enzyme_display_name: phosphodiesterase I

organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H182A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

enzyme: phosphodiesterase I


source_db: oed

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H432N with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

mutation_type: substitution

data_origin: experimental

status: unverified

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H432R with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


mutation_signature: Unknown

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

proof_lines:
Tdp1
wild type
GATCTAAAAGACTT


enzyme_display_name: fructose-2,6-bisphosphate 2-phosphatase

organism: Arabidopsis thaliana

source_db: brenda

kcat_display: Not reported

kcat_over_km_display: Not reported

assay_conditions_summary: pH 6

enzyme: fructose-2,6-bisphosphate 2-phosphatase

source: brenda


substrate_name: fructose-6-phosphate for the 6-phosphofructo-2-kinase activity (at pH 6.0 and 25 degrees Celsius)

source_db: uniprot

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

source: uniprot


substrate_name: ATP for the 6-phosphofructo-2-kinase activity (at pH 6.0 and 25 degrees Celsius)

assay_conditions_summary: cofactor ATP


enzyme_display_name: farnesyl diphosphatase

organism: Saccharolobus solfataricus

substrate_name: geranylgeranyl diphosphate

km_display: Not reported

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

enzyme: farnesyl diphosphatase

substrate: geranylgeranyl diphosphate


substrate_name: (2E,6E)-farnesyl diphosphate

substrate: (2E,6E)-farnesyl diphosphate


organism: Escherichia coli (strain K12)

substrate_name: glycerophosphoethanolamine

verification_status: verified

smiles: C(COP(=O)(O)OCC(CO)O)N

column_label: PMC Table 1 row GPE reports Km 0.22 mM.

normalized_value_unit_evidence: Km normalized_value=0.22 mM

raw_value_unit_evidence: Km raw_value=0.22 raw_unit=mM

row_label: GPE

table_label: Table 1

substrate: glycerophosphoethanolamine

status: verified


substrate_name: glycerophosphoglycerol

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

column_label: PMC Table 1 row GPG reports Km 0.62 mM.

normalized_value_unit_evidence: Km normalized_value=0.62 mM

raw_value_unit_evidence: Km raw_value=0.62 raw_unit=mM

row_label: GPG

substrate: glycerophosphoglycerol


substrate_name: glycerophosphoinositol

column_label: PMC Table 1 row GPI reports Km 0.39 mM.

normalized_value_unit_evidence: Km normalized_value=0.39 mM

raw_value_unit_evidence: Km raw_value=0.39 raw_unit=mM

row_label: GPI

substrate: glycerophosphoinositol


substrate_name: glycerophosphocholine

column_label: PMC Table 1 row GPC reports Km 2.0 mM.

normalized_value_unit_evidence: Km normalized_value=2.0 mM

raw_value_unit_evidence: Km raw_value=2.0 raw_unit=mM

row_label: GPC

substrate: glycerophosphocholine


assay_conditions_summary: pH 9; buffer pH 9

column_label: Table II row Glycerophosphocholine under column Km (mM): 0.28.

raw_value_unit_evidence: Table II row Glycerophosphocholine: Km 0.28 mM; Vmax 180 units/mg.

row_label: Glycerophosphocholine

table_label: Table II


column_label: Table II row Glycerophosphoethanolamine under column Km (mM): 0.24.

raw_value_unit_evidence: Table II row Glycerophosphoethanolamine: Km 0.24 mM; Vmax 213 units/mg.

row_label: Glycerophosphoethanolamine


column_label: Table II row Glycerophosphoglycerol under column Km (mM): 0.35.

raw_value_unit_evidence: Table II row Glycerophosphoglycerol: Km 0.35 mM; Vmax 280 units/mg.

row_label: Glycerophosphoglycerol


substrate_name: glycerophosphoserine

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

column_label: Table II row Glycerophosphoserine under column Km (mM): 0.59.

raw_value_unit_evidence: Table II row Glycerophosphoserine: Km 0.59 mM; Vmax 170 units/mg.

row_label: Glycerophosphoserine

substrate: glycerophosphoserine


column_label: Table II row Glycerophosphoinositol under column Km (mM): 1.0.

normalized_value_unit_evidence: Km 1.0 mM.

raw_value_unit_evidence: Table II row Glycerophosphoinositol: Km 1.0 mM; Vmax 300 units/mg.

row_label: Glycerophosphoinositol


organism: Rattus norvegicus

substrate_name: beta-D-fructose 6-phosphate

assay_conditions_summary: pH 7.5; cofactor ATP

column_label: Table II section Fru-6-P,2-kinase; row K_Fru-6-P (uM); Testis column value 85 +/- 5.

raw_value_unit_evidence: Table II Testis column reports K_Fru-6-P 85 +/- 5 uM.

row_label: Fru-6-P,2-kinase K_Fru-6-P

table_label: Table II: Comparison of the kinetic constants of rat testis (expressed), liver, muscle, and bovine heart Fru-6-P,2-kinase:Fru-2,6-bisphosphatase

substrate: beta-D-fructose 6-phosphate


substrate_name: ATP

column_label: Table II section Fru-6-P,2-kinase; row K_ATP (uM); Testis column value 270 +/- 43.

raw_value_unit_evidence: Table II Testis column reports K_ATP 270 +/- 43 uM.

row_label: Fru-6-P,2-kinase K_ATP

substrate: ATP


substrate_name: beta-D-fructose 2,6-bisphosphate

column_label: Table II section Fru-2,6-bisphosphatase; row K_Fru-2,6-P2 (uM); Testis column value 21 +/- 4.7.

raw_value_unit_evidence: Table II Testis column reports K_Fru-2,6-P2 21 +/- 4.7 uM.

row_label: Fru-2,6-bisphosphatase K_Fru-2,6-P2

substrate: beta-D-fructose 2,6-bisphosphate


enzyme_display_name: aryldialkylphosphatase

organism: Purpureocillium lilacinum

substrate_name: malathion

smiles: CCOC(=O)CC(C(=O)OCC)SP(=S)(OC)OC

enzyme: aryldialkylphosphatase

substrate: malathion


substrate_name: demeton-S

smiles: CCOP(=O)(OCC)SCCSCC

substrate: demeton-S


substrate_name: phosmet

substrate: phosmet


substrate_name: Coumaphos

substrate: Coumaphos


substrate_name: parathion

substrate: parathion


substrate_name: methyl parathion

substrate: methyl parathion


substrate_name: paraoxon

substrate: paraoxon


organism: Sphingopyxis terrae subsp. terrae

substrate_name: 2-ethylhexyl diphenyl phosphate

substrate: 2-ethylhexyl diphenyl phosphate


substrate_name: resorcinol bis(diphenyl phosphate)

substrate: resorcinol bis(diphenyl phosphate)


substrate_name: tricresyl phosphate

substrate: tricresyl phosphate


substrate_name: triphenyl phosphate

substrate: triphenyl phosphate


organism: synthetic construct

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tris

proof_lines: wild-type, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C


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

proof_lines: mutant H115W, in 50 mM Tris buffer, 1 mM CaCl2, pH 8.0, 25°C


organism: Pimelobacter simplex

substrate_name: ethyl parathion

substrate: ethyl parathion


substrate_name: ethyl phenyl parathion

substrate: ethyl phenyl parathion


organism: Agrobacterium tumefaciens

substrate_name: dichlorvos

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

proof_lines: pH 8.0, 37°C, enzyme administered in monkeys in vivo

substrate: dichlorvos


proof_lines: pH 8.0, 25°C, enzyme administered in rats in vivo


enzyme_display_name: exodeoxyribonuclease V

organism: Alcaligenes faecalis

enzyme: exodeoxyribonuclease V


organism: Micrococcus luteus

substrate_name: Double-stranded DNA

substrate: Double-stranded DNA


substrate_name: oligonucleotide (polydT)8 polydA

substrate: oligonucleotide (polydT)8 polydA


organism: Bacillus subtilis

substrate_name: ATP

substrate: ATP


organism: Bos taurus


proof_lines: pH 9.1, 37°C, recombinant enzyme in presence of Co2+

proof_lines: pH 9.1, 37°C, recombinant enzyme in absence of Co2+


organism: Geobacillus stearothermophilus


substrate_name: methyl paraoxon

substrate: methyl paraoxon


substrate_name: ethyl paraoxon

substrate: ethyl paraoxon


enzyme_display_name: exodeoxyribonuclease I

organism: Thermus thermophilus

substrate_name: ssDNA 40 mer

enzyme: exodeoxyribonuclease I

substrate: ssDNA 40 mer


proof_lines: recombinant PON1, in 50 mM Tris buffer, 1 mM NaCl, pH 8.0 at 25°C


proof_lines: nanocapsule MIP-VBTN, at pH 9.0 and 30°C

proof_lines: nanocapsule MIP-VBTNOH, at pH 9.0 and 30°C


organism: Lucilia cuprina

substrate_name: diethylumbelliferyl phosphate

proof_lines: pH 7.5, 25°C, recombinant mutant enzyme G137D

substrate: diethylumbelliferyl phosphate


organism: Vulcanisaeta moutnovskia

substrate_name: ethyl-paraoxon

substrate: ethyl-paraoxon


organism: Homo sapiens

assay_conditions_summary: pH 7.4; 310.15 K; buffer 50 mM Tris-HCl

proof_lines: in 50 mM Tris-HCl buffer, 10 mM CaCl2, pH 7.4

proof_lines: pH 8.0, temperature not specified in the publication


enzyme_display_name: Arylesterase

organism: Saccharolobus solfataricus

substrate_name: phenyl acetate (PA)

column_label: Table 4, row PA, column Km (uM), cell 17 +/- 1 uM

raw_value_unit_evidence: Table 4 row PA, Km (uM) = 17 +/- 1 uM

row_label: PA

table_label: Table 4. Kinetic parameters for hydrolysis of various substrates

enzyme: Arylesterase

substrate: phenyl acetate (PA)


substrate_name: alpha-naphthyl acetate (alpha-NA)

column_label: Table 4, row alpha-NA, column Km (uM), cell 29 +/- 1 uM

raw_value_unit_evidence: Table 4 row alpha-NA, Km (uM) = 29 +/- 1 uM

row_label: alpha-NA

substrate: alpha-naphthyl acetate (alpha-NA)


substrate_name: p-nitrophenyl butyrate (C4)

column_label: Table 4, row Butyrate (C4), column Km (uM), cell 224 +/- 12 uM

raw_value_unit_evidence: Table 4 row Butyrate (C4), Km (uM) = 224 +/- 12 uM

row_label: Butyrate (C4)

substrate: p-nitrophenyl butyrate (C4)


substrate_name: p-nitrophenyl caproate (C6)

column_label: Table 4, row Caproate (C6), column Km (uM), cell 31 +/- 4 uM

raw_value_unit_evidence: Table 4 row Caproate (C6), Km (uM) = 31 +/- 4 uM

row_label: Caproate (C6)

substrate: p-nitrophenyl caproate (C6)


substrate_name: p-nitrophenyl caprylate (C8)

column_label: Table 4, row Caprylate (C8), column Km (uM), cell 28 +/- 2 uM

raw_value_unit_evidence: Table 4 row Caprylate (C8), Km (uM) = 28 +/- 2 uM

row_label: Caprylate (C8)

substrate: p-nitrophenyl caprylate (C8)


substrate_name: p-nitrophenyl laurate (C12)

column_label: Table 4, row Laurate (C12), column Km (uM), cell 122 +/- 5 uM

raw_value_unit_evidence: Table 4 row Laurate (C12), Km (uM) = 122 +/- 5 uM

row_label: Laurate (C12)

substrate: p-nitrophenyl laurate (C12)


substrate_name: p-nitrophenyl palmitate (C16)

column_label: Table 4, row Palmitate (C16), column Km (uM), cell 276 +/- 9 uM

raw_value_unit_evidence: Table 4 row Palmitate (C16), Km (uM) = 276 +/- 9 uM

row_label: Palmitate (C16)

substrate: p-nitrophenyl palmitate (C16)


substrate_name: p-nitrophenyl phosphate

column_label: Table 4, row PNP-phosphate, column Km (uM), cell 234 +/- 14 uM

raw_value_unit_evidence: Table 4 row PNP-phosphate, Km (uM) = 234 +/- 14 uM

row_label: PNP-phosphate

substrate: p-nitrophenyl phosphate


substrate_name: paraoxon

column_label: Table 4, row Paraoxon, column Km (uM), cell 5 +/- 0.5 uM

raw_value_unit_evidence: Table 4 row Paraoxon, Km (uM) = 5 +/- 0.5 uM

row_label: Paraoxon

substrate: paraoxon


column_label: Table 4, row Methyl paraoxon, column Km (uM), cell 246 +/- 18 uM

raw_value_unit_evidence: Table 4 row Methyl paraoxon, Km (uM) = 246 +/- 18 uM

row_label: Methyl paraoxon


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E313A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N133S with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +40, so it is treated as a source-provided variant sequence.

proof_lines: mutant E314A and mutant G11C, pH 10.5, 25°C


substrate_name: phenyl acetate

substrate: phenyl acetate


substrate_name: dihydrocoumarin

substrate: dihydrocoumarin


assay_conditions_summary: pH 8

proof_lines: pH 8.0, recombinant wild-type PON1 genetic variant G2E6


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H134Q to reconstruct the assayed variant sequence.


organism: Flavobacterium sp.

substrate_name: malathion

assay_conditions_summary: pH 7.5; buffer 50 mM HEPES

proof_lines: wild type enzyme, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C

substrate: malathion


substrate_name: demeton-S methyl

smiles: CCSCCSP(=O)(OC)OC

substrate: demeton-S methyl


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/F306V/R319S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/F306V/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme G60V/A80V/I106V/F132D/K185R/D208G/H257W/I274N/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, in 50 mM HEPES buffer, pH 7.5, at pH, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H115W/R192Q with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature H115W/R192K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: methyl paraoxon

substrate: methyl paraoxon


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

assay_conditions_summary: pH 9; buffer 50 mM CHES/CoCl2

proof_lines: surface-displayed recombinant enzyme from fresh cells, in 50 mM CHES/CoCl2 buffer, pH 9.0, with 0.05 mM CoCl2, at 37°C

proof_lines: surface-displayed recombinant enzyme from freeze-thawed cells, in 50 mM CHES/CoCl2 buffer, pH 9.0, with 0.05 mM CoCl2, at 37°C

proof_lines: intracellular-expressed recombinant enzyme from fresh cells, in 50 mM CHES/CoCl2 buffer, pH 9.0, with 0.05 mM CoCl2, at 37°C


substrate_name: Benzyl acetate

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

proof_lines: about, pH 8.0, genetic variant PON1 G2E6

substrate: Benzyl acetate


substrate_name: ethyl acetate

smiles: CCOC(=O)C

substrate: ethyl acetate


substrate_name: 4-acetoxy acetophenone

substrate: 4-acetoxy acetophenone


substrate_name: 4-chlorophenyl diethyl phosphate

substrate: 4-chlorophenyl diethyl phosphate


substrate_name: 3-cyanophenyl diethyl phosphate

substrate: 3-cyanophenyl diethyl phosphate


substrate_name: 4-cyanophenyl diethyl phosphate

substrate: 4-cyanophenyl diethyl phosphate


substrate_name: 2,4-dinitrophenyl diethyl phosphate

substrate: 2,4-dinitrophenyl diethyl phosphate


substrate_name: sarin

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q192R to reconstruct the assayed variant sequence.

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

proof_lines: mutant enzyme Q192R, in 20 mM Tris-HCl with 1 mM CaCl2 (pH 7.4), at 25°C

substrate: sarin


substrate_name: soman

substrate: soman


proof_lines: mutant enzyme Q192R, in 50 mM Tris-HCl with 1 mM CaCl2 (pH 7.4), at 25°C


organism: Sulfolobus acidocaldarius

proof_lines:
pH 8.5, 70°C, Mn2+-containing enzyme
pH 9.0, 75°C


enzyme_display_name: exodeoxyribonuclease III

organism: Helicobacter pylori

substrate_name: DNA; H2O

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

enzyme: exodeoxyribonuclease III

substrate: DNA; H2O


enzyme_display_name: DNA repair nuclease/redox regulator APEX1


enzyme_display_name: Xaa-Pro dipeptidase

organism: Alteromonas sp

substrate_name: a chromogenic soman analog

enzyme: Xaa-Pro dipeptidase

substrate: a chromogenic soman analog


enzyme_display_name: Aryldialkylphosphatase

organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

substrate_name: methyl-paraoxon (at pH 8.0)

enzyme: Aryldialkylphosphatase

substrate: methyl-paraoxon (at pH 8.0)


substrate_name: CMP-coumarin

assay_conditions_summary: pH 8.3; 298.15 K; buffer activity

column_label: Table 1 row CMP-Coumarin, columns kcat (s^-1) and KM (microM), match exported kcat and KM after microM-to-mM conversion.

row_label: CMP-Coumarin

table_label: PMC4068969 Table 1. Phosphotriesterase kinetic parameters

substrate: CMP-coumarin


enzyme_display_name: diisopropyl-fluorophosphatase

organism: Loligo vulgaris

substrate_name: Diisopropyl fluorophosphate; H2O

smiles: CC(C)OP(=O)(OC(C)C)F

enzyme: diisopropyl-fluorophosphatase

substrate: Diisopropyl fluorophosphate; H2O


substrate_name: H2O; Diisopropyl fluorophosphate

substrate: H2O; Diisopropyl fluorophosphate


proof_lines:
pH 8.3, 25°C
pH 9.0, 75°C
pH 8.5, 70°C, Mn2+-containing enzyme


organism: Mycobacterium tuberculosis

substrate_name: N1 duplex DNA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W235S to reconstruct the assayed variant sequence.

substrate: N1 duplex DNA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D251A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y234S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y137S to reconstruct the assayed variant sequence.


enzyme_display_name: DNA-(apurinic or apyrimidinic site) endonuclease

organism: Plasmodium falciparum (isolate 3D7)

substrate_name: DNA gapped template with 3'-OH at the gap (at pH 7.5 and 37 degrees Celsius)

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

proof_lines: kcat is 0.169 sec(-1) with DNA gapped template with 3'-OH at the gap as substrate (at pH 7.5 and 37 degrees Celsius).


enzyme_display_name: exodeoxyribonuclease (lambda-induced)

organism: Lambdavirus lambda

substrate_name: Double-stranded DNA

proof_lines:
at 20°C and pH 7.5
at 37°C and pH 7.5
5'-OH blunt end double-stranded DNA

enzyme: exodeoxyribonuclease (lambda-induced)

substrate: Double-stranded DNA


enzyme_display_name: OLD nuclease

organism: Thermus scotoductus (strain ATCC 700910 / SA-01)

substrate_name: ATP

proof_lines: kcat is 0.44 min(-1) for ATPase at 65 degrees Celsius.

enzyme: OLD nuclease

substrate: ATP


substrate_name: phenyl acetate

column_label: Table 1; row Wild-type HuPON1; phenylacetate hydrolysis; column kcat.

raw_value_unit_evidence: Table 1 Wild-type HuPON1 phenylacetate row: kcat 1236 s^-1.

substrate: phenyl acetate


substrate_name: paraoxon

assay_conditions_summary: pH 8; buffer 50 mM Tris

proof_lines: isoform PON1, pH and temperature not specified in the publication

proof_lines: PON1/human phosphate binding protein (1:1), in 50 mM Tris buffer, 1 mM NaCl, pH 8.0 at 25°C

proof_lines: PON1/human phosphate binding protein (9:1), in 50 mM Tris buffer, 1 mM NaCl, pH 8.0 at 25°C

substrate: paraoxon


organism: Oryctolagus cuniculus

substrate_name: diethyl paraoxon

ki_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I74F/H115W to reconstruct the assayed variant sequence.

proof_lines: pH 10.5, 25°C, recombinant mutant I74F/H115W

substrate: diethyl paraoxon


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I74F/H115W/T332S to reconstruct the assayed variant sequence.

proof_lines: pH 10.5, 25°C, recombinant mutant I74F/H115W/T332S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V346A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I74F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I74F/T332S to reconstruct the assayed variant sequence.

proof_lines: pH 10.5, 25°C, recombinant mutant I74F/T332S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T332S to reconstruct the assayed variant sequence.


organism: Brevundimonas diminuta

substrate_name: H2O; Paraoxon

substrate: H2O; Paraoxon


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S to reconstruct the assayed variant sequence.

proof_lines: expression mutant A80V/I106V/F132D/K185R/D208G/H257W/I274N/S308L/R319S, pH 8.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L271A/Y309A to reconstruct the assayed variant sequence.

proof_lines: mutant L271A/Y309A, pH 8.5, temperature not specified in the publication


substrate_name: 3-fluorophenyl diethyl phosphate

substrate: 3-fluorophenyl diethyl phosphate


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

sequence_source: multiple

proof_lines: pH 10.5, 25°C, recombinant PON1-hFc fusion enzyme

proof_lines: pH 8.0, 37°C, recombinant isozyme L55R192 PON1

proof_lines: pH 8.0, 37°C, recombinant isozyme L55Q192 PON1


substrate_name: dimethyl-paraoxon

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H115W/R192S with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant H115W/R192S

substrate: dimethyl-paraoxon


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H115W/R192A with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant H115W/R192A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H115W/R192W with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant H115W/R192W


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H115W/R192I with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant H115W/R192I


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H115W/R192N with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant H115W/R192N


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H115W/R192K with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant H115W/R192K


substrate_name: diethyl-paraoxon

proof_lines: pH 10.5, 25°C, recombinant PON1 wild-type enzyme

proof_lines: pH 8.0, recombinant wild-type PON1 genetic variant G2E6

substrate: diethyl-paraoxon


organism: Pseudomonas sp.

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

proof_lines: pH 8.0, 38°C, enzyme administered in mice in vivo


substrate_name: O,O-diethyl fluorophosphate

proof_lines: pH 8.0, 25°C, enzyme administered in mice in vivo

substrate: O,O-diethyl fluorophosphate


substrate_name: Tabun

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

substrate: Tabun


substrate_name: p-nitrophenyl caprate (C10)

proof_lines: kcat is 521 sec(-1) with PA as substrate. kcat is 450 sec(-1) with alpha-NA as substrate. kcat is 285 sec(-1) with p-nitrophenyl butyrate (C4) as substrate. kcat is 467 sec(-1) with p-nitrophenyl caproate (C6) as substrate. kcat is 410 sec(

substrate: p-nitrophenyl caprate (C10)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A80V/F132V/K185R/H254Q/H257Y/I274N to reconstruct the assayed variant sequence.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A434 and applied mutation signature A80V/F132V/K185R/H254Q/H257Y/I274N/S308L to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Constants for PTE Variants with APVR (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | RP-APVR kcat (s-1) | RP-APVR Km (mM) | RP-APVR kcat/Km (M-1 s-1) | SP-APVR kcat (s-1) | SP-APVR Km (mM) | SP-APVR kcat/Km (M-1 s-1) | ratio. Table 3, RP-APVR column group, enzyme row for PTE variant A80V/F132V/K185R/H254Q/H257Y/I274N/S308L; column 'kcat (s-1)' = 55; column 'Km (mM)' = 0.16; column 'kcat/Km (M-1 s-1)' = 3.4 x 10^5. captured primary segment: RP-APVR | PTE variant A80V/F132V/K185R/H254Q/H257Y/I274N/S308L | kcat 55 s^-1 | Km 0.16 mM | kcat/Km 3.4 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 55 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 55.0 s^(-1). Km: printed cell 0.16 mM; the printed Km column of this table is already in mM, so no conversion is applied; the paper value used here is 0.16 mM. kcat/Km: printed cell 3.4 x 10^5 M^-1 s^-1 = 340000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 340000 / 1000 = 340.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 55.0 / 0.16 = 343.75 s^-1 mM^-1, against the printed efficiency cell 340.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, RP-APVR column group, enzyme row for PTE variant A80V/F132V/K185R/H254Q/H257Y/I274N/S308L: kcat = 55 s^-1; Km = 0.16 mM; printed kcat/Km = 3.4 x 10^5 M^-1 s^-1.

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A80V/I106C/F132V/K185R/H254Q/H257Y/I274N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A434 and applied mutation signature A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Constants for PTE Variants with APVR (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | RP-APVR kcat (s-1) | RP-APVR Km (mM) | RP-APVR kcat/Km (M-1 s-1) | SP-APVR kcat (s-1) | SP-APVR Km (mM) | SP-APVR kcat/Km (M-1 s-1) | ratio. Table 3, RP-APVR column group, enzyme row for PTE variant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L; column 'kcat (s-1)' = 72; column 'Km (mM)' = 0.23; column 'kcat/Km (M-1 s-1)' = 3.2 x 10^5. captured primary segment: RP-APVR | PTE variant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L | kcat 72 s^-1 | Km 0.23 mM | kcat/Km 3.2 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 72 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 72.0 s^(-1). Km: printed cell 0.23 mM; the printed Km column of this table is already in mM, so no conversion is applied; the paper value used here is 0.23 mM. kcat/Km: printed cell 3.2 x 10^5 M^-1 s^-1 = 320000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 320000 / 1000 = 320.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 72.0 / 0.23 = 313.04347826086956 s^-1 mM^-1, against the printed efficiency cell 320.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, RP-APVR column group, enzyme row for PTE variant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L: kcat = 72 s^-1; Km = 0.23 mM; printed kcat/Km = 3.2 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A434 and applied mutation signature A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Constants for PTE Variants with APVR (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | RP-APVR kcat (s-1) | RP-APVR Km (mM) | RP-APVR kcat/Km (M-1 s-1) | SP-APVR kcat (s-1) | SP-APVR Km (mM) | SP-APVR kcat/Km (M-1 s-1) | ratio. Table 3, RP-APVR column group, enzyme row for PTE variant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L; column 'kcat (s-1)' = 56; column 'Km (mM)' = 0.41; column 'kcat/Km (M-1 s-1)' = 1.4 x 10^5. captured primary segment: RP-APVR | PTE variant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L | kcat 56 s^-1 | Km 0.41 mM | kcat/Km 1.4 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 56 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 56.0 s^(-1). Km: printed cell 0.41 mM; the printed Km column of this table is already in mM, so no conversion is applied; the paper value used here is 0.41 mM. kcat/Km: printed cell 1.4 x 10^5 M^-1 s^-1 = 140000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 140000 / 1000 = 140.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 56.0 / 0.41 = 136.58536585365854 s^-1 mM^-1, against the printed efficiency cell 140.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, RP-APVR column group, enzyme row for PTE variant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L: kcat = 56 s^-1; Km = 0.41 mM; printed kcat/Km = 1.4 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A434 and applied mutation signature F132V/H254Q/H257F/S308L to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Constants for PTE Variants with APVR (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | RP-APVR kcat (s-1) | RP-APVR Km (mM) | RP-APVR kcat/Km (M-1 s-1) | SP-APVR kcat (s-1) | SP-APVR Km (mM) | SP-APVR kcat/Km (M-1 s-1) | ratio. Table 3, RP-APVR column group, enzyme row for PTE variant F132V/H254Q/H257F/S308L; column 'kcat (s-1)' = 50; column 'Km (mM)' = 0.15; column 'kcat/Km (M-1 s-1)' = 3.3 x 10^5. captured primary segment: RP-APVR | PTE variant F132V/H254Q/H257F/S308L | kcat 50 s^-1 | Km 0.15 mM | kcat/Km 3.3 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 50 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 50.0 s^(-1). Km: printed cell 0.15 mM; the printed Km column of this table is already in mM, so no conversion is applied; the paper value used here is 0.15 mM. kcat/Km: printed cell 3.3 x 10^5 M^-1 s^-1 = 330000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 330000 / 1000 = 330.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 50.0 / 0.15 = 333.33333333333337 s^-1 mM^-1, against the printed efficiency cell 330.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, RP-APVR column group, enzyme row for PTE variant F132V/H254Q/H257F/S308L: kcat = 50 s^-1; Km = 0.15 mM; printed kcat/Km = 3.3 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A434 and applied mutation signature H254Q/H257F to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Constants for PTE Variants with APVR (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | RP-APVR kcat (s-1) | RP-APVR Km (mM) | RP-APVR kcat/Km (M-1 s-1) | SP-APVR kcat (s-1) | SP-APVR Km (mM) | SP-APVR kcat/Km (M-1 s-1) | ratio. Table 3, RP-APVR column group, enzyme row for PTE variant H254Q/H257F; column 'kcat (s-1)' = 57; column 'Km (mM)' = 0.36; column 'kcat/Km (M-1 s-1)' = 1.6 x 10^5. captured primary segment: RP-APVR | PTE variant H254Q/H257F | kcat 57 s^-1 | Km 0.36 mM | kcat/Km 1.6 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 57 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 57.0 s^(-1). Km: printed cell 0.36 mM; the printed Km column of this table is already in mM, so no conversion is applied; the paper value used here is 0.36 mM. kcat/Km: printed cell 1.6 x 10^5 M^-1 s^-1 = 160000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 160000 / 1000 = 160.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 57.0 / 0.36 = 158.33333333333334 s^-1 mM^-1, against the printed efficiency cell 160.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, RP-APVR column group, enzyme row for PTE variant H254Q/H257F: kcat = 57 s^-1; Km = 0.36 mM; printed kcat/Km = 1.6 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A434 and applied mutation signature I106C/F132V/H254Q/H257F to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Constants for PTE Variants with APVR (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | RP-APVR kcat (s-1) | RP-APVR Km (mM) | RP-APVR kcat/Km (M-1 s-1) | SP-APVR kcat (s-1) | SP-APVR Km (mM) | SP-APVR kcat/Km (M-1 s-1) | ratio. Table 3, RP-APVR column group, enzyme row for PTE variant I106C/F132V/H254Q/H257F; column 'kcat (s-1)' = 122; column 'Km (mM)' = 2.0; column 'kcat/Km (M-1 s-1)' = 6.0 x 10^4. captured primary segment: RP-APVR | PTE variant I106C/F132V/H254Q/H257F | kcat 122 s^-1 | Km 2.0 mM | kcat/Km 6.0 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 122 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 122.0 s^(-1). Km: printed cell 2.0 mM; the printed Km column of this table is already in mM, so no conversion is applied; the paper value used here is 2.0 mM. kcat/Km: printed cell 6.0 x 10^4 M^-1 s^-1 = 60000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 60000 / 1000 = 60.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 122.0 / 2.0 = 61.0 s^-1 mM^-1, against the printed efficiency cell 60.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, RP-APVR column group, enzyme row for PTE variant I106C/F132V/H254Q/H257F: kcat = 122 s^-1; Km = 2.0 mM; printed kcat/Km = 6.0 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A434 and applied mutation signature I106C/F132V/H254Q/H257F/S308L to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Constants for PTE Variants with APVR (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | RP-APVR kcat (s-1) | RP-APVR Km (mM) | RP-APVR kcat/Km (M-1 s-1) | SP-APVR kcat (s-1) | SP-APVR Km (mM) | SP-APVR kcat/Km (M-1 s-1) | ratio. Table 3, RP-APVR column group, enzyme row for PTE variant I106C/F132V/H254Q/H257F/S308L; column 'kcat (s-1)' = 46; column 'Km (mM)' = 0.18; column 'kcat/Km (M-1 s-1)' = 2.6 x 10^5. captured primary segment: RP-APVR | PTE variant I106C/F132V/H254Q/H257F/S308L | kcat 46 s^-1 | Km 0.18 mM | kcat/Km 2.6 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 46 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 46.0 s^(-1). Km: printed cell 0.18 mM; the printed Km column of this table is already in mM, so no conversion is applied; the paper value used here is 0.18 mM. kcat/Km: printed cell 2.6 x 10^5 M^-1 s^-1 = 260000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 260000 / 1000 = 260.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 46.0 / 0.18 = 255.55555555555557 s^-1 mM^-1, against the printed efficiency cell 260.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, RP-APVR column group, enzyme row for PTE variant I106C/F132V/H254Q/H257F/S308L: kcat = 46 s^-1; Km = 0.18 mM; printed kcat/Km = 2.6 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A434 and applied mutation signature I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Constants for PTE Variants with APVR (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | RP-APVR kcat (s-1) | RP-APVR Km (mM) | RP-APVR kcat/Km (M-1 s-1) | SP-APVR kcat (s-1) | SP-APVR Km (mM) | SP-APVR kcat/Km (M-1 s-1) | ratio. Table 3, RP-APVR column group, enzyme row for PTE variant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L; column 'kcat (s-1)' = 101; column 'Km (mM)' = 0.62; column 'kcat/Km (M-1 s-1)' = 1.6 x 10^5. captured primary segment: RP-APVR | PTE variant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L | kcat 101 s^-1 | Km 0.62 mM | kcat/Km 1.6 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 101 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 101.0 s^(-1). Km: printed cell 0.62 mM; the printed Km column of this table is already in mM, so no conversion is applied; the paper value used here is 0.62 mM. kcat/Km: printed cell 1.6 x 10^5 M^-1 s^-1 = 160000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 160000 / 1000 = 160.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 101.0 / 0.62 = 162.90322580645162 s^-1 mM^-1, against the printed efficiency cell 160.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, RP-APVR column group, enzyme row for PTE variant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L: kcat = 101 s^-1; Km = 0.62 mM; printed kcat/Km = 1.6 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A434 and applied mutation signature A80V/I106C/F132V/K185R/H254Q/H257Y/I274N to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic Parameters for PTE Variants with Paraoxon and DEVX (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | paraoxon kcat (s-1) | paraoxon Km (uM) | paraoxon kcat/Km (M-1 s-1) | DEVX kcat (s-1) | DEVX Km (mM) | DEVX kcat/Km (M-1 s-1) | fold improved. Table 4, paraoxon column group, enzyme row for PTE variant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N; column 'kcat (s-1)' = 35; column 'Km (uM)' = 3.6; column 'kcat/Km (M-1 s-1)' = 9.7 x 10^6. captured primary segment: paraoxon | PTE variant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N | kcat 35 s^-1 | Km 3.6 uM | kcat/Km 9.7 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 35 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 35.0 s^(-1). Km: printed cell 3.6 uM; 3.6 / 1000 = 0.0036 mM; the paper value used here is 0.0036 mM. kcat/Km: printed cell 9.7 x 10^6 M^-1 s^-1 = 9700000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9700000 / 1000 = 9700.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 35.0 / 0.0036 = 9722.222222222223 s^-1 mM^-1, against the printed efficiency cell 9700.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, paraoxon column group, enzyme row for PTE variant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N: kcat = 35 s^-1; Km = 3.6 uM; printed kcat/Km = 9.7 x 10^6 M^-1 s^-1.


column_label: Table 4. Kinetic Parameters for PTE Variants with Paraoxon and DEVX (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | paraoxon kcat (s-1) | paraoxon Km (uM) | paraoxon kcat/Km (M-1 s-1) | DEVX kcat (s-1) | DEVX Km (mM) | DEVX kcat/Km (M-1 s-1) | fold improved. Table 4, paraoxon column group, enzyme row for PTE variant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L; column 'kcat (s-1)' = 103; column 'Km (uM)' = 5.3; column 'kcat/Km (M-1 s-1)' = 1.9 x 10^7. captured primary segment: paraoxon | PTE variant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L | kcat 103 s^-1 | Km 5.3 uM | kcat/Km 1.9 x 10^7 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 103 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 103.0 s^(-1). Km: printed cell 5.3 uM; 5.3 / 1000 = 0.0053 mM; the paper value used here is 0.0053 mM. kcat/Km: printed cell 1.9 x 10^7 M^-1 s^-1 = 19000000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 19000000 / 1000 = 19000.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 103.0 / 0.0053 = 19433.962264150945 s^-1 mM^-1, against the printed efficiency cell 19000.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, paraoxon column group, enzyme row for PTE variant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L: kcat = 103 s^-1; Km = 5.3 uM; printed kcat/Km = 1.9 x 10^7 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A434 and applied mutation signature A80V/I106G/F132V/K185R/H254Q/H257Y/I274N to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic Parameters for PTE Variants with Paraoxon and DEVX (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | paraoxon kcat (s-1) | paraoxon Km (uM) | paraoxon kcat/Km (M-1 s-1) | DEVX kcat (s-1) | DEVX Km (mM) | DEVX kcat/Km (M-1 s-1) | fold improved. Table 4, paraoxon column group, enzyme row for PTE variant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N; column 'kcat (s-1)' = 58; column 'Km (uM)' = 9.2; column 'kcat/Km (M-1 s-1)' = 6.2 x 10^6. captured primary segment: paraoxon | PTE variant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N | kcat 58 s^-1 | Km 9.2 uM | kcat/Km 6.2 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 58 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 58.0 s^(-1). Km: printed cell 9.2 uM; 9.2 / 1000 = 0.0092 mM; the paper value used here is 0.0092 mM. kcat/Km: printed cell 6.2 x 10^6 M^-1 s^-1 = 6200000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6200000 / 1000 = 6200.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 58.0 / 0.0092 = 6304.347826086957 s^-1 mM^-1, against the printed efficiency cell 6200.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, paraoxon column group, enzyme row for PTE variant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N: kcat = 58 s^-1; Km = 9.2 uM; printed kcat/Km = 6.2 x 10^6 M^-1 s^-1.


column_label: Table 4. Kinetic Parameters for PTE Variants with Paraoxon and DEVX (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | paraoxon kcat (s-1) | paraoxon Km (uM) | paraoxon kcat/Km (M-1 s-1) | DEVX kcat (s-1) | DEVX Km (mM) | DEVX kcat/Km (M-1 s-1) | fold improved. Table 4, paraoxon column group, enzyme row for PTE variant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L; column 'kcat (s-1)' = 446; column 'Km (uM)' = 21; column 'kcat/Km (M-1 s-1)' = 2.1 x 10^7. captured primary segment: paraoxon | PTE variant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L | kcat 446 s^-1 | Km 21 uM | kcat/Km 2.1 x 10^7 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 446 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 446.0 s^(-1). Km: printed cell 21 uM; 21 / 1000 = 0.021 mM; the paper value used here is 0.021 mM. kcat/Km: printed cell 2.1 x 10^7 M^-1 s^-1 = 21000000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 21000000 / 1000 = 21000.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 446.0 / 0.021 = 21238.095238095237 s^-1 mM^-1, against the printed efficiency cell 21000.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, paraoxon column group, enzyme row for PTE variant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L: kcat = 446 s^-1; Km = 21 uM; printed kcat/Km = 2.1 x 10^7 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A434 and applied mutation signature F132V/H254Q/H257F to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic Parameters for PTE Variants with Paraoxon and DEVX (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | paraoxon kcat (s-1) | paraoxon Km (uM) | paraoxon kcat/Km (M-1 s-1) | DEVX kcat (s-1) | DEVX Km (mM) | DEVX kcat/Km (M-1 s-1) | fold improved. Table 4, paraoxon column group, enzyme row for PTE variant F132V/H254Q/H257F; column 'kcat (s-1)' = 108; column 'Km (uM)' = 11; column 'kcat/Km (M-1 s-1)' = 1.0 x 10^7. captured primary segment: paraoxon | PTE variant F132V/H254Q/H257F | kcat 108 s^-1 | Km 11 uM | kcat/Km 1.0 x 10^7 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 108 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 108.0 s^(-1). Km: printed cell 11 uM; 11 / 1000 = 0.011 mM; the paper value used here is 0.011 mM. kcat/Km: printed cell 1.0 x 10^7 M^-1 s^-1 = 10000000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 10000000 / 1000 = 10000.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 108.0 / 0.011 = 9818.181818181818 s^-1 mM^-1, against the printed efficiency cell 10000.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, paraoxon column group, enzyme row for PTE variant F132V/H254Q/H257F: kcat = 108 s^-1; Km = 11 uM; printed kcat/Km = 1.0 x 10^7 M^-1 s^-1.


column_label: Table 4. Kinetic Parameters for PTE Variants with Paraoxon and DEVX (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | paraoxon kcat (s-1) | paraoxon Km (uM) | paraoxon kcat/Km (M-1 s-1) | DEVX kcat (s-1) | DEVX Km (mM) | DEVX kcat/Km (M-1 s-1) | fold improved. Table 4, paraoxon column group, enzyme row for PTE variant F132V/H254Q/H257F/S308L; column 'kcat (s-1)' = 66; column 'Km (uM)' = 5.4; column 'kcat/Km (M-1 s-1)' = 1.2 x 10^7. captured primary segment: paraoxon | PTE variant F132V/H254Q/H257F/S308L | kcat 66 s^-1 | Km 5.4 uM | kcat/Km 1.2 x 10^7 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 66 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 66.0 s^(-1). Km: printed cell 5.4 uM; 5.4 / 1000 = 0.0054 mM; the paper value used here is 0.0054 mM. kcat/Km: printed cell 1.2 x 10^7 M^-1 s^-1 = 12000000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 12000000 / 1000 = 12000.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 66.0 / 0.0054 = 12222.22222222222 s^-1 mM^-1, against the printed efficiency cell 12000.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, paraoxon column group, enzyme row for PTE variant F132V/H254Q/H257F/S308L: kcat = 66 s^-1; Km = 5.4 uM; printed kcat/Km = 1.2 x 10^7 M^-1 s^-1.


column_label: Table 4. Kinetic Parameters for PTE Variants with Paraoxon and DEVX (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | paraoxon kcat (s-1) | paraoxon Km (uM) | paraoxon kcat/Km (M-1 s-1) | DEVX kcat (s-1) | DEVX Km (mM) | DEVX kcat/Km (M-1 s-1) | fold improved. Table 4, paraoxon column group, enzyme row for PTE variant H254Q/H257F; column 'kcat (s-1)' = 41; column 'Km (uM)' = 5.3; column 'kcat/Km (M-1 s-1)' = 7.7 x 10^6. captured primary segment: paraoxon | PTE variant H254Q/H257F | kcat 41 s^-1 | Km 5.3 uM | kcat/Km 7.7 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 41 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 41.0 s^(-1). Km: printed cell 5.3 uM; 5.3 / 1000 = 0.0053 mM; the paper value used here is 0.0053 mM. kcat/Km: printed cell 7.7 x 10^6 M^-1 s^-1 = 7700000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7700000 / 1000 = 7700.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 41.0 / 0.0053 = 7735.8490566037735 s^-1 mM^-1, against the printed efficiency cell 7700.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, paraoxon column group, enzyme row for PTE variant H254Q/H257F: kcat = 41 s^-1; Km = 5.3 uM; printed kcat/Km = 7.7 x 10^6 M^-1 s^-1.


column_label: Table 4. Kinetic Parameters for PTE Variants with Paraoxon and DEVX (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | paraoxon kcat (s-1) | paraoxon Km (uM) | paraoxon kcat/Km (M-1 s-1) | DEVX kcat (s-1) | DEVX Km (mM) | DEVX kcat/Km (M-1 s-1) | fold improved. Table 4, paraoxon column group, enzyme row for PTE variant I106C/F132V/H254Q/H257F; column 'kcat (s-1)' = 33; column 'Km (uM)' = 6.7; column 'kcat/Km (M-1 s-1)' = 4.8 x 10^6. captured primary segment: paraoxon | PTE variant I106C/F132V/H254Q/H257F | kcat 33 s^-1 | Km 6.7 uM | kcat/Km 4.8 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 33 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 33.0 s^(-1). Km: printed cell 6.7 uM; 6.7 / 1000 = 0.0067 mM; the paper value used here is 0.0067 mM. kcat/Km: printed cell 4.8 x 10^6 M^-1 s^-1 = 4800000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4800000 / 1000 = 4800.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 33.0 / 0.0067 = 4925.373134328358 s^-1 mM^-1, against the printed efficiency cell 4800.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, paraoxon column group, enzyme row for PTE variant I106C/F132V/H254Q/H257F: kcat = 33 s^-1; Km = 6.7 uM; printed kcat/Km = 4.8 x 10^6 M^-1 s^-1.


column_label: Table 4. Kinetic Parameters for PTE Variants with Paraoxon and DEVX (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | paraoxon kcat (s-1) | paraoxon Km (uM) | paraoxon kcat/Km (M-1 s-1) | DEVX kcat (s-1) | DEVX Km (mM) | DEVX kcat/Km (M-1 s-1) | fold improved. Table 4, paraoxon column group, enzyme row for PTE variant I106C/F132V/H254Q/H257F/S308L; column 'kcat (s-1)' = 38; column 'Km (uM)' = 5.6; column 'kcat/Km (M-1 s-1)' = 6.8 x 10^6. captured primary segment: paraoxon | PTE variant I106C/F132V/H254Q/H257F/S308L | kcat 38 s^-1 | Km 5.6 uM | kcat/Km 6.8 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 38 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 38.0 s^(-1). Km: printed cell 5.6 uM; 5.6 / 1000 = 0.0056 mM; the paper value used here is 0.0056 mM. kcat/Km: printed cell 6.8 x 10^6 M^-1 s^-1 = 6800000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6800000 / 1000 = 6800.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 38.0 / 0.0056 = 6785.714285714286 s^-1 mM^-1, against the printed efficiency cell 6800.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, paraoxon column group, enzyme row for PTE variant I106C/F132V/H254Q/H257F/S308L: kcat = 38 s^-1; Km = 5.6 uM; printed kcat/Km = 6.8 x 10^6 M^-1 s^-1.


column_label: Table 4. Kinetic Parameters for PTE Variants with Paraoxon and DEVX (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | paraoxon kcat (s-1) | paraoxon Km (uM) | paraoxon kcat/Km (M-1 s-1) | DEVX kcat (s-1) | DEVX Km (mM) | DEVX kcat/Km (M-1 s-1) | fold improved. Table 4, paraoxon column group, enzyme row for PTE variant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L; column 'kcat (s-1)' = 85; column 'Km (uM)' = 7.2; column 'kcat/Km (M-1 s-1)' = 1.2 x 10^7. captured primary segment: paraoxon | PTE variant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L | kcat 85 s^-1 | Km 7.2 uM | kcat/Km 1.2 x 10^7 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 85 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 85.0 s^(-1). Km: printed cell 7.2 uM; 7.2 / 1000 = 0.0072 mM; the paper value used here is 0.0072 mM. kcat/Km: printed cell 1.2 x 10^7 M^-1 s^-1 = 12000000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 12000000 / 1000 = 12000.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 85.0 / 0.0072 = 11805.555555555557 s^-1 mM^-1, against the printed efficiency cell 12000.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, paraoxon column group, enzyme row for PTE variant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L: kcat = 85 s^-1; Km = 7.2 uM; printed kcat/Km = 1.2 x 10^7 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A434 and applied mutation signature I106G/F132V/H254Q/H257F to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic Constants for PTE Variants with APVR (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | RP-APVR kcat (s-1) | RP-APVR Km (mM) | RP-APVR kcat/Km (M-1 s-1) | SP-APVR kcat (s-1) | SP-APVR Km (mM) | SP-APVR kcat/Km (M-1 s-1) | ratio. Table 3, RP-APVR column group, enzyme row for PTE variant I106G/F132V/H254Q/H257F; column 'kcat (s-1)' = 100; column 'Km (mM)' = 4; column 'kcat/Km (M-1 s-1)' = 2.4 x 10^4. captured primary segment: RP-APVR | PTE variant I106G/F132V/H254Q/H257F | kcat 100 s^-1 | Km 4 mM | kcat/Km 2.4 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 100 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 100.0 s^(-1). Km: printed cell 4 mM; the printed Km column of this table is already in mM, so no conversion is applied; the paper value used here is 4.0 mM. kcat/Km: printed cell 2.4 x 10^4 M^-1 s^-1 = 24000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 24000 / 1000 = 24.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 100.0 / 4.0 = 25.0 s^-1 mM^-1, against the printed efficiency cell 24.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, RP-APVR column group, enzyme row for PTE variant I106G/F132V/H254Q/H257F: kcat = 100 s^-1; Km = 4 mM; printed kcat/Km = 2.4 x 10^4 M^-1 s^-1.


sequence_variant_note: Mutation signature I106G/F132V/H254Q/H257F/S308L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature I106G/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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

column_label: Table 3. Kinetic Constants for PTE Variants with APVR (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | RP-APVR kcat (s-1) | RP-APVR Km (mM) | RP-APVR kcat/Km (M-1 s-1) | SP-APVR kcat (s-1) | SP-APVR Km (mM) | SP-APVR kcat/Km (M-1 s-1) | ratio. Table 3, RP-APVR column group, enzyme row for wild-type PTE (no mutations); column 'kcat (s-1)' = 84; column 'Km (mM)' = 1.7; column 'kcat/Km (M-1 s-1)' = 4.9 x 10^4. captured primary segment: RP-APVR | wild-type PTE (no mutations) | kcat 84 s^-1 | Km 1.7 mM | kcat/Km 4.9 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 84 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 84.0 s^(-1). Km: printed cell 1.7 mM; the printed Km column of this table is already in mM, so no conversion is applied; the paper value used here is 1.7 mM. kcat/Km: printed cell 4.9 x 10^4 M^-1 s^-1 = 49000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 49000 / 1000 = 49.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 84.0 / 1.7 = 49.411764705882355 s^-1 mM^-1, against the printed efficiency cell 49.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, RP-APVR column group, enzyme row for wild-type PTE (no mutations): kcat = 84 s^-1; Km = 1.7 mM; printed kcat/Km = 4.9 x 10^4 M^-1 s^-1.


sequence_variant_note: Mutation signature A80V/F132V/K185R/H254Q/H257Y/I274N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature A80V/F132V/K185R/H254Q/H257Y/I274N/S308L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature A80V/I106C/F132V/K185R/H254Q/H257Y/I274N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature F132V/H254Q/H257F/S308L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A434 and applied mutation signature I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L/Y309F to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic Parameters for PTE Variants with Paraoxon and DEVX (Biochemistry 2015, 54, 5502-5512); printed column heads enzyme | paraoxon kcat (s-1) | paraoxon Km (uM) | paraoxon kcat/Km (M-1 s-1) | DEVX kcat (s-1) | DEVX Km (mM) | DEVX kcat/Km (M-1 s-1) | fold improved. Table 4, paraoxon column group, enzyme row for PTE variant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L/Y309F; column 'kcat (s-1)' = 131; column 'Km (uM)' = 9.2; column 'kcat/Km (M-1 s-1)' = 1.43 x 10^7. captured primary segment: paraoxon | PTE variant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L/Y309F | kcat 131 s^-1 | Km 9.2 uM | kcat/Km 1.43 x 10^7 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 131 s^-1; the printed turnover column is per second, so no conversion is applied and the paper value is 131.0 s^(-1). Km: printed cell 9.2 uM; 9.2 / 1000 = 0.0092 mM; the paper value used here is 0.0092 mM. kcat/Km: printed cell 1.43 x 10^7 M^-1 s^-1 = 14300000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 14300000 / 1000 = 14300.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 131.0 / 0.0092 = 14239.130434782608 s^-1 mM^-1, against the printed efficiency cell 14300.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, paraoxon column group, enzyme row for PTE variant I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L/Y309F: kcat = 131 s^-1; Km = 9.2 uM; printed kcat/Km = 1.43 x 10^7 M^-1 s^-1.


sequence_variant_note: Mutation signature I106G/F132V/H254Q/H257F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


smiles: CCOP(=O)(OCC)SCCN(C(C)C)C(C)C


sequence_variant_note: Mutation signature F132V/H254Q/H257F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H254Q/H257F to reconstruct the assayed variant sequence.

column_label: SP-APVR kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1) columns

row_label: QF; final substitutions H254Q/H257F

table_label: Table 3


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I106C/F132V/H254Q/H257F to reconstruct the assayed variant sequence.

row_label: CVQFL derivative with wild-type Ser308 restored; final substitutions I106C/F132V/H254Q/H257F


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I106C/F132V/H254Q/H257F/S308L to reconstruct the assayed variant sequence.

raw_value_unit_evidence: Table 3 CVQFL: kcat 21 s^-1; Km 0.19 mM; kcat/Km 1.1 x 10^5 M^-1 s^-1.

row_label: CVQFL; final substitutions I106C/F132V/H254Q/H257F/S308L


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L to reconstruct the assayed variant sequence.

row_label: L7ep-3a; final substitutions I106C/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I106G/F132V/H254Q/H257F to reconstruct the assayed variant sequence.

row_label: CVQFL I106G derivative with wild-type Ser308 restored; final substitutions I106G/F132V/H254Q/H257F


sequence_variant_note: Resolved canonical sequence from uniprotkb:P0A434 and applied mutation signature I106G/F132V/H254Q/H257F/S308L to reconstruct the assayed variant sequence.

row_label: CVQFL-I106G; final substitutions I106G/F132V/H254Q/H257F/S308L


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I106G/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L to reconstruct the assayed variant sequence.

row_label: L7ep-3a I106G; final substitutions I106G/F132V/H254Q/H257Y/A270V/L272M/I274N/S308L


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

raw_value_unit_evidence: Table 3 wild-type: kcat 25 s^-1; Km 4.5 mM; kcat/Km 6 x 10^3 M^-1 s^-1.

row_label: wild-type


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A80V/F132V/K185R/H254Q/H257Y/I274N to reconstruct the assayed variant sequence.

column_label: paraoxon kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1) columns

raw_value_unit_evidence: Table 4 VRN-VQFL-L308S: kcat 15 s^-1; Km 1.7 uM; kcat/Km 8.8 x 10^6 M^-1 s^-1.

row_label: VRN-VQFL derivative with wild-type Ser308 restored; final substitutions A80V/F132V/K185R/H254Q/H257Y/I274N

table_label: Table 4


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A80V/F132V/K185R/H254Q/H257Y/I274N/S308L to reconstruct the assayed variant sequence.

raw_value_unit_evidence: Table 4 VRN-VQFL: kcat 116 s^-1; Km 8 uM; kcat/Km 1.5 x 10^7 M^-1 s^-1.

row_label: VRN-VQFL; final substitutions A80V/F132V/K185R/H254Q/H257Y/I274N/S308L


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


organism: Sphingobium sp. TCM1

substrate_name: methyl 4-nitrophenyl phenyl (S)-phosphate

column_label: Table 2; row (S_P)-5 *; column kcat (s^-1) raw value 0.6 +/- 0.1; column Km (mM) raw value 0.25 +/- 0.07; column kcat/Km (M^-1 s^-1) raw value 2.5 +/- 0.7 x 10^3

normalized_value_unit_evidence: kcat normalized_value=0.6 normalized_unit=s^-1; Km normalized_value=0.25 normalized_unit=mM; kcat/Km normalized_value=2.5 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.6 +/- 0.1 raw_unit=s^-1; Km raw_value=0.25 +/- 0.07 raw_unit=mM; kcat/Km raw_value=2.5 +/- 0.7 x 10^3 raw_unit=M^-1*s^-1

table_label: Table 2. Kinetic constants for Sb-PTE with compounds 1-11.


substrate_name: methyl 4-nitrophenyl propan-2-yl (R)-phosphate

column_label: Table 2; row (R_P)-4; column kcat (s^-1) raw value 5 +/- 2; column Km (mM) raw value 2.3 +/- 0.9; column kcat/Km (M^-1 s^-1) raw value 2.1 +/- 0.1 x 10^3

normalized_value_unit_evidence: kcat normalized_value=5 normalized_unit=s^-1; Km normalized_value=2.3 normalized_unit=mM; kcat/Km normalized_value=2.1 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=5 +/- 2 raw_unit=s^-1; Km raw_value=2.3 +/- 0.9 raw_unit=mM; kcat/Km raw_value=2.1 +/- 0.1 x 10^3 raw_unit=M^-1*s^-1


substrate_name: methyl 4-nitrophenyl propan-2-yl (S)-phosphate

column_label: Table 2, row (SP)-4, column kcat (s^-1), cell 2.05 ± 0.09, normalized 2.05 s^-1; Table 2, row (SP)-4, column Km (mM), cell 0.036 ± 0.006, normalized 0.036 mM; Table 2, row (SP)-4, column kcat/Km (M^-1 s^-1), cell 2.6 ± 0.4 × 104, normalized 26 s^-1 mM^-1

raw_value_unit_evidence: kcat raw 2.05 ± 0.09 s^-1 from Table 2; Km raw 0.036 ± 0.006 mM from Table 2; kcat/Km raw 2.6 ± 0.4 × 104 M^-1 s^-1 from Table 2


substrate_name: methyl bis(4-nitrophenyl) phosphate

column_label: Table 2, row 2, column kcat (s^-1), cell 9 ± 1, normalized 9 s^-1; Table 2, row 2, column Km (mM), cell 0.08 ± 0.02, normalized 0.08 mM; Table 2, row 2, column kcat/Km (M^-1 s^-1), cell 1.1 ± 0.3 × 105, normalized 110 s^-1 mM^-1

raw_value_unit_evidence: kcat raw 9 ± 1 s^-1 from Table 2; Km raw 0.08 ± 0.02 mM from Table 2; kcat/Km raw 1.1 ± 0.3 × 105 M^-1 s^-1 from Table 2

substrate: methyl bis(4-nitrophenyl) phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H115W to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature H115W/R192A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature H115W/R192I could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature H115W/R192K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature H115W/R192N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature H115W/R192S could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature H115W/R192W could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: Paraoxon

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H201N to reconstruct the assayed variant sequence.

substrate: Paraoxon


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H230N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H254N with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H257N with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H55N with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H57N with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


substrate_name: 4-acetylphenyl cyclohexyl methyl (R)-phosphate

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

column_label: Table 2; row (R_P)-7; column kcat (s^-1) raw value 0.36 +/- 0.03; column Km (mM) raw value 0.31 +/- 0.06; column kcat/Km (M^-1 s^-1) raw value 1.1 +/- 0.2 x 10^3

normalized_value_unit_evidence: kcat normalized_value=0.36 normalized_unit=s^-1; Km normalized_value=0.31 normalized_unit=mM; kcat/Km normalized_value=1.1 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.36 +/- 0.03 raw_unit=s^-1; Km raw_value=0.31 +/- 0.06 raw_unit=mM; kcat/Km raw_value=1.1 +/- 0.2 x 10^3 raw_unit=M^-1*s^-1


substrate_name: 4-acetylphenyl cyclohexyl methyl (S)-phosphate

column_label: Table 2; row (S_P)-7; column kcat (s^-1) raw value 0.38 +/- 0.03; column Km (mM) raw value 0.12 +/- 0.02; column kcat/Km (M^-1 s^-1) raw value 3.2 +/- 0.7 x 10^3

normalized_value_unit_evidence: kcat normalized_value=0.38 normalized_unit=s^-1; Km normalized_value=0.12 normalized_unit=mM; kcat/Km normalized_value=3.2 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.38 +/- 0.03 raw_unit=s^-1; Km raw_value=0.12 +/- 0.02 raw_unit=mM; kcat/Km raw_value=3.2 +/- 0.7 x 10^3 raw_unit=M^-1*s^-1


substrate_name: cyclohexyl ethyl 4-nitrophenyl (R)-phosphate

column_label: Table 2, row (RP)-6, column kcat (s^-1), cell 2.5 ± 0.1, normalized 2.5 s^-1; Table 2, row (RP)-6, column Km (mM), cell 0.059 ± 0.007, normalized 0.059 mM; Table 2, row (RP)-6, column kcat/Km (M^-1 s^-1), cell 4.1 ± 0.5 × 104, normalized 41 s^-1 mM^-1

raw_value_unit_evidence: kcat raw 2.5 ± 0.1 s^-1 from Table 2; Km raw 0.059 ± 0.007 mM from Table 2; kcat/Km raw 4.1 ± 0.5 × 104 M^-1 s^-1 from Table 2


substrate_name: cyclohexyl ethyl 4-nitrophenyl (S)-phosphate

column_label: Table 2, row (SP)-6, column kcat (s^-1), cell 2.8 ± 0.2, normalized 2.8 s^-1; Table 2, row (SP)-6, column Km (mM), cell 0.054 ± 0.009, normalized 0.054 mM; Table 2, row (SP)-6, column kcat/Km (M^-1 s^-1), cell 5.1 ± 0.9 × 104, normalized 51 s^-1 mM^-1

raw_value_unit_evidence: kcat raw 2.8 ± 0.2 s^-1 from Table 2; Km raw 0.054 ± 0.009 mM from Table 2; kcat/Km raw 5.1 ± 0.9 × 104 M^-1 s^-1 from Table 2


substrate_name: cyclohexyl methyl 4-nitrophenyl (R)-phosphate

column_label: Table 2; row (R_P)-1; column kcat (s^-1) raw value 6 +/- 1; column Km (mM) raw value 1.1 +/- 0.2; column kcat/Km (M^-1 s^-1) raw value 4.7 +/- 0.3 x 10^3

normalized_value_unit_evidence: kcat normalized_value=6 normalized_unit=s^-1; Km normalized_value=1.1 normalized_unit=mM; kcat/Km normalized_value=4.7 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=6 +/- 1 raw_unit=s^-1; Km raw_value=1.1 +/- 0.2 raw_unit=mM; kcat/Km raw_value=4.7 +/- 0.3 x 10^3 raw_unit=M^-1*s^-1


substrate_name: cyclohexyl methyl 4-nitrophenyl (S)-phosphate

column_label: Table 2, row (SP)-1, column kcat (s^-1), cell 1.11 ± 0.05, normalized 1.11 s^-1; Table 2, row (SP)-1, column Km (mM), cell 0.053 ± 0.007, normalized 0.053 mM; Table 2, row (SP)-1, column kcat/Km (M^-1 s^-1), cell 2.1 ± 0.3 × 104, normalized 21 s^-1 mM^-1

raw_value_unit_evidence: kcat raw 1.11 ± 0.05 s^-1 from Table 2; Km raw 0.053 ± 0.007 mM from Table 2; kcat/Km raw 2.1 ± 0.3 × 104 M^-1 s^-1 from Table 2


substrate_name: cyclohexyl methyl phenyl (R)-phosphate

column_label: Table 2, row (RP)-8, column kcat (s^-1), cell 0.38 ± 0.01, normalized 0.38 s^-1; Table 2, row (RP)-8, column Km (mM), cell 0.006 ± 0.002, normalized 0.006 mM; Table 2, row (RP)-8, column kcat/Km (M^-1 s^-1), cell 1.4 ± 0.2 × 104, normalized 14 s^-1 mM^-1

raw_value_unit_evidence: kcat raw 0.38 ± 0.01 s^-1 from Table 2; Km raw 0.006 ± 0.002 mM from Table 2; kcat/Km raw 1.4 ± 0.2 × 104 M^-1 s^-1 from Table 2

substrate: cyclohexyl methyl phenyl (R)-phosphate


substrate_name: diethyl 4-nitrophenyl phosphate

column_label: Table 2, row 11, column kcat (s^-1), cell 6.5 ± 0.2, normalized 6.5 s^-1; Table 2, row 11, column Km (mM), cell 0.083 ± 0.009, normalized 0.083 mM; Table 2, row 11, column kcat/Km (M^-1 s^-1), cell 7.9 ± 0.9 × 104, normalized 79 s^-1 mM^-1

raw_value_unit_evidence: kcat raw 6.5 ± 0.2 s^-1 from Table 2; Km raw 0.083 ± 0.009 mM from Table 2; kcat/Km raw 7.9 ± 0.9 × 104 M^-1 s^-1 from Table 2

substrate: diethyl 4-nitrophenyl phosphate


substrate_name: dimethyl 4-nitrophenyl phosphate

column_label: Table 2, row 3, column kcat (s^-1), cell 9.1 ± 0.4, normalized 9.1 s^-1; Table 2, row 3, column Km (mM), cell 0.76 ± 0.05, normalized 0.76 mM; Table 2, row 3, column kcat/Km (M^-1 s^-1), cell 1.2 ± 0.1 ×104, normalized 12 s^-1 mM^-1

raw_value_unit_evidence: kcat raw 9.1 ± 0.4 s^-1 from Table 2; Km raw 0.76 ± 0.05 mM from Table 2; kcat/Km raw 1.2 ± 0.1 ×104 M^-1 s^-1 from Table 2

substrate: dimethyl 4-nitrophenyl phosphate


substrate_name: methyl 4-nitrophenyl phenyl (R)-phosphate

column_label: Table 2, row (RP)-5, column kcat (s^-1), cell 6.3 ± 0.3, normalized 6.3 s^-1; Table 2, row (RP)-5, column Km (mM), cell 0.061 ± 0.007, normalized 0.061 mM; Table 2, row (RP)-5, column kcat/Km (M^-1 s^-1), cell 1.0 ± 0.1 × 105, normalized 100 s^-1 mM^-1

raw_value_unit_evidence: kcat raw 6.3 ± 0.3 s^-1 from Table 2; Km raw 0.061 ± 0.007 mM from Table 2; kcat/Km raw 1.0 ± 0.1 × 105 M^-1 s^-1 from Table 2


substrate_name: paraoxon

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W263F with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y97W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y97W/I261F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y97W/I98F/I261F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y97W/W263F to reconstruct the assayed variant sequence.


substrate_name: diisopropylfluorophosphate

substrate: diisopropylfluorophosphate


substrate_name: O-isopropyl methylphosphonofluoridate

proof_lines:
diisopropylfluorophosphate
organophosphorus acid anhydrase
DFP

substrate: O-isopropyl methylphosphonofluoridate


substrate_name: O-pinacolyl methylphosphonofluoridate

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

substrate: O-pinacolyl methylphosphonofluoridate


substrate_name: O-cyclohexyl methylphosphonofluoridate

substrate: O-cyclohexyl methylphosphonofluoridate


organism: Sulfolobus islandicus

substrate_name: malathion

smiles: CCOC(=O)CC(SP(=S)(OC)OC)C(=O)OCC

column_label: PLOS ONE DOI 10.1371/journal.pone.0047028 Table 3; row Malathion (r) (V); columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: Malathion (r) (V)

table_label: Table 3. Kinetic parameters of wild-type SisLac with organophosphate substrates

substrate: malathion


substrate_name: methyl paraoxon

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E14K to reconstruct the assayed variant sequence.

column_label: PLOS ONE DOI 10.1371/journal.pone.0047028 Table 8; row Methyl Paraoxon / SisLac E14K; columns kcat (s^-1), Km (uM), and kcat/Km (10^3 M^-1 s^-1).

row_label: Methyl Paraoxon / SisLac E14K

table_label: Table 8. Kinetic parameters of SisLac mutants with methyl paraoxon

substrate: methyl paraoxon


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E14K/Y34Q to reconstruct the assayed variant sequence.

column_label: PLOS ONE DOI 10.1371/journal.pone.0047028 Table 8; row Methyl Paraoxon / SisLac E14K-Y34Q*; columns kcat (s^-1), Km (uM), kcat/Km (10^3 M^-1 s^-1), and footnote substrate inhibition Ki.

raw_value_unit_evidence: Table 8 row Methyl Paraoxon / SisLac E14K-Y34Q*: kcat 0.86 +/- 0.21 s^-1; Km 620 +/- 198 uM; kcat/Km 1.39 (+/- 0.78) x 10^3 M^-1 s^-1; substrate inhibition Ki 855 +/- 376 uM.

row_label: Methyl Paraoxon / SisLac E14K-Y34Q


column_label: PLOS ONE DOI 10.1371/journal.pone.0047028 Table 3; row Methyl-Paraoxon (II); columns kcat (s^-1), Km (uM), and kcat/Km (10^3 M^-1 s^-1).

row_label: Methyl-Paraoxon (II)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y34Q with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

column_label: PLOS ONE DOI 10.1371/journal.pone.0047028 Table 8; row Methyl Paraoxon / SisLac Y34Q; columns kcat (s^-1), Km (uM), and kcat/Km (10^3 M^-1 s^-1).

row_label: Methyl Paraoxon / SisLac Y34Q


substrate_name: methyl parathion

column_label: PLOS ONE DOI 10.1371/journal.pone.0047028 Table 3; row Methyl-Parathion (IV); columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: Methyl-Parathion (IV)

substrate: methyl parathion


enzyme_display_name: Transferred entry: 3.8.2.2

organism: Sphingobium fuliginis

substrate_name: diisopropyl fluorophosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F132Y with inferred residue-numbering offset -28 to reconstruct the assayed variant sequence.

smiles: CC(C)OP(=O)(F)OC(C)C

enzyme: Transferred entry: 3.8.2.2

substrate: diisopropyl fluorophosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F132Y/L140Y with inferred residue-numbering offset -28 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L140Y with inferred residue-numbering offset -28 to reconstruct the assayed variant sequence.


enzyme_display_name: Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN

organism: Homo sapiens

substrate_name: 1D-myo-inositol 1,3,4-trisphosphate

column_label: ScienceDirect Table 1 row Ins(1,3,4)P3 under column Km (uM) reports 11.5.

table_label: Table 1. Kinetic parameters for PTEN

substrate: 1D-myo-inositol 1,3,4-trisphosphate


column_label: ScienceDirect Table 1 row Ins(1,3,4,5)P4 under column Km (uM) reports 4.6.

enzyme: Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN


column_label: ScienceDirect Table 1 row InsP5 under column Km (uM) reports 7.1; article abstract names this substrate as Ins(1,3,4,5,6)P5.

raw_value_unit_evidence: InsP5 Km 7.1 uM


enzyme_display_name: protein-tyrosine-phosphatase

substrate_name: PGSAAP-pY-LKTKFI

enzyme: protein-tyrosine-phosphatase

substrate: PGSAAP-pY-LKTKFI


substrate_name: PQDKEY-pY-KVKEPG

substrate: PQDKEY-pY-KVKEPG


substrate_name: RKGSGD-pY-MPMSPK

substrate: RKGSGD-pY-MPMSPK


substrate_name: parathion

substrate: parathion


substrate_name: CMP-coumarin

column_label: Table 1 row CMP-Coumarin, columns kcat (s^-1), KM (microM), and kcat/KM (M^-1.s^-1), match exported metrics after unit conversion.

normalized_value_unit_evidence: kcat=0.28 s^-1; KM=0.642 mM; kcat/KM=0.438 s^-1*mM^-1, matching exported 0.4361370716510904 within table rounding/uncertainty.

row_label: CMP-Coumarin

substrate: CMP-coumarin


substrate_name: (1E)-but-1-en-1-yl dibutyl phosphate

smiles: CC/C=C/OP(=O)(OCCCC)OCCCC

column_label: Scheme 1 compound 23 (1E)-but-1-en-1-yl structure; Table 1 row 23; columns Km, superscript-T kcat, and superscript-T kcat/Km.

normalized_value_unit_evidence: Km 0.088 mM; total kcat 0.83 s^-1; total kcat/Km 9.4 s^-1 mM^-1.

raw_value_unit_evidence: Scheme 1 compound 23; Table 1 row 23: Km 0.088 mM; total kcat 0.83 s^-1; total kcat/Km 9.4 x 10^3 M^-1 s^-1.

row_label: compound 23 / total hydrolysis

substrate: (1E)-but-1-en-1-yl dibutyl phosphate


smiles: CCCCOP(=O)(OCCCC)OCC(F)(F)C(C)(F)F

column_label: Scheme 1 compound 24 structure; Table 1 row 24; columns Km, superscript-T kcat, and superscript-T kcat/Km.

normalized_value_unit_evidence: Km 0.11 mM; total kcat 0.36 s^-1; total kcat/Km 3.3 s^-1 mM^-1.

raw_value_unit_evidence: Scheme 1 compound 24; Table 1 row 24: Km 0.11 mM; total kcat 0.36 s^-1; total kcat/Km 3.3 x 10^3 M^-1 s^-1.

row_label: compound 24 / total hydrolysis


substrate_name: dibutyl 3,3-difluorobutyl phosphate

smiles: CCCCOP(=O)(OCCCC)OCCCC

column_label: Scheme 1 compound 26 3,3-difluorobutyl structure; Table 1 row 26; columns Km, superscript-T kcat, and superscript-T kcat/Km.

normalized_value_unit_evidence: Km 0.17 mM; total kcat 0.043 s^-1; total kcat/Km 0.76 s^-1 mM^-1.

raw_value_unit_evidence: Scheme 1 compound 26; Table 1 row 26: Km 0.17 mM; total kcat 0.043 s^-1; total kcat/Km 7.6 x 10^2 M^-1 s^-1.

row_label: compound 26 / total hydrolysis

substrate: dibutyl 3,3-difluorobutyl phosphate


substrate_name: O,O,S-tributyl phosphorothioate

smiles: CCCCOP(=O)(OCCCC)SCCCC

column_label: Scheme 1 compound 22 O,O,S-tributyl structure; Table 1 row 22; columns Km, superscript-T kcat, and superscript-T kcat/Km.

normalized_value_unit_evidence: Km 0.085 mM; total kcat 0.42 s^-1; total kcat/Km 4.9 s^-1 mM^-1.

raw_value_unit_evidence: Scheme 1 compound 22; Table 1 row 22: Km 0.085 mM; total kcat 0.42 s^-1; total kcat/Km 4.9 x 10^3 M^-1 s^-1.

row_label: compound 22 / total hydrolysis

substrate: O,O,S-tributyl phosphorothioate


enzyme_display_name: phosphodiesterase I

organism: Methanocaldococcus jannaschii

substrate_name: 4-Nitrophenyl phosphocholine

substrate: 4-Nitrophenyl phosphocholine


substrate_name: Bis-4-nitrophenyl phosphate

substrate: Bis-4-nitrophenyl phosphate


substrate_name: p-Nitrophenylthymidine phosphate

substrate: p-Nitrophenylthymidine phosphate


substrate_name: paraoxon

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H123A to reconstruct the assayed variant sequence.

substrate: paraoxon


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H123I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H123N to reconstruct the assayed variant sequence.


organism: Triticum aestivum

substrate_name: 2-carboxy-D-arabinitol 1-phosphate

substrate: 2-carboxy-D-arabinitol 1-phosphate


substrate_name: 2-carboxy-D-arabinitol 1,5-bisphosphate

substrate: 2-carboxy-D-arabinitol 1,5-bisphosphate


organism: Saccharolobus solfataricus

substrate_name: malathion

assay_conditions_summary: pH 9; 298.15 K; buffer activity

column_label: Official PMC HTML/XML Table 1 row Malathion (VI) (r) 25 C, columns kcat=(8.9 +/- 0.4) x 10^-4 s^-1, KM=160 +/- 29 uM, kcat/KM=5.56 +/- 1.26 s^-1 M^-1.

row_label: Malathion (VI) (r) 25 C

table_label: Table 1. Organophosphate hydrolase activity characterisation of SsoPox.

substrate: malathion


substrate_name: methyl paraoxon

column_label: Official PMC HTML/XML Table 1 row Methyl-Paraoxon (II) 25 C, columns kcat=2.71 +/- 0.64 s^-1, KM=2142 +/- 676 uM, kcat/KM=(1.27 +/- 0.70) x 10^3 s^-1 M^-1.

row_label: Methyl-Paraoxon (II) 25 C

substrate: methyl paraoxon


substrate_name: methyl parathion

column_label: Official PMC HTML/XML Table 1 row Methyl-Parathion (IV) 25 C, columns kcat=(1.1 +/- 0.02) x 10^-3 s^-1, KM=121 +/- 10 uM, kcat/KM=9.09 +/- 0.9 s^-1 M^-1.

row_label: Methyl-Parathion (IV) 25 C

substrate: methyl parathion


enzyme_display_name: Phospholipid phosphatase 1

organism: Rattus norvegicus

substrate_name: 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate (at pH 6.5 and 37 degrees Celsius)

column_label: Abstract reports apparent Km values for phosphatidate, ceramide 1-phosphate, lysophosphatidate, and sphingosine 1-phosphate as 3.5, 1.9, 0.4, and 4.0 microM respectively.

raw_value_unit_evidence: Km raw_value=3.5 microM raw_unit=microM

row_label: Rat liver plasma membrane anionic phosphatidate phosphohydrolase / phosphatidate

table_label: PubMed XML abstract PMID 8663293

enzyme: Phospholipid phosphatase 1


substrate_name: sphing-4-enine 1-phosphate (at pH 6.5 and 37 degrees Celsius)

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

raw_value_unit_evidence: Km raw_value=4.0 microM raw_unit=microM

row_label: Rat liver plasma membrane anionic phosphatidate phosphohydrolase / sphingosine 1-phosphate


column_label: Abstract states Km values for phosphatidic acid, lysophosphatidic acid, and N-oleoyl ethanolamine phosphatidic acid were, respectively, PAP-2a: 98, 170, 116 microM.

raw_value_unit_evidence: Km raw_value=116 raw_unit=microM

row_label: human PAP-2a with N-oleoyl ethanolamine phosphatidic acid

table_label: PubMed abstract PMID 9607309


enzyme_display_name: nocturnin

organism: Escherichia coli

substrate_name: NADP+

assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+

column_label: PMC HTML Table 2 row CysQ / NADP+ columns Km (mM), kcat (s^-1), and kcat/Km; table footnote reports means +/- SD for three determinations.

row_label: CysQ / NADP+

table_label: Table 2. Kinetic constants for phosphatase activities

enzyme: nocturnin

substrate: NADP+


substrate_name: NADPH

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

column_label: PMC HTML Table 2 row CysQ / NADPH columns Km (mM), kcat (s^-1), and kcat/Km; table footnote reports means +/- SD for three determinations.

row_label: CysQ / NADPH

substrate: NADPH


enzyme_display_name: aryldialkylphosphatase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H115W to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature H115W/R192K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature H115W/R192Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: 4'-phosphooxetanocin A phosphatase

organism: Priestia megaterium

substrate_name: oxetanocin A diphosphate

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

column_label: Table 1 (Summary of kinetic parameters for OxsA with OXT- and deoxyribonucleotide compounds) prints one label column, 'Tested substrate', followed by four numeric columns whose heads are 'KM (uM)', 'Vmax x 10^-3 (U/mg)', 'kcat x 10^-3 (s^-1)' and 'kcat/KM (M^-1 s^-1)' in that printed order; the Vmax and kcat heads carry a shared power-of-ten column scale that belongs to every cell of those two columns. The cited cell set is Table 1, tested substrate row OXT-PP: KM (uM) = 13; Vmax x 10^-3 (U/mg) = 7.8; kcat x 10^-3 (s^-1) = 2.9; kcat/KM (M^-1 s^-1) = 221. The printed uncertainties of that row are KM 13 +/- 3, Vmax 7.8 +/- 0.46, kcat 2.9 +/- 0.17 and kcat/KM 221 +/- 47. The table footnote reads 'See SI Materials and Methods for experimental details.' and '*U/mg = umol/min mg of OxsA.'

normalized_value_unit_evidence: KM: printed Table 1 cell 13 uM; 13 / 1000 = 0.013, so the paper value is 0.013 mM; the exported value is 0.013 mM. kcat: printed Table 1 cell 2.9 x 10^-3 s^-1, read under the printed column scale x 10^-3 that the kcat head carries; 2.9 x 10^-3 = 0.0029, and the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so the paper value is 0.0029 s^(-1); the exported value is 0.0029 s^(-1). kcat/KM: printed Table 1 cell 221 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 221 / 1000 = 0.221 s^(-1)*mM^(-1); the exported value is 0.22307692307692306 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, tested substrate row 'OXT-PP': KM = 13 uM; kcat = 2.9 x 10^-3 s^-1; printed kcat/KM = 221 M^-1 s^-1; Vmax = 7.8 x 10^-3 U/mg.

row_label: Table 1, tested substrate row OXT-PP

table_label: Table 1: Summary of kinetic parameters for OxsA with OXT- and deoxyribonucleotide compounds (PNAS 2016, 113(48):13750-13755)

enzyme: 4'-phosphooxetanocin A phosphatase

substrate: oxetanocin A diphosphate


substrate_name: oxetanocin A triphosphate

column_label: Table 1 (Summary of kinetic parameters for OxsA with OXT- and deoxyribonucleotide compounds) prints one label column, 'Tested substrate', followed by four numeric columns whose heads are 'KM (uM)', 'Vmax x 10^-3 (U/mg)', 'kcat x 10^-3 (s^-1)' and 'kcat/KM (M^-1 s^-1)' in that printed order; the Vmax and kcat heads carry a shared power-of-ten column scale that belongs to every cell of those two columns. The cited cell set is Table 1, tested substrate row OXT-PPP: KM (uM) = 8; Vmax x 10^-3 (U/mg) = 12; kcat x 10^-3 (s^-1) = 4.5; kcat/KM (M^-1 s^-1) = 525. The printed uncertainties of that row are KM 8 +/- 2, Vmax 12 +/- 0.86, kcat 4.5 +/- 0.33 and kcat/KM 525 +/- 121. The table footnote reads 'See SI Materials and Methods for experimental details.' and '*U/mg = umol/min mg of OxsA.'

normalized_value_unit_evidence: KM: printed Table 1 cell 8 uM; 8 / 1000 = 0.008, so the paper value is 0.008 mM; the exported value is 0.008 mM. kcat: printed Table 1 cell 4.5 x 10^-3 s^-1, read under the printed column scale x 10^-3 that the kcat head carries; 4.5 x 10^-3 = 0.0045, and the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so the paper value is 0.0045 s^(-1); the exported value is 0.0045 s^(-1). kcat/KM: printed Table 1 cell 525 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 525 / 1000 = 0.525 s^(-1)*mM^(-1); the exported value is 0.5625 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, tested substrate row 'OXT-PPP': KM = 8 uM; kcat = 4.5 x 10^-3 s^-1; printed kcat/KM = 525 M^-1 s^-1; Vmax = 12 x 10^-3 U/mg.

row_label: Table 1, tested substrate row OXT-PPP

substrate: oxetanocin A triphosphate


organism: Archaeoglobus fulgidus

assay_conditions_summary: pH 8.5; 358.15 K; cofactor NADP+

column_label: PMC HTML Table 2 row AF2372 / NADP+ columns Km (mM), kcat (s^-1), and kcat/Km; table footnote reports means +/- SD for three determinations.

row_label: AF2372 / NADP+


column_label: PMC HTML Table 2 row AF2372 / NADPH columns Km (mM), kcat (s^-1), and kcat/Km; table footnote reports means +/- SD for three determinations.

row_label: AF2372 / NADPH


column_label: PMC HTML Table 2 row MJ0109 / NADP+ columns Km (mM), kcat (s^-1), and kcat/Km; table footnote reports means +/- SD for three determinations.

row_label: MJ0109 / NADP+


column_label: PMC HTML Table 2 row MJ0109 / NADPH columns Km (mM), kcat (s^-1), and kcat/Km; table footnote reports means +/- SD for three determinations.

row_label: MJ0109 / NADPH


enzyme_display_name: [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial

column_label: Results prose; PDP2 row/segment; Mg2+ apparent Km

normalized_value_unit_evidence: normalized: Km=17.4 mM

raw_value_unit_evidence: paper text: apparent Km value of PDP2 for Mg2+ was 17.4 +/- 2.7 mM with n=5

row_label: PDP2 Mg2+ concentration dependence

table_label: Results prose and Figure 4B


enzyme_display_name: [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial

substrate_name: Mg(2+) (in absence of Ca(2+))

smiles: [Mg]

substrate: Mg(2+) (in absence of Ca(2+))


substrate_name: fructose 6-phosphate

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

substrate: fructose 6-phosphate


substrate_name: ATP

substrate: ATP


organism: Haemophilus influenzae


enzyme_display_name: Multiple inositol polyphosphate phosphatase 1


substrate_name: 1D-myo-inositol hexakisphosphate

enzyme: Multiple inositol polyphosphate phosphatase 1

substrate: 1D-myo-inositol hexakisphosphate


substrate_name: beta-D-fructose 6-phosphate

substrate: beta-D-fructose 6-phosphate


substrate_name: beta-D-fructose 2,6-bisphosphate

substrate: beta-D-fructose 2,6-bisphosphate


organism: Streptomyces coelicolor

substrate_name: 4-nitrophenyl phosphate

substrate: 4-nitrophenyl phosphate


substrate_name: phosphotyrosine

column_label: Abstract states the Km for PY hydrolysis by PtpA is 2.7 mM at pH 6.5 and 37 degrees C.

raw_value_unit_evidence: Km raw_value=2.7 raw_unit=mM

row_label: Streptomyces coelicolor PtpA with phosphotyrosine

table_label: PubMed abstract PMID 8550407

substrate: phosphotyrosine


substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


substrate_name: N-acetylglucosamine-phosphate

substrate: N-acetylglucosamine-phosphate


enzyme_display_name: Nocturnin

assay_conditions_summary: cofactor NADPH

enzyme: Nocturnin


organism: Mus musculus

proof_lines:
mouse LPP-1
phosphatidate
lysophosphatidate


organism: Lupinus luteus

column_label: Abstract substrate list reports AppppA (V = 1, Km = 2.0 microM).

raw_value_unit_evidence: Km raw_value=2.0 raw_unit=microM

row_label: Lupinus luteus phosphodiesterase with AppppA

table_label: PubMed abstract PMID 6309793

enzyme: phosphodiesterase I


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

column_label: Abstract substrate list reports NAD (V = 0.8, Km = 9.6 microM).

raw_value_unit_evidence: Km raw_value=9.6 raw_unit=microM

row_label: Lupinus luteus phosphodiesterase with NAD

substrate: NAD+


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: fructose 2,6-bisphosphate

substrate: fructose 2,6-bisphosphate


enzyme_display_name: Dual specificity phosphatase Cdc25

organism: Arabidopsis thaliana

substrate_name: para-nitrophenyl phosphate

enzyme: Dual specificity phosphatase Cdc25

substrate: para-nitrophenyl phosphate


substrate_name: 4-Nitrophenyl phosphate

substrate: 4-Nitrophenyl phosphate


enzyme_display_name: fructose-2,6-bisphosphate 2-phosphatase

organism: Spinacia oleracea

enzyme: fructose-2,6-bisphosphate 2-phosphatase


enzyme_display_name: Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and protein-tyrosine-phosphatase PTEN2A

substrate_name: p-NPP

substrate: p-NPP


substrate_name: beta-D-Fructose 2,6-bisphosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E325A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: beta-D-Fructose 2,6-bisphosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T2K with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


organism: Bacillus subtilis


enzyme_display_name: Dual specificity protein phosphatase 13A

substrate_name: p-nitrophenol phosphate (at pH 6.0)

assay_conditions_summary: pH 6

substrate: p-nitrophenol phosphate (at pH 6.0)


proof_lines: PTP1B vanadate DADEYL


enzyme_display_name: UniProt P17706

source_db: skid

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

source_databases_merged: skid uniprot

enzyme: UniProt P17706

source: skid


enzyme_display_name: Dual specificity protein phosphatase 7

substrate_name: p-nitrophenyl phosphate

enzyme: Dual specificity protein phosphatase 7

substrate: p-nitrophenyl phosphate


enzyme_display_name: ribulose-1,5-bisphosphate 5-phosphatase

organism: Halopiger xanaduensis

source_databases_merged: brenda uniprot

enzyme: ribulose-1,5-bisphosphate 5-phosphatase


enzyme_display_name: Receptor-type tyrosine-protein phosphatase epsilon

substrate_name: fluorescein diphosphate (isoform 1)

substrate: fluorescein diphosphate (isoform 1)


enzyme_display_name: Tyrosine-protein phosphatase CDC14

enzyme: Tyrosine-protein phosphatase CDC14


enzyme_display_name: Glutaredoxin arsenate reductase

organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)

column_label: PMID 14617642 Table 1, Synechocystis rSlr0946 (rSynArsC) row, Km (mM) column = 77. The assay prose identifies pNPP as substrate and states pNPP was varied from 10 to 250 mM.

normalized_value_unit_evidence: Km 77 mM exactly matches expected 77.0 mM.

raw_value_unit_evidence: Table 1 reports Synechocystis rSlr0946 (rSynArsC) Km (mM) = 77 for phosphohydrolase activity; assay prose states pNPP was the substrate.

row_label: Arsenate reductases / Synechocystis rSlr0946 (rSynArsC)

table_label: Table 1. Comparison of the phosphohydrolase activity of the recombinant protein product of ORF slr0946, rSlr0946, with other detoxifying arsenate reductases and several bacterial LMW PTPs

enzyme: Glutaredoxin arsenate reductase


enzyme_display_name: Tyrosine-protein phosphatase non-receptor type 11

substrate_name: pNPP (isoform 1)

substrate: pNPP (isoform 1)


enzyme_display_name: Dual specificity protein phosphatase OPG106

organism: Vaccinia virus (strain Western Reserve)

substrate_name: 3-O-methylfluorescein phosphate

proof_lines:
VH1
3-O-methylfluorescein phosphate
Vaccinia virus

substrate: 3-O-methylfluorescein phosphate


enzyme_display_name: protein-tyrosine-phosphatase

organism: Thermus thermophilus


organism: Gallus gallus

substrate_name: inositol hexakisphosphate

substrate: inositol hexakisphosphate


organism: Homo sapiens

substrate_name: 1D-myo-inositol hexakisphosphate

substrate: 1D-myo-inositol hexakisphosphate


substrate_name: inositol 1,3-bisphosphate (at pH 6 and in presence of MTMR9)


organism: Variola virus (isolate Human/India/Ind3/1967)

enzyme: Dual specificity protein phosphatase OPG106


substrate_name: glycerophosphoinositol

substrate: glycerophosphoinositol


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


enzyme_display_name: Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

assay_conditions_summary: pH 9

column_label: Article results prose states purified recombinant mENPP3 hydrolyzes cGAMP with KM = 76.5 +/- 18.7 uM at pH 9.0 in Figure 2C.

row_label: purified recombinant mouse ENPP3 hydrolyzing cGAMP

table_label: Results prose, Figure 2C


enzyme_display_name: aryldialkylphosphatase

substrate_name: diethyl-paraoxon

enzyme: aryldialkylphosphatase

substrate: diethyl-paraoxon


organism: Bos taurus

substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


organism: Vulcanisaeta moutnovskia

substrate_name: methyl paraoxon

substrate: methyl paraoxon


enzyme_display_name: Aryldialkylphosphatase

organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

substrate_name: paraoxon (at pH 8.0)

enzyme: Aryldialkylphosphatase

substrate: paraoxon (at pH 8.0)


organism: Saccharolobus solfataricus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C258L/I261F/W263A to reconstruct the assayed variant sequence.


substrate_name: ethyl-paraoxon

assay_conditions_summary: pH 8; 343.15 K; buffer activity/lactonase

column_label: Table 2; row ethyl-paraoxon (I); columns kcat (s^-1), KM (uM), kcat/KM (M^-1 s^-1)

row_label: ethyl-paraoxon (I)

table_label: Table 2. Enzymatic characterisation of VmoLac enzyme

substrate: ethyl-paraoxon


enzyme_display_name: Transferred entry: 3.8.2.2

organism: Loligo vulgaris

substrate_name: Diisopropyl fluorophosphate

enzyme: Transferred entry: 3.8.2.2

substrate: Diisopropyl fluorophosphate


substrate_name: diisopropyl fluorophosphate

substrate: diisopropyl fluorophosphate


organism: Brevundimonas diminuta

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


proof_lines: pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F/S308L


proof_lines: pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N


proof_lines: pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N


proof_lines: pH 9.0, 30°C, recombinant mutant H254Q/H257F


proof_lines: pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F


proof_lines: pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F/S308L


proof_lines: pH 9.0, 30°C, recombinant mutant I106C/F132V/H254Q/H257F/S308L


proof_lines: pH 9.0, 30°C, recombinant mutant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N/S308L


proof_lines: pH 9.0, 30°C, recombinant mutant F132V/H254Q/H257F


proof_lines: pH 9.0, 30°C, recombinant mutant A80V/F132V/K185R/H254Q/H257Y/I274N/S308L


proof_lines: pH 9.0, 30°C, recombinant mutant A80V/I106C/F132V/K185R/H254Q/H257Y/I274N/S308L


proof_lines: pH 9.0, 30°C, recombinant mutant I106G/F132V/H254Q/H257F


proof_lines: pH 9.0, 30°C, recombinant mutant A80V/I106G/F132V/K185R/H254Q/H257Y/I274N