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.


enzyme_display_name: benzoate--CoA ligase

organism: Bos taurus

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

source_db: uniprot

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: cofactor ATP

data_origin: experimental

enzyme: benzoate--CoA ligase

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

source: uniprot


substrate_name: hexanoate

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

smiles: CCCCCC(=O)[O-]

substrate: hexanoate


substrate_name: ATP (with hexanoate as substrate)

substrate: ATP (with hexanoate as substrate)


organism: Magnetospirillum sp.

substrate_name: benzoate

source_db: brenda

assay_conditions_summary: pH 9; cofactor CoA

substrate: benzoate

source: brenda


substrate_name: CoA

substrate: CoA


substrate_name: ATP

assay_conditions_summary: pH 9; cofactor ATP

substrate: ATP


enzyme_display_name: 4-hydroxybenzoate--CoA ligase

organism: Arabidopsis thaliana

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

enzyme: 4-hydroxybenzoate--CoA ligase

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.

mutation_type: substitution

enzyme: o-succinylbenzoate--CoA ligase


organism: Thauera aromatica

sequence_source: multiple

source_databases_merged: brenda uniprot


substrate_name: CoASH

substrate: CoASH


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

assay_conditions_summary: cofactor CoA


organism: Anthoceros agrestis

verification_status: corrected

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.

status: corrected


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.


enzyme_display_name: phenylacetate--CoA ligase

organism: Aromatoleum evansii

substrate_name: PA (aerobically at 37 degrees Celsius)

verification_status: verified

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

enzyme: phenylacetate--CoA ligase

substrate: PA (aerobically at 37 degrees Celsius)

status: verified


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)


organism: Azoarcus evansii

source_db: oed

verification_status: unverified

assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP

status: unverified

source: oed


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)


enzyme_display_name: phytanate--CoA ligase

organism: Homo sapiens

substrate_name: hexadecanoate (palmitate)

smiles: CCCCCCCCCCCCCCCC(=O)[O-]

enzyme: phytanate--CoA ligase

substrate: hexadecanoate (palmitate)


organism: Pseudomonas sp.

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


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_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: hexanoate

substrate: hexanoate


substrate_name: octanoate

smiles: CCCCCCCC(=O)[O-]

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

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

assay_conditions_summary: pH 7.5; 297.15 K; cofactor CoA


substrate_name: ATP

assay_conditions_summary: pH 7.5; 297.15 K; cofactor ATP

substrate: ATP


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

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


organism: Rhodopseudomonas palustris

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

km_display: Not reported

ki_unit: mM

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


organism: Paraburkholderia xenovorans

assay_conditions_summary: pH 8


assay_conditions_summary: pH 8; cofactor CoA


assay_conditions_summary: pH 8; cofactor ATP


proof_lines:
anaerobically induced enzyme
2-fluorobenzoate
CoA


assay_conditions_summary: cofactor ATP

proof_lines:
anaerobically induced enzyme
coenzyme A
aerobically induced enzyme


protein_accession_database: NCBI Protein

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


substrate_name: reduced CoA

assay_conditions_summary: cofactor 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


enzyme_display_name: muconolactone Delta-isomerase

organism: Cupriavidus necator

enzyme: muconolactone Delta-isomerase


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

kcat_over_km_origin: calculated


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.


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

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

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

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

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

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'


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.


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'


organism: Pseudomonas sp.

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)

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


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)

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.


substrate_name: 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

substrate: ATP


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


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)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL5'; substrate row 'Cinnamate'; column 'Km (uM)' = 54.4; column 'Vmax (pkat mg^-1)' = 300; column 'Kcat (min^-1)' = 1.02; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 312.

normalized_value_unit_evidence: Km: printed Table I cell 54.4 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 54.4 / 1000 = 0.0544 mM; the exported value is 0.0544 mM. kcat: printed Table I cell 1.02 min^-1 (the Kcat column header prints 'min^-1'); 1.02 / 60 = 0.017 s^(-1); the exported value is 1.02 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 312 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 312 / 1000 = 0.312 s^(-1)*mM^(-1); the exported value is 18.75 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL5', substrate row 'Cinnamate': Km = 54.4 uM; Vmax = 300 pkat mg^-1; Kcat = 1.02 min^-1; printed Kenz = Kcat/Km = 312 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL5', substrate row 'Cinnamate' (catalog accession Q6ZAC1)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL5'; substrate row '4-Coumarate'; column 'Km (uM)' = 10.3; column 'Vmax (pkat mg^-1)' = 830; column 'Kcat (min^-1)' = 2.88; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 4660.

normalized_value_unit_evidence: Km: printed Table I cell 10.3 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 10.3 / 1000 = 0.0103 mM; the exported value is 0.0103 mM. kcat: printed Table I cell 2.88 min^-1 (the Kcat column header prints 'min^-1'); 2.88 / 60 = 0.048 s^(-1); the exported value is 2.88 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 4660 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 4660 / 1000 = 4.66 s^(-1)*mM^(-1); the exported value is 279.6116504854369 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL5', substrate row '4-Coumarate': Km = 10.3 uM; Vmax = 830 pkat mg^-1; Kcat = 2.88 min^-1; printed Kenz = Kcat/Km = 4660 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL5', substrate row '4-Coumarate' (catalog accession Q6ZAC1)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL5'; substrate row 'Caffeate'; column 'Km (uM)' = 26.1; column 'Vmax (pkat mg^-1)' = 240; column 'Kcat (min^-1)' = 0.84; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 535.

normalized_value_unit_evidence: Km: printed Table I cell 26.1 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 26.1 / 1000 = 0.0261 mM; the exported value is 0.0261 mM. kcat: printed Table I cell 0.84 min^-1 (the Kcat column header prints 'min^-1'); 0.84 / 60 = 0.014 s^(-1); the exported value is 0.84 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 535 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 535 / 1000 = 0.535 s^(-1)*mM^(-1); the exported value is 32.183908045977006 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL5', substrate row 'Caffeate': Km = 26.1 uM; Vmax = 240 pkat mg^-1; Kcat = 0.84 min^-1; printed Kenz = Kcat/Km = 535 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL5', substrate row 'Caffeate' (catalog accession Q6ZAC1)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL5'; substrate row 'Ferulate'; column 'Km (uM)' = 6.9; column 'Vmax (pkat mg^-1)' = 590; column 'Kcat (min^-1)' = 2.04; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 4871.

normalized_value_unit_evidence: Km: printed Table I cell 6.9 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 6.9 / 1000 = 0.006900000000000001 mM; the exported value is 0.006900000000000001 mM. kcat: printed Table I cell 2.04 min^-1 (the Kcat column header prints 'min^-1'); 2.04 / 60 = 0.034 s^(-1); the exported value is 2.04 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 4871 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 4871 / 1000 = 4.871 s^(-1)*mM^(-1); the exported value is 295.65217391304344 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL5', substrate row 'Ferulate': Km = 6.9 uM; Vmax = 590 pkat mg^-1; Kcat = 2.04 min^-1; printed Kenz = Kcat/Km = 4871 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL5', substrate row 'Ferulate' (catalog accession Q6ZAC1)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL5'; substrate row 'Sinapate'; column 'Km (uM)' = 58.9; column 'Vmax (pkat mg^-1)' = 920; column 'Kcat (min^-1)' = 3.18; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 899.

normalized_value_unit_evidence: Km: printed Table I cell 58.9 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 58.9 / 1000 = 0.0589 mM; the exported value is 0.0589 mM. kcat: printed Table I cell 3.18 min^-1 (the Kcat column header prints 'min^-1'); 3.18 / 60 = 0.053000000000000005 s^(-1); the exported value is 3.18 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 899 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 899 / 1000 = 0.899 s^(-1)*mM^(-1); the exported value is 53.98981324278438 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL5', substrate row 'Sinapate': Km = 58.9 uM; Vmax = 920 pkat mg^-1; Kcat = 3.18 min^-1; printed Kenz = Kcat/Km = 899 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL5', substrate row 'Sinapate' (catalog accession Q6ZAC1)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL1'; substrate row 'Cinnamate'; column 'Km (uM)' = 9.4; column 'Vmax (pkat mg^-1)' = 100; column 'Kcat (min^-1)' = 0.37; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 663.

normalized_value_unit_evidence: Km: printed Table I cell 9.4 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 9.4 / 1000 = 0.0094 mM; the exported value is 0.0094 mM. kcat: printed Table I cell 0.37 min^-1 (the Kcat column header prints 'min^-1'); 0.37 / 60 = 0.006166666666666667 s^(-1); the exported value is 0.37 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 663 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 663 / 1000 = 0.663 s^(-1)*mM^(-1); the exported value is 39.36170212765957 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL1', substrate row 'Cinnamate': Km = 9.4 uM; Vmax = 100 pkat mg^-1; Kcat = 0.37 min^-1; printed Kenz = Kcat/Km = 663 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL1', substrate row 'Cinnamate' (catalog accession P17814)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL1'; substrate row '4-Coumarate'; column 'Km (uM)' = 11.9; column 'Vmax (pkat mg^-1)' = 130; column 'Kcat (min^-1)' = 0.49; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 681.

normalized_value_unit_evidence: Km: printed Table I cell 11.9 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 11.9 / 1000 = 0.0119 mM; the exported value is 0.0119 mM. kcat: printed Table I cell 0.49 min^-1 (the Kcat column header prints 'min^-1'); 0.49 / 60 = 0.008166666666666666 s^(-1); the exported value is 0.49 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 681 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 681 / 1000 = 0.681 s^(-1)*mM^(-1); the exported value is 41.17647058823529 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL1', substrate row '4-Coumarate': Km = 11.9 uM; Vmax = 130 pkat mg^-1; Kcat = 0.49 min^-1; printed Kenz = Kcat/Km = 681 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL1', substrate row '4-Coumarate' (catalog accession P17814)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL1'; substrate row 'Caffeate'; column 'Km (uM)' = 29.3; column 'Vmax (pkat mg^-1)' = 140; column 'Kcat (min^-1)' = 0.52; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 296.

normalized_value_unit_evidence: Km: printed Table I cell 29.3 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 29.3 / 1000 = 0.0293 mM; the exported value is 0.0293 mM. kcat: printed Table I cell 0.52 min^-1 (the Kcat column header prints 'min^-1'); 0.52 / 60 = 0.008666666666666666 s^(-1); the exported value is 0.52 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 296 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 296 / 1000 = 0.296 s^(-1)*mM^(-1); the exported value is 17.747440273037544 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL1', substrate row 'Caffeate': Km = 29.3 uM; Vmax = 140 pkat mg^-1; Kcat = 0.52 min^-1; printed Kenz = Kcat/Km = 296 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL1', substrate row 'Caffeate' (catalog accession P17814)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL1'; substrate row 'Ferulate'; column 'Km (uM)' = 8.3; column 'Vmax (pkat mg^-1)' = 110; column 'Kcat (min^-1)' = 0.41; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 824.

normalized_value_unit_evidence: Km: printed Table I cell 8.3 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 8.3 / 1000 = 0.0083 mM; the exported value is 0.0083 mM. kcat: printed Table I cell 0.41 min^-1 (the Kcat column header prints 'min^-1'); 0.41 / 60 = 0.006833333333333333 s^(-1); the exported value is 0.41 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 824 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 824 / 1000 = 0.824 s^(-1)*mM^(-1); the exported value is 49.39759036144578 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL1', substrate row 'Ferulate': Km = 8.3 uM; Vmax = 110 pkat mg^-1; Kcat = 0.41 min^-1; printed Kenz = Kcat/Km = 824 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL1', substrate row 'Ferulate' (catalog accession P17814)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL2'; substrate row 'Cinnamate'; column 'Km (uM)' = 21.7; column 'Vmax (pkat mg^-1)' = 299; column 'Kcat (min^-1)' = 1.13; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 867.

normalized_value_unit_evidence: Km: printed Table I cell 21.7 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 21.7 / 1000 = 0.0217 mM; the exported value is 0.0217 mM. kcat: printed Table I cell 1.13 min^-1 (the Kcat column header prints 'min^-1'); 1.13 / 60 = 0.01883333333333333 s^(-1); the exported value is 1.13 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 867 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 867 / 1000 = 0.867 s^(-1)*mM^(-1); the exported value is 52.073732718894 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL2', substrate row 'Cinnamate': Km = 21.7 uM; Vmax = 299 pkat mg^-1; Kcat = 1.13 min^-1; printed Kenz = Kcat/Km = 867 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL2', substrate row 'Cinnamate' (catalog accession Q42982)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL2'; substrate row '4-Coumarate'; column 'Km (uM)' = 16.8; column 'Vmax (pkat mg^-1)' = 629; column 'Kcat (min^-1)' = 2.37; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 2351.

normalized_value_unit_evidence: Km: printed Table I cell 16.8 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 16.8 / 1000 = 0.016800000000000002 mM; the exported value is 0.016800000000000002 mM. kcat: printed Table I cell 2.37 min^-1 (the Kcat column header prints 'min^-1'); 2.37 / 60 = 0.0395 s^(-1); the exported value is 2.37 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 2351 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 2351 / 1000 = 2.351 s^(-1)*mM^(-1); the exported value is 141.07142857142856 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL2', substrate row '4-Coumarate': Km = 16.8 uM; Vmax = 629 pkat mg^-1; Kcat = 2.37 min^-1; printed Kenz = Kcat/Km = 2351 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL2', substrate row '4-Coumarate' (catalog accession Q42982)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL2'; substrate row 'Caffeate'; column 'Km (uM)' = 27.6; column 'Vmax (pkat mg^-1)' = 708; column 'Kcat (min^-1)' = 2.67; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 1612.

normalized_value_unit_evidence: Km: printed Table I cell 27.6 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 27.6 / 1000 = 0.027600000000000003 mM; the exported value is 0.0216 mM. kcat: printed Table I cell 2.67 min^-1 (the Kcat column header prints 'min^-1'); 2.67 / 60 = 0.0445 s^(-1); the exported value is 2.67 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 1612 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 1612 / 1000 = 1.612 s^(-1)*mM^(-1); the exported value is 123.6111111111111 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL2', substrate row 'Caffeate': Km = 27.6 uM; Vmax = 708 pkat mg^-1; Kcat = 2.67 min^-1; printed Kenz = Kcat/Km = 1612 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL2', substrate row 'Caffeate' (catalog accession Q42982)


column_label: Table I. Enzyme activities of recombinant rice 4CLs. Enzyme column block 'Os4CL2'; substrate row 'Ferulate'; column 'Km (uM)' = 2.2; column 'Vmax (pkat mg^-1)' = 613; column 'Kcat (min^-1)' = 2.31; column 'Kenz = Kcat/Km (M^-1 s^-1)' = 17295.

normalized_value_unit_evidence: Km: printed Table I cell 2.2 uM (the journal sets molar units in small capitals, so the column header renders as 'um' and means micromolar); 2.2 / 1000 = 0.0022 mM; the exported value is 0.0022 mM. kcat: printed Table I cell 2.31 min^-1 (the Kcat column header prints 'min^-1'); 2.31 / 60 = 0.0385 s^(-1); the exported value is 2.31 s^(-1), which is the printed per-minute numeral carried under a per-second label. kcat/Km: printed Table I Kenz = Kcat/Km cell 17295 M^-1 s^-1 (the header renders as 'm^-1 s^-1' in the same small-capital style and means per molar per second); 17295 / 1000 = 17.295 s^(-1)*mM^(-1); the exported value is 1050.0 s^(-1)*mM^(-1).; the live export row carries no vmax field.

raw_value_unit_evidence: Table I, enzyme column 'Os4CL2', substrate row 'Ferulate': Km = 2.2 uM; Vmax = 613 pkat mg^-1; Kcat = 2.31 min^-1; printed Kenz = Kcat/Km = 17295 M^-1 s^-1.

row_label: Table I, enzyme column block 'Os4CL2', substrate row 'Ferulate' (catalog accession Q42982)


enzyme_display_name: ribose-5-phosphate isomerase

organism: Cyberlindnera jadinii

substrate_name: D-ribose 5-phosphate

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

proof_lines:
enzyme form III
enzyme form II
enzyme form I

enzyme: ribose-5-phosphate isomerase

substrate: D-ribose 5-phosphate


enzyme_display_name: UDP-glucose 4-epimerase

organism: Davallia divaricata

substrate_name: UDP-alpha-D-galactose

proof_lines: DdUGE1, pH and temperature not specified in the publication

proof_lines: DdUGE2, pH and temperature not specified in the publication

enzyme: UDP-glucose 4-epimerase

substrate: UDP-alpha-D-galactose


organism: Arthrobacter sp

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

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

column_label: PMID 15068371 abstract; enzyme 4-chlorobenzoate:CoA ligase; substrate 4-chlorobenzoate; metric apparent Km; raw value 3.5 microM; normalized value 0.0035 mM.

normalized_value_unit_evidence: 3.5 microM normalized to 0.0035 mM.

raw_value_unit_evidence: PubMed abstract reports apparent Km for 4-chlorobenzoate = 3.5 microM.

row_label: 4-chlorobenzoate:CoA ligase / 4-chlorobenzoate apparent Km

table_label: PubMed abstract prose (PMID 15068371)


column_label: PMID 15068371 abstract; enzyme 4-chlorobenzoate:CoA ligase; substrate CoA; metric apparent Km; raw value 30 microM; normalized value 0.03 mM.

normalized_value_unit_evidence: 30 microM normalized to 0.03 mM.

raw_value_unit_evidence: PubMed abstract reports apparent Km for CoA = 30 microM.

row_label: 4-chlorobenzoate:CoA ligase / CoA apparent Km


column_label: PMID 15068371 abstract; enzyme 4-chlorobenzoate:CoA ligase; substrate ATP; metric apparent Km; raw value 238 microM; normalized value 0.238 mM.

normalized_value_unit_evidence: 238 microM normalized to 0.238 mM.

raw_value_unit_evidence: PubMed abstract reports apparent Km for ATP = 238 microM.

row_label: 4-chlorobenzoate:CoA ligase / ATP apparent Km


enzyme_display_name: maltose alpha-D-glucosyltransferase

organism: Deinococcus radiodurans

substrate_name: maltose

proof_lines: pH 7.6, 30°C, recombinant His6-tagged enzyme

enzyme: maltose alpha-D-glucosyltransferase

substrate: maltose


enzyme_display_name: cellobiose epimerase

organism: Dictyoglomus thermophilum

substrate_name: cellobiose

enzyme: cellobiose epimerase

substrate: cellobiose


organism: Dianthus caryophyllus

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Pyrobaculum neutrophilum


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


substrate_name: Toluate

substrate: Toluate


substrate_name: benzoate

substrate: benzoate


organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)


organism: Mycobacterium tuberculosis

substrate_name: CoA

assay_conditions_summary: pH 7.3; 295.15 K; cofactor CoA

proof_lines: kcat is 7.1 sec(-1) for ligase activity with HIP. kcat is 7.5 sec(-1) for ligase activity with CoASH (at pH 7.3 and 22 degrees Celsius). kcat is 13 sec(-1) for ligase activity with 5alpha-OH HIP (at pH 7.3 and 22 degrees Celsius).


organism: Streptomyces carzinostaticus

substrate_name: 2-hydroxynaphthalene-1-carboxylic acid

proof_lines: pH and temperature not specified in the publication

substrate: 2-hydroxynaphthalene-1-carboxylic acid


substrate_name: Naphthalene-1-carboxylic acid

substrate: Naphthalene-1-carboxylic acid


proof_lines: kcat is 38 min(-1) with 2-hydroxy-7-methoxy-5-methyl-1-naphthoate as substrate. kcat is 8.1 min(-1) with 2-hydroxy-5-methyl-1-naphthoate as substrate. kcat is 93 min(-1) with 2,7-dihydroxy-5-methyl-1-naphthoate as substrate.


organism: Metallosphaera sedula

sequence_source: UniProt A4YDR9

smiles: O=C(O)CCCO

assay_conditions_summary: pH 7.9; 348.15 K; cofactor CoA


enzyme_display_name: 3-(methylthio)propionate--CoA ligase

organism: Ruegeria pomeroyi

substrate_name: Butyrate

sequence_source: UniProt Q5LRT0

smiles: CCCC(=O)O

assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA

enzyme: 3-(methylthio)propionate--CoA ligase

substrate: Butyrate


smiles: CSCCC(=O)O


substrate_name: propionate

substrate: propionate


substrate_name: Acrylate

substrate: Acrylate


substrate_name: Unknown

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

substrate: Unknown


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


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

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

assay_conditions_summary: pH 7.3; cofactor CoA

proof_lines: kcat is 0.75 sec(-1) for 3-oxo-4-cholesten-26-oate--CoA ligase activity (at pH 7.3 and 22 degrees Celsius).

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


organism: Mycolicibacterium smegmatis


substrate_name: 3-oxo-4-cholesten-26-oate (at pH 7.3 and 22 degrees Celsius)


organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)

proof_lines: kcat is 14.9 sec(-1) for ligase activity with MMPA as substrate. kcat is 7.2 sec(-1) for ligase activity with butyrate as substrate. kcat is 3.7 sec(-1) for ligase activity with propionate as substrate. kcat is 1 sec(-1) for ligase activity


enzyme_display_name: L-allo-isoleucine--holo-[CmaA peptidyl-carrier protein] ligase

organism: Pseudomonas savastanoi pv. glycinea

substrate_name: DL-coronamic acid (at pH 7.5 and 25 degrees Celsius)

proof_lines: kcat is 17 min(-1) for ligase activity with L-allo-isoleucine as substrate (at pH 7.5 and 25 degrees Celsius). kcat is 16 min(-1) for ligase activity with L-leucine as substrate (at pH 7.5 and 25 degrees Celsius). kcat is 12 min(-1) for lig


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W424G with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


organism: Candidatus Pelagibacter ubique

column_label: Table 4. Apparent kinetic constants for “Ca. Pelagibacter ubique” HTCC1062 and R. pomeroyi DSS-3 DmdBs; enzyme column PU_DmdB1; row MMPA; columns kcat; kcat/Km; Km; kcat raw_value=29.4 raw_unit=s^-1; kcat/Km raw_value=735 raw_unit=s^-1*mM^-1; Km raw_value=0.04 +/- 0.01 raw_unit=mM

normalized_value_unit_evidence: kcat normalized_value=29.4 normalized_unit=s^-1; kcat/Km normalized_value=735 normalized_unit=s^-1*mM^-1; Km normalized_value=0.04 normalized_unit=mM

row_label: MMPA


column_label: Table 4. Apparent kinetic constants for “Ca. Pelagibacter ubique” HTCC1062 and R. pomeroyi DSS-3 DmdBs; enzyme column PU_DmdB1; row Acrylate; columns kcat; kcat/Km; Km; kcat raw_value=22.3 raw_unit=s^-1; kcat/Km raw_value=50 raw_unit=s^-1*mM^-1; Km raw_value=0.44 +/- 0.04 raw_unit=mM

normalized_value_unit_evidence: kcat normalized_value=22.3 normalized_unit=s^-1; kcat/Km normalized_value=50 normalized_unit=s^-1*mM^-1; Km normalized_value=0.44 normalized_unit=mM

row_label: Acrylate


column_label: Table 4. Apparent kinetic constants for “Ca. Pelagibacter ubique” HTCC1062 and R. pomeroyi DSS-3 DmdBs; enzyme column PU_DmdB1; row Butyrate; columns kcat; kcat/Km; Km; kcat raw_value=43.8 raw_unit=s^-1; kcat/Km raw_value=3,370 raw_unit=s^-1*mM^-1; Km raw_value=0.01 +/- 0.01 raw_unit=mM

normalized_value_unit_evidence: kcat normalized_value=43.8 normalized_unit=s^-1; kcat/Km normalized_value=3370 normalized_unit=s^-1*mM^-1; Km normalized_value=0.01 normalized_unit=mM

row_label: Butyrate


column_label: Table 4. Apparent kinetic constants for “Ca. Pelagibacter ubique” HTCC1062 and R. pomeroyi DSS-3 DmdBs; enzyme column PU_DmdB1; row propionate; columns kcat; kcat/Km; Km; kcat raw_value=17.7 raw_unit=s^-1; kcat/Km raw_value=505 raw_unit=s^-1*mM^-1; Km raw_value=0.04 +/- 0.02 raw_unit=mM

normalized_value_unit_evidence: kcat normalized_value=17.7 normalized_unit=s^-1; kcat/Km normalized_value=505 normalized_unit=s^-1*mM^-1; Km normalized_value=0.04 normalized_unit=mM

row_label: propionate


organism: Candidatus Pelagibacter communis


assay_conditions_summary: pH 7.5; cofactor CoA

column_label: Table 4 row PU_DmdB1 with MMPA gives Km 0.04 mM, kcat 29.4 s^-1, and kcat/Km 735 s^-1 mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.04 normalized_unit=mM; kcat normalized_value=29.4 normalized_unit=s^-1; kcat/Km normalized_value=735 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=0.04 mM; kcat raw_value=29.4 s^-1; kcat/Km raw_value=735 s^-1 mM^-1

row_label: PU_DmdB1 / MMPA (3-(methylthio)propanoate)

table_label: Official PMC full-text Table 4: Apparent kinetic constants for DmdBs


smiles: CCCC(=O)[O-]


organism: Unknown prokaryotic organism

substrate_name: ferulate

assay_conditions_summary: cofactor CoA

column_label: Full text reports the FCS1 Km and Vmax values were 0.1 mM and 36.8 U/mg and Table 1 lists Km 0.1 for the unknown lignin consortium enzyme.

raw_value_unit_evidence: Km raw_value=0.1 mM raw_unit=mM

row_label: FCS1 feruloyl-CoA synthetase / ferulate

table_label: PMC full text Table 1 PMID 30802241


organism: Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157)

substrate_name: MMPA

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

assay_conditions_summary: pH 8

column_label: Table 3. Km values of wild type DmdB and its mutants to different substrates; row Wild type DmdB / To MMPA; column Km to MMPA (mM); raw cell 0.2 +/- 0.02 mM; normalized Km 0.2 mM

normalized_value_unit_evidence: Km=0.2 mM

raw_value_unit_evidence: Wild type DmdB / To MMPA: Km to MMPA (mM)=0.2 +/- 0.02 mM

row_label: Wild type DmdB / To MMPA

substrate: MMPA


substrate_name: ATP

assay_conditions_summary: pH 8; cofactor ATP

column_label: Table 3. Km values of wild type DmdB and its mutants to different substrates; row Wild type DmdB / To ATP; column Km to ATP (mM); raw cell 0.8 +/- 0.05 mM; normalized Km 0.8 mM

normalized_value_unit_evidence: Km=0.8 mM

raw_value_unit_evidence: Wild type DmdB / To ATP: Km to ATP (mM)=0.8 +/- 0.05 mM

row_label: Wild type DmdB / To ATP

substrate: ATP


assay_conditions_summary: pH 8; cofactor CoA

column_label: Table 3. Km values of wild type DmdB and its mutants to different substrates; row Wild type DmdB / To CoA; column Km to CoA (mM); raw cell 0.4 +/- 0.01 mM; normalized Km 0.4 mM

normalized_value_unit_evidence: Km=0.4 mM

raw_value_unit_evidence: Wild type DmdB / To CoA: Km to CoA (mM)=0.4 +/- 0.01 mM

row_label: Wild type DmdB / To CoA

substrate: CoA


assay_conditions_summary: pH 7.5; 343.15 K; cofactor CoA


organism: Ruegeria lacuscaerulensis

smiles: CSCCC(=O)[O-]

assay_conditions_summary: pH 8; 313.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H231A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K526A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K434A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8; 313.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G303P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W326A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D435A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W443A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G441P with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E474A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K438A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E442A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R432A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G440P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P333A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W235A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G302P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W424G with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


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

assay_conditions_summary: pH 8; 297.15 K; cofactor ATP

column_label: PMID 17539640 main article, page 7729, Table 1; row label compound 11 (the 1-naphthoate source row); columns Km (microM), kcat (min^-1), and rel kcat/Km; raw cells 18 +/- 9, 6.7 +/- 1.4, and 5.8 x 10^-3.

normalized_value_unit_evidence: Km 18 microM = 0.018 mM; kcat 6.7 min^-1 / 60 = 0.1116666666666666666666666667 s^-1; the absolute kcat/Km from those same printed central cells is 0.1116666666666666666666666667 / 0.018 = 6.203703703703703703703703704 s^-1 mM^-1. The printed 5.8 x 10^-3 column is relative kcat/Km and is retained only as a row cross-check.

raw_value_unit_evidence: Main-article Table 1 row 11 prints Km 18 +/- 9 microM, kcat 6.7 +/- 1.4 min^-1, and relative kcat/Km 5.8 x 10^-3.

row_label: compound 11 / 1-naphthoate source identity

table_label: JACS 2007 Table 1, Naphthoic Acid Substrate Scope of the NcsB2 CoA Ligase


organism: Pseudomonas syringae

substrate_name: L-allo-isoleucine

column_label: Table 2: Kinetic parameters for CmaA-FLAG as determined by the forward PPi assay; row L-allo-Isoleucine; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); 0.04 +/- 0.01 mM; 0.09 +/- 0.00 min^-1; kcat/Km 2.3 min^-1 mM^-1.

enzyme: L-allo-isoleucine--holo-[CmaA peptidyl-carrier protein] ligase

substrate: L-allo-isoleucine


substrate_name: L-leucine

column_label: Table 2: Kinetic parameters for CmaA-FLAG as determined by the forward PPi assay; row L-Leucine; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); 1.5 +/- 0.1 mM; 1.8 +/- 0.1 min^-1; kcat/Km 1.2 min^-1 mM^-1.

row_label: L-Leucine; Km/kcat/kcat/Km columns

substrate: L-leucine


substrate_name: L-Valine

column_label: Table 2: Kinetic parameters for CmaA-FLAG as determined by the forward PPi assay; row L-Valine; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); 1.2 +/- 0.1 mM; 1.4 +/- 0.1 min^-1; kcat/Km 1.2 min^-1 mM^-1.

row_label: L-Valine; Km/kcat/kcat/Km columns

substrate: L-Valine


substrate_name: L-Isoleucine

column_label: Table 2: Kinetic parameters for CmaA-FLAG as determined by the forward PPi assay; row L-Isoleucine; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); 0.50 +/- 0.06 mM; 0.71 +/- 0.03 min^-1; kcat/Km 1.4 min^-1 mM^-1.

row_label: L-Isoleucine; Km/kcat/kcat/Km columns

substrate: L-Isoleucine


substrate_name: CoA (with MMPA)

assay_conditions_summary: cofactor ATP

substrate: CoA (with MMPA)


substrate_name: ATP (with MMPA)

substrate: ATP (with MMPA)


column_label: Table 4. Apparent kinetic constants for “Ca. Pelagibacter ubique” HTCC1062 and R. pomeroyi DSS-3 DmdBs; enzyme column RPO_DmdB2; row MMPA; columns Km; Km raw_value=0.07 +/- 0.02 raw_unit=mM

raw_value_unit_evidence: Km raw_value=0.07 +/- 0.02 raw_unit=mM


substrate_name: butyrate

column_label: Table 4. Apparent kinetic constants for “Ca. Pelagibacter ubique” HTCC1062 and R. pomeroyi DSS-3 DmdBs; enzyme column RPO_DmdB2; row butyrate; columns Km; Km raw_value=0.12 +/- 0.03 raw_unit=mM

raw_value_unit_evidence: Km raw_value=0.12 +/- 0.03 raw_unit=mM

row_label: butyrate

substrate: butyrate


column_label: Table 4. Apparent kinetic constants for “Ca. Pelagibacter ubique” HTCC1062 and R. pomeroyi DSS-3 DmdBs; enzyme column RPO_DmdB2; row propionate; columns Km; Km raw_value=3.11 +/- 1.13 raw_unit=mM

raw_value_unit_evidence: Km raw_value=3.11 +/- 1.13 raw_unit=mM


substrate_name: acrylate

column_label: Table 4. Apparent kinetic constants for “Ca. Pelagibacter ubique” HTCC1062 and R. pomeroyi DSS-3 DmdBs; enzyme column RPO_DmdB2; row acrylate; columns Km; Km raw_value=5.25 +/- 2.1 raw_unit=mM

raw_value_unit_evidence: Km raw_value=5.25 +/- 2.1 raw_unit=mM

row_label: acrylate

substrate: acrylate


enzyme_display_name: E1 ubiquitin-activating enzyme

organism: Homo sapiens

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

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: above, intrinsic kcat for ubiquitin adenylate formation corrected for saturating ATP and 125I-ubiquitin, mutant enzyme D576E

proof_lines: intrinsic kcat for transthiolation of ubiquitin carrier protein E2 corrected for saturating ATP, 125I-ubiquitin, and ubiquitin carrier protein E2, mutant enzyme D576E

enzyme: E1 ubiquitin-activating enzyme


substrate_name: ubiquitin

substrate: ubiquitin


substrate_name: ubiquitin carrier protein E2

substrate: ubiquitin carrier protein E2


proof_lines: above, intrinsic kcat for ubiquitin adenylate formation corrected for saturating ATP and 125I-ubiquitin, mutant enzyme D576N

proof_lines: intrinsic kcat for transthiolation of ubiquitin carrier protein E2 corrected for saturating ATP, 125I-ubiquitin, and ubiquitin carrier protein E2, mutant enzyme D576N


proof_lines: intrinsic kcat for transthiolation of ubiquitin carrier protein E2 corrected for saturating ATP, 125I-ubiquitin, and ubiquitin carrier protein E2, mutant enzyme K528A

proof_lines: above, intrinsic kcat for ubiquitin adenylate formation corrected for saturating ATP and 125I-ubiquitin, mutant enzyme K528A


proof_lines: above, intrinsic kcat for ubiquitin adenylate formation corrected for saturating ATP and 125I-ubiquitin, mutant enzyme D576A

proof_lines: intrinsic kcat for transthiolation of ubiquitin carrier protein E2 corrected for saturating ATP, 125I-ubiquitin, and ubiquitin carrier protein E2, mutant enzyme D576A


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

proof_lines: intrinsic kcat for transthiolation of ubiquitin carrier protein E2 corrected for saturating ATP, 125I-ubiquitin, and ubiquitin carrier protein E2, wild-type enzyme

proof_lines: above, intrinsic kcat for ubiquitin adenylate formation corrected for saturating ATP and 125I-ubiquitin, wild-type enzyme


substrate_name: Acrylate


substrate_name: propionate


assay_conditions_summary: pH 8.5; 318.15 K; cofactor ATP


substrate_name: Butyrate

substrate: Butyrate


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


substrate_name: valerate

smiles: CCCCC(=O)[O-]

substrate: valerate


substrate: propionate


substrate_name: acetate

substrate: acetate


substrate_name: Oregon Green-labeled ubiquitin

substrate: Oregon Green-labeled ubiquitin


substrate_name: ATP

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

substrate: ATP


substrate_name: L-allo-isoleucine (at pH 7.5 and 25 degrees Celsius)

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


substrate_name: L-leucine (at pH 7.5 and 25 degrees Celsius)

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


substrate_name: L-valine (at pH 7.5 and 25 degrees Celsius)

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


organism: Dictyoglomus turgidum

substrate_name: lactose

proof_lines: purified recombinant His-tagged enzyme, pH 7.0, 70°C

proof_lines: pH and temperature not specified in the publication

substrate: lactose


enzyme_display_name: D-psicose 3-epimerase

organism: Dorea sp. CAG:317

substrate_name: D-fructose

enzyme: D-psicose 3-epimerase

substrate: D-fructose


organism: Diospyros kaki

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Dirofilaria immitis

proof_lines: in 30 mM Tris-HCl, 5 mM MgSO4, 20 mM KCl, pH 7.5, at 30°C

proof_lines: recombinant His-tagged enzyme, pH 7.5, 30°C


organism: Echinococcus granulosus

substrate_name: D-ribose 5-phosphate

substrate: D-ribose 5-phosphate


substrate_name: L-allo-isoleucine

proof_lines: pH 7.5, 25°C, the assay measures the release of diphosphate by means of a coupled enzyme system in which diphosphate drives the reduction of NAD+ to NADH

substrate: L-allo-isoleucine


substrate_name: L-valine

substrate: L-valine


substrate_name: L-leucine

substrate: L-leucine


organism: Mycobacterium tuberculosis

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


organism: Dyadobacter fermentans


enzyme_display_name: UniProt Q8TBC4

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q8TBC4

source: skid


substrate_name: diphosphate

substrate: diphosphate


enzyme_display_name: L-firefly luciferin--CoA ligase

organism: Zophobas atratus

substrate_name: L-firefly luciferin

proof_lines: at pH 8.5, temperature not specified in the publication

enzyme: L-firefly luciferin--CoA ligase

substrate: L-firefly luciferin


assay_conditions_summary: pH 8.5; cofactor ATP


organism: Aquatica lateralis

substrate_name: Ketoprofen

substrate: Ketoprofen


organism: Photinus pyralis

assay_conditions_summary: 298.15 K; cofactor CoA

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


enzyme_display_name: (hydroxyamino)benzene mutase

organism: Ectopseudomonas oleovorans

substrate_name: (hydroxylamino)benzene

assay_conditions_summary: pH 7

enzyme: (hydroxyamino)benzene mutase

substrate: (hydroxylamino)benzene


organism: Enterobacter cloacae

substrate_name: N-acetylglucosamine 6-phosphate

substrate: N-acetylglucosamine 6-phosphate


organism: Pseudomonas aeruginosa (strain UCBPP-PA14)

substrate_name: L-cysteine

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

proof_lines: kcat is 415 min(-1) with L-cysteine as substrate.

substrate: L-cysteine


proof_lines: kcat is 38 min(-1) with L-cysteine as substrate.


enzyme_display_name: UniProt P10378

organism: Escherichia coli

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.8
Raw SKiD Env: Temp=37°C, pH=8

enzyme: UniProt P10378


organism: Pseudomonas syringae pv. syringae

substrate_name: L-serine

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

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

proof_lines: kcat is 29.1 min(-1) with L-threonine as substrate. kcat is 1.23 min(-1) with L-serine as substrate.

substrate: L-serine


substrate_name: L-threonine

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

substrate: L-threonine


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

substrate_name: MbtL-holo

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

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

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

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

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

substrate: MbtL-holo


organism: Pseudomonas aeruginosa

substrate_name: L-Cysteine

substrate: L-Cysteine


enzyme_display_name: thioglycine synthase

organism: Methanosarcina acetivorans

substrate_name: RLGFFGFDLQD

enzyme: thioglycine synthase

substrate: RLGFFGFDLQD


organism: Streptomyces coelicolor

substrate_name: L-proline

substrate: L-proline


organism: Bacillus cereus

substrate_name: ATP

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: L-alanine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C269A to reconstruct the assayed variant sequence.

substrate: L-alanine


substrate_name: D-Alanine

substrate: D-Alanine


enzyme_display_name: malonate--CoA ligase

organism: Rhizobium leguminosarum

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H206L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines: pH 7.0, 30°C, mutant enzyme H206L, cosubstrate: malonate

enzyme: malonate--CoA ligase


substrate_name: malonate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9ZIP5 and applied mutation signature H206L to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-state kinetic constants for MCS activities of the wild type and mutant GST-MCS enzymes (Biochem. J. 1999, 344, 159-166, journal page 162), printed substrate column heads Malonate | ATP | CoA and printed metric row heads Km (uM) | kcat (s-1) | kcat/Km (mM-1 s-1); enzyme block 'H206L', Malonate column: Km cell = 8700 +/- 980; kcat cell = 0.53 +/- 0.28; kcat/Km cell = 0.11.

normalized_value_unit_evidence: Km: printed Table 2 cell 8700 uM; 8700 / 1000 = 8.7 mM; the exported value is 8.7 mM. kcat: printed Table 2 cell 0.53 s-1; the printed unit s-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 0.53 s^(-1); the exported value is 0.53 s^(-1). kcat/Km: printed Table 2 cell 0.11 under the column head kcat/Km (mM-1 s-1); mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.11 s^(-1)*mM^(-1); the exported value is 0.060919540229885064 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 2, enzyme block 'H206L', Malonate column: Km = 8700 +/- 980 uM; kcat = 0.53 +/- 0.28 s-1; kcat/Km = 0.11 under the printed column head kcat/Km (mM-1 s-1).

row_label: Table 2, enzyme block 'H206L', Malonate substrate column

substrate: malonate


substrate_name: CoA

substrate: CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K170M to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant enzyme K170M, cosubstrate: methylmalonate

proof_lines: pH 7.0, 30°C, mutant enzyme K170M, cosubstrate: malonate


substrate_name: methylmalonate

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

source_databases_merged: brenda oed

substrate: methylmalonate


assay_conditions_summary: pH 7; 303.15 K; buffer Assay condition: 100 mM potassium phosphate; cofactor ATP

column_label: Table 3  Steady-state kinetic constants for methyl MCS activities of the wild type and mutant GST-MCS enzymes; enzyme-form block 'Wild type'; column 'Methylmalonate'; metric line 'Km (uM)' = 373 +/- 19; metric line 'kcat (s^-1)' = 2.7 +/- 0.1; metric line 'kcat/Km (mM^-1 . s^-1)' = 7.2.

normalized_value_unit_evidence: kcat: paper cell 2.7 +/- 0.1 s^-1 -> 2.7 s^(-1) (no conversion); catalog holds 2.7 s^(-1). Km: paper cell 373 +/- 19 uM / 1000 = 0.373 mM; catalog holds 0.373 mM. kcat/Km: catalog 7.238605898123325 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells; the printed rounded cell 7.2 mM^-1 . s^-1 is documented in prose.

raw_value_unit_evidence: Table 3, Wild type block, Methylmalonate column: Km (uM) = 373 +/- 19; kcat (s^-1) = 2.7 +/- 0.1; kcat/Km (mM^-1 . s^-1) = 7.2 (rounded printed cell).

row_label: Table 3, enzyme-form block 'Wild type', column 'Methylmalonate'


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

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R168G/K170M to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant enzyme R168G/K170M, cosubstrate: malonate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R168G to reconstruct the assayed variant sequence.


proof_lines: pH 7.0, 30°C, mutant enzyme R168G, cosubstrate: methylmalonate

proof_lines: pH 7.0, 30°C, mutant enzyme R168G, cosubstrate: malonate