organism: Archaeoglobus fulgidus

substrate_name: tributyrin

sequence_source: UniProtKB O28558 direct FASTA lookup

smiles: CCCC(=O)OCC(COC(=O)CCC)OC(=O)CCC

column_label: Table 1 (journal page 31), decoded transcription, enzyme row AFEST, substrate column group Tributyrin (C4): kcat (s^-1) = 95; Km/K0.5 (mM) = 0.05.

normalized_value_unit_evidence: kcat: printed cell 95 s^-1 -> 95.0 s^(-1); the catalog holds 95.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 0.05 mM -> 0.05 mM; the catalog holds 0.05 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 1900.0 s^(-1)*mM^(-1) is the exact quotient 95 / 0.05 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

substrate: tributyrin


enzyme_display_name: carboxylesterase

substrate_name: tripropionin

source_db: oed

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

smiles: CCC(=O)OCC(COC(=O)CC)OC(=O)CC

column_label: Table 1 (journal page 31), decoded transcription, enzyme row AFEST, substrate column group Tripropionin (C3): kcat (s^-1) = 110; Km/K0.5 (mM) = 0.30.

normalized_value_unit_evidence: kcat: printed cell 110 s^-1 -> 110.0 s^(-1); the catalog holds 110.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 0.30 mM -> 0.3 mM; the catalog holds 0.3 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 366.6666666666667 s^(-1)*mM^(-1) is the exact quotient 110 / 0.30 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

table_label: Table 1 (journal page 31) 'Kinetic parameters kcat and K0.5 of the hydrolysis of short chain triacylglycerols by members of the HSL family and other lipolytic and non-lipolytic carboxyesterases'

data_origin: experimental

enzyme: carboxylesterase

substrate: tripropionin

status: verified

source: oed


substrate_name: vinyl propionate

smiles: C=COC(=O)CC

column_label: Table 3 (journal page 32), decoded transcription, enzyme row AFEST, substrate column group Vinyl propionate (C3): kcat (s^-1) = 200; Km/K0.5 (mM) = 7.

normalized_value_unit_evidence: kcat: printed cell 200 s^-1 -> 200.0 s^(-1); the catalog holds 200.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 7 mM -> 7.0 mM; the catalog holds 7.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 28.571428571428573 s^(-1)*mM^(-1) is the exact quotient 200 / 7 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

table_label: Table 3 (journal page 32) 'Kinetic parameters kcat and K0.5 of the hydrolysis of vinyl esters by members of the HSL family and other lipolytic and non-lipolytic carboxyesterases'

substrate: vinyl propionate


substrate_name: Vinylacetate

smiles: C=CCC(=O)O

column_label: Table 3 (journal page 32), decoded transcription, enzyme row AFEST, substrate column group Vinyl acetate (C2): kcat (s^-1) = 50; Km/K0.5 (mM) = 4.

normalized_value_unit_evidence: kcat: printed cell 50 s^-1 -> 50.0 s^(-1); the catalog holds 50.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 4 mM -> 4.0 mM; the catalog holds 4.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 12.5 s^(-1)*mM^(-1) is the exact quotient 50 / 4 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

substrate: Vinylacetate


substrate_name: vinyl butyrate

smiles: C=COC(=O)CCC

column_label: Table 3 (journal page 32), decoded transcription, enzyme row AFEST, substrate column group Vinyl butyrate (C4): kcat (s^-1) = 210; Km/K0.5 (mM) = 2.5.

normalized_value_unit_evidence: kcat: printed cell 210 s^-1 -> 210.0 s^(-1); the catalog holds 210.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 2.5 mM -> 2.5 mM; the catalog holds 2.5 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 84.0 s^(-1)*mM^(-1) is the exact quotient 210 / 2.5 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

substrate: vinyl butyrate


substrate_name: Triacetin

smiles: CC(=O)OCC(COC(C)=O)OC(C)=O

column_label: Table 1 (journal page 31), decoded transcription, enzyme row AFEST, substrate column group Triacetin (C2): kcat (s^-1) = 40; Km/K0.5 (mM) = 10.

normalized_value_unit_evidence: kcat: printed cell 40 s^-1 -> 40.0 s^(-1); the catalog holds 40.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 10 mM -> 10.0 mM; the catalog holds 10.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 4.0 s^(-1)*mM^(-1) is the exact quotient 40 / 10 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

substrate: Triacetin


organism: Aspergillus niger

sequence_source: UniProtKB Q6ED33 direct FASTA lookup

column_label: Table 1 (journal page 31), decoded transcription, enzyme row EstA, substrate column group Triacetin (C2): kcat (s^-1) = 265; Km/K0.5 (mM) = 15.

normalized_value_unit_evidence: kcat: printed cell 265 s^-1 -> 265.0 s^(-1); the catalog holds 265.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 15 mM -> 15.0 mM; the catalog holds 15.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 17.666666666666668 s^(-1)*mM^(-1) is the exact quotient 265 / 15 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


column_label: Table 3 (journal page 32), decoded transcription, enzyme row EstA, substrate column group Vinyl butyrate (C4): kcat (s^-1) = 25; Km/K0.5 (mM) = 2.

normalized_value_unit_evidence: kcat: printed cell 25 s^-1 -> 25.0 s^(-1); the catalog holds 25.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 2 mM -> 2.0 mM; the catalog holds 2.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 12.5 s^(-1)*mM^(-1) is the exact quotient 25 / 2 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


organism: Actinidia eriantha

substrate_name: 4-Methylumbelliferyl butyrate

verification_status: unverified

sequence_source: UniProtKB Q0ZPV7 direct lookup on 2026-05-31

substrate: 4-Methylumbelliferyl butyrate

status: unverified


organism: Aeropyrum pernix

substrate_name: 4-nitrophenyl octanoate

kcat_over_km_display: Not reported

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

substrate: 4-nitrophenyl octanoate


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

mutation_type: substitution


substrate_name: 4-nitrophenyl dodecanoate

substrate: 4-nitrophenyl dodecanoate


organism: Bacillus subtilis


substrate_name: p-Nitrophenyl butyrate

substrate: p-Nitrophenyl butyrate


organism: Cavia porcellus


substrate_name: vinyl laurate

smiles: C=COC(=O)CCCCCCCCCCC

substrate: vinyl laurate


organism: Escherichia coli

substrate_name: p-Nitrophenyl propionate

substrate: p-Nitrophenyl propionate


substrate_name: p-Nitrophenyl acetate

substrate: p-Nitrophenyl acetate


substrate_name: p-Nitrophenyl laurate

substrate: p-Nitrophenyl laurate


substrate_name: p-Nitrophenyl caproate

sequence_source: UniProtKB:P13001 canonical sequence, REST lookup on 2026-05-31; RCSB/SIFTS PDB 1M33 maps BioH to P13001.

substrate: p-Nitrophenyl caproate


organism: Ferroplasma acidiphilum

sequence_source: UniProtKB:Q2PCE5 canonical sequence, REST lookup on 2026-05-31; EMBL AJ850914/CAH64533.1 and RCSB/SIFTS PDB 3WJ2 support the same accession.


substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl hexanoate

substrate: 4-nitrophenyl hexanoate


substrate_name: 4-nitrophenyl propionate

substrate: 4-nitrophenyl propionate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: tributyrin

substrate: tributyrin


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YBQ2 and applied mutation signature W474V/R526V/T560W to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 333.15 K; buffer 50 mmol/L phosphate

column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = S022; second column 'Mutant' = W474V/R526V/T560W; column 'kcat (s−1)' = 23.50; column 'Km (μmol/L)' = 2.43; column 'kcat/Km (s−1 /mmol·L−1)' = 9662.

normalized_value_unit_evidence: kcat: printed Table 2 cell 23.50 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 23.5 s^(-1). Km: printed Table 2 cell 2.43 under the column head μmol/L; 2.43 / 1000 = 0.0024300000000000003 mM; the exported value is 0.00243 mM. kcat/Km: printed Table 2 cell 9662 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 9662.0 s^-1 mM^-1; the exported value is 9670.781893004116 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row S022: kcat = 23.50 in the column head unit s−1; Km = 2.43 in the column head unit μmol/L; printed kcat/Km = 9662 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row S022 (the W474V/R526V/T560W site-directed variant of apAAP)

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YBQ2 and applied mutation signature F488A/R526V/T560W to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = S011; second column 'Mutant' = F488A/R526V/T560W; column 'kcat (s−1)' = 12.08; column 'Km (μmol/L)' = 7.37; column 'kcat/Km (s−1 /mmol·L−1)' = 1638.

normalized_value_unit_evidence: kcat: printed Table 2 cell 12.08 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 12.08 s^(-1). Km: printed Table 2 cell 7.37 under the column head μmol/L; 7.37 / 1000 = 0.00737 mM; the exported value is 0.00737 mM. kcat/Km: printed Table 2 cell 1638 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 1638.0 s^-1 mM^-1; the exported value is 1639.0773405698778 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row S011: kcat = 12.08 in the column head unit s−1; Km = 7.37 in the column head unit μmol/L; printed kcat/Km = 1638 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row S011 (the F488A/R526V/T560W site-directed variant of apAAP)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YBQ2 and applied mutation signature R526V to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = P01; second column 'Mutant' = R526V; column 'kcat (s−1)' = 5.47; column 'Km (μmol/L)' = 11.8; column 'kcat/Km (s−1 /mmol·L−1)' = 462.5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 5.47 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 5.47 s^(-1). Km: printed Table 2 cell 11.8 under the column head μmol/L; 11.8 / 1000 = 0.011800000000000001 mM; the exported value is 0.0118 mM. kcat/Km: printed Table 2 cell 462.5 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 462.5 s^-1 mM^-1; the exported value is 463.5593220338983 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row P01: kcat = 5.47 in the column head unit s−1; Km = 11.8 in the column head unit μmol/L; printed kcat/Km = 462.5 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row P01 (the R526V site-directed variant of apAAP)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YBQ2 and applied mutation signature W474V/F488G/R526V/T560W to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = C01; second column 'Mutant' = W474V/F488G/R526V/T560W; column 'kcat (s−1)' = 26.25; column 'Km (μmol/L)' = 2.34; column 'kcat/Km (s−1 /mmol·L−1)' = 11218.

normalized_value_unit_evidence: kcat: printed Table 2 cell 26.25 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 26.25 s^(-1). Km: printed Table 2 cell 2.34 under the column head μmol/L; 2.34 / 1000 = 0.00234 mM; the exported value is 0.00234 mM. kcat/Km: printed Table 2 cell 11218 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 11218.0 s^-1 mM^-1; the exported value is 11217.948717948717 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row C01: kcat = 26.25 in the column head unit s−1; Km = 2.34 in the column head unit μmol/L; printed kcat/Km = 11218 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row C01 (the W474V/F488G/R526V/T560W site-directed variant of apAAP)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YBQ2 and applied mutation signature F488P/R526V/T560W to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = S013; second column 'Mutant' = F488P/R526V/T560W; column 'kcat (s−1)' = 8.17; column 'Km (μmol/L)' = 3.88; column 'kcat/Km (s−1 /mmol·L−1)' = 2107.

normalized_value_unit_evidence: kcat: printed Table 2 cell 8.17 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 8.17 s^(-1). Km: printed Table 2 cell 3.88 under the column head μmol/L; 3.88 / 1000 = 0.0038799999999999998 mM; the exported value is 0.00388 mM. kcat/Km: printed Table 2 cell 2107 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 2107.0 s^-1 mM^-1; the exported value is 2105.6701030927834 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row S013: kcat = 8.17 in the column head unit s−1; Km = 3.88 in the column head unit μmol/L; printed kcat/Km = 2107 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row S013 (the F488P/R526V/T560W site-directed variant of apAAP)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YBQ2 and applied mutation signature W474A/R526V/T560W to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = S02; second column 'Mutant' = W474A/R526V/T560W; column 'kcat (s−1)' = 12.61; column 'Km (μmol/L)' = 1.83; column 'kcat/Km (s−1 /mmol·L−1)' = 6876.

normalized_value_unit_evidence: kcat: printed Table 2 cell 12.61 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 12.61 s^(-1). Km: printed Table 2 cell 1.83 under the column head μmol/L; 1.83 / 1000 = 0.00183 mM; the exported value is 0.00183 mM. kcat/Km: printed Table 2 cell 6876 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 6876.0 s^-1 mM^-1; the exported value is 6890.710382513661 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row S02: kcat = 12.61 in the column head unit s−1; Km = 1.83 in the column head unit μmol/L; printed kcat/Km = 6876 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row S02 (the W474A/R526V/T560W site-directed variant of apAAP)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YBQ2 and applied mutation signature F488W/R526V/T560W to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = S015; second column 'Mutant' = F488W/R526V/T560W; column 'kcat (s−1)' = 1.73; column 'Km (μmol/L)' = 1.01; column 'kcat/Km (s−1 /mmol·L−1)' = 1712.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.73 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 1.73 s^(-1). Km: printed Table 2 cell 1.01 under the column head μmol/L; 1.01 / 1000 = 0.00101 mM; the exported value is 0.00101 mM. kcat/Km: printed Table 2 cell 1712 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 1712.0 s^-1 mM^-1; the exported value is 1712.8712871287128 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row S015: kcat = 1.73 in the column head unit s−1; Km = 1.01 in the column head unit μmol/L; printed kcat/Km = 1712 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row S015 (the F488W/R526V/T560W site-directed variant of apAAP)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YBQ2 and applied mutation signature F488S/R526V/T560W to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = S012; second column 'Mutant' = F488S/R526V/T560W; column 'kcat (s−1)' = 10.45; column 'Km (μmol/L)' = 5.79; column 'kcat/Km (s−1 /mmol·L−1)' = 1804.

normalized_value_unit_evidence: kcat: printed Table 2 cell 10.45 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 10.45 s^(-1). Km: printed Table 2 cell 5.79 under the column head μmol/L; 5.79 / 1000 = 0.00579 mM; the exported value is 0.00579 mM. kcat/Km: printed Table 2 cell 1804 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 1804.0 s^-1 mM^-1; the exported value is 1804.8359240069083 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row S012: kcat = 10.45 in the column head unit s−1; Km = 5.79 in the column head unit μmol/L; printed kcat/Km = 1804 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row S012 (the F488S/R526V/T560W site-directed variant of apAAP)


column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = WT; second column 'Mutant' = Wild type; column 'kcat (s−1)' = 1.35; column 'Km (μmol/L)' = 8.62; column 'kcat/Km (s−1 /mmol·L−1)' = 157.2.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.35 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 1.35 s^(-1). Km: printed Table 2 cell 8.62 under the column head μmol/L; 8.62 / 1000 = 0.00862 mM; the exported value is 0.00862 mM. kcat/Km: printed Table 2 cell 157.2 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 157.2 s^-1 mM^-1; the exported value is 156.6125290023202 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row WT: kcat = 1.35 in the column head unit s−1; Km = 8.62 in the column head unit μmol/L; printed kcat/Km = 157.2 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row WT (the wild type apAAP parent of that table)


organism: Alicyclobacillus acidocaldarius

substrate_name: p-Nitrophenyl dodecanoate

substrate: p-Nitrophenyl dodecanoate


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


sequence_variant_note: Mutation signature M211S matches the mutant residue at offset +0 and the reference residue at offset -1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


column_label: Table 1 (journal page 31), decoded transcription, enzyme row EST2, substrate column group Triacetin (C2): kcat (s^-1) = 945; Km/K0.5 (mM) = 12.

normalized_value_unit_evidence: kcat: printed cell 945 s^-1 -> 945.0 s^(-1); the catalog holds 945.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 12 mM -> 12.0 mM; the catalog holds 12.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 78.75 s^(-1)*mM^(-1) is the exact quotient 945 / 12 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


substrate_name: vinyl butyrate

column_label: Table 3 (journal page 32), decoded transcription, enzyme row EST2, substrate column group Vinyl butyrate (C4): kcat (s^-1) = 1930; Km/K0.5 (mM) = 3.

normalized_value_unit_evidence: kcat: printed cell 1930 s^-1 -> 1930.0 s^(-1); the catalog holds 1930.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 3 mM -> 3.0 mM; the catalog holds 3.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 643.3333333333334 s^(-1)*mM^(-1) is the exact quotient 1930 / 3 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

substrate: vinyl butyrate


column_label: Table 1 (journal page 31), decoded transcription, enzyme row EST2, substrate column group Tributyrin (C4): kcat (s^-1) = 1290; Km/K0.5 (mM) = 0.07.

normalized_value_unit_evidence: kcat: printed cell 1290 s^-1 -> 1290.0 s^(-1); the catalog holds 1290.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 0.07 mM -> 0.07 mM; the catalog holds 0.07 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 18428.571428571428 s^(-1)*mM^(-1) is the exact quotient 1290 / 0.07 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


organism: Aquamicrobium sp. FPB-1

sequence_source: UniProtKB A0A024CDT8 direct accession lookup


organism: Arabidopsis thaliana

substrate_name: Methyl indole-3-acetate

sequence_source: UniProtKB Q9SG92 direct accession lookup

substrate: Methyl indole-3-acetate


substrate_name: 4-nitrophenyl pentanoate

sequence_source: UniProtKB O28558 direct accession lookup

substrate: 4-nitrophenyl pentanoate


substrate_name: 4-nitrophenyl octanoate

substrate: 4-nitrophenyl octanoate


substrate_name: 4-nitrophenyl palmitate

sequence_source: UniProtKB O28511 direct accession lookup

substrate: 4-nitrophenyl palmitate


organism: Homo sapiens

substrate_name: L-Methylphenidate

substrate: L-Methylphenidate


substrate_name: D-Methylphenidate

substrate: D-Methylphenidate


substrate_name: Irinotecan

substrate: Irinotecan


substrate_name: vinyl laurate

substrate: vinyl laurate


substrate_name: p-Nitrophenyl butyrate

substrate: p-Nitrophenyl butyrate


substrate_name: vinyl propionate

substrate: vinyl propionate


substrate_name: Vinylacetate

substrate: Vinylacetate


enzyme_display_name: Carboxylesterase

substrate_name: 4-nitrophenyl hexanoate

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q2PCE5|exact_accession_lookup and applied mutation signature N248A/P256Q/E257G/S283F to reconstruct the assayed variant sequence.

enzyme: Carboxylesterase

substrate: 4-nitrophenyl hexanoate


substrate_name: 4-nitrophenyl propionate

substrate: 4-nitrophenyl propionate


substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


enzyme_display_name: Carboxylic ester hydrolase Est55

organism: Geobacillus stearothermophilus

substrate_name: p-Nitrophenyl caproate

enzyme: Carboxylic ester hydrolase Est55

substrate: p-Nitrophenyl caproate


enzyme_display_name: Carboxylesterase Est30

enzyme: Carboxylesterase Est30


enzyme_display_name: Liver carboxylesterase 1

kcat_display: Not reported

enzyme: Liver carboxylesterase 1


enzyme_display_name: Carboxylesterase 2

enzyme: Carboxylesterase 2


substrate_name: Capecitabine

sequence_source: UniProtKB:Q6LAP9 checked 2026-05-31; displayed sequence is a 17-aa TrEMBL fragment, not accepted as a resolved full enzyme sequence

substrate: Capecitabine


sequence_source: UniProtKB:O00748 displayed Swiss-Prot canonical sequence, fetched 2026-05-31


substrate_name: tributyrin

substrate: tributyrin


substrate_name: Triacetin

substrate: Triacetin


substrate_name: tripropionin

substrate: tripropionin


organism: Klebsiella sp.

substrate_name: 4-nitrophenyl dodecanoate

sequence_source: UniProtKB Q52NW7 direct accession lookup

substrate: 4-nitrophenyl dodecanoate


substrate_name: 4-nitrophenyl butanoate

substrate: 4-nitrophenyl butanoate


substrate_name: 4-nitrophenyl propanoate

substrate: 4-nitrophenyl propanoate


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB P9WK87 direct accession lookup

column_label: Table 4 (journal page 33), decoded transcription, enzyme row Rv1399c, substrate column group p-NPB (C4): kcat (s^-1) = 185; Km/K0.5 (mM) = 0.05.

normalized_value_unit_evidence: kcat: printed cell 185 s^-1 -> 185.0 s^(-1); the catalog holds 185.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 0.05 mM -> 0.05 mM; the catalog holds 0.05 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 3700.0 s^(-1)*mM^(-1) is the exact quotient 185 / 0.05 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

table_label: Table 4 (journal page 33) 'Kinetic parameters kcat and K0.5 of the hydrolysis of p-NPB by members of the HSL family'


organism: Oryctolagus cuniculus

substrate_name: Resmethrin

sequence_source: UniProtKB P12337 direct accession lookup

substrate: Resmethrin


organism: Pyrobaculum calidifontis

substrate_name: 4-nitrophenyl octanoate

sequence_source: UniProtKB Q8NKS0 direct accession lookup

substrate: 4-nitrophenyl octanoate


organism: Saccharolobus solfataricus

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q97VU1 and applied mutation signature R210A to reconstruct the assayed variant sequence.

column_label: Table 1 on journal page 1154, p-Nitrophenyl butyrate block, enzyme row R210A; column kcat/Km (s^-1 mM^-1) = 17; column Km (mM) = 0.63; column kcat (s^-1) = 10.

normalized_value_unit_evidence: kcat: printed Table 1 cell 10 s^-1; the printed column is already per second, so no unit conversion applies and the value carries over as 10.0 s^(-1). Km: printed Table 1 cell 0.63 mM; the printed column is already in mM, so no unit conversion applies and the value carries over as 0.63 mM. kcat/Km: printed Table 1 cell 17 s^-1 mM^-1; the printed unit is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 17.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R210A, p-Nitrophenyl butyrate block: kcat/Km = 17 s^-1 mM^-1; Km = 0.63 mM; kcat = 10 s^-1.

table_label: Table 1: Kinetic parameters of wild-type SsoPEst and R210A (Biotechnology Letters 2010, volume 32, pages 1151-1157)


sequence_source: UniProtKB M5DDN2 direct accession lookup.


substrate_name: 4-nitrophenyl hexadecanoate

substrate: 4-nitrophenyl hexadecanoate


substrate_name: 4-nitrophenyl decanoate

substrate: 4-nitrophenyl decanoate


organism: Sulfurisphaera tokodaii

sequence_source: UniProtKB Q976W8 direct accession lookup.


sequence_source: UniProtKB Q976W8 direct accession lookup


substrate_name: 4-nitrophenyl tetradecanoate

substrate: 4-nitrophenyl tetradecanoate


substrate_name: Cypermethrin

sequence_source: UniProtKB reviewed accession P23141 (EST1_HUMAN; CES1; liver carboxylesterase 1)

substrate: Cypermethrin


sequence_source: UniProtKB reviewed accession O00748 (EST2_HUMAN; CES2; carboxylesterase 2/cocaine esterase)


substrate_name: p-Nitrophenyl acetate

substrate: p-Nitrophenyl acetate


organism: Sus scrofa

sequence_source: UniProtKB:Q29550 reviewed Swiss-Prot EST1_PIG sequence


substrate_name: Irinotecan

substrate: Irinotecan


substrate_name: p-Nitrophenyl butyrate

substrate: p-Nitrophenyl butyrate


organism: Pyrococcus furiosus

substrate_name: 4-Methylumbelliferyl butyrate

sequence_variant_note: Resolved canonical sequence from UniProt REST accession Q8TZJ1 canonical sequence; W194A reconstructed directly and applied mutation signature W194A to reconstruct the assayed variant sequence.

substrate: 4-Methylumbelliferyl butyrate


substrate_name: 4-Methylumbelliferyl heptanoate

sequence_source: UniProt REST accession Q8TZJ1 canonical sequence

substrate: 4-Methylumbelliferyl heptanoate


sequence_variant_note: Resolved canonical sequence from UniProt REST accession Q8TZJ1 canonical sequence; F198A reconstructed directly and applied mutation signature F198A to reconstruct the assayed variant sequence.


organism: Rhizomucor miehei


substrate_name: vinyl propionate

substrate: vinyl propionate


substrate_name: vinyl laurate

substrate: vinyl laurate


substrate_name: tripropionin

substrate: tripropionin


substrate_name: L-Phenylalanine ethyl ester

sequence_source: UniProtKB reviewed entry Q29550 (EST1_PIG) direct accession lookup

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

substrate: L-Phenylalanine ethyl ester


substrate_name: N-Acetyl-L-phenylalanine ethyl ester

substrate: N-Acetyl-L-phenylalanine ethyl ester


substrate_name: L-Phenylalanine benzyl ester

substrate: L-Phenylalanine benzyl ester


substrate_name: valacyclovir

substrate: valacyclovir


substrate_name: 4-nitrophenyl propanoate

substrate: 4-nitrophenyl propanoate


substrate_name: 4-nitrophenyl pentanoate

substrate: 4-nitrophenyl pentanoate


substrate_name: 4-nitrophenyl hexanoate

substrate: 4-nitrophenyl hexanoate


organism: Pyrobaculum sp.

substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl octanoate

substrate: 4-nitrophenyl octanoate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: 4-nitrophenyl decanoate

substrate: 4-nitrophenyl decanoate


sequence_variant_note: Resolved canonical sequence from uniprot_accession_w194a_reconstruction and applied mutation signature W194A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q29550 direct accession lookup


substrate_name: Triacetin

column_label: Table 1 (journal page 31), decoded transcription, enzyme row PLEst, substrate column group Triacetin (C2): kcat (s^-1) = 60; Km/K0.5 (mM) = 3.

normalized_value_unit_evidence: kcat: printed cell 60 s^-1 -> 60.0 s^(-1); the catalog holds 60.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 3 mM -> 3.0 mM; the catalog holds 3.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 20.0 s^(-1)*mM^(-1) is the exact quotient 60 / 3 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

substrate: Triacetin


column_label: Table 1 (journal page 31), decoded transcription, enzyme row PLEst, substrate column group Tripropionin (C3): kcat (s^-1) = 50; Km/K0.5 (mM) = 0.30.

normalized_value_unit_evidence: kcat: printed cell 50 s^-1 -> 50.0 s^(-1); the catalog holds 50.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 0.30 mM -> 0.3 mM; the catalog holds 0.3 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 166.66666666666669 s^(-1)*mM^(-1) is the exact quotient 50 / 0.30 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


substrate_name: tributyrin

column_label: Table 1 (journal page 31), decoded transcription, enzyme row PLEst, substrate column group Tributyrin (C4): kcat (s^-1) = 70; Km/K0.5 (mM) = 0.05.

normalized_value_unit_evidence: kcat: printed cell 70 s^-1 -> 70.0 s^(-1); the catalog holds 70.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 0.05 mM -> 0.05 mM; the catalog holds 0.05 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 1400.0 s^(-1)*mM^(-1) is the exact quotient 70 / 0.05 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

substrate: tributyrin


substrate_name: Vinylacetate

column_label: Table 3 (journal page 32), decoded transcription, enzyme row PLEst, substrate column group Vinyl acetate (C2): kcat (s^-1) = 315; Km/K0.5 (mM) = 4.

normalized_value_unit_evidence: kcat: printed cell 315 s^-1 -> 315.0 s^(-1); the catalog holds 315.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 4 mM -> 4.0 mM; the catalog holds 4.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 78.75 s^(-1)*mM^(-1) is the exact quotient 315 / 4 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

substrate: Vinylacetate


substrate_name: vinyl propionate

column_label: Table 3 (journal page 32), decoded transcription, enzyme row PLEst, substrate column group Vinyl propionate (C3): kcat (s^-1) = 295; Km/K0.5 (mM) = 5.

normalized_value_unit_evidence: kcat: printed cell 295 s^-1 -> 295.0 s^(-1); the catalog holds 295.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 5 mM -> 5.0 mM; the catalog holds 5.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 59.0 s^(-1)*mM^(-1) is the exact quotient 295 / 5 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

substrate: vinyl propionate


substrate_name: vinyl butyrate

column_label: Table 3 (journal page 32), decoded transcription, enzyme row PLEst, substrate column group Vinyl butyrate (C4): kcat (s^-1) = 460; Km/K0.5 (mM) = 2.

normalized_value_unit_evidence: kcat: printed cell 460 s^-1 -> 460.0 s^(-1); the catalog holds 460.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 2 mM -> 2.0 mM; the catalog holds 2.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 230.0 s^(-1)*mM^(-1) is the exact quotient 460 / 2 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

substrate: vinyl butyrate


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


organism: Saccharolobus shibatae

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5NU42 plus Q249P/G250E reconstruction and applied mutation signature Q249P/G250E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5NU42 plus A241N/Q249P/G250E/F276S reconstruction and applied mutation signature A241N/Q249P/G250E/F276S to reconstruct the assayed variant sequence.


organism: Thermomyces lanuginosus


substrate_name: tripropionin

substrate: tripropionin


substrate_name: p-Nitrophenyl butyrate

substrate: p-Nitrophenyl butyrate


substrate_name: vinyl laurate

substrate: vinyl laurate


organism: Vulcanisaeta moutnovskia


substrate_name: 4-nitrophenyl dodecanoate

substrate: 4-nitrophenyl dodecanoate


substrate_name: 4-nitrophenyl hexadecanoate

substrate: 4-nitrophenyl hexadecanoate


substrate_name: 4-nitrophenyl caprylate

sequence_source: UniProtKB Q97VU1 direct REST FASTA/JSON, sequence version 1

column_label: Table 1 on journal page 1154, p-Nitrophenyl caprylate block, enzyme row Wild-type; column kcat/Km (s^-1 mM^-1) = 63; column Km (uM) = 28; column kcat (s^-1) = 1.7.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.7 s^-1; the printed column is already per second, so no unit conversion applies and the value carries over as 1.7 s^(-1). Km: printed Table 1 cell 28 uM; 1 uM is 1/1000 mM, so 28 / 1000 = 0.028 mM. kcat/Km: printed Table 1 cell 63 s^-1 mM^-1; the printed unit is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 63.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row Wild-type, p-Nitrophenyl caprylate block: kcat/Km = 63 s^-1 mM^-1; Km = 28 uM; kcat = 1.7 s^-1.

substrate: 4-nitrophenyl caprylate


column_label: Table 1 on journal page 1154, p-Nitrophenyl butyrate block, enzyme row Wild-type; column kcat/Km (s^-1 mM^-1) = 5.1; column Km (mM) = 0.93; column kcat (s^-1) = 4.

normalized_value_unit_evidence: kcat: printed Table 1 cell 4 s^-1; the printed column is already per second, so no unit conversion applies and the value carries over as 4.0 s^(-1). Km: printed Table 1 cell 0.93 mM; the printed column is already in mM, so no unit conversion applies and the value carries over as 0.93 mM. kcat/Km: printed Table 1 cell 5.1 s^-1 mM^-1; the printed unit is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 5.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row Wild-type, p-Nitrophenyl butyrate block: kcat/Km = 5.1 s^-1 mM^-1; Km = 0.93 mM; kcat = 4 s^-1.


column_label: Table 1 on journal page 1154, p-Nitrophenyl caprylate block, enzyme row R210A; column kcat/Km (s^-1 mM^-1) = 192; column Km (uM) = 43; column kcat (s^-1) = 7.8.

normalized_value_unit_evidence: kcat: printed Table 1 cell 7.8 s^-1; the printed column is already per second, so no unit conversion applies and the value carries over as 7.8 s^(-1). Km: printed Table 1 cell 43 uM; 1 uM is 1/1000 mM, so 43 / 1000 = 0.043 mM. kcat/Km: printed Table 1 cell 192 s^-1 mM^-1; the printed unit is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 192.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R210A, p-Nitrophenyl caprylate block: kcat/Km = 192 s^-1 mM^-1; Km = 43 uM; kcat = 7.8 s^-1.


enzyme_display_name: acetate kinase

organism: Methanosarcina thermophila

substrate_name: Acetate

sequence_source: reconstructed from UniProtKB:P38502 canonical sequence via H180E; UniProt REST direct check 2026-06-01

smiles: CC(=O)O

enzyme: acetate kinase

substrate: Acetate


substrate_name: ATP

sequence_source: reconstructed from UniProtKB:P38502 canonical sequence via H180Q; UniProt REST direct check 2026-06-01

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

substrate: ATP


sequence_source: reconstructed from UniProtKB:P38502 canonical sequence via H123A; UniProt REST direct check 2026-06-01


sequence_source: reconstructed from UniProtKB:P38502 canonical sequence via H180N; UniProt REST direct check 2026-06-01


sequence_source: reconstructed from UniProtKB:P38502 canonical sequence via H180D; UniProt REST direct check 2026-06-01


sequence_source: reconstructed from UniProtKB:P38502 canonical sequence via H180R; UniProt REST direct check 2026-06-01


organism: Escherichia coli

substrate_name: ADP

assay_conditions_summary: pH 7.5; 283.15 K; cofactor ADP

substrate: ADP


assay_conditions_summary: pH 7.5; 283.15 K; cofactor ATP


substrate_name: acetate

substrate: acetate


substrate_name: acetyl phosphate

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

substrate: acetyl phosphate


substrate_name: Acetate, acetate

substrate: Acetate, acetate


sequence_variant_note: Resolved canonical sequence from UniProtKB P38502 canonical sequence reconstructed with mutation N7A and applied mutation signature N7A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38502 canonical sequence reconstructed with mutation K14R and applied mutation signature K14R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38502 canonical sequence reconstructed with mutation S12T and applied mutation signature S12T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38502 canonical sequence reconstructed with mutation D148N and applied mutation signature D148N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38502 canonical sequence reconstructed with mutation S10T and applied mutation signature S10T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38502 canonical sequence reconstructed with mutation S10A and applied mutation signature S10A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P38502 canonical sequence reconstructed with mutation D148N


sequence_source: UniProtKB P38502 canonical sequence reconstructed with mutation K14R


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical sequence plus direct mutation reconstruction and applied mutation signature H123A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical sequence plus direct mutation reconstruction and applied mutation signature H184A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P38502 canonical sequence plus direct mutation reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical sequence plus direct mutation reconstruction and applied mutation signature H180D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical sequence plus direct mutation reconstruction and applied mutation signature H180K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical sequence plus direct mutation reconstruction and applied mutation signature D148E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical sequence plus direct mutation reconstruction and applied mutation signature S10T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical sequence plus direct mutation reconstruction and applied mutation signature N7D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 direct accession lookup and applied mutation signature G331Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


substrate_name: ITP

sequence_source: UniProtKB:P38502 direct accession lookup

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

substrate: ITP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 direct accession lookup and applied mutation signature G239A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 direct accession lookup and applied mutation signature G239S to reconstruct the assayed variant sequence.


substrate_name: TTP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 direct accession lookup and applied mutation signature G331A to reconstruct the assayed variant sequence.

substrate: TTP


substrate_name: UTP

substrate: UTP


organism: Methylotuvimicrobium alcaliphilum


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: propionate

substrate: propionate


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


substrate_name: formate

smiles: O=CO

substrate: formate


enzyme_display_name: Acetate kinase

enzyme_name_source: UniProt P38502

sequence_variant_note: Resolved canonical sequence from UniProt P38502 canonical sequence reconstructed as H180A after confirming H at canonical position 180; source row links accession P38502 and PMID 10958794. and applied mutation signature H180A to reconstruct the assayed variant sequence.

enzyme: Acetate kinase


sequence_variant_note: Resolved canonical sequence from UniProt P38502 canonical sequence reconstructed as H180K after confirming H at canonical position 180; source row links accession P38502 and PMID 10958794. and applied mutation signature H180K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P38502 canonical sequence reconstructed as H90A after confirming H at canonical position 90; source row links accession P38502 and PMID 10958794. and applied mutation signature H90A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P38502 canonical sequence reconstructed as H60A after confirming H at canonical position 60; source row links accession P38502 and PMID 10958794. and applied mutation signature H60A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P38502 canonical sequence reconstructed as H180N after confirming H at canonical position 180; source row links accession P38502 and PMID 10958794. and applied mutation signature H180N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P38502 canonical sequence reconstructed as H94A after confirming H at canonical position 94; source row links accession P38502 and PMID 10958794. and applied mutation signature H94A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P38502 canonical sequence reconstructed as H208A after confirming H at canonical position 208; source row links accession P38502 and PMID 10958794. and applied mutation signature H208A to reconstruct the assayed variant sequence.


sequence_source: UniProt P38502 canonical sequence reconstructed as H94A after confirming H at canonical position 94; source row links accession P38502 and PMID 10958794.


sequence_source: UniProt REST P38502 canonical sequence; S11T reconstructed after validating the source residue at position 11.

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


sequence_source: UniProt REST P38502 canonical sequence; N211A reconstructed after validating the source residue at position 211.


sequence_source: UniProt REST P38502 canonical sequence; S10A reconstructed after validating the source residue at position 10.


sequence_source: UniProt REST P38502 canonical sequence; D148A reconstructed after validating the source residue at position 148.


sequence_source: UniProt REST P38502 canonical sequence; E384A reconstructed after validating the source residue at position 384.


sequence_source: UniProt REST P38502 canonical sequence; G331Q reconstructed after validating the source residue at position 331.


sequence_source: UniProt REST P38502 canonical sequence.


substrate_name: CTP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical reviewed sequence with selected mutation_signature G331Q applied during review and applied mutation signature G331Q to reconstruct the assayed variant sequence.

substrate: CTP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical reviewed sequence with selected mutation_signature G331A applied during review and applied mutation signature G331A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P38502 canonical reviewed sequence checked directly on 2026-06-01

assay_conditions_summary: pH 7; 355.15 K; cofactor ADP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical reviewed sequence with selected mutation_signature G331Q/I332M applied during review and applied mutation signature G331Q/I332M to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P38502 canonical reviewed sequence with selected mutation_signature G331Q/I332M applied during review

assay_conditions_summary: pH 5.5; 355.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical ACKA_METTE sequence with reviewer-applied S12T substitution and applied mutation signature S12T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical ACKA_METTE sequence with reviewer-applied S11A substitution and applied mutation signature S11A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical ACKA_METTE sequence with reviewer-applied S11T substitution and applied mutation signature S11T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical ACKA_METTE sequence with reviewer-applied N7D substitution and applied mutation signature N7D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical ACKA_METTE sequence with reviewer-applied S12A substitution and applied mutation signature S12A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical ACKA_METTE sequence with reviewer-applied D148A substitution and applied mutation signature D148A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P38502 canonical ACKA_METTE sequence with reviewer-applied K14A substitution and applied mutation signature K14A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P38502 canonical ACKA_METTE sequence with reviewer-applied S11A substitution


sequence_source: UniProtKB:P63411 direct REST lookup

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

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP


organism: Shewanella sp.

sequence_source: UniProtKB:E3W769 direct REST lookup


substrate_name: GTP

sequence_source: UniProtKB P38502 canonical wild-type sequence

substrate: GTP


sequence_variant_note: Resolved canonical sequence from UniProtKB P38502 canonical sequence with G331Q reconstructed after confirming residue 331=G and applied mutation signature G331Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38502 canonical sequence with N211T reconstructed after confirming residue 211=N and applied mutation signature N211T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P38502 canonical sequence with N211S reconstructed after confirming residue 211=N and applied mutation signature N211S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P38502 canonical sequence with G331Q reconstructed after confirming residue 331=G


sequence_variant_note: Resolved canonical sequence from UniProtKB P38502 canonical sequence with G331A reconstructed after confirming residue 331=G and applied mutation signature G331A to reconstruct the assayed variant sequence.


enzyme_display_name: penicillin amidase

substrate_name: Cephaloridine

sequence_source: UniProtKB reviewed canonical sequence P06875 (REST/FASTA checked 2026-06-01)

enzyme: penicillin amidase

substrate: Cephaloridine


substrate_name: p-Nitrophenyl phenylacetate

substrate: p-Nitrophenyl phenylacetate


substrate_name: Benzylpenicilloic acid

substrate: Benzylpenicilloic acid


substrate_name: ethyl 2-phenylacetate

substrate: ethyl 2-phenylacetate


substrate_name: Phenylacetylglycine

substrate: Phenylacetylglycine


substrate_name: Cephalothin

substrate: Cephalothin


substrate_name: phenylacetate 4-nitroanilide

substrate: phenylacetate 4-nitroanilide


sequence_variant_note: Resolved canonical sequence from UniProtKB:P06875 canonical sequence via UniProt REST; beta-chain substitutions use UniProt beta-chain feature start residue 290. and applied mutation signature F24Y with inferred residue-numbering offset +289 to reconstruct the assayed variant sequence.


substrate_name: Methyl 2-phenylacetate

sequence_source: UniProtKB:P06875 canonical sequence via UniProt REST; beta-chain substitutions use UniProt beta-chain feature start residue 290.

substrate: Methyl 2-phenylacetate


substrate_name: amoxicillin

column_label: Table 3 (journal page 2097 (PDF page 6)); substrate row 'amoxicillin'; wild-type column group 'WT'; column 'kcat (s^-1)' = 22; column 'Km (mM)' = 1.1; column 'kcat/Km (mM^-1 s^-1)' = 20.

normalized_value_unit_evidence: kcat: printed Table 3 cell 22 s^-1; already in s^-1, no conversion; the exported value is 22.0 s^(-1). Km: printed Table 3 cell 1.1 mM; already in mM, no conversion; the exported value is 1.1 mM. kcat/Km: printed Table 3 cell 20 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^(-1)*mM^(-1), so the printed cell is 20.0 s^(-1)*mM^(-1); the exported value is 20.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 2097 (PDF page 6)), substrate row 'amoxicillin', wild-type column group 'WT': kcat = 22 s^-1; Km = 1.1 mM; printed kcat/Km = 20 mM^-1 s^-1.

row_label: Table 3, substrate row 'amoxicillin', wild-type column group 'WT'

table_label: Table 3. Steady-state kinetic parameters of wild-type penicillin acylase and the bF24A mutant for the hydrolysis of various acyl donors and antibiotics.

substrate: amoxicillin


substrate_name: D-4-Hydroxyphenylglycine amide

substrate: D-4-Hydroxyphenylglycine amide


substrate_name: D-Phenylglycine amide

column_label: Table 3 (journal page 2097 (PDF page 6)); substrate row 'PGA (D-phenylglycine amide)'; wild-type column group 'WT'; column 'kcat (s^-1)' = 30; column 'Km (mM)' = 40; column 'kcat/Km (mM^-1 s^-1)' = 0.75.

normalized_value_unit_evidence: kcat: printed Table 3 cell 30 s^-1; already in s^-1, no conversion; the exported value is 30.0 s^(-1). Km: printed Table 3 cell 40 mM; already in mM, no conversion; the exported value is 40.0 mM. kcat/Km: printed Table 3 cell 0.75 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^(-1)*mM^(-1), so the printed cell is 0.75 s^(-1)*mM^(-1); the exported value is 0.75 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 2097 (PDF page 6)), substrate row 'PGA (D-phenylglycine amide)', wild-type column group 'WT': kcat = 30 s^-1; Km = 40 mM; printed kcat/Km = 0.75 mM^-1 s^-1.

row_label: Table 3, substrate row 'PGA (D-phenylglycine amide)', wild-type column group 'WT'

substrate: D-Phenylglycine amide


sequence_variant_note: Resolved canonical sequence from UniProtKB:P06875 canonical sequence via UniProt REST; beta-chain substitutions use UniProt beta-chain feature start residue 290. and applied mutation signature F24A with inferred residue-numbering offset +289 to reconstruct the assayed variant sequence.


substrate_name: D-4-Hydroxyphenylglycine methyl ester

substrate: D-4-Hydroxyphenylglycine methyl ester


sequence_variant_note: Resolved canonical sequence from UniProtKB:P06875 canonical sequence via UniProt REST; beta-chain substitutions use UniProt beta-chain feature start residue 290. and applied mutation signature F57Y with inferred residue-numbering offset +289 to reconstruct the assayed variant sequence.


substrate_name: Penicillin G

sequence_source: UniProtKB reviewed entry P06875 direct FASTA

substrate: Penicillin G


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


column_label: Table 1 (journal page 2096 (PDF page 5)); substrate row 'NIPAB (2-nitro-5-[(phenylacetyl)amino]benzoic acid)'; wild-type column group 'WT'; column 'kcat (s^-1)' = 16.2; column 'Km (mM)' = 0.015; column 'kcat/Km (mM^-1 s^-1)' = 1080. The row's fourth column 'KiPAA (mM)' = 0.05 is the product inhibition constant.

normalized_value_unit_evidence: kcat: printed Table 1 cell 16.2 s^-1; already in s^-1, no conversion; the exported value is 16.2 s^(-1). Km: printed Table 1 cell 0.015 mM; already in mM, no conversion; the exported value is 0.011 mM. kcat/Km: printed Table 1 cell 1080 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^(-1)*mM^(-1), so the printed cell is 1080.0 s^(-1)*mM^(-1); the exported value is 1472.7272727272727 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1 (journal page 2096 (PDF page 5)), substrate row 'NIPAB (2-nitro-5-[(phenylacetyl)amino]benzoic acid)', wild-type column group 'WT': kcat = 16.2 s^-1; Km = 0.015 mM; printed kcat/Km = 1080 mM^-1 s^-1.

row_label: Table 1, substrate row 'NIPAB (2-nitro-5-[(phenylacetyl)amino]benzoic acid)', wild-type column group 'WT'

table_label: Table 1. Steady-state kinetic parameters of wild-type and penicillin acylase mutants for the hydrolysis of NIPAB and Ki values for the product phenylacetic acid (PAA).


column_label: Table 3 (journal page 2097 (PDF page 6)); substrate row 'PAAM (2-phenylacetamide)'; wild-type column group 'WT'; column 'kcat (s^-1)' = 50; column 'Km (mM)' = 0.20; column 'kcat/Km (mM^-1 s^-1)' = 250.

normalized_value_unit_evidence: kcat: printed Table 3 cell 50 s^-1; already in s^-1, no conversion; the exported value is 50.0 s^(-1). Km: printed Table 3 cell 0.20 mM; already in mM, no conversion; the exported value is 0.16 mM. kcat/Km: printed Table 3 cell 250 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^(-1)*mM^(-1), so the printed cell is 250.0 s^(-1)*mM^(-1); the exported value is 312.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 2097 (PDF page 6)), substrate row 'PAAM (2-phenylacetamide)', wild-type column group 'WT': kcat = 50 s^-1; Km = 0.20 mM; printed kcat/Km = 250 mM^-1 s^-1.

row_label: Table 3, substrate row 'PAAM (2-phenylacetamide)', wild-type column group 'WT'


sequence_source: UniProtKB:P06875 canonical sequence reconstructed as beta F24->A using UniProt beta chain start 290 plus PMID 11985586 betaF24 label

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


substrate_name: cephalexin

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P06875 and applied mutation signature F24A with inferred residue-numbering offset +289 to reconstruct the assayed variant sequence.

column_label: Table 3 carries one Substrate column and then two enzyme blocks, WT and bF24A, each printing the three column heads k_cat (s^-1), K_m (mM) and k_cat/K_m (mM^-1 s^-1). The cited cell set is the bF24A block of substrate row Cephalexin: k_cat (s^-1) = 9.8; K_m (mM) = 2.8; k_cat/K_m (mM^-1 s^-1) = 3.48.

normalized_value_unit_evidence: kcat: printed Table 3 cell 9.8 s^-1 in the bF24A block of substrate row Cephalexin; the printed turnover column of this table is already per second, so no unit conversion applies and the paper value is 9.8 s^(-1). Km: printed Table 3 cell 2.8 under the column head K_m (mM); the column is already in mM, so no unit conversion applies and the paper value is 2.8 mM. kcat/Km: printed Table 3 cell 3.48 under the column head k_cat/K_m (mM^-1 s^-1); the column is already per millimolar per second, so no unit conversion applies and the paper value is 3.48 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, bF24A enzyme block, substrate row Cephalexin: kcat = 9.8 s^-1; Km = 2.8 mM; printed kcat/Km = 3.48 mM^-1 s^-1.

table_label: Table 3: Steady-state kinetic parameters of wild-type penicillin acylase and the bF24A mutant for the hydrolysis of various acyl donors and antibiotics (Eur. J. Biochem. 2002, 269(8):2093-2100)

substrate: cephalexin


substrate_name: Ampicillin

substrate: Ampicillin


sequence_source: UniProtKB:P06875 canonical sequence reconstructed as beta F57->W using UniProt beta chain start 290 plus PMID 11985586 betaF57 label

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


sequence_source: UniProtKB:P06875 canonical sequence from direct REST lookup

column_label: Table 3 (journal page 2097 (PDF page 6)); substrate row 'ampicillin'; wild-type column group 'WT'; column 'kcat (s^-1)' = 30; column 'Km (mM)' = 2.5; column 'kcat/Km (mM^-1 s^-1)' = 12.

normalized_value_unit_evidence: kcat: printed Table 3 cell 30 s^-1; already in s^-1, no conversion; the exported value is 30.0 s^(-1). Km: printed Table 3 cell 2.5 mM; already in mM, no conversion; the exported value is 2.5 mM. kcat/Km: printed Table 3 cell 12 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^(-1)*mM^(-1), so the printed cell is 12.0 s^(-1)*mM^(-1); the exported value is 12.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 2097 (PDF page 6)), substrate row 'ampicillin', wild-type column group 'WT': kcat = 30 s^-1; Km = 2.5 mM; printed kcat/Km = 12 mM^-1 s^-1.

row_label: Table 3, substrate row 'ampicillin', wild-type column group 'WT'


sequence_source: UniProtKB:P06875 canonical sequence reconstructed as beta F24->W using UniProt beta chain start 290 plus PMID 11985586 betaF24 label

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -4, so it is treated as a source-provided variant sequence.


sequence_source: UniProtKB:P06875 canonical sequence reconstructed as alpha F146->W using UniProt alpha chain start 27 plus PMID 11985586 alphaF146 label

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +9, so it is treated as a source-provided variant sequence.


sequence_source: UniProtKB:P06875 canonical sequence reconstructed as beta F24->L using UniProt beta chain start 290 plus PMID 11985586 betaF24 label

sequence_variant_note: Mutation signature F24L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: cefadroxil

column_label: Table 3 carries one Substrate column and then two enzyme blocks, WT and bF24A, each printing the three column heads k_cat (s^-1), K_m (mM) and k_cat/K_m (mM^-1 s^-1). The cited cell set is the bF24A block of substrate row Cefadroxil: k_cat (s^-1) = 5.2; K_m (mM) = 0.76; k_cat/K_m (mM^-1 s^-1) = 6.87.

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.2 s^-1 in the bF24A block of substrate row Cefadroxil; the printed turnover column of this table is already per second, so no unit conversion applies and the paper value is 5.2 s^(-1). Km: printed Table 3 cell 0.76 under the column head K_m (mM); the column is already in mM, so no unit conversion applies and the paper value is 0.76 mM. kcat/Km: printed Table 3 cell 6.87 under the column head k_cat/K_m (mM^-1 s^-1); the column is already per millimolar per second, so no unit conversion applies and the paper value is 6.87 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, bF24A enzyme block, substrate row Cefadroxil: kcat = 5.2 s^-1; Km = 0.76 mM; printed kcat/Km = 6.87 mM^-1 s^-1.

substrate: cefadroxil


sequence_variant_note: Resolved canonical sequence from UniProt P06875 canonical sequence plus row-specific reconstruction: beta-chain F24 maps to canonical P06875 position 313; residue F313 was replaced with A. and applied mutation signature F24A with inferred residue-numbering offset +289 to reconstruct the assayed variant sequence.


sequence_source: UniProt P06875 canonical sequence; accession checked directly against UniProt on 2026-06-01.

column_label: Table 3 (journal page 2097 (PDF page 6)); substrate row 'cephalexin'; wild-type column group 'WT'; column 'kcat (s^-1)' = 57; column 'Km (mM)' = 1.2; column 'kcat/Km (mM^-1 s^-1)' = 47.5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 57 s^-1; already in s^-1, no conversion; the exported value is 57.0 s^(-1). Km: printed Table 3 cell 1.2 mM; already in mM, no conversion; the exported value is 1.2 mM. kcat/Km: printed Table 3 cell 47.5 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^(-1)*mM^(-1), so the printed cell is 47.5 s^(-1)*mM^(-1); the exported value is 47.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 2097 (PDF page 6)), substrate row 'cephalexin', wild-type column group 'WT': kcat = 57 s^-1; Km = 1.2 mM; printed kcat/Km = 47.5 mM^-1 s^-1.

row_label: Table 3, substrate row 'cephalexin', wild-type column group 'WT'


sequence_source: UniProt P06875 canonical sequence plus row-specific reconstruction: beta-chain F24 maps to canonical P06875 position 313; residue F313 was replaced with A.


substrate_name: D-Phenylglycine methyl ester

substrate: D-Phenylglycine methyl ester


column_label: Table 3 (journal page 2097 (PDF page 6)); substrate row 'cefadroxil'; wild-type column group 'WT'; column 'kcat (s^-1)' = 50; column 'Km (mM)' = 1; column 'kcat/Km (mM^-1 s^-1)' = 50.

normalized_value_unit_evidence: kcat: printed Table 3 cell 50 s^-1; already in s^-1, no conversion; the exported value is 50.0 s^(-1). Km: printed Table 3 cell 1 mM; already in mM, no conversion; the exported value is 1.0 mM. kcat/Km: printed Table 3 cell 50 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^(-1)*mM^(-1), so the printed cell is 50.0 s^(-1)*mM^(-1); the exported value is 50.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 2097 (PDF page 6)), substrate row 'cefadroxil', wild-type column group 'WT': kcat = 50 s^-1; Km = 1 mM; printed kcat/Km = 50 mM^-1 s^-1.

row_label: Table 3, substrate row 'cefadroxil', wild-type column group 'WT'


sequence_variant_note: Resolved canonical sequence from UniProt P06875 canonical sequence plus row-specific reconstruction: beta-chain F57 maps to canonical P06875 position 346; residue F346 was replaced with L. and applied mutation signature F57L with inferred residue-numbering offset +289 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P06875 direct REST lookup on 2026-06-01

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


organism: Kluyvera citrophila

sequence_source: UniProtKB:P07941 direct REST lookup on 2026-06-01


organism: Lysinibacillus sphaericus

substrate_name: Penicillin V

sequence_source: UniProtKB:P12256 direct REST lookup on 2026-06-01

substrate: Penicillin V


sequence_variant_note: Resolved canonical sequence from UniProtKB:P12256 direct REST lookup plus T63S/S110C/N198Y reconstruction on 2026-06-01 and applied mutation signature T63S/S110C/N198Y to reconstruct the assayed variant sequence.


organism: Providencia rettgeri

sequence_source: UniProtKB:A0A2I6UI54 direct REST lookup on 2026-06-01


organism: Streptomyces lavendulae subsp. lavendulae

substrate_name: penicillin G

sequence_source: UniProtKB:Q539C0 direct REST lookup on 2026-06-01

substrate: penicillin G


substrate_name: penicillin K

substrate: penicillin K


sequence_source: UniProtKB Q539C0 direct lookup; sequence version 1.


substrate_name: penicillin F

substrate: penicillin F


substrate_name: penicillin dihydroF

substrate: penicillin dihydroF


organism: Thermus thermophilus

sequence_source: UniProtKB Q72G76 direct lookup plus PMID 23263966 mutation-coordinate reconstruction.

sequence_variant_note: Mutation signature I57F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature L24F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature L188F/L24F/I57F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature S189F matches the mutant residue at offset +0 and the reference residue at offset -4; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


organism: uncultured bacterium

sequence_source: NCBI Protein ADG60270.1 via UniParc UPI0001D2CD09 cross-reference from deleted UniProtKB D6R1Q1

column_label: Table 3 (Kinetic parameters of ACPGA001 PGA), substrate row 'Cephalexin'; column 'kcat (S-1)' = 34.2; column 'Km (uM)' = 25.5; column 'kcat/Km (uM-1 S-1)' = 1.35.

normalized_value_unit_evidence: kcat: printed Table 3 cell 34.2 under the column head kcat (S-1); that column is already per second, so no unit conversion applies and the paper value is 34.2 s^(-1). Km: printed Table 3 cell 25.5 under the column head Km (uM); 25.5 / 1000 = 0.0255 mM. kcat/Km: printed Table 3 cell 1.35 under the column head kcat/Km (uM-1 S-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 1.35 x 1000 = 1350.0 s^(-1)*mM^(-1), and that printed cell is the catalytic efficiency this pass carries over as the paper's own value. Closure disclosure: dividing the two printed component cells of the same substrate row gives 34.2 / 0.0255 = 1341.1764705882356 s^-1 mM^-1, which at the two decimals this column prints would read 1.34 uM^-1 S^-1, while the efficiency cell the table prints for this substrate row stands at 1.35 uM^-1 S^-1.

raw_value_unit_evidence: Table 3, substrate row 'Cephalexin': kcat = 34.2 under the column head kcat (S-1); Km = 25.5 under the column head Km (uM); printed kcat/Km = 1.35 under the column head kcat/Km (uM-1 S-1).

row_label: Table 3, substrate row 'Cephalexin'

table_label: Table 3: Kinetic parameters of ACPGA001 PGA (Biotechnol Lett 2014, 36, 617-625)


sequence_source: UniProtKB P06875 sequence version 2 plus chain-aware PubMed mutation mapping; PMID 11239085 names alphaF146Y; UniProt P06875 places the alpha chain at precursor residues 27-235, so alpha F146 maps to precursor residue 172, which is F in the canonical sequence.

sequence_variant_note: Mutation signature F146Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB P06875 sequence version 2 plus chain-aware PubMed mutation mapping; PMID 11239085 names alphaF146L; UniProt P06875 places the alpha chain at precursor residues 27-235, so alpha F146 maps to precursor residue 172, which is F in the canonical sequence.

sequence_variant_note: Mutation signature F146L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB P06875 FASTA direct lookup, sequence version 2, reviewed Swiss-Prot entry.


sequence_source: UniProtKB P06875 sequence version 2 plus chain-aware PubMed mutation mapping; PMID 11985586 names betaF57 substitutions; UniProt P06875 places the beta chain at precursor residues 290-846, so beta F57 maps to precursor residue 346, which is F in the canonical sequence.

sequence_variant_note: Mutation signature F57A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


column_label: Table 3 carries one Substrate column and then two enzyme blocks, WT and bF24A, each printing the three column heads k_cat (s^-1), K_m (mM) and k_cat/K_m (mM^-1 s^-1). The cited cell set is the bF24A block of substrate row PAAM: k_cat (s^-1) = 3.9; K_m (mM) = 2; k_cat/K_m (mM^-1 s^-1) = 1.94.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.9 s^-1 in the bF24A block of substrate row PAAM; the printed turnover column of this table is already per second, so no unit conversion applies and the paper value is 3.9 s^(-1). Km: printed Table 3 cell 2 under the column head K_m (mM); the column is already in mM, so no unit conversion applies and the paper value is 2.0 mM. kcat/Km: printed Table 3 cell 1.94 under the column head k_cat/K_m (mM^-1 s^-1); the column is already per millimolar per second, so no unit conversion applies and the paper value is 1.94 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, bF24A enzyme block, substrate row PAAM: kcat = 3.9 s^-1; Km = 2 mM; printed kcat/Km = 1.94 mM^-1 s^-1.


substrate_name: cephalothin

sequence_source: NCBI Protein ADG60270.1, linked from PMID 24338159 and UniParc UPI0001D2CD09 cross-reference; UniProt D6R1Q1 itself is deleted/inactive.

column_label: Table 3 (Kinetic parameters of ACPGA001 PGA), substrate row 'Cephalothin'; column 'kcat (S-1)' = 78.3; column 'Km (uM)' = 15.6; column 'kcat/Km (uM-1 S-1)' = 5.02.

normalized_value_unit_evidence: kcat: printed Table 3 cell 78.3 under the column head kcat (S-1); that column is already per second, so no unit conversion applies and the paper value is 78.3 s^(-1). Km: printed Table 3 cell 15.6 under the column head Km (uM); 15.6 / 1000 = 0.0156 mM. kcat/Km: printed Table 3 cell 5.02 under the column head kcat/Km (uM-1 S-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 5.02 x 1000 = 5020.0 s^(-1)*mM^(-1). Quotient disclosure for this substrate row: 78.3 / 0.0156 = 5019.2307692307695 s^-1 mM^-1, which is the catalytic efficiency the catalog carries, and the printed cell 5.02 is that quotient written to the two decimals this column prints.

raw_value_unit_evidence: Table 3, substrate row 'Cephalothin': kcat = 78.3 under the column head kcat (S-1); Km = 15.6 under the column head Km (uM); printed kcat/Km = 5.02 under the column head kcat/Km (uM-1 S-1).

row_label: Table 3, substrate row 'Cephalothin'

substrate: cephalothin


substrate_name: carbenicillin

column_label: Table 3 (Kinetic parameters of ACPGA001 PGA), substrate row 'Carbenicillin'; column 'kcat (S-1)' = 63.7; column 'Km (uM)' = 51.9; column 'kcat/Km (uM-1 S-1)' = 1.23.

normalized_value_unit_evidence: kcat: printed Table 3 cell 63.7 under the column head kcat (S-1); that column is already per second, so no unit conversion applies and the paper value is 63.7 s^(-1). Km: printed Table 3 cell 51.9 under the column head Km (uM); 51.9 / 1000 = 0.0519 mM. kcat/Km: printed Table 3 cell 1.23 under the column head kcat/Km (uM-1 S-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 1.23 x 1000 = 1230.0 s^(-1)*mM^(-1). Quotient disclosure for this substrate row: 63.7 / 0.0519 = 1227.3603082851637 s^-1 mM^-1, which is the catalytic efficiency the catalog carries, and the printed cell 1.23 is that quotient written to the two decimals this column prints.

raw_value_unit_evidence: Table 3, substrate row 'Carbenicillin': kcat = 63.7 under the column head kcat (S-1); Km = 51.9 under the column head Km (uM); printed kcat/Km = 1.23 under the column head kcat/Km (uM-1 S-1).

row_label: Table 3, substrate row 'Carbenicillin'

substrate: carbenicillin


substrate_name: ampicillin

column_label: Table 3 (Kinetic parameters of ACPGA001 PGA), substrate row 'Ampicillin'; column 'kcat (S-1)' = 49.5; column 'Km (uM)' = 94.4; column 'kcat/Km (uM-1 S-1)' = 0.52.

normalized_value_unit_evidence: kcat: printed Table 3 cell 49.5 under the column head kcat (S-1); that column is already per second, so no unit conversion applies and the paper value is 49.5 s^(-1). Km: printed Table 3 cell 94.4 under the column head Km (uM); 94.4 / 1000 = 0.0944 mM. kcat/Km: printed Table 3 cell 0.52 under the column head kcat/Km (uM-1 S-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.52 x 1000 = 520.0 s^(-1)*mM^(-1). Quotient disclosure for this substrate row: 49.5 / 0.0944 = 524.3644067796611 s^-1 mM^-1, which is the catalytic efficiency the catalog carries, and the printed cell 0.52 is that quotient written to the two decimals this column prints.

raw_value_unit_evidence: Table 3, substrate row 'Ampicillin': kcat = 49.5 under the column head kcat (S-1); Km = 94.4 under the column head Km (uM); printed kcat/Km = 0.52 under the column head kcat/Km (uM-1 S-1).

row_label: Table 3, substrate row 'Ampicillin'

substrate: ampicillin


column_label: Table 3 (Kinetic parameters of ACPGA001 PGA), substrate row 'NIPAB'; column 'kcat (S-1)' = 58.3; column 'Km (uM)' = 8.3; column 'kcat/Km (uM-1 S-1)' = 7.02.

normalized_value_unit_evidence: kcat: printed Table 3 cell 58.3 under the column head kcat (S-1); that column is already per second, so no unit conversion applies and the paper value is 58.3 s^(-1). Km: printed Table 3 cell 8.3 under the column head Km (uM); 8.3 / 1000 = 0.0083 mM. kcat/Km: printed Table 3 cell 7.02 under the column head kcat/Km (uM-1 S-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 7.02 x 1000 = 7020.0 s^(-1)*mM^(-1). Quotient disclosure for this substrate row: 58.3 / 0.0083 = 7024.096385542168 s^-1 mM^-1, which is the catalytic efficiency the catalog carries, and the printed cell 7.02 is that quotient written to the two decimals this column prints.

raw_value_unit_evidence: Table 3, substrate row 'NIPAB': kcat = 58.3 under the column head kcat (S-1); Km = 8.3 under the column head Km (uM); printed kcat/Km = 7.02 under the column head kcat/Km (uM-1 S-1).

row_label: Table 3, substrate row 'NIPAB'


substrate_name: amoxycillin

substrate: amoxycillin


substrate_name: cephaloridine

column_label: Table 3 (Kinetic parameters of ACPGA001 PGA), substrate row 'Cephaloridine'; column 'kcat (S-1)' = 66.9; column 'Km (uM)' = 16.4; column 'kcat/Km (uM-1 S-1)' = 4.08.

normalized_value_unit_evidence: kcat: printed Table 3 cell 66.9 under the column head kcat (S-1); that column is already per second, so no unit conversion applies and the paper value is 66.9 s^(-1). Km: printed Table 3 cell 16.4 under the column head Km (uM); 16.4 / 1000 = 0.0164 mM. kcat/Km: printed Table 3 cell 4.08 under the column head kcat/Km (uM-1 S-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 4.08 x 1000 = 4080.0 s^(-1)*mM^(-1). Quotient disclosure for this substrate row: 66.9 / 0.0164 = 4079.268292682927 s^-1 mM^-1, which is the catalytic efficiency the catalog carries, and the printed cell 4.08 is that quotient written to the two decimals this column prints.

raw_value_unit_evidence: Table 3, substrate row 'Cephaloridine': kcat = 66.9 under the column head kcat (S-1); Km = 16.4 under the column head Km (uM); printed kcat/Km = 4.08 under the column head kcat/Km (uM-1 S-1).

row_label: Table 3, substrate row 'Cephaloridine'

substrate: cephaloridine


column_label: Table 3 (Kinetic parameters of ACPGA001 PGA), substrate row 'Penicillin G'; column 'kcat (S-1)' = 64.2; column 'Km (uM)' = 4.6; column 'kcat/Km (uM-1 S-1)' = 13.96.

normalized_value_unit_evidence: kcat: printed Table 3 cell 64.2 under the column head kcat (S-1); that column is already per second, so no unit conversion applies and the paper value is 64.2 s^(-1). Km: printed Table 3 cell 4.6 under the column head Km (uM); 4.6 / 1000 = 0.0046 mM. kcat/Km: printed Table 3 cell 13.96 under the column head kcat/Km (uM-1 S-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 13.96 x 1000 = 13960.0 s^(-1)*mM^(-1). Quotient disclosure for this substrate row: 64.2 / 0.0046 = 13956.521739130436 s^-1 mM^-1, which is the catalytic efficiency the catalog carries, and the printed cell 13.96 is that quotient written to the two decimals this column prints.

raw_value_unit_evidence: Table 3, substrate row 'Penicillin G': kcat = 64.2 under the column head kcat (S-1); Km = 4.6 under the column head Km (uM); printed kcat/Km = 13.96 under the column head kcat/Km (uM-1 S-1).

row_label: Table 3, substrate row 'Penicillin G'


column_label: Table 3 (Kinetic parameters of ACPGA001 PGA), substrate row 'Penicillin V'; column 'kcat (S-1)' = 48.4; column 'Km (uM)' = 39.3; column 'kcat/Km (uM-1 S-1)' = 1.23.

normalized_value_unit_evidence: kcat: printed Table 3 cell 48.4 under the column head kcat (S-1); that column is already per second, so no unit conversion applies and the paper value is 48.4 s^(-1). Km: printed Table 3 cell 39.3 under the column head Km (uM); 39.3 / 1000 = 0.0393 mM. kcat/Km: printed Table 3 cell 1.23 under the column head kcat/Km (uM-1 S-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 1.23 x 1000 = 1230.0 s^(-1)*mM^(-1). Quotient disclosure for this substrate row: 48.4 / 0.0393 = 1231.5521628498727 s^-1 mM^-1, which is the catalytic efficiency the catalog carries, and the printed cell 1.23 is that quotient written to the two decimals this column prints.

raw_value_unit_evidence: Table 3, substrate row 'Penicillin V': kcat = 48.4 under the column head kcat (S-1); Km = 39.3 under the column head Km (uM); printed kcat/Km = 1.23 under the column head kcat/Km (uM-1 S-1).

row_label: Table 3, substrate row 'Penicillin V'


sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q72G76 / EMBL AAS82314.1 / NCBI YP_005941.1 and applied mutation signature L24F/I57F with inferred residue-numbering offset +255 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q72G76 / EMBL AAS82314.1 / NCBI YP_005941.1


sequence_variant_note: Resolved canonical sequence from UniProtKB Q72G76 / EMBL AAS82314.1 / NCBI YP_005941.1 and applied mutation signature L188F to reconstruct the assayed variant sequence.


enzyme_display_name: xylan 1,4-beta-xylosidase

organism: Enterobacter sp.

substrate_name: xylohexaose

sequence_source: UniProtKB:V5J3M5 REST FASTA checked 2026-06-01

enzyme: xylan 1,4-beta-xylosidase

substrate: xylohexaose


organism: Geobacillus stearothermophilus

substrate_name: p-Nitrophenyl-beta-D-xylopyranoside

sequence_source: UniProtKB:Q09LZ0 REST FASTA checked 2026-06-01

substrate: p-Nitrophenyl-beta-D-xylopyranoside


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q09LZ0 REST FASTA checked 2026-06-01 and applied mutation signature E522A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q09LZ0 REST FASTA checked 2026-06-01 and applied mutation signature E335A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q09LZ0 REST FASTA checked 2026-06-01 and applied mutation signature E427A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q09LZ0 REST FASTA checked 2026-06-01 and applied mutation signature D495G to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q09LZ0 REST/FASTA checked 2026-06-01; RCSB 4RHH SIFTS full sequence coverage


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


organism: Arabidopsis thaliana

sequence_source: UniProtKB reviewed accession Q9FLG1 direct REST lookup; source row supplied Q9FLG1.

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


organism: Aspergillus awamori

sequence_source: UniProtKB direct lookup of source accession B5AK91 resolved to reviewed accession Q4AEG8; sequence taken from Q4AEG8.


organism: Aspergillus niger

substrate_name: 4-nitrophenyl beta-D-glucopyranoside

sequence_source: UniProtKB unreviewed accession A0A023J5W7 direct REST lookup; source row supplied A0A023J5W7.

substrate: 4-nitrophenyl beta-D-glucopyranoside


substrate_name: 4-nitrophenyl alpha-L-arabinofuranoside

substrate: 4-nitrophenyl alpha-L-arabinofuranoside


substrate_name: 4-nitrophenyl beta-D-xylopyranoside

substrate: 4-nitrophenyl beta-D-xylopyranoside


substrate_name: xylobiose

substrate: xylobiose


substrate_name: 4-nitrophenyl alpha-L-arabinopyranoside

substrate: 4-nitrophenyl alpha-L-arabinopyranoside


organism: Geobacillus thermoleovorans

sequence_source: UniProtKB direct accession lookup Q2I2N4 on 2026-06-01


substrate_name: xylotriose

substrate: xylotriose


organism: Irpex lacteus

sequence_source: UniProtKB direct accession lookup A0A2U9Q8M3 on 2026-06-01


substrate_name: 3,4-dinitrophenyl beta-D-xylopyranoside

sequence_source: UniProtKB:A0A023J5W7 direct lookup (unreviewed TrEMBL fragment; checked 2026-06-01)

substrate: 3,4-dinitrophenyl beta-D-xylopyranoside


sequence_source: UniProtKB:O00089 direct lookup (reviewed Swiss-Prot precursor; checked 2026-06-01)


organism: Bacillus thermodenitrificans

sequence_source: UniProtKB:V5N4G7 direct lookup (unreviewed TrEMBL fragment; checked 2026-06-01)


organism: Enterobacter ludwigii

substrate_name: 4-nitrophenyl beta-D-xyloside

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

substrate: 4-nitrophenyl beta-D-xyloside


sequence_source: UniProtKB:V5J3M5 direct lookup (unreviewed TrEMBL; checked 2026-06-01)


substrate_name: xylopentaose

substrate: xylopentaose


substrate_name: xylotetraose

substrate: xylotetraose


organism: Medicago sativa

sequence_source: UniProtKB:A5JTQ2 direct REST check; PMID:17615411


organism: Prevotella ruminicola

sequence_source: UniProtKB:D5EY15 direct REST check; PMID:19304844


sequence_variant_note: Mutation signature E594Q matches the mutant residue at offset +0 and the reference residue at offset -7; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


organism: Selenomonas ruminantium

sequence_source: UniProtKB:O52575 direct REST check; PMID:31220489; DOI:10.1016/j.ijbiomac.2019.06.100


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


sequence_source: UniProt Q9ZFM2 REST FASTA and JSON lookup, accessed 2026-06-01


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB O52575 FASTA; C413V reconstructed from canonical O52575 after confirming residue 413 is C. and applied mutation signature C413V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB O52575 FASTA; C101V reconstructed from canonical O52575 after confirming residue 101 is C. and applied mutation signature C101V to reconstruct the assayed variant sequence.


organism: Talaromyces amestolkiae

sequence_source: Direct UniProtKB A0A0H3W535 FASTA.


organism: Trichoderma reesei


substrate_name: Xylohexaose

substrate: Xylohexaose


organism: uncultured rumen bacterium


organism: Thermoanaerobacter saccharolyticum

sequence_source: UniProtKB:P36906 direct lookup on 2026-06-01

assay_conditions_summary: pH 5.5; 310.15 K; buffer 25 mM citrate/25 mM phosphate

column_label: Table 1, substrate row 'mNPX', enzyme line 'Wild-type': column 'kcat (s-1)' = 11; column 'Km (uM)' = 150; column 'kcat/Km (s-1 mM-1)' = 73; the two wild-type-to-mutant ratio columns of that line print 2.1 x 10^3 and 7.0 x 10^4.

normalized_value_unit_evidence: Km: printed Table 1 cell 150 uM; 1 uM is 0.001 mM, so the printed cell converts to 0.15 mM, and the catalog value is 0.15 mM. kcat: printed Table 1 cell 11 s-1; the column head prints s-1, so no unit conversion applies and the printed cell reads 11.0 s^(-1). kcat/Km: printed Table 1 cell 73 s-1 mM-1; the column head already prints s-1 mM-1, so no unit conversion applies and the printed cell reads 73.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 11.0 / 0.15 = 73.33333333333334 s^-1 mM^-1, which is the catalog kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 1 uses.

raw_value_unit_evidence: Table 1, substrate row mNPX, Wild-type enzyme line: kcat = 11 s-1; Km = 150 uM; printed kcat/Km = 73 s-1 mM-1.

row_label: Table 1, substrate row mNPX, wild-type enzyme line

table_label: Table 1: Kinetic Parameters for the Hydrolysis of Aryl Xylosides (Biochemistry 2002, volume 41, number 31, pages 9736-9746); printed columns substrate, pKa, enzyme, kcat (s-1), ratio kcat, Km (uM), kcat/Km (s-1 mM-1) and ratio (kcat/Km)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P36906 and applied mutation signature E160A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 310.15 K; buffer 25 mM citrate/25 mM phosphate

column_label: Table 1, substrate row 'pNPX', enzyme line 'E160A': column 'kcat (s-1)' = 4.0 x 10^-2; column 'Km (uM)' = 1.4 x 10^2; column 'kcat/Km (s-1 mM-1)' = 0.28; the two ratio columns are empty on this line.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.4 x 10^2 uM; 1 uM is 0.001 mM, so the printed cell converts to 0.14 mM, and the catalog value is 0.14 mM. kcat: printed Table 1 cell 4.0 x 10^-2 s-1; the column head prints s-1, so no unit conversion applies and the printed cell reads 0.04 s^(-1). kcat/Km: printed Table 1 cell 0.28 s-1 mM-1; the column head already prints s-1 mM-1, so no unit conversion applies and the printed cell reads 0.28 s^(-1)*mM^(-1); the catalog kcat_over_km 0.2857142857142857 s^(-1)*mM^(-1) is a quotient of two catalog numbers, not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 1, substrate row pNPX, E160A enzyme line: kcat = 4.0 x 10^-2 s-1; Km = 1.4 x 10^2 uM; printed kcat/Km = 0.28 s-1 mM-1.


column_label: Table 1, substrate row '2,5DNPX', enzyme line 'E160A': column 'kcat (s-1)' = 0.84; column 'Km (uM)' = 10; column 'kcat/Km (s-1 mM-1)' = 84; the two ratio columns are empty on this line.

normalized_value_unit_evidence: Km: printed Table 1 cell 10 uM; 1 uM is 0.001 mM, so the printed cell converts to 0.01 mM, and the catalog value is 0.01 mM. kcat: printed Table 1 cell 0.84 s-1; the column head prints s-1, so no unit conversion applies and the printed cell reads 0.84 s^(-1). kcat/Km: printed Table 1 cell 84 s-1 mM-1; the column head already prints s-1 mM-1, so no unit conversion applies and the printed cell reads 84.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 0.84 / 0.01 = 84.0 s^-1 mM^-1, which is the catalog kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 1 uses.

raw_value_unit_evidence: Table 1, substrate row 2,5DNPX, E160A enzyme line: kcat = 0.84 s-1; Km = 10 uM; printed kcat/Km = 84 s-1 mM-1.


column_label: Table 1, substrate row 'pNPX', enzyme line 'Wild-type': column 'kcat (s-1)' = 9.7; column 'Km (uM)' = 36; column 'kcat/Km (s-1 mM-1)' = 270; the two wild-type-to-mutant ratio columns of that line print 2.4 x 10^2 and 9.4 x 10^2.

normalized_value_unit_evidence: Km: printed Table 1 cell 36 uM; 1 uM is 0.001 mM, so the printed cell converts to 0.036 mM, and the catalog value is 0.036 mM. kcat: printed Table 1 cell 9.7 s-1; the column head prints s-1, so no unit conversion applies and the printed cell reads 9.7 s^(-1). kcat/Km: printed Table 1 cell 270 s-1 mM-1; the column head already prints s-1 mM-1, so no unit conversion applies and the printed cell reads 270.0 s^(-1)*mM^(-1); the catalog kcat_over_km 269.44444444444446 s^(-1)*mM^(-1) is a quotient of two catalog numbers, not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 1, substrate row pNPX, Wild-type enzyme line: kcat = 9.7 s-1; Km = 36 uM; printed kcat/Km = 270 s-1 mM-1.

row_label: Table 1, substrate row pNPX, wild-type enzyme line


column_label: Table 1, substrate row '3,4DNPX', enzyme line 'E160A': column 'kcat (s-1)' = 0.78; column 'Km (uM)' = 14; column 'kcat/Km (s-1 mM-1)' = 56; the two ratio columns are empty on this line.

normalized_value_unit_evidence: Km: printed Table 1 cell 14 uM; 1 uM is 0.001 mM, so the printed cell converts to 0.014 mM, and the catalog value is 0.014 mM. kcat: printed Table 1 cell 0.78 s-1; the column head prints s-1, so no unit conversion applies and the printed cell reads 0.78 s^(-1). kcat/Km: printed Table 1 cell 56 s-1 mM-1; the column head already prints s-1 mM-1, so no unit conversion applies and the printed cell reads 56.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 0.78 / 0.014 = 55.714285714285715 s^-1 mM^-1, which is the catalog kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 1 uses.

raw_value_unit_evidence: Table 1, substrate row 3,4DNPX, E160A enzyme line: kcat = 0.78 s-1; Km = 14 uM; printed kcat/Km = 56 s-1 mM-1.


organism: Thermobifida halotolerans

substrate_name: p-nitrophenyl alpha-L-arabinoside

sequence_source: UniProtKB:A0A399G7U0 direct lookup on 2026-06-01

substrate: p-nitrophenyl alpha-L-arabinoside


substrate_name: Xylotetraose

sequence_source: UniProtKB:Q92458 direct lookup on 2026-06-01

substrate: Xylotetraose


organism: Talaromyces purpureogenus

sequence_source: UniProtKB C3W4Y2 direct accession lookup, sequence version 2, primary accession C3W4Y2.


substrate_name: 4-nitrophenyl alpha-D-xylopyranoside

substrate: 4-nitrophenyl alpha-D-xylopyranoside


sequence_source: UniProtKB P36906 direct accession lookup, reviewed Swiss-Prot entry XYNB_THESA, sequence version 1.

column_label: Table 1, substrate row '3,4DNPX', enzyme line 'Wild-type': column 'kcat (s-1)' = 8.9; column 'Km (uM)' = 10; column 'kcat/Km (s-1 mM-1)' = 900; the two wild-type-to-mutant ratio columns of that line print 11 and 16.

normalized_value_unit_evidence: Km: printed Table 1 cell 10 uM; 1 uM is 0.001 mM, so the printed cell converts to 0.01 mM, and the catalog value is 0.01 mM. kcat: printed Table 1 cell 8.9 s-1; the column head prints s-1, so no unit conversion applies and the printed cell reads 8.9 s^(-1). kcat/Km: printed Table 1 cell 900 s-1 mM-1; the column head already prints s-1 mM-1, so no unit conversion applies and the printed cell reads 900.0 s^(-1)*mM^(-1); the catalog kcat_over_km 890.0 s^(-1)*mM^(-1) is a quotient of two catalog numbers, not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 1, substrate row 3,4DNPX, Wild-type enzyme line: kcat = 8.9 s-1; Km = 10 uM; printed kcat/Km = 900 s-1 mM-1.

row_label: Table 1, substrate row 3,4DNPX, wild-type enzyme line


column_label: Table 1, substrate row 'oNPX', enzyme line 'E160A': column 'kcat (s-1)' = 9.0 x 10^-2; column 'Km (uM)' = 80; column 'kcat/Km (s-1 mM-1)' = 1.1; the two ratio columns are empty on this line.

normalized_value_unit_evidence: Km: printed Table 1 cell 80 uM; 1 uM is 0.001 mM, so the printed cell converts to 0.08 mM, and the catalog value is 0.08 mM. kcat: printed Table 1 cell 9.0 x 10^-2 s-1; the column head prints s-1, so no unit conversion applies and the printed cell reads 0.09 s^(-1). kcat/Km: printed Table 1 cell 1.1 s-1 mM-1; the column head already prints s-1 mM-1, so no unit conversion applies and the printed cell reads 1.1 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 0.09 / 0.08 = 1.125 s^-1 mM^-1, which is the catalog kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 1 uses.

raw_value_unit_evidence: Table 1, substrate row oNPX, E160A enzyme line: kcat = 9.0 x 10^-2 s-1; Km = 80 uM; printed kcat/Km = 1.1 s-1 mM-1.


column_label: Table 1, substrate row '2,5DNPX', enzyme line 'Wild-type': column 'kcat (s-1)' = 7.3; column 'Km (uM)' = 11; column 'kcat/Km (s-1 mM-1)' = 670; the two wild-type-to-mutant ratio columns of that line print 8.7 and 7.9.

normalized_value_unit_evidence: Km: printed Table 1 cell 11 uM; 1 uM is 0.001 mM, so the printed cell converts to 0.011 mM, and the catalog value is 0.011 mM. kcat: printed Table 1 cell 7.3 s-1; the column head prints s-1, so no unit conversion applies and the printed cell reads 7.3 s^(-1). kcat/Km: printed Table 1 cell 670 s-1 mM-1; the column head already prints s-1 mM-1, so no unit conversion applies and the printed cell reads 670.0 s^(-1)*mM^(-1); the catalog kcat_over_km 663.6363636363636 s^(-1)*mM^(-1) is a quotient of two catalog numbers, not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 1, substrate row 2,5DNPX, Wild-type enzyme line: kcat = 7.3 s-1; Km = 11 uM; printed kcat/Km = 670 s-1 mM-1.

row_label: Table 1, substrate row 2,5DNPX, wild-type enzyme line


column_label: Table 1, substrate row 'oNPX', enzyme line 'Wild-type': column 'kcat (s-1)' = 9.9; column 'Km (uM)' = 46; column 'kcat/Km (s-1 mM-1)' = 220; the two wild-type-to-mutant ratio columns of that line print 110 and 1.9 x 10^2.

normalized_value_unit_evidence: Km: printed Table 1 cell 46 uM; 1 uM is 0.001 mM, so the printed cell converts to 0.046 mM, and the catalog value is 0.046 mM. kcat: printed Table 1 cell 9.9 s-1; the column head prints s-1, so no unit conversion applies and the printed cell reads 9.9 s^(-1). kcat/Km: printed Table 1 cell 220 s-1 mM-1; the column head already prints s-1 mM-1, so no unit conversion applies and the printed cell reads 220.0 s^(-1)*mM^(-1); the catalog kcat_over_km 215.21739130434784 s^(-1)*mM^(-1) is a quotient of two catalog numbers, not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 1, substrate row oNPX, Wild-type enzyme line: kcat = 9.9 s-1; Km = 46 uM; printed kcat/Km = 220 s-1 mM-1.

row_label: Table 1, substrate row oNPX, wild-type enzyme line


column_label: Table 1, substrate row 'mNPX', enzyme line 'E160A': column 'kcat (s-1)' = 5.2 x 10^-3; column 'Km (uM)' = 4.9 x 10^3; column 'kcat/Km (s-1 mM-1)' = 1.1 x 10^-3; the two ratio columns are empty on this line.

normalized_value_unit_evidence: Km: printed Table 1 cell 4.9 x 10^3 uM; 1 uM is 0.001 mM, so the printed cell converts to 4.9 mM, and the catalog value is 4.9 mM. kcat: printed Table 1 cell 5.2 x 10^-3 s-1; the column head prints s-1, so no unit conversion applies and the printed cell reads 0.0052 s^(-1), which supersedes the catalog value 0.005 s^(-1). kcat/Km: printed Table 1 cell 1.1 x 10^-3 s-1 mM-1; the column head already prints s-1 mM-1, so no unit conversion applies and the printed cell reads 0.0011 s^(-1)*mM^(-1); the catalog kcat_over_km 0.001020408163265306 s^(-1)*mM^(-1) is a quotient of two catalog numbers, not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 1, substrate row mNPX, E160A enzyme line: kcat = 5.2 x 10^-3 s-1; Km = 4.9 x 10^3 uM; printed kcat/Km = 1.1 x 10^-3 s-1 mM-1.