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

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

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

km_unit: mM

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

status: unverified


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)

source_db: brenda

source_license: CC BY 4.0

ki_unit: mM

sequence_source: multiple

assay_conditions_summary: pH 6

source_databases_merged: brenda uniprot

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

source: brenda


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


organism: Homo sapiens

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

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


enzyme_display_name: protein-tyrosine-phosphatase

substrate_name: 4-Nitrophenyl phosphate; H2O

enzyme: protein-tyrosine-phosphatase

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


source_db: uniprot

source: uniprot


organism: Mus musculus

verification_status: verified

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

status: verified


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

data_origin: experimental

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

km_display: Not reported

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.

mutation_type: substitution

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


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


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: bis-pNPP (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

enzyme: Phosphatase/phosphodiesterase DR_1281

substrate: bis-pNPP (at pH 8.5)


enzyme_display_name: Multiple inositol polyphosphate phosphatase 1

organism: Rattus norvegicus


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

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: 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


enzyme_display_name: UniProt P34913

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_rest_accession:Q00684 and applied mutation signature D50N to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row D50N, pNPP half of the table; column kcat (s^-1) = 0.14; column Km (mM) = 0.40; column kcat/Km (M^-1 s^-1) = 350. captured primary segment: Cdc14 D50N | substrate pNPP (p-nitrophenyl phosphate) | kcat 0.14 s^-1 | Km 0.40 mM | kcat/Km 350 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 0.14 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 0.14 s^(-1). Km: printed cell 0.40 under the column head Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.40 mM. kcat/Km: printed cell 350 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 350 / 1000 = 0.35 s^-1 mM^-1. Quotient disclosure for this cell set: 0.14 / 0.4 = 0.35 s^-1 mM^-1, beside the printed catalytic-efficiency cell 0.35 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row D50N, pNPP half of the table: kcat = 0.14 s^-1; Km = 0.40 mM; printed kcat/Km = 350 M^-1 s^-1.

substrate: 4-Nitrophenyl phosphate

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q00684 and applied mutation signature E168Q to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row E168Q, pNPP half of the table; column kcat (s^-1) = 4.7; column Km (mM) = 12.9; column kcat/Km (M^-1 s^-1) = 364. captured primary segment: Cdc14 E168Q | substrate pNPP (p-nitrophenyl phosphate) | kcat 4.7 s^-1 | Km 12.9 mM | kcat/Km 364 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 4.7 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 4.7 s^(-1). Km: printed cell 12.9 under the column head Km (mM); mM is already canonical, so no unit conversion applies and the value is 12.9 mM. kcat/Km: printed cell 364 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 364 / 1000 = 0.364 s^-1 mM^-1. Quotient disclosure for this cell set: 4.7 / 12.9 = 0.3643410852713178 s^-1 mM^-1, beside the printed catalytic-efficiency cell 0.364 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row E168Q, pNPP half of the table: kcat = 4.7 s^-1; Km = 12.9 mM; printed kcat/Km = 364 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q00684 and applied mutation signature E171Q to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row E171Q, pNPP half of the table; column kcat (s^-1) = 0.94; column Km (mM) = 2.8; column kcat/Km (M^-1 s^-1) = 336. captured primary segment: Cdc14 E171Q | substrate pNPP (p-nitrophenyl phosphate) | kcat 0.94 s^-1 | Km 2.8 mM | kcat/Km 336 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 0.94 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 0.94 s^(-1). Km: printed cell 2.8 under the column head Km (mM); mM is already canonical, so no unit conversion applies and the value is 2.8 mM. kcat/Km: printed cell 336 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 336 / 1000 = 0.336 s^-1 mM^-1. Quotient disclosure for this cell set: 0.94 / 2.8 = 0.3357142857142857 s^-1 mM^-1, beside the printed catalytic-efficiency cell 0.336 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row E171Q, pNPP half of the table: kcat = 0.94 s^-1; Km = 2.8 mM; printed kcat/Km = 336 M^-1 s^-1.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q00684 and applied mutation signature E174Q to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row E174Q, pNPP half of the table; column kcat (s^-1) = 4.3; column Km (mM) = 11.2; column kcat/Km (M^-1 s^-1) = 383. captured primary segment: Cdc14 E174Q | substrate pNPP (p-nitrophenyl phosphate) | kcat 4.3 s^-1 | Km 11.2 mM | kcat/Km 383 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 4.3 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 4.3 s^(-1). Km: printed cell 11.2 under the column head Km (mM); mM is already canonical, so no unit conversion applies and the value is 11.2 mM. kcat/Km: printed cell 383 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 383 / 1000 = 0.383 s^-1 mM^-1. Quotient disclosure for this cell set: 4.3 / 11.2 = 0.38392857142857145 s^-1 mM^-1, beside the printed catalytic-efficiency cell 0.383 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row E174Q, pNPP half of the table: kcat = 4.3 s^-1; Km = 11.2 mM; printed kcat/Km = 383 M^-1 s^-1.

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q00684 and applied mutation signature E308Q to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row E308Q, pNPP half of the table; column kcat (s^-1) = 4.0; column Km (mM) = 11.3; column kcat/Km (M^-1 s^-1) = 353. captured primary segment: Cdc14 E308Q | substrate pNPP (p-nitrophenyl phosphate) | kcat 4.0 s^-1 | Km 11.3 mM | kcat/Km 353 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 4.0 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 4.0 s^(-1). Km: printed cell 11.3 under the column head Km (mM); mM is already canonical, so no unit conversion applies and the value is 11.3 mM. kcat/Km: printed cell 353 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 353 / 1000 = 0.353 s^-1 mM^-1. Quotient disclosure for this cell set: 4.0 / 11.3 = 0.35398230088495575 s^-1 mM^-1, beside the printed catalytic-efficiency cell 0.353 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row E308Q, pNPP half of the table: kcat = 4.0 s^-1; Km = 11.3 mM; printed kcat/Km = 353 M^-1 s^-1.


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

column_label: Table 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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q00684 and applied mutation signature D129N to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row D129N, DiFMUP half of the table; column kcat (s^-1) = 0.13; column Km (uM) = 0.79; column kcat/Km (M^-1 s^-1) = 160,000. captured primary segment: Cdc14 D129N | substrate DiFMUP (6,8-difluoro-4-methylumbelliferyl phosphate) | kcat 0.13 s^-1 | Km 0.79 uM | kcat/Km 160,000 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 0.13 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 0.13 s^(-1). Km: printed cell 0.79 under the column head Km (uM); 1 uM is 0.001 mM, so 0.79 / 1000 = 0.00079 mM. kcat/Km: printed cell 160,000 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 160000 / 1000 = 160 s^-1 mM^-1. Quotient disclosure for this cell set: 0.13 / 0.00079 = 164.55696202531647 s^-1 mM^-1, beside the printed catalytic-efficiency cell 160 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row D129N, DiFMUP half of the table: kcat = 0.13 s^-1; Km = 0.79 uM; printed kcat/Km = 160,000 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q00684 and applied mutation signature D143N to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row D143N, DiFMUP half of the table; column kcat (s^-1) = 5.4; column Km (uM) = 6.1; column kcat/Km (M^-1 s^-1) = 880,000. captured primary segment: Cdc14 D143N | substrate DiFMUP (6,8-difluoro-4-methylumbelliferyl phosphate) | kcat 5.4 s^-1 | Km 6.1 uM | kcat/Km 880,000 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 5.4 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 5.4 s^(-1). Km: printed cell 6.1 under the column head Km (uM); 1 uM is 0.001 mM, so 6.1 / 1000 = 0.0061 mM. kcat/Km: printed cell 880,000 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 880000 / 1000 = 880 s^-1 mM^-1. Quotient disclosure for this cell set: 5.4 / 0.0061 = 885.2459016393443 s^-1 mM^-1, beside the printed catalytic-efficiency cell 880 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row D143N, DiFMUP half of the table: kcat = 5.4 s^-1; Km = 6.1 uM; printed kcat/Km = 880,000 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q00684 and applied mutation signature D177N to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row D177N, DiFMUP half of the table; column kcat (s^-1) = 1.1; column Km (uM) = 0.71; column kcat/Km (M^-1 s^-1) = 1,500,000. captured primary segment: Cdc14 D177N | substrate DiFMUP (6,8-difluoro-4-methylumbelliferyl phosphate) | kcat 1.1 s^-1 | Km 0.71 uM | kcat/Km 1,500,000 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 1.1 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 1.1 s^(-1). Km: printed cell 0.71 under the column head Km (uM); 1 uM is 0.001 mM, so 0.71 / 1000 = 0.00071 mM. kcat/Km: printed cell 1,500,000 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1500000 / 1000 = 1500 s^-1 mM^-1. Quotient disclosure for this cell set: 1.1 / 0.00071 = 1549.2957746478874 s^-1 mM^-1, beside the printed catalytic-efficiency cell 1500 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row D177N, DiFMUP half of the table: kcat = 1.1 s^-1; Km = 0.71 uM; printed kcat/Km = 1,500,000 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q00684 and applied mutation signature D253A to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row D253A, DiFMUP half of the table; column kcat (s^-1) = 0.007; column Km (uM) = 0.0079; column kcat/Km (M^-1 s^-1) = 880,000. captured primary segment: Cdc14 D253A | substrate DiFMUP (6,8-difluoro-4-methylumbelliferyl phosphate) | kcat 0.007 s^-1 | Km 0.0079 uM | kcat/Km 880,000 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 0.007 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 0.007 s^(-1). Km: printed cell 0.0079 under the column head Km (uM); 1 uM is 0.001 mM, so 0.0079 / 1000 = 0.0000079 mM. kcat/Km: printed cell 880,000 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 880000 / 1000 = 880 s^-1 mM^-1. Quotient disclosure for this cell set: 0.007 / 0.0000079 = 886.0759493670886 s^-1 mM^-1, beside the printed catalytic-efficiency cell 880 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row D253A, DiFMUP half of the table: kcat = 0.007 s^-1; Km = 0.0079 uM; printed kcat/Km = 880,000 M^-1 s^-1.


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


column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row D129N, pNPP half of the table; column kcat (s^-1) = 0.13; column Km (mM) = 0.87; column kcat/Km (M^-1 s^-1) = 149. captured primary segment: Cdc14 D129N | substrate pNPP (p-nitrophenyl phosphate) | kcat 0.13 s^-1 | Km 0.87 mM | kcat/Km 149 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 0.13 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 0.13 s^(-1). Km: printed cell 0.87 under the column head Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.87 mM. kcat/Km: printed cell 149 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 149 / 1000 = 0.149 s^-1 mM^-1. Quotient disclosure for this cell set: 0.13 / 0.87 = 0.14942528735632185 s^-1 mM^-1, beside the printed catalytic-efficiency cell 0.149 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row D129N, pNPP half of the table: kcat = 0.13 s^-1; Km = 0.87 mM; printed kcat/Km = 149 M^-1 s^-1.


column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row D143N, pNPP half of the table; column kcat (s^-1) = 3.5; column Km (mM) = 9.6; column kcat/Km (M^-1 s^-1) = 364. captured primary segment: Cdc14 D143N | substrate pNPP (p-nitrophenyl phosphate) | kcat 3.5 s^-1 | Km 9.6 mM | kcat/Km 364 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 3.5 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 3.5 s^(-1). Km: printed cell 9.6 under the column head Km (mM); mM is already canonical, so no unit conversion applies and the value is 9.6 mM. kcat/Km: printed cell 364 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 364 / 1000 = 0.364 s^-1 mM^-1. Quotient disclosure for this cell set: 3.5 / 9.6 = 0.3645833333333333 s^-1 mM^-1, beside the printed catalytic-efficiency cell 0.364 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row D143N, pNPP half of the table: kcat = 3.5 s^-1; Km = 9.6 mM; printed kcat/Km = 364 M^-1 s^-1.


column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row D177N, pNPP half of the table; column kcat (s^-1) = 0.86; column Km (mM) = 1.0; column kcat/Km (M^-1 s^-1) = 860. captured primary segment: Cdc14 D177N | substrate pNPP (p-nitrophenyl phosphate) | kcat 0.86 s^-1 | Km 1.0 mM | kcat/Km 860 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 0.86 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 0.86 s^(-1). Km: printed cell 1.0 under the column head Km (mM); mM is already canonical, so no unit conversion applies and the value is 1.0 mM. kcat/Km: printed cell 860 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 860 / 1000 = 0.86 s^-1 mM^-1. Quotient disclosure for this cell set: 0.86 / 1 = 0.86 s^-1 mM^-1, beside the printed catalytic-efficiency cell 0.86 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row D177N, pNPP half of the table: kcat = 0.86 s^-1; Km = 1.0 mM; printed kcat/Km = 860 M^-1 s^-1.


column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row D253A, pNPP half of the table; column kcat (s^-1) = 0.007; column Km (mM) = 0.11; column kcat/Km (M^-1 s^-1) = 60. captured primary segment: Cdc14 D253A | substrate pNPP (p-nitrophenyl phosphate) | kcat 0.007 s^-1 | Km 0.11 mM | kcat/Km 60 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 0.007 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 0.007 s^(-1). Km: printed cell 0.11 under the column head Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.11 mM. kcat/Km: printed cell 60 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 60 / 1000 = 0.06 s^-1 mM^-1. Quotient disclosure for this cell set: 0.007 / 0.11 = 0.06363636363636363 s^-1 mM^-1, beside the printed catalytic-efficiency cell 0.06 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row D253A, pNPP half of the table: kcat = 0.007 s^-1; Km = 0.11 mM; printed kcat/Km = 60 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q00684 and applied mutation signature D253N to reconstruct the assayed variant sequence.

column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row D253N, pNPP half of the table; column kcat (s^-1) = 0.09; column Km (mM) = 5.75; column kcat/Km (M^-1 s^-1) = 16. captured primary segment: Cdc14 D253N | substrate pNPP (p-nitrophenyl phosphate) | kcat 0.09 s^-1 | Km 5.75 mM | kcat/Km 16 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 0.09 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 0.09 s^(-1). Km: printed cell 5.75 under the column head Km (mM); mM is already canonical, so no unit conversion applies and the value is 5.75 mM. kcat/Km: printed cell 16 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 16 / 1000 = 0.016 s^-1 mM^-1. Quotient disclosure for this cell set: 0.09 / 5.75 = 0.01565217391304348 s^-1 mM^-1, beside the printed catalytic-efficiency cell 0.016 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row D253N, pNPP half of the table: kcat = 0.09 s^-1; Km = 5.75 mM; printed kcat/Km = 16 M^-1 s^-1.


column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row D253N, DiFMUP half of the table; column kcat (s^-1) = 0.08; column Km (uM) = 0.25; column kcat/Km (M^-1 s^-1) = 320,000. captured primary segment: Cdc14 D253N | substrate DiFMUP (6,8-difluoro-4-methylumbelliferyl phosphate) | kcat 0.08 s^-1 | Km 0.25 uM | kcat/Km 320,000 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 0.08 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 0.08 s^(-1). Km: printed cell 0.25 under the column head Km (uM); 1 uM is 0.001 mM, so 0.25 / 1000 = 0.00025 mM. kcat/Km: printed cell 320,000 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 320000 / 1000 = 320 s^-1 mM^-1. Quotient disclosure for this cell set: 0.08 / 0.00025 = 320.0 s^-1 mM^-1, beside the printed catalytic-efficiency cell 320 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row D253N, DiFMUP half of the table: kcat = 0.08 s^-1; Km = 0.25 uM; printed kcat/Km = 320,000 M^-1 s^-1.


column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row E168Q, DiFMUP half of the table; column kcat (s^-1) = 8.7; column Km (uM) = 16.6; column kcat/Km (M^-1 s^-1) = 520,000. captured primary segment: Cdc14 E168Q | substrate DiFMUP (6,8-difluoro-4-methylumbelliferyl phosphate) | kcat 8.7 s^-1 | Km 16.6 uM | kcat/Km 520,000 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 8.7 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 8.7 s^(-1). Km: printed cell 16.6 under the column head Km (uM); 1 uM is 0.001 mM, so 16.6 / 1000 = 0.0166 mM. kcat/Km: printed cell 520,000 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 520000 / 1000 = 520 s^-1 mM^-1. Quotient disclosure for this cell set: 8.7 / 0.0166 = 524.0963855421687 s^-1 mM^-1, beside the printed catalytic-efficiency cell 520 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row E168Q, DiFMUP half of the table: kcat = 8.7 s^-1; Km = 16.6 uM; printed kcat/Km = 520,000 M^-1 s^-1.


column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row E174Q, DiFMUP half of the table; column kcat (s^-1) = 8.2; column Km (uM) = 9.6; column kcat/Km (M^-1 s^-1) = 850,000. captured primary segment: Cdc14 E174Q | substrate DiFMUP (6,8-difluoro-4-methylumbelliferyl phosphate) | kcat 8.2 s^-1 | Km 9.6 uM | kcat/Km 850,000 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 8.2 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 8.2 s^(-1). Km: printed cell 9.6 under the column head Km (uM); 1 uM is 0.001 mM, so 9.6 / 1000 = 0.0096 mM. kcat/Km: printed cell 850,000 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 850000 / 1000 = 850 s^-1 mM^-1. Quotient disclosure for this cell set: 8.2 / 0.0096 = 854.1666666666666 s^-1 mM^-1, beside the printed catalytic-efficiency cell 850 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row E174Q, DiFMUP half of the table: kcat = 8.2 s^-1; Km = 9.6 uM; printed kcat/Km = 850,000 M^-1 s^-1.


column_label: Table II: Kinetic parameters of wild-type and mutant Cdc14 phosphatases with both pNPP and DiFMUP as substrates (J. Biol. Chem. 2004, 279(29):30459-30468), printed column heads Cdc14 | pNPP kcat (s^-1) | pNPP Km (mM) | pNPP kcat/Km (M^-1 s^-1) | DiFMUP kcat (s^-1) | DiFMUP Km (uM) | DiFMUP kcat/Km (M^-1 s^-1). Table II, Cdc14 row E308Q, DiFMUP half of the table; column kcat (s^-1) = 5.7; column Km (uM) = 8.7; column kcat/Km (M^-1 s^-1) = 650,000. captured primary segment: Cdc14 E308Q | substrate DiFMUP (6,8-difluoro-4-methylumbelliferyl phosphate) | kcat 5.7 s^-1 | Km 8.7 uM | kcat/Km 650,000 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed cell 5.7 under the column head kcat (s^-1); that unit is already canonical, so no unit conversion applies and the value is 5.7 s^(-1). Km: printed cell 8.7 under the column head Km (uM); 1 uM is 0.001 mM, so 8.7 / 1000 = 0.0087 mM. kcat/Km: printed cell 650,000 under the column head kcat/Km (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 650000 / 1000 = 650 s^-1 mM^-1. Quotient disclosure for this cell set: 5.7 / 0.0087 = 655.1724137931035 s^-1 mM^-1, beside the printed catalytic-efficiency cell 650 s^-1 mM^-1.

raw_value_unit_evidence: Table II, Cdc14 row E308Q, DiFMUP half of the table: kcat = 5.7 s^-1; Km = 8.7 uM; printed kcat/Km = 650,000 M^-1 s^-1.


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

column_label: Table 1 (Summary of kinetic parameters for OxsA with OXT- and deoxyribonucleotide compounds) prints one label column, 'Tested substrate', followed by four numeric columns whose heads are 'KM (uM)', 'Vmax x 10^-3 (U/mg)', 'kcat x 10^-3 (s^-1)' and 'kcat/KM (M^-1 s^-1)' in that printed order; the Vmax and kcat heads carry a shared power-of-ten column scale that belongs to every cell of those two columns. The cited cell set is Table 1, tested substrate row dADP: KM (uM) = 53; Vmax x 10^-3 (U/mg) = 7.1; kcat x 10^-3 (s^-1) = 2.6; kcat/KM (M^-1 s^-1) = 51. The printed uncertainties of that row are KM 53 +/- 11, Vmax 7.1 +/- 0.35, kcat 2.6 +/- 0.13 and kcat/KM 51 +/- 10. The table footnote reads 'See SI Materials and Methods for experimental details.' and '*U/mg = umol/min mg of OxsA.'

normalized_value_unit_evidence: KM: printed Table 1 cell 53 uM; 53 / 1000 = 0.053, so the paper value is 0.053 mM; the exported value is 0.053 mM. kcat: printed Table 1 cell 2.6 x 10^-3 s^-1, read under the printed column scale x 10^-3 that the kcat head carries; 2.6 x 10^-3 = 0.0026, and the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so the paper value is 0.0026 s^(-1); the exported value is 0.0026 s^(-1). kcat/KM: printed Table 1 cell 51 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 51 / 1000 = 0.051 s^(-1)*mM^(-1); the exported value is 0.0490566037735849 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, tested substrate row 'dADP': KM = 53 uM; kcat = 2.6 x 10^-3 s^-1; printed kcat/KM = 51 M^-1 s^-1; Vmax = 7.1 x 10^-3 U/mg.

row_label: Table 1, tested substrate row dADP

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

enzyme: 4'-phosphooxetanocin A phosphatase

substrate: dADP


substrate_name: dAMP

column_label: Table 1 (Summary of kinetic parameters for OxsA with OXT- and deoxyribonucleotide compounds) prints one label column, 'Tested substrate', followed by four numeric columns whose heads are 'KM (uM)', 'Vmax x 10^-3 (U/mg)', 'kcat x 10^-3 (s^-1)' and 'kcat/KM (M^-1 s^-1)' in that printed order; the Vmax and kcat heads carry a shared power-of-ten column scale that belongs to every cell of those two columns. The cited cell set is Table 1, tested substrate row dAMP: KM (uM) = 22; Vmax x 10^-3 (U/mg) = 9.8; kcat x 10^-3 (s^-1) = 3.7; kcat/KM (M^-1 s^-1) = 167. The printed uncertainties of that row are KM 22 +/- 2, Vmax 9.8 +/- 0.24, kcat 3.7 +/- 0.094 and kcat/KM 167 +/- 16. The table footnote reads 'See SI Materials and Methods for experimental details.' and '*U/mg = umol/min mg of OxsA.'

normalized_value_unit_evidence: KM: printed Table 1 cell 22 uM; 22 / 1000 = 0.022, so the paper value is 0.022 mM; the exported value is 0.022 mM. kcat: printed Table 1 cell 3.7 x 10^-3 s^-1, read under the printed column scale x 10^-3 that the kcat head carries; 3.7 x 10^-3 = 0.0037, and the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so the paper value is 0.0037 s^(-1); the exported value is 0.0037 s^(-1). kcat/KM: printed Table 1 cell 167 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 167 / 1000 = 0.167 s^(-1)*mM^(-1); the exported value is 0.1681818181818182 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, tested substrate row 'dAMP': KM = 22 uM; kcat = 3.7 x 10^-3 s^-1; printed kcat/KM = 167 M^-1 s^-1; Vmax = 9.8 x 10^-3 U/mg.

row_label: Table 1, tested substrate row dAMP

substrate: dAMP


substrate_name: dATP

column_label: Table 1 (Summary of kinetic parameters for OxsA with OXT- and deoxyribonucleotide compounds) prints one label column, 'Tested substrate', followed by four numeric columns whose heads are 'KM (uM)', 'Vmax x 10^-3 (U/mg)', 'kcat x 10^-3 (s^-1)' and 'kcat/KM (M^-1 s^-1)' in that printed order; the Vmax and kcat heads carry a shared power-of-ten column scale that belongs to every cell of those two columns. The cited cell set is Table 1, tested substrate row dATP: KM (uM) = 155; Vmax x 10^-3 (U/mg) = 58; kcat x 10^-3 (s^-1) = 22; kcat/KM (M^-1 s^-1) = 142. The printed uncertainties of that row are KM 155 +/- 18, Vmax 58 +/- 2.4, kcat 22 +/- 0.83 and kcat/KM 142 +/- 17. The table footnote reads 'See SI Materials and Methods for experimental details.' and '*U/mg = umol/min mg of OxsA.'

normalized_value_unit_evidence: KM: printed Table 1 cell 155 uM; 155 / 1000 = 0.155, so the paper value is 0.155 mM; the exported value is 0.155 mM. kcat: printed Table 1 cell 22 x 10^-3 s^-1, read under the printed column scale x 10^-3 that the kcat head carries; 22 x 10^-3 = 0.022, and the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so the paper value is 0.022 s^(-1); the exported value is 0.022 s^(-1). kcat/KM: printed Table 1 cell 142 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 142 / 1000 = 0.142 s^(-1)*mM^(-1); the exported value is 0.14193548387096774 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells, and that quotient written in the paper's own unit to the whole number its efficiency column prints is 142 M^-1 s^-1, the printed cell.

raw_value_unit_evidence: Table 1, tested substrate row 'dATP': KM = 155 uM; kcat = 22 x 10^-3 s^-1; printed kcat/KM = 142 M^-1 s^-1; Vmax = 58 x 10^-3 U/mg.

row_label: Table 1, tested substrate row 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

column_label: Table 1 (Summary of kinetic parameters for OxsA with OXT- and deoxyribonucleotide compounds) prints one label column, 'Tested substrate', followed by four numeric columns whose heads are 'KM (uM)', 'Vmax x 10^-3 (U/mg)', 'kcat x 10^-3 (s^-1)' and 'kcat/KM (M^-1 s^-1)' in that printed order; the Vmax and kcat heads carry a shared power-of-ten column scale that belongs to every cell of those two columns. The cited cell set is Table 1, tested substrate row OXT-P: KM (uM) = 11; Vmax x 10^-3 (U/mg) = 3.2; kcat x 10^-3 (s^-1) = 1.2; kcat/KM (M^-1 s^-1) = 106. The printed uncertainties of that row are KM 11 +/- 3, Vmax 3.2 +/- 0.20, kcat 1.2 +/- 0.077 and kcat/KM 106 +/- 30. The table footnote reads 'See SI Materials and Methods for experimental details.' and '*U/mg = umol/min mg of OxsA.'

normalized_value_unit_evidence: KM: printed Table 1 cell 11 uM; 11 / 1000 = 0.011, so the paper value is 0.011 mM; the exported value is 0.008 mM. kcat: printed Table 1 cell 1.2 x 10^-3 s^-1, read under the printed column scale x 10^-3 that the kcat head carries; 1.2 x 10^-3 = 0.0012, and the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so the paper value is 0.0012 s^(-1); the exported value is 0.0012 s^(-1). kcat/KM: printed Table 1 cell 106 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 106 / 1000 = 0.106 s^(-1)*mM^(-1); the catalog row carries no catalytic-efficiency value, so this record exports none.

raw_value_unit_evidence: Table 1, tested substrate row 'OXT-P': KM = 11 uM; kcat = 1.2 x 10^-3 s^-1; printed kcat/KM = 106 M^-1 s^-1; Vmax = 3.2 x 10^-3 U/mg.

row_label: Table 1, tested substrate row OXT-P

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

assay_conditions_summary: pH 7

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