Y239A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic parameters of Nt4CL2 mutants; row Y239A / 4-coumarate; Km, kcat, and kcat/Km columns.

row_label: Y239A / 4-coumarate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y239F to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Parameters for Nt4CL2 Variants against 4-Coumaric Acid; row Y239F / 4-coumaric acid; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); Y239F / 4-coumaric acid: kcat 4.47 +/- 0.096 s^-1; Km 6.9 +/- 0.6 uM; kcat/Km (6.478 +/- 0.139) x 10^5 M^-1 s^-1. Normalized directly by unit conversion to kcat=4.47 s^-1; Km=0.0069 mM; kcat/Km=647.8 s^-1*mM^-1.

row_label: Y239F / 4-coumaric acid


row_label: Table 1, acetyl-CoA-forming direction, propionate as acyl substrate, varied substrate Propionate


column_label: Table 1 (Apparent kinetic parameters for EhACD in each direction of the reaction), acetate-forming direction, propionyl-CoA as acyl substrate, varied-substrate row 'Propionyl-CoA'; column 'Km (mM)' = 0.032 ± 0.002; column 'kcat (s^-1)' = 21 ± 0.6; column 'kcat/Km (s^-1 mM^-1)' = 650 ± 63. Table 1 prints no further kinetic column.

row_label: Table 1, acetate-forming direction, propionyl-CoA as acyl substrate, varied substrate Propionyl-CoA


substrate_name: caffeate

substrate: caffeate


substrate_name: ferulate

substrate: ferulate


assay_conditions_summary: pH 6; 310.15 K; cofactor CoA


assay_conditions_summary: pH 7; 310.15 K; cofactor ADP


assay_conditions_summary: pH 6; 310.15 K; cofactor ATP


substrate_name: CoA

substrate: CoA


organism: Columba livia

substrate_name: succinate (for A-SCS)

assay_conditions_summary: cofactor ATP

substrate: succinate (for A-SCS)


substrate_name: CoA (for A-SCS)

substrate: CoA (for A-SCS)


substrate_name: succinyl-CoA (for A-SCS)

substrate: succinyl-CoA (for A-SCS)


substrate_name: phosphate (for A-SCS)

substrate: phosphate (for A-SCS)


substrate_name: ATP

substrate: ATP


substrate_name: ADP

substrate: ADP


column_label: Table 2. Steady-State Kinetic Parameters for Nt4CL2 against Hydroxycinnamates; row Caffeic Acid / wild type; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); Caffeic Acid / wild type: kcat 2.652 +/- 0.162 s^-1; Km 1.0 +/- 0.2 uM; kcat/Km (2.652 +/- 0.162) x 10^6 M^-1 s^-1. Normalized directly by unit conversion to kcat=2.652 s^-1; Km=0.001 mM; kcat/Km=2652.0 s^-1*mM^-1.

row_label: Caffeic Acid / wild type


column_label: Table 2. Steady-State Kinetic Parameters for Nt4CL2 against Hydroxycinnamates; row Ferulic Acid / wild type; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); Ferulic Acid / wild type: kcat 3.576 +/- 0.132 s^-1; Km 2.9 +/- 0.4 uM; kcat/Km (1.233 +/- 0.046) x 10^6 M^-1 s^-1. Normalized directly by unit conversion to kcat=3.576 s^-1; Km=0.0029 mM; kcat/Km=1233.0 s^-1*mM^-1.

row_label: Ferulic Acid / wild type


substrate_name: sinapinate

column_label: Table 2. Steady-State Kinetic Parameters for Nt4CL2 against Hydroxycinnamates; row Sinapinic Acid / wild type; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); Sinapinic Acid / wild type: kcat 0.018 +/- 0.000 s^-1; Km 1321.9 +/- 103.9 uM; kcat/Km 13.617 +/- 0.000 M^-1 s^-1. Normalized directly by unit conversion to kcat=0.018 s^-1; Km=1.3219 mM; kcat/Km=0.013617 s^-1*mM^-1.

row_label: Sinapinic Acid / wild type

substrate: sinapinate


organism: Solanum lycopersicum

substrate_name: oxalate

assay_conditions_summary: pH 8

proof_lines: isoform AAE3-1, at pH 8.0, temperature not specified in the publication

substrate: oxalate


organism: Ocimum tenuiflorum


substrate_name: trans-cinnamate

substrate: trans-cinnamate


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

substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: phosphate

substrate: phosphate


organism: Lysinibacillus sphaericus

substrate_name: CoASH

column_label: PMID 1445232 abstract; substrate CoASH; metric apparent Km; raw value 33 microM; normalized value 0.033 mM.

normalized_value_unit_evidence: 33 microM normalized to 0.033 mM.

raw_value_unit_evidence: Abstract reports apparent Km for CoASH = 33 microM.

row_label: pimeloyl-CoA synthase / CoASH apparent Km

table_label: Open PMC/PubMed abstract prose (PMID 1445232)

substrate: CoASH


substrate_name: pimelate

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

column_label: PMID 1445232 abstract; substrate pimelate; metric apparent Km; raw value 145 microM; normalized value 0.145 mM.

normalized_value_unit_evidence: 145 microM normalized to 0.145 mM.

raw_value_unit_evidence: Abstract reports apparent Km for pimelate = 145 microM.

row_label: pimeloyl-CoA synthase / pimelate apparent Km

substrate: pimelate


column_label: PMID 1445232 abstract; paper substrate ATP.Mg2-; package substrate ATP; metric apparent Km; raw value 170 microM; normalized value 0.17 mM.

normalized_value_unit_evidence: 170 microM normalized to 0.17 mM.

raw_value_unit_evidence: Abstract reports apparent Km for ATP.Mg2- = 170 microM.

row_label: pimeloyl-CoA synthase / ATP.Mg2- apparent Km


column_label: Official PMC Table 1 row '4-Coumarate', column 'Km, uM': 432

raw_value_unit_evidence: Km column reports 432 uM

table_label: Table 1. Kinetic properties of At4CL4 in vitro


column_label: Official PMC Table 1 row 'Caffeate', column 'Km, uM': 186

raw_value_unit_evidence: Km column reports 186 uM

row_label: Caffeate


column_label: Official PMC Table 1 row 'Ferulate', column 'Km, uM': 26

raw_value_unit_evidence: Km column reports 26 uM

row_label: Ferulate


substrate_name: sinapate

column_label: Official PMC Table 1 row 'Sinapate', column 'Km, uM': 20

raw_value_unit_evidence: Km column reports 20 uM

row_label: Sinapate

substrate: sinapate


organism: Clostridium scindens (strain JCM 10418 / VPI 12708)

substrate_name: cholate

substrate: cholate


organism: Acetobacterium woodii


substrate_name: caffeate

assay_conditions_summary: pH 7

substrate: caffeate


organism: Vigna umbellata

assay_conditions_summary: pH 4.5; cofactor CoA

column_label: Abstract reports recombinant VuAAE3 protein has specific activity against oxalate, with Km = 121+/-8.2 microM and Vmax of 7.7+/-0.88 micromol min-1 mg-1 protein.

raw_value_unit_evidence: Km raw_value=121+/-8.2 microM raw_unit=microM

row_label: recombinant Vigna umbellata VuAAE3 / oxalate

table_label: PubMed XML abstract PMID 27650448


organism: Lathyrus oleraceus

substrate_name: CoA

substrate: CoA


column_label: Figure 4A and Kinetic Studies prose report hBACS cholate Km 2.8 uM.

raw_value_unit_evidence: Km raw_value=2.8 raw_unit=uM

row_label: hBACS / cholate

table_label: Figure 4 - Kinetic analysis / Kinetic Studies prose


substrate_name: hexadecanoate (palmitate)

smiles: CCCCCCCCCCCCCCCC(=O)[O-]

substrate: hexadecanoate (palmitate)


organism: Pyrococcus furiosus

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

assay_conditions_summary: pH 6.5; 328.15 K; cofactor ADP

proof_lines: pH 6.5, 55°C, recombinant wild-type enzyme


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

proof_lines:
pH 6.5, 55°C, mutant enzyme H257Dalpha
pH 6.5, 55°C, mutant enzyme E217Dalpha


proof_lines:
pH 6.5, 55°C, mutant enzyme E217Dalpha
pH 6.5, 55°C, mutant enzyme H257Dalpha


assay_conditions_summary: pH 6.5; 328.15 K; cofactor ATP


substrate_name: acetate

substrate: acetate


substrate_name: succinate

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

substrate: succinate


organism: Rattus norvegicus

substrate_name: chenodeoxycholic acid

substrate: chenodeoxycholic acid


organism: Nicotiana tabacum


substrate_name: ferulate

substrate: ferulate


organism: Petroselinum crispum

substrate_name: Coenzyme A; 4-Coumarate; ATP

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

substrate: Coenzyme A; 4-Coumarate; ATP


substrate_name: isoferulate

substrate: isoferulate


substrate_name: cinnamate

substrate: cinnamate


substrate_name: azelate

proof_lines: pH and temperature not specified in the publication

substrate: azelate


substrate_name: suberate

substrate: suberate


substrate_name: Glutarate

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

substrate: Glutarate


substrate_name: adipate

substrate: adipate


substrate_name: ATP

substrate: ATP


proof_lines: recombinant wild-type enzyme, pH 7.8, 30°C


organism: Haloarcula marismortui

substrate_name: ADP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP

substrate: ADP


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: phosphate

substrate: phosphate


organism: Solanum tuberosum


substrate_name: caffeate

substrate: caffeate


substrate_name: p-methoxycinnamate

substrate: p-methoxycinnamate


organism: Thermococcus kodakarensis

substrate_name: thioglycolate

substrate: thioglycolate


substrate_name: phenylacetate

substrate: phenylacetate


substrate_name: acetate

substrate: acetate


substrate_name: Isobutyrate

substrate: Isobutyrate


substrate_name: CoA

substrate: CoA


organism: Pinus taeda

proof_lines: isoform 4CL3, pH and temperature not specified in the publication

proof_lines: isoform 4CL1, pH and temperature not specified in the publication


substrate_name: ferulate

substrate: ferulate


substrate_name: cinnamate

substrate: cinnamate


organism: Arabidopsis thaliana

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K457S to reconstruct the assayed variant sequence.

column_label: Table 2; row Lys457/Ser; column Km caffeate (uM); raw cell 5.

normalized_value_unit_evidence: Km caffeate: 5 uM = 0.005 mM.

raw_value_unit_evidence: Table 2 row Lys457/Ser, Km caffeate column: 5 uM; all values are averages of three independent determinations.

table_label: Table 2 | Enzymatic properties of heterologously expressed At4CL2 variants


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K211S to reconstruct the assayed variant sequence.

column_label: Table 2; row Lys211/Ser; column Km caffeate (uM); raw cell 14.

normalized_value_unit_evidence: Km caffeate: 14 uM = 0.014 mM.

raw_value_unit_evidence: Table 2 row Lys211/Ser, Km caffeate column: 14 uM; all values are averages of three independent determinations.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C403A to reconstruct the assayed variant sequence.

column_label: Table 2; row Cys403/Ala; column Km caffeate (uM); raw cell 18.

normalized_value_unit_evidence: Km caffeate: 18 uM = 0.018 mM.

raw_value_unit_evidence: Table 2 row Cys403/Ala, Km caffeate column: 18 uM; all values are averages of three independent determinations.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E401Q to reconstruct the assayed variant sequence.

column_label: Table 2; row Glu401/Gln; column Km caffeate (uM); raw cell 28.

normalized_value_unit_evidence: Km caffeate: 28 uM = 0.028 mM.

raw_value_unit_evidence: Table 2 row Glu401/Gln, Km caffeate column: 28 uM; all values are averages of three independent determinations.


column_label: Table 2; row Lys457/Ser; column Km ATP (uM); raw cell 29.

raw_value_unit_evidence: Table 2 row Lys457/Ser, Km ATP column: 29 uM; all values are averages of three independent determinations.


column_label: Table 2; row Lys211/Ser; column Km ATP (uM); raw cell 151.

raw_value_unit_evidence: Table 2 row Lys211/Ser, Km ATP column: 151 uM; all values are averages of three independent determinations.


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

column_label: Table 2; Wild-type row; column Km ATP (uM); raw cell 163. The Cys403/Ala row contains 173.

normalized_value_unit_evidence: Paper Km ATP: 163 uM = 0.163 mM; current value is 0.173 mM.

raw_value_unit_evidence: Table 2 Wild-type row, Km ATP column: 163 uM; 173 uM belongs to the Cys403/Ala row; all values are averages of three independent determinations.

row_label: Wild-type


column_label: Table 2; row Glu401/Gln; column Km ATP (uM); raw cell 240.

raw_value_unit_evidence: Table 2 row Glu401/Gln, Km ATP column: 240 uM; all values are averages of three independent determinations.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R449Q to reconstruct the assayed variant sequence.


column_label: Table 2; row Arg449/Gln; column Km ATP (uM); raw cell 1507.

raw_value_unit_evidence: Table 2 row Arg449/Gln, Km ATP column: 1507 uM; all values are averages of three independent determinations.


organism: Haloferax volcanii

assay_conditions_summary: pH 7.5; 315.15 K; cofactor ADP


assay_conditions_summary: pH 7.5; 315.15 K; cofactor ATP


organism: Populus tomentosa

assay_conditions_summary: cofactor CoA

proof_lines: isoform 4CL2, pH and temperature not specified in the publication

proof_lines: isoform 4CL5, pH and temperature not specified in the publication


organism: Sorbus aucuparia

assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA


organism: Pueraria montana var. lobata

substrate_name: trans-cinnamate

substrate: trans-cinnamate


organism: Populus trichocarpa

proof_lines:
isoform 4Cl4, at pH 7.0 and 30°C
isoform 4Cl5, at pH 7.0 and 30°C


organism: Lysinibacillus sphaericus


substrate_name: heptanedioate

substrate: heptanedioate


organism: Halococcus saccharolyticus

assay_conditions_summary: pH 9; 310.15 K; cofactor ADP


assay_conditions_summary: pH 9; 310.15 K; cofactor ATP


organism: Populus trichocarpa x Populus deltoides


organism: Populus tremuloides


proof_lines: 4CL1 with 4-coumarate as substrate, pH 7.5, 30°C


assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

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


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


organism: Aquifex aeolicus


organism: Rattus norvegicus

substrate_name: chenodeoxycholate

proof_lines: native recombinant enzyme expressed in Sf9 microsomes

substrate: chenodeoxycholate


substrate_name: oxalate

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: pH 8.0, temperature not specified in the publication

substrate: oxalate


assay_conditions_summary: pH 7; 303.15 K; cofactor CoA

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


enzyme_display_name: glutamine--tRNA ligase

organism: Escherichia coli

substrate_name: L-glutamine

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

proof_lines:
reaction with tRNA(2'H)Gln
Gln

enzyme: glutamine--tRNA ligase

substrate: L-glutamine


organism: Corynebacterium amycolatum

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: pH 8.0, 30°C, fusion protein CaBioWF. 8-amino-7-oxononanoic acid synthase, i.e. AON synthase, encoded by BioF. ATP-dependent, pimeloyl-CoA synthetase, i.e. PCAS, encoded by BioW


organism: Camellia sinensis var. sinensis

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

proof_lines:
isoform 4CL1, at pH 7.5 and 30°C
isoform 4CL2, at pH 7.5 and 30°C


proof_lines:
isoform 4CL2, at pH 7.5 and 30°C
isoform 4CL1, at pH 7.5 and 30°C


enzyme_display_name: proline--tRNA ligase

substrate_name: L-proline

enzyme: proline--tRNA ligase

substrate: L-proline


enzyme_display_name: arginine--tRNA ligase

substrate_name: tRNAArg(ACG)

proof_lines: tRNA from Escherichia coli, pH and temperature not specified in the publication

proof_lines: tRNA from Glycine max. pH and temperature not specified in the publication

proof_lines: transfer RNA isoacceptor for arginine UCU

enzyme: arginine--tRNA ligase

substrate: tRNAArg(ACG)


enzyme_display_name: cysteine--tRNA ligase

substrate_name: L-cysteine

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

enzyme: cysteine--tRNA ligase

substrate: L-cysteine


enzyme_display_name: glutamate--tRNA ligase

substrate_name: tRNAGlu

proof_lines: pH 7.2, 37°C, recombinant His-tagged enzyme

enzyme: glutamate--tRNA ligase

substrate: tRNAGlu


substrate_name: L-Glutamine; ATP; tRNA(Gln)

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines:
versus glutamine
pH 7.0, 37°C
pH 7.2, 37°C, versus L-glutamine

substrate: L-Glutamine; ATP; tRNA(Gln)


enzyme_display_name: phenylalanine--tRNA ligase

organism: Gallus gallus

substrate_name: 2'-deoxyadenosine 5'-triphosphate

enzyme: phenylalanine--tRNA ligase

substrate: 2'-deoxyadenosine 5'-triphosphate


enzyme_display_name: glycine--tRNA ligase

proof_lines:
acceptor stem mutant substrate
mutant substrate

enzyme: glycine--tRNA ligase


substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Geobacillus stearothermophilus

assay_conditions_summary: pH 8; 328.15 K; cofactor ATP

proof_lines: ATP-diphosphate exchange reaction, pH 8, 55°C


enzyme_display_name: propionate--CoA ligase

organism: Ralstonia solanacearum

substrate_name: Acrylate

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

enzyme: propionate--CoA ligase

substrate: Acrylate


proof_lines:
pH 8.0, 37°C
37°C, pH 8.0, cosubstrate: propanoate


substrate_name: Butyrate

smiles: CCCC(=O)[O-]

substrate: Butyrate


substrate_name: propionate

substrate: propionate


substrate_name: CoA

substrate: CoA


substrate_name: acetate

substrate: acetate


substrate_name: L-Cysteinyl-tRNACys

proof_lines:
steady-state
pH 7.0, 37°C

substrate: L-Cysteinyl-tRNACys


organism: Rhodotorula glutinis

substrate_name: linoleic acid

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

substrate: linoleic acid


substrate_name: oleic acid

smiles: CCCCCCCCC=CCCCCCCCC(=O)O

substrate: oleic acid


substrate_name: stearic acid

smiles: CCCCCCCCCCCCCCCCCC(=O)O

substrate: stearic acid


substrate_name: palmitic acid

smiles: CCCCCCCCCCCCCCCC(=O)O

substrate: palmitic acid


enzyme_display_name: [citrate (pro-3S)-lyase] ligase

organism: Clostridium sphenoides

substrate_name: ATP; Citrate (pro-3S)-lyase (thiol form); Acetate

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

enzyme: [citrate (pro-3S)-lyase] ligase


enzyme_display_name: acetoacetate--CoA ligase

organism: Zoogloea ramigera

substrate_name: Coenzyme A; Acetoacetate; ATP

enzyme: acetoacetate--CoA ligase

substrate: Coenzyme A; Acetoacetate; ATP


substrate_name: acetoacetate

substrate: acetoacetate


organism: Synechococcus elongatus


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate_name: hexanoic acid

smiles: CCCCCC(=O)O

assay_conditions_summary: pH 7.8; 298.15 K; buffer that applies to every line of the table; cofactor ATP

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'Hexanoic acid (C6)'; column 'Km (uM)' = 129; column 'kcat (min^-1)' = 0.11; column 'kcat/Km (uM^-1 min^-1)' = 0.0008. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 129 uM; 1 uM is one thousandth of 1 mM, so 129 / 1000 = 0.129 mM; the exported value is 0.129 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 0.11 min^-1; the printed head is per minute, so 0.11 / 60 = 0.0018333333333333333 s^(-1); the proposed kcat is 0.0018333333333333333 s^(-1). kcat/Km: printed Table 2 cell 0.0008 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.0008 times 1000 divided by 60 = 0.013333333333333334 s^(-1)*mM^(-1); the proposed kcat/Km is 0.013333333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'Hexanoic acid (C6)': Km cell = 129 uM; kcat cell = 0.11 min^-1; printed kcat/Km cell = 0.0008 uM^-1 min^-1.

table_label: Table 2: acyl chain length selectivity and kinetic parameters of FadD33 (J. Biol. Chem. 2013, 288(39):28116-28125), PDF page 5 of 10; printed column heads Enzyme/Substrate, Km (uM), kcat (min^-1) and kcat/Km (uM^-1 min^-1)

substrate: hexanoic acid


substrate_name: decanoic acid

smiles: CCCCCCCCCC(=O)O

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'Decanoic acid (C10)'; column 'Km (uM)' = 121; column 'kcat (min^-1)' = 1.5; column 'kcat/Km (uM^-1 min^-1)' = 0.012. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 121 uM; 1 uM is one thousandth of 1 mM, so 121 / 1000 = 0.121 mM; the exported value is 0.121 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 1.5 min^-1; the printed head is per minute, so 1.5 / 60 = 0.025 s^(-1); the proposed kcat is 0.025 s^(-1). kcat/Km: printed Table 2 cell 0.012 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.012 times 1000 divided by 60 = 0.2 s^(-1)*mM^(-1); the proposed kcat/Km is 0.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'Decanoic acid (C10)': Km cell = 121 uM; kcat cell = 1.5 min^-1; printed kcat/Km cell = 0.012 uM^-1 min^-1.

substrate: decanoic acid


substrate_name: lauric acid

smiles: CCCCCCCCCCCC(=O)O

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'Lauric acid (C12)'; column 'Km (uM)' = 21; column 'kcat (min^-1)' = 2.4; column 'kcat/Km (uM^-1 min^-1)' = 0.110. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 21 uM; 1 uM is one thousandth of 1 mM, so 21 / 1000 = 0.021 mM; the exported value is 0.021 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 2.4 min^-1; the printed head is per minute, so 2.4 / 60 = 0.04 s^(-1); the proposed kcat is 0.04 s^(-1). kcat/Km: printed Table 2 cell 0.110 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.110 times 1000 divided by 60 = 1.8333333333333335 s^(-1)*mM^(-1); the proposed kcat/Km is 1.8333333333333335 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'Lauric acid (C12)': Km cell = 21 uM; kcat cell = 2.4 min^-1; printed kcat/Km cell = 0.110 uM^-1 min^-1.

substrate: lauric acid


column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'Palmitic acid (C16)'; column 'Km (uM)' = 1.9; column 'kcat (min^-1)' = 4.2; column 'kcat/Km (uM^-1 min^-1)' = 2.3. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.9 uM; 1 uM is one thousandth of 1 mM, so 1.9 / 1000 = 0.0019 mM; the exported value is 0.0019 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 4.2 min^-1; the printed head is per minute, so 4.2 / 60 = 0.07 s^(-1); the proposed kcat is 0.07 s^(-1). kcat/Km: printed Table 2 cell 2.3 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 2.3 times 1000 divided by 60 = 38.333333333333336 s^(-1)*mM^(-1); the proposed kcat/Km is 38.333333333333336 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'Palmitic acid (C16)': Km cell = 1.9 uM; kcat cell = 4.2 min^-1; printed kcat/Km cell = 2.3 uM^-1 min^-1.


substrate_name: ATP

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'ATP'; column 'Km (uM)' = 15; column 'kcat (min^-1)' = 1.3; column 'kcat/Km (uM^-1 min^-1)' = 0.085. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 15 uM; 1 uM is one thousandth of 1 mM, so 15 / 1000 = 0.015 mM; the exported value is 0.015 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 1.3 min^-1; the printed head is per minute, so 1.3 / 60 = 0.021666666666666667 s^(-1); the proposed kcat is 0.021666666666666667 s^(-1). kcat/Km: printed Table 2 cell 0.085 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.085 times 1000 divided by 60 = 1.416666666666667 s^(-1)*mM^(-1); the proposed kcat/Km is 1.416666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'ATP': Km cell = 15 uM; kcat cell = 1.3 min^-1; printed kcat/Km cell = 0.085 uM^-1 min^-1.


organism: Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)

substrate_name: butyrate

proof_lines: kcat is 16.2 sec(-1) for ligase activity with propionate as substrate. kcat is 8.4 sec(-1) for ligase activity with butyrate as substrate. kcat is 6.4 sec(-1) for ligase activity with acetate as substrate. kcat is 5.6 sec(-1) for ligase act

substrate: butyrate


substrate_name: valerate

smiles: CCCCC(=O)[O-]

substrate: valerate


proof_lines: kcat is 0.24 sec(-1) for ligase activity with 4HB as substrate. kcat is 0.23 sec(-1) for ligase activity with butyrate as substrate. kcat is 0.22 sec(-1) for ligase activity with valerate as substrate. kcat is 0.21 sec(-1) for ligase activi


substrate_name: propionate


organism: Sulfurisphaera tokodaii

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


assay_conditions_summary: pH 8.4; 338.15 K; cofactor ATP

substrate: ATP


substrate_name: decanoate

smiles: CCCCCCCCCC(=O)[O-]

proof_lines: kcat is 16.1 min(-1) with decanoate as substrate (PubMed:23364516). kcat is 11.2 min(-1) with dodecanoate as substrate (PubMed:23364516). kcat is 4.2 min(-1) with tetradecanoate as substrate (PubMed:23364516).

substrate: decanoate


substrate_name: dodecanoate

smiles: CCCCCCCCCCCC(=O)[O-]

substrate: dodecanoate


substrate_name: tetradecanoate

smiles: CCCCCCCCCCCCCC(=O)[O-]

substrate: tetradecanoate


organism: Humulus lupulus

proof_lines: kcat is 18.3 min(-1) with 2-methylpropanoate as substrate (PubMed:23300257). kcat is 10.5 min(-1) with 2-methylbutanoate as substrate (PubMed:23300257). kcat is 167 min(-1) with CoA as substrate (PubMed:23300257).


substrate_name: CoA

substrate: CoA


organism: Vibrio harveyi

substrate_name: palmitoleic acid

smiles: CCCCCCC=CCCCCCCCC(=O)O

substrate: palmitoleic acid


substrate_name: Unknown

substrate: Unknown


substrate_name: MbtL-holo

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'MbtL-holo'; column 'Km (uM)' = 106; column 'kcat (min^-1)' = 2.0; column 'kcat/Km (uM^-1 min^-1)' = 0.018. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 106 uM; 1 uM is one thousandth of 1 mM, so 106 / 1000 = 0.106 mM; the exported value is 0.106 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 2.0 min^-1; the printed head is per minute, so 2.0 / 60 = 0.03333333333333333 s^(-1); the proposed kcat is 0.03333333333333333 s^(-1). kcat/Km: printed Table 2 cell 0.018 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.018 times 1000 divided by 60 = 0.3 s^(-1)*mM^(-1); the proposed kcat/Km is 0.3 s^(-1)*mM^(-1). The live catalog row for this substrate holds no kcat/Km value, so the printed efficiency cell is recorded here as evidence only.

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'MbtL-holo': Km cell = 106 uM; kcat cell = 2.0 min^-1; printed kcat/Km cell = 0.018 uM^-1 min^-1.

substrate: MbtL-holo


organism: Lacrimispora sphenoides

substrate_name: citrate lyase

substrate: citrate lyase


organism: Rubrivivax gelatinosus


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 0.150 min(-1) with dodecanoate as substrate (PubMed:19477415). kcat is 2.04 min(-1) with dodecanoate as substrate (PubMed:26900152). kcat is 0.123 min(-1) with tetradecanoate as substrate (PubMed:19477415). kcat is 0.98 min(-1) with


substrate_name: hexadecanoate

smiles: CCCCCCCCCCCCCCCC(=O)[O-]

substrate: hexadecanoate


enzyme_display_name: arachidonate--CoA ligase

organism: Homo sapiens

enzyme: arachidonate--CoA ligase


organism: Rattus norvegicus


substrate_name: palmitate

substrate: palmitate


substrate_name: oleate

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

substrate: oleate


substrate_name: arachidonate

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

substrate: arachidonate


organism: Mycobacterium marinum (strain ATCC BAA-535 / M)

proof_lines: kcat is 1.51 min(-1) with dodecanoate as substrate (PubMed:26900152). kcat is 0.69 min(-1) with tetradecanoate as substrate (PubMed:26900152).


substrate_name: Acetoacetate; ATP; Coenzyme A

column_label: Results paragraph immediately after Fig. 4; metric Km for acetoacetate; prose/figure-associated evidence, not a table cell

normalized_value_unit_evidence: Km 0.07 mM

raw_value_unit_evidence: The measured K,n of the enzyme for acetoacetate was 70 Am, with the concentrations of the other substrates being 50 wlvl CoA and 1.25 mm ATP. OCR renders micro-units as A/wlvl/mm in this extraction; interpreted as 70 uM, 50 uM CoA, and 1.25 mM ATP from context.

row_label: rat liver cytosolic acetoacetyl-CoA synthetase; acetoacetate varied

table_label: Results/Fig. 4 prose

substrate: Acetoacetate; ATP; Coenzyme A


substrate_name: Coenzyme A; Acetate; ATP

substrate: Coenzyme A; Acetate; ATP


substrate_name: acyl-carrier protein

substrate: acyl-carrier protein


substrate_name: arachidonate (Isoform 1)

substrate: arachidonate (Isoform 1)


substrate_name: acetate

substrate: acetate


substrate_name: butyrate

smiles: CCCC(=O)[O-]

substrate: butyrate


substrate_name: propionate

column_label: PubMed abstract reports recombinant ACSS3 propionate Km = 0.19 mM; this matches the current row value.

raw_value_unit_evidence: Km raw_value=0.19 mM raw_unit=mM

row_label: Prose segment: recombinant ACSS3 propionate

table_label: PubMed PMID 28003429 abstract

substrate: propionate


organism: Mus musculus


organism: Chloroflexus aurantiacus


substrate_name: NADPH

assay_conditions_summary: pH 7.8; 328.15 K; cofactor NADPH

column_label: The Catalytic Properties section reports apparent Km values for 3-hydroxypropionate, NADPH, ATP, and CoA; NADPH maps to the second value, 10 uM.

raw_value_unit_evidence: NADPH apparent Km 10 uM

row_label: NADPH

table_label: ScienceDirect full-text Results prose: Catalytic Properties of Propionyl-CoA Synthase

substrate: NADPH


substrate_name: CoA

assay_conditions_summary: pH 7.8; 328.15 K; cofactor CoA

column_label: The Catalytic Properties section reports apparent Km values for 3-hydroxypropionate, NADPH, ATP, and CoA; CoA maps to the fourth value, 10 uM.

raw_value_unit_evidence: CoA apparent Km 10 uM

row_label: CoA

substrate: CoA


substrate_name: ATP

assay_conditions_summary: pH 7.8; 328.15 K; cofactor ATP

column_label: The Catalytic Properties section reports apparent Km values for 3-hydroxypropionate, NADPH, ATP, and CoA; ATP maps to the third value, 50 uM.

raw_value_unit_evidence: ATP apparent Km 50 uM

row_label: ATP

substrate: ATP


assay_conditions_summary: cofactor CoA


substrate_name: ATP (Isoform 1)

substrate: ATP (Isoform 1)


substrate_name: CoA (Isoform 1)

substrate: CoA (Isoform 1)


substrate_name: palmitate (Isoform 1)

substrate: palmitate (Isoform 1)


substrate_name: oleate (Isoform 1)

substrate: oleate (Isoform 1)


substrate_name: linoleate (when expressed in bacteria)

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

substrate: linoleate (when expressed in bacteria)


substrate_name: arachidonate (when expressed in bacteria)


substrate_name: stearate (when expreesed in bacteria)

smiles: CCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: stearate (when expreesed in bacteria)


substrate_name: linoleate (when expreesed in bacteria)

substrate: linoleate (when expreesed in bacteria)


substrate_name: stearate

substrate: stearate


substrate_name: oleate

substrate: oleate


substrate_name: linoleate

substrate: linoleate


substrate_name: arachidonate

substrate: arachidonate


substrate_name: butyrate


substrate_name: isobutyrate

substrate: isobutyrate


column_label: Abstract reports reaction rates for ATP, acetate and citrate lyase followed Michaelis-Menten kinetics with Km values 0.14 mM, 5 mM and 37 nM respectively.

raw_value_unit_evidence: Km raw_value=0.14 mM raw_unit=mM

row_label: Rhodopseudomonas/Rubrivivax citrate lyase ligase / ATP

table_label: PubMed XML abstract PMID 7128585


substrate_name: acetate

raw_value_unit_evidence: Km raw_value=5 mM raw_unit=mM

row_label: Rhodopseudomonas/Rubrivivax citrate lyase ligase / acetate

substrate: acetate


organism: Ralstonia solanacearum


substrate_name: Coenzyme A

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

substrate: Coenzyme A


substrate_name: hexadecanoate (palmitate)

substrate: hexadecanoate (palmitate)


substrate_name: palmitic acid (at pH 7.5)

substrate: palmitic acid (at pH 7.5)


substrate_name: (9Z)-octadecenoate (oleate)

smiles: CCCCCCCCCCCCCCCC=CC(=O)[O-]

substrate: (9Z)-octadecenoate (oleate)


column_label: Table I row Km value (mM) for acetate reports 66 for active CL-ligase.

raw_value_unit_evidence: Km raw_value=66 mM raw_unit=mM

row_label: Active CL-ligase from C. sphenoides / acetate

table_label: Table I, PMID 2512994 PDF


substrate_name: ATP

substrate: ATP


organism: Salmonella enterica

substrate_name: ATP; Coenzyme A; Propanoate

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

substrate: ATP; Coenzyme A; Propanoate


substrate_name: Butyrate

substrate: Butyrate


substrate_name: CoA

proof_lines:
pH 8.0, 37°C
45°C, pH 7.0, cosubstrate: propanoate
pH 7.5, 37°C

substrate: CoA


substrate_name: Acrylate

substrate: Acrylate


proof_lines:
pH 8.0, 37°C
45°C, pH 7.0: cosubstrate: propanoate
pH 7.5, 37°C


substrate_name: propionate

substrate: propionate


organism: Escherichia coli

substrate_name: stearic acid

smiles: CCCCCCCCCCCCCCCCCC(=O)O

substrate: stearic acid


substrate_name: myristic acid

smiles: CCCCCCCCCCCCCC(=O)O

substrate: myristic acid


substrate_name: palmitoleic acid

proof_lines: cis-vaccenic acid, oleic acid, linoleic acid

substrate: palmitoleic acid


substrate_name: lauric acid

substrate: lauric acid


substrate_name: Decanoic acid

smiles: CCCCCCCCCC(=O)O

substrate: Decanoic acid


substrate_name: octanoic acid

smiles: CCCCCCCC(=O)O

substrate: octanoic acid


organism: Metallosphaera sedula

assay_conditions_summary: pH 8.4; 318.15 K; cofactor CoA

proof_lines: pH 8.4, 45°C, coupled spectrophotometric assay


substrate_name: propanoate

substrate: propanoate


substrate_name: arachidonate

substrate: arachidonate


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


substrate_name: palmitic acid

smiles: CCCCCCCCCCCCCCCC(=O)O

substrate: palmitic acid


substrate_name: oleic acid

smiles: CCCCCCCCC=CCCCCCCCC(=O)O

substrate: oleic acid


substrate_name: acetoacetate

substrate: acetoacetate


substrate_name: ATP

substrate: ATP


organism: Klebsiella aerogenes


substrate_name: acetyl adenylate

substrate: acetyl adenylate


substrate_name: acetate

substrate: acetate


substrate_name: CoA

substrate: CoA


organism: Oryctolagus cuniculus


organism: Streptomyces lividans


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


sequence_source: UniProtKB/Swiss-Prot A0A0G2K047

assay_conditions_summary: pH 8; cofactor ATP


substrate_name: Butyrate

substrate: Butyrate


organism: Bos taurus

proof_lines:
mammary gland enzyme, cow
cow liver enzyme


organism: Cavia porcellus


substrate_name: propionyl-AMP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

substrate: propionyl-AMP


substrate_name: diphosphate

substrate: diphosphate


proof_lines:
cow liver enzyme
mammary gland enzyme, cow


proof_lines:
ATP, propanoate
mamary gland enzyme, cow,
cow liver enzyme


organism: Geobacillus stearothermophilus

substrate_name: L-arginine

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

proof_lines: ATP-diphosphate exchange reaction, pH 8, 37°C

substrate: L-arginine


organism: Glycine max

substrate_name: tRNAArg(ACG)

proof_lines: tRNA from Escherichia coli, pH and temperature not specified in the publication

proof_lines: tRNA from Glycine max, pH and temperature not specified in the publication

substrate: tRNAArg(ACG)


substrate_name: E. coli acyl-carrier protein

proof_lines: fatty acids with shorter chain length than 12

substrate: E. coli acyl-carrier protein


organism: Haemophilus influenzae

substrate_name: L-Phe

substrate: L-Phe


organism: Sinorhizobium meliloti


organism: Homo sapiens

substrate_name: tRNAGlu

substrate: tRNAGlu


enzyme_display_name: 4-coumarate--CoA ligase

substrate_name: sinapate

enzyme: 4-coumarate--CoA ligase

substrate: sinapate


substrate_name: propanoate

substrate: propanoate


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Helicobacter pylori

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication


enzyme_display_name: succinate--CoA ligase (ADP-forming)

substrate_name: succinate

assay_conditions_summary: pH 8; 310.15 K; cofactor ADP

enzyme: succinate--CoA ligase (ADP-forming)

substrate: succinate


enzyme_display_name: beta-phosphoglucomutase

organism: Lactobacillus delbrueckii subsp. lactis

substrate_name: beta-D-glucose 1-phosphate

enzyme: beta-phosphoglucomutase

substrate: beta-D-glucose 1-phosphate


enzyme_display_name: DNA 3'-5' helicase

organism: Lathyrus oleraceus

proof_lines: pH 8.0, 37°C, inhibition of DNA helicase activity

proof_lines: pH 8.0, 37°C, inhibition of ATPase activity

enzyme: DNA 3'-5' helicase


enzyme_display_name: glutamine synthetase

enzyme: glutamine synthetase


enzyme_display_name: glucose-6-phosphate isomerase

substrate_name: glucose 6-phosphate

enzyme: glucose-6-phosphate isomerase

substrate: glucose 6-phosphate


enzyme_display_name: oxalate--CoA ligase

organism: Glycine soja

substrate_name: oxalate

assay_conditions_summary: pH 8; cofactor CoA

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

enzyme: oxalate--CoA ligase

substrate: oxalate


enzyme_display_name: cysteine-S-conjugate beta-lyase

organism: Latilactobacillus sakei

substrate_name: L-cysteine

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

proof_lines: pH 10.0, 35°C, recombinant His-tagged enzyme

enzyme: cysteine-S-conjugate beta-lyase

substrate: L-cysteine


substrate_name: ATP

assay_conditions_summary: pH 5.12; 310.15 K; cofactor ATP

proof_lines:
ATP-diphosphate exchange, pH 5.12, 37°C
ATP-diphosphate exchange, 17°C, pH 7.5
ATP-diphosphate exchange, 19°C, pH 7.5

substrate: ATP


enzyme_display_name: peptidylprolyl isomerase

organism: Legionella pneumophila

enzyme: peptidylprolyl isomerase


enzyme_display_name: lactoylglutathione lyase

organism: Leishmania donovani

substrate_name: reduced trypanothione

proof_lines: recombinant enzyme, pH 7.2, room temperature

enzyme: lactoylglutathione lyase

substrate: reduced trypanothione


substrate_name: L-phenylalanine

proof_lines: wild type mitochondrial enzyme, at pH 8.5 and 37°C

substrate: L-phenylalanine


enzyme_display_name: DNA topoisomerase (ATP-hydrolyzing)

assay_conditions_summary: cofactor ATP

proof_lines: recombinant 116 kDa mutant, ATP hydrolysis activity, in presence of DNA

proof_lines: recombinant 116 kDa mutant, ATP hydrolysis activity, in absence of DNA

enzyme: DNA topoisomerase (ATP-hydrolyzing)


organism: Lathyrus sativus

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA


organism: Leishmania major

substrate_name: alpha-D-glucose 1-phosphate

proof_lines: pH and temperature not specified in the publication

substrate: alpha-D-glucose 1-phosphate


substrate_name: L-glutamate

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

substrate: L-glutamate


organism: Levilactobacillus brevis


enzyme_display_name: L-arabinose isomerase

substrate_name: L-arabinose

enzyme: L-arabinose isomerase

substrate: L-arabinose


organism: Leishmania mexicana mexicana

substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


enzyme_display_name: triose-phosphate isomerase

organism: Leishmania mexicana

enzyme: triose-phosphate isomerase


enzyme_display_name: glutamate racemase

organism: Limosilactobacillus fermentum

substrate_name: D-Glu

enzyme: glutamate racemase

substrate: D-Glu


enzyme_display_name: coproporphyrin ferrochelatase

organism: Listeria monocytogenes

enzyme: coproporphyrin ferrochelatase


enzyme_display_name: serine racemase

organism: Macrostomum lignano

substrate_name: D-serine

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

enzyme: serine racemase

substrate: D-serine


substrate_name: D-glyceraldehyde 3-phosphate

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

substrate: D-glyceraldehyde 3-phosphate


organism: Malus domestica

substrate_name: L-arginine

substrate: L-arginine


enzyme_display_name: maltose epimerase

substrate_name: beta-maltose

enzyme: maltose epimerase

substrate: beta-maltose


substrate_name: (R,S)-S-adenosylmethionine

substrate: (R,S)-S-adenosylmethionine


organism: Mesocricetus auratus


enzyme_display_name: UDP-glucose 4-epimerase

organism: Magallana gigas

substrate_name: UDP-alpha-D-galactose

enzyme: UDP-glucose 4-epimerase

substrate: UDP-alpha-D-galactose


organism: Manihot esculenta

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication


organism: Methanococcus maripaludis

substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


organism: Methanocaldococcus jannaschii


enzyme_display_name: lysine 2,3-aminomutase

substrate_name: L-lysine

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

enzyme: lysine 2,3-aminomutase

substrate: L-lysine


enzyme_display_name: lysine--tRNA ligase

substrate_name: Escherichia coli tRNALys CNBr-treated

enzyme: lysine--tRNA ligase

substrate: Escherichia coli tRNALys CNBr-treated


enzyme_display_name: serine--tRNA ligase

organism: Methanosarcina barkeri

substrate_name: tRNASer(GGA)

proof_lines:
pH 7.2, 37°C, bacterial type SerRS
pH 7.2, 37°C, methanogenic SerRS
methanogenic type seryl-tRNA synthetase

enzyme: serine--tRNA ligase

substrate: tRNASer(GGA)


enzyme_display_name: arachidonate--CoA ligase

organism: Rattus norvegicus

substrate_name: CoA

proof_lines:
pH 8, 37°C, 70-day-old rats
pH 8, 37°C, 10-day-old rats

enzyme: arachidonate--CoA ligase

substrate: CoA


substrate_name: ATP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: L-serine

substrate: L-serine


organism: Metallosphaera sedula

assay_conditions_summary: pH 7.9; 348.15 K; cofactor CoA


enzyme_display_name: O-phosphoserine--tRNA ligase

substrate_name: tRNACys

enzyme: O-phosphoserine--tRNA ligase

substrate: tRNACys


enzyme_display_name: proline--tRNA ligase

organism: Methanothermobacter thermautotrophicus

substrate_name: tRNAPro

proof_lines: presence of bovine serum albumine, 50°C, pH 7.5

proof_lines: presence of leucyl-tRNA synthetase, 50°C, pH 7.5

enzyme: proline--tRNA ligase

substrate: tRNAPro


enzyme_display_name: glutamate--tRNA ligase

substrate_name: tRNAGln(UUG)

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

enzyme: glutamate--tRNA ligase

substrate: tRNAGln(UUG)


enzyme_display_name: isopentenyl-diphosphate Delta-isomerase

substrate_name: isopentenyl diphosphate

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

enzyme: isopentenyl-diphosphate Delta-isomerase

substrate: isopentenyl diphosphate


enzyme_display_name: D-cysteine desulfhydrase

organism: Methylorubrum extorquens

substrate_name: D-cysteine

enzyme: D-cysteine desulfhydrase

substrate: D-cysteine


enzyme_display_name: methylmalonyl-CoA mutase

assay_conditions_summary: 310.15 K; cofactor CoA

proof_lines: presence of P-loop GTPase MeaB and GDP, 37°C

enzyme: methylmalonyl-CoA mutase


enzyme_display_name: methionine gamma-lyase

organism: Micromonospora echinospora

substrate_name: L-methionine

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

enzyme: methionine gamma-lyase

substrate: L-methionine


enzyme_display_name: medium-chain acyl-CoA ligase

organism: Mus musculus

substrate_name: Unknown

enzyme: medium-chain acyl-CoA ligase

substrate: Unknown


enzyme_display_name: pyrrolysine--tRNA(Pyl) ligase

organism: Methanosarcina thermophila

substrate_name: more

proof_lines: equilibrium binding analysis, dissociation constants of the enzyme with tRNAPyl from different species, overview

enzyme: pyrrolysine--tRNA(Pyl) ligase

substrate: more


enzyme_display_name: prostaglandin-D synthase

proof_lines: in the presence of 500 mM guanidinium hydrochloride

enzyme: prostaglandin-D synthase


enzyme_display_name: serine racemase

substrate_name: L-aspartate

enzyme: serine racemase

substrate: L-aspartate


enzyme_display_name: protoporphyrin ferrochelatase

substrate_name: protoporphyrin IX

proof_lines: mutant P255G, under strictly anaerobic conditions

enzyme: protoporphyrin ferrochelatase

substrate: protoporphyrin IX


enzyme_display_name: glutamine synthetase

enzyme: glutamine synthetase


enzyme_display_name: lactoylglutathione lyase

proof_lines: inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics, competitive inhibition, pH 7.0, 30°C

proof_lines: inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics from 0.5 to 2 microM, competitive inhibition, pH 7.0, 30°C

enzyme: lactoylglutathione lyase


proof_lines: pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction

proof_lines: pH 8.0, 37°C, presence of 1 mM ATP, racemization reaction


enzyme_display_name: plus-end-directed kinesin ATPase

proof_lines: recombinant K888 mutants S175A and S175D, pH and temperature not specified in the publication

enzyme: plus-end-directed kinesin ATPase


enzyme_display_name: peptidylprolyl isomerase

sequence_source: UniProtKB FASTA (Q9QUR7)

enzyme: peptidylprolyl isomerase


enzyme_display_name: aldose 1-epimerase

substrate_name: alpha-D-glucose

enzyme: aldose 1-epimerase

substrate: alpha-D-glucose


enzyme_display_name: cysteine-S-conjugate beta-lyase

enzyme: cysteine-S-conjugate beta-lyase


enzyme_display_name: long-chain-fatty-acid--CoA ligase

substrate_name: oleate

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

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: at pH 7.5, temperature not specified in the publication

enzyme: long-chain-fatty-acid--CoA ligase

substrate: oleate


enzyme_display_name: alanine racemase

organism: Mycobacterium avium

substrate_name: D-Ala

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

enzyme: alanine racemase

substrate: D-Ala


substrate_name: arachidonate

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

substrate: arachidonate


assay_conditions_summary: 298.15 K; cofactor ATP

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

proof_lines: KIF16B, at 25°C, pH not specified in the publication

proof_lines: KIF13B, at 25°C, pH not specified in the publication


organism: Mycobacterium tuberculosis

substrate_name: (R)-pantoate

substrate: (R)-pantoate


organism: Mimosa pudica

substrate_name: cystathionine

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

substrate: cystathionine


enzyme_display_name: triose-phosphate isomerase

substrate_name: D-glyceraldehyde 3-phosphate

enzyme: triose-phosphate isomerase

substrate: D-glyceraldehyde 3-phosphate


enzyme_display_name: adenylate cyclase

substrate_name: ATP

proof_lines: recombinant adenylyl cclase, in the presence of Mn2+

proof_lines: recombinant adenylyl cclase, in the presence of Mg2+

enzyme: adenylate cyclase

substrate: ATP


enzyme_display_name: ribose-5-phosphate isomerase

substrate_name: D-ribose 5-phosphate

enzyme: ribose-5-phosphate isomerase

substrate: D-ribose 5-phosphate


enzyme_display_name: DNA 3'-5' helicase

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines:
pH 7.5, in presence of 1 mM Ni2+
pH 7.5, in presence of 1 mM Mn2+
pH 7.5, in presence of 1 mM Co2+

enzyme: DNA 3'-5' helicase


proof_lines: pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate


enzyme_display_name: chorismate mutase

substrate_name: chorismate

enzyme: chorismate mutase

substrate: chorismate


enzyme_display_name: alpha-methylacyl-CoA racemase

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines: recombinant six-His tagged enzyme, 50 mM Tris-HCl, 0.2% octyl-beta-D-glucopyranoside, pH 8.0 at 37°C

proof_lines: recombinant enzyme, 50 mM Tris-HCl, 0.2% octyl-beta-D-glucopyranoside, pH 8.0 at 37°C

enzyme: alpha-methylacyl-CoA racemase


proof_lines: 4-[[2-(3,4-dimethoxyphenyl)ethyl]amino]-3-nitro-5-sulfamoylbenzoic acid shows the most potent inhibition with Ki value of 0.0057 mM against MtCM

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: UDP-galactopyranose mutase

proof_lines:
under reducing conditions
pH 7.5, 37°C, recombinant enzyme
under non-reducing (native) conditions

enzyme: UDP-galactopyranose mutase


enzyme_display_name: 3-oxocholest-4-en-26-oate--CoA ligase

enzyme: 3-oxocholest-4-en-26-oate--CoA ligase


substrate_name: (R)-pristanoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: (R)-pristanoyl-CoA


enzyme_display_name: o-succinylbenzoate--CoA ligase

proof_lines: versus ATP, pH and temperature not specified in the publication

proof_lines: versus 2-succinylbenzoate, pH and temperature not specified in the publication

enzyme: o-succinylbenzoate--CoA ligase


enzyme_display_name: coproporphyrin ferrochelatase

substrate_name: coproporphyrin III

enzyme: coproporphyrin ferrochelatase

substrate: coproporphyrin III


substrate_name: dihydroxyacetone phosphate

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

substrate: dihydroxyacetone phosphate


organism: Bacillus anthracis

proof_lines: pH 7.5, temperature not specified in the publication

proof_lines: kcat is 7.1 min(-1) with 3,4-DHBA as substrate. kcat is 9.1 min(-1) with ATP as substrate.

source_databases_merged: brenda uniprot


organism: Nitrosopumilus maritimus (strain SCM1)

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: UniProt P14900

organism: Escherichia coli

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P14900


enzyme_display_name: UniProt P9WJL3

enzyme: UniProt P9WJL3


substrate_name: meso-diaminopimelic acid

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

substrate: meso-diaminopimelic acid


organism: Pseudomonas aeruginosa (strain UCBPP-PA14)

substrate_name: salicylate

proof_lines: kcat is 74 min(-1) with salicylate as substrate.

substrate: salicylate


proof_lines: in 100 mM Tris-Tricine, pH 8.5, temperature not specified in the publication


substrate_name: acetate

substrate: acetate


substrate_name: propionate

substrate: propionate


enzyme_display_name: isochorismate synthase

enzyme: isochorismate synthase


organism: Erysipelothrix rhusiopathiae

substrate_name: L-alanine

proof_lines: pH 9.6, 37°C, recombinant mutant MurEEr(HDNR/DNPR)

substrate: L-alanine


assay_conditions_summary: pH 9.6; 310.15 K; cofactor ATP

proof_lines: pH 9.6, 37°C, recombinant His-tagged enzyme


organism: Thermotoga maritima


substrate_name: D-Lysine

substrate: D-Lysine


assay_conditions_summary: 341.15 K; cofactor ATP


substrate_name: L-ornithine

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

substrate: L-ornithine


enzyme_display_name: long-chain fatty acid adenylase/transferase FadD23

substrate_name: palmitate

smiles: CCCCCCCCCCCCCCCC(=O)O

assay_conditions_summary: pH 7

substrate: palmitate


substrate_name: laurate

smiles: CCCCCCCCCCCC(=O)[O-]

enzyme: long-chain fatty acid adenylase/transferase FadD23

substrate: laurate


enzyme_display_name: dihydrofolate synthase

organism: Serratia indica

proof_lines:
with addition of 100 mM K+
with addition of 7.5 mM K+

enzyme: dihydrofolate synthase


substrate_name: L-Glu

substrate: L-Glu


organism: Lathyrus oleraceus


substrate_name: ATP

substrate: ATP


substrate_name: Glu

substrate: Glu


organism: Lacticaseibacillus casei

substrate_name: D-Ala

substrate: D-Ala


organism: Streptococcus pyogenes


enzyme_display_name: enterobactin synthase

organism: Escherichia coli (strain K12)

substrate_name: L-serine

column_label: Table 2. Measured values of Km and kcat for L-serine, ATP, and some alternate substrates of EntF in the ATP-PPi exchange reaction^a Table 2, substrate row 'L-Serine': column 'Km (mM)' = 0.26; column 'kcat (min^-1)' = 760; column 'kcat/Km' = 2,900.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 760 min^-1 (printed column header 'kcat (min^-1)'; the same turnover number is printed again in the Results sentence and in the Abstract for L-serine); 760 / 60 = 12.666666666667 s^(-1). The exported value is 760.0 s^(-1), which is the printed minute-based number carried into a second-based field WITHOUT the 60-fold conversion. Km: the printed Table 2 cell is 0.26 mM, already the export unit; the exported value is 0.26 mM. kcat/Km: the printed Table 2 cell is 2,900 in the column's implied min^-1 mM^-1 (the header prints no unit literal); 2,900 / 60 = 48.333333333333 s^(-1)*mM^(-1); the exported value is 2923.076923076923 s^(-1)*mM^(-1), which is the bare quotient of the export's own unconverted kcat and its Km. The cited Table 2 row prints no fourth numeric column.

row_label: Table 2, substrate row 'L-Serine'

enzyme: enterobactin synthase

substrate: L-serine


column_label: Table 2. Measured values of Km and kcat for L-serine, ATP, and some alternate substrates of EntF in the ATP-PPi exchange reaction^a Table 2, substrate row 'ATP': column 'Km (mM)' = 0.75; column 'kcat (min^-1)' = 660; column 'kcat/Km' = 880.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 660 min^-1 (printed column header 'kcat (min^-1)'; the same turnover number is printed again in the Results sentence and in the Abstract for L-serine); 660 / 60 = 11 s^(-1). The exported value is 660.0 s^(-1), which is the printed minute-based number carried into a second-based field WITHOUT the 60-fold conversion. Km: the printed Table 2 cell is 0.75 mM, already the export unit; the exported value is 0.75 mM. kcat/Km: the printed Table 2 cell is 880 in the column's implied min^-1 mM^-1 (the header prints no unit literal); 880 / 60 = 14.666666666667 s^(-1)*mM^(-1); the exported value is 880.0 s^(-1)*mM^(-1), which is the bare quotient of the export's own unconverted kcat and its Km. The cited Table 2 row prints no fourth numeric column.

row_label: Table 2, substrate row 'ATP'


substrate_name: O-acetyl-L-serine

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

column_label: Table 2. Measured values of Km and kcat for L-serine, ATP, and some alternate substrates of EntF in the ATP-PPi exchange reaction^a Table 2, substrate row '(O)Ac-L-serine': column 'Km (mM)' = 5.0; column 'kcat (min^-1)' = 720; column 'kcat/Km' = 150.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 720 min^-1 (printed column header 'kcat (min^-1)'; the same turnover number is printed again in the Results sentence and in the Abstract for L-serine); 720 / 60 = 12 s^(-1). The exported value is 720.0 s^(-1), which is the printed minute-based number carried into a second-based field WITHOUT the 60-fold conversion. Km: the printed Table 2 cell is 5.0 mM, already the export unit; the exported value is 5.0 mM. kcat/Km: the printed Table 2 cell is 150 in the column's implied min^-1 mM^-1 (the header prints no unit literal); 150 / 60 = 2.5 s^(-1)*mM^(-1); the exported value is 144.0 s^(-1)*mM^(-1), which is the bare quotient of the export's own unconverted kcat and its Km. The cited Table 2 row prints no fourth numeric column.

row_label: Table 2, substrate row '(O)Ac-L-serine'

substrate: O-acetyl-L-serine


substrate_name: L-beta-chloroalanine

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

column_label: Table 2. Measured values of Km and kcat for L-serine, ATP, and some alternate substrates of EntF in the ATP-PPi exchange reaction^a Table 2, substrate row 'beta-Cl-L-alanine': column 'Km (mM)' = 8.0; column 'kcat (min^-1)' = 870; column 'kcat/Km' = 110.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 870 min^-1 (printed column header 'kcat (min^-1)'; the same turnover number is printed again in the Results sentence and in the Abstract for L-serine); 870 / 60 = 14.5 s^(-1). The exported value is 870.0 s^(-1), which is the printed minute-based number carried into a second-based field WITHOUT the 60-fold conversion. Km: the printed Table 2 cell is 8.0 mM, already the export unit; the exported value is 8.0 mM. kcat/Km: the printed Table 2 cell is 110 in the column's implied min^-1 mM^-1 (the header prints no unit literal); 110 / 60 = 1.833333333333 s^(-1)*mM^(-1); the exported value is 108.75 s^(-1)*mM^(-1), which is the bare quotient of the export's own unconverted kcat and its Km. The cited Table 2 row prints no fourth numeric column.

substrate: L-beta-chloroalanine


substrate_name: S-methyl-L-cysteine

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

column_label: Table 2. Measured values of Km and kcat for L-serine, ATP, and some alternate substrates of EntF in the ATP-PPi exchange reaction^a Table 2, substrate row '(S)methyl-L-cysteine': column 'Km (mM)' = 3.1; column 'kcat (min^-1)' = 38; column 'kcat/Km' = 12.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 38 min^-1 (printed column header 'kcat (min^-1)'; the same turnover number is printed again in the Results sentence and in the Abstract for L-serine); 38 / 60 = 0.633333333333 s^(-1). The exported value is 38.0 s^(-1), which is the printed minute-based number carried into a second-based field WITHOUT the 60-fold conversion. Km: the printed Table 2 cell is 3.1 mM, already the export unit; the exported value is 3.1 mM. kcat/Km: the printed Table 2 cell is 12 in the column's implied min^-1 mM^-1 (the header prints no unit literal); 12 / 60 = 0.2 s^(-1)*mM^(-1); the exported value is 12.258064516129032 s^(-1)*mM^(-1), which is the bare quotient of the export's own unconverted kcat and its Km. The cited Table 2 row prints no fourth numeric column.

substrate: S-methyl-L-cysteine


assay_conditions_summary: pH 7.8; 298.15 K; cofactor ATP

column_label: Table 1: Kinetic Parameters of EntE (Biochemistry 2010, 49(17):3648-3657), substrate row '3-hydroxybenzoic acid', wild-type EntE; column 'Km (uM)' = 70; column 'kcat (s-1)' = 0.30; column 'kcat/Km (M-1 s-1)' = 4.6 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.30 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.3 s^(-1); the exported value is 0.3 s^(-1). Km: printed Table 1 cell 70 uM; 70 / 1000 = 0.07 mM; the paper value is 0.07 mM; the exported value is 0.07 mM. kcat/Km: printed Table 1 cell 4.6 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.6 x 10^3 / 1000 = 4.6 s^-1 mM^-1; the paper value is 4.6 s^(-1)*mM^(-1); the exported value is 4.285714285714286 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate row '3-hydroxybenzoic acid', wild-type EntE: Km = 70 uM; kcat = 0.30 s-1; printed kcat/Km = 4.6 x 10^3 M-1 s-1.


substrate_name: salicylic acid

substrate: salicylic acid


assay_conditions_summary: pH 7.8; cofactor ATP

proof_lines: kcat is 0.3 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with 3-hydroxybenzoate as substrate (at pH 7.8 and 25 degrees Celsius). kcat is 0.8 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with salicylate as substrate (at pH


assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADH

column_label: Table 1: Kinetic Parameters of EntE (Biochemistry 2010, 49(17):3648-3657), substrate row 'DHB', wild-type EntE; column 'Km (uM)' = 2.5; column 'kcat (s-1)' = 2.8; column 'kcat/Km (M-1 s-1)' = 8.8 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.8 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 2.8 s^(-1); the exported value is 2.8 s^(-1). Km: printed Table 1 cell 2.5 uM; 2.5 / 1000 = 0.0025 mM; the paper value is 0.0025 mM; the exported value is 0.0025 mM. kcat/Km: printed Table 1 cell 8.8 x 10^5 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.8 x 10^5 / 1000 = 880 s^-1 mM^-1; the paper value is 880.0 s^(-1)*mM^(-1); the exported value is 1120.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate row 'DHB', wild-type EntE: Km = 2.5 uM; kcat = 2.8 s-1; printed kcat/Km = 8.8 x 10^5 M-1 s-1.

row_label: Table 1, substrate row 'DHB' (2,3-dihydroxybenzoic acid), wild-type EntE


substrate_name: 4-aminosalicylic acid

substrate: 4-aminosalicylic acid


organism: Lactobacillus casei

assay_conditions_summary: cofactor ATP


proof_lines: kcat is 25 min(-1) with 7,8-dihydropteroate as substrate (at 30 degrees Celsius).


substrate_name: ATP (in the assay for DHFS activity)

substrate: ATP (in the assay for DHFS activity)


substrate_name: glutamate (in the assay for DHFS activity)


organism: Nitrosopumilus maritimus

substrate_name: CoA

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

substrate: CoA


substrate_name: Butanoate

smiles: CCCC(=O)[O-]

substrate: Butanoate


enzyme_display_name: carnosine synthase

organism: Rattus norvegicus

substrate_name: beta-Ala

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

proof_lines:
olfactory bulb
spinal cord
cerebellum

enzyme: carnosine synthase

substrate: beta-Ala


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

proof_lines:
spinal cord
cerebellum
olfactory bulbs


enzyme_display_name: marinolic acid--CoA ligase

organism: Pseudoalteromonas sp. (strain SANK 73390)

substrate_name: pseudomonic acid A

proof_lines: kcat is 3.2 sec(-1) with pseudomonic acid C as substrate. kcat is 3.0 sec(-1) with pseudomonic acid A as substrate. kcat is 0.005 sec(-1) with octanoic acid as substrate.

enzyme: marinolic acid--CoA ligase

substrate: pseudomonic acid A


substrate_name: octanoic acid

smiles: CCCCCCCC(=O)O

substrate: octanoic acid


substrate_name: salicylate (at pH 7.8 and 25 degrees Celsius)


substrate_name: D-pantetheine (at pH 7.8 and 25 degrees Celsius)

smiles: CC(C)(CO)C(C(=O)NCCC(=O)NCCS)O


substrate_name: D-Glu

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

proof_lines: The optimum activity is at 11-16 mM for potassium phosphate and at 5 mM for Mg(2+).

substrate: D-Glu


substrate_name: UDP-N-acetylmuramoyl-L-alanine

substrate: UDP-N-acetylmuramoyl-L-alanine


organism: Pseudoalteromonas sp. SANK 73390

substrate_name: pseudomonic acid C

substrate: pseudomonic acid C


substrate_name: 4,5-dihydroisochorismate (at pH 7 and 37 degrees Celsius)

proof_lines: kcat is 600 min(-1) for isochorismatase activity with isochorismate as substrate (at pH 7 and 37 degrees Celsius). kcat is 540 min(-1) for isochorismatase activity with 3-[(1-carboxylatoethenyl)oxy]-cyclohepta-1,6-diene-1-carboxylate as sub


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

source_databases_merged: sabio_rk skid uniprot


substrate_name: UDP-N-acetylmuramoyl-L-Ala-D-Glu

substrate: UDP-N-acetylmuramoyl-L-Ala-D-Glu


organism: Mycobacterium tuberculosis

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

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


organism: Enterococcus faecalis


organism: Haemophilus influenzae


organism: Staphylococcus aureus


organism: Escherichia coli

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


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)


organism: Gallus gallus

substrate_name: L-Histidine; ATP; beta-Alanine

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

source_databases_merged: sabio_rk brenda uniprot

substrate: L-Histidine; ATP; beta-Alanine


organism: Homo sapiens

substrate_name: L-Histidine; beta-Alanine; ATP

substrate: L-Histidine; beta-Alanine; ATP


organism: Mus musculus


substrate_name: ATP; L-Histidine; beta-Alanine

substrate: ATP; L-Histidine; beta-Alanine


substrate_name: ATP; L-Glutamate; Dihydropteroate

substrate: ATP; L-Glutamate; Dihydropteroate


organism: Plasmodium falciparum

substrate_name: Unknown

substrate: Unknown


organism: Nostoc sp. PCC 7120 = FACHB-418

substrate_name: DL-meso-diaminopimelic acid

proof_lines:
untagged enzyme, at pH 7.6 and 37°C
His-tagged enzyme, at pH 7.6 and 37°C

substrate: DL-meso-diaminopimelic acid


organism: Physcomitrium patens

proof_lines:
His-tagged enzyme, at pH 7.6 and 37°C
untagged enzyme, at pH 7.6 and 37°C


substrate_name: phosphopantetheinylated EntB

column_label: Table 1: Kinetic Parameters of EntE (Biochemistry 2010, 49(17):3648-3657), substrate row 'holo-EntB-ArCP', wild-type EntE; column 'Km (uM)' = 2.9; column 'kcat (s-1)' = 2.8; column 'kcat/Km (M-1 s-1)' = 9.8 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.8 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 2.8 s^(-1); the exported value is 2.8 s^(-1). Km: printed Table 1 cell 2.9 uM; 2.9 / 1000 = 0.0029 mM; the paper value is 0.0029 mM; the exported value is 0.0004 mM. kcat/Km: printed Table 1 cell 9.8 x 10^5 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9.8 x 10^5 / 1000 = 980 s^-1 mM^-1; the paper value is 980.0 s^(-1)*mM^(-1); the catalog row carries no efficiency value.

raw_value_unit_evidence: Table 1, substrate row 'holo-EntB-ArCP', wild-type EntE: Km = 2.9 uM; kcat = 2.8 s-1; printed kcat/Km = 9.8 x 10^5 M-1 s-1.

row_label: Table 1, substrate row 'holo-EntB-ArCP' (phosphopantetheinylated EntB-ArCP), wild-type EntE

substrate: phosphopantetheinylated EntB


substrate_name: D-Glutamate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature K115A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9.4; 310.15 K; buffer 0.1 M Tris-HCl; cofactor ATP

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row K115A; column kcat (min^-1) = 0.26; column Km D-Glu (uM) = 128; column kcat/Km D-Glu (min^-1 uM^-1) = 0.0020.

raw_value_unit_evidence: Table 2, protein row K115A, D-Glu column group: kcat = 0.26 min^-1; Km D-Glu = 128 uM; printed kcat/Km D-Glu = 0.0020 min^-1 uM^-1.

table_label: Table 2: Kinetic Constants of the MurD Mutant Proteins (Biochemistry 1999, 38(38):12240-12247)

substrate: D-Glutamate


sequence_variant_note: Mutation signature K198A matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -8, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature N268A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row N268A; column kcat (min^-1) = 307; column Km D-Glu (uM) = 264; column kcat/Km D-Glu (min^-1 uM^-1) = 1.16.

raw_value_unit_evidence: Table 2, protein row N268A, D-Glu column group: kcat = 307 min^-1; Km D-Glu = 264 uM; printed kcat/Km D-Glu = 1.16 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature N271A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row N271A; column kcat (min^-1) = 18; column Km D-Glu (uM) = 53; column kcat/Km D-Glu (min^-1 uM^-1) = 0.34.

raw_value_unit_evidence: Table 2, protein row N271A, D-Glu column group: kcat = 18 min^-1; Km D-Glu = 53 uM; printed kcat/Km D-Glu = 0.34 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature R302A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row R302A; column kcat (min^-1) = 188; column Km D-Glu (uM) = 74; column kcat/Km D-Glu (min^-1 uM^-1) = 2.54.

raw_value_unit_evidence: Table 2, protein row R302A, D-Glu column group: kcat = 188 min^-1; Km D-Glu = 74 uM; printed kcat/Km D-Glu = 2.54 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature R425A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row R425A; column kcat (min^-1) = 32; column Km D-Glu (uM) = 5160; column kcat/Km D-Glu (min^-1 uM^-1) = 0.0062.

raw_value_unit_evidence: Table 2, protein row R425A, D-Glu column group: kcat = 32 min^-1; Km D-Glu = 5160 uM; printed kcat/Km D-Glu = 0.0062 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature Y194F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row Y194F; column kcat (min^-1) = 32; column Km D-Glu (uM) = 53; column kcat/Km D-Glu (min^-1 uM^-1) = 0.60.

raw_value_unit_evidence: Table 2, protein row Y194F, D-Glu column group: kcat = 32 min^-1; Km D-Glu = 53 uM; printed kcat/Km D-Glu = 0.60 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature D317A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row D317A; column kcat (min^-1) = 1.3; column Km UMA (uM) = 57; column kcat/Km UMA (min^-1 uM^-1) = 0.023.

raw_value_unit_evidence: Table 2, protein row D317A, UMA column group: kcat = 1.3 min^-1; Km UMA = 57 uM; printed kcat/Km UMA = 0.023 min^-1 uM^-1.


substrate_name: ATP

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row N271A; column kcat (min^-1) = 18; column Km ATP (uM) = 1580; column kcat/Km ATP (min^-1 uM^-1) = 0.011.

raw_value_unit_evidence: Table 2, protein row N271A, ATP column group: kcat = 18 min^-1; Km ATP = 1580 uM; printed kcat/Km ATP = 0.011 min^-1 uM^-1.

substrate: ATP


column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row R302A; column kcat (min^-1) = 188; column Km ATP (uM) = 2000; column kcat/Km ATP (min^-1 uM^-1) = 0.094.

raw_value_unit_evidence: Table 2, protein row R302A, ATP column group: kcat = 188 min^-1; Km ATP = 2000 uM; printed kcat/Km ATP = 0.094 min^-1 uM^-1.


column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row R425A; column kcat (min^-1) = 32; column Km ATP (uM) = 183; column kcat/Km ATP (min^-1 uM^-1) = 0.17.

raw_value_unit_evidence: Table 2, protein row R425A, ATP column group: kcat = 32 min^-1; Km ATP = 183 uM; printed kcat/Km ATP = 0.17 min^-1 uM^-1.


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


column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row Y194F; column kcat (min^-1) = 32; column Km ATP (uM) = 144; column kcat/Km ATP (min^-1 uM^-1) = 0.22.

raw_value_unit_evidence: Table 2, protein row Y194F, ATP column group: kcat = 32 min^-1; Km ATP = 144 uM; printed kcat/Km ATP = 0.22 min^-1 uM^-1.