enzyme_display_name: UniProt P13981

organism: Pseudomonas aeruginosa

substrate_name: L-canavanine

smiles: C(CON=C(N)N)C(C(=O)O)N

enzyme: UniProt P13981

substrate: L-canavanine


substrate_name: L-arginine

source_db: skid

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY-NC-ND 4.0

km_unit: mM

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

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

data_origin: experimental

substrate: L-arginine

source: skid


enzyme_display_name: lysosomal Pro-Xaa carboxypeptidase

organism: Homo sapiens

substrate_name: prekallikrein

source_db: brenda

verification_status: unverified

kcat_display: Not reported

kcat_over_km_display: Not reported

source_license: CC BY 4.0

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

proof_lines: determined by an in vitro assay using human recombinant PRCP

enzyme: lysosomal Pro-Xaa carboxypeptidase

substrate: prekallikrein

status: unverified

source: brenda


enzyme_display_name: methionyl aminopeptidase

substrate_name: Met-Ala-Ser

smiles: CC(C(=O)NC(CO)C(=O)O)NC(=O)C(CCSC)N

enzyme: methionyl aminopeptidase

substrate: Met-Ala-Ser


enzyme_display_name: tripeptidyl-peptidase II

substrate_name: Ala-Ala-Phe-p-nitroanilide

enzyme: tripeptidyl-peptidase II

substrate: Ala-Ala-Phe-p-nitroanilide


enzyme_display_name: UniProt Q0P9V0

organism: Campylobacter jejuni subsp. jejuni serotype O:2

substrate_name: agmatine

smiles: C(CCN=C(N)N)CN

enzyme: UniProt Q0P9V0

substrate: agmatine


enzyme_display_name: UniProt Q9ZN18

organism: Helicobacter pylori

enzyme: UniProt Q9ZN18


enzyme_display_name: UniProt Q9UM07

substrate_name: benzoyl-L-arginine methyl ester

enzyme: UniProt Q9UM07

substrate: benzoyl-L-arginine methyl ester


substrate_name: benzoyl-L-arginine ethyl ester

substrate: benzoyl-L-arginine ethyl ester


substrate_name: benzoyl-L-arginine

proof_lines:
Raw SKiD Env: Temp=37°C, pH=-----
Raw SKiD Env: Temp=37°C, pH=7.5

substrate: benzoyl-L-arginine


enzyme_display_name: UniProt Q9Y2J8

substrate_name: Nalpha-benzoyl-L-arginine

enzyme: UniProt Q9Y2J8

substrate: Nalpha-benzoyl-L-arginine


enzyme_display_name: UniProt Q9ULC6

substrate_name: benzoyl-L-Arg ethyl ester

enzyme: UniProt Q9ULC6

substrate: benzoyl-L-Arg ethyl ester


substrate_name: benzoyl-L-Arg

substrate: benzoyl-L-Arg


enzyme_display_name: UniProt Q9I6K2

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

sequence_source: multiple

source_databases_merged: brenda skid

enzyme: UniProt Q9I6K2


enzyme_display_name: tripeptidyl-peptidase I

enzyme: tripeptidyl-peptidase I


enzyme_display_name: cytosol alanyl aminopeptidase

substrate_name: Val-p-nitroanilide

proof_lines: with 1 mM dithiothreitol, in 10 mM Tris-HCl, pH 7.4, at 37°C

enzyme: cytosol alanyl aminopeptidase

substrate: Val-p-nitroanilide


enzyme_display_name: dipeptidyl-peptidase IV

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y547F to reconstruct the assayed variant sequence.

mutation_type: substitution

enzyme: dipeptidyl-peptidase IV


substrate_name: Met-Pro-p-nitroanilide

proof_lines: in 40 mM HEPES, pH 8.0, and 100 mM NaCl, at 23°C

proof_lines: pH 7.5, 30°C, in presence of 0.01 mM CoCl2

substrate: Met-Pro-p-nitroanilide


proof_lines: extracted from human glioblastoma cells LNZ308

proof_lines: extracted from human glioblastoma cells LN18


enzyme_display_name: endothelin-converting enzyme 1

proof_lines: pH not specified in the publication, temperature not specified in the publication

proof_lines: in the presence of K49-P1-20, at pH 6.3 and 37°C

proof_lines: in the absence of K49-P1-20, at pH 6.3 and 37°C

enzyme: endothelin-converting enzyme 1


enzyme_display_name: diguanidinobutanase

organism: Unknown

substrate_name: Unknown

source_db: unknown

km_display: Not reported

source_license: see source

smiles: C(CCN=C(N)N)CN=C(N)N

enzyme: diguanidinobutanase

substrate: Unknown

source: unknown


smiles: C(CCCN=C(N)N)CCCN=C(N)N


smiles: C(CCCN=C(N)N)CCN=C(N)N


smiles: C(CCN=C(N)N)CCN=C(N)N


smiles: C(CCCN=C(N)N)CCN


smiles: C(CCN)CCN=C(N)N


substrate_name: L-Ala-L-Ala-L-Ala 4-nitroanilide

substrate: L-Ala-L-Ala-L-Ala 4-nitroanilide


enzyme_display_name: cytosine deaminase

organism: Pseudomonas chlororaphis subsp. aureofaciens

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

enzyme: cytosine deaminase


organism: Aspergillus fumigatus

substrate_name: cytosine

substrate: cytosine


enzyme_display_name: UniProt Q07729

organism: Saccharomyces cerevisiae

substrate_name: ammeline

enzyme: UniProt Q07729

substrate: ammeline


enzyme_display_name: UniProt P19079

organism: Bacillus subtilis

substrate_name: deoxycytidine

enzyme: UniProt P19079

substrate: deoxycytidine


substrate_name: cytidine

substrate: cytidine


enzyme_display_name: cytidine deaminase

organism: Mycobacterium tuberculosis

source_db: oed

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E47D with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

enzyme: cytidine deaminase

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E47Q with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.


substrate_name: BRI peptide (1-23)

proof_lines: pH 7.8, 25°C, glycosylated recombinant soluble enzyme ectodomain

proof_lines: pH 7.8, 25°C, deglycosylated recombinant soluble enzyme ectodomain bound to adenosine deaminase

substrate: BRI peptide (1-23)


enzyme_display_name: agmatinase

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

enzyme: agmatinase


enzyme_display_name: UniProt P11586

proof_lines:
Raw SKiD Env: Temp=30°C, pH=-----
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P11586


enzyme_display_name: UniProt Q9I2U6

enzyme: UniProt Q9I2U6


enzyme_display_name: Bifunctional protein FolD

organism: Photobacterium phosphoreum

substrate_name: NADP(+)

source_db: uniprot

enzyme: Bifunctional protein FolD

substrate: NADP(+)

source: uniprot


substrate_name: NAD(+)

substrate: NAD(+)


enzyme_display_name: UniProt O41078

organism: Paramecium bursaria Chlorella virus 1

substrate_name: dCTP

enzyme: UniProt O41078

substrate: dCTP


substrate_name: dCMP

substrate: dCMP


enzyme_display_name: UniProt P28248

organism: Escherichia coli

enzyme: UniProt P28248


substrate_name: collagen type I alpha-2 chain

proof_lines: 1-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C

proof_lines: 2-protonated enzyme, 50 mM Tris-HCl, 0.1 M NaCl, 10 mM CaCl2 plus 0.05% Brij 35,at pH 7.3 and 37°C

proof_lines: pH not specified in the publication, 37°C, MMP-1: 1-protonated

substrate: collagen type I alpha-2 chain


assay_conditions_summary: pH 4.3; 310.15 K; buffer sodium acetate

proof_lines: in sodium acetate buffer (50 mM, pH 5.0), 0.05% Triton X-100


enzyme_display_name: UniProt Q5SH52

organism: Thermus thermophilus

substrate_name: GTP

enzyme: UniProt Q5SH52

substrate: GTP


substrate_name: GDP

substrate: GDP


enzyme_display_name: tripeptidyl-peptidase II

substrate_name: Arg-Arg-Ala-(phospho)Ser-Val-Ala

enzyme: tripeptidyl-peptidase II

substrate: Arg-Arg-Ala-(phospho)Ser-Val-Ala


enzyme_display_name: cytosol nonspecific dipeptidase

substrate_name: anserine

proof_lines:
pH 8.0, 37°C
pH 8.0, 37°C, calculated by BRENDA

enzyme: cytosol nonspecific dipeptidase

substrate: anserine


enzyme_display_name: UniProt P0C2P0

organism: Aspergillus terreus

substrate_name: blasticidin S

enzyme: UniProt P0C2P0

substrate: blasticidin S


enzyme_display_name: UniProt O28344

organism: Archaeoglobus fulgidus

enzyme: UniProt O28344


enzyme_display_name: UniProt Q9HZ64

substrate_name: adenosine

enzyme: UniProt Q9HZ64

substrate: adenosine


enzyme_display_name: UniProt A6Q234

organism: Nitratiruptor sp. SB155-2

enzyme: UniProt A6Q234


enzyme_display_name: UniProt Q9RW45

organism: Deinococcus radiodurans

enzyme: UniProt Q9RW45


enzyme_display_name: membrane dipeptidase

organism: Homo sapiens

substrate_name: L-Leu-L-Leu

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

proof_lines:
enzyme form F
enzyme form S

enzyme: membrane dipeptidase

substrate: L-Leu-L-Leu


enzyme_display_name: S-adenosylhomocysteine deaminase

organism: Rhizobium rhizogenes

substrate_name: terbuthylazine

proof_lines: pH and temperature not specified in the publication

enzyme: S-adenosylhomocysteine deaminase

substrate: terbuthylazine


organism: Streptomyces albus

substrate_name: S-adenosyl-L-homocysteine

substrate: S-adenosyl-L-homocysteine


enzyme_display_name: sepiapterin deaminase

organism: Bombyx mori

substrate_name: sepiapterin

enzyme: sepiapterin deaminase

substrate: sepiapterin


enzyme_display_name: tRNA(adenine(34)) deaminase

organism: Trypanosoma brucei

substrate_name: adenine34 in tRNAVal

proof_lines: 27°C, pH 8.0, mutant enzyme V254L, mutation in subunit ADAT3

enzyme: tRNA(adenine(34)) deaminase

substrate: adenine34 in tRNAVal


proof_lines: 27°C, pH 8.0, mutant enzyme C136A, mutation in subunit ADAT2


proof_lines: 27°C, pH 8.0, mutant enzyme V254T, mutation in subunit ADAT2


enzyme_display_name: nitrilase

organism: Pseudomonas putida

enzyme: nitrilase


organism: Alcaligenes sp.

substrate_name: mandelonitrile

substrate: mandelonitrile


organism: Synechocystis sp. PCC 6803

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F202V with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P194A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P194A/F202V to reconstruct the assayed variant sequence.


enzyme_display_name: Arylacetonitrilase

organism: Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4)

substrate_name: phenylacetonitrile

enzyme: Arylacetonitrilase

substrate: phenylacetonitrile


substrate_name: (R,S)-mandelonitrile

substrate: (R,S)-mandelonitrile


organism: Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371)


enzyme_display_name: 8-oxoguanine deaminase

organism: unidentified

substrate_name: guanine

enzyme: 8-oxoguanine deaminase

substrate: guanine


substrate_name: isocytosine

substrate: isocytosine


mutation_signature: Δ5

mutation_type: deletion

proof_lines: 27°C, pH 8.0, mutant enzyme C-terDELTA5, mutation in subunit ADAT2


enzyme_display_name: S-methyl-5'-thioadenosine deaminase

organism: Plasmodium falciparum

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T174I to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme T174I

enzyme: S-methyl-5'-thioadenosine deaminase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F136L to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme F136L


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D176A/L179H with inferred residue-numbering offset -32 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme D176A/L179H


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D176M with inferred residue-numbering offset -32 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme D176M


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T174A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme T174A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D176A with inferred residue-numbering offset -32 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme D176A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C27Q/L227I with inferred residue-numbering offset +16 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme C27Q/L227I


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

proof_lines: pH 8.0, temperature not specified in the publication, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L179H with inferred residue-numbering offset -32 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme L179H


organism: Amycolatopsis methanolica


organism: Methanocaldococcus jannaschii

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

assay_conditions_summary: pH 9

proof_lines: pH and temperature not specified in the publication, mutant enzyme Y136R/E150R

proof_lines: mutant enzyme Y136R/E150R, at pH 9.0 and 60°C


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


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


proof_lines: pH and temperature not specified in the publication, wild-type enzyme


proof_lines: pH and temperature not specified in the publication, mutant enzyme E150R


proof_lines: pH and temperature not specified in the publication, mutant enzyme Y136R


enzyme_display_name: 5'-deoxyadenosine deaminase

organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

substrate_name: 5'-deoxyadenosine (at pH 9 and 60 degrees Celsius)

proof_lines: kcat is 120000 sec(-1) for 5'-deoxyadenosine deamination. kcat is 160 sec(-1) for S-methyl-5'-thioadenosine deamination. kcat is 1300 sec(-1) for S-adenosyl-L-homocysteine deamination. kcat is 110 sec(-1) for adenosine deamination (at pH 9

enzyme: 5'-deoxyadenosine deaminase


substrate_name: S-methyl-5'-thioadenosine (at pH 9 and 60 degrees Celsius)


substrate_name: S-adenosyl-L-homocysteine (at pH 9 and 60 degrees Celsius)


substrate_name: adenosine (at pH 9 and 60 degrees Celsius)


organism: Pectobacterium atrosepticum

substrate_name: D-serine

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

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

proof_lines: pH and temperature not specified in the publication

substrate: D-serine


substrate_name: D-cysteine

smiles: C(C(C(=O)O)N)S

substrate: D-cysteine


substrate_name: beta-Chloro-D-alanine

smiles: C(C(C(=O)O)N)Cl

substrate: beta-Chloro-D-alanine


enzyme_display_name: glucosamine-6-phosphate deaminase

substrate_name: D-glucosamine 6-phosphate

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

mutation_type: truncation

proof_lines: recombinant isozyme GNPDA1 268 truncation mutant, pH 8.0, 30°C, kinetic method 2

enzyme: glucosamine-6-phosphate deaminase

substrate: D-glucosamine 6-phosphate


proof_lines: recombinant isozyme GNPDA1 275 truncation mutant, pH 8.0, 30°C, kinetic method 1

proof_lines: recombinant isozyme GNPDA1 275 truncation mutant, pH 8.0, 30°C, kinetic method 2


proof_lines: recombinant wild-type isozyme GNPDA1, pH 8.0, 30°C, kinetic method 1, in presence of saturating concentration of N-acetylglucosamine 6-phosphate

proof_lines: recombinant wild-type isozyme GNPDA1, pH 8.0, 30°C, kinetic method 2, in presence of saturating concentration of N-acetylglucosamine 6-phosphate

proof_lines: recombinant wild-type isozyme GNPDA1, pH 8.0, 30°C, kinetic method 1, in absence of N-acetylglucosamine 6-phosphate


verification_status: verified

column_label: Table 2 row WT / 5'-dA; column Mean Km (mM) +/- SD = 0.014 +/- 0.0012

row_label: WT; substrate 5'-dA

substrate: 5'-deoxyadenosine (at pH 9 and 60 degrees Celsius)

status: verified


substrate: S-methyl-5'-thioadenosine (at pH 9 and 60 degrees Celsius)


column_label: Table 2 row WT / SAH; column Mean Km (mM) +/- SD = 1.1 +/- 1.3

normalized_value_unit_evidence: Km 1.1 mM

row_label: WT; substrate SAH

substrate: S-adenosyl-L-homocysteine (at pH 9 and 60 degrees Celsius)


column_label: Table 2 row WT / Ad; column Mean Km (mM) +/- SD = 0.15 +/- 0.0047

normalized_value_unit_evidence: Km 0.15 mM

row_label: WT; substrate Ad

substrate: adenosine (at pH 9 and 60 degrees Celsius)


enzyme_display_name: aliphatic nitrilase

organism: Unknown

substrate_name: Unknown

enzyme: aliphatic nitrilase

substrate: Unknown


organism: Enterobacter cancerogenus


organism: Shewanella denitrificans

substrate_name: alpha-D-glucosamine 6-phosphate

substrate: alpha-D-glucosamine 6-phosphate


enzyme_display_name: GTP cyclohydrolase II

organism: Streptomyces coelicolor

substrate_name: GTP

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M120D to reconstruct the assayed variant sequence.

proof_lines: M120D variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol

enzyme: GTP cyclohydrolase II

substrate: GTP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y326F to reconstruct the assayed variant sequence.

proof_lines: variant Y326F, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M120W to reconstruct the assayed variant sequence.

proof_lines: M120W variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M120E to reconstruct the assayed variant sequence.

proof_lines: M120E variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y123F with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

proof_lines: SCO 2687, variant Y123F, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y326M to reconstruct the assayed variant sequence.

proof_lines: variant Y326M, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M120H to reconstruct the assayed variant sequence.

proof_lines: M120H variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O88011 and applied mutation signature M120T to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetic Parameters and Product Distributions Observed with Native Recombinant M120 Variants of SCO 6655), variant row 'Thr'; column 'KM(GTP) (uM)' = 150; column 'kcat (min-1)' = 0.34; column 'kcat/KM(GTP) (M-1 min-1)' = 2 x 10^3.

raw_value_unit_evidence: Table 3, variant row 'Thr': KM(GTP) (uM) = 150; kcat (min-1) = 0.34; printed kcat/KM(GTP) (M-1 min-1) = 2 x 10^3.

row_label: Table 3, variant row 'Thr'

table_label: Table 3: Steady-State Kinetic Parameters and Product Distributions Observed with Native Recombinant M120 Variants of SCO 6655 (Biochemistry 2008, 47(8):2592-2600)

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O88011 and applied mutation signature M120A to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetic Parameters and Product Distributions Observed with Native Recombinant M120 Variants of SCO 6655), variant row 'Ala'; column 'KM(GTP) (uM)' = 59; column 'kcat (min-1)' = 0.7; column 'kcat/KM(GTP) (M-1 min-1)' = 1.2 x 10^4.

raw_value_unit_evidence: Table 3, variant row 'Ala': KM(GTP) (uM) = 59; kcat (min-1) = 0.7; printed kcat/KM(GTP) (M-1 min-1) = 1.2 x 10^4.

row_label: Table 3, variant row 'Ala'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O88011 and applied mutation signature M120F to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetic Parameters and Product Distributions Observed with Native Recombinant M120 Variants of SCO 6655), variant row 'Phe'; column 'KM(GTP) (uM)' = 19; column 'kcat (min-1)' = 0.78; column 'kcat/KM(GTP) (M-1 min-1)' = 4.1 x 10^4.

raw_value_unit_evidence: Table 3, variant row 'Phe': KM(GTP) (uM) = 19; kcat (min-1) = 0.78; printed kcat/KM(GTP) (M-1 min-1) = 4.1 x 10^4.

row_label: Table 3, variant row 'Phe'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O88011 and applied mutation signature M120G to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetic Parameters and Product Distributions Observed with Native Recombinant M120 Variants of SCO 6655), variant row 'Gly'; column 'KM(GTP) (uM)' = 190; column 'kcat (min-1)' = 0.95; column 'kcat/KM(GTP) (M-1 min-1)' = 5.0 x 10^3.

raw_value_unit_evidence: Table 3, variant row 'Gly': KM(GTP) (uM) = 190; kcat (min-1) = 0.95; printed kcat/KM(GTP) (M-1 min-1) = 5.0 x 10^3.

row_label: Table 3, variant row 'Gly'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O88011 and applied mutation signature M120C to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetic Parameters and Product Distributions Observed with Native Recombinant M120 Variants of SCO 6655), variant row 'Cys'; column 'KM(GTP) (uM)' = 67; column 'kcat (min-1)' = 1.1; column 'kcat/KM(GTP) (M-1 min-1)' = 1.6 x 10^4.

raw_value_unit_evidence: Table 3, variant row 'Cys': KM(GTP) (uM) = 67; kcat (min-1) = 1.1; printed kcat/KM(GTP) (M-1 min-1) = 1.6 x 10^4.

row_label: Table 3, variant row 'Cys'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O88011 and applied mutation signature M120I to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetic Parameters and Product Distributions Observed with Native Recombinant M120 Variants of SCO 6655), variant row 'Ile'; column 'KM(GTP) (uM)' = 15; column 'kcat (min-1)' = 1.3; column 'kcat/KM(GTP) (M-1 min-1)' = 8.7 x 10^4.

raw_value_unit_evidence: Table 3, variant row 'Ile': KM(GTP) (uM) = 15; kcat (min-1) = 1.3; printed kcat/KM(GTP) (M-1 min-1) = 8.7 x 10^4.

row_label: Table 3, variant row 'Ile'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9KYI5 and applied mutation signature D127A to reconstruct the assayed variant sequence.

column_label: Table 1 (Steady-State Kinetic Parameters and Product Distributions Observed with His6-Tagged Variants of SCO 2687), variant row 'Asp127Ala'; column 'KM(GTP) (uM)' = 85; column 'kcat (min-1)' = 1.3; column 'kcat/KM(GTP) (M-1 min-1)' = 1.6 x 10^4.

raw_value_unit_evidence: Table 1, variant row 'Asp127Ala': KM(GTP) (uM) = 85; kcat (min-1) = 1.3; printed kcat/KM(GTP) (M-1 min-1) = 1.6 x 10^4.

row_label: Table 1, variant row 'Asp127Ala'

table_label: Table 1: Steady-State Kinetic Parameters and Product Distributions Observed with His6-Tagged Variants of SCO 2687 (Biochemistry 2008, 47(8):2592-2600)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O88011 and applied mutation signature M120Y to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetic Parameters and Product Distributions Observed with Native Recombinant M120 Variants of SCO 6655), variant row 'Tyr'; column 'KM(GTP) (uM)' = 8; column 'kcat (min-1)' = 1.4; column 'kcat/KM(GTP) (M-1 min-1)' = 1.9 x 10^5.

raw_value_unit_evidence: Table 3, variant row 'Tyr': KM(GTP) (uM) = 8; kcat (min-1) = 1.4; printed kcat/KM(GTP) (M-1 min-1) = 1.9 x 10^5.

row_label: Table 3, variant row 'Tyr'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O88011 and applied mutation signature M120S to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetic Parameters and Product Distributions Observed with Native Recombinant M120 Variants of SCO 6655), variant row 'Ser'; column 'KM(GTP) (uM)' = 33; column 'kcat (min-1)' = 1.4; column 'kcat/KM(GTP) (M-1 min-1)' = 4 x 10^4.

raw_value_unit_evidence: Table 3, variant row 'Ser': KM(GTP) (uM) = 33; kcat (min-1) = 1.4; printed kcat/KM(GTP) (M-1 min-1) = 4 x 10^4.

row_label: Table 3, variant row 'Ser'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O88011 and applied mutation signature M120N to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetic Parameters and Product Distributions Observed with Native Recombinant M120 Variants of SCO 6655), variant row 'Asn'; column 'KM(GTP) (uM)' = 67; column 'kcat (min-1)' = 1.8; column 'kcat/KM(GTP) (M-1 min-1)' = 2.7 x 10^4.

raw_value_unit_evidence: Table 3, variant row 'Asn': KM(GTP) (uM) = 67; kcat (min-1) = 1.8; printed kcat/KM(GTP) (M-1 min-1) = 2.7 x 10^4.

row_label: Table 3, variant row 'Asn'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O88011 and applied mutation signature M120Q to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetic Parameters and Product Distributions Observed with Native Recombinant M120 Variants of SCO 6655), variant row 'Gln'; column 'KM(GTP) (uM)' = 11; column 'kcat (min-1)' = 2.0; column 'kcat/KM(GTP) (M-1 min-1)' = 1.8 x 10^5.

raw_value_unit_evidence: Table 3, variant row 'Gln': KM(GTP) (uM) = 11; kcat (min-1) = 2.0; printed kcat/KM(GTP) (M-1 min-1) = 1.8 x 10^5.

row_label: Table 3, variant row 'Gln'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9KYI5 and applied mutation signature Y123M to reconstruct the assayed variant sequence.

column_label: Table 2 (Zinc Content, Steady-State Kinetic Parameters, and Product Distributions Observed with Wild-Type and Met, Tyr, and Phe Site-Directed Variants of GCH II Intragenomic Homologues of S. coelicolor), variant row 'Tyr123Met'; column 'KM(GTP) (uM)' = 48; column 'kcat (min-1)' = 5.8; column 'kcat/KM(GTP) (M-1 min-1)' = 1.2 x 10^5.

raw_value_unit_evidence: Table 2, variant row 'Tyr123Met': KM(GTP) (uM) = 48; kcat (min-1) = 5.8; printed kcat/KM(GTP) (M-1 min-1) = 1.2 x 10^5.

row_label: Table 2, variant row 'Tyr123Met'

table_label: Table 2: Zinc Content, Steady-State Kinetic Parameters, and Product Distributions Observed with Wild-Type and Met, Tyr, and Phe Site-Directed Variants of GCH II Intragenomic Homologues of S. coelicolor (Biochemistry 2008, 47(8):2592-2600)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M120K to reconstruct the assayed variant sequence.

proof_lines: M120K variant, 1 mM substrate, 0.1 M Tris-HCl, pH 8, 5 mM MgCl2, 0.5 mM dithiothreitol


enzyme_display_name: single-stranded DNA cytosine deaminase

organism: Homo sapiens

substrate_name: TTCA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H29N with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

enzyme: single-stranded DNA cytosine deaminase

substrate: TTCA


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

proof_lines: APOBEC3A loop 1 lengthening, pH 7.5, 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H29S with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H29R with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature W15Y/W224Y/Y254W to reconstruct the assayed variant sequence.

proof_lines: mutant W15Y/W224Y/Y254W, pH 7.5, S0.5-value 0.5 mM


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature W15Y/F174W/W224Y to reconstruct the assayed variant sequence.

proof_lines: mutant W15Y/F174W/W224Y, pH 7.5, S0.5-value 3.4 mM


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature W15Y to reconstruct the assayed variant sequence.

proof_lines:
mutant W15Y, pH 7.5
mutant W15Y, pH 7.5, S0.5-value 5.8 mM


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature W224Y to reconstruct the assayed variant sequence.

proof_lines:
mutant W224Y, pH 7.5
mutant W224Y, pH 7.5, S0.5-value 4.8 mM


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature W15Y/W224Y to reconstruct the assayed variant sequence.

proof_lines: mutant W15Y/W224Y, pH 7.5, S0.5-value 5.0 mM


enzyme_display_name: Adenosine deaminase

organism: Plasmodium cynomolgi (strain B)

substrate_name: adenosine (at pH 8)

proof_lines: kcat is 5.3 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.31 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:19728741).

enzyme: Adenosine deaminase

substrate: adenosine (at pH 8)


substrate_name: 5'-methylthioadenosine (MTA) (at pH 8)

substrate: 5'-methylthioadenosine (MTA) (at pH 8)


organism: Giardia duodenalis

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

assay_conditions_summary: pH 7

proof_lines: HisC-tagged wild type enzyme, with D-fructose 6-phosphate as substrate, at pH 7.0 and 37°C

proof_lines: untagged wild type enzyme, with D-fructose 6-phosphate as substrate, at pH 7.0 and 37°C

proof_lines: HisN-tagged wild type enzyme, with D-fructose 6-phosphate as substrate, at pH 7.0 and 37°C


substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


enzyme_display_name: UniProt P46926

proof_lines: kcat is 228 sec(-1) for conversion of alpha-D-glucosamine 6-phosphate into beta-D-fructose 6-phosphate (in the presence of GlcNAc6P). kcat is 0.14 sec(-1) for conversion of alpha-D-glucosamine 6-phosphate into beta-D-fructose 6-phosphate (i

source_databases_merged: skid uniprot

enzyme: UniProt P46926


enzyme_display_name: Glucosamine-6-phosphate deaminase 1

substrate_name: beta-D-fructose 6-phosphate (in the presence of GlcNAc6P)

enzyme: Glucosamine-6-phosphate deaminase 1


substrate_name: NH4(+) (in the presence of GlcNAc6P)

substrate: NH4(+) (in the presence of GlcNAc6P)


organism: Plasmodium knowlesi

proof_lines: kcat is 6.8 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 0.51 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:19728741).


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

substrate_name: guanine

proof_lines: kcat is 3.3 sec(-1) with guanine as substrate. kcat is 3.9 sec(-1) with isocytosine as substrate.

substrate: guanine


substrate_name: isocytosine

substrate: isocytosine


organism: Plasmodium berghei (strain Anka)

column_label: PMC Table 2 row P. berghei Adenosine Km column reports 57 +/- 2 uM.

normalized_value_unit_evidence: Km normalized_value=0.057 mM

raw_value_unit_evidence: Km raw_value=57 raw_unit=uM

row_label: P. berghei

table_label: Table 2


column_label: PMC Table 2 row P. berghei MTA Km column reports 4.4 +/- 0.6 uM.

normalized_value_unit_evidence: Km normalized_value=0.0044 mM

raw_value_unit_evidence: Km raw_value=4.4 raw_unit=uM


enzyme_display_name: UniProt Q9X034

organism: Thermotoga maritima

substrate_name: adenosine

proof_lines: pH and temperature not specified in the publication

source_databases_merged: brenda skid uniprot

enzyme: UniProt Q9X034

substrate: adenosine


assay_conditions_summary: pH 8; 303.15 K; buffer composition Primary measurement evidence: evidence location type: figure

column_label: Figure S3: UV spectra for the conversion of SAH, MTA, and adenosine to SIH, MTI, and inosine as catalyzed by Tm0936 and the associated plots for the measurement of the kinetic constants (Nature 2007 Supplementary Information, PDF page 18); kinetics panel titled 'Kinetic Parameters for Tm0936 with 5'-Methylthioadenosine pH 8.0 and 30 oC'; parameter line 'kcat' = 7.2 s-1; parameter line 'Km' = 44 uM; parameter line 'kcat/Km' = 1.4 x 10^5 M-1s-1; parameter line 'Ki' = 1.9 mM (every value printed as a numeral with its standard deviation).

normalized_value_unit_evidence: kcat: printed Figure S3 panel line kcat = 7.2 s^-1; the printed unit s^-1 is already the export unit (this panel prints no min^-1 kinetic value), so no unit conversion applies and the paper value is 7.2 s^(-1); the exported value is 7.2 s^(-1). Km: printed Figure S3 panel line Km = 44 uM; 44 / 1000 = 0.044 mM; the paper value is 0.044 mM; the exported value is 0.044 mM. kcat/Km: printed Figure S3 panel line kcat/Km = 1.4 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.4 x 10^5 / 1000 = 140.0 s^(-1)*mM^(-1); the exported value is 163.63636363636365 s^(-1)*mM^(-1), the full-precision quotient of the two printed component values. Ki: printed Figure S3 panel line Ki = 1.9 mM; the catalog row stores no Ki value and this pass does not add one.

raw_value_unit_evidence: Figure S3, kinetics panel 'Kinetic Parameters for Tm0936 with 5'-Methylthioadenosine pH 8.0 and 30 oC': kcat = 7.2 s^-1; Km = 44 uM; printed kcat/Km = 1.4 x 10^5 M^-1 s^-1; printed Ki = 1.9 mM.

row_label: Figure S3, kinetics panel titled 'Kinetic Parameters for Tm0936 with 5'-Methylthioadenosine pH 8.0 and 30 oC'


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K208E to reconstruct the assayed variant sequence.

proof_lines: mutant K208E, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate


sequence_variant_note: Mutation signature R172A/K208E could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant R172A/K208E, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K208V to reconstruct the assayed variant sequence.

proof_lines: mutant K208V, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature R172A to reconstruct the assayed variant sequence.

proof_lines: mutant R172A, Michaelis-Hill equation, presence of saturating concentration of allosteric activator N-acetylglucose-6-phosphate


enzyme_display_name: inorganic diphosphatase

organism: Pyrococcus furiosus

substrate_name: ADP

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

enzyme: inorganic diphosphatase

substrate: ADP


substrate_name: UDP

substrate: UDP


substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: GDP

substrate: GDP


substrate_name: CDP

substrate: CDP


substrate_name: IDP

substrate: IDP


substrate_name: ATP

substrate: ATP


substrate_name: CTP

substrate: CTP


substrate_name: UTP

substrate: UTP


substrate_name: ITP

substrate: ITP


substrate_name: Triphosphate

substrate: Triphosphate


substrate_name: diphosphate

substrate: diphosphate


enzyme_display_name: UniProt P37487

organism: Bacillus subtilis

substrate_name: imidodiphosphoric acid

enzyme: UniProt P37487

substrate: imidodiphosphoric acid


enzyme_display_name: UniProt P56153

organism: Helicobacter pylori

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

enzyme: UniProt P56153


enzyme_display_name: UniProt P95765

organism: Streptococcus gordonii

enzyme: UniProt P95765


substrate_name: GTP

substrate: GTP


enzyme_display_name: Nucleoside triphosphate pyrophosphohydrolase/pyrophosphatase MazG

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

substrate_name: CTP (at pH 8 and at 70 degrees Celsius)

substrate: CTP (at pH 8 and at 70 degrees Celsius)


substrate_name: dGTP (at pH 8 and at 70 degrees Celsius)

enzyme: Nucleoside triphosphate pyrophosphohydrolase/pyrophosphatase MazG


substrate_name: GTP (at pH 8 and at 70 degrees Celsius)

substrate: GTP (at pH 8 and at 70 degrees Celsius)


substrate_name: ATP (at pH 8 and at 70 degrees Celsius)

substrate: ATP (at pH 8 and at 70 degrees Celsius)


substrate_name: UTP (at pH 8 and at 70 degrees Celsius)

substrate: UTP (at pH 8 and at 70 degrees Celsius)


substrate_name: dTTP (at pH 8 and at 70 degrees Celsius)


substrate_name: dCTP (at pH 8 and at 70 degrees Celsius)


substrate_name: dATP (at pH 8 and at 70 degrees Celsius)


enzyme_display_name: Pyrophosphatase PpaX

organism: Bacillus subtilis (strain 168)

substrate_name: pyrophosphate

enzyme: Pyrophosphatase PpaX

substrate: pyrophosphate


enzyme_display_name: UniProt P97687

organism: Rattus norvegicus

substrate_name: AMPCPP

enzyme: UniProt P97687

substrate: AMPCPP


enzyme_display_name: UniProt Q27895

organism: Toxoplasma gondii

substrate_name: ATP

enzyme: UniProt Q27895


enzyme_display_name: Apyrase 2

organism: Arabidopsis thaliana

enzyme: Apyrase 2


enzyme_display_name: Apyrase 1

enzyme: Apyrase 1


enzyme_display_name: UniProt P84142

organism: Pyrococcus horikoshii

substrate_name: benzoyl phosphate

proof_lines:
Raw SKiD Env: Temp=45°C, pH=5.3
Raw SKiD Env: Temp=40°C, pH=5.3
Raw SKiD Env: Temp=30°C, pH=5.3

enzyme: UniProt P84142

substrate: benzoyl phosphate


enzyme_display_name: UniProt A5F8G9

organism: Vibrio cholerae

substrate_name: acetyl phosphate

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=and
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt A5F8G9

substrate: acetyl phosphate


organism: Plasmodium vivax (strain Salvador I)

substrate_name: adenosine (at pH 8)

column_label: PMC Table 2 row P. vivax Adenosine Km column reports 60 +/- 6 uM.

normalized_value_unit_evidence: Km normalized_value=0.06 mM

raw_value_unit_evidence: Km raw_value=60 raw_unit=uM

row_label: P. vivax

substrate: adenosine (at pH 8)


substrate_name: 5'-methylthioadenosine (MTA) (at pH 8)

column_label: PMC Table 2 row P. vivax MTA Km column reports 9.5 +/- 0.8 uM.

normalized_value_unit_evidence: Km normalized_value=0.0095 mM

raw_value_unit_evidence: Km raw_value=9.5 raw_unit=uM

substrate: 5'-methylthioadenosine (MTA) (at pH 8)


enzyme_display_name: glucosamine-6-phosphate deaminase

organism: Escherichia coli

substrate_name: D-glucosamine 6-phosphate

proof_lines: wild-type, modified with bimane at C164, pH 7.5, 30°C

proof_lines: wild-type, modified with bimane at C206, pH 7.5, 30°C

proof_lines: wild-type, modified with dansyl-aminoethyl moiety at C164, pH 7.5, 30°C

enzyme: glucosamine-6-phosphate deaminase

substrate: D-glucosamine 6-phosphate


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

proof_lines: mutant C118S/C228S/C239S, pH 7.5, 30°C, calculated from Hill-equation in absence of allosteric activator


substrate_name: D-fructose 6-phosphate

proof_lines: pH 7.7, 30°C, in presence of 0.5 mM N-acetylglucosamine 6-phosphate

substrate: D-fructose 6-phosphate


proof_lines: pH 7.7, 30°C, in presence of 0.25 mM N-acetylglucosamine 6-phosphate


enzyme_display_name: Adenosine deaminase

organism: Plasmodium falciparum (isolate 3D7)

proof_lines: kcat is 4.1 sec(-1) with adenosine as substrate (PubMed:31002765). kcat is 5.6 sec(-1) with adenosine as substrate (PubMed:19728741). kcat is 13.92 sec(-1) with 5'-methylthioadenosine as substrate (PubMed:31002765). kcat is 5.8 sec(-1) with

enzyme: Adenosine deaminase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y254F to reconstruct the assayed variant sequence.

proof_lines: pH 7.7, 30°C, mutant enzyme Y254F in presence of N-acetylglucosamine 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y254T to reconstruct the assayed variant sequence.

proof_lines: pH 7.7, 30°C, mutant enzyme Y254T in presence of N-acetylglucosamine 6-phosphate


enzyme_display_name: Bifunctional TENA-E protein

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

proof_lines: kcat is 0.00281 sec(-1) for formylamino-HMP. kcat is 0.00015 sec(-1) for amino-HMP.

enzyme: Bifunctional TENA-E protein


organism: Methanopyrus kandleri

proof_lines:
recombinant enzyme
1 M K2HPO4
0.6 M K2HPO4


enzyme_display_name: Glucosamine-6-phosphate deaminase 1

organism: Bos taurus

proof_lines: kcat is 61.6 sec(-1) for conversion of alpha-D-glucosamine 6-phosphate into beta-D-fructose 6-phosphate (in the presence of GlcNAc6P). kcat is 0.37 sec(-1) for conversion of alpha-D-glucosamine 6-phosphate into beta-D-fructose 6-phosphate (

enzyme: Glucosamine-6-phosphate deaminase 1


substrate_name: NH4(+) (in the presence of GlcNAc6P)

substrate: NH4(+) (in the presence of GlcNAc6P)


enzyme_display_name: Aminopyrimidine aminohydrolase

proof_lines: kcat is 1.7 min(-1) for the hydrolysis of 4-amino-5-aminomethyl-2-methylpyrimidine.

enzyme: Aminopyrimidine aminohydrolase


proof_lines: kcat is 22.0 min(-1) for the hydrolysis of 4-amino-5-aminomethyl-2-methylpyrimidine. Catalyzes the hydrolysis of aminopyrimidine 100 times faster than the hydrolysis of thiamine.


enzyme_display_name: apyrase

substrate_name: dGTP

enzyme: apyrase

substrate: dGTP


substrate_name: dATP

substrate: dATP


enzyme_display_name: UniProt O35000

substrate_name: alpha-D-glucosamine 6-phosphate

column_label: Official JBC full-text visible article, abstract and kinetic analysis prose for BsuNagB

normalized_value_unit_evidence: paper kcat 28 s^-1 and Km 0.13 mM; sheet kcat 110 s^-1 and Km 1.5 mM

raw_value_unit_evidence: BsuNagB kcat 28 s-1; Km(app) 0.13 mM; kinetic text kcat = 28 +/- 6 s-1 and Km(GlcN-6-P) = 0.13 +/- 0.02 mM

row_label: BsuNagB monomeric glucosamine-6-phosphate deaminase; GlcN-6-P

table_label: Official JBC full-text visible prose

enzyme: UniProt O35000

substrate: alpha-D-glucosamine 6-phosphate


substrate_name: glucosamine 6-phosphate

normalized_value_unit_evidence: Km 0.13 mM

substrate: glucosamine 6-phosphate


organism: Staphylococcus aureus (strain MRSA252)

substrate_name: thiamine

proof_lines: kcat is 4.07 msec(-1) for the hydrolysis of thiamine.

substrate: thiamine


enzyme_display_name: UniProt Q9BY32

organism: Homo sapiens

substrate_name: dITP

enzyme: UniProt Q9BY32

substrate: dITP


substrate_name: xanthosine 5'-triphosphate

substrate: xanthosine 5'-triphosphate


substrate_name: ITP

substrate: ITP


enzyme_display_name: UniProt P97675

enzyme: UniProt P97675


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


substrate_name: ADP-ribose

substrate: ADP-ribose


enzyme_display_name: Nucleoside triphosphate pyrophosphohydrolase/pyrophosphatase MazG

substrate_name: CTP (at pH 8 and at 70 degrees Celsius)

substrate: CTP (at pH 8 and at 70 degrees Celsius)


substrate_name: dGTP (at pH 8 and at 70 degrees Celsius)

enzyme: Nucleoside triphosphate pyrophosphohydrolase/pyrophosphatase MazG


substrate_name: GTP (at pH 8 and at 70 degrees Celsius)

substrate: GTP (at pH 8 and at 70 degrees Celsius)


substrate_name: ATP (at pH 8 and at 70 degrees Celsius)

substrate: ATP (at pH 8 and at 70 degrees Celsius)


substrate_name: UTP (at pH 8 and at 70 degrees Celsius)

substrate: UTP (at pH 8 and at 70 degrees Celsius)


substrate_name: dTTP (at pH 8 and at 70 degrees Celsius)


substrate_name: dCTP (at pH 8 and at 70 degrees Celsius)


substrate_name: dATP (at pH 8 and at 70 degrees Celsius)


enzyme_display_name: Endopolyphosphatase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: dATP

enzyme: Endopolyphosphatase

substrate: dATP


enzyme_display_name: UniProt Q9UKK9

substrate_name: ADP-mannose

enzyme: UniProt Q9UKK9

substrate: ADP-mannose


substrate_name: NAD(+)


substrate_name: NADH


substrate_name: NADP(+)


substrate_name: NADPH


substrate_name: ATP


substrate_name: CTP


substrate_name: GTP


substrate_name: TTP


substrate_name: ADP-ribose


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


substrate_name: D-glucosamine 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y121W with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

substrate: D-glucosamine 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y121T with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


enzyme_display_name: Bifunctional TH2 protein, mitochondrial

substrate_name: thiamine monophosphate

proof_lines: kcat is 13.5 sec(-1) for thiamine monophosphate.

enzyme: Bifunctional TH2 protein, mitochondrial

substrate: thiamine monophosphate


enzyme_display_name: UniProt P0A759

substrate_name: alpha-D-glucosamine 6-phosphate

proof_lines:
recombinant enzyme, pH 7.4, 37°C
pH 7.7, 30°C
pH 7.8, 25°C

enzyme: UniProt P0A759

substrate: alpha-D-glucosamine 6-phosphate


enzyme_display_name: nucleoside-triphosphate phosphatase

organism: Deinococcus radiodurans

substrate_name: IDP

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

proof_lines: substrate concentration between 0.01 and 4.0 mM, 37°C

enzyme: nucleoside-triphosphate phosphatase

substrate: IDP


substrate_name: ITP

substrate: ITP


substrate_name: dITP

substrate: dITP


substrate_name: ATP

assay_conditions_summary: 310.15 K; cofactor ATP

substrate: ATP


substrate_name: ADP

assay_conditions_summary: 310.15 K; cofactor ADP

substrate: ADP


substrate_name: dCTP

substrate: dCTP


substrate_name: dATP

substrate: dATP


substrate_name: GTP

substrate: GTP


substrate_name: GDP

substrate: GDP


substrate_name: dGTP

substrate: dGTP


substrate_name: dGDP

substrate: dGDP


substrate_name: dADP

substrate: dADP


enzyme_display_name: exopolyphosphatase

organism: Chlorobaculum tepidum

enzyme: exopolyphosphatase


substrate_name: guanosine 5'-tetraphosphate

substrate: guanosine 5'-tetraphosphate


enzyme_display_name: nucleotide diphosphatase

organism: Sus scrofa

substrate_name: H2O; p-Nitrophenylthymidine phosphate

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

enzyme: nucleotide diphosphatase

substrate: H2O; p-Nitrophenylthymidine phosphate


substrate_name: p-Nitrophenylthymidine phosphate; H2O

substrate: p-Nitrophenylthymidine phosphate; H2O


substrate_name: alpha-D-glucosamine 6-phosphate (in the absence of GlcNAc6P)


organism: Saccharomyces cerevisiae


assay_conditions_summary: pH 7.5; 296.15 K; cofactor ATP

proof_lines:
pH 7.5, 23°C
pH 7.5, 23°C, in presence of poly(A)40


substrate_name: CTP

substrate: CTP


substrate_name: UTP

substrate: UTP


substrate_name: dTTP

substrate: dTTP


column_label: Table 2 row UTP columns Km mM; kcat sec^-1; kcat/Km mM^-1 sec^-1

row_label: UTP

table_label: Table 2. Kinetic parameters for DR_0079


column_label: Table 2 row CTP columns Km mM; kcat sec^-1; kcat/Km mM^-1 sec^-1

row_label: CTP


substrate_name: TTP

column_label: Table 2 row TTP columns Km mM; kcat sec^-1; kcat/Km mM^-1 sec^-1

row_label: TTP

substrate: TTP


substrate_name: TDP

column_label: Table 2 row TDP columns Km mM and kcat sec^-1

row_label: TDP

substrate: TDP


substrate_name: dCDP

column_label: Table 2 row dCDP columns Km mM; kcat sec^-1; kcat/Km mM^-1 sec^-1

row_label: dCDP

substrate: dCDP


substrate_name: UDP

column_label: Table 2 row UDP columns Km mM; kcat sec^-1; kcat/Km mM^-1 sec^-1

row_label: UDP

substrate: UDP


substrate_name: CDP

column_label: Table 2 row CDP columns Km mM; kcat sec^-1; kcat/Km mM^-1 sec^-1

row_label: CDP

substrate: CDP


enzyme_display_name: glucosamine-6-phosphate deaminase

substrate_name: D-glucosamine 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature F174A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 30°C, mutant F174A, in presence of N-acetylglucosamine 6-phosphate

enzyme: glucosamine-6-phosphate deaminase

substrate: D-glucosamine 6-phosphate


organism: Myxococcus xanthus

substrate_name: Tetraphosphate

proof_lines: wild-type, pH 8, 40°C, presence of Mg2+, K+

substrate: Tetraphosphate


substrate_name: Triphosphate

proof_lines: wild-type, pH 9, 30°C, presence of Mg2+, K+

substrate: Triphosphate


mutation_signature: deletion of C-terminal domain / K+ deletion of C-terminal domain

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

proof_lines: deletion of C-terminal domain, pH 8, 35°C, presence of Mg2+, K+


proof_lines: fusion protein of the Ppx2 C-terminal domain to Ppx1, pH 8, 35°C, presence of Mg2+, K+


organism: Lens culinaris

substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


substrate_name: thymidine 5'-monophosphate p-nitrophenyl ester


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Glaesserella parasuis

substrate_name: nicotinamide guanine dinucleotide

substrate: nicotinamide guanine dinucleotide


proof_lines: biphasic hydrolysis, functions in a manner indicative of negative cooperativity


substrate_name: FAD

assay_conditions_summary: cofactor FAD

substrate: FAD


substrate_name: coenzyme A

assay_conditions_summary: cofactor CoA

substrate: coenzyme A


organism: Trypanosoma evansi

substrate_name: UTP

proof_lines: pH 7.5, 25°C, recombinant enzyme, in presence of 10 mM KCl, 0.5 mM CaCl2, 10 mM MgCl2, 10 mM glucose, and 100 mM sucrose

substrate: UTP


substrate_name: ADP

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ADP

substrate: ADP


substrate_name: ITP

substrate: ITP


substrate_name: GTP

substrate: GTP


substrate_name: ATP

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: pH 7.5, 25°C, recombinant enzyme, in absence of cations

proof_lines: pH 7.5, 25°C, recombinant enzyme, in presence of Ca2+

proof_lines: pH 7.5, 25°C, recombinant enzyme, in presence of Na+

substrate: ATP


organism: mammalian orthoreovirus

substrate_name: RNA

proof_lines: wild-type transcriptase cofactor my2, 22°C, 6.5-7.0

substrate: RNA


substrate_name: CTP

substrate: CTP


assay_conditions_summary: 295.15 K; cofactor ATP


organism: Hordeum vulgare

substrate_name: ADP-ribose

assay_conditions_summary: cofactor ADP

substrate: ADP-ribose


substrate_name: ADP-glucose

substrate: ADP-glucose


substrate_name: bis-p-nitrophenyl phosphate

substrate: bis-p-nitrophenyl phosphate


substrate_name: CDP-glucose

substrate: CDP-glucose


substrate_name: UDP-glucose

substrate: UDP-glucose


organism: Opuntia ficus-indica

substrate_name: NADP+

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

substrate: NADP+


substrate_name: NAD+

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NADPH

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: NADH

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

substrate: NADH


organism: Glycine max

assay_conditions_summary: cofactor ATP


substrate_name: UDP

substrate: UDP


proof_lines: 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA

proof_lines: 2 mM Co2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA


proof_lines: H107N mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA


proof_lines: H108N mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA


proof_lines: D106A mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA


proof_lines: R128H mutant, 2 mM Mg2+ as cofactor, 0.1 M Tris-HCl, pH 7.2, 0.05 mM EGTA


substrate_name: guanosine 5'-tetraphosphate

substrate: guanosine 5'-tetraphosphate


substrate_name: adenosine 5'-tetraphosphate

substrate: adenosine 5'-tetraphosphate


organism: Solanum tuberosum


substrate_name: 5',5'-diadenosine diphosphate; 5',5'-diadenosine triphosphate; 7-methyl 5'-guanosine 2'-O-methylguanosine triphosphate; 5',5'-diadenosine tetraphosphate; thymidine 5'-diphospho 5'-thymidine; thymidine 3'-monophosphate p-nitrophenyl ester; bis(p-nitrophenylphosphate); bis; thymidine 5'-alpha-naphthylphosphate; thymidine 3'-diphospho 3'-thymidine; thymidine 3'-alpha-naphthylphosphate


substrate_name: dATP

substrate: dATP


organism: Bothrops jararaca

substrate_name: bis(4-nitrophenyl) phosphate

proof_lines:
in 0.1 M glycine.NaOH, pH 8.9, at 37°C
in 0.1 M glycine-NaOH, pH 8.9, at 37°C

substrate: bis(4-nitrophenyl) phosphate


enzyme_display_name: adenosine-tetraphosphatase

enzyme: adenosine-tetraphosphatase


proof_lines: pH 4.75, 50 mM sodium acetate, 5 mM CoCl2


substrate_name: thymidine 5'-monophosphate p-nitrophenyl ester


substrate_name: p-nitrophenylphosphate

substrate: p-nitrophenylphosphate


organism: Vigna radiata var. radiata

substrate_name: FAD

proof_lines:
value for dimeric form, biphasic
value for monomeric form
value for tetrameric form

substrate: FAD


organism: Rhipicephalus microplus

assay_conditions_summary: pH 7.5; 301.15 K; buffer 50 mM Tris-HCl

proof_lines: mitochondrial fraction from eggs in the segmentation stage, in 50 mM Tris-HCl, 5 mM MgCl2, pH 7.5

proof_lines: nuclear fraction from eggs in the segmentation stage, in 50 mM Tris-HCl, 5 mM MgCl2, pH 7.5

proof_lines: in 50 mM Tris-HCl buffer (pH 7.2), at 28°C


substrate_name: Triphosphate

assay_conditions_summary: pH 7.2; 301.15 K; buffer 50 mM Tris-HCl

substrate: Triphosphate


organism: Homo sapiens

substrate_name: Tetraphosphate

proof_lines: wild-type, presence of Mg2+, pH 7.2, 25°C

substrate: Tetraphosphate


enzyme_display_name: ADP-ribose diphosphatase

organism: Artemia sp.

substrate_name: ADPribose

enzyme: ADP-ribose diphosphatase

substrate: ADPribose


organism: Tethya aurantium

proof_lines:
exopolyphosphatase II
exopolyphosphatase I


organism: Oryctolagus cuniculus


substrate_name: inosine tetraphosphate

substrate: inosine tetraphosphate


enzyme_display_name: nucleoside-triphosphatase

organism: SARS coronavirus

substrate_name: H2O; ATP

enzyme: nucleoside-triphosphatase

substrate: H2O; ATP


organism: Streptomyces coelicolor

substrate_name: ATP

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: wild-type, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication

substrate: ATP


enzyme_display_name: endopolyphosphatase

organism: Trypanosoma brucei

enzyme: endopolyphosphatase


organism: Brassica oleracea

assay_conditions_summary: cofactor NADH


enzyme_display_name: CDP-glycerol diphosphatase

organism: Bacillus subtilis

substrate_name: CDP-glycerol

enzyme: CDP-glycerol diphosphatase

substrate: CDP-glycerol


organism: Thermus thermophilus

substrate_name: ADP-ribose

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

assay_conditions_summary: pH 7.6; cofactor ADP

proof_lines:
mutant enzyme E82Q, in presence of Mg2+
mutant enzyme E82Q, in presence of Zn2+
25°C, pH 7.6, mutant enzyme E82Q

substrate: ADP-ribose


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

proof_lines:
mutant enzyme E86Q, in presence of Mg2+
mutant enzyme E86Q, in presence of Zn2+
25°C, pH 7.6, mutant enzyme E86Q


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

proof_lines: mutant enzyme D126N, in presence of Mg2+


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

proof_lines: mutant enzyme E129Q, in presence of Mg2+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D128N with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D128N, in presence of Mg2+


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

proof_lines: mutant enzyme E127Q, in presence of Mg2+


proof_lines:
mutant enzyme E86Q, in presence of Mg2+
mutant enzyme E86Q, in presence of Zn2+


proof_lines:
wild-type enzyme, in presence of Mg2+
wild-type enzyme, in presence of Zn2+


proof_lines:
mutant enzyme E82Q, in presence of Zn2+
mutant enzyme E82Q, in presence of Mg2+


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


proof_lines:
25°C, pH 7.6, wild-type enzyme
wild-type enzyme, in presence of Zn2+
wild-type enzyme, in presence of Mg2+


substrate_name: ADP-glucose

substrate: ADP-glucose


organism: Synechocystis sp.

assay_conditions_summary: pH 8; 310.15 K; cofactor ADP

proof_lines: 37°C, pH 8.0, ADP-ribose pyrophosphatase Slr1134

proof_lines: 37°C, pH 8.0, ADP-ribose pyrophosphatase Slr0920

proof_lines: 37°C, pH 8.0, ADP-ribose pyrophosphatase Sll1054


enzyme_display_name: UniProt Q9QY93

organism: Mus musculus

substrate_name: CTP

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: Activity is higher with 5-iodo-dCTP, followed by 5-bromo-dCTP, dCTP, 5-methyl-dCTP and 5-chloro-dCTP. Hydrolyzes 2-chloro-dATP and 2-hydroxy-dATP with lower efficiency, and has even lower activity with dATP, dTTP and dUTP (in vitro). Does n

enzyme: UniProt Q9QY93

substrate: CTP


substrate_name: dTTP

substrate: dTTP


substrate_name: dCTP

substrate: dCTP


organism: Lupinus luteus

substrate_name: adenosine 5'-tetraphosphate

substrate: adenosine 5'-tetraphosphate


enzyme_display_name: Probable bifunctional dTTP/UTP pyrophosphatase/methyltransferase protein

proof_lines: kcat is 0.7 sec(-1) with dTTP as substrate. kcat is 0.7 sec(-1) with UTP as substrate. kcat is 0.8 sec(-1) with CTP as substrate. kcat is 0.3 sec(-1) with dCTP as substrate. kcat is 1.5 sec(-1) with m(5)UTP as substrate. kcat is 3.7 sec(-1)


substrate_name: UTP

enzyme: Probable bifunctional dTTP/UTP pyrophosphatase/methyltransferase protein

substrate: UTP


substrate_name: pseudo-UTP

substrate: pseudo-UTP


enzyme_display_name: dTTP/UTP pyrophosphatase

organism: Escherichia coli (strain K12)

proof_lines: kcat is 15.4 sec(-1) with dTTP as substrate. kcat is 15.2 sec(-1) with UTP as substrate. kcat is 4.9 sec(-1) with CTP as substrate. kcat is 18.2 sec(-1) with m(5)UTP as substrate. kcat is 9.2 sec(-1) with m(5)CTP as substrate. kcat is 10.5

enzyme: dTTP/UTP pyrophosphatase


organism: Bacillus subtilis (strain 168)

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

column_label: Table 1 BSU28050 WT dTTP row reports KM = 50.6 +/- 2.1 microM.

raw_value_unit_evidence: Km raw_value=50.6 +/- 2.1 raw_unit=microM

row_label: BSU28050 / WT / dTTP

table_label: Table 1. Kinetic Parameters of the Wild-Type and Mutant Maf Proteins


column_label: Table 1 BSU28050 WT UTP row reports KM = 72.4 +/- 5.2 microM.

raw_value_unit_evidence: Km raw_value=72.4 +/- 5.2 raw_unit=microM

row_label: BSU28050 / WT / UTP


column_label: Table 1 BSU28050 WT CTP row reports KM = 25.0 +/- 0.8 microM.

raw_value_unit_evidence: Km raw_value=25.0 +/- 0.8 raw_unit=microM

row_label: BSU28050 / WT / CTP


column_label: Table 1 BSU28050 WT m5CTP row reports KM = 7.8 +/- 0.2 microM.

raw_value_unit_evidence: Km raw_value=7.8 +/- 0.2 raw_unit=microM

row_label: BSU28050 / WT / m5CTP


column_label: Table 1 BSU28050 WT pseudoUTP row reports KM = 5.7 +/- 0.3 microM.

raw_value_unit_evidence: Km raw_value=5.7 +/- 0.3 raw_unit=microM

row_label: BSU28050 / WT / pseudoUTP


enzyme_display_name: UniProt Q9H773

substrate_name: dUTP

proof_lines: pH not specified in the publication, temperature not specified in the publication

enzyme: UniProt Q9H773

substrate: dUTP


substrate_name: dATP

substrate: dATP


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


enzyme_display_name: Cyclic GMP-AMP phosphodiesterase SMPDL3A

assay_conditions_summary: pH 5; cofactor ATP

column_label: Table 2, substrate row ATP, Km (uM) column.

row_label: ATP


assay_conditions_summary: pH 5; cofactor ADP

column_label: Table 2, substrate row ADP-ribose, Km (uM) column.

row_label: ADP-ribose

enzyme: Cyclic GMP-AMP phosphodiesterase SMPDL3A


substrate_name: CDP-ethanolamine

column_label: Table 2, substrate row CDP-ethanolamine, Km (uM) column.

row_label: CDP-ethanolamine

substrate: CDP-ethanolamine


substrate_name: CDP-choline

column_label: Table 2, substrate row CDP-choline, Km (uM) column.

row_label: CDP-choline

substrate: CDP-choline


enzyme_display_name: Ectonucleotide pyrophosphatase/phosphodiesterase family member 1

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


enzyme: Ectonucleotide pyrophosphatase/phosphodiesterase family member 1


substrate_name: 3',5'-cyclic AMP

substrate: 3',5'-cyclic AMP


enzyme_display_name: UniProt Q9UKK9

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: UniProt Q9UKK9


enzyme_display_name: ADP-sugar pyrophosphatase

enzyme: ADP-sugar pyrophosphatase


substrate_name: dGDP

substrate: dGDP


substrate_name: dADP

substrate: dADP


organism: Corynebacterium glutamicum

substrate_name: Triphosphate

proof_lines: in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2

substrate: Triphosphate


substrate_name: Tetraphosphate

substrate: Tetraphosphate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 5.7 sec(-1) with dTTP as substrate. kcat is 2.6 sec(-1) with UTP as substrate. kcat is 1.2 sec(-1) with CTP as substrate. kcat is 2.2 sec(-1) with m(5)UTP as substrate. kcat is 5.3 sec(-1) with pseudo-UTP as substrate.


enzyme_display_name: Nudix hydrolase 2

organism: Arabidopsis thaliana

substrate_name: ADP-ribose (at pH 8 and 37 degrees Celsius)

assay_conditions_summary: pH 8; cofactor ADP

proof_lines: kcat is 0.12 sec(-1) with ADP-ribose as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15878881). kcat is 0.01 sec(-1) with NADH as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15878881).

enzyme: Nudix hydrolase 2


substrate_name: NADH (at pH 8 and 37 degrees Celsius)

assay_conditions_summary: pH 8; cofactor NADH

substrate: NADH (at pH 8 and 37 degrees Celsius)


enzyme_display_name: Nudix hydrolase 10

substrate_name: ADP-ribose

assay_conditions_summary: cofactor ADP

proof_lines: kcat is 0.06 sec(-1) with ADP-ribose as substrate.

enzyme: Nudix hydrolase 10

substrate: ADP-ribose


enzyme_display_name: exopolyphosphatase

organism: Trypanosoma brucei brucei

substrate_name: ADP

assay_conditions_summary: pH 7.4; cofactor ADP

enzyme: exopolyphosphatase

substrate: ADP


substrate_name: ATP

assay_conditions_summary: pH 7.4; cofactor ATP

substrate: ATP


enzyme_display_name: UniProt P06802

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

enzyme: UniProt P06802


substrate_name: CTP

substrate: CTP


substrate_name: UTP


substrate_name: GTP

substrate: GTP


organism: Staphylococcus aureus (strain N315)

column_label: Wiley kinetic table wild-type row ATP column Km (uM) reports 380 +/- 73.2

normalized_value_unit_evidence: 0.38 mM ATP Km

row_label: Wild-type ATP / Km

table_label: PMID 33955674 Wiley table - Kinetic parameters of S. aureus Ntdp wild-type and mutant proteins


column_label: Table 2 column ADP row Km (uM) reports 96.3 +/- 34.1

normalized_value_unit_evidence: 0.0963 mM ADP Km

row_label: ADP / Km

table_label: PMID 27422825 PMC5009239 Table 2 - Kinetic parameters of NDP hydrolysis by SA1684 protein


column_label: Wiley kinetic table wild-type row GTP column Km (uM) reports 84.7 +/- 15.9

normalized_value_unit_evidence: 0.0847 mM GTP Km

row_label: Wild-type GTP / Km


substrate_name: GDP

column_label: Table 2 column GDP row Km (uM) reports 102 +/- 31

normalized_value_unit_evidence: 0.102 mM GDP Km

row_label: GDP / Km

substrate: GDP


enzyme_display_name: dCTP diphosphatase

substrate_name: dCTP

mutation_signature: truncated protein

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

assay_conditions_summary: pH 8

proof_lines: truncated protein, residues 22-134, pH 8, 22°C

enzyme: dCTP diphosphatase

substrate: dCTP


enzyme_display_name: Nucleotide triphosphate diphosphatase NUDT15

organism: Homo sapiens

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 2 (febs17202-tbl-0002); enzyme NUDT15; metric row Km (microM), Mean; substrate column GPP.

normalized_value_unit_evidence: Km=0.0187 mM after converting 18.7 microM to mM.

raw_value_unit_evidence: Table 2 NUDT15 Km Mean column GPP = 18.7 microM.

row_label: NUDT15 GPP

table_label: Table 2 (NUDT15 kinetic parameters)


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 2 (febs17202-tbl-0002); enzyme NUDT15; metric row Km (microM), Mean; substrate column IPPP.

normalized_value_unit_evidence: Km=0.0636 mM after converting 63.6 microM to mM.

raw_value_unit_evidence: Table 2 NUDT15 Km Mean column IPPP = 63.6 microM.

row_label: NUDT15 IPPP

enzyme: Nucleotide triphosphate diphosphatase NUDT15


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 2 (febs17202-tbl-0002); enzyme NUDT15; metric row Km (microM), Mean; substrate column DMAPP.

normalized_value_unit_evidence: Km=0.1593 mM after converting 159.3 microM to mM.

raw_value_unit_evidence: Table 2 NUDT15 Km Mean column DMAPP = 159.3 microM.

row_label: NUDT15 DMAPP


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

column_label: Table 2 (febs17202-tbl-0002); enzyme NUDT15; metric row Km (microM), Mean; substrate column FPP.

normalized_value_unit_evidence: Km=0.0763 mM after converting 76.3 microM to mM.

raw_value_unit_evidence: Table 2 NUDT15 Km Mean column FPP = 76.3 microM.

row_label: NUDT15 FPP


enzyme_display_name: Nucleoside triphosphatase NudI

substrate_name: dUTP

proof_lines: kcat is 21 sec(-1) with dUTP as substrate, and 15 sec(-1) with dTTP as substrate.

enzyme: Nucleoside triphosphatase NudI

substrate: dUTP


substrate_name: dTTP

substrate: dTTP


enzyme_display_name: UniProt Q57609

organism: Methanocaldococcus jannaschii

proof_lines: pH 8.0, 70°C, GTP cyclohydrolase activity

proof_lines: pH 8.0, 70°C, diphosphate phosphohydrolase activity

enzyme: UniProt Q57609


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: CDP

proof_lines: kcat is 24.9 min(-1) with ADP as substrate. kcat is 21.4 min(-1) with GDP as substrate. kcat is 45.8 min(-1) with CDP as substrate. kcat is 83.3 min(-1) with UDP as substrate. kcat is 40.8 min(-1) with TDP as substrate.

substrate: CDP


substrate_name: UDP

substrate: UDP


enzyme_display_name: glucosamine-6-phosphate deaminase

organism: Escherichia coli

substrate_name: alpha-D-glucosamine 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C228S/C239S/D165C/S206W to reconstruct the assayed variant sequence.

proof_lines: mutant C118Ser/C228S/C239S/D165C/S206W, at pH 7.8 and 30°C

enzyme: glucosamine-6-phosphate deaminase

substrate: alpha-D-glucosamine 6-phosphate


enzyme_display_name: Exopolyphosphatase 1

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

assay_conditions_summary: cofactor ATP

proof_lines: kcat is 10.2 sec(-1) with polyP(14) as substrate. kcat is 7.3 sec(-1) with polyP(60) as substrate. kcat is 6.7 sec(-1) with polyP(130) as substrate. kcat is 1.9 sec(-1) with ATP as substrate.

enzyme: Exopolyphosphatase 1


enzyme_display_name: Exopolyphosphatase 2

proof_lines: kcat is 4.4 sec(-1) with ATP as substrate.

enzyme: Exopolyphosphatase 2


organism: Amycolatopsis methanolica

proof_lines: pH 8.5, 60°C, recombinant His-tagged enzyme


organism: Staphylococcus aureus


substrate_name: D-Cystine

smiles: C(C(C(=O)O)N)SSCC(C(=O)O)N

proof_lines: pH and temperature not specified in the publication

substrate: D-Cystine


enzyme_display_name: Glucosamine-6-phosphate deaminase

organism: Thermococcus kodakarensis

smiles: N

column_label: Official PMC full text Table 1 row Ammonia (at 8 mM Fru6P), amination direction, reports kcat, Km, and kcat/Km.

normalized_value_unit_evidence: Km=17.0 mM; kcat=39.6 s^-1; kcat/Km=2.3294117647058825 s^-1 mM^-1 from displayed kcat/Km ratio

row_label: Amination; Ammonia (at 8 mM Fru6P)

table_label: PMC HTML Table 1: Kinetic properties of GlmD_Tk

source_databases_merged: brenda uniprot

enzyme: Glucosamine-6-phosphate deaminase


organism: Methylobacterium radiotolerans


substrate_name: dGTP (at pH 7.5)

proof_lines: Has a 10-fold higher catalytic efficiency toward dGTP compared to 8-oxo-dGTP. kcat is 0.58 sec(-1) with dGTP as substrate (at pH 8.0 and 22 degrees Celsius) (PubMed:38944687). kcat is 0.72 sec(-1) with (2E)-geranyl diphosphate as substrate

substrate: dGTP (at pH 7.5)


substrate_name: 8-oxo-dGTP (at pH 7.5)

substrate: 8-oxo-dGTP (at pH 7.5)


organism: Cyberlindnera saturnus


organism: Leishmania major

substrate_name: (Polyphosphate)n

smiles: N#N

substrate: (Polyphosphate)n


enzyme_display_name: Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

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

column_label: PMID 29717535 Figure 2G, Michaelis-Menten parameters of the purified enzyme; Wild-type block; ATP row; Km (uM) column; 61.5 +/- 6.4.

raw_value_unit_evidence: Figure 2G Wild-type ATP row, Km column: 61.5 +/- 6.4 uM.

row_label: Wild-type / ATP

table_label: Figure 2G. Michaelis-Menten parameters of the purified enzyme

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


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

column_label: PMID 29717535 Figure 2G, Michaelis-Menten parameters of the purified enzyme; Wild-type block; UTP row; Km (uM) column; 120.3 +/- 10.5.

raw_value_unit_evidence: Figure 2G Wild-type UTP row, Km column: 120.3 +/- 10.5 uM.

row_label: Wild-type / UTP

enzyme: Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

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


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

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

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


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

column_label: PMID 29717535 Figure 2G, Michaelis-Menten parameters of the purified enzyme; Wild-type block; GTP row; Km (uM) column; 123.7 +/- 6.6.

raw_value_unit_evidence: Figure 2G Wild-type GTP row, Km column: 123.7 +/- 6.6 uM.

row_label: Wild-type / GTP

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


substrate_name: ADP-ribose

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7
Raw SKiD Env: Temp=37°C, pH=8

substrate: ADP-ribose


substrate_name: 8-oxo-dGTP (at pH 10.0)

assay_conditions_summary: pH 10

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.

substrate: 8-oxo-dGTP (at pH 10.0)


enzyme_display_name: Bifunctional D-cysteine desulfhydrase/1-aminocyclopropane-1-carboxylate deaminase, mitochondrial

substrate_name: D-cysteine

proof_lines: kcat is 6 sec(-1) for D-cysteine as substrate.

substrate: D-cysteine


organism: Trypanosoma brucei

substrate_name: pentasodium triphosphate

proof_lines: in 50 mM HEPES, pH 7.8, 0.05 mM EGTA,1 mM MgCl2, at 30°C

substrate: pentasodium triphosphate


enzyme_display_name: Cyclic GMP-AMP phosphodiesterase SMPDL3A

substrate_name: ADP

proof_lines: kcat is 2.6 sec(-1) with 2',3'-cGAMP as substrate (PubMed:37890481). kcat is 3.77 sec(-1) with ATP as substrate (PubMed:37890481).

substrate: ADP


enzyme_display_name: Genome polyprotein

organism: Poliovirus type 1 (strain Mahoney)

substrate_name: ATP

enzyme: Genome polyprotein

substrate: ATP


enzyme: Cyclic GMP-AMP phosphodiesterase SMPDL3A


enzyme_display_name: UniProt Q9H773

proof_lines: in 50 mM Tris, pH 8.0, 100 mM KCl, 5 mM MgCl2, 100 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 37°C

proof_lines: pH not specified in the publication, temperature not specified in the publication

enzyme: UniProt Q9H773


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

assay_conditions_summary: pH 7.5; cofactor ATP


organism: Methylobacterium nodulans


enzyme_display_name: UniProt D3WZ85

organism: Bradyrhizobium sp. JS329

proof_lines: pH and temperature not specified in the publication, enzyme in presence of Co2+

proof_lines: pH and temperature not specified in the publication, enzyme in presence of Zn2+

proof_lines: pH and temperature not specified in the publication, enzyme in presence of Mn2+

enzyme: UniProt D3WZ85


assay_conditions_summary: pH 9; cofactor ATP


enzyme_display_name: ADP-ribose pyrophosphatase

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: Riboflavin biosynthesis protein VVA0006

organism: Vibrio vulnificus (strain YJ016)

proof_lines: kcat is 137 sec(-1) with 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine as substrate. kcat is 0.07 sec(-1) with 5-amino-6-(5-phospho-D-ribosylamino)uracil as substrate.

enzyme: Riboflavin biosynthesis protein VVA0006


enzyme_display_name: GTP cyclohydrolase II

substrate_name: H2O; GTP

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

enzyme: GTP cyclohydrolase II

substrate: H2O; GTP


organism: Methanopyrus kandleri

substrate_name: formyl-tetrahydromethanopterin

substrate: formyl-tetrahydromethanopterin


organism: Methanothermus fervidus


enzyme_display_name: S-adenosylhomocysteine deaminase

organism: Thermotoga maritima

substrate_name: S-Adenosyl-L-homocysteine; H2O

enzyme: S-adenosylhomocysteine deaminase

substrate: S-Adenosyl-L-homocysteine; H2O


enzyme_display_name: dCTP deaminase (dUMP-forming)

organism: Methanocaldococcus jannaschii

substrate_name: H2O; dCTP

enzyme: dCTP deaminase (dUMP-forming)

substrate: H2O; dCTP


enzyme_display_name: Diphosphoinositol polyphosphate phosphohydrolase 1

organism: Homo sapiens


organism: Rattus norvegicus

enzyme: Diphosphoinositol polyphosphate phosphohydrolase 1


enzyme_display_name: Diphosphoinositol polyphosphate phosphohydrolase DDP1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


enzyme_display_name: Endopolyphosphatase

enzyme: Endopolyphosphatase


enzyme_display_name: exopolyphosphatase

organism: Escherichia coli

substrate_name: H2O; Polyphosphate

enzyme: exopolyphosphatase

substrate: H2O; Polyphosphate


enzyme_display_name: S-methyl-5'-thioadenosine deaminase

substrate_name: H2O; 5'-Deoxy-5'-(methylthio)adenosine

enzyme: S-methyl-5'-thioadenosine deaminase

substrate: H2O; 5'-Deoxy-5'-(methylthio)adenosine


enzyme_display_name: tRNA-specific adenosine-34 deaminase catalytic subunit TAD2

substrate_name: tRNA(Ser)(anticodon AGA)

substrate: tRNA(Ser)(anticodon AGA)


enzyme_display_name: tRNA(Ala)(adenine(37)) deaminase

organism: Saccharomyces cerevisiae

substrate_name: adenine37 in tRNAAla

enzyme: tRNA(Ala)(adenine(37)) deaminase

substrate: adenine37 in tRNAAla


enzyme_display_name: glucosamine-6-phosphate deaminase

organism: Bacillus subtilis

substrate_name: D-Glucosamine 6-phosphate; H2O

enzyme: glucosamine-6-phosphate deaminase

substrate: D-Glucosamine 6-phosphate; H2O


organism: Pseudomonas putida

substrate_name: 1-Aminocyclopropane-1-carboxylate; H2O

substrate: 1-Aminocyclopropane-1-carboxylate; H2O


enzyme_display_name: nucleoside-triphosphate diphosphatase

substrate_name: ITP; H2O

enzyme: nucleoside-triphosphate diphosphatase

substrate: ITP; H2O


enzyme_display_name: nucleotide diphosphatase

substrate_name: H2O; 8-oxo-dGTP

column_label: Figure 1c row NUDT15, substrate 8-oxo-dGTP, column kcat.

row_label: NUDT15 / 8-oxo-dGTP

table_label: Figure 1c kinetic parameters

enzyme: nucleotide diphosphatase

substrate: H2O; 8-oxo-dGTP


substrate_name: dGTP; H2O

column_label: Figure 1c row NUDT15, substrate dGTP, column Km.

raw_value_unit_evidence: Km 42 uM

row_label: NUDT15 / dGTP

substrate: dGTP; H2O


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

row_label: MTH1 / 8-oxo-dGTP


organism: Hordeum vulgare

substrate_name: H2O; ADP alpha-D-glucoside

substrate: H2O; ADP alpha-D-glucoside


substrate_name: XTP; H2O

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 live export row stores no kcat_over_km field for this identity, so the printed cell is carried in the typed kcat_over_km_provenance only.

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; H2O


enzyme_display_name: UniProt Q9QY93

organism: Mus musculus

proof_lines:
pH 8.0, 30°C
Raw SKiD Env: Temp=30°C, pH=8

enzyme: UniProt Q9QY93


enzyme_display_name: ADP-ribose diphosphatase

organism: Arabidopsis thaliana

substrate_name: ADPribose; H2O

enzyme: ADP-ribose diphosphatase

substrate: ADPribose; H2O


organism: Bacillus methanolicus


enzyme_display_name: Genome polyprotein

organism: Kokobera virus

substrate_name: ATPase of serine protease NS3

enzyme: Genome polyprotein

substrate: ATPase of serine protease NS3


enzyme_display_name: Cyclic GMP-AMP phosphodiesterase SMPDL3A

substrate_name: ATP at pH 5

substrate: ATP at pH 5


enzyme_display_name: Polyprotein P1234

organism: Semliki forest virus

substrate_name: nsP2 RNA triphosphatase activity (at pH 8.0)

enzyme: Polyprotein P1234


organism: Venezuelan equine encephalitis virus (strain 3880)

substrate_name: a 12 residues substrate for nsp2 protease activity


organism: Venezuelan equine encephalitis virus (strain Trinidad donkey)

substrate: a 12 residues substrate for nsp2 protease activity


enzyme_display_name: CDP-glycerol diphosphatase

substrate_name: CDPglycerol; H2O

enzyme: CDP-glycerol diphosphatase

substrate: CDPglycerol; H2O


substrate_name: H2O; ADPribose

substrate: H2O; ADPribose


organism: Classical swine fever virus (strain Alfort/Tuebingen)

substrate_name: Sub-UpU

substrate: Sub-UpU


organism: Dengue virus type 2 (strain Puerto Rico/PR159-S1/1969)

substrate_name: N-acetyl-Gly-Arg-Arg-AMC

substrate: N-acetyl-Gly-Arg-Arg-AMC


enzyme_display_name: nucleoside-triphosphatase

organism: Homo sapiens

substrate_name: H2O; ATP

enzyme: nucleoside-triphosphatase

substrate: H2O; ATP


enzyme_display_name: single-stranded DNA cytosine deaminase

substrate_name: CCCA

proof_lines: APOBEC3A loop 1 lengthening, pH 7.5, 37°C

enzyme: single-stranded DNA cytosine deaminase

substrate: CCCA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H29S with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H29N with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


enzyme_display_name: 2-aminomuconate deaminase

organism: Ectopseudomonas oleovorans

substrate_name: Unknown

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

enzyme: 2-aminomuconate deaminase

substrate: Unknown


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


proof_lines: wild-type, modified with bimane at C206, pH 7.5, 30°C

proof_lines: wild-type, modified with bimane at C164, pH 7.5, 30°C


enzyme_display_name: Riboflavin biosynthesis protein VVA0006

organism: Vibrio vulnificus (strain YJ016)

enzyme: Riboflavin biosynthesis protein VVA0006


enzyme_display_name: Riboflavin biosynthesis protein PYRD, chloroplastic


enzyme_display_name: dCTP deaminase, dUMP-forming

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 0.18 sec(-1) with dCTP as substrate. kcat is 0.33 sec(-1) with dUTP as substrate.

enzyme: dCTP deaminase, dUMP-forming


enzyme_display_name: tRNA-specific adenosine deaminase

organism: Escherichia coli (strain K12)

enzyme: tRNA-specific adenosine deaminase


enzyme_display_name: DNA dC->dU-editing enzyme APOBEC-3G

substrate_name: 2'-deoxycytidine in single-stranded DNA

proof_lines: kcat is 0.11 min(-1) with 2'-deoxycytidine in single-stranded DNA as substrate.

enzyme: DNA dC->dU-editing enzyme APOBEC-3G

substrate: 2'-deoxycytidine in single-stranded DNA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H29R with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


enzyme_display_name: Exopolyphosphatase 2

proof_lines: kcat is 4.4 sec(-1) with ATP as substrate.

enzyme: Exopolyphosphatase 2


enzyme_display_name: Exopolyphosphatase 1

proof_lines: kcat is 10.2 sec(-1) with polyP(14) as substrate. kcat is 7.3 sec(-1) with polyP(60) as substrate. kcat is 6.7 sec(-1) with polyP(130) as substrate. kcat is 1.9 sec(-1) with ATP as substrate.

enzyme: Exopolyphosphatase 1


enzyme_display_name: Exopolyphosphatase

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

proof_lines: kcat is 57.02 sec(-1) for hydrolase activity with polyP(75) as substrate. kcat is 53.03 sec(-1) for hydrolase activity with polyP(65) as substrate. kcat is 41.23 sec(-1) for hydrolase activity with polyP(45) as substrate. kcat is 40.20 sec(

enzyme: Exopolyphosphatase


enzyme_display_name: exopolyphosphatase

organism: Saccharomyces cerevisiae

substrate_name: Polyphosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N35H with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

enzyme: exopolyphosphatase

substrate: Polyphosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D127N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H148N to reconstruct the assayed variant sequence.


enzyme_display_name: glucosamine-6-phosphate deaminase

organism: Escherichia coli

substrate_name: D-Glucosamine 6-phosphate; H2O

proof_lines: pH 7.8, 25°C, substrate?: D-glucosamine-6-phosphate

source_databases_merged: sabio_rk brenda uniprot

enzyme: glucosamine-6-phosphate deaminase

substrate: D-Glucosamine 6-phosphate; H2O


organism: Giardia duodenalis


enzyme_display_name: Glucosamine-6-phosphate deaminase

organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

proof_lines: kcat is 97.5 sec(-1) with GlcN6P as substrate. kcat is 44.2 sec(-1) with Fru6P as substrate. kcat is 39.6 sec(-1) with ammonia as substrate.

enzyme: Glucosamine-6-phosphate deaminase


enzyme_display_name: 5-nitroanthranilic acid aminohydrolase

organism: Bradyrhizobium sp

enzyme: 5-nitroanthranilic acid aminohydrolase


enzyme_display_name: Zinc-dependent endopolyphosphatase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

enzyme: Zinc-dependent endopolyphosphatase


organism: Corynebacterium glutamicum


organism: Bacteriophage phi-6


enzyme_display_name: Genome polyprotein

organism: Dengue virus type 2 (strain Thailand/NGS-C/1944)

substrate_name: triphosphorylated RNA

proof_lines: Vmax with 0.65 nmol/s/ug enzyme for RTPase activity with triphosphorylated RNA as substrate.

enzyme: Genome polyprotein

substrate: triphosphorylated RNA


organism: Staphylococcus aureus (strain N315)

substrate_name: TDP

proof_lines: kcat is 34 min(-1) with ATP as substrate. kcat is 138 min(-1) with ADP as substrate. kcat is 104 min(-1) with GTP as substrate. kcat is 42 min(-1) with GDP as substrate.

proof_lines: kcat is 24.9 min(-1) with ADP as substrate. kcat is 21.4 min(-1) with GDP as substrate. kcat is 45.8 min(-1) with CDP as substrate. kcat is 83.3 min(-1) with UDP as substrate. kcat is 40.8 min(-1) with TDP as substrate.

substrate: TDP


enzyme_display_name: dTTP/UTP pyrophosphatase

organism: Bacillus subtilis (strain 168)

proof_lines: kcat is 11.6 sec(-1) with dTTP as substrate. kcat is 4.9 sec(-1) with UTP as substrate. kcat is 7.1 sec(-1) with CTP as substrate. kcat is 2.4 sec(-1) with m(5)UTP as substrate. kcat is 8.5 sec(-1) with m(5)CTP as substrate. kcat is 7.2 sec

enzyme: dTTP/UTP pyrophosphatase


enzyme_display_name: nucleotide diphosphatase

organism: Dictyostelium discoideum

proof_lines: competitive inhibition of formycin 5'-triphosphate hydrolysis

enzyme: nucleotide diphosphatase


enzyme_display_name: Nucleoside triphosphatase NudI

proof_lines: kcat is 21 sec(-1) with dUTP as substrate, and 15 sec(-1) with dTTP as substrate.

enzyme: Nucleoside triphosphatase NudI


proof_lines: kcat is 15.4 sec(-1) with dTTP as substrate. kcat is 15.2 sec(-1) with UTP as substrate. kcat is 4.9 sec(-1) with CTP as substrate. kcat is 18.2 sec(-1) with m(5)UTP as substrate. kcat is 9.2 sec(-1) with m(5)CTP as substrate. kcat is 10.5


enzyme_display_name: Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

organism: Homo sapiens

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


enzyme_display_name: nucleoside-triphosphate diphosphatase

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

enzyme: nucleoside-triphosphate diphosphatase


enzyme_display_name: Probable bifunctional dTTP/UTP pyrophosphatase/methyltransferase protein

proof_lines: kcat is 0.7 sec(-1) with dTTP as substrate. kcat is 0.7 sec(-1) with UTP as substrate. kcat is 0.8 sec(-1) with CTP as substrate. kcat is 0.3 sec(-1) with dCTP as substrate. kcat is 1.5 sec(-1) with m(5)UTP as substrate. kcat is 3.7 sec(-1)


proof_lines: kcat is 5.7 sec(-1) with dTTP as substrate. kcat is 2.6 sec(-1) with UTP as substrate. kcat is 1.2 sec(-1) with CTP as substrate. kcat is 2.2 sec(-1) with m(5)UTP as substrate. kcat is 5.3 sec(-1) with pseudo-UTP as substrate.


enzyme_display_name: Nucleoside triphosphate pyrophosphohydrolase/pyrophosphatase MazG

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H149N to reconstruct the assayed variant sequence.


enzyme_display_name: Polyphosphatase

enzyme: Polyphosphatase


organism: Trypanosoma brucei brucei


enzyme_display_name: UniProt Q9H773

proof_lines: in 50 mM Tris, pH 8.0, 100 mM KCl, 5 mM MgCl2, 100 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 37°C

enzyme: UniProt Q9H773


enzyme_display_name: ADP-ribose diphosphatase

organism: Arabidopsis thaliana

proof_lines: kcat is 0.12 sec(-1) with ADP-ribose as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15878881). kcat is 0.01 sec(-1) with NADH as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15878881).

enzyme: ADP-ribose diphosphatase


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

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation L196A, substrate 2',3'-cAMP, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).


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

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation C253A, substrate 2',3'-cAMP, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).


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

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation F210A, substrate 2',3'-cAMP, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).


sequence_variant_note: Resolved canonical sequence from ncbi_genpept_accession:AHG56452.1 and applied mutation signature F37A to reconstruct the assayed variant sequence.

column_label: Table 1 row F37A / 2',3'-cAMP; columns kcat (s^-1), Km (microM), and kcat/Km (M^-1 s^-1). Mismatch fields: kcat csv 4.5 s^-1 vs paper 36 s^-1; kcat/Km csv 0.882352941176471 s^-1*mM^-1 vs paper 7 s^-1*mM^-1.

table_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants.


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

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation F37A+L196A, substrate 2',3'-cAMP, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: current kcat 19 s^-1; paper kcat 19 +/- 2 s^-1; current Km 4.8 mM; paper Km 4800 +/- 900 uM = 4.8 mM; current kcat/Km 3.95833 s^-1 mM^-1; paper kcat/Km 4000 +/- 1000 M^-1 s^-1 = 4 s^-1 mM^-1


sequence_variant_note: Resolved canonical sequence from ncbi_genpept_accession:AHG56452.1 and applied mutation signature F37A/L196F to reconstruct the assayed variant sequence.

column_label: Table 1 row F37A+L196F / 2',3'-cAMP; columns kcat (s^-1), Km (microM), and kcat/Km (M^-1 s^-1). Mismatch fields: kcat csv 5 s^-1 vs paper 28 s^-1; kcat/Km csv 0.704225352112676 s^-1*mM^-1 vs paper 3.9 s^-1*mM^-1.


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

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation F37A+L196F+C253A, substrate 2',3'-cAMP, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: current kcat 20 s^-1; paper kcat 20 +/- 3 s^-1; current Km 5.2 mM; paper Km 5200 +/- 1000 uM = 5.2 mM; current kcat/Km 3.84615 s^-1 mM^-1; paper kcat/Km 4000 +/- 800 M^-1 s^-1 = 4 s^-1 mM^-1


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

table_label: Table 1

row_label: F37Y / 2´,3´-cAMP

column_label: Table 1; mutation row F37Y; substrate row 2´,3´-cAMP; columns kcat, Km, kcat/Km

raw_value_unit_evidence: paper Table 1 cells: kcat=70 ± 18 s^-1; km=2500 ± 180 uM; kcat_over_km=28000 ± 5000 M^-1 s^-1

normalized_value_unit_evidence: normalized: kcat=70 s^-1; km=2.5 mM; kcat_over_km=28 s^-1 mM^-1


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

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation H111A, substrate 2',3'-cAMP, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).


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

column_label: Table 1. Kinetic parameters of human ADPRibase-Mn and mutants, row mutation H111N, substrate 2',3'-cAMP, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).


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

proof_lines: kcat is 0.06 sec(-1) with ADP-ribose as substrate.


substrate_name: ADPribose; H2O

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_display_name: ADP-ribose pyrophosphatase

enzyme: ADP-ribose pyrophosphatase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

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

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

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


organism: Thermus thermophilus

substrate_name: CDP-ribose

substrate: CDP-ribose


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

substrate: ADPribose; H2O