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.


enzyme_display_name: ADP-ribose diphosphatase

organism: Thermus thermophilus

substrate_name: ADP alpha-D-glucoside

source_db: oed

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 7.63; 298.15 K; cofactor ADP

proof_lines: Thermus thermophilus ADP-ribose pyrophosphatase

data_origin: experimental

enzyme: ADP-ribose diphosphatase

substrate: ADP alpha-D-glucoside

status: unverified

source: oed


substrate_name: ADPribose

verification_status: corrected

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.

mutation_type: substitution

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.

substrate: ADPribose

status: corrected


verification_status: verified

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.

status: verified


kcat_over_km_origin: calculated

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.


organism: Homo sapiens

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

kcat_display: Not reported

kcat_over_km_display: Not reported

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

substrate: TTP

source: uniprot


enzyme_display_name: dCTP diphosphatase

organism: Mus musculus

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


enzyme_display_name: nucleotide diphosphatase

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

enzyme: nucleotide diphosphatase

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.

table_label: Table 2

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_db: brenda

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

source: brenda


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

organism: Rattus norvegicus

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


verification_status: disputed

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

assay_conditions_summary: cofactor 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


enzyme_display_name: nucleotide diphosphatase

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

enzyme: nucleotide diphosphatase


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

assay_conditions_summary: cofactor ATP


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

organism: Homo sapiens

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

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

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

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

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)

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

table_label: Table 1

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


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

column_label: Supplemental Table S1 PhnM section row RPnTP column Km (uM)=56 +/- 12

raw_value_unit_evidence: Supplemental Table S1 row RPnTP: Km=56 +/- 12 uM

row_label: RPnTP

table_label: Supplemental Table S1: Kinetic constants for the reactions catalyzed by PhnI and PhnM


column_label: Supplemental Table S1 PhnM section row RTP column Km (uM)=98 +/- 12

raw_value_unit_evidence: Supplemental Table S1 row RTP: Km=98 +/- 12 uM

row_label: RTP

enzyme: Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase


column_label: Supplemental Table S1 PhnM section row RDP column Km (uM)=200 +/- 32

raw_value_unit_evidence: Supplemental Table S1 row RDP: Km=200 +/- 32 uM

row_label: RDP


enzyme_display_name: UniProt Q9WPH5

organism: Hepacivirus C

substrate_name: ATP

enzyme: UniProt Q9WPH5

substrate: ATP


enzyme_display_name: UniProt P38919

enzyme: UniProt P38919


enzyme_display_name: UniProt Q9Q6P4

organism: West Nile virus

enzyme: UniProt Q9Q6P4


enzyme_display_name: Genome polyprotein

organism: Hepatitis GB virus B

substrate_name: ATP for NS3 NTPase

enzyme: Genome polyprotein

substrate: ATP for NS3 NTPase


substrate_name: CTP for NS3 NTPase

substrate: CTP for NS3 NTPase


substrate_name: UTP for NS3 NTPase

substrate: UTP for NS3 NTPase


substrate_name: dATP for NS3 NTPase

substrate: dATP for NS3 NTPase


substrate_name: dCTP for NS3 NTPase

substrate: dCTP for NS3 NTPase


substrate_name: dTTP for NS3 NTPase

substrate: dTTP for NS3 NTPase


enzyme_display_name: UniProt Q980M3

organism: Saccharolobus solfataricus

substrate_name: GTP

proof_lines:
Raw SKiD Env: Temp=50°C, pH=7.5
Raw SKiD Env: Temp=50°C, pH=7.4
Raw SKiD Env: Temp=50°C, pH=7.8

enzyme: UniProt Q980M3

substrate: GTP


enzyme_display_name: UniProt Q980A5

proof_lines:
Raw SKiD Env: Temp=60°C, pH=-----
Raw SKiD Env: Temp=50°C, pH=7.8
Raw SKiD Env: Temp=75°C, pH=7.8

enzyme: UniProt Q980A5


enzyme_display_name: UniProt P60785

enzyme: UniProt P60785


enzyme_display_name: GTP cyclohydrolase II

enzyme: GTP cyclohydrolase II


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

column_label: Supplemental Table S1 PhnM section row RPnTP columns kcat (s^-1)=6.4 +/- 0.3, Km (uM)=56 +/- 12, kcat/Km (M^-1s^-1)=(1.1 +/- 0.2) x 10^5

normalized_value_unit_evidence: kcat 6.4 s^-1 from explicit paper cell; kcat_over_km 110 s^-1 mM^-1 from explicit paper cell; km 0.056 mM from explicit paper cell


substrate_name: D-Ribose 5-diphosphate

column_label: Supplemental Table S1 PhnM section row RDP columns kcat (s^-1)=0.08 +/- 0.01, Km (uM)=200 +/- 32, kcat/Km (M^-1s^-1)=(0.38 +/- 0.03) x 10^3

normalized_value_unit_evidence: kcat=0.08 s^-1; Km=0.200 mM; kcat_over_km=0.4 s^-1*mM^-1 from kcat/Km cells; table ratio column rounds to 0.38 s^-1*mM^-1

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

substrate: D-Ribose 5-diphosphate


substrate_name: D-Ribose 5-phosphate

proof_lines: D-ribose-5-phosphate pyrophosphate RTP

substrate: D-Ribose 5-phosphate


enzyme_display_name: UniProt P83788

organism: Pseudomonas fluorescens

km_display: Not reported

enzyme: UniProt P83788


substrate_name: L-kynurenine

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.8
Raw SKiD Env: Temp=37°C, pH=8

substrate: L-kynurenine


substrate_name: O-benzoyl-L-serine

substrate: O-benzoyl-L-serine


enzyme_display_name: UniProt Q8NFP7

organism: Homo sapiens

enzyme: UniProt Q8NFP7


column_label: Table I row PP-InsP5, hDIPP3-alpha, Km column.

normalized_value_unit_evidence: 0.088 uM normalizes to 0.000088 mM.

raw_value_unit_evidence: Table I reports PP-InsP5 alpha Km 0.088 uM.

row_label: PP-InsP5, isoform alpha / hDIPP3-alpha

table_label: Table I, Catalytic properties of the hDIPP3 isoforms

enzyme: Diphosphoinositol polyphosphate phosphohydrolase 3-alpha


column_label: Table I row PP-InsP5, hDIPP3-beta, Km column.

normalized_value_unit_evidence: 0.053 uM normalizes to 0.000053 mM.

raw_value_unit_evidence: Table I reports PP-InsP5 beta Km 0.053 uM.

row_label: PP-InsP5, isoform beta / hDIPP3-beta

enzyme: Diphosphoinositol polyphosphate phosphohydrolase 3-beta


column_label: Table I row Ap6A, hDIPP3-beta, Km column.

normalized_value_unit_evidence: 43 uM normalizes to 0.043 mM, not exported 0.013 mM.

raw_value_unit_evidence: Table I reports Ap6A beta Km 43 uM.

row_label: Ap6A, isoform beta / hDIPP3-beta


enzyme_display_name: S-methyl-5'-thioadenosine deaminase

organism: Pseudomonas aeruginosa

substrate_name: adenosine

enzyme: S-methyl-5'-thioadenosine deaminase

substrate: adenosine


enzyme_display_name: nucleotide diphosphatase

substrate_name: dITP

column_label: Table I; row dITP; columns Km (mM), kcat (s^-1), kcat/Km (10^3 M^-1 s^-1).

normalized_value_unit_evidence: kcat 360 s^-1 from explicit paper cell; kcat_over_km 1160 s^-1 mM^-1 from explicit paper cell; km 0.31 mM from explicit paper cell

table_label: Table I

enzyme: nucleotide diphosphatase

substrate: dITP


substrate_name: ITP

column_label: Table I; row ITP; columns Km (mM), kcat (s^-1), kcat/Km (10^3 M^-1 s^-1).

normalized_value_unit_evidence: kcat 580 s^-1 from explicit paper cell; kcat_over_km 1140 s^-1 mM^-1 from explicit paper cell; km 0.51 mM from explicit paper cell


substrate_name: XTP

column_label: Table I; row XTP; columns Km (mM), kcat (s^-1), kcat/Km (10^3 M^-1 s^-1).

normalized_value_unit_evidence: kcat 640 s^-1 from explicit paper cell; kcat_over_km 1120 s^-1 mM^-1 from explicit paper cell; km 0.57 mM from explicit paper cell

row_label: XTP

substrate: XTP


enzyme_display_name: UniProt P96965

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

enzyme: UniProt P96965


organism: Pseudomonas putida

substrate_name: catechol

substrate: catechol


enzyme_display_name: exopolyphosphatase

organism: Trypanosoma brucei brucei

substrate_name: ADP

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

enzyme: exopolyphosphatase

substrate: ADP


substrate_name: ATP

substrate: ATP


enzyme_display_name: glucosamine-6-phosphate deaminase

organism: Thermococcus kodakarensis

substrate_name: D-fructose 6-phosphate

column_label: Official PMC full text Table 1 row Fru6P (at 170 mM ammonia), amination direction, reports kcat, Km, and kcat/Km.

normalized_value_unit_evidence: Km=1.10 mM; kcat=44.2 s^-1; kcat/Km=40.18181818181818 s^-1 mM^-1 from displayed kcat/Km ratio

row_label: Amination; Fru6P (at 170 mM ammonia)

table_label: PMC HTML Table 1: Kinetic properties of GlmD_Tk

enzyme: glucosamine-6-phosphate deaminase

substrate: D-fructose 6-phosphate


substrate_name: D-glucosamine 6-phosphate

column_label: Official PMC full text Table 1 row GlcN6P, deamination direction, reports kcat, Km, and kcat/Km.

normalized_value_unit_evidence: Km=0.339 mM; kcat=97.5 s^-1; kcat/Km=287.6106194690265 s^-1 mM^-1 from displayed kcat/Km ratio

row_label: Deamination; GlcN6P

substrate: D-glucosamine 6-phosphate


organism: Escherichia coli

substrate_name: meta-ring fission intermediate

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

substrate: meta-ring fission intermediate


organism: Flavobacterium sp.

substrate_name: 2-hydroxy-5-methylmuconic semialdehyde

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

substrate: 2-hydroxy-5-methylmuconic semialdehyde


substrate_name: 2-hydroxymuconic semialdehyde

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

substrate: 2-hydroxymuconic semialdehyde


organism: Rhodococcus globerulus


substrate_name: D-Glucosamine 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H164C/C118S/C228S/C239S to reconstruct the assayed variant sequence.

substrate: D-Glucosamine 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S206C/C118S/C228S/C239S to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt A0ACD6B9C3

organism: Sphingobium sp. SYK-6

enzyme: UniProt A0ACD6B9C3


enzyme_display_name: Nudix hydrolase 7

organism: Arabidopsis thaliana

substrate_name: NADH

enzyme: Nudix hydrolase 7

substrate: NADH


substrate_name: ADP-ribose

substrate: ADP-ribose


enzyme_display_name: cyclohexane-1,3-dione hydrolase

organism: Clostridium sp.

enzyme: cyclohexane-1,3-dione hydrolase


organism: Janthinobacterium sp. J3


organism: Arthrobacter sp. YC-RL1


organism: Pseudomonas sp.


organism: Burkholderia xenovorans


organism: Metapseudomonas resinovorans

substrate_name: HOPDA (at pH 7.5 and 25 degrees Celsius)

assay_conditions_summary: pH 7.5; buffer 50 mM sodium phosphate

column_label: PMID 12619671 DOI 10.1016/S0006-291X(03)00375-9 Table 1; rows CarCCA10 / 6-Phenyl HODA and CarCCA10 / HODA; Km (uM) column.

normalized_value_unit_evidence: 6-Phenyl HODA Km normalizes to 0.00251 mM; HODA kinetic parameters are not determined.

raw_value_unit_evidence: Table 1 row CarCCA10 / 6-Phenyl HODA gives Km 2.51 uM; the separate HODA row reports ND for Km, kcat, and kcat/Km because of low activity.

row_label: CarCCA10 / 6-Phenyl HODA; CarCCA10 / HODA

table_label: Table 1. Kinetic parameters of native CarCCA10, ht-CarCCA10, and ht-CarCJ3


organism: Burkholderia cepacia


organism: Mycobacterium tuberculosis

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

source_databases_merged: sabio_rk skid uniprot


substrate_name: H2O; 3-Methylcatechol ring-fission product


organism: Cupriavidus necator

proof_lines:
isoenzyme HODHII
isoenzyme HODHI


proof_lines:
isoenzyme HODHI
isoenzyme HODHII


proof_lines: kcat is 2.14 sec(-1) for 6-phenyl-HODA (at 50 mM sodium phosphate, pH 7.5, 25 degrees Celsius).


organism: Comamonas testosteroni

substrate_name: Unknown

substrate: Unknown


organism: Escherichia coli (strain K12)

substrate_name: 2-hydroxy-6-oxononadienedioate (at pH 8)

proof_lines: kcat is 28 sec(-1) for hydrolase activity with 2-hydroxy-6-oxononadienedioate as substrate.


source_databases_merged: sabio_rk brenda uniprot


organism: Paraburkholderia xenovorans

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H265A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D237N to reconstruct the assayed variant sequence.


column_label: Table 4, HMSH row 2-HMS, columns KM, kcat, kcat/KM.

row_label: HMSH / 2-HMS

table_label: Table 4


column_label: Table 4, HMSH row HODA, columns KM, kcat, kcat/KM.

row_label: HMSH / HODA


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature S112A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P47229 and applied mutation signature R188K with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, BphD block, variant row R188K; column KM (uM) = 2.0; column kcat (s^-1) = 0.009; column kcat/KM (M^-1 s^-1) = 2.8 x 10^3. captured primary segment: BphD R188K | KM 2.0 uM | kcat 0.009 s^-1 | kcat/KM 2.8 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 2.0 uM; 1 uM is 1/1000 mM, so 2.0 / 1000 = 0.002 mM. kcat: printed Table 2 kcat cell 0.009 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 0.009 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 2.8 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2800 / 1000 = 2.8 s^(-1)*mM^(-1). The catalog stores no catalytic-efficiency value for this measurement, so this pass reports the printed cell in the typed ratio provenance only and adds no kcat_over_km metric. Quotient disclosure for this row: 0.009 / 0.002 = 4.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, BphD block, variant row R188K: KM = 2.0 uM; kcat = 0.009 s^-1; printed kcat/KM = 2.8 x 10^3 M^-1 s^-1.

row_label: Table 2, BphD block, variant row R188K


column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, BphD block, enzyme row wild-type BphD; column KM (uM) = 2.0; column kcat (s^-1) = 6.5; column kcat/KM (M^-1 s^-1) = 3.3 x 10^6. captured primary segment: wild-type BphD | KM 2.0 uM | kcat 6.5 s^-1 | kcat/KM 3.3 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 2.0 uM; 1 uM is 1/1000 mM, so 2.0 / 1000 = 0.002 mM. kcat: printed Table 2 kcat cell 6.5 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 6.5 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 3.3 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3300000 / 1000 = 3300.0 s^(-1)*mM^(-1). The catalog stores no catalytic-efficiency value for this measurement, so this pass reports the printed cell in the typed ratio provenance only and adds no kcat_over_km metric. Quotient disclosure for this row: 6.5 / 0.002 = 3250.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, BphD block, enzyme row wild-type BphD: KM = 2.0 uM; kcat = 6.5 s^-1; printed kcat/KM = 3.3 x 10^6 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P47229 and applied mutation signature R188Q with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, BphD block, variant row R188Q; column KM (uM) = 28.2; column kcat (s^-1) = 0.016; column kcat/KM (M^-1 s^-1) = 5.7 x 10^2. captured primary segment: BphD R188Q | KM 28.2 uM | kcat 0.016 s^-1 | kcat/KM 5.7 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 28.2 uM; 1 uM is 1/1000 mM, so 28.2 / 1000 = 0.0282 mM. kcat: printed Table 2 kcat cell 0.016 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 0.016 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 5.7 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 570 / 1000 = 0.57 s^(-1)*mM^(-1). The catalog stores no catalytic-efficiency value for this measurement, so this pass reports the printed cell in the typed ratio provenance only and adds no kcat_over_km metric. Quotient disclosure for this row: 0.016 / 0.0282 = 0.5673758865248227 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, BphD block, variant row R188Q: KM = 28.2 uM; kcat = 0.016 s^-1; printed kcat/KM = 5.7 x 10^2 M^-1 s^-1.

row_label: Table 2, BphD block, variant row R188Q


organism: Pseudomonas putida

substrate_name: 3-methylcatechol ring-fission product

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature H249A to reconstruct the assayed variant sequence.

substrate: 3-methylcatechol ring-fission product


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P77044 and applied mutation signature C261A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, MhpC block, variant row C261A; column KM (uM) = 4.2; column kcat (s^-1) = 12; column kcat/KM (M^-1 s^-1) = 2.9 x 10^6. captured primary segment: MhpC C261A | KM 4.2 uM | kcat 12 s^-1 | kcat/KM 2.9 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 4.2 uM; 1 uM is 1/1000 mM, so 4.2 / 1000 = 0.0042 mM. kcat: printed Table 2 kcat cell 12 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 12.0 s^(-1). kcat/Km: printed Table 2 kcat/KM 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 = 2900.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 12.0 / 0.0042 = 2857.1428571428573 s^-1 mM^-1, which is the value the catalog carries, and the printed catalytic-efficiency cell 2.9 x 10^6 M^-1 s^-1 is that same quotient written to the two significant figures the table uses.

raw_value_unit_evidence: Table 2, MhpC block, variant row C261A: KM = 4.2 uM; kcat = 12 s^-1; printed kcat/KM = 2.9 x 10^6 M^-1 s^-1.

row_label: Table 2, MhpC block, variant row C261A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P77044 and applied mutation signature F173D with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, MhpC block, variant row F173D; column KM (uM) = 10; column kcat (s^-1) = 0.26; column kcat/KM (M^-1 s^-1) = 2.6 x 10^4. captured primary segment: MhpC F173D | KM 10 uM | kcat 0.26 s^-1 | kcat/KM 2.6 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 10 uM; 1 uM is 1/1000 mM, so 10 / 1000 = 0.01 mM. kcat: printed Table 2 kcat cell 0.26 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 0.26 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 2.6 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 26000 / 1000 = 26.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.26 / 0.01 = 26.0 s^-1 mM^-1, the same value as the printed catalytic-efficiency cell, so this row closes on its own printed cells.

raw_value_unit_evidence: Table 2, MhpC block, variant row F173D: KM = 10 uM; kcat = 0.26 s^-1; printed kcat/KM = 2.6 x 10^4 M^-1 s^-1.

row_label: Table 2, MhpC block, variant row F173D


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P77044 and applied mutation signature F173G with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, MhpC block, variant row F173G; column KM (uM) = 58; column kcat (s^-1) = 7.5; column kcat/KM (M^-1 s^-1) = 1.3 x 10^5. captured primary segment: MhpC F173G | KM 58 uM | kcat 7.5 s^-1 | kcat/KM 1.3 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 58 uM; 1 uM is 1/1000 mM, so 58 / 1000 = 0.058 mM. kcat: printed Table 2 kcat cell 7.5 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 7.5 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 1.3 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 130000 / 1000 = 130.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 7.5 / 0.058 = 129.3103448275862 s^-1 mM^-1, which is the value the catalog carries, and the printed catalytic-efficiency cell 1.3 x 10^5 M^-1 s^-1 is that same quotient written to the two significant figures the table uses.

raw_value_unit_evidence: Table 2, MhpC block, variant row F173G: KM = 58 uM; kcat = 7.5 s^-1; printed kcat/KM = 1.3 x 10^5 M^-1 s^-1.

row_label: Table 2, MhpC block, variant row F173G


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P77044 and applied mutation signature N109A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, MhpC block, variant row N109A; column KM (uM) = 4.0; column kcat (s^-1) = 0.13; column kcat/KM (M^-1 s^-1) = 3.3 x 10^4. captured primary segment: MhpC N109A | KM 4.0 uM | kcat 0.13 s^-1 | kcat/KM 3.3 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 4.0 uM; 1 uM is 1/1000 mM, so 4.0 / 1000 = 0.004 mM. kcat: printed Table 2 kcat cell 0.13 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 0.13 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 3.3 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 33000 / 1000 = 33.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.13 / 0.004 = 32.5 s^-1 mM^-1, against the printed catalytic-efficiency cell 33.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MhpC block, variant row N109A: KM = 4.0 uM; kcat = 0.13 s^-1; printed kcat/KM = 3.3 x 10^4 M^-1 s^-1.

row_label: Table 2, MhpC block, variant row N109A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P77044 and applied mutation signature N109H with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, MhpC block, variant row N109H; column KM (uM) = 4.0; column kcat (s^-1) = 0.08; column kcat/KM (M^-1 s^-1) = 1.9 x 10^4. captured primary segment: MhpC N109H | KM 4.0 uM | kcat 0.08 s^-1 | kcat/KM 1.9 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 4.0 uM; 1 uM is 1/1000 mM, so 4.0 / 1000 = 0.004 mM. kcat: printed Table 2 kcat cell 0.08 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 0.08 s^(-1). kcat/Km: printed Table 2 kcat/KM 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 = 19.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.08 / 0.004 = 20.0 s^-1 mM^-1, against the printed catalytic-efficiency cell 19.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MhpC block, variant row N109H: KM = 4.0 uM; kcat = 0.08 s^-1; printed kcat/KM = 1.9 x 10^4 M^-1 s^-1.

row_label: Table 2, MhpC block, variant row N109H


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P77044 and applied mutation signature R188K with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, MhpC block, variant row R188K; column KM (uM) = 38; column kcat (s^-1) = 0.74; column kcat/KM (M^-1 s^-1) = 1.9 x 10^4. captured primary segment: MhpC R188K | KM 38 uM | kcat 0.74 s^-1 | kcat/KM 1.9 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 38 uM; 1 uM is 1/1000 mM, so 38 / 1000 = 0.038 mM. kcat: printed Table 2 kcat cell 0.74 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 0.74 s^(-1). kcat/Km: printed Table 2 kcat/KM 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 = 19.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.74 / 0.038 = 19.473684210526315 s^-1 mM^-1, which is the value the catalog carries, and the printed catalytic-efficiency cell 1.9 x 10^4 M^-1 s^-1 is that same quotient written to the two significant figures the table uses.

raw_value_unit_evidence: Table 2, MhpC block, variant row R188K: KM = 38 uM; kcat = 0.74 s^-1; printed kcat/KM = 1.9 x 10^4 M^-1 s^-1.

row_label: Table 2, MhpC block, variant row R188K


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P77044 and applied mutation signature R188Q with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, MhpC block, variant row R188Q; column KM (uM) = 77; column kcat (s^-1) = 0.10; column kcat/KM (M^-1 s^-1) = 1.4 x 10^3. captured primary segment: MhpC R188Q | KM 77 uM | kcat 0.10 s^-1 | kcat/KM 1.4 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 77 uM; 1 uM is 1/1000 mM, so 77 / 1000 = 0.077 mM. kcat: printed Table 2 kcat cell 0.10 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 0.1 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 1.4 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1400 / 1000 = 1.4 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.1 / 0.077 = 1.2987012987012987 s^-1 mM^-1, against the printed catalytic-efficiency cell 1.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MhpC block, variant row R188Q: KM = 77 uM; kcat = 0.10 s^-1; printed kcat/KM = 1.4 x 10^3 M^-1 s^-1.

row_label: Table 2, MhpC block, variant row R188Q


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P77044 and applied mutation signature W264G with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, MhpC block, variant row W264G; column KM (uM) = 125; column kcat (s^-1) = 2.7; column kcat/KM (M^-1 s^-1) = 2.1 x 10^4. captured primary segment: MhpC W264G | KM 125 uM | kcat 2.7 s^-1 | kcat/KM 2.1 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 125 uM; 1 uM is 1/1000 mM, so 125 / 1000 = 0.125 mM. kcat: printed Table 2 kcat cell 2.7 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 2.7 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 2.1 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 21000 / 1000 = 21.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 2.7 / 0.125 = 21.6 s^-1 mM^-1, against the printed catalytic-efficiency cell 21.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MhpC block, variant row W264G: KM = 125 uM; kcat = 2.7 s^-1; printed kcat/KM = 2.1 x 10^4 M^-1 s^-1.

row_label: Table 2, MhpC block, variant row W264G


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S112C to reconstruct the assayed variant sequence.


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

proof_lines: pH 7.5, 25°C, recombinant wild-type BphD, with 12940 mM methanol


column_label: Table III, Steady-state kinetic parameters of B. cepacia LB400 BphD with monochlorinated HOPDAs row 3-Cl HOPDA: Km column 0.54 (0.02) uM, kcat column 0.0089 (0.0001) s^-1, kcat/Km x 10^-5 column 0.16 (0.01) M^-1 s^-1.

row_label: 3-Cl HOPDA


column_label: Table III, Steady-state kinetic parameters of B. cepacia LB400 BphD with monochlorinated HOPDAs row 5-Cl HOPDA: Km column 4.9 (0.1) uM, kcat column 1.53 (0.01) s^-1, kcat/Km x 10^-5 column 3.11 (0.05) M^-1 s^-1.

row_label: 5-Cl HOPDA


column_label: Table III, Steady-state kinetic parameters of B. cepacia LB400 BphD with monochlorinated HOPDAs row 8-Cl HOPDA: Km column 0.33 (0.02) uM, kcat column 2.10 (0.03) s^-1, kcat/Km x 10^-5 column 64 (3) M^-1 s^-1.

row_label: 8-Cl HOPDA


column_label: Table III, Steady-state kinetic parameters of B. cepacia LB400 BphD with monochlorinated HOPDAs row 9-Cl HOPDA: Km column 0.46 (0.03) uM, kcat column 3.9 (0.1) s^-1, kcat/Km x 10^-5 column 85 (4) M^-1 s^-1.

row_label: 9-Cl HOPDA


column_label: Table III, Steady-state kinetic parameters of B. cepacia LB400 BphD with monochlorinated HOPDAs row 10-Cl HOPDA: Km column 0.13 (0.01) uM, kcat column 3.13 (0.04) s^-1, kcat/Km x 10^-5 column 246 (13) M^-1 s^-1.

row_label: 10-Cl HOPDA


column_label: Table III, Steady-state kinetic parameters of B. cepacia LB400 BphD with monochlorinated HOPDAs row HOPDA: Km column 0.19 (0.01) uM, kcat column 4.18 (0.03) s^-1, kcat/Km x 10^-5 column 225 (6) M^-1 s^-1.

row_label: HOPDA


enzyme_display_name: Nudix hydrolase 23, chloroplastic

substrate_name: FAD

assay_conditions_summary: cofactor FAD

enzyme: Nudix hydrolase 23, chloroplastic

substrate: FAD


assay_conditions_summary: cofactor ADP


enzyme_display_name: Nucleoside-triphosphatase THEP1

organism: Aquifex aeolicus (strain VF5)

assay_conditions_summary: buffer 25 uL; cofactor ATP

column_label: Abstract/Fig. 7 kinetic annotation for ATP; Km value 5.5 +/- 1.4 x 10^-6 M.

normalized_value_unit_evidence: 5.5 +/- 1.4 x 10^-6 M normalizes to 0.0055 mM, matching the export.

raw_value_unit_evidence: Paper reports Km = 5.5 +/- 1.4 x 10^-6 M for ATP.

row_label: ATP hydrolysis

table_label: Abstract and Fig. 7: aaTHEP1 hydrolyzes ATP and GTP obeying Michaelis-Menten equation

enzyme: Nucleoside-triphosphatase THEP1


substrate_name: GTP

column_label: Abstract/Fig. 7 kinetic annotation for GTP; Km value 45 +/- 25 x 10^-6 M.

normalized_value_unit_evidence: 45 +/- 25 x 10^-6 M normalizes to 0.045 mM, matching the export.

raw_value_unit_evidence: Paper reports Km = 45 +/- 25 x 10^-6 M for GTP.

row_label: GTP hydrolysis

substrate: GTP


column_label: Table 4, HMSH row HMMS, columns KM, kcat, kcat/KM.

row_label: HMSH / HMMS


column_label: Table 4, HMSH row HODA, columns KM, kcat, kcat/KM.

row_label: HMSH / HODA


column_label: Table 4, HMSH row 2-HMS, columns KM, kcat, kcat/KM.

row_label: HMSH / 2-HMS


enzyme_display_name: nucleoside-triphosphate phosphatase

organism: Bacteriophage phi-6

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines:
bacteriophage phi-6
P4
NTPase

enzyme: nucleoside-triphosphate phosphatase


substrate_name: UTP

substrate: UTP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H114A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H263A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S110A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S110G with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S40A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


enzyme_display_name: m7GpppX diphosphatase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: m7GpppG (homodimer)

proof_lines: kcat is 0.012 sec(-1) with m7GpppG as substrate (homodimer). kcat is 0.0015 sec(-1) with m7GpppG as substrate (heterodimer). kcat is 0.0017 sec(-1) with m7GDP as substrate (homodimer). kcat is 0.0005 sec(-1) with m7GDP as substrate (heterod

enzyme: m7GpppX diphosphatase

substrate: m7GpppG (homodimer)


substrate_name: m7GDP (homodimer)

substrate: m7GDP (homodimer)


organism: Dyella ginsengisoli

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148P to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148I 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.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148A to reconstruct the assayed variant sequence.


enzyme_display_name: cyclohexane-1,2-dione hydrolase

organism: Azoarcus sp.

proof_lines:
cyclohexane-1,2-dione hydrolase
Azoarcus sp. strain 22Lin
cyclohexane-1,2-dione

enzyme: cyclohexane-1,2-dione hydrolase


column_label: PMC2804191 HTML lines 1535-1560 define Table 2 columns and units; lines 1564-1567 give row HOPDA: Km 8 (1) uM, kcat 0.066 (0.005) s^-1, kcat/Km 9 (1) mM^-1 s^-1.

normalized_value_unit_evidence: Km 0.008 mM; kcat 0.066 s^-1; kcat/Km 9 s^-1*mM^-1 from the primary Table 2 HOPDA row. Exported kcat/Km is 8.25 s^-1*mM^-1 and does not equal the primary paper value.

table_label: Table 2: Steady-state kinetic parameters of HsaD with HOPDA, HOPODA, and DSHA


column_label: PMC2804191 HTML lines 1535-1560 define Table 2 columns and units; lines 1570-1573 give row HOPODA: Km 310 (70) uM, kcat 0.33 (0.06) s^-1, kcat/Km 1.06 (0.06) mM^-1 s^-1.

normalized_value_unit_evidence: Km 0.310 mM; kcat 0.33 s^-1; kcat/Km 1.06 s^-1*mM^-1 from the primary Table 2 HOPODA row. Exported kcat/Km is 1.0645161290322582 s^-1*mM^-1 and does not exactly equal the primary paper value.

row_label: HOPODA


enzyme_display_name: Nucleotide triphosphate diphosphatase NUDT15

organism: Mus musculus

column_label: Abstract reports mMTH2 protein hydrolyzes 8-oxo-dGTP to 8-oxo-dGMP, with Km of 32 microM.

raw_value_unit_evidence: Km raw_value=32 microM raw_unit=microM

row_label: Mouse MTH2 / 8-oxo-dGTP

table_label: PubMed XML abstract PMID 12767940


enzyme: Nucleotide triphosphate diphosphatase NUDT15


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148L to reconstruct the assayed variant sequence.


enzyme_display_name: diadenosine hexaphosphate hydrolase (ATP-forming)


enzyme: diadenosine hexaphosphate hydrolase (ATP-forming)


organism: Saccharomyces cerevisiae

substrate_name: 7-methylguanosine 5'-diphosphate

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)

substrate: 7-methylguanosine 5'-diphosphate


column_label: Table 2, Dcs1 homodimer row for m7GpppG, reports KM 0.14 uM, kcat 12.0 x 10^-3 s^-1, and independently printed kcat/KM 8.6 x 10^4 M^-1 s^-1.

row_label: Dcs1 homodimer / m7GpppG


substrate_name: dTTP

column_label: Table 1 reports dTTP Km 0.09 mM, Vmax 0.06 mM s^-1, kcat 43 s^-1, kcat/Km 503 mM^-1 s^-1, N 2.2; KM and kcat match, but kcat/Km differs from the current export

normalized_value_unit_evidence: KM normalized_value=0.09 normalized_unit=mM; kcat normalized_value=43 normalized_unit=s^-1; kcat_over_km normalized_value=503 normalized_unit=s^-1*mM^-1; current_export_kcat_over_km=477.77777777777777 s^-1*mM^-1

raw_value_unit_evidence: KM raw_value=0.09 raw_unit=mM; kcat raw_value=43 raw_unit=s^-1; kcat_over_km raw_value=503 raw_unit=s^-1*mM^-1 for dTTP

row_label: YhdE dTTP row; KM, kcat, and kcat/KM columns

table_label: PMID 25658941 PMC HTML Table 1

substrate: dTTP


column_label: Table 1 reports UTP Km 0.5 mM, Vmax 0.14 mM s^-1, kcat 95 s^-1, kcat/Km 191 mM^-1 s^-1, N 1.9; KM and kcat match, but kcat/Km differs from the current export

normalized_value_unit_evidence: KM normalized_value=0.5 normalized_unit=mM; kcat normalized_value=95 normalized_unit=s^-1; kcat_over_km normalized_value=191 normalized_unit=s^-1*mM^-1; current_export_kcat_over_km=190 s^-1*mM^-1

raw_value_unit_evidence: KM raw_value=0.5 raw_unit=mM; kcat raw_value=95 raw_unit=s^-1; kcat_over_km raw_value=191 raw_unit=s^-1*mM^-1 for UTP

row_label: YhdE UTP row; KM, kcat, and kcat/KM columns


enzyme_display_name: GTP cyclohydrolase II

organism: Meyerozyma guilliermondii

enzyme: GTP cyclohydrolase II