substrate_name: D-glucose 1-phosphate

substrate: D-glucose 1-phosphate


enzyme_display_name: phosphoenolpyruvate phosphatase

organism: Brassica nigra

substrate_name: ATP

source_db: brenda

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 5.6; 298.15 K; cofactor ATP

enzyme: phosphoenolpyruvate phosphatase

substrate: ATP

status: unverified

source: brenda


substrate_name: 2,3 diphosphoglycerate

substrate: 2,3 diphosphoglycerate


substrate_name: 4-nitrophenyl phosphate

substrate: 4-nitrophenyl phosphate


substrate_name: D-gluconate 6-phosphate

substrate: D-gluconate 6-phosphate


substrate_name: ADP

assay_conditions_summary: pH 5.6; 298.15 K; cofactor ADP

substrate: ADP


substrate_name: phytic acid

substrate: phytic acid


substrate_name: D-glucose 6-phosphate

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

substrate: D-glucose 6-phosphate


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Brassica rapa subsp. oleifera

substrate_name: phosphoenolpyruvate

substrate: phosphoenolpyruvate


enzyme_display_name: alkylacetylglycerophosphatase

organism: Tetrahymena pyriformis

smiles: CC(=O)OC(CO)COP(=O)(O)O

proof_lines: pH 7.0, 37°C, mitochondrial and microsomal fractions

enzyme: alkylacetylglycerophosphatase


enzyme_display_name: sugar-terminal-phosphatase

organism: Thermotoga maritima

substrate_name: erythrose 4-phosphate

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

enzyme: sugar-terminal-phosphatase

substrate: erythrose 4-phosphate


substrate_name: fructose 6-phosphate

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

substrate: fructose 6-phosphate


enzyme_display_name: Triple specificity protein phosphatase PtpB

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: P-Ser

source_db: uniprot

verification_status: verified

protein_accession_database: UniProt

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

assay_conditions_summary: pH 6

column_label: Official PMC article HTML Table 1, row P-Ser, Km column reports 0.44 mM with reported SEM 0.08. Local HTML line refs: PMC1948985_pmc_article.html lines 1449-1473.

normalized_value_unit_evidence: Paper Table 1 P-Ser Km mean is 0.44 mM, matching the export Km 0.44 mM.

raw_value_unit_evidence: Table 1 row P-Ser reports Km 0.44 +/- 0.08 mM.

row_label: P-Ser

table_label: Table 1. Kinetic parameters of MptpB towards different phosphorylated substrates

data_origin: experimental

substrate: P-Ser

status: verified

source: uniprot


substrate_name: pNPP

proof_lines: kcat is 60.0 sec(-1) with P-Tyr as substrate. kcat is 18.32 sec(-1) with P-Ser as substrate. kcat is 12.5 sec(-1) with P-Thr as substrate. kcat is 159.57 sec(-1) with P-Tyr insulin as substrate. kcat is 158.31 sec(-1) with P-Tyr EGFR as sub

enzyme: Triple specificity protein phosphatase PtpB

substrate: pNPP


enzyme_display_name: Low molecular weight protein-tyrosine phosphatase A

substrate_name: phosphotyrosine

assay_conditions_summary: pH 5

proof_lines: kcat is 12.6 sec(-1) with pNPP as substrate at pH 5.0. kcat is 1313 sec(-1) with pNPP as substrate at pH 6.0. kcat is 1334 sec(-1) with pNPP as substrate at pH 7.0 (PubMed:17975835). kcat is 13.73 sec(-1) with pNPP as substrate. kcat is 6.7

substrate: phosphotyrosine


enzyme_display_name: Phosphatase/phosphodiesterase DR_1281

organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

substrate_name: PEP (at pH 6.5)

column_label: Table III row PEP under columns pH 6.5 and Km (mM): 0.36 +/- 0.07.

row_label: PEP

table_label: Table III

enzyme: Phosphatase/phosphodiesterase DR_1281

substrate: PEP (at pH 6.5)


column_label: Table III row 2',3'-cAMP under columns pH 6.5 and Km (mM): 0.55 +/- 0.05.


column_label: Table III row 2',3'-cCMP under columns pH 6.5 and Km (mM): 0.87 +/- 0.11.


column_label: Table III row 2',3'-cGMP under columns pH 6.5 and Km (mM): 1.28 +/- 0.12.


substrate_name: pNPP (at pH 8.5)

column_label: Table III row pNPP under columns pH 8.5 and Km (mM): 0.08 +/- 0.006.

row_label: pNPP

substrate: pNPP (at pH 8.5)


substrate_name: pNP-TMP (at pH 8.5)

proof_lines: kcat is 0.18 sec(-1) with PEP as substrate. kcat is 0.38 sec(-1) with 2',3'-cAMP as substrate. kcat is 0.32 sec(-1) with 2',3'-cCMP as substrate. kcat is 0.42 sec(-1) with 2',3'-cGMP as substrate. kcat is 0.20 sec(-1) with pNPP as substrate

substrate: pNP-TMP (at pH 8.5)


enzyme_display_name: Dual specificity protein phosphatase TpbA

organism: Pseudomonas aeruginosa (strain UCBPP-PA14)

proof_lines: kcat is 0.00162 sec(-1) with pNPP as substrate.


enzyme_display_name: protein-tyrosine-phosphatase

organism: Shewanella sp.

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H44N with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

mutation_type: substitution

enzyme: protein-tyrosine-phosphatase


organism: Homo sapiens

substrate_name: p-nitrophenyl phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T36E with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7

substrate: p-nitrophenyl phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L29A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S35E with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F28A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C129S with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


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

proof_lines: kcat is 0.0076 sec(-1) with pNPP as substrate.

enzyme: Dual specificity protein phosphatase TpbA


organism: Rattus norvegicus

substrate_name: [Pyruvate dehydrogenase (lipoamide)] phosphate; H2O

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


organism: Escherichia coli


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

organism: Arabidopsis thaliana

substrate_name: fructose-2,6-bisphosphate for the fructose-2,6-bisphosphatase activity (at pH 6.0 and 25 degrees Celsius)

sequence_source: multiple

source_databases_merged: brenda uniprot

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


organism: Bos taurus

substrate_name: beta-D-Fructose 2,6-bisphosphate; H2O

substrate: beta-D-Fructose 2,6-bisphosphate; H2O


organism: Gallus gallus

substrate_name: D-Fructose 2,6-bisphosphate; H2O

substrate: D-Fructose 2,6-bisphosphate; H2O


substrate_name: H2O; D-Fructose 2,6-bisphosphate

substrate: H2O; D-Fructose 2,6-bisphosphate


substrate_name: 4-Nitrophenyl phosphate; H2O

substrate: 4-Nitrophenyl phosphate; H2O


substrate_name: H2O; 4-Nitrophenyl phosphate

substrate: H2O; 4-Nitrophenyl phosphate


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


substrate_name: Protein tyrosine phosphate; H2O

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

substrate: Protein tyrosine phosphate; H2O


organism: Mus musculus

column_label: PMID 16797546 Results section and Fig. 1a, Eya1(ED) hydrolysis of pNPP: kcat = 56 s^-1 and Km = 1.8 mM.

raw_value_unit_evidence: Results prose reports kcat = 56 s^-1 and Km = 1.8 mM for Eya1(ED) toward pNPP.

row_label: mouse Eya1(ED) / pNPP

table_label: Results prose plus Fig. 1a


enzyme_display_name: Dual specificity phosphatase 21

substrate_name: a peptide

enzyme: Dual specificity phosphatase 21

substrate: a peptide


substrate_name: H2O; Fluorescein diphosphate

substrate: H2O; Fluorescein diphosphate


enzyme_display_name: Tyrosine-protein phosphatase non-receptor type 11

substrate_name: nAChR (isoform 1)

substrate: nAChR (isoform 1)


organism: Staphylococcus aureus


enzyme_display_name: UniProt Q7WG29

organism: Bordetella bronchiseptica

substrate_name: D-fructose 1,6-bisphosphate

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q7WG29

substrate: D-fructose 1,6-bisphosphate

source: skid


enzyme_display_name: Type II inositol polyphosphate 5-phosphatase 15

substrate_name: PtdIns(4,5)P2 (at pH 7.0 and 22 degrees Celsius)


organism: Bacillus subtilis

substrate_name: Proteine tyrosine phosphate; H2O

substrate: Proteine tyrosine phosphate; H2O


substrate_name: H2O; Proteine tyrosine phosphate

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

substrate: H2O; Proteine tyrosine phosphate


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


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature R47N/D48N with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

proof_lines: isoform PTP1B, mutant R47N/D48N, pH 7.0, 25°C

substrate: Unknown


substrate_name: difluoromethylumbelliferyl phosphate

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature S295F with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

substrate: difluoromethylumbelliferyl phosphate


enzyme_display_name: Dual specificity phosphatase 29

substrate_name: para-nitrophenylphosphate (at pH 5.5)

proof_lines: kcat is 0.330 sec(-1) for para-nitrophenylphosphate.

enzyme: Dual specificity phosphatase 29

substrate: para-nitrophenylphosphate (at pH 5.5)


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature R362K with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

proof_lines: Ki value for inhibition of mutant Shp2 R362K


enzyme_display_name: Glycerol-3-phosphate phosphatase

proof_lines: Given the respective intracellular concentrations of glycerol-3-phosphate and 2-phosphoglycolate, glycerol-3-phosphate with a concentration of 2 to 10 mM is most probably the physiological substrate.

enzyme: Glycerol-3-phosphate phosphatase


substrate_name: 4-nitrophenyl phosphate

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature S19A with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant S19A, pH and temperature not specified in the publication

substrate: 4-nitrophenyl phosphate


enzyme_display_name: UniProt Q9H0P0

enzyme: UniProt Q9H0P0


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


enzyme_display_name: Ecdysteroid-phosphate phosphatase

organism: Bombyx mori

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -1, so it is treated as a source-provided variant sequence.

proof_lines: kcat is 0.94 sec(-1) for E22P. kcat is 14.57 sec(-1) for 20E22P. kcat is 3.53 sec(-1) for 2dE22P. kcat is 0.14 sec(-1) for 22d20E3P.

enzyme: Ecdysteroid-phosphate phosphatase


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature R47V/D48N with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature F182H with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, isoform PTP1B, mutant F182H


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature D48N with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: isoform PTP1B, mutant D48N, pH 7.0, 25°C


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature S19E with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant S19E, pH and temperature not specified in the publication


substrate_name: PLQR(pY)SEDP

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature S39E with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant S39E, pH and temperature not specified in the publication

substrate: PLQR(pY)SEDP


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


substrate_name: beta-D-Fructose 2,6-bisphosphate; H2O

substrate: beta-D-Fructose 2,6-bisphosphate; H2O


substrate_name: H2O; beta-D-Fructose 2,6-bisphosphate

substrate: H2O; beta-D-Fructose 2,6-bisphosphate


substrate_name: H2O; D-Fructose 2,6-bisphosphate

kcat_over_km_origin: calculated

substrate: H2O; D-Fructose 2,6-bisphosphate


organism: Spinacia oleracea

substrate_name: D-Fructose 2,6-bisphosphate; H2O

substrate: D-Fructose 2,6-bisphosphate; H2O


substrate_name: H2O; 4-Nitrophenyl phosphate

substrate: H2O; 4-Nitrophenyl phosphate


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Saccharomyces cerevisiae


enzyme_display_name: Glutaredoxin arsenate reductase

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

enzyme: Glutaredoxin arsenate reductase


enzyme_display_name: Phosphoenolpyruvate phosphatase

organism: Allium cepa

enzyme: Phosphoenolpyruvate phosphatase


organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

substrate_name: bis-pNPP (at pH 8.5)

substrate: bis-pNPP (at pH 8.5)


enzyme_display_name: Multiple inositol polyphosphate phosphatase 1


organism: Triticum aestivum


enzyme_display_name: Magnesium-dependent phosphatase 1

proof_lines: Dephosphorylates ribose-5-phosphate, 2-deoxy-ribose-5-phosphate, phosphotyrosine, arabinose-5-phosphate, fructose-6-phosphate, 5'-CMP, pNPP, 5'-AMP and glucose-6-phosphate with a decreasing relative rate of 1, 0.9, 0.8, 0.6, 0.5, 0.2, 0.2,

enzyme: Magnesium-dependent phosphatase 1


proof_lines: kcat is 0.1 sec(-1) with glycerol-3-phosphate.


substrate_name: H2O; Fluorescein diphosphate


enzyme_display_name: Low molecular weight protein-tyrosine phosphatase A

substrate_name: free O-phosphotyrosine

substrate: free O-phosphotyrosine


enzyme_display_name: Triple specificity protein phosphatase PtpB

substrate_name: P-tyr

proof_lines: kcat is 60.0 sec(-1) with P-Tyr as substrate. kcat is 18.32 sec(-1) with P-Ser as substrate. kcat is 12.5 sec(-1) with P-Thr as substrate. kcat is 159.57 sec(-1) with P-Tyr insulin as substrate. kcat is 158.31 sec(-1) with P-Tyr EGFR as sub

substrate: P-tyr


organism: Rattus norvegicus


enzyme_display_name: UniProt P34913

organism: Homo sapiens

substrate_name: 1-myristoyl-sn-glycerol 3-phosphate

smiles: CCCCCCCCCCCCCC(=O)OCC(COP(=O)(O)O)O

enzyme: UniProt P34913

substrate: 1-myristoyl-sn-glycerol 3-phosphate


enzyme_display_name: UniProt O30298

organism: Archaeoglobus fulgidus

substrate_name: NADP+

enzyme: UniProt O30298

substrate: NADP+


substrate_name: NADPH

substrate: NADPH


enzyme_display_name: UniProt Q57573

organism: Methanocaldococcus jannaschii

enzyme: UniProt Q57573


enzyme_display_name: Low molecular weight protein-tyrosine-phosphatase PtpB

substrate_name: p-nitrophenyl-phosphate (at pH 6.2 and 37 degrees Celsius)


enzyme_display_name: Low molecular weight protein-tyrosine-phosphatase PtpA

substrate: p-nitrophenyl-phosphate (at pH 6.2 and 37 degrees Celsius)


enzyme_display_name: protein-tyrosine-phosphatase

organism: Vaccinia virus


organism: Variola virus

substrate_name: 4-Nitrophenyl phosphate; H2O

substrate: 4-Nitrophenyl phosphate; H2O


organism: Yersinia enterocolitica


organism: Gallus gallus

substrate_name: myo-Inositol hexakisphosphate; H2O

substrate: myo-Inositol hexakisphosphate; H2O


enzyme_display_name: phosphodiesterase I

organism: Acetivibrio thermocellus

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

proof_lines: pH 8.0, 45°C, mutant H264Q, presence of Ni2+

proof_lines: pH 8.0, 45°C, mutant H264Q, presence of Mn2+

enzyme: phosphodiesterase I


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

proof_lines: pH 8.0, 45°C, wild-type, presence of Ni2+

proof_lines: pH 8.0, 45°C, wild-type, presence of Mn2+


proof_lines: pH 8.0, 45°C, mutant H376D, presence of Mn2+


proof_lines: pH 8.0, 45°C, mutant D236A, presence of Ni2+

proof_lines: pH 8.0, 45°C, mutant D236A, presence of Mn2+


proof_lines: pH 8.0, 45°C, mutant H189D, presence of Mn2+


proof_lines: pH 8.0, 45°C, mutant H189Q, presence of Mn2+


proof_lines: pH 8.0, 45°C, mutant R237K, presence of Ni2+


proof_lines: pH 8.0, 45°C, mutant H189A, presence of Mn2+


proof_lines: pH 8.0, 45°C, mutant D392E, presence of Mn2+


proof_lines: pH 8.0, 45°C, mutant D236N, presence of Ni2+

proof_lines: pH 8.0, 45°C, mutant D236N, presence of Mn2+


proof_lines: pH 8.0, 45°C, mutant H264N, presence of Ni2+


proof_lines: pH 8.0, 45°C, mutant D392N, presence of Mn2+


proof_lines: pH 8.0, 45°C, mutant H264A, presence of Ni2+


proof_lines: pH 8.0, 45°C, mutant R237A, presence of Ni2+


proof_lines: pH 8.0, 45°C, mutant R237Q, presence of Ni2+


proof_lines: pH 8.0, 45°C, mutant H376N, presence of Mn2+


proof_lines: pH 8.0, 45°C, mutant H264D, presence of Mn2+


proof_lines: pH 8.0, 45°C, mutant H189E, presence of Mn2+


substrate_name: 4-Nitrophenyl phosphate

source_db: oed

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D50N with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

substrate: 4-Nitrophenyl phosphate

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E168Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E171Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E174Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E308Q to reconstruct the assayed variant sequence.


verification_status: corrected

column_label: Table I. Kinetic parameters of Cdc14-catalyzed hydrolysis of small molecule aryl phosphate substrates; row pNPP / 4-Nitrophenyl phosphate; kcat column raw 4.5 s^-1 normalized 4.5 s^-1; Km column raw 10.6 mM normalized 10.6 mM; kcat/Km column raw 424 M^-1 s^-1 normalized 0.424 s^-1 mM^-1

row_label: pNPP / 4-Nitrophenyl phosphate

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D129N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D143N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D177N with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D253A to reconstruct the assayed variant sequence.


substrate_name: 2-Chloro-4-nitrophenyl phosphate

column_label: Table I. Kinetic parameters of Cdc14-catalyzed hydrolysis of small molecule aryl phosphate substrates; row 2-Cl-4-NO2 / 2-Chloro-4-nitrophenyl phosphate; kcat column raw 3.09 s^-1 normalized 3.09 s^-1; Km column raw 0.4 mM normalized 0.4 mM; kcat/Km column raw 7725 M^-1 s^-1 normalized 7.725 s^-1 mM^-1

substrate: 2-Chloro-4-nitrophenyl phosphate


substrate_name: 3-O-Methylfluorescein phosphate

column_label: Table I. Kinetic parameters of Cdc14-catalyzed hydrolysis of small molecule aryl phosphate substrates; row OMFP / 3-O-Methylfluorescein phosphate; kcat column raw 3.4 s^-1 normalized 3.4 s^-1; Km column raw 1.0 mM normalized 1.0 mM; kcat/Km column raw 3400 M^-1 s^-1 normalized 3.4 s^-1 mM^-1

row_label: OMFP / 3-O-Methylfluorescein phosphate

substrate: 3-O-Methylfluorescein phosphate


substrate_name: 4-Chlorophenyl phosphate

column_label: Table I. Kinetic parameters of Cdc14-catalyzed hydrolysis of small molecule aryl phosphate substrates; row 4-Cl / 4-Chlorophenyl phosphate; kcat column raw 4.2 s^-1 normalized 4.2 s^-1; Km column raw 11.1 mM normalized 11.1 mM; kcat/Km column raw 376 M^-1 s^-1 normalized 0.376 s^-1 mM^-1

row_label: 4-Cl / 4-Chlorophenyl phosphate

substrate: 4-Chlorophenyl phosphate


substrate_name: 4-Cyanophenyl phosphate

column_label: Table I. Kinetic parameters of Cdc14-catalyzed hydrolysis of small molecule aryl phosphate substrates; row 4-CN / 4-Cyanophenyl phosphate; kcat column raw 3.35 s^-1 normalized 3.35 s^-1; Km column raw 10.8 mM normalized 10.8 mM; kcat/Km column raw 311 M^-1 s^-1 normalized 0.311 s^-1 mM^-1

row_label: 4-CN / 4-Cyanophenyl phosphate

substrate: 4-Cyanophenyl phosphate


substrate_name: 4-Methylumbelliferyl phosphate

column_label: Table I. Kinetic parameters of Cdc14-catalyzed hydrolysis of small molecule aryl phosphate substrates; row MUP / 4-Methylumbelliferyl phosphate; kcat column raw 7.0 s^-1 normalized 7.0 s^-1; Km column raw 2.1 mM normalized 2.1 mM; kcat/Km column raw 3305 M^-1 s^-1 normalized 3.305 s^-1 mM^-1

row_label: MUP / 4-Methylumbelliferyl phosphate

substrate: 4-Methylumbelliferyl phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D253N to reconstruct the assayed variant sequence.


column_label: Table I. Kinetic parameters of Cdc14-catalyzed hydrolysis of small molecule aryl phosphate substrates; row DiFMUP / 6,8-Difluoro-4-methylumbelliferyl phosphate; kcat column raw 8.1 s^-1 normalized 8.1 s^-1; Km column raw 10.5 uM normalized 0.0105 mM; kcat/Km column raw 771000 M^-1 s^-1 normalized 771.0 s^-1 mM^-1


substrate_name: beta-Naphthyl phosphate

column_label: Table I. Kinetic parameters of Cdc14-catalyzed hydrolysis of small molecule aryl phosphate substrates; row beta-Naph / beta-Naphthyl phosphate; kcat column raw 4.2 s^-1 normalized 4.2 s^-1; Km column raw 2.0 mM normalized 2.0 mM; kcat/Km column raw 2000 M^-1 s^-1 normalized 2.0 s^-1 mM^-1

row_label: beta-Naph / beta-Naphthyl phosphate

substrate: beta-Naphthyl phosphate


substrate_name: Phenyl phosphate

substrate: Phenyl phosphate


organism: Rhizobium leguminosarum

substrate_name: p-nitrophenyl ethyl phosphate

proof_lines: mutant enzyme C57A, at 30°C, in 44 mM succinic acid, 33 mM imidazole, 33 mM diethanolamine, pH 7.5

substrate: p-nitrophenyl ethyl phosphate


substrate_name: p-Nitrophenyl phenylphosphonate

substrate: p-Nitrophenyl phenylphosphonate


proof_lines: kcat below 0.17 sec-1, mutant enzyme Y105A, at 30°C, in 44 mM succinic acid, 33 mM imidazole, 33 mM diethanolamine, pH 7.5

proof_lines: Km above 70 mM, mutant enzyme Y105A, at 30°C, in 44 mM succinic acid, 33 mM imidazole, 33 mM diethanolamine, pH 7.5


proof_lines: mutant enzyme H218A, at 30°C, in 44 mM succinic acid, 33 mM imidazole, 33 mM diethanolamine, pH 7.5


proof_lines: mutant enzyme T107A, at 30°C, in 44 mM succinic acid, 33 mM imidazole, 33 mM diethanolamine, pH 7.5


proof_lines: mutant enzyme N78A, at 30°C, in 44 mM succinic acid, 33 mM imidazole, 33 mM diethanolamine, pH 7.5


proof_lines: mutant enzyme C57S, at 30°C, in 44 mM succinic acid, 33 mM imidazole, 33 mM diethanolamine, pH 7.5


proof_lines: mutant enzyme Y105A, at 30°C, in 44 mM succinic acid, 33 mM imidazole, 33 mM diethanolamine, pH 7.5


proof_lines: mutant enzyme K337A, at 30°C, in 44 mM succinic acid, 33 mM imidazole, 33 mM diethanolamine, pH 7.5


proof_lines: wild type enzyme, at 30°C, in 44 mM succinic acid, 33 mM imidazole, 33 mM diethanolamine, pH 7.5


proof_lines: mutant enzyme Q13A, at 30°C, in 44 mM succinic acid, 33 mM imidazole, 33 mM diethanolamine, pH 7.5


organism: Arabidopsis thaliana

assay_conditions_summary: cofactor FMN


substrate_name: FMN

substrate: FMN


substrate_name: p-Nitrophenylphosphorylcholine

substrate: p-Nitrophenylphosphorylcholine


substrate_name: bis-p-nitrophenyl phosphate

substrate: bis-p-nitrophenyl phosphate


enzyme_display_name: nocturnin

substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

proof_lines: pH and temperature not specified in the publication

enzyme: nocturnin

substrate: NADP+


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


organism: Flammulina velutipes


substrate_name: bis(p-nitrophenyl) phosphate

substrate: bis(p-nitrophenyl) phosphate


organism: Avena sativa

substrate_name: p-nitrophenylthymidine 5'-phosphate

substrate: p-nitrophenylthymidine 5'-phosphate


enzyme_display_name: 2-lysophosphatidate phosphatase

organism: Arachis hypogaea

substrate_name: oleoyl-sn-glycerol 3-phosphate

enzyme: 2-lysophosphatidate phosphatase

substrate: oleoyl-sn-glycerol 3-phosphate


organism: Escherichia coli

proof_lines: pH 8.5, 37°C, presence of 0.5 mM phosphate


organism: Lactobacillus acidophilus

substrate_name: Adenylyl-3',5'-guanosine; H2O

substrate: Adenylyl-3',5'-guanosine; H2O


substrate_name: CpU

substrate: CpU


substrate_name: ApG

substrate: ApG


organism: Beta vulgaris

substrate_name: 4-nitrophenyl uridine 5'-phosphate

substrate: 4-nitrophenyl uridine 5'-phosphate


organism: Xanthomonas axonopodis

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: Ectonucleotide pyrophosphatase/phosphodiesterase family member 1

organism: Homo sapiens

substrate_name: ATP

assay_conditions_summary: cofactor ATP

proof_lines: kcat is 5.51 sec(-1) with ATP as substrate (PubMed:28011303). kcat is 5.65 sec(-1) with AP4A as substrate (PubMed:28011303). kcat is 5.36 sec(-1) with 2',3'-cGAMP as substrate (PubMed:28011303). kcat is 1.96 sec(-1) with UTP as substrate (P

substrate: ATP


enzyme: Ectonucleotide pyrophosphatase/phosphodiesterase family member 1


substrate_name: UTP

substrate: UTP


substrate_name: 3',5'-cyclic AMP

substrate: 3',5'-cyclic AMP


enzyme_display_name: Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

substrate_name: ATP (at pH 7.5 and 37 degrees Celsius)

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: kcat is 1.52 sec(-1) for ATP hydrolysis (at pH 7.5 and 37 degrees Celsius). kcat is 3.37 sec(-1) for GTP hydrolysis (at pH 7.5 and 37 degrees Celsius). kcat is 6.36 sec(-1) for UTP hydrolysis (at pH 7.5 and 37 degrees Celsius). kcat is 9.14

substrate: ATP (at pH 7.5 and 37 degrees Celsius)


substrate_name: UTP (at pH 7.5 and 37 degrees Celsius)

enzyme: Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

substrate: UTP (at pH 7.5 and 37 degrees Celsius)


substrate_name: CTP (at pH 7.5 and 37 degrees Celsius)

substrate: CTP (at pH 7.5 and 37 degrees Celsius)


substrate_name: GTP (at pH 7.5 and 37 degrees Celsius)

substrate: GTP (at pH 7.5 and 37 degrees Celsius)


substrate_name: P(1),P(3)-bis(5'-adenosyl) triphosphate (at pH 8.5 and 37 degrees Celsius)


organism: Mus musculus

proof_lines: kcat is 16 sec(-1) with ATP as substrate. kcat is 200 sec(-1) with UTP as substrate. kcat is 820 sec(-1) with GTP as substrate. kcat is 8.7 sec(-1) with CTP as substrate.


substrate_name: GTP

substrate: GTP


substrate_name: CTP

substrate: CTP


substrate_name: 1-oleoyl-2-lyso-sn-glycerol 3-phosphate

substrate: 1-oleoyl-2-lyso-sn-glycerol 3-phosphate


enzyme_display_name: Phospholipid phosphatase 1

organism: Rattus norvegicus

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

enzyme: Phospholipid phosphatase 1


organism: Archaeoglobus fulgidus

substrate_name: NADP+; H2O

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

substrate: NADP+; H2O


substrate_name: H2O; NADP+

substrate: H2O; NADP+


organism: Methanocaldococcus jannaschii


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H182A with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 9; cofactor ATP


enzyme_display_name: UniProt P09598

organism: Bacillus cereus

enzyme: UniProt P09598


enzyme_display_name: UniProt Q53728

organism: Streptomyces antibioticus

substrate_name: dioleoyl-phosphatidylcholine

enzyme: UniProt Q53728

substrate: dioleoyl-phosphatidylcholine


enzyme_display_name: 4'-phosphooxetanocin A phosphatase

organism: Priestia megaterium

substrate_name: dADP

assay_conditions_summary: pH 8

proof_lines: kcat is 0.0012 sec(-1) with OXT-A-P as substrate. kcat is 0.0029 sec(-1) with OXT-A-PP as substrate. kcat is 0.0045 sec(-1) with OXT-A-PPP as substrate. kcat is 0.0037 sec(-1) with dAMP as substrate. kcat is 0.0026 sec(-1) with dADP as subs

enzyme: 4'-phosphooxetanocin A phosphatase

substrate: dADP


substrate_name: dAMP

substrate: dAMP


substrate_name: dATP

substrate: dATP


organism: Bos taurus

substrate_name: H2O; 4-Nitrophenyl phenyl phosphonate

substrate: H2O; 4-Nitrophenyl phenyl phosphonate


enzyme_display_name: nucleoside-triphosphate diphosphatase

assay_conditions_summary: cofactor ADP

enzyme: nucleoside-triphosphate diphosphatase


organism: Hordeum vulgare

substrate_name: p-nitrophenylthymidine 5'-phosphate

substrate: p-nitrophenylthymidine 5'-phosphate


organism: Lupinus luteus

substrate_name: diadenosine 5',5'''-P1,P3-triphosphate

substrate: diadenosine 5',5'''-P1,P3-triphosphate


substrate_name: H2O; Bis-4-nitrophenyl phosphate

substrate: H2O; Bis-4-nitrophenyl phosphate


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: Diacylglycerol pyrophosphate phosphatase 1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


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

organism: Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6)

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

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


substrate_name: oxetanocin A 5'-phosphate

substrate: oxetanocin A 5'-phosphate


substrate_name: H2O; p-Nitrophenylthymidine phosphate

substrate: H2O; p-Nitrophenylthymidine phosphate


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

substrate_name: D-Fructose 2,6-bisphosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D128A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

column_label: Table II Fru-2,6-Pase row D128A, columns KFru 2,6-P2, Vmax/Et, and V/KFru2,6P2Et; K column normalized from uM to mM, and kcat/Km normalized from the explicit K and Vmax cells with the printed V/K column retained in raw evidence.

normalized_value_unit_evidence: Km 0.00016 mM, kcat 0.017 s^-1, kcat/Km 106.25 s^-1*mM^-1; printed V/K column normalizes to 110 s^-1*mM^-1.

raw_value_unit_evidence: Table II row D128A reports Fru-2,6-Pase KFru 2,6-P2 0.16 uM, Vmax/Et 0.017 s^-1, and printed V/KFru2,6P2Et 110000 M^-1 s^-1; kcat/Km evidence uses 0.017/0.16 uM from the explicit K and Vmax cells.

table_label: Table II: Kinetic constants of rat testis Fru 6-P,2-kinase:Fru-2,6-Pase and the mutant enzymes

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

substrate: D-Fructose 2,6-bisphosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D128E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II Fru-2,6-Pase row D128E, columns KFru 2,6-P2, Vmax/Et, and V/KFru2,6P2Et; K column normalized from uM to mM, and kcat/Km normalized from the explicit K and Vmax cells with the printed V/K column retained in raw evidence.

raw_value_unit_evidence: Table II row D128E reports Fru-2,6-Pase KFru 2,6-P2 0.07 uM, Vmax/Et 0.013 s^-1, and printed V/KFru2,6P2Et 190000 M^-1 s^-1; kcat/Km evidence uses 0.013/0.07 uM from the explicit K and Vmax cells.


sequence_variant_note: Resolved canonical sequence from ncbi_genbank_accession:AAA41163.1 and applied mutation signature D128K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II Fru-2,6-Pase row D128K, columns KFru 2,6-P2, Vmax/Et, and V/KFru2,6P2Et; K column normalized from uM to mM, and kcat/Km normalized from the explicit K and Vmax cells with the printed V/K column retained in raw evidence.

raw_value_unit_evidence: Table II row D128K reports Fru-2,6-Pase KFru 2,6-P2 0.06 uM, Vmax/Et 0.0079 s^-1, and printed V/KFru2,6P2Et 130000 M^-1 s^-1; kcat/Km evidence uses 0.0079/0.06 uM from the explicit K and Vmax cells.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D128N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II Fru-2,6-Pase columns KFru 2,6-P2, Vmax/Et, and V/KFru2,6P2Et; K column normalized from uM to mM and V/K from M^-1 s^-1 to mM^-1 s^-1.

raw_value_unit_evidence: Table II row D128N reports Fru-2,6-Pase KFru 2,6-P2 0.03 uM, Vmax/Et 0.012 s^-1, and V/KFru2,6P2Et 400,000 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from ncbi_genbank_accession:AAA41163.1 and applied mutation signature D128S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II Fru-2,6-Pase row D128S, columns KFru 2,6-P2, Vmax/Et, and V/KFru2,6P2Et; K column normalized from uM to mM, and kcat/Km normalized from the explicit K and Vmax cells with the printed V/K column retained in raw evidence.

normalized_value_unit_evidence: Km 0.00008 mM, kcat 0.017 s^-1, kcat/Km 212.5 s^-1*mM^-1; printed V/K column normalizes to 210 s^-1*mM^-1.

raw_value_unit_evidence: Table II row D128S reports Fru-2,6-Pase KFru 2,6-P2 0.08 uM, Vmax/Et 0.017 s^-1, and printed V/KFru2,6P2Et 210000 M^-1 s^-1; kcat/Km evidence uses 0.017/0.08 uM from the explicit K and Vmax cells.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N73A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II Fru-2,6-Pase row N73A, columns KFru 2,6-P2, Vmax/Et, and V/KFru2,6P2Et; K column normalized from uM to mM, and kcat/Km normalized from the explicit K and Vmax cells with the printed V/K column retained in raw evidence.

raw_value_unit_evidence: Table II row N73A reports Fru-2,6-Pase KFru 2,6-P2 0.12 uM, Vmax/Et 0.028 s^-1, and printed V/KFru2,6P2Et 230000 M^-1 s^-1; kcat/Km evidence uses 0.028/0.12 uM from the explicit K and Vmax cells.


sequence_variant_note: Resolved canonical sequence from ncbi_genbank_accession:AAA41163.1 and applied mutation signature N73D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II Fru-2,6-Pase row N73D, columns KFru 2,6-P2, Vmax/Et, and V/KFru2,6P2Et; K column normalized from uM to mM, and kcat/Km normalized from the explicit K and Vmax cells with the printed V/K column retained in raw evidence.

raw_value_unit_evidence: Table II row N73D reports Fru-2,6-Pase KFru 2,6-P2 0.04 uM, Vmax/Et 0.011 s^-1, and printed V/KFru2,6P2Et 280000 M^-1 s^-1; kcat/Km evidence uses 0.011/0.04 uM from the explicit K and Vmax cells.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T130A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

raw_value_unit_evidence: Table II row T130A reports Fru-2,6-Pase KFru 2,6-P2 0.06 uM, Vmax/Et 0.027 s^-1, and V/KFru2,6P2Et 450,000 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from ncbi_genbank_accession:AAA41163.1 and applied mutation signature T130S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II Fru-2,6-Pase row T130S, columns KFru 2,6-P2, Vmax/Et, and V/KFru2,6P2Et; K column normalized from uM to mM, and kcat/Km normalized from the explicit K and Vmax cells with the printed V/K column retained in raw evidence.

raw_value_unit_evidence: Table II row T130S reports Fru-2,6-Pase KFru 2,6-P2 0.07 uM, Vmax/Et 0.044 s^-1, and printed V/KFru2,6P2Et 630000 M^-1 s^-1; kcat/Km evidence uses 0.044/0.07 uM from the explicit K and Vmax cells.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T130V with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II Fru-2,6-Pase row T130V, columns KFru 2,6-P2, Vmax/Et, and V/KFru2,6P2Et; K column normalized from uM to mM, and kcat/Km normalized from the explicit K and Vmax cells with the printed V/K column retained in raw evidence.

raw_value_unit_evidence: Table II row T130V reports Fru-2,6-Pase KFru 2,6-P2 0.07 uM, Vmax/Et 0.039 s^-1, and printed V/KFru2,6P2Et 560000 M^-1 s^-1; kcat/Km evidence uses 0.039/0.07 uM from the explicit K and Vmax cells.


sequence_variant_note: Resolved canonical sequence from ncbi_genbank_accession:AAA41163.1 and applied mutation signature T52A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II Fru-2,6-Pase row T52A, columns KFru 2,6-P2, Vmax/Et, and V/KFru2,6P2Et; K column normalized from uM to mM, and kcat/Km normalized from the explicit K and Vmax cells with the printed V/K column retained in raw evidence.

raw_value_unit_evidence: Table II row T52A reports Fru-2,6-Pase KFru 2,6-P2 0.08 uM, Vmax/Et 0.036 s^-1, and printed V/KFru2,6P2Et 450000 M^-1 s^-1; kcat/Km evidence uses 0.036/0.08 uM from the explicit K and Vmax cells.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T52A/D128A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II Fru-2,6-Pase row T52A/D128A, columns KFru 2,6-P2, Vmax/Et, and V/KFru2,6P2Et; K column normalized from uM to mM, and kcat/Km normalized from the explicit K and Vmax cells with the printed V/K column retained in raw evidence.

normalized_value_unit_evidence: Km 0.00016 mM, kcat 0.0092 s^-1, kcat/Km 57.5 s^-1*mM^-1; printed V/K column normalizes to 58 s^-1*mM^-1.

raw_value_unit_evidence: Table II row T52A/D128A reports Fru-2,6-Pase KFru 2,6-P2 0.16 uM, Vmax/Et 0.0092 s^-1, and printed V/KFru2,6P2Et 58000 M^-1 s^-1; kcat/Km evidence uses 0.0092/0.16 uM from the explicit K and Vmax cells.


sequence_variant_note: Resolved canonical sequence from ncbi_genbank_accession:AAA41163.1 and applied mutation signature T52S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II Fru-2,6-Pase row T52S, columns KFru 2,6-P2, Vmax/Et, and V/KFru2,6P2Et; K column normalized from uM to mM, and kcat/Km normalized from the explicit K and Vmax cells with the printed V/K column retained in raw evidence.

normalized_value_unit_evidence: Km 0.00005 mM, kcat 0.016 s^-1, kcat/Km 320.0 s^-1*mM^-1; printed V/K column normalizes to 320 s^-1*mM^-1.

raw_value_unit_evidence: Table II row T52S reports Fru-2,6-Pase KFru 2,6-P2 0.05 uM, Vmax/Et 0.016 s^-1, and printed V/KFru2,6P2Et 320000 M^-1 s^-1; kcat/Km evidence uses 0.016/0.05 uM from the explicit K and Vmax cells.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T52S/D128A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II Fru-2,6-Pase row T52S/D128A, columns KFru 2,6-P2, Vmax/Et, and V/KFru2,6P2Et; K column normalized from uM to mM, and kcat/Km normalized from the explicit K and Vmax cells with the printed V/K column retained in raw evidence.

raw_value_unit_evidence: Table II row T52S/D128A reports Fru-2,6-Pase KFru 2,6-P2 0.09 uM, Vmax/Et 0.046 s^-1, and printed V/KFru2,6P2Et 510000 M^-1 s^-1; kcat/Km evidence uses 0.046/0.09 uM from the explicit K and Vmax cells.


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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

column_label: Table II row WT, Fru-2,6-Pase column KFru 2,6-P2 raw cell 0.04 microM, normalized 4e-05 mM; column Vmax/Et raw cell 0.013 s^-1, normalized 0.013 s^-1; column V/KFru2,6P2Et raw cell 330,000 M^-1*s^-1, normalized 330 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.00004 normalized_unit=mM; kcat normalized_value=0.013 normalized_unit=s^-1; kcat/Km normalized_value=330 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: KFru 2,6-P2 raw_value=0.04 raw_unit=microM; Vmax/Et raw_value=0.013 raw_unit=s^-1; V/KFru2,6P2Et raw_value=330,000 raw_unit=M^-1*s^-1

row_label: WT

table_label: Table II. Kinetic constants of rat testis Fru 6-P,2-kinase:Fru-2,6-Pase and the mutant enzymes


sequence_variant_note: Resolved canonical sequence from ncbi_genbank_accession:AAA41163.1 and applied mutation signature Y197F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II Fru-2,6-Pase row Y197F, columns KFru 2,6-P2, Vmax/Et, and V/KFru2,6P2Et; K column normalized from uM to mM, and kcat/Km normalized from the explicit K and Vmax cells with the printed V/K column retained in raw evidence.

raw_value_unit_evidence: Table II row Y197F reports Fru-2,6-Pase KFru 2,6-P2 0.14 uM, Vmax/Et 0.017 s^-1, and printed V/KFru2,6P2Et 120000 M^-1 s^-1; kcat/Km evidence uses 0.017/0.14 uM from the explicit K and Vmax cells.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y197S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II Fru-2,6-Pase row Y197S, columns KFru 2,6-P2, Vmax/Et, and V/KFru2,6P2Et; K column normalized from uM to mM, and kcat/Km normalized from the explicit K and Vmax cells with the printed V/K column retained in raw evidence.

raw_value_unit_evidence: Table II row Y197S reports Fru-2,6-Pase KFru 2,6-P2 0.13 uM, Vmax/Et 0.031 s^-1, and printed V/KFru2,6P2Et 240000 M^-1 s^-1; kcat/Km evidence uses 0.031/0.13 uM from the explicit K and Vmax cells.


substrate_name: 4-Nitrophenyl phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D48T with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

enzyme: protein-tyrosine-phosphatase

substrate: 4-Nitrophenyl phosphate


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N50E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R53N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +10, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W49Y with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


proof_lines: low molecular mass phosphotyrosine protein phosphatase


substrate_name: phosphotyrosine

substrate: phosphotyrosine


enzyme_display_name: UniProt Q92484

substrate_name: CDP-choline

enzyme: UniProt Q92484

substrate: CDP-choline


substrate_name: ADP-ribose

substrate: ADP-ribose


substrate_name: ATP

substrate: ATP


substrate_name: CDP-ethanolamine

substrate: CDP-ethanolamine


substrate_name: ADP

substrate: ADP


organism: Bacillus sp. (in: firmicutes)

substrate_name: bis(p-nitrophenyl)phosphate

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

substrate: bis(p-nitrophenyl)phosphate


enzyme_display_name: UniProt Q9X1T1

organism: Thermotoga maritima

enzyme: UniProt Q9X1T1


organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)

substrate_name: cAMP

substrate: cAMP


organism: Homo sapiens

substrate_name: 4-nitrophenyl phosphate

assay_conditions_summary: pH 7; 295.15 K; buffer pNPP were carried out in 1xPTP

column_label: Table 1 (Kinetic Constants of Wild-Type and Mutant TCPTPs Assayed with pNPP), enzyme row wild-type; column kcat (s-1) = 5.1; column KM (mM) = 2.5; column kcat/KM (mM-1 s-1) = 2.1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.1 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 5.1 s^(-1). Km: printed Table 1 cell 2.5 mM; the Michaelis-constant column of this paper is already in millimolar, so no unit conversion applies and the paper value is 2.5 mM. kcat/Km: printed Table 1 cell 2.1 mM-1 s-1; the efficiency column of this paper is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 2.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row wild-type: kcat = 5.1 s-1; KM = 2.5 mM; printed kcat/KM = 2.1 mM-1 s-1.

row_label: Table 1, enzyme row wild-type

table_label: Table 1: Kinetic Constants of Wild-Type and Mutant TCPTPs Assayed with pNPP (Biochemistry 2008, 47, 4491-4500)

substrate: 4-nitrophenyl phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E187C with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P17706 and applied mutation signature E187C/S188C to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic Constants of Wild-Type and Mutant TCPTPs Assayed with pNPP), enzyme row E187C/S188C; column kcat (s-1) = 5.4; column KM (mM) = 2.3; column kcat/KM (mM-1 s-1) = 2.4.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.4 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 5.4 s^(-1). Km: printed Table 1 cell 2.3 mM; the Michaelis-constant column of this paper is already in millimolar, so no unit conversion applies and the paper value is 2.3 mM. kcat/Km: printed Table 1 cell 2.4 mM-1 s-1; the efficiency column of this paper is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 2.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row E187C/S188C: kcat = 5.4 s-1; KM = 2.3 mM; printed kcat/KM = 2.4 mM-1 s-1.

row_label: Table 1, enzyme row E187C/S188C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P17706 and applied mutation signature F183C to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic Constants of Wild-Type and Mutant TCPTPs Assayed with pNPP), enzyme row F183C; column kcat (s-1) = 0.83; column KM (mM) = 3.1; column kcat/KM (mM-1 s-1) = 0.26.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.83 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 0.83 s^(-1). Km: printed Table 1 cell 3.1 mM; the Michaelis-constant column of this paper is already in millimolar, so no unit conversion applies and the paper value is 3.1 mM. kcat/Km: printed Table 1 cell 0.26 mM-1 s-1; the efficiency column of this paper is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.26 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row F183C: kcat = 0.83 s-1; KM = 3.1 mM; printed kcat/KM = 0.26 mM-1 s-1.

row_label: Table 1, enzyme row F183C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G184C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P181C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P17706 and applied mutation signature P181C/E187C to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic Constants of Wild-Type and Mutant TCPTPs Assayed with pNPP), enzyme row P181C/E187C; column kcat (s-1) = 6.4; column KM (mM) = 0.85; column kcat/KM (mM-1 s-1) = 7.6.

normalized_value_unit_evidence: kcat: printed Table 1 cell 6.4 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 6.4 s^(-1). Km: printed Table 1 cell 0.85 mM; the Michaelis-constant column of this paper is already in millimolar, so no unit conversion applies and the paper value is 0.85 mM. kcat/Km: printed Table 1 cell 7.6 mM-1 s-1; the efficiency column of this paper is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 7.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row P181C/E187C: kcat = 6.4 s-1; KM = 0.85 mM; printed kcat/KM = 7.6 mM-1 s-1.

row_label: Table 1, enzyme row P181C/E187C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P181C/P186C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P186C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P17706 and applied mutation signature P186C/E187C to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic Constants of Wild-Type and Mutant TCPTPs Assayed with pNPP), enzyme row P186C/E187C; column kcat (s-1) = 1.7; column KM (mM) = 3.1; column kcat/KM (mM-1 s-1) = 0.53.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.7 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 1.7 s^(-1). Km: printed Table 1 cell 3.1 mM; the Michaelis-constant column of this paper is already in millimolar, so no unit conversion applies and the paper value is 3.1 mM. kcat/Km: printed Table 1 cell 0.53 mM-1 s-1; the efficiency column of this paper is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.53 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row P186C/E187C: kcat = 1.7 s-1; KM = 3.1 mM; printed kcat/KM = 0.53 mM-1 s-1.

row_label: Table 1, enzyme row P186C/E187C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P17706 and applied mutation signature V185C to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic Constants of Wild-Type and Mutant TCPTPs Assayed with pNPP), enzyme row V185C; column kcat (s-1) = 3.9; column KM (mM) = 2.7; column kcat/KM (mM-1 s-1) = 1.5.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.9 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 3.9 s^(-1). Km: printed Table 1 cell 2.7 mM; the Michaelis-constant column of this paper is already in millimolar, so no unit conversion applies and the paper value is 2.7 mM. kcat/Km: printed Table 1 cell 1.5 mM-1 s-1; the efficiency column of this paper is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 1.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row V185C: kcat = 3.9 s-1; KM = 2.7 mM; printed kcat/KM = 1.5 mM-1 s-1.

row_label: Table 1, enzyme row V185C


organism: Thermococcus kodakarensis

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

assay_conditions_summary: pH 5; 293.15 K; buffer 100 uL reaction

column_label: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins; row Wild type; columns under 60 C: kcat (s^-1), KM (mM), and kcat/KM (s^-1 mM^-1); cells are kcat 30.0 +/- 1.5 s^-1, KM 0.276 +/- 0.042 mM, kcat/KM 109 +/- 7 s^-1 mM^-1.

raw_value_unit_evidence: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins row Wild type, 60 C: kcat (s^-1) = 30.0 +/- 1.5; KM (mM) = 0.276 +/- 0.042; kcat/KM (s^-1 mM^-1) = 109 +/- 7.

row_label: Wild type


enzyme_display_name: UniProt O76074

substrate_name: cGMP

enzyme: UniProt O76074

substrate: cGMP


enzyme_display_name: UniProt P52731

organism: Gallus gallus

enzyme: UniProt P52731


enzyme_display_name: UniProt P16330

organism: Mus musculus

substrate_name: 2',3'-Cyclic AMP

enzyme: UniProt P16330

substrate: 2',3'-Cyclic AMP


enzyme_display_name: protein-tyrosine-phosphatase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D63A to reconstruct the assayed variant sequence.

column_label: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins; row D63A; columns under 60 C: kcat (s^-1), KM (mM), and kcat/KM (s^-1 mM^-1); cells are kcat 1.29 +/- 0.047 s^-1, KM 0.0274 +/- 0.0106 mM, kcat/KM 47.1 +/- 0.1 s^-1 mM^-1.

raw_value_unit_evidence: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins row D63A, 60 C: kcat (s^-1) = 1.29 +/- 0.047; KM (mM) = 0.0274 +/- 0.0106; kcat/KM (s^-1 mM^-1) = 47.1 +/- 0.1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D63N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D63N/E132A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E132A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

column_label: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins; row E132A; columns under 60 C: kcat (s^-1), KM (mM), and kcat/KM (s^-1 mM^-1); cells are kcat 3.83 +/- 0.14 s^-1, KM 0.0230 +/- 0.0084 mM, kcat/KM 167 +/- 5 s^-1 mM^-1.

raw_value_unit_evidence: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins row E132A, 60 C: kcat (s^-1) = 3.83 +/- 0.14; KM (mM) = 0.0230 +/- 0.0084; kcat/KM (s^-1 mM^-1) = 167 +/- 5.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E132L with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

column_label: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins; row E132L; columns under 60 C: kcat (s^-1), KM (mM), and kcat/KM (s^-1 mM^-1); cells are kcat 2.97 +/- 0.15 s^-1, KM 0.251 +/- 0.423 mM, kcat/KM 11.8 +/- 0.7 s^-1 mM^-1.

raw_value_unit_evidence: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins row E132L, 60 C: kcat (s^-1) = 2.97 +/- 0.15; KM (mM) = 0.251 +/- 0.423; kcat/KM (s^-1 mM^-1) = 11.8 +/- 0.7.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E132Q with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

column_label: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins; row E132Q; columns under 60 C: kcat (s^-1), KM (mM), and kcat/KM (s^-1 mM^-1); cells are kcat 8.82 +/- 0.13 s^-1, KM 0.150 +/- 0.062 mM, kcat/KM 58.8 +/- 0.4 s^-1 mM^-1.

raw_value_unit_evidence: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins row E132Q, 60 C: kcat (s^-1) = 8.82 +/- 0.13; KM (mM) = 0.150 +/- 0.062; kcat/KM (s^-1 mM^-1) = 58.8 +/- 0.4.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G95A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

column_label: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins; row G95A; columns under 20 C: kcat (s^-1), KM (mM), and kcat/KM (s^-1 mM^-1); cells are kcat 4.17 +/- 0.12 s^-1, KM 0.0682 +/- 0.0084 mM, kcat/KM 61.1 +/- 0.5 s^-1 mM^-1.

raw_value_unit_evidence: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins row G95A, 20 C: kcat (s^-1) = 4.17 +/- 0.12; KM (mM) = 0.0682 +/- 0.0084; kcat/KM (s^-1 mM^-1) = 61.1 +/- 0.5.


column_label: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins; row G95A; columns under 60 C: kcat (s^-1), KM (mM), and kcat/KM (s^-1 mM^-1); cells are kcat 35.8 +/- 0.7 s^-1, KM 0.106 +/- 0.010 mM, kcat/KM 338 +/- 4 s^-1 mM^-1.

raw_value_unit_evidence: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins row G95A, 60 C: kcat (s^-1) = 35.8 +/- 0.7; KM (mM) = 0.106 +/- 0.010; kcat/KM (s^-1 mM^-1) = 338 +/- 4.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q136A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins; row Q136A; columns under 60 C: kcat (s^-1), KM (mM), and kcat/KM (s^-1 mM^-1); cells are kcat 0.460 +/- 0.015 s^-1, KM 0.135 +/- 0.016 mM, kcat/KM 3.41 +/- 0.03 s^-1 mM^-1.

raw_value_unit_evidence: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins row Q136A, 60 C: kcat (s^-1) = 0.460 +/- 0.015; KM (mM) = 0.135 +/- 0.016; kcat/KM (s^-1 mM^-1) = 3.41 +/- 0.03.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R124A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

column_label: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins; row R124A; columns under 60 C: kcat (s^-1), KM (mM), and kcat/KM (s^-1 mM^-1); cells are kcat 1.59 +/- 0.65 s^-1, KM 0.301 +/- 0.109 mM, kcat/KM 5.28 +/- 0.01 s^-1 mM^-1.

raw_value_unit_evidence: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins row R124A, 60 C: kcat (s^-1) = 1.59 +/- 0.65; KM (mM) = 0.301 +/- 0.109; kcat/KM (s^-1 mM^-1) = 5.28 +/- 0.01.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R124E with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

column_label: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins; row R124E; columns under 60 C: kcat (s^-1), KM (mM), and kcat/KM (s^-1 mM^-1); cells are kcat 0.188 +/- 0.052 s^-1, KM 0.258 +/- 0.043 mM, kcat/KM 0.729 +/- 0.043 s^-1 mM^-1.

raw_value_unit_evidence: Fig 5C panel C, Kinetic parameters of 11 types of Tk-PTP proteins row R124E, 60 C: kcat (s^-1) = 0.188 +/- 0.052; KM (mM) = 0.258 +/- 0.043; kcat/KM (s^-1 mM^-1) = 0.729 +/- 0.043.


organism: Yersinia enterocolitica

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R216A with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R228A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R228K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R236A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R295A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R409A with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R409K with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R437A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R437K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R440K with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


substrate_name: 3-Chlorophenyl phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C17A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: 3-Chlorophenyl phosphate


substrate_name: 3-Nitrophenyl phosphate

substrate: 3-Nitrophenyl phosphate


substrate_name: 4-Cyanophenyl phosphate

substrate: 4-Cyanophenyl phosphate


substrate_name: 4-Ethylphenyl phosphate

substrate: 4-Ethylphenyl phosphate


substrate_name: 4-Fluorophenyl phosphate

substrate: 4-Fluorophenyl phosphate


substrate_name: 4-Nitrophenyl phosphate

substrate: 4-Nitrophenyl phosphate


substrate_name: 4-Trifluoromethylphenyl phosphate

substrate: 4-Trifluoromethylphenyl phosphate


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


enzyme_display_name: Dual specificity protein phosphatase 23

substrate_name: p-nitrophenylphosphate

enzyme: Dual specificity protein phosphatase 23

substrate: p-nitrophenylphosphate


organism: Staphylococcus aureus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C15A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C82S with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C89L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q446A with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q446E with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q446M with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q446N with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q450A with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q450E with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q450M with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


column_label: ScienceDirect article HTML Table II; row label Wild type in the pH 5.0 block; columns kcat, Km, and kcat/Km.

raw_value_unit_evidence: Table II wild-type row in the pH 5.0 block reports kcat 816 +/- 29 s^-1, Km 2.50 +/- 0.26 mM, and kcat/Km 326 +/- 35 s^-1 mM^-1.

row_label: pH 5.0 block, Wild type

table_label: Table II: Kinetic parameters of the Yersinia PTPase and its conserved Gln mutants


column_label: ScienceDirect article HTML Table II; row label Wild type in the pH 8.0 block; columns kcat, Km, and kcat/Km.

raw_value_unit_evidence: Table II wild-type row in the pH 8.0 block reports kcat 3.84 +/- 0.22 s^-1, Km 1.79 +/- 0.34 mM, and kcat/Km 2.1 +/- 0.4 s^-1 mM^-1.

row_label: pH 8.0 block, Wild type


organism: Sus scrofa

substrate_name: glycerol 1,2-cyclic phosphate

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

substrate: glycerol 1,2-cyclic phosphate


enzyme_display_name: UniProt Q08499

enzyme: UniProt Q08499


enzyme_display_name: UniProt O60658

substrate_name: guanosine 3',5'-cyclic phosphate

enzyme: UniProt O60658

substrate: guanosine 3',5'-cyclic phosphate


substrate_name: adenosine 3',5'-cyclic phosphate

substrate: adenosine 3',5'-cyclic phosphate


enzyme_display_name: UniProt Q6S996

organism: Leishmania major

enzyme: UniProt Q6S996


organism: Rattus norvegicus


organism: Rattus sp.


substrate_name: UDP-N-acetylglucosamine

substrate: UDP-N-acetylglucosamine


substrate_name: N-acetylglucosamine 1-phosphate

substrate: N-acetylglucosamine 1-phosphate


enzyme_display_name: 2-lysophosphatidate phosphatase

substrate_name: 1-myristoyl-sn-glycerol 3-phosphate

column_label: Table 2 columns #, KM (microM), kcat (10^-3 s^-1), and kcat/KM (10^-3 s^-1 microM^-1); Table 2 row 16; Table 1 compound 16 = 1-myristoyl-2-hydroxy-3-glycerophosphate.

table_label: PMC JATS Table 2: Kinetic constants of recombinant purified human sEH for lipid phosphates

enzyme: 2-lysophosphatidate phosphatase

substrate: 1-myristoyl-sn-glycerol 3-phosphate


column_label: Table 2 columns #, KM (microM), kcat (10^-3 s^-1), and kcat/KM (10^-3 s^-1 microM^-1); Table 2 row 20*; Table 1 compound 20 = 1-arachidonoyl-2-hydroxy-3-glycerophosphate.

raw_value_unit_evidence: KM 13 +/- 2 microM; kcat 250 +/- 16 in 10^-3 s^-1; kcat/KM 20 +/- 2 in 10^-3 s^-1 microM^-1; asterisk footnote: high substrate concentrations caused inhibition.


row_label: Table 2 row 16; Table 1 compound 16 = 1-myristoyl-2-hydroxy-3-glycerophosphate


substrate_name: 1-oleoyl-2-lyso-sn-glycerol 3-phosphate

column_label: Table 2 columns #, KM (microM), kcat (10^-3 s^-1), and kcat/KM (10^-3 s^-1 microM^-1); Table 2 row 19*; Table 1 compound 19 = 1-oleoyl-2-hydroxy-3-glycerophosphate.

raw_value_unit_evidence: KM 6.9 +/- 0.2 microM; kcat 177 +/- 1 in 10^-3 s^-1; kcat/KM 25 +/- 1 in 10^-3 s^-1 microM^-1; asterisk footnote: high substrate concentrations caused inhibition.

substrate: 1-oleoyl-2-lyso-sn-glycerol 3-phosphate


column_label: Table 2 columns #, KM (microM), kcat (10^-3 s^-1), and kcat/KM (10^-3 s^-1 microM^-1); Table 2 row 18; Table 1 compound 18 = 1-stearyl-2-hydroxy-3-glycerophosphate.


organism: Clostridium perfringens

proof_lines: in 0.1 M sodium phosphate, pH 7.3, at 30°C


substrate_name: Mannosylphosphodolichol

substrate: Mannosylphosphodolichol


enzyme_display_name: UniProt A0QVM9

organism: Mycolicibacterium smegmatis

substrate_name: cyclic di-3',5'-adenylate

enzyme: UniProt A0QVM9

substrate: cyclic di-3',5'-adenylate


substrate_name: cyclic di-3',5'-guanylate

substrate: cyclic di-3',5'-guanylate


enzyme_display_name: UniProt A0A0U1MUE2

enzyme: UniProt A0A0U1MUE2


enzyme_display_name: Glycerophosphodiester phosphodiesterase

organism: Bacillus subtilis (strain 168)

substrate_name: glycerophosphoglycerol

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

proof_lines: kcat is 1275 min(-1) with glycerophosphoglycerol as substrate. kcat is 1517 min(-1) with bis-glycerophosphoglycerol as substrate.

enzyme: Glycerophosphodiester phosphodiesterase

substrate: glycerophosphoglycerol


enzyme_display_name: 3',5'-cyclic-AMP phosphodiesterase

substrate_name: 3',5'-Cyclic AMP; H2O

enzyme: 3',5'-cyclic-AMP phosphodiesterase

substrate: 3',5'-Cyclic AMP; H2O


enzyme_display_name: UniProt O69787

organism: Sinorhizobium meliloti

substrate_name: 4-nitrophenyl methylphosphonate

enzyme: UniProt O69787

substrate: 4-nitrophenyl methylphosphonate


substrate_name: choline O-sulfate

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.6
Raw SKiD Env: Temp=25°C, pH=7.5

substrate: choline O-sulfate


substrate_name: 4-nitrophenyl sulfate

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=25°C, pH=7.6

substrate: 4-nitrophenyl sulfate


substrate_name: 4-Methylumbelliferyl sulfate

substrate: 4-Methylumbelliferyl sulfate


organism: Bacillus thuringiensis

substrate_name: H2O; D-myo-Inositol 1,2-cyclic phosphate


substrate_name: sn-Glycero-3-phospho-1-inositol; H2O

substrate: sn-Glycero-3-phospho-1-inositol; H2O


organism: Bos taurus


enzyme_display_name: glycerophosphodiester phosphodiesterase

organism: Escherichia coli

substrate_name: sn-Glycero 3-phosphoethanolamine; H2O

enzyme: glycerophosphodiester phosphodiesterase

substrate: sn-Glycero 3-phosphoethanolamine; H2O


substrate_name: H2O; sn-Glycero-3-phospho-1-inositol

proof_lines: Measured in the presence of 10 mM magnesium chloride at 37 degrees Celsius.

substrate: H2O; sn-Glycero-3-phospho-1-inositol


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature Δ102 to reconstruct the assayed variant sequence.

mutation_type: deletion


organism: Arabidopsis thaliana

substrate_name: Glycerophosphoglycerol; H2O

substrate: Glycerophosphoglycerol; H2O


substrate_name: H2O; sn-Glycero-3-phosphocholine

substrate: H2O; sn-Glycero-3-phosphocholine


organism: Bacillus altitudinis

substrate_name: bis(pNPP)

proof_lines: kcat is 1.42 sec(-1) with bis(pNPP) as substrate.

substrate: bis(pNPP)


substrate_name: bis-glycerophosphoglycerol

substrate: bis-glycerophosphoglycerol


organism: Klebsiella aerogenes

substrate_name: bis(pNPP) (in the presence of Fe(2+))

proof_lines: kcat is 2.78 sec(-1) with bis(pNPP) as substrate (in the presence of Fe(2+)) (PubMed:18678932). kcat is 0.176 sec(-1) with bis(pNPP) as substrate (in the presence of Zn(2+)) (PubMed:18678932). kcat is 0.107 sec(-1) with bis(pNPP) as substra

substrate: bis(pNPP) (in the presence of Fe(2+))


substrate_name: p-nitrophenyl phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N80D with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

substrate: p-nitrophenyl phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N80A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


substrate_name: glycerophosphoserine

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

column_label: PMC Table 1 row GPS reports kcat 2.8 s^-1.

normalized_value_unit_evidence: kcat normalized_value=2.8 s^-1

raw_value_unit_evidence: kcat raw_value=2.8 raw_unit=s^-1

row_label: GPS

table_label: Table 1

substrate: glycerophosphoserine


column_label: PMC Table 1 row GPS reports Km 0.66 mM.

normalized_value_unit_evidence: Km normalized_value=0.66 mM

raw_value_unit_evidence: Km raw_value=0.66 raw_unit=mM


enzyme_display_name: UniProt P0A433

organism: Flavobacterium sp.

substrate_name: paraoxon

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

enzyme: UniProt P0A433

substrate: paraoxon


enzyme_display_name: UniProt Q93LD7

organism: Agrobacterium tumefaciens

substrate_name: methyl parathion

enzyme: UniProt Q93LD7

substrate: methyl parathion


enzyme_display_name: UniProt Q7SIG4

organism: Loligo vulgaris

substrate_name: diisopropyl fluorophosphate

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.5

enzyme: UniProt Q7SIG4

substrate: diisopropyl fluorophosphate


enzyme_display_name: glycosulfatase

organism: Charonia lampas

substrate_name: N-acetyl-D-glucosamine 6-sulfate

enzyme: glycosulfatase

substrate: N-acetyl-D-glucosamine 6-sulfate


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


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.


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.


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

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


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


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


enzyme_display_name: farnesyl diphosphatase

organism: Saccharolobus solfataricus

substrate_name: geranylgeranyl diphosphate

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

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

substrate: glycerophosphoethanolamine


substrate_name: glycerophosphoglycerol

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


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


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

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


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

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


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


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

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

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

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

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


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


organism: Saccharolobus solfataricus

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.