organism: Cryptosporidium parvum

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

proof_lines: pH 7.5, temperature not specified in the publication


enzyme_display_name: hexokinase

substrate_name: D-fructose

source_db: brenda

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

data_origin: experimental

enzyme: hexokinase

substrate: D-fructose

source: brenda


substrate_name: ATP

assay_conditions_summary: pH 7.5; cofactor ATP

substrate: ATP


organism: Nicotiana tabacum

substrate_name: D-glucose

verification_status: unverified

kcat_display: Not reported

kcat_over_km_display: Not reported

proof_lines: pH 8.4, 30°C, recombinant isozyme hexokinase 2

substrate: D-glucose

status: unverified


organism: Trypanosoma brucei


verification_status: verified

assay_conditions_summary: pH 7.9; cofactor ATP

status: verified


organism: Arabidopsis thaliana

substrate_name: glucose

source_db: uniprot

proof_lines: Measured in yeast lacking glucose and hexose kinase activity.

substrate: glucose

source: uniprot


substrate_name: fructose

substrate: fructose


organism: Saccharomyces cerevisiae

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

proof_lines:
S-nitrosoglutathione treated enzyme
Raw SKiD Env: Temp=-----, pH=-----

source_databases_merged: brenda skid


organism: Bos taurus

proof_lines: pH 7.2, 37°C, recombinant catalytic C-terminal domain

proof_lines: pH 7.2, 37°C, recombinant full length enzyme


assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP


organism: Kluyveromyces lactis

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ATP

proof_lines: pH 7.4, 25°C, recombinant enzyme at 1.0 mg/ml

proof_lines: pH 7.4, 25°C, recombinant enzyme at 0.001 mg/ml


organism: Rattus norvegicus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D84A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: cofactor ATP

proof_lines:
HK I and its D84A mutant
HK I+ and its D84A mutant


proof_lines: recombinant wild-type hexokinase I, D84A, D84E and D84K mutants


organism: Mus musculus

proof_lines: pH and temperature not specified in the publication


organism: Homo sapiens

proof_lines: wild-type and nonaggregating interface mutant hexokinase I, pH 7.8


organism: Ascaris suum

substrate_name: Glucose; ATP

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

substrate: Glucose; ATP


organism: Aspergillus niger


organism: Bacteroides fragilis

substrate_name: D-Glucose; ATP

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

substrate: D-Glucose; ATP


organism: Botrytis cinerea

substrate_name: ATP; D-Glucose

substrate: ATP; D-Glucose


organism: Candida albicans


organism: Solanum tuberosum

substrate_name: glucose; mannose

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

substrate: glucose; mannose


organism: Xenopus laevis

assay_conditions_summary: pH 8; 295.15 K; cofactor ATP

proof_lines: enzyme isolated from dehydrated frogs, pH 8.0, 22°C


organism: Schwanniomyces occidentalis


assay_conditions_summary: pH 7.1; 298.15 K; cofactor ATP

proof_lines: wild type enzyme, in 25 mM HEPES (pH 7.1), at 25°C


enzyme_display_name: DNA-directed DNA polymerase

substrate_name: dTTP (in presence of 2 mM of Mn(2+))

proof_lines: kcat is 0.05 sec(-1) for dTTP (in presence of 2 mM of Mn(2+)). kcat is 0.02 sec(-1) for dTTP (in presence of 50 uM of Mn(2+)). kcat is 0.01 sec(-1) for dTTP (in presence of 2 mM of Mg(2+)).

enzyme: DNA-directed DNA polymerase

substrate: dTTP (in presence of 2 mM of Mn(2+))


organism: Plasmodium falciparum


organism: Entamoeba histolytica


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

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP


sequence_source: multiple

sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature A456V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.1; 303.15 K; cofactor ATP

proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant A456V


organism: Trypanosoma cruzi

proof_lines: natural hexokinase from epimastigotes, at pH 7.5

proof_lines: recombinant hexokinase expressed in Escherichia coli XL-1 Blue, at pH 7.5


proof_lines: natural and recombinant hexokinase, expressed in Escherichia coli XL-1 Blue, at pH 7.5


organism: Leishmania mexicana

substrate_name: ATP; Glucose

substrate: ATP; Glucose


organism: Macrobrachium nipponense

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Nicotiana tabacum


organism: Ogataea angusta


organism: Rattus norvegicus


organism: Saccharomyces cerevisiae


organism: Schistosoma mansoni

assay_conditions_summary: pH 8.5; cofactor ATP


organism: Sulfolobus tokodaii

substrate_name: D-Mannose; ATP

assay_conditions_summary: pH 7.5; 323.15 K; cofactor ATP

substrate: D-Mannose; ATP


organism: Oncorhynchus mykiss


organism: Pisum sativum


substrate_name: D-Glucose; ITP

substrate: D-Glucose; ITP


organism: Sus scrofa


organism: Thermoproteus tenax


organism: Toxoplasma gondii


organism: Triticum aestivum

substrate_name: Fructose; ATP

substrate: Fructose; ATP


organism: Trypanosoma brucei


organism: Entamoeba histolytica

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V183T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant HXK1 V183T


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V183T/I270S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant HXK1 V183T/I270S


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S144T/V183T/I270S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant HXK1 S144T/V183T/I270S


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S144T/R265T/Y266F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant HXK1 S144T/R265T/Y266F


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S144T/V183T/I270S/R265T/Y266F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant HXK1 S144T/V183T/I270S/R265T/Y266F


organism: Homo sapiens

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

proof_lines: nonaggregating interface mutant hexokinase I, pH 7.8


organism: Bos taurus

proof_lines: pH 7.2, 37°C, recombinant full length enzyme, versus MgATP2-

proof_lines: pH 7.2, 37°C, recombinant catalytic C-terminal domain, versus MgATP2-


organism: Cryptosporidium parvum

proof_lines: pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V183T/I270S/R265T/Y266F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant HXK1 V183T/I270S/R265T/Y266F


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I270S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant HXK1 I270S


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R265T/Y266F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant HXK1 R265T/Y266F


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S144T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant HXK1 S144T


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A464P/E465G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant isozyme HK1 A464P/E465G


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

mutation_type: insertion

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant isozyme HK1 Gln466 7 AA insertion His467


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Δ16 to reconstruct the assayed variant sequence.

mutation_type: deletion

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) wildtype delta16 (aa 17-916)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D209A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant D209A (aa 17-916)


sequence_variant_note: Mutation signature D657A matches the mutant residue at offset -4 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant D657A (aa 17-916)


proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant N166R


sequence_variant_note: Resolved canonical sequence from selected_batch_sequence_residue_checked_against_mutation_signature and applied mutation signature S151A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant S151A


sequence_variant_note: Resolved canonical sequence from selected_batch_sequence_residue_checked_against_mutation_signature and applied mutation signature S151G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant S151G


sequence_variant_note: Resolved canonical sequence from selected_batch_sequence_residue_checked_against_mutation_signature and applied mutation signature S151C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant S151C


proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant N166R-S151A


organism: Mus musculus

sequence_variant_note: Resolved canonical sequence from uniprot_p17710_direct_reconstruction and applied mutation signature S603A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant S603A


sequence_variant_note: Mutation signature K558R could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant K558R


sequence_variant_note: Mutation signature K558M could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant K558M


sequence_variant_note: Mutation signature E708A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant E708A


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -2, so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant E742A


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

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant C-terminal half


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D84A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

proof_lines:
HK I+ and its D84A mutant
D84A mutant of HK I


sequence_variant_note: Mutation signature D84A matches the mutant residue at offset -2 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant isozyme Type I D84A


sequence_variant_note: Mutation signature D84K matches the mutant residue at offset -7 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant isozyme Type I D84K


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


sequence_variant_note: Mutation signature D84E matches the mutant residue at offset -8 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant isozyme Type I D84E


organism: Schizosaccharomyces pombe

substrate_name: ATP; D-Mannose

substrate: ATP; D-Mannose


substrate_name: ATP; D-Fructose

substrate: ATP; D-Fructose


organism: Solanum chacoense


organism: Solanum tuberosum

proof_lines: Measured in yeast lacking glucose and hexose kinase activity.

source_databases_merged: sabio_rk brenda uniprot


proof_lines: uncomplexed ATP4-, hexokinase III, at 30°C, pH 7.2

proof_lines: uncomplexed, hexokinase III, at 30°C, pH 7.2


proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant HK2C1 (C-terminus of HK1)


organism: Trypanosoma cruzi

proof_lines: natural hexokinase from epimastigotes, at pH 7.5

proof_lines: recombinant hexokinase expressed in Escherichia coli, at pH 7.5


sequence_variant_note: Mutation signature E260A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant E260A


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +13, so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant D209A


sequence_variant_note: Mutation signature S155A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant S155A


organism: Rattus norvegicus

sequence_variant_note: Resolved canonical sequence from reconstructed_variant_sequence and applied mutation signature S603A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant S603A (N-terminal half of type II isozyme)


sequence_variant_note: Resolved canonical sequence from reconstructed_variant_sequence and applied mutation signature D447S/S603A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant D447S/S603A (N-terminal half of type II isozyme)


sequence_variant_note: Mutation signature G174R/S603A matches the mutant residue at offset +0 and the reference residue at offset +23; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: hexokinase(Enzyme) mutant G174R/S603A (N-terminal half of type II isozyme)


organism: Gallus gallus

substrate_name: D-Fructose 6-phosphate; ATP

substrate: D-Fructose 6-phosphate; ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H242A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

proof_lines: Ki above 10 mM, mutant enzyme H242A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: Ki above 10 mM, mutant enzyme H242A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme H242A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant 4 N-terminal and 4 C-terminal subunits


mutation_signature: N-terminal truncation mutant

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

mutation_type: truncation

proof_lines: N-terminal truncation mutant, pH 7.1, 25°C


organism: Lactobacillus acidophilus


organism: Bacteriophage RB69

substrate_name: DNA; dATP

sequence_variant_note: Resolved canonical sequence from uniprot_accession plus direct reconstruction from Q38087 canonical sequence and applied mutation signature D222A/D327A/N564A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant D222A/D327A/N564A

substrate: DNA; dATP


substrate_name: dGDP

source_db: oed

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession plus direct reconstruction from Q38087 canonical sequence and applied mutation signature D222A/D327A/K560A to reconstruct the assayed variant sequence.

substrate: dGDP

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession plus direct reconstruction from Q38087 canonical sequence and applied mutation signature D222A/D327A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant D222A/D327A


sequence_variant_note: Resolved canonical sequence from uniprot_accession plus direct reconstruction from Q38087 canonical sequence and applied mutation signature D222A/D327A/K483A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant D222A/D327A/K483A


substrate_name: dATP; DNA

sequence_variant_note: Resolved canonical sequence from uniprot_accession plus direct reconstruction from Q38087 canonical sequence and applied mutation signature D222A/D327A/R482A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant D222A/D327A/R482A

substrate: dATP; DNA


sequence_source: uniprot_accession plus direct reconstruction from Q38087 canonical sequence

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant D222A/D327A/K560A


organism: Lactococcus lactis subsp. lactis

substrate_name: ATP; D-Fructose 6-phosphate

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

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant Lac- Gal d

substrate: ATP; D-Fructose 6-phosphate


substrate_name: Fructose 6-phosphate; ATP

sequence_variant_note: Resolved canonical sequence from reconstructed_variant_sequence and applied mutation signature Y139F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant Tyr139Phe His6-tagged

substrate: Fructose 6-phosphate; ATP


substrate_name: ATP; Fructose 6-phosphate

sequence_variant_note: Resolved canonical sequence from reconstructed_variant_sequence and applied mutation signature K226G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant Lys226Gly His6-tagged

substrate: ATP; Fructose 6-phosphate


organism: [Bacillus] caldotenax

substrate_name: deoxynucleoside triphosphate

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

proof_lines: equimolar mixture of all nucleotides, pH 7.5, 70°C

substrate: deoxynucleoside triphosphate


organism: Bacillus subtilis

substrate_name: dGTP; DNA

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant drug resistant

substrate: dGTP; DNA


sequence_variant_note: Resolved canonical sequence from reconstructed_variant_sequence and applied mutation signature D222A/D327A/Y567A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant D222A/D327A/Y567A


sequence_variant_note: Resolved canonical sequence from selected_batch_reconstructed_from_uniprot_Q38087 and applied mutation signature D222A/D327A/K486A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant D222A/D327A/K486A


substrate_name: DNA; dGTP

sequence_variant_note: Mutation signature S624C matches the mutant residue at offset -15 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant S624C

substrate: DNA; dGTP


sequence_variant_note: Resolved canonical sequence from selected_batch_reconstructed_from_uniprot_Q38087 and applied mutation signature D621A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant D621A


sequence_variant_note: Resolved canonical sequence from selected_batch_reconstructed_from_uniprot_Q38087 and applied mutation signature Y708A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant Y708A


sequence_variant_note: Resolved canonical sequence from selected_batch_reconstructed_from_uniprot_Q38087 and applied mutation signature E686A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant E686A


substrate_name: dCTP; DNA

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession_Q38087 and applied mutation signature T587A/Y391A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant T587A/Y391A

substrate: dCTP; DNA


organism: Bacteriophage T4

substrate_name: DNA; H2O

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

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant D112N

substrate: DNA; H2O


substrate_name: H2O; DNA

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant D324A

substrate: H2O; DNA


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession_P04415 and applied mutation signature E114A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant E114A


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession_P04415 and applied mutation signature D112A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant D112A


proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant D219A


sequence_variant_note: Resolved canonical sequence from UniProt Q38087 direct FASTA check plus local substitution reconstruction and applied mutation signature Y391F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant Y391F


substrate_name: DNA; dCTP

sequence_variant_note: Resolved canonical sequence from UniProt Q38087 direct FASTA check plus local substitution reconstruction and applied mutation signature T587A/Y391F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant T587A/Y391F

substrate: DNA; dCTP


sequence_variant_note: Resolved canonical sequence from UniProt Q38087 direct FASTA check plus local substitution reconstruction and applied mutation signature Y567F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant Y567F


sequence_variant_note: Resolved canonical sequence from UniProt Q38087 direct FASTA check plus local substitution reconstruction and applied mutation signature Y391A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant Y391A


sequence_variant_note: Resolved canonical sequence from UniProt Q38087 direct FASTA check plus local substitution reconstruction and applied mutation signature T587A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant T587A


sequence_variant_note: Resolved canonical sequence from UniProt Q38087 direct FASTA check plus local substitution reconstruction and applied mutation signature Y567A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant Y567A


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y824A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y824A, in 50 mM Tris-HCl (pH 7.8), 1 mM dithiothreitol, at 25°C


organism: Homo sapiens

sequence_variant_note: Mutation signature Y52E matches the mutant residue at offset +1 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant Y52E


substrate_name: dTTP; DNA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E895A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant E895A

substrate: dTTP; DNA


substrate_name: DNA; dTTP

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y951F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant Y951F

substrate: DNA; dTTP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y955A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant Y955A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y951A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant Y951A


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature D219A/D324A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant D219A/D324A


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature R821A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R821A, in 50 mM Tris-HCl (pH 7.8), 1 mM dithiothreitol, at 25°C


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature R822A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R822A, in 50 mM Tris-HCl (pH 7.8), 1 mM dithiothreitol, at 25°C


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature R822A/Y824A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R822A/Y824A in 50 mM Tris-HCl (pH 7.8), 1 mM dithiothreitol, at 25°C


sequence_variant_note: Mutation signature R823A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme R823A, in 50 mM Tris-HCl (pH 7.8), 1 mM dithiothreitol, at 25°C


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

proof_lines: wild type enzyme, in 50 mM Tris-HCl (pH 7.8), 1 mM dithiothreitol, at 25°C


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: dNTPs

proof_lines: kcat is 22 sec(-1) for polymerase activity (PubMed:27487482). kcat is 10 min(-1) for polymerase activity (PubMed:39490679). kcat is 1.69 min(-1) for polymerase activity on dA template with dTTP (PubMed:35220686, PubMed:32636411). kcat is 1.

substrate: dNTPs


organism: Saccharolobus solfataricus

proof_lines: pH 7.5, 60°C, incorporation opposite the 5-thymine of a cis-syn thymine dimer of the template

proof_lines: pH 7.4, 37°C, steady-state kinetics for single nucleotide primer extension with guanine as template

proof_lines: pH 7.5, 60°C, incorporation opposite the 5-thymine of an nondamaged template


substrate_name: dTTP

verification_status: corrected

assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM Tris-HCl

column_label: TABLE 2 (Steady-state kinetics of dNTP incorporation opposite G by Dpo 1, Dpo2, Dpo3, and Dpo4); Polymerase column = Dpo2; dNTP column = T (dTTP); column 'Km (uM)' = 3700 +/- 1300; column 'kcat (min^-1)' = 0.0000072 +/- 0.0000009; column 'kcat/Km (min^-1 uM^-1)' = 1.9 x 10^-9; column 'fins' = 3.5 x 10^-4.

normalized_value_unit_evidence: Km: printed TABLE 2 cell 3700 uM; 3700 / 1000 = 3.7 mM. kcat: printed TABLE 2 cell 0.0000072 min^-1, under the column head 'kcat' whose unit line reads 'min' with the superscript -1; one min^-1 is 1/60 s^-1, so 0.0000072 / 60 = 0.00000012 s^-1. kcat/Km: printed TABLE 2 cell 1.9 x 10^-9 min^-1 uM^-1, under the column head 'kcat/Km' whose unit line reads 'min' with the superscript -1 followed by 'uM' with the superscript -1; one min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 0.0000000019 x 1000 / 60 = 0.00000003166666666666667 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 2, Polymerase Dpo2, dNTP row T (dTTP): Km = 3700 uM; kcat = 0.0000072 min^-1; printed kcat/Km = 1.9 x 10^-9 min^-1 uM^-1.

row_label: TABLE 2, Polymerase block 'Dpo2', dNTP row 'T' (incoming nucleotide dTTP), insertion opposite template G

table_label: TABLE 2: Steady-state kinetics of dNTP incorporation opposite G by Dpo 1, Dpo2, Dpo3, and Dpo4 (J. Biol. Chem. 2011, 286(36):31180-31193)

substrate: dTTP

status: corrected


substrate_name: dCTP

column_label: TABLE 2 (Steady-state kinetics of dNTP incorporation opposite G by Dpo 1, Dpo2, Dpo3, and Dpo4); Polymerase column = Dpo2; dNTP column = C (dCTP); column 'Km (uM)' = 9.8 +/- 2.1; column 'kcat (min^-1)' = 0.000053 +/- 0.000003; column 'kcat/Km (min^-1 uM^-1)' = 5.4 x 10^-6; column 'fins' = 1.

normalized_value_unit_evidence: Km: printed TABLE 2 cell 9.8 uM; 9.8 / 1000 = 0.0098 mM. kcat: printed TABLE 2 cell 0.000053 min^-1, under the column head 'kcat' whose unit line reads 'min' with the superscript -1; one min^-1 is 1/60 s^-1, so 0.000053 / 60 = 0.0000008833333333333334 s^-1. kcat/Km: printed TABLE 2 cell 5.4 x 10^-6 min^-1 uM^-1, under the column head 'kcat/Km' whose unit line reads 'min' with the superscript -1 followed by 'uM' with the superscript -1; one min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 0.0000054 x 1000 / 60 = 0.00009 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 2, Polymerase Dpo2, dNTP row C (dCTP): Km = 9.8 uM; kcat = 0.000053 min^-1; printed kcat/Km = 5.4 x 10^-6 min^-1 uM^-1.

row_label: TABLE 2, Polymerase block 'Dpo2', dNTP row 'C' (incoming nucleotide dCTP), insertion opposite template G

substrate: dCTP


substrate_name: dATP

column_label: TABLE 2 (Steady-state kinetics of dNTP incorporation opposite G by Dpo 1, Dpo2, Dpo3, and Dpo4); Polymerase column = Dpo3; dNTP column = A (dATP); column 'Km (uM)' = 390 +/- 10; column 'kcat (min^-1)' = 0.000016 +/- 0.000001; column 'kcat/Km (min^-1 uM^-1)' = 4.1 x 10^-8; column 'fins' = 5.7 x 10^-3.

normalized_value_unit_evidence: Km: printed TABLE 2 cell 390 uM; 390 / 1000 = 0.39 mM. kcat: printed TABLE 2 cell 0.000016 min^-1, under the column head 'kcat' whose unit line reads 'min' with the superscript -1; one min^-1 is 1/60 s^-1, so 0.000016 / 60 = 0.00000026666666666666667 s^-1. kcat/Km: printed TABLE 2 cell 4.1 x 10^-8 min^-1 uM^-1, under the column head 'kcat/Km' whose unit line reads 'min' with the superscript -1 followed by 'uM' with the superscript -1; one min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 0.000000040999999999999997 x 1000 / 60 = 0.0000006833333333333333 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 2, Polymerase Dpo3, dNTP row A (dATP): Km = 390 uM; kcat = 0.000016 min^-1; printed kcat/Km = 4.1 x 10^-8 min^-1 uM^-1.

row_label: TABLE 2, Polymerase block 'Dpo3', dNTP row 'A' (incoming nucleotide dATP), insertion opposite template G

substrate: dATP


substrate_name: dGTP

column_label: TABLE 2 (Steady-state kinetics of dNTP incorporation opposite G by Dpo 1, Dpo2, Dpo3, and Dpo4); Polymerase column = Dpo3; dNTP column = G (dGTP); column 'Km (uM)' = 190 +/- 40; column 'kcat (min^-1)' = 0.000013 +/- 0.000001; column 'kcat/Km (min^-1 uM^-1)' = 6.8 x 10^-8; column 'fins' = 9.5 x 10^-3.

normalized_value_unit_evidence: Km: printed TABLE 2 cell 190 uM; 190 / 1000 = 0.19 mM. kcat: printed TABLE 2 cell 0.000013 min^-1, under the column head 'kcat' whose unit line reads 'min' with the superscript -1; one min^-1 is 1/60 s^-1, so 0.000013 / 60 = 0.00000021666666666666665 s^-1. kcat/Km: printed TABLE 2 cell 6.8 x 10^-8 min^-1 uM^-1, under the column head 'kcat/Km' whose unit line reads 'min' with the superscript -1 followed by 'uM' with the superscript -1; one min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 0.000000068 x 1000 / 60 = 0.0000011333333333333334 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 2, Polymerase Dpo3, dNTP row G (dGTP): Km = 190 uM; kcat = 0.000013 min^-1; printed kcat/Km = 6.8 x 10^-8 min^-1 uM^-1.

row_label: TABLE 2, Polymerase block 'Dpo3', dNTP row 'G' (incoming nucleotide dGTP), insertion opposite template G

substrate: dGTP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y955F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant Y955F


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

proof_lines: SABIO-RK modifier species: DNA-directed DNA polymerase(Enzyme) mutant DNA polymerase lambda (lacking BRCT-like and Proline-rich domains)


substrate_name: DNA with an intact AP site

assay_conditions_summary: pH 7

proof_lines: kcat is 0.075 sec(-1) for 5'-deoxyribose-phosphate lyase activity (at pH 7.0 and 37 degrees Celsius) (PubMed:9614142). kcat is 0.004 sec(-1) for AP lyase activity (at pH 7.0 and 37 degrees Celsius) (PubMed:9614142).

substrate: DNA with an intact AP site


substrate_name: Unknown

sequence_variant_note: Mutation context was captured, but multiple structural mutation events could not be translated into an exact protein sequence safely.

proof_lines: kcat is 87 sec(-1) for DNA synthesis by Pol-delta4 and 19 sec(-1) for Pol-delta3. kcat for exonuclease activity determined using a 26mer/40mer duplex DNA gives a value of 0.003 sec(-1) for Pol-delta4 and 0.026 sec(-1) for Pol-delta3. When u

substrate: Unknown


organism: Human alphaherpesvirus 1

assay_conditions_summary: pH 8; 310.15 K; buffer context in 50 mM Tris-HCl

proof_lines: in 50 mM Tris-HCl (pH 8.0), 8 mM MgCl2, and 0.5 mM dithiohtreitol, at 37°C


organism: Thermococcus waiotapuensis

substrate_name: DNAn

sequence_variant_note: Mutation signature H633R could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.6, 75°C, mM of template, in the presence of an excess of annealed primer, wild-type enzyme

proof_lines: pH 8.6, 75°C, mM of each nucleotide in an equimolar mixture of the four nucleotides, wild-type enzyme

proof_lines: pH 8.6, 75°C, mM of template, in the presence of an excess of annealed prime, wild-type enzyme

substrate: DNAn


proof_lines: pH 8.6, 75°C, mM of template, in the presence of an excess of annealed primer, mutant enzyme H633R

proof_lines: pH 8.6, 75°C, mM of each nucleotide in an equimolar mixture of the four nucleotides, mutant enzyme H633R


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D222A/D327A/K560A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D222A/D327A/N564A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D222A/D327A/R482A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D222A/D327A/Y567A to reconstruct the assayed variant sequence.


substrate_name: dGDP

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D222A/D327A/K486A to reconstruct the assayed variant sequence.

substrate: dGDP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D222A/D327A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D222A/D327A/K483A to reconstruct the assayed variant sequence.


organism: Entamoeba histolytica

substrate_name: D-Glucose

column_label: PMID 10613700 Results 3.2 same prose segment for HXK2 glucose; kcat and glucose Km are reported together and kcat/Km is locked from those values.

raw_value_unit_evidence: Results section 3.2: kcat 237 s^-1 and apparent Km for glucose 47 uM for HXK2.

row_label: HXK2 glucose, optimal purified preparation prose segment

table_label: Results section 3.2 kinetic-properties prose

substrate: D-Glucose


substrate_name: D-Mannose

substrate: D-Mannose


substrate_name: D-glucose

substrate: D-glucose


substrate_name: D-fructose

substrate: D-fructose


substrate_name: ATP

substrate: ATP


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: fructose 6-phosphate

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

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

substrate: fructose 6-phosphate


substrate_name: fructose 1,6-bisphosphate (for gluconeogenic reaction)


substrate_name: ADP (for gluconeogenic reaction)

assay_conditions_summary: cofactor ADP

substrate: ADP (for gluconeogenic reaction)


substrate_name: IDP (for gluconeogenic reaction)

substrate: IDP (for gluconeogenic reaction)


substrate_name: GDP (for gluconeogenic reaction)

substrate: GDP (for gluconeogenic reaction)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I270S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R265T/Y266F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S144T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S144T/R265T/Y266F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S144T/V183T/I270S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S144T/V183T/I270S/R265T/Y266F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V183T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V183T/I270S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V183T/I270S/R265T/Y266F to reconstruct the assayed variant sequence.


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


organism: Solanum chacoense

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

column_label: Table 3. Kinetic constants of pure ScHK2; row D-Glucose; column Kmapp (mM): raw value 0.023 +/- 0.003 mM, normalized value 0.023 mM; column kcat (s^-1): raw value 5.01 +/- 0.75 s^-1, normalized value 5.01 s^-1; column kcat/Kmapp (mM^-1 s^-1): the table prints only 218, a rounded two-significant-figure value, so the absolute ratio recorded here is the quotient of this same row's own two printed cells, 5.01 / 0.023 = 217.82608695652172 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; raw value: 5.01 +/- 0.75; raw unit: s^-1; normalized value: 5.01; normalized unit: s^-1; metric: Km; raw value: 0.023 +/- 0.003; raw unit: mM; normalized value: 0.023; normalized unit: mM; metric: kcat/Km; the table prints only the rounded cell 218 mM^-1 s^-1, so the absolute ratio recorded here is the quotient of this row's own two printed cells; normalized value: 217.82608695652172; normalized unit: s^-1 mM^-1; assay condition: Purified hexahistidine-tagged recombinant ScHK2 hexokinase from Solanum chacoense expressed in Escherichia coli; HK reaction coupled to the glucose-6-phosphate dehydrogenase (EC 1.1.1.49) reaction and assayed at 30 C by monitoring NAD+ reduction at 340 nm; 200 uL reaction mixture containing 50 mM Tris-HCl, pH 8.0, 50 mM KCl, 5 mM MgCl2, 5 mM DTT and 0.3 mM NAD+; apparent Km values calculated from the Michaelis-Menten equation by non-linear least-squares regression and kcat values calculated from the Vmax of Michaelis-Menten plots using a subunit molecular mass of 56,776 Da.

raw_value_unit_evidence: Table 3. Kinetic constants of pure ScHK2 (journal page 336), row D-Glucose: the Kmapp (mM) column prints 0.023 +/- 0.003; the kcat (s^-1) column prints 5.01 +/- 0.75; the kcat/Kmapp (mM^-1 s^-1) column prints 218. Footnote a: For hexoses and ATP, kinetic parameters are given as means +/- SE of values from three independent enzyme preparations.

row_label: D-Glucose


substrate_name: GTP

column_label: Table 3. Kinetic constants of pure ScHK2; row GTP; column Kmapp (mM): raw value 0.231 mM, normalized value 0.231 mM; column kcat (s^-1): raw value 0.85 s^-1, normalized value 0.85 s^-1; column kcat/Kmapp (mM^-1 s^-1): the table prints only 3.7, a rounded two-significant-figure value, so the absolute ratio recorded here is the quotient of this same row's own two printed cells, 0.85 / 0.231 = 3.679653679653679 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; raw value: 0.85; raw unit: s^-1; normalized value: 0.85; normalized unit: s^-1; metric: Km; raw value: 0.231; raw unit: mM; normalized value: 0.231; normalized unit: mM; metric: kcat/Km; the table prints only the rounded cell 3.7 mM^-1 s^-1, so the absolute ratio recorded here is the quotient of this row's own two printed cells; normalized value: 3.679653679653679; normalized unit: s^-1 mM^-1; assay condition: Purified hexahistidine-tagged recombinant ScHK2 hexokinase from Solanum chacoense expressed in Escherichia coli; HK reaction coupled to the glucose-6-phosphate dehydrogenase (EC 1.1.1.49) reaction and assayed at 30 C by monitoring NAD+ reduction at 340 nm; 200 uL reaction mixture containing 50 mM Tris-HCl, pH 8.0, 50 mM KCl, 5 mM MgCl2, 5 mM DTT and 0.3 mM NAD+; apparent Km values calculated from the Michaelis-Menten equation by non-linear least-squares regression and kcat values calculated from the Vmax of Michaelis-Menten plots using a subunit molecular mass of 56,776 Da.

raw_value_unit_evidence: Table 3. Kinetic constants of pure ScHK2 (journal page 336), row GTP: the Kmapp (mM) column prints 0.231; the kcat (s^-1) column prints 0.85; the kcat/Kmapp (mM^-1 s^-1) column prints 3.7. Footnote a: Values for TTP, GTP, UTP, and CTP, are representative of two independent enzyme preparations.

row_label: GTP

substrate: GTP


substrate_name: UTP

column_label: Table 3. Kinetic constants of pure ScHK2; row UTP; column Kmapp (mM): raw value 2.2 mM, normalized value 2.2 mM; column kcat (s^-1): raw value 3.02 s^-1, normalized value 3.02 s^-1; column kcat/Kmapp (mM^-1 s^-1): the table prints only 1.4, a rounded two-significant-figure value, so the absolute ratio recorded here is the quotient of this same row's own two printed cells, 3.02 / 2.2 = 1.3727272727272726 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; raw value: 3.02; raw unit: s^-1; normalized value: 3.02; normalized unit: s^-1; metric: Km; raw value: 2.2; raw unit: mM; normalized value: 2.2; normalized unit: mM; metric: kcat/Km; the table prints only the rounded cell 1.4 mM^-1 s^-1, so the absolute ratio recorded here is the quotient of this row's own two printed cells; normalized value: 1.3727272727272726; normalized unit: s^-1 mM^-1; assay condition: Purified hexahistidine-tagged recombinant ScHK2 hexokinase from Solanum chacoense expressed in Escherichia coli; HK reaction coupled to the glucose-6-phosphate dehydrogenase (EC 1.1.1.49) reaction and assayed at 30 C by monitoring NAD+ reduction at 340 nm; 200 uL reaction mixture containing 50 mM Tris-HCl, pH 8.0, 50 mM KCl, 5 mM MgCl2, 5 mM DTT and 0.3 mM NAD+; apparent Km values calculated from the Michaelis-Menten equation by non-linear least-squares regression and kcat values calculated from the Vmax of Michaelis-Menten plots using a subunit molecular mass of 56,776 Da.

raw_value_unit_evidence: Table 3. Kinetic constants of pure ScHK2 (journal page 336), row UTP: the Kmapp (mM) column prints 2.2; the kcat (s^-1) column prints 3.02; the kcat/Kmapp (mM^-1 s^-1) column prints 1.4. Footnote a: Values for TTP, GTP, UTP, and CTP, are representative of two independent enzyme preparations.

row_label: UTP

substrate: UTP


substrate_name: dTTP

substrate: dTTP


substrate_name: dUTP

substrate: dUTP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D222A/D327A/K560A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D222A/D327A/N564A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D222A/D327A/R482A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D222A/D327A/Y567A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

table_label: Table 3. Kinetic constants of pure ScHK2


column_label: Table 3. Kinetic constants of pure ScHK2; row ATP; column Kmapp (mM): raw value 0.061 +/- 0.01 mM, normalized value 0.061 mM; column kcat (s^-1): raw value 3.50 +/- 0.37 s^-1, normalized value 3.5 s^-1; column kcat/Kmapp (mM^-1 s^-1): the table prints only 57, a rounded two-significant-figure value, so the absolute ratio recorded here is the quotient of this same row's own two printed cells, 3.5 / 0.061 = 57.37704918032787 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; raw value: 3.50 +/- 0.37; raw unit: s^-1; normalized value: 3.5; normalized unit: s^-1; metric: Km; raw value: 0.061 +/- 0.01; raw unit: mM; normalized value: 0.061; normalized unit: mM; metric: kcat/Km; the table prints only the rounded cell 57 mM^-1 s^-1, so the absolute ratio recorded here is the quotient of this row's own two printed cells; normalized value: 57.37704918032787; normalized unit: s^-1 mM^-1; assay condition: Purified hexahistidine-tagged recombinant ScHK2 hexokinase from Solanum chacoense expressed in Escherichia coli; HK reaction coupled to the glucose-6-phosphate dehydrogenase (EC 1.1.1.49) reaction and assayed at 30 C by monitoring NAD+ reduction at 340 nm; 200 uL reaction mixture containing 50 mM Tris-HCl, pH 8.0, 50 mM KCl, 5 mM MgCl2, 5 mM DTT and 0.3 mM NAD+; apparent Km values calculated from the Michaelis-Menten equation by non-linear least-squares regression and kcat values calculated from the Vmax of Michaelis-Menten plots using a subunit molecular mass of 56,776 Da.

raw_value_unit_evidence: Table 3. Kinetic constants of pure ScHK2 (journal page 336), row ATP: the Kmapp (mM) column prints 0.061 +/- 0.01; the kcat (s^-1) column prints 3.50 +/- 0.37; the kcat/Kmapp (mM^-1 s^-1) column prints 57. Footnote a: For hexoses and ATP, kinetic parameters are given as means +/- SE of values from three independent enzyme preparations.

row_label: ATP


substrate_name: TTP

column_label: Table 3. Kinetic constants of pure ScHK2; row TTP; column Kmapp (mM): raw value 0.231 mM, normalized value 0.231 mM; column kcat (s^-1): raw value 1.42 s^-1, normalized value 1.42 s^-1; column kcat/Kmapp (mM^-1 s^-1): the table prints only 6.1, a rounded two-significant-figure value, so the absolute ratio recorded here is the quotient of this same row's own two printed cells, 1.42 / 0.231 = 6.147186147186146 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; raw value: 1.42; raw unit: s^-1; normalized value: 1.42; normalized unit: s^-1; metric: Km; raw value: 0.231; raw unit: mM; normalized value: 0.231; normalized unit: mM; metric: kcat/Km; the table prints only the rounded cell 6.1 mM^-1 s^-1, so the absolute ratio recorded here is the quotient of this row's own two printed cells; normalized value: 6.147186147186146; normalized unit: s^-1 mM^-1; assay condition: Purified hexahistidine-tagged recombinant ScHK2 hexokinase from Solanum chacoense expressed in Escherichia coli; HK reaction coupled to the glucose-6-phosphate dehydrogenase (EC 1.1.1.49) reaction and assayed at 30 C by monitoring NAD+ reduction at 340 nm; 200 uL reaction mixture containing 50 mM Tris-HCl, pH 8.0, 50 mM KCl, 5 mM MgCl2, 5 mM DTT and 0.3 mM NAD+; apparent Km values calculated from the Michaelis-Menten equation by non-linear least-squares regression and kcat values calculated from the Vmax of Michaelis-Menten plots using a subunit molecular mass of 56,776 Da.

raw_value_unit_evidence: Table 3. Kinetic constants of pure ScHK2 (journal page 336), row TTP: the Kmapp (mM) column prints 0.231; the kcat (s^-1) column prints 1.42; the kcat/Kmapp (mM^-1 s^-1) column prints 6.1. Footnote a: Values for TTP, GTP, UTP, and CTP, are representative of two independent enzyme preparations.

row_label: TTP

substrate: TTP


substrate_name: CTP

column_label: Table 3. Kinetic constants of pure ScHK2; row CTP; column Kmapp (mM): raw value 2.0 mM, normalized value 2.0 mM; column kcat (s^-1): raw value 1.61 s^-1, normalized value 1.61 s^-1; column kcat/Kmapp (mM^-1 s^-1): the table prints only 0.8, a rounded two-significant-figure value, so the absolute ratio recorded here is the quotient of this same row's own two printed cells, 1.61 / 2.0 = 0.805 s^-1 mM^-1.

normalized_value_unit_evidence: metric: kcat; raw value: 1.61; raw unit: s^-1; normalized value: 1.61; normalized unit: s^-1; metric: Km; raw value: 2.0; raw unit: mM; normalized value: 2.0; normalized unit: mM; metric: kcat/Km; the table prints only the rounded cell 0.8 mM^-1 s^-1, so the absolute ratio recorded here is the quotient of this row's own two printed cells; normalized value: 0.805; normalized unit: s^-1 mM^-1; assay condition: Purified hexahistidine-tagged recombinant ScHK2 hexokinase from Solanum chacoense expressed in Escherichia coli; HK reaction coupled to the glucose-6-phosphate dehydrogenase (EC 1.1.1.49) reaction and assayed at 30 C by monitoring NAD+ reduction at 340 nm; 200 uL reaction mixture containing 50 mM Tris-HCl, pH 8.0, 50 mM KCl, 5 mM MgCl2, 5 mM DTT and 0.3 mM NAD+; apparent Km values calculated from the Michaelis-Menten equation by non-linear least-squares regression and kcat values calculated from the Vmax of Michaelis-Menten plots using a subunit molecular mass of 56,776 Da.

raw_value_unit_evidence: Table 3. Kinetic constants of pure ScHK2 (journal page 336), row CTP: the Kmapp (mM) column prints 2.0; the kcat (s^-1) column prints 1.61; the kcat/Kmapp (mM^-1 s^-1) column prints 0.8. Footnote a: Values for TTP, GTP, UTP, and CTP, are representative of two independent enzyme preparations.

row_label: CTP

substrate: CTP


column_label: Table 3 row ATP; columns Kmapp (mM), kcat (s^-1), and kcat/Kmapp (mM^-1 s^-1).

normalized_value_unit_evidence: Central values are Kmapp 0.061 mM, kcat 3.5 s^-1, and independently printed kcat/Kmapp 57.0 s^-1 mM^-1.

table_label: Table 3, Kinetic constants of pure ScHK2


column_label: Table 3 row CTP; columns Kmapp (mM), kcat (s^-1), and kcat/Kmapp (mM^-1 s^-1).

normalized_value_unit_evidence: Central values are Kmapp 2.0 mM, kcat 1.61 s^-1, and independently printed kcat/Kmapp 0.8 s^-1 mM^-1.

raw_value_unit_evidence: CTP: Kmapp 2.0 mM; kcat 1.61 s^-1; kcat/Kmapp 0.8 mM^-1 s^-1


substrate_name: D-Fructose

column_label: Table 3 row D-Fructose; columns Kmapp (mM), kcat (s^-1), and kcat/Kmapp (mM^-1 s^-1).

normalized_value_unit_evidence: Central values are Kmapp 5.2 mM, kcat 3.78 s^-1, and independently printed kcat/Kmapp 0.7 s^-1 mM^-1.

row_label: D-Fructose

substrate: D-Fructose


organism: Helianthus annuus


assay_conditions_summary: pH 7; 295.15 K; cofactor ATP


enzyme_display_name: exo-alpha-sialidase

organism: Bacteroides thetaiotaomicron

enzyme: exo-alpha-sialidase


organism: Clostridium perfringens

substrate_name: Unknown

substrate: Unknown


organism: Corynebacterium diphtheriae


organism: Cutibacterium acnes


organism: Danio rerio


sequence_source: UniProtKB reviewed accession Q9Y3R4; direct REST lookup on 2026-05-25


sequence_source: UniProtKB reviewed accession Q9UQ49; direct REST lookup on 2026-05-25; variant reconstructed from mutation signature A160G/H277F

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

proof_lines: recombinant mutants A160G and H277F, pH 5.0, 37°C


sequence_source: UniProtKB reviewed accession Q9UQ49; direct REST lookup on 2026-05-25; variant reconstructed from mutation signature R48S


sequence_source: UniProtKB reviewed accession Q9UQ49; direct REST lookup on 2026-05-25; variant reconstructed from mutation signature H277F


sequence_source: UniProtKB reviewed accession Q9UQ49; direct REST lookup on 2026-05-25; variant reconstructed from mutation signature R48N


sequence_source: UniProtKB reviewed accession Q9UQ49; direct REST lookup on 2026-05-25; variant reconstructed from mutation signature A160G

sequence_variant_note: Mutation signature A160G matches the mutant residue at offset +0 and the reference residue at offset -3; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB reviewed accession Q9UQ49; direct REST lookup on 2026-05-25

proof_lines: recombinant wild-type enzyme, pH 5.0, 37°C


sequence_source: UniProtKB reviewed accession Q9UQ49; direct REST lookup on 2026-05-25; variant reconstructed from mutation signature E51S

sequence_variant_note: Mutation signature E51S matches the mutant residue at offset +0 and the reference residue at offset -8; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


organism: Aspergillus fumigatus

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q4WQS0 direct REST/FASTA lookup; Y358H reconstructed from canonical sequence and applied mutation signature Y358H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y358H, pH 5.2, 16 mM sodium tartrate, at 37°C


sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

proof_lines: mutant enzyme R71L, pH 5.2, 16 mM sodium tartrate, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q4WQS0 direct REST/FASTA lookup; D84A reconstructed from canonical sequence and applied mutation signature D84A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D84A, pH 5.2, 16 mM sodium tartrate, at 37°C


sequence_source: UniProtKB:Q4WQS0 direct REST/FASTA lookup

proof_lines: wild type enzyme, pH 5.2, 16 mM sodium tartrate, at 37°C


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB:Q4WQS0 direct REST/FASTA lookup from source-provided SKiD accession

source: skid


organism: Aspergillus terreus

sequence_source: UniProtKB:Q0CMX0 direct REST/FASTA lookup

proof_lines: in 100 mM sodium acetate, at pH 4.0 and 37°C


organism: Avian orthoavulavirus 1

sequence_source: UniProtKB:Q9Q2W5 direct REST/FASTA lookup from source-provided SKiD accession


organism: avian paramyxovirus 1

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9Q2W5 direct REST/FASTA lookup; S418A reconstructed from source-provided accession but paper strain needs arbitration and applied mutation signature S418A to reconstruct the assayed variant sequence.


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from UniProt Q9UQ49 canonical sequence plus selected mutation M87G; residue check on 2026-05-25 confirmed canonical M87 before reconstruction. and applied mutation signature M87G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UQ49 canonical sequence plus selected mutation H277F; residue check on 2026-05-25 confirmed canonical H277 before reconstruction. and applied mutation signature H277F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UQ49 canonical sequence plus selected mutation A160G; residue check on 2026-05-25 confirmed canonical A160 before reconstruction. and applied mutation signature A160G to reconstruct the assayed variant sequence.


organism: Influenza A virus

sequence_source: UniProt REST direct check on 2026-05-25: queried P03469, primary accession P03469.


sequence_source: UniProt REST direct check on 2026-05-25: queried P03468, primary accession P03468.


sequence_source: UniProt REST direct check on 2026-05-25: queried secondary accession Q288X1, live primary accession Q1K9J1.


sequence_source: UniProt REST direct check on 2026-05-25: queried Q8JSD9, primary accession Q8JSD9.


sequence_source: UniProt REST direct check on 2026-05-25: queried Q20N24, primary accession Q20N24.


organism: influenza A virus H1N1

sequence_variant_note: Resolved canonical sequence from UniProtKB:C3W6G3 REST lookup on 2026-05-25; applied H275Y and applied mutation signature H275Y to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H275Y, at 37°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:C3W6G3 REST lookup on 2026-05-25; applied H275Y/S247N and applied mutation signature H275Y/S247N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H275Y/S247N, at 37°C, pH not specified in the publication


sequence_source: UniProtKB:C3W6G3 REST lookup on 2026-05-25

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


organism: influenza A virus H5N1

sequence_source: UniProtKB:A5Z227 REST lookup on 2026-05-25


organism: Influenza B virus

sequence_source: UniProtKB:P03474 REST lookup on 2026-05-25


sequence_variant_note: Resolved canonical sequence from UniProtKB:P03474 REST lookup on 2026-05-25; applied D149E and applied mutation signature D149E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P03474 REST lookup on 2026-05-25; applied R150K and applied mutation signature R150K to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q9Q2W5 canonical sequence fetched directly on 2026-05-25


sequence_source: UniProtKB:Q9Q2W5 canonical sequence fetched directly on 2026-05-25, with Y262F applied after confirming residue 262 is Y


organism: Bacteroides fragilis

sequence_source: UniProtKB:Q5L868 direct lookup redirects to UniProtKB:A0A380YS77 canonical sequence, fetched on 2026-05-25


substrate_name: sialic acid

substrate: sialic acid


sequence_source: UniProtKB:Q8AAK9 canonical sequence fetched directly on 2026-05-25


proof_lines:
pH 7.0 and 37°C
Raw SKiD Env: Temp=37°C, pH=7


sequence_source: UniProtKB:Q1K9L1 canonical sequence


organism: influenza A virus

substrate_name: fetuin

sequence_source: UniProtKB:A0A076VGS2 canonical sequence

substrate: fetuin


sequence_source: UniProtKB:C7FH46 canonical sequence

proof_lines:
at pH 5.5 and 37°C
Raw SKiD Env: Temp=37°C, pH=5.5


sequence_source: UniProtKB:C3W6G3 canonical sequence

proof_lines: wild type enzyme, at 37°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:C3W6G3 canonical sequence with direct 1-based substitution reconstruction H275Y/I223V and applied mutation signature H275Y/I223V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H275Y/I223V, at 37°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:C3W6G3 canonical sequence with direct 1-based substitution reconstruction I223V and applied mutation signature I223V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I223V, at 37°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:C3W6G3 canonical sequence with direct 1-based substitution reconstruction S247N and applied mutation signature S247N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S247N, at 37°C, pH not specified in the publication


organism: Glutamicibacter nicotianae

substrate_name: glucomacropeptide

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

proof_lines:
37°C, sialidase isoenzyme NA2
37°C, sialidase isoenzyme NA1

substrate: glucomacropeptide


organism: Aeropyrum pernix

substrate_name: D-glucose 6-phosphate

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

assay_conditions_summary: pH 6.7; 358.15 K; cofactor ATP

substrate: D-glucose 6-phosphate


substrate_name: adenosine

substrate: adenosine


substrate_name: fructose

substrate: fructose


substrate_name: D-ribose 5-phosphate

substrate: D-ribose 5-phosphate


substrate_name: D-ribose

substrate: D-ribose


organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)

substrate_name: 4-methylumbelliferyl alpha-D-N-acetylneuraminic acid (MUN)


substrate_name: ganglioside GD1a

substrate: ganglioside GD1a


substrate_name: ganglioside GM3 (in the presence of Triton X-100)


sequence_source: UniProtKB:P03474 canonical FASTA (sp|P03474|NRAM_INBLE Neuraminidase OS=Influenza B virus (strain B/Lee/1940) OX=518987 GN=NA PE=1 SV=1) with selected R374N substitution applied after coordinate check on 2026-05-25

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


sequence_source: UniProtKB:P03474 canonical FASTA (sp|P03474|NRAM_INBLE Neuraminidase OS=Influenza B virus (strain B/Lee/1940) OX=518987 GN=NA PE=1 SV=1) with selected R374K substitution applied after coordinate check on 2026-05-25


sequence_source: UniProtKB:P03474 canonical FASTA (sp|P03474|NRAM_INBLE Neuraminidase OS=Influenza B virus (strain B/Lee/1940) OX=518987 GN=NA PE=1 SV=1) with selected E275D substitution applied after coordinate check on 2026-05-25


sequence_source: UniProtKB:P03474 canonical FASTA (sp|P03474|NRAM_INBLE Neuraminidase OS=Influenza B virus (strain B/Lee/1940) OX=518987 GN=NA PE=1 SV=1) with selected E117G substitution applied after coordinate check on 2026-05-25


sequence_source: UniProtKB:P03474 canonical FASTA (sp|P03474|NRAM_INBLE Neuraminidase OS=Influenza B virus (strain B/Lee/1940) OX=518987 GN=NA PE=1 SV=1) with selected R223K substitution applied after coordinate check on 2026-05-25


organism: Micromonospora viridifaciens

substrate_name: phenyl alpha-sialoside

sequence_source: UniProtKB:Q02834 canonical FASTA (sp|Q02834|NANH_MICVI Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1) with selected Y370G substitution applied after coordinate check on 2026-05-25

substrate: phenyl alpha-sialoside


sequence_source: UniProtKB:Q02834 canonical FASTA (sp|Q02834|NANH_MICVI Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1) with selected E260D substitution applied after coordinate check on 2026-05-25


sequence_source: UniProtKB:Q02834 canonical FASTA (sp|Q02834|NANH_MICVI Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1) with selected E260C substitution applied after coordinate check on 2026-05-25


sequence_source: UniProtKB:Q02834 reviewed Swiss-Prot; REST check 2026-05-25


organism: Mumps orthorubulavirus

sequence_source: UniProtKB:P19762 reviewed Swiss-Prot; PMID 34778199 methods cite P19762-1

proof_lines: at pH 7.4, temperature not specified in the publication


organism: Porphyromonas gingivalis

sequence_source: GenBank:AUR47485.1 and RCSB PDB:8GN6; source UniProt A0A1R4DV85 is deleted/inactive


organism: Tannerella forsythia

sequence_variant_note: Resolved canonical sequence from UniProtKB:G8UIQ1 canonical sequence with PMID 35916484/PDB author-numbering offset -13 applied and applied mutation signature R306A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:G8UIQ1 canonical sequence with PMID 35916484/PDB author-numbering offset -13 applied and applied mutation signature V236Y with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:G8UIQ1 unreviewed TrEMBL; REST check 2026-05-25; RCSB 7QYP maps to G8UIQ1


sequence_variant_note: Resolved canonical sequence from UniProtKB:G8UIQ1 canonical sequence with PMID 35916484/PDB author-numbering offset -13 applied and applied mutation signature V236Q with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:G8UIQ1 canonical sequence with PMID 35916484/PDB author-numbering offset -13 applied and applied mutation signature I456Y with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


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

proof_lines: mutant enzyme N234Y/S235Y, at pH 7.4 and 25°C

proof_lines: mutant enzyme N234YS235Y, at pH 7.4 and 25°C


organism: Treponema denticola

sequence_source: UniProtKB REST/FASTA accession Q73QH2 checked 2026-05-25

proof_lines: in 70 mM sodium citrate, at pH 7.0 and 37°C


organism: Trichophyton rubrum

sequence_source: UniProtKB REST/FASTA accession A0A178EUH2 checked 2026-05-25

proof_lines: in 100 mM sodium acetate,at pH 4.0 and 37°C


organism: Geobacillus stearothermophilus

substrate_name: ATP

assay_conditions_summary: pH 8.2; 303.15 K; cofactor ATP

column_label: Table 2: Alternative Nucleoside Triphosphate Substrates (Biochemistry 1994, 33(11):3424-3431); row ATP; the Michaelis constant 0.07 mM comes from the column Km(NTP) (mM) of that row, whose footnote a states that Fru-6P concentration was kept fixed at 1.0 mM (saturating) for these determinations; the turnover number 112 s-1 comes from the Results text eq 3 fit of the forward reaction, which is the 100 percent reference of the Table 2 column % of kcat(ATP) and is the only forward-reaction turnover number the article prints. There is no kcat/Km column.

normalized_value_unit_evidence: kcat: printed value 112 s-1; already in s^-1, so no unit conversion applies; the paper value is 112.0 s^(-1). Km: printed cell 0.07 mM; already in mM, so no unit conversion applies; the paper value is 0.07 mM. kcat/Km: this article prints no kcat/Km cell for this measurement, so the catalog value 1599.9999999999998 s^(-1)*mM^(-1) is not a printed value; it is the quotient 112 / 0.07 of this measurement's own two printed values, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, row ATP: Km = 0.07 mM printed in the column Km(NTP) (mM). Results text, forward reaction fit to eq 3 with A as MgATP and B as Fru-6P: kcat = 112 s-1. No kcat/Km value is printed for this measurement.

row_label: Table 2, row ATP, alternative nucleoside triphosphate substrates, read with the forward-reaction turnover number of the Results text

substrate: ATP


substrate_name: D-Fructose 1,6-bisphosphate

assay_conditions_summary: pH 8.2; 303.15 K; cofactor ADP

column_label: Results text, reverse reaction initial velocity analysis (Biochemistry 1994, 33(11):3424-3431); the paragraph states that the initial velocity data were fit to the equation for a rapid-equilibrium random or ordered bireactant mechanism (eq 3), assuming that A is MgADP and B is Fru-1,6BP, and prints kcat = 3.2 s-1 together with Kb = 0.44 mM, the Michaelis constant of substrate B, which that fit declares to be Fru-1,6BP. The same paragraph prints Ka = 0.11 mM for MgADP and the two dissociation constants Kia and Kib. There is no kcat/Km value.

normalized_value_unit_evidence: kcat: printed value 3.2 s-1; already in s^-1, so no unit conversion applies; the paper value is 3.2 s^(-1). Km: printed value 0.44 mM; already in mM, so no unit conversion applies; the paper value is 0.44 mM. kcat/Km: this article prints no kcat/Km cell for this measurement, so the catalog value 7.272727272727273 s^(-1)*mM^(-1) is not a printed value; it is the quotient 3.2 / 0.44 of this measurement's own two printed values, typed derived_same_measurement.

raw_value_unit_evidence: Results text, reverse reaction fit to eq 3 with A as MgADP and B as Fru-1,6BP: kcat = 3.2 s-1 and Kb = 0.44 mM, the Michaelis constant of substrate B, Fru-1,6BP. No kcat/Km value is printed for this measurement.

row_label: Results text, reverse reaction initial velocity fit to eq 3 with A as MgADP and B as Fru-1,6BP

substrate: D-Fructose 1,6-bisphosphate


substrate_name: GTP

substrate: GTP


substrate_name: UTP

substrate: UTP


organism: Homo sapiens

substrate_name: dATP (at 30 degrees Celsius)

substrate: dATP (at 30 degrees Celsius)


substrate_name: dGTP (at 30 degrees Celsius)

substrate: dGTP (at 30 degrees Celsius)


substrate_name: dCTP (at 30 degrees Celsius)

substrate: dCTP (at 30 degrees Celsius)


substrate_name: dTTP (at 30 degrees Celsius)

substrate: dTTP (at 30 degrees Celsius)


enzyme_display_name: mandelate racemase

organism: Pseudomonas putida

sequence_source: UniProtKB P11444 canonical FASTA direct check plus selected source mutation_signature V22L; V22L checked against canonical residue V22.

enzyme: mandelate racemase


sequence_source: UniProtKB P11444 canonical FASTA direct check plus selected source mutation_signature Y54A; Y54A checked against canonical residue Y54.

sequence_variant_note: Mutation signature Y54A matches the mutant residue at offset +0 and the reference residue at offset -4; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB P11444 canonical FASTA direct check plus selected source mutation_signature V26I; V26I checked against canonical residue V26.


sequence_source: UniProtKB P11444 canonical FASTA direct check plus selected source mutation_signature Y54I; Y54I checked against canonical residue Y54.

sequence_variant_note: Mutation signature Y54I matches the mutant residue at offset +0 and the reference residue at offset -4; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB P11444 canonical FASTA direct check plus selected source mutation_signature Y54F; Y54F checked against canonical residue Y54.

sequence_variant_note: Mutation signature Y54F matches the mutant residue at offset +0 and the reference residue at offset -4; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB P11444 FASTA direct check; reviewed Swiss-Prot mandelate racemase from Pseudomonas putida.


sequence_source: UniProtKB P11444 canonical sequence reconstructed with selected mutation signature


sequence_variant_note: Mutation signature Y54V matches the mutant residue at offset +0 and the reference residue at offset -4; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature Y54L matches the mutant residue at offset +0 and the reference residue at offset -4; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


substrate_name: (R)-mandelamide

substrate: (R)-mandelamide


sequence_variant_note: Mutation signature V26I/Y54I matches the mutant residue at offset +0 and the reference residue at offset -4; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB REST FASTA P11444 canonical sequence; reconstructed V29F after confirming canonical residue 29 is V.

proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29F


substrate_name: (R)-mandelate

sequence_source: UniProtKB REST FASTA P11444 canonical sequence.

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

substrate: (R)-mandelate


sequence_source: UniProtKB REST FASTA P11444 canonical sequence; reconstructed V22A after confirming canonical residue 22 is V.

proof_lines:
mutant V22A, pH 7.5, 25°C
pH 7.5, 3.3 mM Mg2+, mutant V22A
pH 7.5, 3.3 mM Mg2+ mutant V22A


sequence_source: UniProtKB REST FASTA P11444 canonical sequence; reconstructed V29L after confirming canonical residue 29 is V.

proof_lines:
mutant V29L, pH 7.5, 25°C
pH 7.5, 3.3 mM Mg2+, mutant V29L
pH 7.5, 25°C, mutant V29L


substrate_name: (S)-trifluorolactate

substrate: (S)-trifluorolactate


substrate_name: (R)-trifluorolactate

substrate: (R)-trifluorolactate


sequence_source: UniProtKB REST FASTA P11444 canonical sequence; reconstructed V26I after confirming canonical residue 26 is V.


sequence_source: UniProtKB REST FASTA P11444 canonical sequence; reconstructed L319F after confirming canonical residue 319 is L.


sequence_source: UniProtKB:P11444 canonical sequence with V26L reconstructed after direct residue check


sequence_source: UniProtKB:P11444 canonical sequence with Y54F reconstructed after direct residue check


sequence_source: UniProtKB:P11444 canonical sequence with Y54L reconstructed after direct residue check


sequence_source: UniProtKB:P11444 canonical sequence with V26I/Y54I reconstructed after direct residue checks


sequence_source: UniProtKB:P11444 canonical sequence

column_label: Table 1: Kinetic parameters of the wild type and mutants towards R-3-chloromandelic acid, R-mandelamide and R-2-naphthylglycolate (Enzyme and Microbial Technology 55 (2014) 121-127); row 'WT' of the 'R-Mandelamide' section; column 'Km (mM)' = 1.13; column 'kcat (s^-1)' = 11.03; column 'kcat/Km (M^-1 s^-1)' = 9.79 x 10^3

normalized_value_unit_evidence: Km: printed Table 1 cell 1.13 mM; the cell is already in mM, so no unit conversion applies; 1.13 mM. kcat: printed Table 1 cell 11.03 s^-1, which is 11.03 s^-1; the cell is already in s^-1, so no unit conversion applies (this paper prints no min^-1 kinetic cell). kcat/Km: printed Table 1 cell 9.79 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9.79 x 10^3 / 1000 = 9.79 s^-1 mM^-1. The printed efficiency cell is the paper's own fitted primary value, so this pass carries 9.79 s^-1 mM^-1 for kcat/Km.

raw_value_unit_evidence: Table 1, section 'R-Mandelamide', row 'WT': Km cell 1.13 mM; kcat cell 11.03 s^-1; printed kcat/Km cell 9.79 x 10^3 M^-1 s^-1.

row_label: Table 1, section 'R-Mandelamide', printed row label 'WT'


column_label: Table 1: Kinetic parameters of the wild type and mutants towards R-3-chloromandelic acid, R-mandelamide and R-2-naphthylglycolate (Enzyme and Microbial Technology 55 (2014) 121-127); row 'WT' of the 'R-3-Chloromandelic acid' section; column 'Km (mM)' = 1.89; column 'kcat (s^-1)' = 4.69 x 10^2; column 'kcat/Km (M^-1 s^-1)' = 2.49 x 10^5

normalized_value_unit_evidence: Km: printed Table 1 cell 1.89 mM; the cell is already in mM, so no unit conversion applies; 1.89 mM. kcat: printed Table 1 cell 4.69 x 10^2 s^-1, which is 469.0 s^-1; the cell is already in s^-1, so no unit conversion applies (this paper prints no min^-1 kinetic cell). kcat/Km: printed Table 1 cell 2.49 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.49 x 10^5 / 1000 = 249.0 s^-1 mM^-1. The printed efficiency cell is the paper's own fitted primary value, so this pass carries 249.0 s^-1 mM^-1 for kcat/Km.

raw_value_unit_evidence: Table 1, section 'R-3-Chloromandelic acid', row 'WT': Km cell 1.89 mM; kcat cell 4.69 x 10^2 s^-1; printed kcat/Km cell 2.49 x 10^5 M^-1 s^-1.

row_label: Table 1, section 'R-3-Chloromandelic acid', printed row label 'WT'


sequence_source: UniProtKB:P11444 canonical sequence with V26I/Y54V reconstructed after direct residue checks

sequence_variant_note: Mutation signature V26I/Y54V matches the mutant residue at offset +0 and the reference residue at offset -4; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P11444 canonical sequence with V26S reconstructed after direct residue check


sequence_source: UniProt REST P11444 canonical sequence checked on 2026-05-25; mutation V26A applied after validating the canonical residue coordinate.

proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A


sequence_source: UniProt REST P11444 canonical sequence checked on 2026-05-25; mutation V22I/V29L applied after validating the canonical residue coordinate.

proof_lines: mutant V22I/V29L, pH 7.5, 25°C, presence of 20 mM Mg2+

proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22I/V29L


substrate_name: (S)-Mandelate

sequence_source: UniProt REST P11444 canonical sequence checked on 2026-05-25; mutation V26A/V29L applied after validating the canonical residue coordinate.

proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A/V29L

substrate: (S)-Mandelate


sequence_source: UniProt REST P11444 canonical sequence checked on 2026-05-25; mutation V22F applied after validating the canonical residue coordinate.

proof_lines: pH 7.5, mutant V22F, addition of either 10 mM (R)- or (S)-mandelate


sequence_source: UniProt REST P11444 canonical sequence checked on 2026-05-25; mutation T24S applied after validating the canonical residue coordinate.

proof_lines: pH 7.5, mutant T24S, addition of either 10 mM (R)- or (S)-mandelate


sequence_source: UniProt REST P11444 canonical sequence checked on 2026-05-25; mutation V26F applied after validating the canonical residue coordinate.

proof_lines: pH 7.5, mutant V26F, addition of either 10 mM (R)- or (S)-mandelate


sequence_source: UniProt REST P11444 canonical sequence checked on 2026-05-25; mutation V22I applied after validating the canonical residue coordinate.

proof_lines: mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+


sequence_source: UniProt REST P11444 canonical sequence checked on 2026-05-25; mutation A25V applied after validating the canonical residue coordinate.

proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant A25V


sequence_source: UniProt P11444 FASTA retrieved directly; V26I and Y54V applied after confirming P11444 has V at 26 and Y at 54.


sequence_source: UniProt P11444 FASTA retrieved directly; V29L applied after confirming P11444 has V at 29.


sequence_source: UniProt P11444 FASTA retrieved directly; Y54A applied after confirming P11444 has Y at 54.


sequence_source: UniProt P11444 FASTA retrieved directly; V26S applied after confirming P11444 has V at 26.


sequence_source: UniProt P11444 FASTA retrieved directly; V22I applied after confirming P11444 has V at 22.


sequence_source: UniProt P11444 FASTA checked directly; variant sequence not reconstructed because Y45F conflicts with the P11444 reference residue at position 45.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11444 and applied mutation signature V22I/V29I to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer Tris-HCl

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(R)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I/V29I': Km = 15.10 mM, kcat = 2.60 s^(-1), kcat/Km = 172.25 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 15.10 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 15.1 mM. kcat: printed Table 2 cell 2.60 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 2.6 s^(-1). kcat/Km: printed Table 2 cell 172.25 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 172.25 / 1000 = 0.17225 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (R)-2-CMA half of the printed line for enzyme form V22I/V29I: Km = 15.10 mM; kcat = 2.60 s^(-1); printed kcat/Km = 172.25 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11444 and applied mutation signature V22I/V29I/Y54F to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(R)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I/V29I/Y54F': Km = 14.52 mM, kcat = 2.57 s^(-1), kcat/Km = 176.70 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 14.52 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 14.52 mM. kcat: printed Table 2 cell 2.57 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 2.57 s^(-1). kcat/Km: printed Table 2 cell 176.70 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 176.70 / 1000 = 0.1767 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (R)-2-CMA half of the printed line for enzyme form V22I/V29I/Y54F: Km = 14.52 mM; kcat = 2.57 s^(-1); printed kcat/Km = 176.70 M^-1 s^-1.


sequence_source: UniProtKB:P11444 canonical FASTA, direct lookup on 2026-05-25

assay_conditions_summary: pH 7.5; 298.15 K; buffer Na-HEPES

proof_lines: recombinant mandelate racemase, putative misfolded form with N-terminal hexahistidine tag, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2

proof_lines: recombinant mandelate racemase represents correctly folded enzyme, with N-terminal hexahistidine tag, in Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2


sequence_source: UniProtKB:P11444 canonical FASTA with validated F52W substitution, reconstructed on 2026-05-25


sequence_source: UniProtKB:P11444 canonical FASTA with validated Y54W substitution, reconstructed on 2026-05-25

sequence_variant_note: Mutation signature Y54W matches the mutant residue at offset +0 and the reference residue at offset -4; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P11444 canonical FASTA with validated F52W/Y54W substitutions, reconstructed on 2026-05-25

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


sequence_source: UniProtKB:P11444 canonical FASTA with validated V26L substitution, reconstructed on 2026-05-25

proof_lines:
mutant V26L, pH 7.5, 25°C
pH 7.5, 3.3 mM Mg2+, mutant V26L
pH 7.5, 25°C, mutant V26L


sequence_source: UniProtKB:P11444 canonical FASTA with validated V29A substitution, reconstructed on 2026-05-25

proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29A


organism: Unknown

substrate_name: Unknown

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

substrate: Unknown


sequence_source: UniProt P11444 FASTA direct check, canonical wild-type sequence

proof_lines: pH 7.5, 25°C, recombinant wild-type enzyme

proof_lines: wild-type, pH 7.5, 25°C, presence of 20 mM Mg2+


column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(S)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I/V29I/Y54F': Km = 17.94 mM, kcat = 3.49 s^(-1), kcat/Km = 194.69 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 17.94 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 17.94 mM. kcat: printed Table 2 cell 3.49 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 3.49 s^(-1). kcat/Km: printed Table 2 cell 194.69 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 194.69 / 1000 = 0.19469 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (S)-2-CMA half of the printed line for enzyme form V22I/V29I/Y54F: Km = 17.94 mM; kcat = 3.49 s^(-1); printed kcat/Km = 194.69 M^-1 s^-1.


row_label: Table 2, (R)-2-CMA half of the printed line for enzyme form V22I/V29I

table_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid


column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(R)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'WT': Km = 14.82 mM, kcat = 0.90 s^(-1), kcat/Km = 60.74 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 14.82 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 14.82 mM. kcat: printed Table 2 cell 0.90 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 0.9 s^(-1). kcat/Km: printed Table 2 cell 60.74 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 60.74 / 1000 = 0.06074 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (R)-2-CMA half of the printed line for enzyme form WT: Km = 14.82 mM; kcat = 0.90 s^(-1); printed kcat/Km = 60.74 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11444 and applied mutation signature V29I to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(S)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V29I': Km = 14.35 mM, kcat = 1.83 s^(-1), kcat/Km = 127.66 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 14.35 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 14.35 mM. kcat: printed Table 2 cell 1.83 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 1.83 s^(-1). kcat/Km: printed Table 2 cell 127.66 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 127.66 / 1000 = 0.12766 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (S)-2-CMA half of the printed line for enzyme form V29I: Km = 14.35 mM; kcat = 1.83 s^(-1); printed kcat/Km = 127.66 M^-1 s^-1.


column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(S)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I/V29I': Km = 13.74 mM, kcat = 2.35 s^(-1), kcat/Km = 159.31 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 13.74 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 13.74 mM. kcat: printed Table 2 cell 2.35 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 2.35 s^(-1). kcat/Km: printed Table 2 cell 159.31 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 159.31 / 1000 = 0.15931 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (S)-2-CMA half of the printed line for enzyme form V22I/V29I: Km = 13.74 mM; kcat = 2.35 s^(-1); printed kcat/Km = 159.31 M^-1 s^-1.


organism: Thermoproteus tenax


substrate_name: D-glucose

substrate: D-glucose


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


substrate_name: D-fructose

substrate: D-fructose


sequence_source: UniProtKB P11444 REST/FASTA direct check; single-substitution reconstruction Y137L from canonical sequence.


sequence_source: UniProtKB P11444 REST/FASTA direct check; single-substitution reconstruction Y137S from canonical sequence.


sequence_source: UniProtKB P11444 REST/FASTA direct check; single-substitution reconstruction K166R from canonical sequence.

sequence_variant_note: Mutation signature K166R matches the mutant residue at offset +0 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines:
pH 7.5, 25°C, mutant enzyme K166R
mutant K166R
25°C, pH 7.5, mutant enzyme K166R


sequence_source: UniProtKB P11444 REST/FASTA direct check; single-substitution reconstruction K164R from canonical sequence.

sequence_variant_note: Mutation signature K164R matches the mutant residue at offset +0 and the reference residue at offset +2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines:
pH 7.5, 25°C, mutant enzyme K164R
25°C, pH 7.5, mutant enzyme K164R


sequence_source: UniProtKB P11444 REST/FASTA direct check; single-substitution reconstruction L93R from canonical sequence.


sequence_source: UniProtKB P11444 REST/FASTA direct check; single-substitution reconstruction L93N from canonical sequence.


sequence_source: UniProtKB P11444 REST/FASTA direct check; single-substitution reconstruction L93A from canonical sequence.


sequence_source: UniProtKB P11444 REST/FASTA direct check; single-substitution reconstruction L93F from canonical sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11444 and applied mutation signature V22I to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(R)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I': Km = 15.51 mM, kcat = 1.82 s^(-1), kcat/Km = 117.82 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 15.51 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 15.51 mM. kcat: printed Table 2 cell 1.82 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 1.82 s^(-1). kcat/Km: printed Table 2 cell 117.82 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 117.82 / 1000 = 0.11782 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (R)-2-CMA half of the printed line for enzyme form V22I: Km = 15.51 mM; kcat = 1.82 s^(-1); printed kcat/Km = 117.82 M^-1 s^-1.


column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(R)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V29I': Km = 11.99 mM, kcat = 1.45 s^(-1), kcat/Km = 121.37 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 11.99 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 11.99 mM. kcat: printed Table 2 cell 1.45 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 1.45 s^(-1). kcat/Km: printed Table 2 cell 121.37 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 121.37 / 1000 = 0.12137 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (R)-2-CMA half of the printed line for enzyme form V29I: Km = 11.99 mM; kcat = 1.45 s^(-1); printed kcat/Km = 121.37 M^-1 s^-1.


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


proof_lines: 25°C, pH 7.5, mutant enzyme tmMR-thiaLys


proof_lines: 25°C, pH 7.5, mutant enzyme C92S/C264S/166thiaK


sequence_source: UniProtKB:P11444 canonical FASTA with validated Y137F substitution, checked 2026-05-25


sequence_source: UniProtKB:P11444 canonical FASTA with validated Y137T substitution, checked 2026-05-25


row_label: Table 2, (R)-2-CMA half of the printed line for enzyme form V22I/V29I/Y54F


column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(S)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I': Km = 19.91 mM, kcat = 2.47 s^(-1), kcat/Km = 123.97 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 19.91 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 19.91 mM. kcat: printed Table 2 cell 2.47 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 2.47 s^(-1). kcat/Km: printed Table 2 cell 123.97 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 123.97 / 1000 = 0.12397 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (S)-2-CMA half of the printed line for enzyme form V22I: Km = 19.91 mM; kcat = 2.47 s^(-1); printed kcat/Km = 123.97 M^-1 s^-1.


row_label: Table 2, (R)-2-CMA half of the printed line for enzyme form V29I


sequence_source: UniProtKB P11444 canonical FASTA fetched 2026-05-25.

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(S)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'WT': Km = 17.74 mM, kcat = 0.99 s^(-1), kcat/Km = 56.34 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 17.74 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 17.74 mM. kcat: printed Table 2 cell 0.99 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 0.99 s^(-1). kcat/Km: printed Table 2 cell 56.34 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 56.34 / 1000 = 0.05634 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (S)-2-CMA half of the printed line for enzyme form WT: Km = 17.74 mM; kcat = 0.99 s^(-1); printed kcat/Km = 56.34 M^-1 s^-1.


organism: Escherichia coli

substrate_name: ITP

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

proof_lines:
pH 7.2, 30°C
Raw SKiD Env: Temp=30°C, pH=7.2

substrate: ITP


assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP


substrate_name: CTP

substrate: CTP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11444 FASTA; row-specific L93K reconstruction after confirming canonical residue L at position 93. and applied mutation signature L93K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11444 FASTA; row-specific L93W reconstruction after confirming canonical residue L at position 93. and applied mutation signature L93W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11444 FASTA; row-specific L93D reconstruction after confirming canonical residue L at position 93. and applied mutation signature L93D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P11444 FASTA; row-specific D270N reconstruction after confirming canonical residue D at position 270. and applied mutation signature D270N to reconstruct the assayed variant sequence.


organism: Saccharolobus solfataricus

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


substrate_name: dCTP

substrate: dCTP


substrate_name: dPTP

substrate: dPTP


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


substrate_name: fructose 6-phosphate

substrate: fructose 6-phosphate


organism: African swine fever virus (strain Badajoz 1971 Vero-adapted)

substrate_name: dGTP

substrate: dGTP


substrate_name: dATP

substrate: dATP


substrate_name: dTTP

substrate: dTTP


substrate_name: dGTP (insertion opposite abasic site)

substrate: dGTP (insertion opposite abasic site)