column_label: Table 2: Kinetic parameters Vmax, Km, and kcat and deduced catalytic efficiency kcat/Km of reconstituted HCM subunits HcmA and wild-type HcmB incubated with 2-hydroxyisobutyryl-CoA and both 3-hydroxybutyryl-CoA enantiomers at pH 6.6 and 30 C (J. Biol. Chem. 2015, 290(15):9727-9737); variant block 'HcmA D117V', substrate row '2-Hydroxyisobutyryl-CoA'; column 'Km' in uM = 61.4; column 'kcat' in min^-1 = 2.68; column 'kcat/Km' in mM^-1 min^-1 = 43.6; column 'Vmax' in nmol min^-1 mg^-1 is printed for the same row.

raw_value_unit_evidence: Table 2, variant block 'HcmA D117V', substrate row '2-Hydroxyisobutyryl-CoA': Km = 61.4 uM; kcat = 2.68 min^-1; printed kcat/Km = 43.6 mM^-1 min^-1.


enzyme_display_name: 2-hydroxyisobutanoyl-CoA mutase

organism: Aquincola tertiaricarbonis

source_db: brenda

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_source: multiple

sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature D117V to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 6.6; cofactor CoA

proof_lines: pH 6.6, 30°C, mutant enzyme D117V (mutation in subunit HcmA)

data_origin: experimental

enzyme: 2-hydroxyisobutanoyl-CoA mutase

source: brenda


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:I3VE77 and applied mutation signature D117V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.6; 303.15 K; buffer 50 mM potassium phosphate; cofactor CoA

column_label: Table 3: Kinetic parameters Vmax, Km, and kcat and deduced catalytic efficiency kcat/Km of reconstituted HCM subunits HcmA and wild-type HcmB incubated with pivalyl- and isovaleryl-CoA at pH 6.6 and 30 C (J. Biol. Chem. 2015, 290(15):9727-9737); variant block 'HcmA D117V', substrate row 'Pivalyl-CoA'; column 'Km' in uM = 43.5; column 'kcat' in min^-1 = 8.37; column 'kcat/Km' in mM^-1 min^-1 = 192; column 'Vmax' in nmol min^-1 mg^-1 is printed for the same row.

raw_value_unit_evidence: Table 3, variant block 'HcmA D117V', substrate row 'Pivalyl-CoA': Km = 43.5 uM; kcat = 8.37 min^-1; printed kcat/Km = 192 mM^-1 min^-1.

status: corrected


substrate_name: pivalyl-CoA

source_db: uniprot

mutation_signature: Unknown

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

assay_conditions_summary: pH 6.6; 303.15 K; cofactor CoA

column_label: Table 3 | Wild-type HcmA | substrate Pivalyl-CoA | condition pH 6.6, 30 °C | Vmax 11.8 ± 0.73 nmol min^-1 mg^-1 | Km 374 ± 46 µM | kcat 0.98 ± 0.06 min^-1 | kcat/Km 2.6 ± 0.4 mM^-1 min^-1

row_label: Wild-type HcmA / Pivalyl-CoA

table_label: Table 3: kinetic parameters for pivalyl- and isovaleryl-CoA with reconstituted HCM

substrate: pivalyl-CoA

source: uniprot


substrate_name: isovaleryl-CoA

column_label: Table 3 | Wild-type HcmA | substrate Isovaleryl-CoA | condition pH 6.6, 30 °C | Vmax 8.20 ± 0.34 nmol min^-1 mg^-1 | Km 288 ± 18 µM | kcat 0.68 ± 0.03 min^-1 | kcat/Km 2.4 ± 0.2 mM^-1 min^-1

row_label: Wild-type HcmA / Isovaleryl-CoA

substrate: isovaleryl-CoA


raw_value_unit_evidence: Table 3 | Wild-type HcmA | substrate Pivalyl-CoA | condition pH 6.6, 30 °C | Vmax 11.8 ± 0.73 nmol min^-1 mg^-1 | Km 374 ± 46 µM | kcat 0.98 ± 0.06 min^-1 | kcat/Km 2.6 ± 0.4 mM^-1 min^-1


raw_value_unit_evidence: Table 3 | Wild-type HcmA | substrate Isovaleryl-CoA | condition pH 6.6, 30 °C | Vmax 8.20 ± 0.34 nmol min^-1 mg^-1 | Km 288 ± 18 µM | kcat 0.68 ± 0.03 min^-1 | kcat/Km 2.4 ± 0.2 mM^-1 min^-1


enzyme_display_name: D-psicose 3-epimerase

organism: Clostridium sp.

substrate_name: D-fructose

kcat_over_km_display: Not reported

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

proof_lines: pH 8.0, 65°C, in presence of 0.2 mM Co2+

enzyme: D-psicose 3-epimerase

substrate: D-fructose


enzyme_display_name: methylaspartate mutase

organism: Clostridium cochlearium

substrate_name: Unknown

kcat_display: Not reported

km_display: Not reported

ki_unit: mM

assay_conditions_summary: pH 7

proof_lines: pH and temperature not specified in the publication

enzyme: methylaspartate mutase

substrate: Unknown


enzyme_display_name: lysine 2,3-aminomutase

substrate_name: L-Lys

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

enzyme: lysine 2,3-aminomutase

substrate: L-Lys


organism: Clostridium subterminale

assay_conditions_summary: pH 8; 310.15 K; buffer 0.2 M Na-EPPS

proof_lines: at pH 8.0, 37°C, in 0.2 M Na-EPPS buffer


organism: Clostridium tetanomorphum

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


enzyme_display_name: steroid Delta-isomerase

organism: Comamonas testosteroni

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

proof_lines: 25°C, pH 6.5, solvent D2O, mutant enzyme D38A

proof_lines: 25°C, pH 8.5, solvent D2O, mutant enzyme D38A

proof_lines: 25°C, pH 6.5, solvent H2O, mutant enzyme D38A

enzyme: steroid Delta-isomerase


verification_status: unverified

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D38E to reconstruct the assayed variant sequence.

proof_lines:
mutant D38E, pH 7.0, 5.4°C
mutant D38E, pH 7.0, 10.3°C
mutant D38E, pH 7.0, 15.3°C

status: unverified


enzyme_display_name: UDP-galactopyranose mutase

organism: Corynebacterium diphtheriae

proof_lines: pH 7.0, temperature not specified in the publication

enzyme: UDP-galactopyranose mutase


proof_lines:
wild-type, pH 6.6, 30°C
pH 6.6, 30°C, wild-type enzyme


enzyme_display_name: (-)-kolavenyl diphosphate synthase

organism: Salvia divinorum

substrate_name: geranylgeranyl diphosphate

source_db: oed

enzyme: (-)-kolavenyl diphosphate synthase

substrate: geranylgeranyl diphosphate

source: oed


enzyme_display_name: UniProt P23971

organism: Bacillus subtilis

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P23971

source: skid


substrate_name: ATP

substrate: ATP


substrate_name: CoA

substrate: CoA


enzyme_display_name: UniProt B4EL89

organism: Burkholderia cenocepacia

enzyme: UniProt B4EL89


substrate_name: phenylacetate

substrate: phenylacetate


organism: Cucurbita pepo

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Cucurbita maxima


enzyme_display_name: Delta(3)-Delta(2)-enoyl-CoA isomerase

organism: Cucumis sativus

assay_conditions_summary: cofactor CoA

enzyme: Delta(3)-Delta(2)-enoyl-CoA isomerase


enzyme_display_name: peptidylprolyl isomerase

organism: Corynebacterium glutamicum

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: peptidylprolyl isomerase


enzyme_display_name: muconolactone Delta-isomerase

organism: Cupriavidus necator

enzyme: muconolactone Delta-isomerase


enzyme_display_name: alanine racemase

substrate_name: L-alanine

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

enzyme: alanine racemase

substrate: L-alanine


enzyme_display_name: benzoate--CoA ligase

organism: Anaerobic bacterium

substrate_name: benzoate

assay_conditions_summary: cofactor ATP

enzyme: benzoate--CoA ligase

substrate: benzoate


substrate_name: CoASH

substrate: CoASH


enzyme_display_name: dicarboxylate--CoA ligase

organism: Rattus norvegicus

enzyme: dicarboxylate--CoA ligase


substrate_name: dodecanedioic acid

smiles: C(CCCCCC(=O)O)CCCCC(=O)O

substrate: dodecanedioic acid


enzyme_display_name: phenylacetate--CoA ligase

organism: Penicillium chrysogenum

assay_conditions_summary: pH 8.5; 303.15 K; cofactor CoA

proof_lines: pH 8.5, 30°C, recombinant enzyme, with phenylacetic acid

proof_lines: pH 8.5, 30°C, recombinant enzyme, with trans-cinnamic acid

enzyme: phenylacetate--CoA ligase


assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP


substrate_name: Butyric acid

smiles: CCCC(=O)O

substrate: Butyric acid


substrate_name: trans-cinnamic acid

substrate: trans-cinnamic acid


substrate_name: myristic acid

smiles: CCCCCCCCCCCCCC(=O)O

substrate: myristic acid


substrate_name: propionic acid

smiles: CCC(=O)O

substrate: propionic acid


organism: Clarkia breweri


assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP


assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA


substrate_name: palmitate

smiles: CCCCCCCCCCCCCCCC(=O)O

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

substrate: palmitate


substrate_name: stearate

smiles: CCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: stearate


substrate_name: Phenoxyacetate

proof_lines:
recombinant enzyme, pH 7.5, 30°C
pH 8.5, 30°C, recombinant enzyme

substrate: Phenoxyacetate


substrate_name: caprylate

smiles: CCCCCCCC(=O)[O-]

substrate: caprylate


substrate_name: caproate

smiles: CCCCCC(=O)[O-]

substrate: caproate


proof_lines:
recombinant enzyme, pH 7.5, 30°C
pH 8.5, 30°C, recombinant enzyme
pH 6.8, 37°C


substrate_name: caprate

smiles: CCCCCCCCCC(=O)[O-]

substrate: caprate


organism: Petunia hybrida

assay_conditions_summary: pH 8.5; buffer 50 mM Tris/K phosphate/Na citrate; cofactor CoA

column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-4CL1', substrate (acid) row 't-Cinnamic'; column 'Km (uM)' prints 149.4; column 'Vmax (pkat mg^-1)' prints 14680; column 'kcat (s^-1)' prints 0.847; column 'kcat/Km (mM^-1 s^-1)' prints 6.43; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.847 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.847 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 149.4 uM; 149.4 / 1000 = 0.1494 mM; the exported value is 0.1494 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 6.43 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 6.43 s^-1 mM^-1. The exported ratio 5.669344042838018 s^(-1)*mM^(-1) is the quotient 0.847 / 0.1494 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 6.43 and kcat and Km are unchanged.


substrate_name: 4-coumaric acid

column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-4CL1', substrate (acid) row '4-Coumaric'; column 'Km (uM)' prints 16.4; column 'Vmax (pkat mg^-1)' prints 25797; column 'kcat (s^-1)' prints 1.488; column 'kcat/Km (mM^-1 s^-1)' prints 84.32; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.488 s^-1; already in s^-1, no unit conversion applies; the exported value is 1.488 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 16.4 uM; 16.4 / 1000 = 0.0164 mM; the exported value is 0.016399999999999998 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 84.32 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 84.32 s^-1 mM^-1. The exported ratio 90.73170731707319 s^(-1)*mM^(-1) is the quotient 1.488 / 0.016399999999999998 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 84.32 and kcat and Km are unchanged.

substrate: 4-coumaric acid


substrate_name: caffeic acid

column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-4CL1', substrate (acid) row 'Caffeic'; column 'Km (uM)' prints 47.8; column 'Vmax (pkat mg^-1)' prints 63200; column 'kcat (s^-1)' prints 3.645; column 'kcat/Km (mM^-1 s^-1)' prints 70.14; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.645 s^-1; already in s^-1, no unit conversion applies; the exported value is 3.645 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 47.8 uM; 47.8 / 1000 = 0.0478 mM; the exported value is 0.047799999999999995 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 70.14 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 70.14 s^-1 mM^-1. The exported ratio 76.25523012552301 s^(-1)*mM^(-1) is the quotient 3.645 / 0.047799999999999995 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 70.14 and kcat and Km are unchanged.

substrate: caffeic acid


substrate_name: ferulic acid

column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-4CL1', substrate (acid) row 'Ferulic'; column 'Km (uM)' prints 15.2; column 'Vmax (pkat mg^-1)' prints 41377; column 'kcat (s^-1)' prints 2.39; column 'kcat/Km (mM^-1 s^-1)' prints 145.37; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.39 s^-1; already in s^-1, no unit conversion applies; the exported value is 2.39 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 15.2 uM; 15.2 / 1000 = 0.0152 mM; the exported value is 0.0152 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 145.37 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 145.37 s^-1 mM^-1. The exported ratio 157.23684210526318 s^(-1)*mM^(-1) is the quotient 2.39 / 0.0152 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 145.37 and kcat and Km are unchanged.

substrate: ferulic acid


substrate_name: benzoic acid

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

substrate: benzoic acid


substrate_name: CoA

column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-4CL1', substrate (acid) row 'CoA'; column 'Km (uM)' prints 9.9; column 'Vmax (pkat mg^-1)' prints 8451; column 'kcat (s^-1)' prints 0.487; column 'kcat/Km (mM^-1 s^-1)' prints 49.46; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.487 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.487 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 9.9 uM; 9.9 / 1000 = 0.0099 mM; the exported value is 0.0099 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 49.46 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 49.46 s^-1 mM^-1. The exported ratio 49.19191919191918 s^(-1)*mM^(-1) is the quotient 0.487 / 0.0099 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 49.46 and kcat and Km are unchanged.

substrate: CoA


substrate_name: geranylgeranyl diphosphate

proof_lines: kcat is 0.88 sec(-1) with geranylgeranyl diphosphate as substrate.

source_databases_merged: brenda uniprot

substrate: geranylgeranyl diphosphate


organism: Geobacter metallireducens

substrate_name: benzoate

protein_accession_database: NCBI Protein

sequence_source: NCBI RefSeq protein WP_004513062.1

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

substrate: benzoate


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: phytanate--CoA ligase

organism: Homo sapiens

enzyme: phytanate--CoA ligase


organism: Thauera aromatica


enzyme_display_name: 4-hydroxybenzoate--CoA ligase

organism: Pseudomonas sp.

enzyme: 4-hydroxybenzoate--CoA ligase


organism: Bos taurus

substrate_name: ATP (with (R)-lipoate as substrate)

substrate: ATP (with (R)-lipoate as substrate)


organism: Rhodopseudomonas palustris

substrate_name: Coenzyme A; ATP; Benzoate

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

substrate: Coenzyme A; ATP; Benzoate


substrate_name: ATP; Coenzyme A; 4-Hydroxybenzoate

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

substrate: ATP; Coenzyme A; 4-Hydroxybenzoate


organism: Azoarcus evansii

substrate_name: ATP; Coenzyme A; Phenylacetic acid

substrate: ATP; Coenzyme A; Phenylacetic acid


verification_status: verified

assay_conditions_summary: pH 8; 304.15 K; cofactor CoA

column_label: Figure S11 caption gives row substrate BadA with 3-chlorobenzoate (3-Cl-BzO) with metric cells KM = 289 ± 23 µM and kcat = 0.33 ± 0.011 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 289 µM normalizes to 0.29 mM; kcat 0.33 s-1 normalizes to 0.33 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 0.33 / 0.29 = 1.1379310344827587 s^-1*mM^-1. Caption KM 289 uM = 0.289 mM is carried in the export rounded to 0.29 mM; caption kcat 0.33 s-1 is carried unrounded.

raw_value_unit_evidence: Figure S11 caption, row BadA with 3-chlorobenzoate (3-Cl-BzO): KM = 289 ± 23 µM and kcat = 0.33 ± 0.011 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 3-chlorobenzoate (3-Cl-BzO)

table_label: Supporting Information Figure S11

status: verified


column_label: Figure S6 caption gives row substrate BadA with 3-cyclohexen-1-carboxylate (3-Cyc) with metric cells KM = 56.2 ± 9.1 µM and kcat = 16 ± 1.03 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 56.2 µM normalizes to 0.056 mM; kcat 16.0 s-1 normalizes to 16.0 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 16.0 / 0.056 = 285.7142857142857 s^-1*mM^-1. Caption KM 56.2 uM = 0.0562 mM is carried in the export rounded to 0.056 mM; caption kcat 16 s-1 is carried unrounded.

raw_value_unit_evidence: Figure S6 caption, row BadA with 3-cyclohexen-1-carboxylate (3-Cyc): KM = 56.2 ± 9.1 µM and kcat = 16 ± 1.03 s-1. The caption prints no kcat/KM cell.

table_label: Supporting Information Figure S6


column_label: Figure S8 caption gives row substrate BadA with 3-fluorobenzoate (3-F-BzO) with metric cells KM = 73 ± 11 µM and kcat = 35 ± 1.45 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 73 µM normalizes to 0.073 mM; kcat 35.0 s-1 normalizes to 35.0 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 35.0 / 0.073 = 479.45205479452056 s^-1*mM^-1. Caption KM 73 uM = 0.073 mM and caption kcat 35 s-1 are carried in the export unrounded.

raw_value_unit_evidence: Figure S8 caption, row BadA with 3-fluorobenzoate (3-F-BzO): KM = 73 ± 11 µM and kcat = 35 ± 1.45 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 3-fluorobenzoate (3-F-BzO)

table_label: Supporting Information Figure S8


column_label: Figure S3 caption gives row substrate BadA with 3-Furoate (3-Fur) with metric cells KM = 70.8 ± 12.3 µM and kcat = 6.74 ± 0.48 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 70.8 µM normalizes to 0.071 mM; kcat 6.7 s-1 normalizes to 6.7 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 6.7 / 0.071 = 94.3661971830986 s^-1*mM^-1. Caption KM 70.8 uM = 0.0708 mM and caption kcat 6.74 s-1 are carried in the export rounded to 0.071 mM and 6.7 s^-1.

raw_value_unit_evidence: Figure S3 caption, row BadA with 3-Furoate (3-Fur): KM = 70.8 ± 12.3 µM and kcat = 6.74 ± 0.48 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 3-Furoate (3-Fur)

table_label: Supporting Information Figure S3


column_label: Figure S20 caption gives row substrate BadA with 3-methylbenzoate (3-Me-BzO) with metric cells KM = 215 ± 25.6 µM and kcat = 0.54 ± 0.018 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 215 µM normalizes to 0.215 mM; kcat 0.54 s-1 normalizes to 0.54 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 0.54 / 0.215 = 2.511627906976744 s^-1*mM^-1. Caption KM 215 uM = 0.215 mM and caption kcat 0.54 s-1 are carried in the export unrounded.

raw_value_unit_evidence: Figure S20 caption, row BadA with 3-methylbenzoate (3-Me-BzO): KM = 215 ± 25.6 µM and kcat = 0.54 ± 0.018 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 3-methylbenzoate (3-Me-BzO)

table_label: Supporting Information Figure S20


column_label: Figure S15 caption gives row substrate BadA with 4-aminobenzoate (4-NH2-BzO) with metric cells KM = 25.3 ± 3.01 µM and kcat = 0.18 ± 0.0043 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 25.3 µM normalizes to 0.025 mM; kcat 0.18 s-1 normalizes to 0.18 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 0.18 / 0.025 = 7.199999999999999 s^-1*mM^-1. Caption KM 25.3 uM = 0.0253 mM is carried in the export rounded to 0.025 mM; caption kcat 0.18 s-1 is carried unrounded.

raw_value_unit_evidence: Figure S15 caption, row BadA with 4-aminobenzoate (4-NH2-BzO): KM = 25.3 ± 3.01 µM and kcat = 0.18 ± 0.0043 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 4-aminobenzoate (4-NH2-BzO)

table_label: Supporting Information Figure S15


column_label: Figure S12 caption gives row substrate BadA with 4-chlorobenzoate (4-Cl-BzO) with metric cells KM = 83.2 ± 11.1 µM and kcat = 0.29 ± 0.012 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 83.2 µM normalizes to 0.083 mM; kcat 0.29 s-1 normalizes to 0.29 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 0.29 / 0.083 = 3.4939759036144573 s^-1*mM^-1. Caption KM 83.2 uM = 0.0832 mM is carried in the export rounded to 0.083 mM; caption kcat 0.29 s-1 is carried unrounded.

raw_value_unit_evidence: Figure S12 caption, row BadA with 4-chlorobenzoate (4-Cl-BzO): KM = 83.2 ± 11.1 µM and kcat = 0.29 ± 0.012 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 4-chlorobenzoate (4-Cl-BzO)

table_label: Supporting Information Figure S12


column_label: Figure S9 caption gives row substrate BadA with 4-fluorobenzoate (4-F-BzO) with metric cells KM = 6.6 ± 0.9 µM and kcat = 22 ± 0.66 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 6.6 µM normalizes to 0.0066 mM; kcat 22.0 s-1 normalizes to 22.0 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 22.0 / 0.0066 = 3333.3333333333335 s^-1*mM^-1. Caption KM 6.6 uM = 0.0066 mM and caption kcat 22 s-1 are carried in the export unrounded.

raw_value_unit_evidence: Figure S9 caption, row BadA with 4-fluorobenzoate (4-F-BzO): KM = 6.6 ± 0.9 µM and kcat = 22 ± 0.66 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 4-fluorobenzoate (4-F-BzO)

table_label: Supporting Information Figure S9


column_label: Figure S21 caption gives row substrate BadA with 4-methylbenzoate (4-Me-BzO) with metric cells KM = 590 ± 73 µM and kcat = 0.7 ± 0.035 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 590 µM normalizes to 0.59 mM; kcat 0.7 s-1 normalizes to 0.7 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 0.7 / 0.59 = 1.1864406779661016 s^-1*mM^-1. Caption KM 590 uM = 0.59 mM and caption kcat 0.7 s-1 are carried in the export unrounded.

raw_value_unit_evidence: Figure S21 caption, row BadA with 4-methylbenzoate (4-Me-BzO): KM = 590 ± 73 µM and kcat = 0.7 ± 0.035 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 4-methylbenzoate (4-Me-BzO)

table_label: Supporting Information Figure S21


substrate_name: butyrate

smiles: CCCC(=O)[O-]

substrate: butyrate


substrate_name: decanoate

substrate: decanoate


substrate_name: hexanoate

substrate: hexanoate


substrate_name: laurate

smiles: CCCCCCCCCCCC(=O)[O-]

substrate: laurate


substrate_name: phenylacetate

substrate: phenylacetate


substrate_name: salicylate

substrate: salicylate


column_label: Figure S1 caption gives wild-type benzoate row KM=4.40 +/- 0.65 uM and kcat=27.5 +/- 0.87 s^-1; Figure S27 is Lys427Ala mutant and has kcat=0.05 s^-1, also not this no-mutation row

raw_value_unit_evidence: Figure S1 reports KM=4.40 +/- 0.65 uM and kcat=27.5 +/- 0.87 s^-1 for wild-type BadA

row_label: wild-type BadA with benzoate (BzO)

table_label: Supporting Information Figure S1


substrate_name: cyclohexane carboxylate

column_label: Figure S4 caption gives row substrate cyclohexane carboxylate and metric cells KM=1466 +/- 213 uM and kcat=13.5 +/- 1.07 s^-1

normalized_value_unit_evidence: KM=1.466 mM from 1466 uM; export rounded KM=1.47 mM; kcat=13.5 s^-1; export kcat/KM=9.183673469387756 s^-1*mM^-1 from rounded KM

row_label: BadA with cyclohexane carboxylate (Cyc)

table_label: Supporting Information Figure S4

substrate: cyclohexane carboxylate


column_label: Figure S2 caption gives row substrate thiophene-2-carboxylate and metric cells KM=37 +/- 5.7 uM and kcat=4.8 +/- 0.23 s^-1

raw_value_unit_evidence: Figure S2 reports KM=37 +/- 5.7 uM and kcat=4.8 +/- 0.23 s^-1

row_label: BadA with thiophene-2-carboxylate (Thio-2-C)

table_label: Supporting Information Figure S2


column_label: Figure S17 caption gives row substrate 3-hydroxybenzoate and metric cells KM=229 +/- 18 uM and kcat=1.8 +/- 0.04 s^-1

raw_value_unit_evidence: Figure S17 reports KM=229 +/- 18 uM and kcat=1.8 +/- 0.04 s^-1

row_label: BadA with 3-hydroxybenzoate (3-OH-BzO)

table_label: Supporting Information Figure S17


substrate_name: caprate

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

column_label: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Capric acid (C10)'; column 'Km mmol/L' = 0.070; column 'kcat s−1' = 0.102; column 'kcat/Km L mmol−1 s−1' = 1.455.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.070 mmol/L; 1 mmol/L is 1 mM, so the normalized value is 0.07 mM, which is the value the catalog carries. kcat: printed Table 3 cell 0.102 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 0.102 s^(-1), which is the value the catalog carries. kcat/Km: printed Table 3 cell 1.455 L mmol^-1 s^-1; L mmol^-1 s^-1 is the reciprocal of mmol/L per second, so it is already s^-1 mM^-1 and no unit conversion applies, giving 1.455 s^(-1)*mM^(-1). The catalog carries 1.4571428571428569 s^(-1)*mM^(-1), which is the plain quotient 0.102 / 0.070 = 1.4571428571428569 of the two component cells; the paper's own efficiency cell for this substrate is 1.455, an independently fitted primary value printed to three decimals, and it is proposed in place of the quotient.

raw_value_unit_evidence: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Capric acid (C10)': column 'Km mmol/L' prints 0.070; column 'kcat s−1' prints 0.102; column 'kcat/Km L mmol−1 s−1' prints 1.455.

row_label: Table 3, PhlC block, substrate row 'Capric acid (C10)'

table_label: Table 3: Apparent kinetic parameters of Phl, PhlB, and PhlC (Folia Microbiologica 2011, 56:246-252)

substrate: caprate


substrate_name: caproate

column_label: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Caproic acid (C6)'; column 'Km mmol/L' = 0.026; column 'kcat s−1' = 0.076; column 'kcat/Km L mmol−1 s−1' = 2.917.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.026 mmol/L; 1 mmol/L is 1 mM, so the normalized value is 0.026 mM, which is the value the catalog carries. kcat: printed Table 3 cell 0.076 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 0.076 s^(-1), which is the value the catalog carries. kcat/Km: printed Table 3 cell 2.917 L mmol^-1 s^-1; L mmol^-1 s^-1 is the reciprocal of mmol/L per second, so it is already s^-1 mM^-1 and no unit conversion applies, giving 2.917 s^(-1)*mM^(-1). The catalog carries 2.9230769230769234 s^(-1)*mM^(-1), which is the plain quotient 0.076 / 0.026 = 2.9230769230769234 of the two component cells; the paper's own efficiency cell for this substrate is 2.917, an independently fitted primary value printed to three decimals, and it is proposed in place of the quotient.

raw_value_unit_evidence: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Caproic acid (C6)': column 'Km mmol/L' prints 0.026; column 'kcat s−1' prints 0.076; column 'kcat/Km L mmol−1 s−1' prints 2.917.

row_label: Table 3, PhlC block, substrate row 'Caproic acid (C6)'

substrate: caproate


substrate_name: caprylate

column_label: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Caprylic acid (C8)'; column 'Km mmol/L' = 0.046; column 'kcat s−1' = 0.073; column 'kcat/Km L mmol−1 s−1' = 1.575.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.046 mmol/L; 1 mmol/L is 1 mM, so the normalized value is 0.046 mM, which is the value the catalog carries. kcat: printed Table 3 cell 0.073 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 0.073 s^(-1), which is the value the catalog carries. kcat/Km: printed Table 3 cell 1.575 L mmol^-1 s^-1; L mmol^-1 s^-1 is the reciprocal of mmol/L per second, so it is already s^-1 mM^-1 and no unit conversion applies, giving 1.575 s^(-1)*mM^(-1). The catalog carries 1.5869565217391304 s^(-1)*mM^(-1), which is the plain quotient 0.073 / 0.046 = 1.5869565217391304 of the two component cells; the paper's own efficiency cell for this substrate is 1.575, an independently fitted primary value printed to three decimals, and it is proposed in place of the quotient.

raw_value_unit_evidence: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Caprylic acid (C8)': column 'Km mmol/L' prints 0.046; column 'kcat s−1' prints 0.073; column 'kcat/Km L mmol−1 s−1' prints 1.575.

row_label: Table 3, PhlC block, substrate row 'Caprylic acid (C8)'

substrate: caprylate


substrate_name: palmitate

column_label: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Palmitic acid (C16)'; column 'Km mmol/L' = 0.092; column 'kcat s−1' = 0.026; column 'kcat/Km L mmol−1 s−1' = 0.283.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.092 mmol/L; 1 mmol/L is 1 mM, so the normalized value is 0.092 mM, which is the value the catalog carries. kcat: printed Table 3 cell 0.026 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 0.026 s^(-1), which is the value the catalog carries. kcat/Km: printed Table 3 cell 0.283 L mmol^-1 s^-1; L mmol^-1 s^-1 is the reciprocal of mmol/L per second, so it is already s^-1 mM^-1 and no unit conversion applies, giving 0.283 s^(-1)*mM^(-1) as the printed efficiency. The plain quotient of the two printed component cells is 0.026 / 0.092 = 0.2826086956521739 s^-1 mM^-1, which is the value the catalog carries, and the printed efficiency cell 0.283 is that same quotient written to the three decimals Table 3 prints.

raw_value_unit_evidence: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Palmitic acid (C16)': column 'Km mmol/L' prints 0.092; column 'kcat s−1' prints 0.026; column 'kcat/Km L mmol−1 s−1' prints 0.283.

row_label: Table 3, PhlC block, substrate row 'Palmitic acid (C16)'

substrate: palmitate


substrate_name: Phenoxyacetate

column_label: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Phenoxyacetic acid'; column 'Km mmol/L' = 0.257; column 'kcat s−1' = 0.063; column 'kcat/Km L mmol−1 s−1' = 0.247.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.257 mmol/L; 1 mmol/L is 1 mM, so the normalized value is 0.257 mM, which is the value the catalog carries. kcat: printed Table 3 cell 0.063 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 0.063 s^(-1), which is the value the catalog carries. kcat/Km: printed Table 3 cell 0.247 L mmol^-1 s^-1; L mmol^-1 s^-1 is the reciprocal of mmol/L per second, so it is already s^-1 mM^-1 and no unit conversion applies, giving 0.247 s^(-1)*mM^(-1). The catalog carries 0.245136186770428 s^(-1)*mM^(-1), which is the plain quotient 0.063 / 0.257 = 0.245136186770428 of the two component cells; the paper's own efficiency cell for this substrate is 0.247, an independently fitted primary value printed to three decimals, and it is proposed in place of the quotient.

raw_value_unit_evidence: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Phenoxyacetic acid': column 'Km mmol/L' prints 0.257; column 'kcat s−1' prints 0.063; column 'kcat/Km L mmol−1 s−1' prints 0.247.

row_label: Table 3, PhlC block, substrate row 'Phenoxyacetic acid'

substrate: Phenoxyacetate


column_label: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Phenylacetic acid'; column 'Km mmol/L' = 0.809; column 'kcat s−1' = 0.099; column 'kcat/Km L mmol−1 s−1' = 0.124.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.809 mmol/L; 1 mmol/L is 1 mM, so the normalized value is 0.809 mM, which is the value the catalog carries. kcat: printed Table 3 cell 0.099 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 0.099 s^(-1), which is the value the catalog carries. kcat/Km: printed Table 3 cell 0.124 L mmol^-1 s^-1; L mmol^-1 s^-1 is the reciprocal of mmol/L per second, so it is already s^-1 mM^-1 and no unit conversion applies, giving 0.124 s^(-1)*mM^(-1). The catalog carries 0.12237330037082818 s^(-1)*mM^(-1), which is the plain quotient 0.099 / 0.809 = 0.12237330037082818 of the two component cells; the paper's own efficiency cell for this substrate is 0.124, an independently fitted primary value printed to three decimals, and it is proposed in place of the quotient.

raw_value_unit_evidence: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Phenylacetic acid': column 'Km mmol/L' prints 0.809; column 'kcat s−1' prints 0.099; column 'kcat/Km L mmol−1 s−1' prints 0.124.

row_label: Table 3, PhlC block, substrate row 'Phenylacetic acid'


substrate_name: stearate

column_label: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Stearic acid (C18)'; column 'Km mmol/L' = 0.841; column 'kcat s−1' = 0.062; column 'kcat/Km L mmol−1 s−1' = 0.074.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.841 mmol/L; 1 mmol/L is 1 mM, so the normalized value is 0.841 mM, which is the value the catalog carries. kcat: printed Table 3 cell 0.062 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 0.062 s^(-1), which is the value the catalog carries. kcat/Km: printed Table 3 cell 0.074 L mmol^-1 s^-1; L mmol^-1 s^-1 is the reciprocal of mmol/L per second, so it is already s^-1 mM^-1 and no unit conversion applies, giving 0.074 s^(-1)*mM^(-1) as the printed efficiency. The plain quotient of the two printed component cells is 0.062 / 0.841 = 0.0737217598097503 s^-1 mM^-1, which is the value the catalog carries, and the printed efficiency cell 0.074 is that same quotient written to the three decimals Table 3 prints.

raw_value_unit_evidence: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Stearic acid (C18)': column 'Km mmol/L' prints 0.841; column 'kcat s−1' prints 0.062; column 'kcat/Km L mmol−1 s−1' prints 0.074.

row_label: Table 3, PhlC block, substrate row 'Stearic acid (C18)'

substrate: stearate


column_label: Figure S5 caption gives row substrate BadA with 1-cyclohexen-1-carboxylate (1-Cyc) with metric cells KM = 52 ± 7.1 µM and kcat = 5.6 ± 0.24 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 52 uM normalizes to 0.052 mM, carried in the export at its stored precision as 0.05 mM; kcat 5.6 s-1 normalizes to 5.6 s^-1, carried unrounded; kcat/KM is not printed by the paper, so it is the export-normalized quotient 5.6 / 0.05 = 111.99999999999999 s^-1*mM^-1.

raw_value_unit_evidence: Figure S5 caption, row BadA with 1-cyclohexen-1-carboxylate (1-Cyc): KM = 52 ± 7.1 µM and kcat = 5.6 ± 0.24 s-1. The caption prints no kcat/KM cell.

table_label: Supporting Information Figure S5


column_label: Figure S13 caption gives row substrate BadA with 2-aminobenzoate (2-NH2-BzO) with metric cells KM = 21 ± 2.3 µM and kcat = 3.9 ± 0.1 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 21 uM normalizes to 0.021 mM, carried in the export unrounded as 0.021 mM; kcat 3.9 s-1 normalizes to 3.9 s^-1, carried unrounded; kcat/KM is not printed by the paper, so it is the export-normalized quotient 3.9 / 0.021 = 185.7142857142857 s^-1*mM^-1.

raw_value_unit_evidence: Figure S13 caption, row BadA with 2-aminobenzoate (2-NH2-BzO): KM = 21 ± 2.3 µM and kcat = 3.9 ± 0.1 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 2-aminobenzoate (2-NH2-BzO)

table_label: Supporting Information Figure S13


column_label: Figure S10 caption gives row substrate BadA with 2-chlorobenzoate (2-Cl-BzO) with metric cells KM = 126 ± 12.3 µM and kcat = 2.21 ± 0.068 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 126 uM normalizes to 0.126 mM, carried in the export at its stored precision as 0.13 mM; kcat 2.21 s-1 normalizes to 2.21 s^-1, carried in the export at its stored precision as 2.2 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 2.2 / 0.13 = 16.923076923076923 s^-1*mM^-1.

raw_value_unit_evidence: Figure S10 caption, row BadA with 2-chlorobenzoate (2-Cl-BzO): KM = 126 ± 12.3 µM and kcat = 2.21 ± 0.068 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 2-chlorobenzoate (2-Cl-BzO)

table_label: Supporting Information Figure S10


column_label: Figure S22 caption gives row substrate BadA with 2-cyanobenzoate (2-CN-BzO) with metric cells KM = 213 ± 22 µM and kcat = 0.11 ± 0.0034 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 213 uM normalizes to 0.213 mM, carried in the export unrounded as 0.213 mM; kcat 0.11 s-1 normalizes to 0.11 s^-1, carried unrounded; kcat/KM is not printed by the paper, so it is the export-normalized quotient 0.11 / 0.213 = 0.5164319248826291 s^-1*mM^-1.

raw_value_unit_evidence: Figure S22 caption, row BadA with 2-cyanobenzoate (2-CN-BzO): KM = 213 ± 22 µM and kcat = 0.11 ± 0.0034 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 2-cyanobenzoate (2-CN-BzO)

table_label: Supporting Information Figure S22


column_label: Figure S7 caption gives row substrate BadA with 2-fluorobenzoate (2-F-BzO) with metric cells KM = 8.1 ± 0.91 µM and kcat = 34 ± 0.7 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 8.1 uM normalizes to 0.0081 mM, carried in the export unrounded as 0.0081 mM; kcat 34 s-1 normalizes to 34.0 s^-1, carried unrounded; kcat/KM is not printed by the paper, so it is the export-normalized quotient 34.0 / 0.0081 = 4197.530864197531 s^-1*mM^-1.

raw_value_unit_evidence: Figure S7 caption, row BadA with 2-fluorobenzoate (2-F-BzO): KM = 8.1 ± 0.91 µM and kcat = 34 ± 0.7 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 2-fluorobenzoate (2-F-BzO)

table_label: Supporting Information Figure S7


column_label: Figure S23 caption gives row substrate BadA with 2-methoxybenzoate (2-MeO-BzO) with metric cells KM = 789 ± 82 µM and kcat = 0.011 ± 0.00052 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 789 uM normalizes to 0.789 mM, carried in the export unrounded as 0.789 mM; kcat 0.011 s-1 normalizes to 0.011 s^-1, carried unrounded; kcat/KM is not printed by the paper, so it is the export-normalized quotient 0.011 / 0.789 = 0.013941698352344739 s^-1*mM^-1.

raw_value_unit_evidence: Figure S23 caption, row BadA with 2-methoxybenzoate (2-MeO-BzO): KM = 789 ± 82 µM and kcat = 0.011 ± 0.00052 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 2-methoxybenzoate (2-MeO-BzO)

table_label: Supporting Information Figure S23


column_label: Figure S19 caption gives row substrate BadA with 2-methylbenzoate (2-Me-BzO) with metric cells KM = 44 ± 6 µM and kcat = 1.2 ± 0.042 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 44 uM normalizes to 0.044 mM, carried in the export unrounded as 0.044 mM; kcat 1.2 s-1 normalizes to 1.2 s^-1, carried unrounded; kcat/KM is not printed by the paper, so it is the export-normalized quotient 1.2 / 0.044 = 27.272727272727273 s^-1*mM^-1.

raw_value_unit_evidence: Figure S19 caption, row BadA with 2-methylbenzoate (2-Me-BzO): KM = 44 ± 6 µM and kcat = 1.2 ± 0.042 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 2-methylbenzoate (2-Me-BzO)

table_label: Supporting Information Figure S19


column_label: Figure S24 caption gives row substrate BadA with 2-nitrobenzoate (2-NO2-BzO) with metric cells KM = 2015 ± 167 µM and kcat = 0.27 ± 0.011 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 2015 uM normalizes to 2.015 mM, carried in the export unrounded as 2.015 mM; kcat 0.27 s-1 normalizes to 0.27 s^-1, carried unrounded; kcat/KM is not printed by the paper, so it is the export-normalized quotient 0.27 / 2.015 = 0.13399503722084366 s^-1*mM^-1.

raw_value_unit_evidence: Figure S24 caption, row BadA with 2-nitrobenzoate (2-NO2-BzO): KM = 2015 ± 167 µM and kcat = 0.27 ± 0.011 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 2-nitrobenzoate (2-NO2-BzO)

table_label: Supporting Information Figure S24


column_label: Figure S14 caption gives row substrate BadA with 3-aminobenzoate (3-NH2-BzO) with metric cells KM = 174 ± 32 µM and kcat = 1.8 ± 0.1 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 174 uM normalizes to 0.174 mM, carried in the export unrounded as 0.174 mM; kcat 1.8 s-1 normalizes to 1.8 s^-1, carried unrounded; kcat/KM is not printed by the paper, so it is the export-normalized quotient 1.8 / 0.174 = 10.344827586206897 s^-1*mM^-1.

raw_value_unit_evidence: Figure S14 caption, row BadA with 3-aminobenzoate (3-NH2-BzO): KM = 174 ± 32 µM and kcat = 1.8 ± 0.1 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 3-aminobenzoate (3-NH2-BzO)

table_label: Supporting Information Figure S14


substrate_name: stearate (when expressed in bacteria)

substrate: stearate (when expressed in bacteria)


substrate_name: oleate (when expressed in bacteria)

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

substrate: oleate (when expressed in bacteria)


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)

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


organism: Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)

substrate_name: benzoate

substrate: benzoate


substrate_name: ATP

substrate: ATP


substrate_name: CoA

substrate: CoA


organism: Arabidopsis thaliana

substrate_name: trans-cinnamate

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

column_label: Table 2 (Kinetic Properties of Recombinant At4g19010), printed substrate row 't-Cinnamate': column 'K_m (uM)' = 112; column 'k_cat (s^-1)' = 0.7; column 'k_cat/K_m (s^-1 mM^-1)' = 6.

normalized_value_unit_evidence: K_m: printed Table 2 cell 112 uM; 1 uM is 0.001 mM, so 112 / 1000 = 0.112 mM, and the exported value is 0.112 mM. k_cat: printed Table 2 cell 0.7 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 0.7 s^(-1). k_cat/K_m: printed Table 2 cell 6 s^-1 mM^-1; the column head is already the export's own unit, so no unit conversion applies and the printed cell reads 6.0 s^-1 mM^-1. Quotient disclosure for this row: 0.7 / 0.112 = 6.249999999999999 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 2 uses.

raw_value_unit_evidence: Table 2, printed substrate row 't-Cinnamate': K_m = 112 uM; k_cat = 0.7 s^-1; printed k_cat/K_m = 6 s^-1 mM^-1.

table_label: Table 2: Kinetic Properties of Recombinant At4g19010 (The Plant Cell 2014, volume 26, number 5, pages 1938-1948); printed column heads K_m (uM), k_cat (s^-1) and k_cat/K_m (s^-1 mM^-1)

substrate: trans-cinnamate


substrate_name: p-coumarate

column_label: Table 2 (Kinetic Properties of Recombinant At4g19010), printed substrate row 'p-Coumarate': column 'K_m (uM)' = 125; column 'k_cat (s^-1)' = 2.1; column 'k_cat/K_m (s^-1 mM^-1)' = 17.

normalized_value_unit_evidence: K_m: printed Table 2 cell 125 uM; 1 uM is 0.001 mM, so 125 / 1000 = 0.125 mM, and the exported value is 0.125 mM. k_cat: printed Table 2 cell 2.1 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 2.1 s^(-1). k_cat/K_m: printed Table 2 cell 17 s^-1 mM^-1; the column head is already the export's own unit, so no unit conversion applies and the printed cell reads 17.0 s^-1 mM^-1. Quotient disclosure for this row: 2.1 / 0.125 = 16.8 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 2 uses.

raw_value_unit_evidence: Table 2, printed substrate row 'p-Coumarate': K_m = 125 uM; k_cat = 2.1 s^-1; printed k_cat/K_m = 17 s^-1 mM^-1.

substrate: p-coumarate


substrate_name: ferulate

column_label: Table 2 (Kinetic Properties of Recombinant At4g19010), printed substrate row 'Ferulate': column 'K_m (uM)' = 113; column 'k_cat (s^-1)' = 3.6; column 'k_cat/K_m (s^-1 mM^-1)' = 32.

normalized_value_unit_evidence: K_m: printed Table 2 cell 113 uM; 1 uM is 0.001 mM, so 113 / 1000 = 0.113 mM, and the exported value is 0.113 mM. k_cat: printed Table 2 cell 3.6 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 3.6 s^(-1). k_cat/K_m: printed Table 2 cell 32 s^-1 mM^-1; the column head is already the export's own unit, so no unit conversion applies and the printed cell reads 32.0 s^-1 mM^-1. Quotient disclosure for this row: 3.6 / 0.113 = 31.858407079646017 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 2 uses.

raw_value_unit_evidence: Table 2, printed substrate row 'Ferulate': K_m = 113 uM; k_cat = 3.6 s^-1; printed k_cat/K_m = 32 s^-1 mM^-1.

substrate: ferulate


substrate_name: caffeate

column_label: Table 2 (Kinetic Properties of Recombinant At4g19010), printed substrate row 'Caffeate': column 'K_m (uM)' = 85; column 'k_cat (s^-1)' = 2.4; column 'k_cat/K_m (s^-1 mM^-1)' = 28.

normalized_value_unit_evidence: K_m: printed Table 2 cell 85 uM; 1 uM is 0.001 mM, so 85 / 1000 = 0.085 mM, and the exported value is 0.085 mM. k_cat: printed Table 2 cell 2.4 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 2.4 s^(-1). k_cat/K_m: printed Table 2 cell 28 s^-1 mM^-1; the column head is already the export's own unit, so no unit conversion applies and the printed cell reads 28.0 s^-1 mM^-1. Quotient disclosure for this row: 2.4 / 0.085 = 28.235294117647054 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 2 uses.

raw_value_unit_evidence: Table 2, printed substrate row 'Caffeate': K_m = 85 uM; k_cat = 2.4 s^-1; printed k_cat/K_m = 28 s^-1 mM^-1.

substrate: caffeate


column_label: Table 2 (Kinetic Properties of Recombinant At4g19010), printed substrate row '4-Hydroxybenzoate': column 'K_m (uM)' = 67; column 'k_cat (s^-1)' = 0.01; column 'k_cat/K_m (s^-1 mM^-1)' = 0.15.

normalized_value_unit_evidence: K_m: printed Table 2 cell 67 uM; 1 uM is 0.001 mM, so 67 / 1000 = 0.067 mM, and the exported value is 0.067 mM. k_cat: printed Table 2 cell 0.01 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 0.01 s^(-1). k_cat/K_m: printed Table 2 cell 0.15 s^-1 mM^-1; the column head is already the export's own unit, so no unit conversion applies and the printed cell reads 0.15 s^-1 mM^-1. Quotient disclosure for this row: 0.01 / 0.067 = 0.14925373134328357 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 2 uses.

raw_value_unit_evidence: Table 2, printed substrate row '4-Hydroxybenzoate': K_m = 67 uM; k_cat = 0.01 s^-1; printed k_cat/K_m = 0.15 s^-1 mM^-1.


substrate_name: (R)-lipoate with ATP as phosphate donor

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

substrate: (R)-lipoate with ATP as phosphate donor


substrate_name: hexanoate

substrate: hexanoate


substrate_name: ATP (with hexanoate as substrate)

substrate: ATP (with hexanoate as substrate)


organism: Magnetospirillum sp.

assay_conditions_summary: pH 9; cofactor CoA


assay_conditions_summary: pH 9; cofactor ATP


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


enzyme_display_name: o-succinylbenzoate--CoA ligase

organism: Mycolicibacterium phlei

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H341A to reconstruct the assayed variant sequence.

enzyme: o-succinylbenzoate--CoA ligase


substrate_name: CoASH

substrate: CoASH


organism: Anthoceros agrestis

assay_conditions_summary: pH 7.2; cofactor ATP

column_label: Table 2 Kinetic data for Aa4HBCL for its substrates 4HBA, CoA and ATP. Table 2, substrate row '4HBA', enzyme Aa4HBCL; column 'Km (uM)' = 664.2; column 'Kcat (1/s)' = 1.1; column 'kcat/Km (1/s mM)' = 1.7.

normalized_value_unit_evidence: Km: printed cell 664.2 uM; 664.2 / 1000 = 0.6642 mM; the exported value is 0.664 mM. kcat: printed cell 1.1 in the column headed 'Kcat (1/s)'; 1/s is s^(-1), no conversion; the exported value is 1.1 s^(-1). kcat/Km: printed cell 1.7 in the column headed 'kcat/Km (1/s mM)'; 1/s mM is s^(-1)*mM^(-1), no conversion; the exported value is 1.6566265060240963 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate row '4HBA', enzyme Aa4HBCL: Km = 664.2 uM; Kcat = 1.1 1/s; printed kcat/Km = 1.7 1/s mM.


column_label: Table 2 Kinetic data for Aa4HBCL for its substrates 4HBA, CoA and ATP. Table 2, substrate row 'ATP', enzyme Aa4HBCL; column 'Km (uM)' = 1175.3; column 'Kcat (1/s)' = 1.6; column 'kcat/Km (1/s mM)' = 1.3.

normalized_value_unit_evidence: Km: printed cell 1175.3 uM; 1175.3 / 1000 = 1.1753 mM; the exported value is 1.175 mM. kcat: printed cell 1.6 in the column headed 'Kcat (1/s)'; 1/s is s^(-1), no conversion; the exported value is 1.6 s^(-1). kcat/Km: printed cell 1.3 in the column headed 'kcat/Km (1/s mM)'; 1/s mM is s^(-1)*mM^(-1), no conversion; the exported value is 1.3617021276595744 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate row 'ATP', enzyme Aa4HBCL: Km = 1175.3 uM; Kcat = 1.6 1/s; printed kcat/Km = 1.3 1/s mM.


assay_conditions_summary: pH 7.2; cofactor CoA

column_label: Table 2 Kinetic data for Aa4HBCL for its substrates 4HBA, CoA and ATP. Table 2, substrate row 'CoA', enzyme Aa4HBCL; column 'Km (uM)' = 247.8; column 'Kcat (1/s)' = 2.2; column 'kcat/Km (1/s mM)' = 8.7.

normalized_value_unit_evidence: Km: printed cell 247.8 uM; 247.8 / 1000 = 0.2478 mM; the exported value is 0.248 mM. kcat: printed cell 2.2 in the column headed 'Kcat (1/s)'; 1/s is s^(-1), no conversion; the exported value is 2.2 s^(-1). kcat/Km: printed cell 8.7 in the column headed 'kcat/Km (1/s mM)'; 1/s mM is s^(-1)*mM^(-1), no conversion; the exported value is 8.870967741935484 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate row 'CoA', enzyme Aa4HBCL: Km = 247.8 uM; Kcat = 2.2 1/s; printed kcat/Km = 8.7 1/s mM.


organism: Aromatoleum evansii

substrate_name: PA (aerobically at 37 degrees Celsius)

smiles: [Pa]

column_label: Primary-paper PMC Table 3 lists Km (uM) with PA = 14 in the aerobically induced isoenzyme column.

raw_value_unit_evidence: PA Km 14 uM

row_label: PA row under Km (uM) with / aerobically induced isoenzyme

table_label: Table 3: Characteristics of the PA-CoA ligase isoenzyme

substrate: PA (aerobically at 37 degrees Celsius)


substrate_name: CoA (aerobically at 37 degrees Celsius)

column_label: Primary-paper PMC Table 3 lists Km (uM) with CoA = 45 in the aerobically induced isoenzyme column.

raw_value_unit_evidence: CoA Km 45 uM

row_label: CoA row under Km (uM) with / aerobically induced isoenzyme

substrate: CoA (aerobically at 37 degrees Celsius)


substrate_name: ATP (aerobically at 37 degrees Celsius)

column_label: Primary-paper PMC Table 3 lists Km (uM) with ATP = 60 in the aerobically induced isoenzyme column.

raw_value_unit_evidence: ATP Km 60 uM

row_label: ATP row under Km (uM) with / aerobically induced isoenzyme

substrate: ATP (aerobically at 37 degrees Celsius)


assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP


substrate_name: Coenzyme A

substrate: Coenzyme A


substrate_name: phenylacetic acid

substrate: phenylacetic acid


organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

substrate_name: ATP (at 50 degrees Celsius and pH 7.5)

column_label: Rendered page 31 and PDF text state apparent Km values for phenylacetate, CoA, and ATP were 6, 30, and 50 uM, respectively.

normalized_value_unit_evidence: Full-text body normalized ATP Km=0.05 mM; CatLog row=0.006 mM.

raw_value_unit_evidence: Full-text body: ATP maps to 50 uM in the phenylacetate, CoA, ATP order; abstract/UniProt instead map ATP to 6 uM.

row_label: apparent Km values sentence; substrate ATP

table_label: PMID 18414813 Springer PDF page 31 body text

substrate: ATP (at 50 degrees Celsius and pH 7.5)


substrate_name: CoA (at 50 degrees Celsius and pH 7.5)

substrate: CoA (at 50 degrees Celsius and pH 7.5)


substrate_name: PA (at 50 degrees Celsius and pH 7.5)

normalized_value_unit_evidence: Full-text body normalized PA Km=0.006 mM; CatLog row=0.05 mM.

raw_value_unit_evidence: Full-text body: phenylacetate maps to 6 uM in the phenylacetate, CoA, ATP order; abstract/UniProt instead map phenylacetate/PA to 50 uM.

row_label: apparent Km values sentence; substrate phenylacetate/PA

substrate: PA (at 50 degrees Celsius and pH 7.5)


substrate_name: hexadecanoate (palmitate)

smiles: CCCCCCCCCCCCCCCC(=O)[O-]

substrate: hexadecanoate (palmitate)


substrate_name: ATP

assay_conditions_summary: pH 7.8; cofactor ATP

column_label: Abstract reports apparent Km values for 4-hydroxybenzoate, ATP, and coenzyme A as 37 microM, 77 microM, and 125 microM respectively.

raw_value_unit_evidence: Km raw_value=77 microM raw_unit=microM

row_label: Pseudomonas sp. 4-hydroxybenzoate-CoA ligase / ATP

table_label: PubMed XML abstract PMID 8477728

substrate: ATP


substrate_name: coenzyme A

assay_conditions_summary: pH 7.8; cofactor CoA

raw_value_unit_evidence: Km raw_value=125 microM raw_unit=microM

row_label: Pseudomonas sp. 4-hydroxybenzoate-CoA ligase / coenzyme A

substrate: coenzyme A


organism: Mus musculus


substrate_name: octanoate

substrate: octanoate


organism: Pseudomonas putida

substrate_name: ATP (at 30 degrees Celsius and pH 8.2)

assay_conditions_summary: pH 8.2; 303.15 K; cofactor ATP

column_label: Primary PDF page 1 kinetic statement maps ATP to Km = 9.7 mM; page 2 results prose repeats the same ordered ATP, CoA, PAA Km values.

raw_value_unit_evidence: PDF page 1 kinetic statement: Km for ATP, CoA, and PAA are 9.7, 1.0, and 16.5 mM respectively; mapped row ATP to 9.7 mM by the ordered substrate list.

row_label: ATP

table_label: PMID 2324116 PDF page 1 article abstract/summary kinetic statement; repeated in page 2 results prose

substrate: ATP (at 30 degrees Celsius and pH 8.2)


substrate_name: CoA (at 30 degrees Celsius and pH 8.2)

assay_conditions_summary: pH 8.2; 303.15 K; cofactor CoA

column_label: Primary PDF page 1 kinetic statement maps CoA to Km = 1.0 mM; page 2 results prose repeats the same ordered ATP, CoA, PAA Km values.

raw_value_unit_evidence: PDF page 1 kinetic statement: Km for ATP, CoA, and PAA are 9.7, 1.0, and 16.5 mM respectively; mapped row CoA to 1.0 mM by the ordered substrate list.

row_label: CoA

substrate: CoA (at 30 degrees Celsius and pH 8.2)


substrate_name: PA (at 30 degrees Celsius and pH 8.2)

column_label: Primary PDF page 1 kinetic statement maps PAA / CatLog PA to Km = 16.5 mM; page 2 results prose repeats the same ordered ATP, CoA, PAA Km values.

raw_value_unit_evidence: PDF page 1 kinetic statement: Km for ATP, CoA, and PAA are 9.7, 1.0, and 16.5 mM respectively; mapped row PAA / CatLog PA to 16.5 mM by the ordered substrate list.

row_label: PAA / CatLog PA

substrate: PA (at 30 degrees Celsius and pH 8.2)


substrate_name: CoA

substrate: CoA


substrate_name: o-succinylbenzoate

substrate: o-succinylbenzoate


organism: Bacillus subtilis

assay_conditions_summary: pH 7.5; 297.15 K; cofactor CoA


assay_conditions_summary: pH 7.5; 297.15 K; cofactor ATP


proof_lines: pH 7.5, 24°C, recombinant wild-type enzyme


assay_conditions_summary: cofactor CoA


proof_lines: pH 8.0, 31°C, recombinant wild-type enzyme


substrate_name: benzoate

substrate: benzoate


organism: Burkholderia cenocepacia

proof_lines: pH and temperature not specified in the publication


substrate_name: phenylacetate

substrate: phenylacetate


organism: Bacillus anthracis

assay_conditions_summary: pH 7.5; 294.15 K; cofactor ATP

proof_lines: pH 7.5, 21°C, recombinant His-tagged enzyme


substrate_name: Unknown

proof_lines: pH 7.5, 21°C, versus ATP, recombinant enzyme

proof_lines: pH 7.5, 21°C, versus 2-succinylbenzoate, recombinant enzyme

proof_lines: pH 7.5, 21°C, versus CoA, recombinant enzyme

substrate: Unknown


assay_conditions_summary: 310.15 K; cofactor CoA


assay_conditions_summary: 310.15 K; cofactor ATP


organism: Escherichia coli

assay_conditions_summary: cofactor ATP


organism: Paraburkholderia xenovorans

assay_conditions_summary: pH 8


assay_conditions_summary: pH 8; cofactor CoA


assay_conditions_summary: pH 8; cofactor ATP


organism: Pseudomonas sp.


proof_lines:
anaerobically induced enzyme
2-fluorobenzoate
CoA


proof_lines:
anaerobically induced enzyme
coenzyme A
aerobically induced enzyme


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_390957.1 and applied mutation signature T155A/T156A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor CoA

column_label: Table 2 columns Protein, Substrate, kcat (min^-1), KM (uM), and kcat/KM (min^-1 M^-1); row matched by protein/mutation and substrate.

table_label: Table 2, The single substrate kinetic constants of wild-type and mutant BsMenE


assay_conditions_summary: pH 7.5; cofactor ATP


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_390957.1 and applied mutation signature T155A to reconstruct the assayed variant sequence.

row_label: T155A; ATP


row_label: T155A; CoA


row_label: T155A; OSB


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_390957.1 and applied mutation signature T152A to reconstruct the assayed variant sequence.

column_label: Table 2 columns Protein, Substrate, kcat, KM, and kcat/KM; row matched by mutant T152A and substrate ATP.

raw_value_unit_evidence: Table 2 row T152A ATP: kcat 8.1 min^-1; KM 3500 uM; kcat/KM 2300 min^-1 M^-1.

row_label: T152A; ATP

table_label: Table 2, single substrate kinetic constants of wild-type and mutant BsMenE


column_label: Table 2 columns Protein, Substrate, kcat, KM, and kcat/KM; row matched by mutant T152A and substrate OSB.

raw_value_unit_evidence: Table 2 row T152A OSB: kcat 8.2 min^-1; KM 880 uM; kcat/KM 9400 min^-1 M^-1.

row_label: T152A; OSB


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_390957.1 and applied mutation signature T156A to reconstruct the assayed variant sequence.

row_label: T156A; CoA


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_390957.1 and applied mutation signature R382A to reconstruct the assayed variant sequence.

column_label: Table 2 columns Protein, Substrate, kcat, KM, and kcat/KM; row matched by mutant R382A and substrate OSB.

raw_value_unit_evidence: Table 2 row R382A OSB: kcat 9 min^-1; KM 57 uM; kcat/KM 160000 min^-1 M^-1.

row_label: R382A; OSB


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_390957.1 and applied mutation signature R382K to reconstruct the assayed variant sequence.

column_label: Table 2 columns Protein, Substrate, kcat, KM, and kcat/KM; row matched by mutant R382K and substrate CoA.

raw_value_unit_evidence: Table 2 row R382K CoA: kcat 9.7 min^-1; KM 3000 uM; kcat/KM 3200 min^-1 M^-1.

row_label: R382K; CoA


row_label: R382K; ATP


column_label: Table 2 columns Protein, Substrate, kcat, KM, and kcat/KM; row matched by mutant T152A and substrate CoA.

raw_value_unit_evidence: Table 2 row T152A CoA: kcat 12.4 min^-1; KM 260 uM; kcat/KM 48000 min^-1 M^-1.

row_label: T152A; CoA


row_label: T156A; OSB


row_label: T156A; ATP


row_label: R382A; ATP


column_label: Table 2 columns Protein, Substrate, kcat, KM, and kcat/KM; row matched by mutant R382K and substrate OSB.

raw_value_unit_evidence: Table 2 row R382K OSB: kcat 13.7 min^-1; KM 66 uM; kcat/KM 210000 min^-1 M^-1.

row_label: R382K; OSB


column_label: Table 2 columns Protein, Substrate, kcat, KM, and kcat/KM; row matched by mutant R382A and substrate CoA.

raw_value_unit_evidence: Table 2 row R382A CoA: kcat 17 min^-1; KM 2700 uM; kcat/KM 6300 min^-1 M^-1.

row_label: R382A; CoA


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_390957.1 and applied mutation signature G154P to reconstruct the assayed variant sequence.

row_label: G154P; ATP


column_label: Table 2 columns Protein, Substrate, kcat, KM, and kcat/KM; row matched by mutant G154P and substrate OSB.

raw_value_unit_evidence: Table 2 row G154P OSB: kcat 130 min^-1; KM 120 uM; kcat/KM 1.1e+06 min^-1 M^-1.

row_label: G154P; OSB


organism: Rhodopseudomonas palustris


substrate_name: reduced CoA

substrate: reduced CoA


assay_conditions_summary: pH 7.8; 303.15 K; cofactor ATP


organism: Rattus norvegicus

substrate_name: phytanic acid

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

substrate: phytanic acid


organism: Thermus thermophilus

assay_conditions_summary: pH 7.8; 348.15 K; cofactor ATP


enzyme_display_name: 2-furoate--CoA ligase

enzyme: 2-furoate--CoA ligase


proof_lines:
anaerobically induced enzyme
benzoate, , aerobically induced enzyme


organism: Cupriavidus necator


enzyme_display_name: anthranilate--CoA ligase

assay_conditions_summary: 301.15 K; cofactor CoA

proof_lines:
28°C, isoenzyme E3
28°C, isoenzyme E2
isoenzyme E2

enzyme: anthranilate--CoA ligase


proof_lines:
isoenzyme E2
isoenzyme E3


proof_lines:
isoenzyme E3
isoenzyme E2


organism: Thauera aromatica


enzyme_display_name: 4-chlorobenzoate--CoA ligase

organism: Alcaligenes sp. AL3007

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8GN86 and applied mutation signature D402A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

column_label: Table 3: The steady-state kinetic constants kcat and Km measured for the CBL forms of this study in 50 mM K+HEPES (pH 7.5, 25 °C) containing 15 mM MgCl2 (Biochemistry 2009, 48(19):4115-4125); printed column heads CBL | Substrate | kcat (s-1) | KM (μM) | kcat/KM (s-1 M -1) | x-Fold decrease in kcat/KM. Table 3, enzyme row 'D402A', substrate row '4-CB'; column 'kcat (s-1)' = 0.96; column 'KM (μM)' = 2.3; column 'kcat/KM (s-1 M -1)' = 4 x 10^5. captured primary segment: D402A | 4-CB | kcat 0.96 s^-1 | Km 2.3 uM | kcat/Km 4 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 2.3 uM; 1 uM is 1/1000 mM, so 2.3 / 1000 = 0.0023 mM. kcat: printed Table 3 kcat cell 0.96 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.96 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 4 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4 x 10^5 / 1000 = 400.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.96 / 0.0023 = 417.39130434782606 s^-1 mM^-1, alongside the printed efficiency cell 400.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'D402A', substrate row '4-CB': kcat = 0.96 s^-1; KM = 2.3 uM; kcat/KM = 4 x 10^5 M^-1 s^-1.

enzyme: 4-chlorobenzoate--CoA ligase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D402A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8GN86 and applied mutation signature D402P to reconstruct the assayed variant sequence.

column_label: Table 3: The steady-state kinetic constants kcat and Km measured for the CBL forms of this study in 50 mM K+HEPES (pH 7.5, 25 °C) containing 15 mM MgCl2 (Biochemistry 2009, 48(19):4115-4125); printed column heads CBL | Substrate | kcat (s-1) | KM (μM) | kcat/KM (s-1 M -1) | x-Fold decrease in kcat/KM. Table 3, enzyme row 'D402P', substrate row 'ATP'; column 'kcat (s-1)' = 2.82 x 10^-2; column 'KM (μM)' = 13.1; column 'kcat/KM (s-1 M -1)' = 2 x 10^3. captured primary segment: D402P | ATP | kcat 2.82 x 10^-2 s^-1 | Km 13.1 uM | kcat/Km 2 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 13.1 uM; 1 uM is 1/1000 mM, so 13.1 / 1000 = 0.0131 mM. kcat: printed Table 3 kcat cell 2.82 x 10^-2 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.0282 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 2 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2 x 10^3 / 1000 = 2.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.0282 / 0.0131 = 2.1526717557251906 s^-1 mM^-1, alongside the printed efficiency cell 2.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'D402P', substrate row 'ATP': kcat = 2.82 x 10^-2 s^-1; KM = 13.1 uM; kcat/KM = 2 x 10^3 M^-1 s^-1.


column_label: Table 3: The steady-state kinetic constants kcat and Km measured for the CBL forms of this study in 50 mM K+HEPES (pH 7.5, 25 °C) containing 15 mM MgCl2 (Biochemistry 2009, 48(19):4115-4125); printed column heads CBL | Substrate | kcat (s-1) | KM (μM) | kcat/KM (s-1 M -1) | x-Fold decrease in kcat/KM. Table 3, enzyme row 'D402P', substrate row '4-CB'; column 'kcat (s-1)' = 3.4 x 10^-2; column 'KM (μM)' = 1.2; column 'kcat/KM (s-1 M -1)' = 3 x 10^4. captured primary segment: D402P | 4-CB | kcat 3.4 x 10^-2 s^-1 | Km 1.2 uM | kcat/Km 3 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 1.2 uM; 1 uM is 1/1000 mM, so 1.2 / 1000 = 0.0012 mM. kcat: printed Table 3 kcat cell 3.4 x 10^-2 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.034 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 3 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3 x 10^4 / 1000 = 30.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.034 / 0.0012 = 28.33333333333334 s^-1 mM^-1, alongside the printed efficiency cell 30.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'D402P', substrate row '4-CB': kcat = 3.4 x 10^-2 s^-1; KM = 1.2 uM; kcat/KM = 3 x 10^4 M^-1 s^-1.


column_label: Table 3: The steady-state kinetic constants kcat and Km measured for the CBL forms of this study in 50 mM K+HEPES (pH 7.5, 25 °C) containing 15 mM MgCl2 (Biochemistry 2009, 48(19):4115-4125); printed column heads CBL | Substrate | kcat (s-1) | KM (μM) | kcat/KM (s-1 M -1) | x-Fold decrease in kcat/KM. Table 3, enzyme row 'D402P', substrate row 'CoA'; column 'kcat (s-1)' = 3.7 x 10^-2; column 'KM (μM)' = 2000; column 'kcat/KM (s-1 M -1)' = 2 x 10^1. captured primary segment: D402P | CoA | kcat 3.7 x 10^-2 s^-1 | Km 2000 uM | kcat/Km 2 x 10^1 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 2000 uM; 1 uM is 1/1000 mM, so 2000 / 1000 = 2.0 mM. kcat: printed Table 3 kcat cell 3.7 x 10^-2 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.037 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 2 x 10^1 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2 x 10^1 / 1000 = 0.02 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.037 / 2.0 = 0.0185 s^-1 mM^-1, alongside the printed efficiency cell 0.02 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'D402P', substrate row 'CoA': kcat = 3.7 x 10^-2 s^-1; KM = 2000 uM; kcat/KM = 2 x 10^1 M^-1 s^-1.


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


column_label: Table 3: The steady-state kinetic constants kcat and Km measured for the CBL forms of this study in 50 mM K+HEPES (pH 7.5, 25 °C) containing 15 mM MgCl2 (Biochemistry 2009, 48(19):4115-4125); printed column heads CBL | Substrate | kcat (s-1) | KM (μM) | kcat/KM (s-1 M -1) | x-Fold decrease in kcat/KM. Table 3, enzyme row 'Wild type', substrate row 'CoA'; column 'kcat (s-1)' = 9.3; column 'KM (μM)' = 310; column 'kcat/KM (s-1 M -1)' = 3 x 10^4. captured primary segment: Wild type | CoA | kcat 9.3 s^-1 | Km 310 uM | kcat/Km 3 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 310 uM; 1 uM is 1/1000 mM, so 310 / 1000 = 0.31 mM. kcat: printed Table 3 kcat cell 9.3 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 9.3 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 3 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3 x 10^4 / 1000 = 30.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 9.3 / 0.31 = 30.000000000000004 s^-1 mM^-1, alongside the printed efficiency cell 30.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'Wild type', substrate row 'CoA': kcat = 9.3 s^-1; KM = 310 uM; kcat/KM = 3 x 10^4 M^-1 s^-1.


enzyme_display_name: 3-hydroxybenzoate--CoA ligase

organism: Centaurium erythraea

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

assay_conditions_summary: pH 7.5; 308.15 K; cofactor CoA

enzyme: 3-hydroxybenzoate--CoA ligase


assay_conditions_summary: pH 7.5; 308.15 K; cofactor ATP


enzyme_display_name: trans-feruloyl-CoA synthase

organism: Streptomyces sp

substrate_name: ferulate (at pH 7.0 and 30 degrees Celsius)

assay_conditions_summary: pH 7

column_label: PubMed abstract reports Fcs apparent Km = 0.35 mM for ferulic acid.

raw_value_unit_evidence: Km raw_value=0.35 mM raw_unit=mM

row_label: Fcs / ferulic acid Km

table_label: PubMed PMID 23840666 abstract

enzyme: trans-feruloyl-CoA synthase


substrate_name: Coenzyme A; 4-Chlorobenzoate; ATP

substrate: Coenzyme A; 4-Chlorobenzoate; ATP


enzyme_display_name: 3-hydroxypropionyl-CoA synthase

organism: Metallosphaera sedula

substrate_name: 3-Hydroxypropanoate; Coenzyme A; ATP

enzyme: 3-hydroxypropionyl-CoA synthase

substrate: 3-Hydroxypropanoate; Coenzyme A; ATP


organism: Sulfolobus tokodaii

substrate_name: ATP; Coenzyme A; 3-Hydroxypropanoate

substrate: ATP; Coenzyme A; 3-Hydroxypropanoate


substrate_name: 3-Hydroxybenzoate; ATP; Coenzyme A

substrate: 3-Hydroxybenzoate; ATP; Coenzyme A


organism: Arabidopsis thaliana


organism: Oryza sativa subsp. japonica

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 1.02 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 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


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


substrate_name: ferulic acid

assay_conditions_summary: pH 7; cofactor CoA

column_label: PubMed PMID 23840666 abstract prose, Fcs / ferulic acid Vmax value.

normalized_value_unit_evidence: Vmax=78.2 umol/min/mg.

raw_value_unit_evidence: The PubMed abstract reports Fcs Vmax 78.2 U mg-1 for ferulic acid.

row_label: Fcs / ferulic acid Vmax

substrate: ferulic acid


organism: Nicotiana tabacum

column_label: Table 2. Steady-State Kinetic Parameters for Nt4CL2 against Hydroxycinnamates; row 4-Coumaric acid / wild type; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); 4-Coumaric acid / wild type: kcat 3.978 +/- 0.252 s^-1; Km 1.5 +/- 0.4 uM; kcat/Km (2.652 +/- 0.168) x 10^6 M^-1 s^-1. Normalized directly by unit conversion to kcat=3.978 s^-1; Km=0.0015 mM; kcat/Km=2652.0 s^-1*mM^-1.

row_label: 4-Coumaric acid / wild type


substrate_name: (E)-caffeate

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

substrate: (E)-caffeate


substrate_name: (E)-ferulate

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: (E)-ferulate


substrate_name: (E)-sinapate

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 Sinapinic Acid; column KM (uM) = 1,321.9; column kcat (s^-1) = 0.018; column kcat/KM (M^-1 s^-1) = 13.617. captured primary segment: Nt4CL2 | Sinapinic Acid | Km 1,321.9 uM | kcat 0.018 s^-1 | kcat/Km 13.617 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 1,321.9 uM; 1321.9 / 1000 = 1.3219 mM. kcat: printed Table 2 cell 0.018 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 0.018 s^(-1). kcat/Km: printed Table 2 cell 13.617 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell becomes 0.013617 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.018 / 1.3219 = 0.01361676374914895 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate row Sinapinic Acid: KM = 1,321.9 uM; kcat = 0.018 s^-1; printed kcat/KM = 13.617 M^-1 s^-1.

row_label: Table 2, substrate row Sinapinic Acid

substrate: (E)-sinapate


row_label: Table 3, enzyme row 'D402A', substrate row '4-CB'

table_label: Table 3: The steady-state kinetic constants kcat and Km measured for the CBL forms of this study in 50 mM K+HEPES (pH 7.5, 25 °C) containing 15 mM MgCl2 (Biochemistry 2009, 48(19):4115-4125); printed column heads CBL | Substrate | kcat (s-1) | KM (μM) | kcat/KM (s-1 M -1) | x-Fold decrease in kcat/KM


row_label: Table 3, enzyme row 'D402P', substrate row '4-CB'


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D402A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: ATP


row_label: Table 3, enzyme row 'D402P', substrate row 'ATP'


substrate_name: CoA


row_label: Table 3, enzyme row 'D402P', substrate row 'CoA'


row_label: Table 3, enzyme row 'Wild type', substrate row 'CoA'


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E306Q with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G163I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G166I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K169M to reconstruct the assayed variant sequence.


substrate_name: Coenzyme A

substrate: Coenzyme A


organism: Pseudomonas sp. (strain CBS-3)


substrate_name: benzoate


smiles: O=C(O)CCO

assay_conditions_summary: pH 8.5; 318.15 K; cofactor CoA

column_label: Table 4; 3-Hydroxypropionate row; Apparent Km, kcat, and Apparent kcat/Km columns

normalized_value_unit_evidence: Central values normalize to Km = 0.18 mM; kcat = 5.7 s^-1; Apparent kcat/Km = 32 s^-1 mM^-1

raw_value_unit_evidence: Table 4 3-Hydroxypropionate row: Apparent Km = 0.18 +/- 0.03 mM; kcat = 5.7 +/- 0.3 s^-1; Apparent kcat/Km = 3.2 x 10^4 M^-1 s^-1 with printed uncertainty 0.2 in the scaled cell

table_label: Table 4. Substrate specificity of 3-hydroxypropionyl-CoA synthetase from Metallosphaera sedula


substrate_name: Acrylate

column_label: Table 4; Acrylate row; Apparent Km, kcat, and Apparent kcat/Km columns

normalized_value_unit_evidence: Central values normalize to Km = 1.42 mM; kcat = 5.4 s^-1; Apparent kcat/Km = 4 s^-1 mM^-1

raw_value_unit_evidence: Table 4 Acrylate row: Apparent Km = 1.42 +/- 0.20 mM; kcat = 5.4 +/- 0.2 s^-1; Apparent kcat/Km = 0.4 x 10^4 M^-1 s^-1 with printed uncertainty 0.04 in the scaled cell

row_label: Acrylate

substrate: Acrylate


substrate_name: propionate

column_label: Table 4; Propionate row; Apparent Km, kcat, and Apparent kcat/Km columns

normalized_value_unit_evidence: Central values normalize to Km = 0.12 mM; kcat = 5.6 s^-1; Apparent kcat/Km = 47 s^-1 mM^-1

raw_value_unit_evidence: Table 4 Propionate row: Apparent Km = 0.12 +/- 0.02 mM; kcat = 5.6 +/- 0.2 s^-1; Apparent kcat/Km = 4.7 x 10^4 M^-1 s^-1 with printed uncertainty 0.2 in the scaled cell

row_label: Propionate

substrate: propionate


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

assay_conditions_summary: cofactor CoA

column_label: PMC Table 4 row 3-Hydroxypropionate, column Apparent Km (mM), reports 0.18 +/- 0.03.

normalized_value_unit_evidence: Km normalized 0.18 mM.

raw_value_unit_evidence: Km raw 0.18 +/- 0.03 mM for 3-Hydroxypropionate.


assay_conditions_summary: cofactor ATP

column_label: PMC Table 3 row M. sedula, column Apparent Km value (uM), reports ATP, 45.

normalized_value_unit_evidence: Km normalized 0.045 mM.

raw_value_unit_evidence: Km raw 45 uM for ATP in the M. sedula apparent Km value cell.

row_label: M. sedula; ATP apparent Km entry

table_label: Table 3. Molecular and catalytic properties of 3-hydroxypropionyl-CoA synthetase from M. sedula and the recombinant enzyme from S. tokodaii


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

substrate_name: anthranilate

substrate: anthranilate


substrate: CoA


column_label: 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


substrate_name: caffeate

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

raw_value_unit_evidence: Km column reports 186 uM

row_label: Caffeate

substrate: caffeate


substrate_name: ferulate

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

raw_value_unit_evidence: Km column reports 26 uM

row_label: Ferulate

substrate: ferulate


substrate_name: sinapate

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

raw_value_unit_evidence: Km column reports 20 uM

row_label: Sinapate

substrate: sinapate


substrate_name: cinnamate

column_label: Table 1 / At4CL1 / Cinnamate / K m (uM): raw Km 6320 uM; normalized Km 6.32 mM.

raw_value_unit_evidence: Table 1 row At4CL1 / Cinnamate reports K m 6320 uM.

row_label: At4CL1 / Cinnamate

table_label: Table 1. Kinetic properties of recombinant Arabidopsis 4CLs

substrate: cinnamate


column_label: Table 1 / At4CL1 / 4-coumarate / K m (uM): raw Km 38 uM; normalized Km 0.038 mM.

raw_value_unit_evidence: Table 1 row At4CL1 / 4-coumarate reports K m 38 uM.

row_label: At4CL1 / 4-coumarate


column_label: Table 1 / At4CL1 / Caffeate / K m (uM): raw Km 11 uM; normalized Km 0.011 mM.

raw_value_unit_evidence: Table 1 row At4CL1 / Caffeate reports K m 11 uM.

row_label: At4CL1 / Caffeate


column_label: Table 1 / At4CL1 / Ferulate / K m (uM): raw Km 199 uM; normalized Km 0.199 mM.

raw_value_unit_evidence: Table 1 row At4CL1 / Ferulate reports K m 199 uM.

row_label: At4CL1 / Ferulate


column_label: Table 1 / At4CL3 / Cinnamate / K m (uM): raw Km 2070 uM; normalized Km 2.07 mM.

raw_value_unit_evidence: Table 1 row At4CL3 / Cinnamate reports K m 2070 uM.

row_label: At4CL3 / Cinnamate


column_label: Table 1 / At4CL3 / 4-coumarate / K m (uM): raw Km 23 uM; normalized Km 0.023 mM.

raw_value_unit_evidence: Table 1 row At4CL3 / 4-coumarate reports K m 23 uM.

row_label: At4CL3 / 4-coumarate


column_label: Table 1 / At4CL3 / Caffeate / K m (uM): raw Km 374 uM; normalized Km 0.374 mM.

raw_value_unit_evidence: Table 1 row At4CL3 / Caffeate reports K m 374 uM.

row_label: At4CL3 / Caffeate


column_label: Table 1 / At4CL3 / Ferulate / K m (uM): raw Km 166 uM; normalized Km 0.166 mM.

raw_value_unit_evidence: Table 1 row At4CL3 / Ferulate reports K m 166 uM.

row_label: At4CL3 / Ferulate


organism: Pseudomonas sp.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G163I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E306Q with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G166I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K169M to reconstruct the assayed variant sequence.


column_label: Table 1: Steady-State Kinetic Constants of Wild-Type and Mutant 4-CBA:CoA Ligase (Biochemistry 1997, 36, 15650-15659); enzyme row WT, substrate column 4-CBA; the kcat value 34 s-1 comes from the kcat (s-1) block of the 4-CBA column and the Michaelis constant 14 µM comes from the Km (µM) block of the same column. There is no kcat/Km column in this table.

normalized_value_unit_evidence: kcat: printed Table 1 cell 34 s-1; already in s^-1, no unit conversion applies, so the paper value is 34.0 s^(-1). Km: printed Table 1 cell 14 µM; 1 µM is 0.001 mM, so 14 / 1000 = 0.014 mM. kcat/Km: this article prints no kcat/Km cell for this measurement, so the exported 2428.5714285714284 s^(-1)*mM^(-1) is not a printed value; it is the quotient 34 / 0.014 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, enzyme row WT, 4-CBA column: kcat = 34 s-1 (printed in the kcat (s-1) block); Km = 14 µM (printed in the Km (µM) block). Table 1 has no kcat/Km column and this article prints no kcat/Km value for this measurement.

row_label: Table 1, row WT, 4-CBA column


column_label: Table 1: Steady-State Kinetic Constants of Wild-Type and Mutant 4-CBA:CoA Ligase (Biochemistry 1997, 36, 15650-15659); enzyme row WT, substrate column CoA; the kcat value 39 s-1 comes from the kcat (s-1) block of the CoA column and the Michaelis constant 85 µM comes from the Km (µM) block of the same column. There is no kcat/Km column in this table.

normalized_value_unit_evidence: kcat: printed Table 1 cell 39 s-1; already in s^-1, no unit conversion applies, so the paper value is 39.0 s^(-1). Km: printed Table 1 cell 85 µM; 1 µM is 0.001 mM, so 85 / 1000 = 0.085 mM. kcat/Km: this article prints no kcat/Km cell for this measurement, so the exported 458.8235294117647 s^(-1)*mM^(-1) is not a printed value; it is the quotient 39 / 0.085 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, enzyme row WT, CoA column: kcat = 39 s-1 (printed in the kcat (s-1) block); Km = 85 µM (printed in the Km (µM) block). Table 1 has no kcat/Km column and this article prints no kcat/Km value for this measurement.

row_label: Table 1, row WT, CoA column


column_label: Table 1: Steady-State Kinetic Constants of Wild-Type and Mutant 4-CBA:CoA Ligase (Biochemistry 1997, 36, 15650-15659); enzyme row WT, substrate column ATP; the kcat value 54 s-1 comes from the kcat (s-1) block of the ATP column and the Michaelis constant 308 µM comes from the Km (µM) block of the same column. There is no kcat/Km column in this table.

normalized_value_unit_evidence: kcat: printed Table 1 cell 54 s-1; already in s^-1, no unit conversion applies, so the paper value is 54.0 s^(-1). Km: printed Table 1 cell 308 µM; 1 µM is 0.001 mM, so 308 / 1000 = 0.308 mM. kcat/Km: this article prints no kcat/Km cell for this measurement, so the exported 175.32467532467533 s^(-1)*mM^(-1) is not a printed value; it is the quotient 54 / 0.308 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, enzyme row WT, ATP column: kcat = 54 s-1 (printed in the kcat (s-1) block); Km = 308 µM (printed in the Km (µM) block). Table 1 has no kcat/Km column and this article prints no kcat/Km value for this measurement.

row_label: Table 1, row WT, ATP column


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL4'; substrate row 'Cinnamate'; column 'Km (uM)' = 15.7; column 'Vmax (pkat mg^-1)' = 350; column 'Kcat (min^-1)' = 1.28; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 1361.

normalized_value_unit_evidence: Km: printed Table I cell 15.7 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 15.7 / 1000 = 0.0157 mM; the exported value is 0.0157 mM. kcat: printed Table I cell 1.28 min^-1 (the Kcat column header prints 'min^-1'); 1.28 / 60 = 0.021333333333333333 s^(-1); the exported value is 1.28 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 1361 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 1361 / 1000 = 1.361 s^(-1)*mM^(-1); the exported value is 81.52866242038218 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL4', substrate row 'Cinnamate': Km = 15.7 uM; Vmax = 350 pkat mg^-1; Kcat = 1.28 min^-1; printed Kenz = Kcat/Km = 1361 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL4', substrate row 'Cinnamate' (catalog accession Q67W82)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL4'; substrate row '4-Coumarate'; column 'Km (uM)' = 3.9; column 'Vmax (pkat mg^-1)' = 770; column 'Kcat (min^-1)' = 2.82; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 12176.

normalized_value_unit_evidence: Km: printed Table I cell 3.9 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 3.9 / 1000 = 0.0039 mM; the exported value is 0.0039 mM. kcat: printed Table I cell 2.82 min^-1 (the Kcat column header prints 'min^-1'); 2.82 / 60 = 0.047 s^(-1); the exported value is 2.82 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 12176 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 12176 / 1000 = 12.176 s^(-1)*mM^(-1); the exported value is 723.0769230769231 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL4', substrate row '4-Coumarate': Km = 3.9 uM; Vmax = 770 pkat mg^-1; Kcat = 2.82 min^-1; printed Kenz = Kcat/Km = 12176 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL4', substrate row '4-Coumarate' (catalog accession Q67W82)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL4'; substrate row 'Caffeate'; column 'Km (uM)' = 5.8; column 'Vmax (pkat mg^-1)' = 590; column 'Kcat (min^-1)' = 2.16; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 6206.

normalized_value_unit_evidence: Km: printed Table I cell 5.8 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 5.8 / 1000 = 0.0058 mM; the exported value is 0.0058 mM. kcat: printed Table I cell 2.16 min^-1 (the Kcat column header prints 'min^-1'); 2.16 / 60 = 0.036000000000000004 s^(-1); the exported value is 2.16 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 6206 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 6206 / 1000 = 6.206 s^(-1)*mM^(-1); the exported value is 372.4137931034483 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL4', substrate row 'Caffeate': Km = 5.8 uM; Vmax = 590 pkat mg^-1; Kcat = 2.16 min^-1; printed Kenz = Kcat/Km = 6206 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL4', substrate row 'Caffeate' (catalog accession Q67W82)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL4'; substrate row 'Ferulate'; column 'Km (uM)' = 4.6; column 'Vmax (pkat mg^-1)' = 520; column 'Kcat (min^-1)' = 1.92; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 6956.

normalized_value_unit_evidence: Km: printed Table I cell 4.6 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 4.6 / 1000 = 0.0046 mM; the exported value is 0.0046 mM. kcat: printed Table I cell 1.92 min^-1 (the Kcat column header prints 'min^-1'); 1.92 / 60 = 0.032 s^(-1); the exported value is 1.92 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 6956 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 6956 / 1000 = 6.956 s^(-1)*mM^(-1); the exported value is 417.39130434782606 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL4', substrate row 'Ferulate': Km = 4.6 uM; Vmax = 520 pkat mg^-1; Kcat = 1.92 min^-1; printed Kenz = Kcat/Km = 6956 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL4', substrate row 'Ferulate' (catalog accession Q67W82)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL3'; substrate row 'Cinnamate'; column 'Km (uM)' = 28.2; column 'Vmax (pkat mg^-1)' = 3010; column 'Kcat (min^-1)' = 10.92; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 6458.

normalized_value_unit_evidence: Km: printed Table I cell 28.2 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 28.2 / 1000 = 0.0282 mM; the exported value is 0.0282 mM. kcat: printed Table I cell 10.92 min^-1 (the Kcat column header prints 'min^-1'); 10.92 / 60 = 0.182 s^(-1); the exported value is 10.92 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 6458 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 6458 / 1000 = 6.458 s^(-1)*mM^(-1); the exported value is 387.2340425531915 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL3', substrate row 'Cinnamate': Km = 28.2 uM; Vmax = 3010 pkat mg^-1; Kcat = 10.92 min^-1; printed Kenz = Kcat/Km = 6458 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL3', substrate row 'Cinnamate' (catalog accession Q6ETN3)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL3'; substrate row '4-Coumarate'; column 'Km (uM)' = 4.9; column 'Vmax (pkat mg^-1)' = 4700; column 'Kcat (min^-1)' = 17.10; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 58521.

normalized_value_unit_evidence: Km: printed Table I cell 4.9 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 4.9 / 1000 = 0.004900000000000001 mM; the exported value is 0.004900000000000001 mM. kcat: printed Table I cell 17.10 min^-1 (the Kcat column header prints 'min^-1'); 17.10 / 60 = 0.28500000000000003 s^(-1); the exported value is 17.1 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 58521 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 58521 / 1000 = 58.521 s^(-1)*mM^(-1); the exported value is 3489.7959183673465 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL3', substrate row '4-Coumarate': Km = 4.9 uM; Vmax = 4700 pkat mg^-1; Kcat = 17.10 min^-1; printed Kenz = Kcat/Km = 58521 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL3', substrate row '4-Coumarate' (catalog accession Q6ETN3)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL3'; substrate row 'Caffeate'; column 'Km (uM)' = 10.9; column 'Vmax (pkat mg^-1)' = 4210; column 'Kcat (min^-1)' = 15.30; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 23330.

normalized_value_unit_evidence: Km: printed Table I cell 10.9 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 10.9 / 1000 = 0.0109 mM; the exported value is 0.0109 mM. kcat: printed Table I cell 15.30 min^-1 (the Kcat column header prints 'min^-1'); 15.30 / 60 = 0.255 s^(-1); the exported value is 15.3 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 23330 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 23330 / 1000 = 23.33 s^(-1)*mM^(-1); the exported value is 1403.6697247706422 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL3', substrate row 'Caffeate': Km = 10.9 uM; Vmax = 4210 pkat mg^-1; Kcat = 15.30 min^-1; printed Kenz = Kcat/Km = 23330 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL3', substrate row 'Caffeate' (catalog accession Q6ETN3)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL3'; substrate row 'Ferulate'; column 'Km (uM)' = 3.5; column 'Vmax (pkat mg^-1)' = 4930; column 'Kcat (min^-1)' = 17.94; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 84943.

normalized_value_unit_evidence: Km: printed Table I cell 3.5 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 3.5 / 1000 = 0.0035 mM; the exported value is 0.0035 mM. kcat: printed Table I cell 17.94 min^-1 (the Kcat column header prints 'min^-1'); 17.94 / 60 = 0.29900000000000004 s^(-1); the exported value is 17.94 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 84943 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 84943 / 1000 = 84.943 s^(-1)*mM^(-1); the exported value is 5125.714285714286 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL3', substrate row 'Ferulate': Km = 3.5 uM; Vmax = 4930 pkat mg^-1; Kcat = 17.94 min^-1; printed Kenz = Kcat/Km = 84943 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL3', substrate row 'Ferulate' (catalog accession Q6ETN3)