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


enzyme_display_name: glucosamine-6-phosphate deaminase

organism: Escherichia coli

substrate_name: D-fructose 6-phosphate

source_db: brenda

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

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

data_origin: experimental

enzyme: glucosamine-6-phosphate deaminase

substrate: D-fructose 6-phosphate

status: unverified

source: brenda


kcat_display: Not reported

kcat_over_km_display: Not reported

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)

substrate_name: adenosine (at pH 8)

source_db: uniprot

protein_accession_database: UniProt

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

assay_conditions_summary: pH 8

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

substrate: adenosine (at pH 8)

source: uniprot


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

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


substrate_name: D-glucosamine 6-phosphate

km_display: Not reported

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

mutation_type: substitution

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

substrate: D-glucosamine 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

organism: Arabidopsis thaliana

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

organism: Helicobacter pylori

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

enzyme: Aminopyrimidine aminohydrolase


organism: Bacillus subtilis (strain 168)

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

organism: Bacillus subtilis

substrate_name: dGTP

enzyme: apyrase

substrate: dGTP


substrate_name: dATP

substrate: dATP


enzyme_display_name: UniProt O35000

substrate_name: alpha-D-glucosamine 6-phosphate

source_db: skid

verification_status: corrected

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

sequence_source: multiple

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

source_databases_merged: skid uniprot

enzyme: UniProt O35000

substrate: alpha-D-glucosamine 6-phosphate

status: corrected

source: skid


substrate_name: glucosamine 6-phosphate

verification_status: verified

normalized_value_unit_evidence: Km 0.13 mM

substrate: glucosamine 6-phosphate

status: verified


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

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q9BY32

substrate: dITP


substrate_name: xanthosine 5'-triphosphate

substrate: xanthosine 5'-triphosphate


substrate_name: ITP

substrate: ITP


enzyme_display_name: UniProt P97675

organism: Rattus norvegicus

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

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: 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

kcat_over_km_origin: calculated

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

source_databases_merged: brenda skid

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

source_db: oed

enzyme: exopolyphosphatase

source: oed


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)

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

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


assay_conditions_summary: pH 9

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

organism: Escherichia coli

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.

mutation_type: deletion

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


organism: Homo sapiens

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


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+


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

source_databases_merged: brenda skid uniprot

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

organism: Homo sapiens

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)

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

table_label: Table 2


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.

mutation_type: truncation

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

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)

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

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

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


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

organism: Homo sapiens

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

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

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: 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

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

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

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


substrate_name: ADP-ribose

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

row_label: F37Y / ADP-ribose

substrate: ADP-ribose


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

row_label: H111A / ADP-ribose


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

row_label: H111N / ADP-ribose


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

row_label: L196A / ADP-ribose


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

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

row_label: N110A / ADP-ribose


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

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

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

row_label: Q27H / ADP-ribose


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

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

row_label: R43A / ADP-ribose


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

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

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

row_label: Wild type / ADP-ribose


substrate_name: cADP-ribose

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

row_label: C253A / cADP-ribose

substrate: cADP-ribose


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

row_label: F37A+L196F+C253A / cADP-ribose


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


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


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


row_label: Wild type / 2´,3´-cAMP

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

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

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


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

row_label: C253A / ADP-ribose


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

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

row_label: F210A / ADP-ribose


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

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

row_label: F37A / ADP-ribose


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

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

row_label: F37A+L196A / ADP-ribose


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

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

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

row_label: F37A+L196F / ADP-ribose


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

row_label: F37A+L196F+C253A / ADP-ribose


substrate_name: CDP-choline

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 CDP-choline, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

row_label: L196A / CDP-choline

substrate: CDP-choline


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

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

row_label: N110A / CDP-choline


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

row_label: Q27H / CDP-choline


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

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

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

row_label: Wild type / CDP-choline


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

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

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

row_label: Wild type / cADPR


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 CDP-choline, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

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

row_label: C253A / CDP-choline


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 CDP-choline, columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

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

row_label: F210A / CDP-choline


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

row_label: F37A / CDP-choline


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

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

row_label: F37A+L196A / CDP-choline


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

row_label: F37A+L196F / CDP-choline


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

row_label: F37A+L196F+C253A / CDP-choline


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

row_label: F37Y / CDP-choline


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

row_label: H111A / CDP-choline


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

row_label: H111N / CDP-choline


organism: Oryza sativa

substrate_name: UDP-glucose

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

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

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

row_label: UDP-glucose / NPP1

substrate: UDP-glucose


substrate_name: CDP-glucose

assay_conditions_summary: pH 6

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

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

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

row_label: CDP-glucose / NPP1

substrate: CDP-glucose


substrate_name: ADP-glucose

assay_conditions_summary: pH 6; cofactor ADP

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

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

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

row_label: ADP-glucose / NPP1

substrate: ADP-glucose


assay_conditions_summary: pH 4.5; cofactor ADP

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

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

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

row_label: ADP-glucose / NPP6


substrate_name: GDP-mannose

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

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

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

row_label: GDP-mannose / NPP1

substrate: GDP-mannose


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

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

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

row_label: ADP-ribose / NPP1


substrate_name: adenosine 5'-phosphosulfate

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

row_label: APS / NPP6

substrate: adenosine 5'-phosphosulfate


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

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

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

row_label: APS / NPP1


substrate_name: ADP

assay_conditions_summary: pH 4.5; 310.15 K; cofactor ADP

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

row_label: ADP / NPP6

substrate: ADP


assay_conditions_summary: pH 6; 310.15 K; cofactor ADP

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

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

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

row_label: ADP / NPP1


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


substrate_name: ATP

assay_conditions_summary: pH 4.5; 310.15 K; cofactor ATP

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

row_label: ATP / NPP1

substrate: ATP


assay_conditions_summary: pH 6; 310.15 K; cofactor ATP

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

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

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


substrate_name: GDP

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

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

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

row_label: GDP / NPP2

substrate: GDP


substrate_name: diphosphate

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

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

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

row_label: PPi / NPP6

substrate: diphosphate


assay_conditions_summary: pH 6; cofactor ATP


assay_conditions_summary: pH 4.5; cofactor ATP


substrate_name: TDP-glucose

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

row_label: TDP-glucose / NPP1

substrate: TDP-glucose


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

row_label: TDP-glucose / NPP6


substrate_name: IDP

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

row_label: IDP / NPP2

substrate: IDP


substrate_name: CDP

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

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

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

row_label: CDP / NPP2

substrate: CDP


substrate_name: UDP

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

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

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

row_label: UDP / NPP6

substrate: UDP


organism: Mus musculus

substrate_name: H2O; 8-oxo-dGTP

substrate: H2O; 8-oxo-dGTP


substrate_name: ATP; H2O

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

substrate: ATP; H2O


substrate_name: TDP

substrate: TDP


organism: Rattus norvegicus

substrate_name: p-Nitrophenylthymidine phosphate; H2O

substrate: p-Nitrophenylthymidine phosphate; H2O


assay_conditions_summary: cofactor NADH


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

row_label: Bis-p-NPP / NPP6


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

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

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

row_label: NPP2 | CDP


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

row_label: PPi / NPP2


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

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

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

row_label: NPP2 | IDP


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

row_label: TDP / NPP2


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

row_label: UDP / NPP2


substrate_name: UDP-glucose

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

row_label: UDP-glucose / NPP1

substrate: UDP-glucose


substrate_name: ADPribose

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

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

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

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

substrate: ADPribose


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

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

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

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


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

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

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

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


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

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

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

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


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

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

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

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


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

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

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

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


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

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

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

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


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

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

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

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


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

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

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

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


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

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

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

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


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

assay_conditions_summary: pH 7.63; 298.15 K; cofactor ADP


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

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

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

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