substrate_name: ADP-ribose

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation F37Y, substrate ADP-ribose, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: F37Y / ADP-ribose

substrate: ADP-ribose


enzyme_display_name: ADP-ribose diphosphatase

organism: Homo sapiens

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H111A to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation H111A, substrate ADP-ribose, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: H111A / ADP-ribose

data_origin: experimental

enzyme: ADP-ribose diphosphatase

status: corrected

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H111N to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation H111N, substrate ADP-ribose, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: H111N / ADP-ribose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L196A to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation L196A, substrate ADP-ribose, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: L196A / ADP-ribose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N110A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation N110A, substrate ADP-ribose, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: N110A / ADP-ribose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q27H with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation Q27H, substrate ADP-ribose, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: current kcat 10 s^-1; paper kcat 10 +/- 3 s^-1; current Km 0.2 mM; paper Km 200 +/- 14 uM = 0.2 mM; current kcat/Km 50 s^-1 mM^-1; paper kcat/Km 52000 +/- 10000 M^-1 s^-1 = 52 s^-1 mM^-1

row_label: Q27H / ADP-ribose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R43A to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation R43A, substrate ADP-ribose, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: R43A / ADP-ribose


verification_status: verified

mutation_signature: Unknown

kcat_over_km_origin: calculated

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

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants; row Wild type / ADP-ribose; columns kcat column raw 35 +/- 11 normalized 35 s^-1; Km column raw 60 +/- 8 uM normalized 0.06 mM; kcat/Km column raw 590000 +/- 160000 M^-1 s^-1 normalized from same-row kcat and Km as 583.3333333333334 s^-1*mM^-1; export values for required/current metrics match these normalized values.

normalized_value_unit_evidence: kcat normalized_value=35 normalized_unit=s^-1; Km normalized_value=0.06 normalized_unit=mM; kcat/Km normalized_value=583.3333333333334 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=590000 +/- 160000 M^-1 s^-1

raw_value_unit_evidence: kcat raw_value=35 +/- 11 raw_unit=s^-1; Km raw_value=60 +/- 8 raw_unit=uM; kcat/Km raw_value=590000 +/- 160000 raw_unit=M^-1 s^-1

row_label: Wild type / ADP-ribose

status: verified


substrate_name: cADP-ribose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C253A to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation C253A, substrate cADP-ribose, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: C253A / cADP-ribose

substrate: cADP-ribose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F37A/L196F/C253A to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation F37A+L196F+C253A, substrate cADP-ribose, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: F37A+L196F+C253A / cADP-ribose


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation N110A, substrate 2',3'-cAMP, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation Q27H, substrate 2',3'-cAMP, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation R43A, substrate 2',3'-cAMP, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).


table_label: Table 1

row_label: Wild type / 2´,3´-cAMP

column_label: Table 1; mutation row Wild type; substrate row 2´,3´-cAMP; columns kcat, Km, kcat/Km

raw_value_unit_evidence: paper Table 1 cells: kcat=60 ± 13 s^-1; km=2400 ± 300 uM; kcat_over_km=25000 ± 6000 M^-1 s^-1

normalized_value_unit_evidence: normalized: kcat=60 s^-1; km=2.4 mM; kcat_over_km=25 s^-1 mM^-1


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation C253A, substrate ADP-ribose, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: C253A / ADP-ribose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F210A to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation F210A, substrate ADP-ribose, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: current kcat 19 s^-1; paper kcat 19 +/- 3 s^-1; current Km 2.1 mM; paper Km 2100 +/- 100 uM = 2.1 mM; current kcat/Km 9.04762 s^-1 mM^-1; paper kcat/Km 9000 +/- 1000 M^-1 s^-1 = 9 s^-1 mM^-1

row_label: F210A / ADP-ribose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F37A to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation F37A, substrate ADP-ribose, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: F37A / ADP-ribose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F37A/L196A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation F37A+L196A, substrate ADP-ribose, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: current kcat 7 s^-1; paper kcat 7 +/- 2 s^-1; current Km 1.15 mM; paper Km 1150 +/- 500 uM = 1.15 mM; current kcat/Km 6.08696 s^-1 mM^-1; paper kcat/Km 6000 +/- 2000 M^-1 s^-1 = 6 s^-1 mM^-1

row_label: F37A+L196A / ADP-ribose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F37A/L196F with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation F37A+L196F, substrate ADP-ribose, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: current kcat 8 s^-1; paper kcat 8 +/- 1 s^-1; current Km 1.6 mM; paper Km 1600 +/- 100 uM = 1.6 mM; current kcat/Km 5 s^-1 mM^-1; paper kcat/Km 4800 +/- 200 M^-1 s^-1 = 4.8 s^-1 mM^-1

row_label: F37A+L196F / ADP-ribose


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation F37A+L196F+C253A, substrate ADP-ribose, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: F37A+L196F+C253A / ADP-ribose


substrate_name: CDP-choline

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation L196A, substrate CDP-choline, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: L196A / CDP-choline

substrate: CDP-choline


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation N110A, substrate CDP-choline, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: current kcat 5.7 s^-1; paper kcat 5.7 +/- 1.4 s^-1; current Km 4 mM; paper Km 4000 +/- 1100 uM = 4 mM; current kcat/Km 1.425 s^-1 mM^-1; paper kcat/Km 1500 +/- 400 M^-1 s^-1 = 1.5 s^-1 mM^-1

row_label: N110A / CDP-choline


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation Q27H, substrate CDP-choline, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: Q27H / CDP-choline


verification_status: unverified

status: unverified


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants; row Wild type / CDP-choline; columns kcat column raw 50 +/- 4 normalized 50 s^-1; Km column raw 350 +/- 60 uM normalized 0.35 mM; kcat/Km column raw 150000 +/- 30000 M^-1 s^-1 normalized from same-row kcat and Km as 142.85714285714286 s^-1*mM^-1; export values for required/current metrics match these normalized values.

normalized_value_unit_evidence: kcat normalized_value=50 normalized_unit=s^-1; Km normalized_value=0.35 normalized_unit=mM; kcat/Km normalized_value=142.85714285714286 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=150000 +/- 30000 M^-1 s^-1

raw_value_unit_evidence: kcat raw_value=50 +/- 4 raw_unit=s^-1; Km raw_value=350 +/- 60 raw_unit=uM; kcat/Km raw_value=150000 +/- 30000 raw_unit=M^-1 s^-1

row_label: Wild type / CDP-choline


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants; row Wild type / cADPR; columns kcat column raw 3.2 +/- 0.2 normalized 3.2 s^-1; Km column raw 780 +/- 200 uM normalized 0.78 mM; kcat/Km column raw 4000 +/- 1000 M^-1 s^-1 normalized from same-row kcat and Km as 4.102564102564103 s^-1*mM^-1; export values for required/current metrics match these normalized values.

normalized_value_unit_evidence: kcat normalized_value=3.2 normalized_unit=s^-1; Km normalized_value=0.78 normalized_unit=mM; kcat/Km normalized_value=4.102564102564103 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=4000 +/- 1000 M^-1 s^-1

raw_value_unit_evidence: kcat raw_value=3.2 +/- 0.2 raw_unit=s^-1; Km raw_value=780 +/- 200 raw_unit=uM; kcat/Km raw_value=4000 +/- 1000 raw_unit=M^-1 s^-1

row_label: Wild type / cADPR


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation C253A, substrate CDP-choline, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: current kcat 79 s^-1; paper kcat 79 +/- 7 s^-1; current Km 0.5 mM; paper Km 500 +/- 70 uM = 0.5 mM; current kcat/Km 158 s^-1 mM^-1; paper kcat/Km 160000 +/- 20000 M^-1 s^-1 = 160 s^-1 mM^-1

row_label: C253A / CDP-choline


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation F210A, substrate CDP-choline, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: current kcat 50 s^-1; paper kcat 50 +/- 12 s^-1; current Km 11 mM; paper Km 11000 +/- 2600 uM = 11 mM; current kcat/Km 4.54545 s^-1 mM^-1; paper kcat/Km 4000 +/- 100 M^-1 s^-1 = 4 s^-1 mM^-1

row_label: F210A / CDP-choline


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation F37A, substrate CDP-choline, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: F37A / CDP-choline


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation F37A+L196A, substrate CDP-choline, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: current kcat 25 s^-1; paper kcat 25 +/- 5 s^-1; current Km 1.25 mM; paper Km 1250 +/- 250 uM = 1.25 mM; current kcat/Km 20 s^-1 mM^-1; paper kcat/Km 21000 +/- 8000 M^-1 s^-1 = 21 s^-1 mM^-1

row_label: F37A+L196A / CDP-choline


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation F37A+L196F, substrate CDP-choline, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: F37A+L196F / CDP-choline


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation F37A+L196F+C253A, substrate CDP-choline, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: F37A+L196F+C253A / CDP-choline


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F37Y to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation F37Y, substrate CDP-choline, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: F37Y / CDP-choline


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation H111A, substrate CDP-choline, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: H111A / CDP-choline


column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation H111N, substrate CDP-choline, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: H111N / CDP-choline


enzyme_display_name: nucleotide diphosphatase

organism: Oryza sativa

substrate_name: UDP-glucose

source_db: brenda

column_label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row UDP-glucose / NPP1, column NPP1; kcat s^-1, raw cell 282, normalized 282 s^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row UDP-glucose / NPP1, column NPP1; kcat/Km s^-1 M^-1, raw cell 1.93 x 10^5, normalized 193 s^-1*mM^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row UDP-glucose / NPP1, column NPP1; Km mM, raw cell 1.5, normalized 1.5 mM

normalized_value_unit_evidence: kcat normalized_value=282 normalized_unit=s^-1; kcat/Km normalized_value=193 normalized_unit=s^-1*mM^-1; Km normalized_value=1.5 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=282 raw_unit=s^-1 raw_cell=282; kcat/Km raw_value=193000 raw_unit=M^-1*s^-1 raw_cell=1.93 x 10^5; Km raw_value=1.5 raw_unit=mM raw_cell=1.5

row_label: UDP-glucose / NPP1

enzyme: nucleotide diphosphatase

substrate: UDP-glucose

source: brenda


substrate_name: CDP-glucose

assay_conditions_summary: pH 6

column_label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row CDP-glucose / NPP1, column NPP1; kcat s^-1, raw cell 125, normalized 125 s^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row CDP-glucose / NPP1, column NPP1; kcat/Km s^-1 M^-1, raw cell 1.93 x 10^5, normalized 193 s^-1*mM^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row CDP-glucose / NPP1, column NPP1; Km mM, raw cell 0.9, normalized 0.9 mM

normalized_value_unit_evidence: kcat normalized_value=125 normalized_unit=s^-1; kcat/Km normalized_value=193 normalized_unit=s^-1*mM^-1; Km normalized_value=0.9 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=125 raw_unit=s^-1 raw_cell=125; kcat/Km raw_value=193000 raw_unit=M^-1*s^-1 raw_cell=1.93 x 10^5; Km raw_value=0.9 raw_unit=mM raw_cell=0.9

row_label: CDP-glucose / NPP1

substrate: CDP-glucose


substrate_name: ADP-glucose

assay_conditions_summary: pH 6; cofactor ADP

column_label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row ADP-glucose / NPP1, column NPP1; kcat s^-1, raw cell 214, normalized 214 s^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row ADP-glucose / NPP1, column NPP1; kcat/Km s^-1 M^-1, raw cell 2.50 x 10^5, normalized 250 s^-1*mM^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row ADP-glucose / NPP1, column NPP1; Km mM, raw cell 0.8, normalized 0.8 mM

normalized_value_unit_evidence: kcat normalized_value=214 normalized_unit=s^-1; kcat/Km normalized_value=250 normalized_unit=s^-1*mM^-1; Km normalized_value=0.8 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=214 raw_unit=s^-1 raw_cell=214; kcat/Km raw_value=250000 raw_unit=M^-1*s^-1 raw_cell=2.50 x 10^5; Km raw_value=0.8 raw_unit=mM raw_cell=0.8

row_label: ADP-glucose / NPP1

substrate: ADP-glucose


assay_conditions_summary: pH 4.5; cofactor ADP

column_label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row ADP-glucose / NPP6, column NPP6; kcat s^-1, raw cell 130, normalized 130 s^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row ADP-glucose / NPP6, column NPP6; kcat/Km s^-1 M^-1, raw cell 1.93 x 10^5, normalized 193 s^-1*mM^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row ADP-glucose / NPP6, column NPP6; Km mM, raw cell 0.7, normalized 0.7 mM

normalized_value_unit_evidence: kcat normalized_value=130 normalized_unit=s^-1; kcat/Km normalized_value=193 normalized_unit=s^-1*mM^-1; Km normalized_value=0.7 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=130 raw_unit=s^-1 raw_cell=130; kcat/Km raw_value=193000 raw_unit=M^-1*s^-1 raw_cell=1.93 x 10^5; Km raw_value=0.7 raw_unit=mM raw_cell=0.7

row_label: ADP-glucose / NPP6


substrate_name: GDP-mannose

column_label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row GDP-mannose / NPP1, column NPP1; kcat s^-1, raw cell 151, normalized 151 s^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row GDP-mannose / NPP1, column NPP1; kcat/Km s^-1 M^-1, raw cell 1.90 x 10^5, normalized 190 s^-1*mM^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row GDP-mannose / NPP1, column NPP1; Km mM, raw cell 0.8, normalized 0.8 mM

normalized_value_unit_evidence: kcat normalized_value=151 normalized_unit=s^-1; kcat/Km normalized_value=190 normalized_unit=s^-1*mM^-1; Km normalized_value=0.8 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=151 raw_unit=s^-1 raw_cell=151; kcat/Km raw_value=190000 raw_unit=M^-1*s^-1 raw_cell=1.90 x 10^5; Km raw_value=0.8 raw_unit=mM raw_cell=0.8

row_label: GDP-mannose / NPP1

substrate: GDP-mannose


column_label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row ADP-ribose / NPP1, column NPP1; kcat s^-1, raw cell 370, normalized 370 s^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row ADP-ribose / NPP1, column NPP1; kcat/Km s^-1 M^-1, raw cell 2.48 x 10^5, normalized 248 s^-1*mM^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row ADP-ribose / NPP1, column NPP1; Km mM, raw cell 1.4, normalized 1.4 mM

normalized_value_unit_evidence: kcat normalized_value=370 normalized_unit=s^-1; kcat/Km normalized_value=248 normalized_unit=s^-1*mM^-1; Km normalized_value=1.4 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=370 raw_unit=s^-1 raw_cell=370; kcat/Km raw_value=248000 raw_unit=M^-1*s^-1 raw_cell=2.48 x 10^5; Km raw_value=1.4 raw_unit=mM raw_cell=1.4

row_label: ADP-ribose / NPP1


substrate_name: adenosine 5'-phosphosulfate

column_label: Table 2, row 'APS', NPP6 columns Km, kcat, kcat/Km. PMC article HTML preserves the Plant and Cell Physiology primary kinetic table. Table units are Km mM, kcat s^-1, and kcat/Km s^-1 M^-1; kcat/Km is normalized to s^-1 mM^-1 by dividing by 1000.

row_label: APS / NPP6

table_label: Table 2

substrate: adenosine 5'-phosphosulfate


column_label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row APS / NPP1, column NPP1; kcat s^-1, raw cell 329, normalized 329 s^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row APS / NPP1, column NPP1; kcat/Km s^-1 M^-1, raw cell 1.09 x 10^5, normalized 109 s^-1*mM^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row APS / NPP1, column NPP1; Km mM, raw cell 3, normalized 3 mM

normalized_value_unit_evidence: kcat normalized_value=329 normalized_unit=s^-1; kcat/Km normalized_value=109 normalized_unit=s^-1*mM^-1; Km normalized_value=3 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=329 raw_unit=s^-1 raw_cell=329; kcat/Km raw_value=109000 raw_unit=M^-1*s^-1 raw_cell=1.09 x 10^5; Km raw_value=3 raw_unit=mM raw_cell=3

row_label: APS / NPP1


substrate_name: ADP

assay_conditions_summary: pH 4.5; 310.15 K; cofactor ADP

column_label: Table 2, row 'ADP', NPP6 columns Km, kcat, kcat/Km. PMC article HTML preserves the Plant and Cell Physiology primary kinetic table. Table units are Km mM, kcat s^-1, and kcat/Km s^-1 M^-1; kcat/Km is normalized to s^-1 mM^-1 by dividing by 1000.

row_label: ADP / NPP6

substrate: ADP


assay_conditions_summary: pH 6; 310.15 K; cofactor ADP

column_label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row ADP / NPP1, column NPP1; kcat s^-1, raw cell 449, normalized 449 s^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row ADP / NPP1, column NPP1; kcat/Km s^-1 M^-1, raw cell 1.00 x 10^5, normalized 100 s^-1*mM^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row ADP / NPP1, column NPP1; Km mM, raw cell 4.3, normalized 4.3 mM

normalized_value_unit_evidence: kcat normalized_value=449 normalized_unit=s^-1; kcat/Km normalized_value=100 normalized_unit=s^-1*mM^-1; Km normalized_value=4.3 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=449 raw_unit=s^-1 raw_cell=449; kcat/Km raw_value=100000 raw_unit=M^-1*s^-1 raw_cell=1.00 x 10^5; Km raw_value=4.3 raw_unit=mM raw_cell=4.3

row_label: ADP / NPP1


table_label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6


substrate_name: ATP

assay_conditions_summary: pH 4.5; 310.15 K; cofactor ATP

column_label: Table 2, row 'ATP', NPP1 columns Km, kcat, kcat/Km. PMC article HTML preserves the Plant and Cell Physiology primary kinetic table. Table units are Km mM, kcat s^-1, and kcat/Km s^-1 M^-1; kcat/Km is normalized to s^-1 mM^-1 by dividing by 1000.

row_label: ATP / NPP1

substrate: ATP


assay_conditions_summary: pH 6; 310.15 K; cofactor ATP

column_label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row ATP / NPP1, column NPP1; kcat s^-1, raw cell 415, normalized 415 s^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row ATP / NPP1, column NPP1; kcat/Km s^-1 M^-1, raw cell 2.03 x 10^5, normalized 203 s^-1*mM^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row ATP / NPP1, column NPP1; Km mM, raw cell 2.1, normalized 2.1 mM

normalized_value_unit_evidence: kcat normalized_value=415 normalized_unit=s^-1; kcat/Km normalized_value=203 normalized_unit=s^-1*mM^-1; Km normalized_value=2.1 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=415 raw_unit=s^-1 raw_cell=415; kcat/Km raw_value=203000 raw_unit=M^-1*s^-1 raw_cell=2.03 x 10^5; Km raw_value=2.1 raw_unit=mM raw_cell=2.1


substrate_name: GDP

column_label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row GDP / NPP2, column NPP2; kcat s^-1, raw cell 28, normalized 28 s^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row GDP / NPP2, column NPP2; kcat/Km s^-1 M^-1, raw cell 0.32 x 10^5, normalized 32 s^-1*mM^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row GDP / NPP2, column NPP2; Km mM, raw cell 0.9, normalized 0.9 mM

normalized_value_unit_evidence: kcat normalized_value=28 normalized_unit=s^-1; kcat/Km normalized_value=32 normalized_unit=s^-1*mM^-1; Km normalized_value=0.9 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=28 raw_unit=s^-1 raw_cell=28; kcat/Km raw_value=32000 raw_unit=M^-1*s^-1 raw_cell=0.32 x 10^5; Km raw_value=0.9 raw_unit=mM raw_cell=0.9

row_label: GDP / NPP2

substrate: GDP


substrate_name: diphosphate

column_label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row PPi / NPP6, column NPP6; kcat s^-1, raw cell 79, normalized 79 s^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row PPi / NPP6, column NPP6; kcat/Km s^-1 M^-1, raw cell 1.75 x 10^5, normalized 175 s^-1*mM^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row PPi / NPP6, column NPP6; Km mM, raw cell 0.5, normalized 0.5 mM

normalized_value_unit_evidence: kcat normalized_value=79 normalized_unit=s^-1; kcat/Km normalized_value=175 normalized_unit=s^-1*mM^-1; Km normalized_value=0.5 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=79 raw_unit=s^-1 raw_cell=79; kcat/Km raw_value=175000 raw_unit=M^-1*s^-1 raw_cell=1.75 x 10^5; Km raw_value=0.5 raw_unit=mM raw_cell=0.5

row_label: PPi / NPP6

substrate: diphosphate


assay_conditions_summary: pH 6; cofactor ATP


assay_conditions_summary: pH 4.5; cofactor ATP


substrate_name: TDP-glucose

km_display: Not reported

column_label: Table 2, row 'TDP-glucose', NPP1 columns Km, kcat, kcat/Km. PMC article HTML preserves the Plant and Cell Physiology primary kinetic table. Table units are Km mM, kcat s^-1, and kcat/Km s^-1 M^-1; kcat/Km is normalized to s^-1 mM^-1 by dividing by 1000.

row_label: TDP-glucose / NPP1

substrate: TDP-glucose


column_label: Table 2, row 'TDP-glucose', NPP6 columns Km, kcat, kcat/Km. PMC article HTML preserves the Plant and Cell Physiology primary kinetic table. Table units are Km mM, kcat s^-1, and kcat/Km s^-1 M^-1; kcat/Km is normalized to s^-1 mM^-1 by dividing by 1000.

row_label: TDP-glucose / NPP6


substrate_name: IDP

column_label: Table 2, row 'IDP', NPP2 columns Km, kcat, kcat/Km. PMC article HTML preserves the Plant and Cell Physiology primary kinetic table. Table units are Km mM, kcat s^-1, and kcat/Km s^-1 M^-1; kcat/Km is normalized to s^-1 mM^-1 by dividing by 1000.

row_label: IDP / NPP2

substrate: IDP


substrate_name: CDP

column_label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row CDP / NPP2, column NPP2; kcat s^-1, raw cell 89, normalized 89 s^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row CDP / NPP2, column NPP2; kcat/Km s^-1 M^-1, raw cell 0.47 x 10^5, normalized 47 s^-1*mM^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row CDP / NPP2, column NPP2; Km mM, raw cell 1.9, normalized 1.9 mM

normalized_value_unit_evidence: kcat normalized_value=89 normalized_unit=s^-1; kcat/Km normalized_value=47 normalized_unit=s^-1*mM^-1; Km normalized_value=1.9 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=89 raw_unit=s^-1 raw_cell=89; kcat/Km raw_value=47000 raw_unit=M^-1*s^-1 raw_cell=0.47 x 10^5; Km raw_value=1.9 raw_unit=mM raw_cell=1.9

row_label: CDP / NPP2

substrate: CDP


substrate_name: UDP

column_label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row UDP / NPP6, column NPP6; kcat s^-1, raw cell 104, normalized 104 s^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row UDP / NPP6, column NPP6; kcat/Km s^-1 M^-1, raw cell 2.03 x 10^5, normalized 203 s^-1*mM^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row UDP / NPP6, column NPP6; Km mM, raw cell 0.5, normalized 0.5 mM

normalized_value_unit_evidence: kcat normalized_value=104 normalized_unit=s^-1; kcat/Km normalized_value=203 normalized_unit=s^-1*mM^-1; Km normalized_value=0.5 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=104 raw_unit=s^-1 raw_cell=104; kcat/Km raw_value=203000 raw_unit=M^-1*s^-1 raw_cell=2.03 x 10^5; Km raw_value=0.5 raw_unit=mM raw_cell=0.5

row_label: UDP / NPP6

substrate: UDP


organism: Mus musculus

substrate_name: H2O; 8-oxo-dGTP

kcat_display: Not reported

kcat_over_km_display: Not reported

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

substrate: H2O; 8-oxo-dGTP


enzyme_display_name: nucleoside-triphosphate diphosphatase

substrate_name: ATP; H2O

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

assay_conditions_summary: cofactor ATP

enzyme: nucleoside-triphosphate diphosphatase

substrate: ATP; H2O


substrate_name: TDP

substrate: TDP


organism: Rattus norvegicus

substrate_name: p-Nitrophenylthymidine phosphate; H2O

substrate: p-Nitrophenylthymidine phosphate; H2O


assay_conditions_summary: cofactor NADH


column_label: Table 2, row 'Bis-p-NPP', NPP6 columns Km, kcat, kcat/Km. PMC article HTML preserves the Plant and Cell Physiology primary kinetic table. Table units are Km mM, kcat s^-1, and kcat/Km s^-1 M^-1; kcat/Km is normalized to s^-1 mM^-1 by dividing by 1000.

row_label: Bis-p-NPP / NPP6


column_label: Table label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6. Row: CDP. Enzyme column group: NPP2. Columns read: K m (mM) cell 1.9, k cat (s^-1) cell 89, k cat / K m (s^-1 M^-1) cell 0.47 x 10^5. metric: kcat; raw value: 89; raw unit: s^-1; normalized value: 89.0 s^(-1); metric: Km; raw value: 1.9; raw unit: mM; normalized value: 1.9 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 46.8421052631579 s^-1 mM^-1 derived as this row's kcat divided by Km; assay condition: Purified recombinant rice NPP1/NPP2/NPP6 from transgenic rice cells; the enzyme assay was carried out at a substrate concentration of 0.1-10 mM, at 37 C, and at optimal pH; the data give the averages of duplicate experiments; no mutation. Export row conditions: pH 4.5; 310.15 K.

normalized_value_unit_evidence: NPP2 columns of Table 2 row CDP: kcat 89 s^-1 = 89.0 s^(-1) (identity); Km 1.9 mM = 1.9 mM (identity); kcat/Km 46.8421052631579 s^-1 mM^-1 (quotient of this row's own kcat and Km cells, 89 / 1.9). The printed kcat/Km cell 0.47 x 10^5 s^-1 M^-1 divided by 1000 is 47 s^-1 mM^-1. In the flattened article HTML the multiplication sign renders as ×, superscript exponents and minus signs are flattened, and the header splits metric names, so the printed cell `0.47 × 10 5` is the paper's 0.47 x 10^5, `k cat (s −1 )` is kcat in s^-1, `K m (mM)` is Km in mM, and `k cat / K m (s −1 M −1 )` is kcat/Km in s^-1 M^-1.

raw_value_unit_evidence: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 | header row of Table 2: Substrates NPP1 NPP2 NPP6 K m (mM) V max (U mg −1 ) a k cat (s −1 ) k cat / K m (s −1 M −1 ) K m (mM) V max (U mg −1 ) k cat (s −1 ) k cat / K m (s −1 M −1 ) K m (mM) V max (U mg −1 ) k cat (s −1 ) k cat /K m (s −1 M −1 ) | row: CDP NT NT NT NT 1.9 76 89 0.47 × 10 5 NT NT NT NT | The four NPP2 cells of the CDP row read: K m = 1.9 mM; V max = 76 U mg^-1; k cat = 89 s^-1; k cat / K m = 0.47 x 10^5 s^-1 M^-1. NPP1 and NPP6 cells are NT (not tested).

row_label: NPP2 | CDP


column_label: Table 2, row 'PPi', NPP2 columns Km, kcat, kcat/Km. PMC article HTML preserves the Plant and Cell Physiology primary kinetic table. Table units are Km mM, kcat s^-1, and kcat/Km s^-1 M^-1; kcat/Km is normalized to s^-1 mM^-1 by dividing by 1000.

row_label: PPi / NPP2


column_label: Table label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6. Row: IDP. Enzyme column group: NPP2. Columns read: K m (mM) cell 2.2, k cat (s^-1) cell 88, k cat / K m (s^-1 M^-1) cell 0.40 x 10^5. metric: kcat; raw value: 88; raw unit: s^-1; normalized value: 88.0 s^(-1); metric: Km; raw value: 2.2; raw unit: mM; normalized value: 2.2 mM; metric: kcat/Km; raw value: 0.40 x 10^5; raw unit: s^-1 M^-1; normalized value: 40.0 s^-1 mM^-1; assay condition: Purified recombinant rice NPP1/NPP2/NPP6 from transgenic rice cells; the enzyme assay was carried out at a substrate concentration of 0.1-10 mM, at 37 C, and at optimal pH; the data give the averages of duplicate experiments; no mutation. Export row conditions: pH 4.5; 310.15 K.

normalized_value_unit_evidence: NPP2 columns of Table 2 row IDP: kcat 88 s^-1 = 88.0 s^(-1) (identity); Km 2.2 mM = 2.2 mM (identity); kcat/Km printed cell 0.40 x 10^5 s^-1 M^-1 divided by 1000 = 40.0 s^-1 mM^-1, which also equals the quotient of this row's own kcat and Km cells (88 / 2.2 = 40.0). In the flattened article HTML the multiplication sign renders as ×, superscript exponents and minus signs are flattened, and the header splits metric names, so the printed cell `0.47 × 10 5` is the paper's 0.47 x 10^5, `k cat (s −1 )` is kcat in s^-1, `K m (mM)` is Km in mM, and `k cat / K m (s −1 M −1 )` is kcat/Km in s^-1 M^-1.

raw_value_unit_evidence: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 | header row of Table 2: Substrates NPP1 NPP2 NPP6 K m (mM) V max (U mg −1 ) a k cat (s −1 ) k cat / K m (s −1 M −1 ) K m (mM) V max (U mg −1 ) k cat (s −1 ) k cat / K m (s −1 M −1 ) K m (mM) V max (U mg −1 ) k cat (s −1 ) k cat /K m (s −1 M −1 ) | row: IDP NT NT NT NT 2.2 75 88 0.40 × 10 5 NT NT NT NT | The four NPP2 cells of the IDP row read: K m = 2.2 mM; V max = 75 U mg^-1; k cat = 88 s^-1; k cat / K m = 0.40 x 10^5 s^-1 M^-1. NPP1 and NPP6 cells are NT (not tested).

row_label: NPP2 | IDP


column_label: Table 2, row 'TDP', NPP2 columns Km, kcat, kcat/Km. PMC article HTML preserves the Plant and Cell Physiology primary kinetic table. Table units are Km mM, kcat s^-1, and kcat/Km s^-1 M^-1; kcat/Km is normalized to s^-1 mM^-1 by dividing by 1000.

row_label: TDP / NPP2


column_label: Table 2, row 'UDP', NPP2 columns Km, kcat, kcat/Km. PMC article HTML preserves the Plant and Cell Physiology primary kinetic table. Table units are Km mM, kcat s^-1, and kcat/Km s^-1 M^-1; kcat/Km is normalized to s^-1 mM^-1 by dividing by 1000.

row_label: UDP / NPP2


substrate_name: UDP-glucose

column_label: Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row UDP-glucose / NPP1, column NPP1; kcat s^-1, raw cell 282, normalized 282 s^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row UDP-glucose / NPP1, column NPP1; kcat/Km s^-1 M^-1, raw cell 1.93 x 10^5, normalized 193 s^-1*mM^-1; Table 2. Kinetic parameters of NPP1, NPP2 and NPP6 row UDP-glucose / NPP1, column NPP1; Km mM, raw cell 1.5, normalized 1.5 mM

row_label: UDP-glucose / NPP1

substrate: UDP-glucose


organism: Thermus thermophilus

substrate_name: ADPribose

sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature L68A to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row L68A; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=5.93 s^-1; km paper=0.31 mM; kcat/Km paper=18.9 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row L68A: Km 0.31 +/- 0.03 mM; kcat 5.93 +/- 0.13 s^-1; kcat/Km 1.89 x 10^4 M^-1 s^-1.

substrate: ADPribose


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature Q52A to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row Q52A; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=6.74 s^-1; km paper=0.24 mM; kcat/Km paper=28.6 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row Q52A: Km 0.24 +/- 0.03 mM; kcat 6.74 +/- 0.24 s^-1; kcat/Km 2.86 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature R18Q to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row R18Q; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=17.05 s^-1; km paper=0.12 mM; kcat/Km paper=148 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row R18Q: Km 0.12 +/- 0.01 mM; kcat 17.05 +/- 0.22 s^-1; kcat/Km 1.48 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature R27Q to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row R27Q; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=12.90 s^-1; km paper=0.14 mM; kcat/Km paper=95.6 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row R27Q: Km 0.14 +/- 0.04 mM; kcat 12.90 +/- 0.22 s^-1; kcat/Km 9.56 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature R54Q to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row R54Q; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=0.0411 s^-1; km paper=0.65 mM; kcat/Km paper=0.0626 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row R54Q: Km 0.65 +/- 0.06 mM; kcat (4.11 +/- 0.10) x 10^-2 s^-1; kcat/Km 6.26 x 10 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature R81Q to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row R81Q; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=0.0350 s^-1; km paper=0.027 mM; kcat/Km paper=1.29 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row R81Q: Km (0.27 +/- 0.01) x 10^-1 mM; kcat (3.50 +/- 0.28) x 10^-2 s^-1; kcat/Km 1.29 x 10^3 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature S102A to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row S102A; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=2.43 s^-1; km paper=0.69 mM; kcat/Km paper=3.51 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row S102A: Km 0.69 +/- 0.04 mM; kcat 2.43 +/- 0.05 s^-1; kcat/Km 3.51 x 10^3 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature S153A to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row S153A; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=3.30 s^-1; km paper=0.10 mM; kcat/Km paper=34.4 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row S153A: Km 0.10 +/- 0.01 mM; kcat 3.30 +/- 0.06 s^-1; kcat/Km 3.44 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature T110A to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row T110A; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=2.65 s^-1; km paper=0.06 mM; kcat/Km paper=43.0 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row T110A: Km 0.06 +/- 0.01 mM; kcat 2.65 +/- 0.04 s^-1; kcat/Km 4.30 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature T155A to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row T155A; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=2.42 s^-1; km paper=0.05 mM; kcat/Km paper=52.5 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row T155A: Km 0.05 +/- 0.01 mM; kcat 2.42 +/- 0.03 s^-1; kcat/Km 5.25 x 10^4 M^-1 s^-1.


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

assay_conditions_summary: pH 7.63; 298.15 K; cofactor ADP


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature Y28Q to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row Y28Q; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=10.04 s^-1; km paper=0.40 mM; kcat/Km paper=25.1 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row Y28Q: Km 0.40 +/- 0.03 mM; kcat 10.04 +/- 0.21 s^-1; kcat/Km 2.51 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature Y99F to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row Y99F; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=3.32 s^-1; km paper=0.09 mM; kcat/Km paper=37.7 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row Y99F: Km 0.09 +/- 0.01 mM; kcat 3.32 +/- 0.04 s^-1; kcat/Km 3.77 x 10^4 M^-1 s^-1.


substrate_name: ADP alpha-D-glucoside

proof_lines: Thermus thermophilus ADP-ribose pyrophosphatase

substrate: ADP alpha-D-glucoside


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature E108Q to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row E108Q; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=2.97 s^-1; km paper=0.29 mM; kcat/Km paper=10.4 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row E108Q: Km 0.29 +/- 0.02 mM; kcat 2.97 +/- 0.05 s^-1; kcat/Km 1.04 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature E63Q to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row E63Q; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=0.23 s^-1; km paper=0.40 mM; kcat/Km paper=0.575 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row E63Q: Km 0.40 +/- 0.03 mM; kcat 0.23 +/- 0.01 s^-1; kcat/Km 5.75 x 10^2 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E70Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature E73Q to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row E73Q; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=2.07 s^-1; km paper=0.036 mM; kcat/Km paper=56.4 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row E73Q: Km (0.36 +/- 0.07) x 10^-1 mM; kcat 2.07 +/- 0.08 s^-1; kcat/Km 5.64 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E82Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature E85Q to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row E85Q; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=1.12 s^-1; km paper=0.043 mM; kcat/Km paper=25.9 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row E85Q: Km (0.43 +/- 0.06) x 10^-1 mM; kcat 1.12 +/- 0.03 s^-1; kcat/Km 2.59 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E86Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature H33A to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row H33A; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=4.16 s^-1; km paper=0.42 mM; kcat/Km paper=9.93 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row H33A: Km 0.42 +/- 0.06 mM; kcat 4.16 +/- 0.18 s^-1; kcat/Km 9.93 x 10^3 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q84CU3;embl_protein:BAC67698.1;pdb:1V8M and applied mutation signature I19A to reconstruct the assayed variant sequence.

column_label: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR; row I19A; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1), with kcat/Km normalized to s^-1*mM^-1.

normalized_value_unit_evidence: kcat paper=5.68 s^-1; km paper=1.24 mM; kcat/Km paper=4.58 s^-1*mM^-1

raw_value_unit_evidence: Table 1 | Kinetic Parameters of TtADPRase Mutants for ADPR, row I19A: Km 1.24 +/- 0.07 mM; kcat 5.68 +/- 0.23 s^-1; kcat/Km 4.58 x 10^3 M^-1 s^-1.


substrate_name: ADP-D-ribose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L98A to reconstruct the assayed variant sequence.

substrate: ADP-D-ribose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q82A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R111Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R196Q with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 310.15 K; cofactor ADP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R51Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R84Q with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W28A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W28A/W46A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W46A to reconstruct the assayed variant sequence.


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

column_label: Table 2. Kinetic parameters of wild-type and mutant hNUDT5; row Wild type; columns Km (uM), kcat (s^-1), kcat/Km (M^-1 s^-1); cells Km 22.3 +/- 2.2, kcat 11.8 +/- 0.1, kcat/Km 5.3 x 105.

normalized_value_unit_evidence: Km normalized_value=0.0223 normalized_unit=mM; kcat normalized_value=11.8 normalized_unit=s^-1; kcat/Km normalized_value=530 normalized_unit=s^-1 mM^-1.

row_label: Wild type


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C139A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D133A 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 D133N 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 D164A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D164N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E112Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E115Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E116Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E166Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E93Q to reconstruct the assayed variant sequence.


substrate_name: TTP

source_db: uniprot

proof_lines:
non-specific nucleoside triphosphatase
Walker A motif
Walker B motif

substrate: TTP

source: uniprot


enzyme_display_name: dCTP diphosphatase

column_label: Table 2. Kinetic parameters for nucleoside triphosphate pyrophosphohydrolase activity of RS21-C6 protein; row 5-Me-dCTP; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 M^-1); kcat 1.33 s^-1; Km 48.5 uM; kcat/Km 27400 s^-1 M^-1; normalized kcat 1.33 s^-1; Km 0.0485 mM; kcat/Km 27.4 s^-1*mM^-1

enzyme: dCTP diphosphatase


substrate_name: CTP

substrate: CTP


substrate_name: dATP

column_label: Table 2. Kinetic parameters for nucleoside triphosphate pyrophosphohydrolase activity of RS21-C6 protein; row dATP; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 M^-1); kcat 0.53 s^-1; Km 118 uM; kcat/Km 4490 s^-1 M^-1; normalized kcat 0.53 s^-1; Km 0.118 mM; kcat/Km 4.49 s^-1*mM^-1

row_label: dATP

substrate: dATP


substrate_name: dCTP

column_label: Table 2. Kinetic parameters for nucleoside triphosphate pyrophosphohydrolase activity of RS21-C6 protein; row dCTP; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 M^-1); kcat 1.37 s^-1; Km 44.1 uM; kcat/Km 31100 s^-1 M^-1; normalized kcat 1.37 s^-1; Km 0.0441 mM; kcat/Km 31.1 s^-1*mM^-1

row_label: dCTP

substrate: dCTP


substrate_name: dTTP

column_label: Table 2. Kinetic parameters for nucleoside triphosphate pyrophosphohydrolase activity of RS21-C6 protein; row dTTP; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 M^-1); kcat 0.76 s^-1; Km 407 uM; kcat/Km 1870 s^-1 M^-1; normalized kcat 0.76 s^-1; Km 0.407 mM; kcat/Km 1.87 s^-1*mM^-1

row_label: dTTP

substrate: dTTP


substrate_name: dUTP

column_label: Table 2. Kinetic parameters for nucleoside triphosphate pyrophosphohydrolase activity of RS21-C6 protein; row dUTP; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 M^-1); kcat 0.76 s^-1; Km 484 uM; kcat/Km 1570 s^-1 M^-1; normalized kcat 0.76 s^-1; Km 0.484 mM; kcat/Km 1.57 s^-1*mM^-1

row_label: dUTP

substrate: dUTP


organism: Thermotoga maritima

substrate_name: ATP

assay_conditions_summary: pH 8; 343.15 K; cofactor ATP

column_label: Table I row ATP; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table I row ATP: Km=1.0 ± 0.3 mM; kcat=11.82 ± 4.7 min^-1; explicit kcat/Km=11.9 min^-1 mM^-1.

row_label: ATP

table_label: Table I

substrate: ATP


column_label: Table I row CTP; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table I row CTP: Km=0.4 ± 0.1 mM; kcat=6.4 ± 1.0 min^-1; explicit kcat/Km=17.9 min^-1 mM^-1.

row_label: CTP


column_label: Table I row dATP; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table I row dATP: Km=3.2 ± 0.8 mM; kcat=67.2 ± 8.6 min^-1; explicit kcat/Km=20.9 min^-1 mM^-1.


column_label: Table I row dCTP; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table I row dCTP: Km=1.7 ± 0.1 mM; kcat=59.6 ± 2.1 min^-1; explicit kcat/Km=34.3 min^-1 mM^-1.


substrate_name: dGTP

column_label: Table I row dGTP; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table I row dGTP: Km=1.0 ± 0.3 mM; kcat=56.6 ± 3.5 min^-1; explicit kcat/Km=56.0 min^-1 mM^-1.

row_label: dGTP

substrate: dGTP


column_label: Table I row dTTP; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table I row dTTP: Km=1.5 ± 0.4 mM; kcat=38.7 ± 6.7 min^-1; explicit kcat/Km=26.5 min^-1 mM^-1.


substrate_name: GTP

column_label: Table I row GTP; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table I row GTP: Km=1.0 ± 0.1 mM; kcat=41.4 ± 3.2 min^-1; explicit kcat/Km=40.6 min^-1 mM^-1.

row_label: GTP

substrate: GTP


substrate_name: UTP

column_label: Table I row UTP; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table I row UTP: Km=1.1 ± 0.2 mM; kcat=10.6 ± 1.6 min^-1; explicit kcat/Km=9.8 min^-1 mM^-1.

row_label: UTP

substrate: UTP


enzyme_display_name: nucleoside-triphosphate phosphatase

substrate_name: ADP

assay_conditions_summary: pH 7; 298.15 K; cofactor ADP

column_label: table Table 2; row ADP; columns kcat, Km, kcat/Km; ScienceDirect Table 2 row ADP under columns Kcat x 10^-3, Km (uM), and Kcat/Km x 10^3.

enzyme: nucleoside-triphosphate phosphatase

substrate: ADP


assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

column_label: table Table 2; row ATP; columns kcat, Km, kcat/Km; ScienceDirect Table 2 row ATP under columns Kcat x 10^-3, Km (uM), and Kcat/Km x 10^3.


column_label: table Table 2; row CTP; columns kcat, Km, kcat/Km; ScienceDirect Table 2 row CTP under columns Kcat x 10^-3, Km (uM), and Kcat/Km x 10^3.


column_label: table Table 2; row TTP; columns kcat, Km, kcat/Km; ScienceDirect Table 2 row TTP under columns Kcat x 10^-3, Km (uM), and Kcat/Km x 10^3; package substrate is standardized as dTTP.


column_label: table Table 2; row GTP; columns kcat, Km, kcat/Km; ScienceDirect Table 2 row GTP under columns Kcat x 10^-3, Km (uM), and Kcat/Km x 10^3.


column_label: table Table 2; row UTP; columns kcat, Km, kcat/Km; ScienceDirect Table 2 row UTP under columns Kcat x 10^-3, Km (uM), and Kcat/Km x 10^3.


assay_conditions_summary: pH 7; buffer methods; cofactor ATP

column_label: ScienceDirect full-text HTML Table 2, row ATP, Km column = 5 +/- 1 uM.

raw_value_unit_evidence: Table 2 ATP row, Km column = 5 +/- 1 uM.


assay_conditions_summary: pH 7; buffer methods; cofactor ADP

column_label: ScienceDirect full-text HTML Table 2, row ADP, Km column = 46 +/- 16 uM.

raw_value_unit_evidence: Table 2 ADP row, Km column = 46 +/- 16 uM.

row_label: ADP


assay_conditions_summary: pH 7; buffer methods

column_label: ScienceDirect full-text HTML Table 2, row GTP, Km column = 4 +/- 1 uM.

raw_value_unit_evidence: Table 2 GTP row, Km column = 4 +/- 1 uM.


column_label: ScienceDirect full-text HTML Table 2, row CTP, Km column = 6 +/- 1 uM.

raw_value_unit_evidence: Table 2 CTP row, Km column = 6 +/- 1 uM.


enzyme_display_name: UniProt Q9H773

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

sequence_source: multiple

normalized_value_unit_evidence: Km normalized_value=0.0092 normalized_unit=mM; kcat normalized_value=3.0 normalized_unit=s^-1; kcat/Km normalized_value=322 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=9.2 +/- 0.3 raw_unit=uM; kcat raw_value=3.0 +/- 0.1 raw_unit=s^-1; kcat/Km raw_value=322000 raw_unit=s^-1*M^-1

table_label: Figure 2. Kinetic parameters for the NTP pyrophosphohydrolase reaction

source_databases_merged: brenda skid

enzyme: UniProt Q9H773


normalized_value_unit_evidence: Km normalized_value=0.0365 normalized_unit=mM; kcat normalized_value=9.3 normalized_unit=s^-1; kcat/Km normalized_value=256 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=36.5 +/- 2.7 raw_unit=uM; kcat raw_value=9.3 +/- 0.8 raw_unit=s^-1; kcat/Km raw_value=256000 raw_unit=s^-1*M^-1


column_label: Figure 2 row 5hme-dCTP; columns kcat s^-1, Km uM, kcat/Km s^-1*M^-1; raw cells 5.6 +/- 0.1, 62.9 +/- 0.7, 90000; normalized cells 5.6 s^-1, 0.0629 mM, 90 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.0629 normalized_unit=mM; kcat normalized_value=5.6 normalized_unit=s^-1; kcat/Km normalized_value=90 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=62.9 +/- 0.7 raw_unit=uM; kcat raw_value=5.6 +/- 0.1 raw_unit=s^-1; kcat/Km raw_value=90000 raw_unit=s^-1*M^-1


normalized_value_unit_evidence: Km normalized_value=0.0168 normalized_unit=mM; kcat normalized_value=6.2 normalized_unit=s^-1; kcat/Km normalized_value=371 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=16.8 +/- 5.25 raw_unit=uM; kcat raw_value=6.2 +/- 1.0 raw_unit=s^-1; kcat/Km raw_value=371000 raw_unit=s^-1*M^-1


normalized_value_unit_evidence: Km normalized_value=0.0333 normalized_unit=mM; kcat normalized_value=4.8 normalized_unit=s^-1; kcat/Km normalized_value=143 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=33.3 +/- 4.4 raw_unit=uM; kcat raw_value=4.8 +/- 0.4 raw_unit=s^-1; kcat/Km raw_value=143000 raw_unit=s^-1*M^-1


normalized_value_unit_evidence: Km normalized_value=0.0793 normalized_unit=mM; kcat normalized_value=2.0 normalized_unit=s^-1; kcat/Km normalized_value=25 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=79.3 +/- 6.9 raw_unit=uM; kcat raw_value=2.0 +/- 0.1 raw_unit=s^-1; kcat/Km raw_value=25000 raw_unit=s^-1*M^-1


normalized_value_unit_evidence: Km normalized_value=0.0476 normalized_unit=mM; kcat normalized_value=5.7 normalized_unit=s^-1; kcat/Km normalized_value=119 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=47.6 +/- 2.7 raw_unit=uM; kcat raw_value=5.7 +/- 0.2 raw_unit=s^-1; kcat/Km raw_value=119000 raw_unit=s^-1*M^-1


column_label: Figure 2 row dTTP; columns kcat s^-1, Km uM, kcat/Km s^-1*M^-1; raw cells 1.8 +/- 0.1, 65.0 +/- 3.9, 28000; normalized cells 1.8 s^-1, 0.065 mM, 28 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.065 normalized_unit=mM; kcat normalized_value=1.8 normalized_unit=s^-1; kcat/Km normalized_value=28 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=65.0 +/- 3.9 raw_unit=uM; kcat raw_value=1.8 +/- 0.1 raw_unit=s^-1; kcat/Km raw_value=28000 raw_unit=s^-1*M^-1


enzyme_display_name: dCTP pyrophosphatase 1

substrate_name: CTP (at pH 8.0 and 25 degrees Celsius)

assay_conditions_summary: pH 8; cofactor ATP

enzyme: dCTP pyrophosphatase 1

substrate: CTP (at pH 8.0 and 25 degrees Celsius)


enzyme_display_name: CDP-glycerol diphosphatase

substrate_name: CDPglycerol

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP

enzyme: CDP-glycerol diphosphatase

substrate: CDPglycerol


substrate_name: ADP-ribose

assay_conditions_summary: cofactor ADP

substrate: ADP-ribose


substrate_name: CDP-choline

substrate: CDP-choline


substrate_name: CDP-ethanolamine

substrate: CDP-ethanolamine


substrate_name: CDP-glycerol

substrate: CDP-glycerol


enzyme_display_name: UniProt O66548

organism: Aquifex aeolicus

substrate_name: P1,P6-bis(5'-adenosyl) hexaphosphate

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt O66548

substrate: P1,P6-bis(5'-adenosyl) hexaphosphate

source: skid


substrate_name: P1,P5-bis(5'-adenosyl) pentaphosphate

substrate: P1,P5-bis(5'-adenosyl) pentaphosphate


substrate_name: P1,P4-bis(5'-adenosyl) tetraphosphate

substrate: P1,P4-bis(5'-adenosyl) tetraphosphate


enzyme_display_name: UniProt Q9U2M7

organism: Caenorhabditis elegans

enzyme: UniProt Q9U2M7


substrate_name: dATP

substrate: dATP


organism: Triticum aestivum

substrate_name: NAD(+)

substrate: NAD(+)


substrate_name: NADH

substrate: NADH


substrate_name: NADP(+)

substrate: NADP(+)


substrate_name: NADPH

substrate: NADPH


substrate_name: ATP

substrate: ATP


substrate_name: CTP

substrate: CTP


substrate_name: GTP

substrate: GTP


substrate_name: TTP

substrate: TTP


enzyme_display_name: UniProt P03195

organism: Human gammaherpesvirus 4

substrate_name: dUTP

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

enzyme: UniProt P03195

substrate: dUTP


enzyme_display_name: UniProt P33317

organism: Saccharomyces cerevisiae

substrate_name: UTP

enzyme: UniProt P33317

substrate: UTP


enzyme_display_name: UniProt Q77J78

organism: white spot syndrome virus

enzyme: UniProt Q77J78


enzyme_display_name: UniProt P9WNS5

organism: Mycobacterium tuberculosis

enzyme: UniProt P9WNS5


enzyme_display_name: UniProt A0A2X0SE53

organism: African swine fever virus

enzyme: UniProt A0A2X0SE53


enzyme_display_name: UniProt Q9STG6

organism: Arabidopsis thaliana

enzyme: UniProt Q9STG6


enzyme_display_name: S-methyl-5'-thioadenosine deaminase

organism: Methanocaldococcus jannaschii

substrate_name: adenosine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q58936 and applied mutation signature E150R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9; 333.15 K; buffer the Bis-Tris propane

column_label: Table 2: Kinetic parameters of DadD and mutants with 5'-dA, MTA, SAH, and Ad (Journal of Bacteriology 2014, 196(5):1064-1072), DadD E150R block, substrate row 'Ad'; column 'Mean Km (mM) +/- SD' = 0.15 +/- 0.047; column 'kcat (s^-1)' = 1.1 x 10^2; column 'kcat/Km (M^-1 s^-1)' = 7.5 x 10^5.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.15 mM; the column head prints mM, so no unit conversion applies; the paper value is 0.15 mM. kcat: printed Table 2 cell 1.1 x 10^2 s^-1 = 110 s^-1; the column head prints s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 7.5 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 750000 / 1000 = 750 s^(-1)*mM^(-1).

row_label: Table 2, DadD E150R block, Ad row

enzyme: S-methyl-5'-thioadenosine deaminase

substrate: adenosine


column_label: Table 2 row WT / Ad; columns Mean Km (mM) +/- SD, kcat (s^-1), kcat/Km (M^-1 s^-1)

row_label: WT; substrate Ad


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q58936 and applied mutation signature Y136R to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of DadD and mutants with 5'-dA, MTA, SAH, and Ad (Journal of Bacteriology 2014, 196(5):1064-1072), DadD Y136R block, substrate row 'Ad'; column 'Mean Km (mM) +/- SD' = 0.072 +/- 0.0018; column 'kcat (s^-1)' = 1.4 x 10^2; column 'kcat/Km (M^-1 s^-1)' = 2.9 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.072 mM; the column head prints mM, so no unit conversion applies; the paper value is 0.07199999999999999 mM. kcat: printed Table 2 cell 1.4 x 10^2 s^-1 = 140 s^-1; the column head prints s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 2.9 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2900000 / 1000 = 2900 s^(-1)*mM^(-1).

row_label: Table 2, DadD Y136R block, Ad row


column_label: Table 2: Kinetic parameters of DadD and mutants with 5'-dA, MTA, SAH, and Ad (Journal of Bacteriology 2014, 196(5):1064-1072), DadD E150R block, substrate row 'MTA'; column 'Mean Km (mM) +/- SD' = 0.048 +/- 0.0029; column 'kcat (s^-1)' = 2.0 x 10^2; column 'kcat/Km (M^-1 s^-1)' = 4.2 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.048 mM; the column head prints mM, so no unit conversion applies; the paper value is 0.048 mM. kcat: printed Table 2 cell 2.0 x 10^2 s^-1 = 200 s^-1; the column head prints s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 4.2 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4200000 / 1000 = 4200 s^(-1)*mM^(-1).

row_label: Table 2, DadD E150R block, MTA row


column_label: Table 2 row WT / MTA; columns Mean Km (mM) +/- SD, kcat (s^-1), kcat/Km (M^-1 s^-1)

row_label: WT; substrate MTA


column_label: Table 2: Kinetic parameters of DadD and mutants with 5'-dA, MTA, SAH, and Ad (Journal of Bacteriology 2014, 196(5):1064-1072), DadD Y136R block, substrate row 'MTA'; column 'Mean Km (mM) +/- SD' = 0.022 +/- 0.0019; column 'kcat (s^-1)' = 2.2 x 10^2; column 'kcat/Km (M^-1 s^-1)' = 1.1 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.022 mM; the column head prints mM, so no unit conversion applies; the paper value is 0.022 mM. kcat: printed Table 2 cell 2.2 x 10^2 s^-1 = 220 s^-1; the column head prints s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 1.1 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 11000000 / 1000 = 11000 s^(-1)*mM^(-1).

row_label: Table 2, DadD Y136R block, MTA row


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q58936 and applied mutation signature Y136R/E150R to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of DadD and mutants with 5'-dA, MTA, SAH, and Ad (Journal of Bacteriology 2014, 196(5):1064-1072), DadD Y136R/E150R block, substrate row 'MTA'; column 'Mean Km (mM) +/- SD' = 0.073 +/- 0.0054; column 'kcat (s^-1)' = 1.39; column 'kcat/Km (M^-1 s^-1)' = 1.9 x 10^4.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.073 mM; the column head prints mM, so no unit conversion applies; the paper value is 0.073 mM. kcat: printed Table 2 cell 1.39 s^-1 = 1.39 s^-1; the column head prints s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 1.9 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 19000 / 1000 = 19 s^(-1)*mM^(-1).

row_label: Table 2, DadD Y136R/E150R block, MTA row


enzyme_display_name: UniProt Q9QY93

column_label: Table 2. Kinetic parameters for nucleoside triphosphate pyrophosphohydrolase activity of RS21-C6 protein; row dUTP; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 M^-1); kcat 0.76 s^-1; Km 484 uM; kcat/Km 1570 s^-1 M^-1; normalized kcat 0.76 s^-1; Km 0.484 mM; kcat/Km 1.57 s^-1*mM^-1

enzyme: UniProt Q9QY93


column_label: Table 2. Kinetic parameters for nucleoside triphosphate pyrophosphohydrolase activity of RS21-C6 protein; row 2-OH-dATP; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 M^-1); kcat 1.39 s^-1; Km 169 uM; kcat/Km 8220 s^-1 M^-1; normalized kcat 1.39 s^-1; Km 0.169 mM; kcat/Km 8.22 s^-1*mM^-1


column_label: Table 2. Kinetic parameters for nucleoside triphosphate pyrophosphohydrolase activity of RS21-C6 protein; row 2-Cl-dATP; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 M^-1); kcat 1.57 s^-1; Km 107 uM; kcat/Km 14700 s^-1 M^-1; normalized kcat 1.57 s^-1; Km 0.107 mM; kcat/Km 14.7 s^-1*mM^-1


table_label: Table 2. Kinetic parameters for nucleoside triphosphate pyrophosphohydrolase activity of RS21-C6 protein


column_label: Table 2. Kinetic parameters for nucleoside triphosphate pyrophosphohydrolase activity of RS21-C6 protein; row 5-Br-dCTP; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 M^-1); kcat 1.49 s^-1; Km 21.7 uM; kcat/Km 68700 s^-1 M^-1; normalized kcat 1.49 s^-1; Km 0.0217 mM; kcat/Km 68.7 s^-1*mM^-1


column_label: Table 2. Kinetic parameters for nucleoside triphosphate pyrophosphohydrolase activity of RS21-C6 protein; row 5-Cl-dCTP; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 M^-1); kcat 1.50 s^-1; Km 50.0 uM; kcat/Km 30000 s^-1 M^-1; normalized kcat 1.5 s^-1; Km 0.05 mM; kcat/Km 30 s^-1*mM^-1


column_label: Table 2. Kinetic parameters for nucleoside triphosphate pyrophosphohydrolase activity of RS21-C6 protein; row 5-F-dUTP; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 M^-1); kcat 0.58 s^-1; Km 304 uM; kcat/Km 1900 s^-1 M^-1; normalized kcat 0.58 s^-1; Km 0.304 mM; kcat/Km 1.9 s^-1*mM^-1


column_label: Table 2. Kinetic parameters for nucleoside triphosphate pyrophosphohydrolase activity of RS21-C6 protein; row 5-OH-dCTP; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 M^-1); kcat 0.87 s^-1; Km 164 uM; kcat/Km 5300 s^-1 M^-1; normalized kcat 0.87 s^-1; Km 0.164 mM; kcat/Km 5.3 s^-1*mM^-1


column_label: Table 2. Kinetic parameters for nucleoside triphosphate pyrophosphohydrolase activity of RS21-C6 protein; row 5-I-dCTP; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 M^-1); kcat 0.94 s^-1; Km 3.9 uM; kcat/Km 241000 s^-1 M^-1; normalized kcat 0.94 s^-1; Km 0.0039 mM; kcat/Km 241 s^-1*mM^-1


enzyme_display_name: nucleotide diphosphatase

verification_status: disputed

enzyme: nucleotide diphosphatase

status: disputed


substrate_name: dGTP

substrate: dGTP


substrate_name: dTTP

substrate: dTTP


substrate_name: ITP

column_label: Table 2: Kinetic parameters of Mj0226 with various nucleotides (Nature Structural Biology 1999, volume 6, pages 691-696); printed column heads Kcat (s-1) | Km (mM) | Kcat / Km, the efficiency column carrying the quotient unit s-1 mM-1 of its two component heads. Table 2, row ITP; column Kcat (s-1) = 911.72; column Km (mM) = 0.15; column Kcat / Km = 5998.16. captured primary segment: ITP | Kcat 911.72 s-1 | Km 0.15 mM | Kcat / Km 5998.16 s-1 mM-1

normalized_value_unit_evidence: Kcat: printed Table 2 cell 911.72 s-1; the column head prints s-1, so no unit conversion applies and the paper value is 911.72 s^(-1); the exported value is 911.72 s^(-1). Km: printed Table 2 cell 0.15 mM; the column head prints mM, so no unit conversion applies and the paper value is 0.15 mM; the exported value is 0.15 mM. Kcat / Km: printed Table 2 cell 5998.16; the efficiency column is the quotient of the s-1 and mM columns, so its unit is s-1 mM-1 and the printed cell is 5998.16 s^(-1)*mM^(-1) with no unit conversion; the exported value 6078.133333333334 s^(-1)*mM^(-1) is the quotient 911.72 / 0.15 = 6078.133333333333 of the two printed component cells, whereas the paper's own printed efficiency cell is 5998.16; the printed cell governs and kcat_over_km is corrected to 5998.16 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row ITP: Kcat = 911.72 s-1; Km = 0.15 mM; printed Kcat / Km = 5998.16 (the efficiency head carries the quotient unit s-1 mM-1 of the Kcat (s-1) and Km (mM) heads).

row_label: Table 2, row ITP

substrate: ITP


substrate_name: XTP

column_label: Table 2: Kinetic parameters of Mj0226 with various nucleotides (Nature Structural Biology 1999, volume 6, pages 691-696); printed column heads Kcat (s-1) | Km (mM) | Kcat / Km, the efficiency column carrying the quotient unit s-1 mM-1 of its two component heads. Table 2, row XTP; column Kcat (s-1) = 1009.37; column Km (mM) = 0.10; column Kcat / Km = 10195.66. captured primary segment: XTP | Kcat 1009.37 s-1 | Km 0.10 mM | Kcat / Km 10195.66 s-1 mM-1

normalized_value_unit_evidence: Kcat: printed Table 2 cell 1009.37 s-1; the column head prints s-1, so no unit conversion applies and the paper value is 1009.37 s^(-1); the exported value is 1009.37 s^(-1). Km: printed Table 2 cell 0.10 mM; the column head prints mM, so no unit conversion applies and the paper value is 0.1 mM; the exported value is 0.1 mM. Kcat / Km: printed Table 2 cell 10195.66; the efficiency column is the quotient of the s-1 and mM columns, so its unit is s-1 mM-1 and the printed cell is 10195.66 s^(-1)*mM^(-1) with no unit conversion; the exported value 10093.699999999999 s^(-1)*mM^(-1) is the quotient 1009.37 / 0.10 = 10093.7 of the two printed component cells, whereas the paper's own printed efficiency cell is 10195.66; the printed cell governs and kcat_over_km is corrected to 10195.66 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row XTP: Kcat = 1009.37 s-1; Km = 0.10 mM; printed Kcat / Km = 10195.66 (the efficiency head carries the quotient unit s-1 mM-1 of the Kcat (s-1) and Km (mM) heads).

row_label: Table 2, row XTP

substrate: XTP


enzyme_display_name: 5'/3'-nucleotidase SurE

organism: Escherichia coli (strain K12)

column_label: JBC full-text kinetic parameter table; SurE row for 5'-AMP with Mn2+; column Km (mM).

normalized_value_unit_evidence: normalized Km=0.32 mM; export Km=0.32 mM.

raw_value_unit_evidence: JBC full-text table row SurE, 5'-AMP, Mn2+; column Km = 0.32 +/- 0.04 mM.

row_label: SurE / 5'-AMP / Mn2+

table_label: JBC full-text kinetic parameter table

enzyme: 5'/3'-nucleotidase SurE


column_label: JBC full-text kinetic parameter table; SurE row for 5'-GMP with Mn2+; column Km (mM).

normalized_value_unit_evidence: normalized Km=0.26 mM; export Km=0.26 mM.

raw_value_unit_evidence: JBC full-text table row SurE, 5'-GMP, Mn2+; column Km = 0.26 +/- 0.05 mM.

row_label: SurE / 5'-GMP / Mn2+


column_label: JBC full-text kinetic parameter table; SurE row for 5'-dGMP with Mn2+; column Km (mM).

normalized_value_unit_evidence: normalized Km=0.28 mM; export Km=0.28 mM.

raw_value_unit_evidence: JBC full-text table row SurE, 5'-dGMP, Mn2+; column Km = 0.28 +/- 0.04 mM.

row_label: SurE / 5'-dGMP / Mn2+


column_label: JBC full-text kinetic parameter table; SurE row for 3'-AMP with Mn2+; column Km (mM).

normalized_value_unit_evidence: normalized Km=0.10 mM; export Km=0.1 mM.

raw_value_unit_evidence: JBC full-text table row SurE, 3'-AMP, Mn2+; column Km = 0.10 +/- 0.01 mM.

row_label: SurE / 3'-AMP / Mn2+


column_label: JBC full-text kinetic parameter table; SurE row for 3'-CMP with Mn2+; column Km (mM).

normalized_value_unit_evidence: normalized Km=0.37 mM; export Km=0.37 mM.

raw_value_unit_evidence: JBC full-text table row SurE, 3'-CMP, Mn2+; column Km = 0.37 +/- 0.08 mM.

row_label: SurE / 3'-CMP / Mn2+


substrate_name: pNPP

column_label: JBC full-text kinetic parameter table; SurE row for pNPP with Mn2+; column Km (mM).

normalized_value_unit_evidence: normalized Km=2.49 mM; export Km=2.49 mM.

raw_value_unit_evidence: JBC full-text table row SurE, pNPP, Mn2+; column Km = 2.49 +/- 0.47 mM.

row_label: SurE / pNPP / Mn2+

substrate: pNPP


enzyme_display_name: ADP-ribose diphosphatase

substrate_name: ADPribose

assay_conditions_summary: pH 8; 310.15 K; cofactor ADP

column_label: JBC PMID 15878881 Table 2 - kinetic parameters of Arabidopsis cytosolic Nudix hydrolases; row ADP-ribose / AtNUDT10; columns Km=27.4 +/- 2.1 uM, kcat=0.06 s^-1, kcat/Km=6.3 x 10^2 s^-1 M^-1.

normalized_value_unit_evidence: km normalized_value=0.0274 normalized_unit=mM; kcat normalized_value=0.06 normalized_unit=s^-1; kcat/Km normalized_value=0.63 normalized_unit=s^-1*mM^-1; current_export_kcat=0.06 s^-1; current_export_kcat_over_km=2.2222222222222223 s^-1*mM^-1; current_export_km=0.027 mM

raw_value_unit_evidence: Km raw_value=27.4 +/- 2.1 raw_unit=uM; kcat raw_value=0.06 raw_unit=s^-1; kcat/Km raw_value=6.3 x 10^2 raw_unit=s^-1 M^-1

row_label: ADP-ribose / AtNUDT10

enzyme: ADP-ribose diphosphatase

substrate: ADPribose


column_label: JBC PMID 15878881 Table 2 - kinetic parameters of Arabidopsis cytosolic Nudix hydrolases; row ADP-ribose / AtNUDT2; columns Km=16.9 +/- 2.3 uM, kcat=0.12 s^-1, kcat/Km=7.0 x 10^3 s^-1 M^-1.

normalized_value_unit_evidence: km normalized_value=0.0169 normalized_unit=mM; kcat normalized_value=0.12 normalized_unit=s^-1; kcat/Km normalized_value=7 normalized_unit=s^-1*mM^-1; current_export_kcat=0.12 s^-1; current_export_kcat_over_km=7.058823529411764 s^-1*mM^-1; current_export_km=0.017 mM

raw_value_unit_evidence: Km raw_value=16.9 +/- 2.3 raw_unit=uM; kcat raw_value=0.12 raw_unit=s^-1; kcat/Km raw_value=7.0 x 10^3 raw_unit=s^-1 M^-1

row_label: ADP-ribose / AtNUDT2


column_label: JBC PMID 15878881 Table 2 - kinetic parameters of Arabidopsis cytosolic Nudix hydrolases; row ADP-ribose / AtNUDT6; columns Km=23.0 +/- 0.9 uM, kcat=0.11 s^-1, kcat/Km=4.6 x 10^3 s^-1 M^-1.

normalized_value_unit_evidence: km normalized_value=0.023 normalized_unit=mM; kcat normalized_value=0.11 normalized_unit=s^-1; kcat/Km normalized_value=4.6 normalized_unit=s^-1*mM^-1; current_export_kcat=0.11 s^-1; current_export_kcat_over_km=4.782608695652174 s^-1*mM^-1; current_export_km=0.023 mM

raw_value_unit_evidence: Km raw_value=23.0 +/- 0.9 raw_unit=uM; kcat raw_value=0.11 raw_unit=s^-1; kcat/Km raw_value=4.6 x 10^3 raw_unit=s^-1 M^-1

row_label: ADP-ribose / AtNUDT6


column_label: JBC PMID 15878881 Table 2 - kinetic parameters of Arabidopsis cytosolic Nudix hydrolases; row ADP-ribose / AtNUDT7; columns Km=23.2 +/- 6.3 uM, kcat=0.12 s^-1, kcat/Km=5.3 x 10^3 s^-1 M^-1.

normalized_value_unit_evidence: km normalized_value=0.0232 normalized_unit=mM; kcat normalized_value=0.12 normalized_unit=s^-1; kcat/Km normalized_value=5.3 normalized_unit=s^-1*mM^-1; current_export_kcat=0.12 s^-1; current_export_kcat_over_km=5.217391304347826 s^-1*mM^-1; current_export_km=0.023 mM

raw_value_unit_evidence: Km raw_value=23.2 +/- 6.3 raw_unit=uM; kcat raw_value=0.12 raw_unit=s^-1; kcat/Km raw_value=5.3 x 10^3 raw_unit=s^-1 M^-1

row_label: ADP-ribose / AtNUDT7


enzyme_display_name: Nudix hydrolase 6

substrate_name: ADP-ribose

column_label: JBC PMID 15878881 Table 2 - kinetic parameters of Arabidopsis cytosolic Nudix hydrolases; row ADP-ribose / AtNUDT6; columns Km=23.0 +/- 0.9 uM.

normalized_value_unit_evidence: km normalized_value=0.023 normalized_unit=mM; current_export_km=0.023 mM

raw_value_unit_evidence: Km raw_value=23.0 +/- 0.9 raw_unit=uM

enzyme: Nudix hydrolase 6

substrate: ADP-ribose


substrate_name: NADH

column_label: JBC PMID 15878881 Table 2 - kinetic parameters of Arabidopsis cytosolic Nudix hydrolases; row NADH / AtNUDT6; columns Km=13.7 +/- 0.4 uM.

normalized_value_unit_evidence: km normalized_value=0.0137 normalized_unit=mM; current_export_km=0.0137 mM

raw_value_unit_evidence: Km raw_value=13.7 +/- 0.4 raw_unit=uM

row_label: NADH / AtNUDT6

substrate: NADH


organism: Homo sapiens

column_label: Figure 1c row MTH1, substrate 8-oxo-dGTP, columns kcat, Km, and kcat/Km.

row_label: MTH1 / 8-oxo-dGTP

table_label: Figure 1c kinetic parameters


column_label: Figure 1c row NUDT15, substrate 8-oxo-dGTP, columns kcat, Km, and kcat/Km.

row_label: NUDT15 / 8-oxo-dGTP


column_label: Figure 1c row MTH1, substrate dGTP, columns kcat, Km, and kcat/Km.

row_label: MTH1 / dGTP


column_label: Figure 1c row NUDT15, substrate dGTP, columns kcat, Km, and kcat/Km.

row_label: NUDT15 / dGTP


assay_conditions_summary: pH 9; 310.15 K; cofactor ATP

column_label: Substrate Specificity paragraph, ATP entry, metric labels kcat and Km; no printed kcat/Km column

raw_value_unit_evidence: Results prose: ATP kcat=16 s^-1 and Km=46 uM

row_label: ATP substrate in kinetic-analysis prose

table_label: PNAS/PMC Results section: Substrate Specificity


column_label: Substrate Specificity paragraph, CTP entry, metric labels kcat and Km; no printed kcat/Km column

normalized_value_unit_evidence: Km=1.2 mM; kcat=8.7 s^-1; kcat/Km=7.25 s^-1 mM^-1 calculated from 8.7/1.2

raw_value_unit_evidence: Results prose: CTP kcat=8.7 s^-1 and Km=1.2 mM

row_label: CTP substrate in kinetic-analysis prose


column_label: Substrate Specificity paragraph, GTP entry, metric labels kcat and Km; no printed kcat/Km column

raw_value_unit_evidence: Results prose: GTP kcat=820 s^-1 and Km=4.2 mM

row_label: GTP substrate in kinetic-analysis prose


column_label: Substrate Specificity paragraph, UTP entry, metric labels kcat and Km; no printed kcat/Km column

raw_value_unit_evidence: Results prose: UTP kcat=200 s^-1 and Km=4.3 mM

row_label: UTP substrate in kinetic-analysis prose


organism: Dictyostelium discoideum


substrate_name: AMPPCP

substrate: AMPPCP


substrate_name: Formycin 5'-triphosphate

substrate: Formycin 5'-triphosphate


substrate_name: UDP-N-acetyl-alpha-D-glucosamine

substrate: UDP-N-acetyl-alpha-D-glucosamine


enzyme_display_name: glucosamine-6-phosphate deaminase

organism: Giardia duodenalis

substrate_name: D-glucosamine 6-phosphate

enzyme: glucosamine-6-phosphate deaminase

substrate: D-glucosamine 6-phosphate


substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


enzyme_display_name: UniProt O95989

enzyme: UniProt O95989


enzyme_display_name: UniProt Q8NFP7

enzyme: UniProt Q8NFP7


enzyme_display_name: UniProt P0A776

organism: Escherichia coli

enzyme: UniProt P0A776


enzyme_display_name: UniProt Q96DE0

substrate_name: ADP

enzyme: UniProt Q96DE0

substrate: ADP


organism: Thermus thermophilus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D126N with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E127Q to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E129Q to reconstruct the assayed variant sequence.


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

substrate_name: S-adenosyl-L-homocysteine

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

assay_conditions_summary: pH 8

column_label: Table 2 row S-adenosyl-L-homocysteine, column Km (uM), gives 210 +/- 40 uM; Figure S3 repeats Km=(0.21 +/- 0.04) mM for SAH.

raw_value_unit_evidence: Km raw=210 +/- 40 uM; Table 2 also gives kcat 12.2 +/- 0.8 s^-1 and kcat/Km 5.8 x 10^4 M^-1 s^-1 for the same row.

row_label: S-adenosyl-L-homocysteine

table_label: Table 2: Docking ranks and Tm0936 catalytic constants for five predicted substrates

substrate: S-adenosyl-L-homocysteine


column_label: Table 2 row 5-Methyl-thioadenosine, column Km (uM), gives 44 +/- 4 uM; Figure S3 repeats Km=(44 +/- 4) uM for MTA at pH 8.0 and 30 C.

raw_value_unit_evidence: Km raw=44 +/- 4 uM; Table 2 also gives kcat 7.2 +/- 0.2 s^-1 and kcat/Km 1.4 x 10^5 M^-1 s^-1 for the same row.


column_label: Table 2 row Adenosine, column Km (uM), gives 250 +/- 40 uM; Figure S3 repeats Km=(0.25 +/- 0.04) mM for adenosine at pH 8.0 and 30 C.

raw_value_unit_evidence: Km raw=250 +/- 40 uM; Table 2 also gives kcat 2.3 +/- 0.2 s^-1 and kcat/Km 9.2 x 10^3 M^-1 s^-1 for the same row.

row_label: Adenosine


enzyme_display_name: diadenosine hexaphosphate hydrolase (ATP-forming)

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


enzyme: diadenosine hexaphosphate hydrolase (ATP-forming)


enzyme_display_name: diadenosine hexaphosphate hydrolase (AMP-forming)


enzyme: diadenosine hexaphosphate hydrolase (AMP-forming)


organism: Orthopoxvirus vaccinia


substrate_name: XDP

proof_lines: kcat is 0.931 sec(-1) with IDP. kcat is 0.966 sec(-1) with dIDP. kcat is 0.518 sec(-1) with GDP. kcat is 0.492 sec(-1) with dGDP. kcat is 2.6 sec(-1) with XDP. kcat is 3.06 sec(-1) with ITP. kcat is 3.2 sec(-1) with dITP. The catalytic effi

source_databases_merged: skid uniprot

substrate: XDP


enzyme_display_name: U8 snoRNA-decapping enzyme

substrate_name: IDP (at 37 degrees Celsius)

assay_conditions_summary: pH 7.5; buffer reaction

column_label: Table 1; row IDP; column Km (uM) raw value 0.062

raw_value_unit_evidence: Km raw_value=0.062 raw_unit=uM

row_label: IDP

table_label: Table 1. Kinetic parameters of His-NUDT16

enzyme: U8 snoRNA-decapping enzyme

substrate: IDP (at 37 degrees Celsius)


substrate_name: dIDP (at 37 degrees Celsius)

column_label: Table 1; row dIDP; column Km (uM) raw value 0.088

raw_value_unit_evidence: Km raw_value=0.088 raw_unit=uM

row_label: dIDP

substrate: dIDP (at 37 degrees Celsius)


substrate_name: GDP (at 37 degrees Celsius)

column_label: Table 1; row GDP; column Km (uM) raw value 0.33

raw_value_unit_evidence: Km raw_value=0.33 raw_unit=uM

row_label: GDP

substrate: GDP (at 37 degrees Celsius)


substrate_name: dGDP (at 37 degrees Celsius)

column_label: Table 1. Kinetic parameters of His-NUDT16; row dGDP; Km 0.319 uM; normalized: km 0.000319 mM

row_label: dGDP

substrate: dGDP (at 37 degrees Celsius)


substrate_name: dITP (at 37 degrees Celsius)

column_label: Table 1. Kinetic parameters of His-NUDT16; row dITP; Km 24.1 uM; normalized: km 0.0241 mM

raw_value_unit_evidence: Km 24.1 uM

row_label: dITP

substrate: dITP (at 37 degrees Celsius)


enzyme_display_name: 8-oxo-dGDP phosphatase NUDT18

proof_lines: kcat is 0.78 sec(-1) for (2E)-geranyl diphosphate as substrate (at pH 8.0 and 22 degrees Celsius) (PubMed:38944687). kcat is 0.55 sec(-1) with (R)-5-diphosphomevalonate as substrate (at pH 8.0 and 22 degrees Celsius) (PubMed:38944687). kcat

enzyme: 8-oxo-dGDP phosphatase NUDT18


substrate_name: IDP

substrate: IDP


substrate_name: dIDP

substrate: dIDP


substrate_name: GDP

substrate: GDP


substrate_name: dGDP

substrate: dGDP


substrate_name: ITP

substrate: ITP


substrate_name: dITP

substrate: dITP


enzyme_display_name: Nudix hydrolase DR_1025

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

proof_lines: kcat is 0.18 sec(-1) with 8-oxo-dGTP as substrate measured by the Pi sensor assay. kcat is 0.29 sec(-1) with 8-oxo-dGTP as substrate measured by the Fiske-SubbaRow assay. kcat is 0.13 sec(-1) with 8-oxo-GTP as substrate.

enzyme: Nudix hydrolase DR_1025


enzyme_display_name: ADP-sugar pyrophosphatase

substrate_name: ADP-D-ribose

assay_conditions_summary: pH 7; cofactor ADP

proof_lines: kcat is 0.369 min(-1) for 8-OH-dGDP. kcat is 0.538 min(-1) for 8-OH-dADP. kcat is 0.226 min(-1) for 2-OH-dADP. kcat is 0.209 min(-1) for 5-CHO-dUDP. kcat is 0.929 min(-1) for dGDP. kcat is 0.365 min(-1) for dADP.

enzyme: ADP-sugar pyrophosphatase

substrate: ADP-D-ribose


assay_conditions_summary: pH 10; cofactor ADP


enzyme_display_name: ADP-ribose pyrophosphatase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 14.4 sec(-1) with ADPR as substrate (in the presence of Mg(2+) ions). kcat is 28.9 sec(-1) with ADPR as substrate (in the presence of Mn(2+) ions) (PubMed:27683242). kcat is 0.0164 sec(-1) with 8-oxo-dGDP as substrate (PubMed:234635

enzyme: ADP-ribose pyrophosphatase


enzyme_display_name: UniProt Q0P8U5

organism: Campylobacter jejuni

enzyme: UniProt Q0P8U5


enzyme_display_name: UniProt Q06151

organism: Saccharomyces cerevisiae

substrate_name: 7-methylguanosine 5'-diphosphate

assay_conditions_summary: pH 7; 303.15 K; buffer 10 mM Tris-HCl pH 7

column_label: Table 2, Dcs1 homodimer row for m7GDP, reports KM 0.26 uM, kcat 1.7 x 10^-3 s^-1, and independently printed kcat/KM 6.5 x 10^3 M^-1 s^-1.

row_label: Dcs1 homodimer / m7GDP (text extraction renders m7Gpp)

table_label: Primary article PDF page 5 / printed page 374, Table 2

enzyme: UniProt Q06151

substrate: 7-methylguanosine 5'-diphosphate


column_label: Table 3. Substrate specificity of the NUDT5 protein; row 8-OH-dGDP; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

normalized_value_unit_evidence: km paper=0.0021 mM

raw_value_unit_evidence: Table 3. Substrate specificity of the NUDT5 protein, row 8-OH-dGDP: Km 2.1 uM; kcat 0.369 min^-1; kcat/Km 0.176 min^-1 uM^-1.


column_label: Table 3. Substrate specificity of the NUDT5 protein; row 8-OH-dADP; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

normalized_value_unit_evidence: km paper=0.0029 mM

raw_value_unit_evidence: Table 3. Substrate specificity of the NUDT5 protein, row 8-OH-dADP: Km 2.9 uM; kcat 0.538 min^-1; kcat/Km 0.186 min^-1 uM^-1.


column_label: Table 3. Substrate specificity of the NUDT5 protein; row 2-OH-dADP; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

normalized_value_unit_evidence: km paper=0.0088 mM

raw_value_unit_evidence: Table 3. Substrate specificity of the NUDT5 protein, row 2-OH-dADP: Km 8.8 uM; kcat 0.226 min^-1; kcat/Km 0.026 min^-1 uM^-1.


column_label: Table 3. Substrate specificity of the NUDT5 protein; row dGDP; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

normalized_value_unit_evidence: km paper=0.0076 mM

raw_value_unit_evidence: Table 3. Substrate specificity of the NUDT5 protein, row dGDP: Km 7.6 uM; kcat 0.929 min^-1; kcat/Km 0.122 min^-1 uM^-1.


substrate_name: dADP

column_label: Table 3. Substrate specificity of the NUDT5 protein; row dADP; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

normalized_value_unit_evidence: km paper=0.0126 mM

raw_value_unit_evidence: Table 3. Substrate specificity of the NUDT5 protein, row dADP: Km 12.6 uM; kcat 0.365 min^-1; kcat/Km 0.029 min^-1 uM^-1.

row_label: dADP

substrate: dADP


enzyme_display_name: Diphosphoinositol polyphosphate phosphohydrolase 1


organism: Rattus norvegicus

enzyme: Diphosphoinositol polyphosphate phosphohydrolase 1


enzyme_display_name: alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase

substrate_name: D-Ribose 5-triphosphate; H2O

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

substrate: D-Ribose 5-triphosphate; H2O


enzyme_display_name: UniProt Q75UV1

column_label: Row Ap6A / ATP; columns Product, kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat 4.1 s^-1; Km 0.0014 mM; kcat/Km 2928.57 s^-1 mM^-1 from table kcat/Km column 2.9 x 10^6 M^-1 s^-1 and same-row kcat/Km quotient

raw_value_unit_evidence: Table I. Kinetic constants for Ndx1, row Ap6A / ATP: kcat 4.1 s^-1; Km 1.4 uM; kcat/Km 2.9 x 10^6 M^-1 s^-1.

row_label: Ap6A / ATP

table_label: Table I. Kinetic constants for Ndx1

source_databases_merged: brenda skid uniprot

enzyme: UniProt Q75UV1


enzyme_display_name: Diadenosine hexaphosphate hydrolase

substrate_name: p4A (at 25 degrees Celsius)

proof_lines: kcat is 4.1 sec(-1) with Ap6A (at 25 degrees Celsius). kcat is 1.4 sec(-1) with p4A (at 25 degrees Celsius). kcat is 0.52 sec(-1) with Ap5A (at 25 degrees Celsius). kcat is 0.27 sec(-1) with Ap4A (at 25 degrees Celsius).

enzyme: Diadenosine hexaphosphate hydrolase

substrate: p4A (at 25 degrees Celsius)


substrate_name: Ap4A (at 25 degrees Celsius)

assay_conditions_summary: cofactor ATP

column_label: Row Ap4A / ATP, AMP; column Km (uM).

raw_value_unit_evidence: Table I. Kinetic constants for Ndx1, row Ap4A / ATP, AMP: kcat 0.27 s^-1; Km 1.1 uM; kcat/Km 2.5 x 10^5 M^-1 s^-1.

row_label: Ap4A / ATP, AMP

substrate: Ap4A (at 25 degrees Celsius)


enzyme_display_name: 8-oxo-dGDP phosphatase

substrate_name: 8-oxo-dGDP; H2O

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

enzyme: 8-oxo-dGDP phosphatase

substrate: 8-oxo-dGDP; H2O


substrate_name: ADPR (in the presence of Mg(2+) ions)

substrate: ADPR (in the presence of Mg(2+) ions)


enzyme_display_name: m7GpppX diphosphatase

organism: Caenorhabditis elegans

proof_lines: N-terminally tagged protein, pH 7.2, 20°C

proof_lines: C-terminally tagged protein, pH 7.2, 20°C

source_databases_merged: brenda uniprot

enzyme: m7GpppX diphosphatase


proof_lines:
pH 7.0, 30°C, Dcs1 homodimer
Raw SKiD Env: Temp=30°C, pH=7


substrate_name: Ap5A (at 25 degrees Celsius)

ki_unit: mM

substrate: Ap5A (at 25 degrees Celsius)


substrate_name: H2O; Diadenosine hexaphosphate

substrate: H2O; Diadenosine hexaphosphate


enzyme_display_name: Diphosphoinositol polyphosphate phosphohydrolase 3-alpha


enzyme_display_name: Diphosphoinositol polyphosphate phosphohydrolase 3-beta


enzyme_display_name: Diphosphoinositol polyphosphate phosphohydrolase DDP1


substrate_name: ADP-ribose

column_label: Table 1 row ADP-ribose, expressed-enzyme kinetic columns: Km 39 +/- 2 uM.

row_label: ADP-ribose

substrate: ADP-ribose


substrate_name: CDP-choline

column_label: Table 1 row CDP-choline, expressed-enzyme kinetic columns: Km 300 +/- 22 uM.

row_label: CDP-choline

substrate: CDP-choline


substrate_name: CDP-ethanolamine

column_label: Table 1 row CDP-ethanolamine, expressed-enzyme kinetic columns: Km 1422 +/- 99 uM.

row_label: CDP-ethanolamine

substrate: CDP-ethanolamine


substrate_name: CDP-glycerol

column_label: Table 1 row CDP-glycerol, expressed-enzyme kinetic columns: Km 304 +/- 59 uM.

row_label: CDP-glycerol

substrate: CDP-glycerol


substrate_name: ADP

column_label: Table 1 row ADP, expressed-enzyme kinetic columns: Km 201 +/- 30 uM.

row_label: ADP

substrate: ADP


substrate_name: (2E)-geranyl diphosphate (at pH 8.0 and 22 degrees Celsius)

assay_conditions_summary: pH 8; buffer tris acetate pH 8.0

column_label: Table 1 (febs17202-tbl-0001); enzyme NUDT18; metric row Km (microM), Mean; substrate column GPP.

normalized_value_unit_evidence: Km=0.0037 mM after converting 3.7 microM to mM.

raw_value_unit_evidence: Table 1 NUDT18 Km Mean column GPP = 3.7 microM.

row_label: NUDT18 GPP

table_label: Table 1 (NUDT18 kinetic parameters)


substrate_name: dimethylallyl diphosphate (at pH 8.0 and 22 degrees Celsius)

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

column_label: Table 1 (febs17202-tbl-0001); enzyme NUDT18; metric row Km (microM), Mean; substrate column DMAPP.

normalized_value_unit_evidence: Km=0.0098 mM after converting 9.8 microM to mM.

raw_value_unit_evidence: Table 1 NUDT18 Km Mean column DMAPP = 9.8 microM.

row_label: NUDT18 DMAPP


substrate_name: isopentenyl diphosphate (at pH 8.0 and 22 degrees Celsius)

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

column_label: Table 1 (febs17202-tbl-0001); enzyme NUDT18; metric row Km (microM), Mean; substrate column IPPP.

normalized_value_unit_evidence: Km=0.0124 mM after converting 12.4 microM to mM.

raw_value_unit_evidence: Table 1 NUDT18 Km Mean column IPPP = 12.4 microM.

row_label: NUDT18 IPPP


substrate_name: (2E,6E,10E)-geranylgeranyl diphosphate (at pH 8.0 and 22 degrees Celsius)

column_label: Table 1 (febs17202-tbl-0001); enzyme NUDT18; metric row Km (microM), Mean; substrate column GGPP.

normalized_value_unit_evidence: Km=0.0179 mM after converting 17.9 microM to mM.

raw_value_unit_evidence: Table 1 NUDT18 Km Mean column GGPP = 17.9 microM.

row_label: NUDT18 GGPP


substrate_name: (2E,6E)-farnesyl diphosphate (at pH 8.0 and 22 degrees Celsius)

column_label: Table 1 (febs17202-tbl-0001); enzyme NUDT18; metric row Km (microM), Mean; substrate column FPP.

normalized_value_unit_evidence: Km=0.0188 mM after converting 18.8 microM to mM.

raw_value_unit_evidence: Table 1 NUDT18 Km Mean column FPP = 18.8 microM.

row_label: NUDT18 FPP


substrate_name: (R)-5-diphosphomevalonate (at pH 8.0 and 22 degrees Celsius)

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

column_label: Table 1 (febs17202-tbl-0001); enzyme NUDT18; metric row Km (microM), Mean; substrate column MPP.

normalized_value_unit_evidence: Km=0.0268 mM after converting 26.8 microM to mM.

raw_value_unit_evidence: Table 1 NUDT18 Km Mean column MPP = 26.8 microM.

row_label: NUDT18 MPP


sequence_variant_note: Mutation signature N255A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


table_label: Table 3. Substrate specificity of the NUDT5 protein


column_label: Table 3. Substrate specificity of the NUDT5 protein; row 5-CHO-dUDP; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table 3. Substrate specificity of the NUDT5 protein, row 5-CHO-dUDP: Km 4.0 uM; kcat 0.209 min^-1; kcat/Km 0.052 min^-1 uM^-1.


column_label: Table 3. Substrate specificity of the NUDT5 protein; row 8-OH-dADP; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).


column_label: Table 3. Substrate specificity of the NUDT5 protein; row 8-OH-dGDP; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).


substrate_name: dADP

column_label: Table 3. Substrate specificity of the NUDT5 protein; row dADP; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).


enzyme_display_name: inosine diphosphate phosphatase

substrate_name: dGDP

assay_conditions_summary: pH 7.5; 310.15 K; buffer reaction

column_label: Table 1. Kinetic parameters of His-NUDT16; row dGDP; kcat 0.492 min^-1; Km 0.319 uM; kcat/Km 25.7 x 10^3 s^-1 M^-1; normalized: kcat 0.0082 s^-1; km 0.000319 mM; kcat_over_km 25.7 s^-1 mM^-1

row_label: dGDP

enzyme: inosine diphosphate phosphatase

substrate: dGDP


substrate_name: dIDP

column_label: Table 1. Kinetic parameters of His-NUDT16; row dIDP; kcat 0.96 min^-1; Km 0.088 uM; kcat/Km 183 x 10^3 s^-1 M^-1; normalized: kcat 0.016 s^-1; km 8.8e-05 mM; kcat_over_km 183 s^-1 mM^-1

row_label: dIDP

substrate: dIDP


substrate_name: dITP

column_label: Table 1. Kinetic parameters of His-NUDT16; row dITP; kcat 3.20 min^-1; Km 24.1 uM; kcat/Km 2.21 x 10^3 s^-1 M^-1; normalized: kcat 0.0533333333333333 s^-1; km 0.0241 mM; kcat_over_km 2.21 s^-1 mM^-1

row_label: dITP

substrate: dITP


substrate_name: GDP

column_label: Table 1. Kinetic parameters of His-NUDT16; row GDP; kcat 0.51 min^-1; Km 0.330 uM; kcat/Km 26.1 x 10^3 s^-1 M^-1; normalized: kcat 0.0085 s^-1; km 0.00033 mM; kcat_over_km 26.1 s^-1 mM^-1

row_label: GDP

substrate: GDP


substrate_name: IDP

column_label: Table 1. Kinetic parameters of His-NUDT16; row IDP; kcat 0.93 min^-1; Km 0.062 uM; kcat/Km 251 x 10^3 s^-1 M^-1; normalized: kcat 0.0155 s^-1; km 6.2e-05 mM; kcat_over_km 251 s^-1 mM^-1

row_label: IDP

substrate: IDP


substrate_name: ITP

substrate: ITP


substrate_name: XDP

substrate: XDP


substrate_name: diguanosine pentaphosphate (Gp5G) (at 25 degrees Celsius)


substrate_name: diguanosine tetraphosphate (Gp4G) (at 25 degrees Celsius)


substrate_name: ADP

assay_conditions_summary: pH 7.5; 310.15 K; buffer C pH 7; cofactor ADP

column_label: Table 1 row ADP; columns Km (uM) This work, kcat (min^-1) This work, kcat/Km (10^3 s^-1 M^-1) This work

table_label: Table 1. Kinetic parameters of NUDT16 towards ITP, XDP and ADP


column_label: Table 1 row ITP; columns Km (uM) This work, kcat (min^-1) This work, kcat/Km (10^3 s^-1 M^-1) This work

row_label: ITP


column_label: Table 1 row XDP; columns Km (uM) This work, kcat (min^-1) This work, kcat/Km (10^3 s^-1 M^-1) This work

row_label: XDP


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

column_label: Table I, row Ap6A, column Km (microM)=56; same row products=p4A + ADP (76%); p5A + AMP (24%), kcat=0.4 s^-1.

raw_value_unit_evidence: Ap6A: Km=56 microM; products=p4A + ADP (76%); p5A + AMP (24%); Vmax=1 units mg^-1; kcat=0.4 s^-1; kcat/Km=6.4 x10^3 M^-1 s^-1

table_label: Table I. Products and kinetic constants

enzyme: Diphosphoinositol polyphosphate phosphohydrolase DDP1