sequence_source: UniProtKB:A2QAN3 canonical sequence, direct lookup 2026-05-24, with selected-batch mutation signature W806S applied

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant W806S His6-tagged


enzyme_display_name: beta-galactosidase

organism: Aspergillus niger

substrate_name: Lactose; H2O

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

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

km_unit: mM

sequence_source: UniProtKB:A2QAN3 canonical sequence, direct lookup 2026-05-24, with selected-batch mutation signature Y304F/Y355H/N357G applied

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: beta-galactosidase(Enzyme) mutant Y304F/Y355H/N357G His6-tagged

enzyme: beta-galactosidase

substrate: Lactose; H2O


sequence_source: UniProtKB:A2QAN3 canonical sequence, direct lookup 2026-05-24, with selected-batch mutation signature Y304F applied

sequence_variant_note: Mutation signature Y304F matches the mutant residue at offset +0 and the reference residue at offset -10; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

mutation_type: substitution

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant Y304F His6-tagged


organism: Escherichia coli

substrate_name: H2O; o-Nitrophenyl beta-D-galactopyranoside 6-phosphate

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

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H540F


substrate_name: o-Nitrophenyl beta-D-galactopyranoside 6-phosphate; H2O

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H540N


substrate_name: H2O; o-Nitrophenyl-beta-D-galactoside

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H357F

substrate: H2O; o-Nitrophenyl-beta-D-galactoside


substrate_name: o-Nitrophenyl-beta-D-galactoside; H2O

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H357N

substrate: o-Nitrophenyl-beta-D-galactoside; H2O


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H357L


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H357D


organism: Homo sapiens

kcat_display: Not reported

mutation_signature: Unknown

sequence_source: UniProtKB:P16278 direct lookup 2026-05-24

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


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant I-cell disease


verification_status: unverified

sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 plus selected-source mutation signature E461K and applied mutation signature E461K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E461K

status: unverified


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 plus selected-source mutation signature E461Q and applied mutation signature E461Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E461Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 plus selected-source mutation signature E461D and applied mutation signature E461D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E461D


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 plus selected-source mutation signature E461G and applied mutation signature E461G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E461G


sequence_source: UniProtKB:P06864 canonical context only

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant psi epg0

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant epg a


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 plus selected-source mutation signature E461H and applied mutation signature E461H with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E461H


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00722 plus selected-source mutation signature H540E and applied mutation signature H540E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H540E

substrate: H2O; o-Nitrophenyl beta-D-galactopyranoside 6-phosphate


organism: Kluyveromyces lactis

sequence_source: UniProtKB:P00723 direct accession lookup (2026-05-24)


organism: Lactobacillus casei

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


organism: Lactobacillus delbrueckii subsp. bulgaricus

sequence_source: UniProtKB:P0C1Y0 direct accession lookup (2026-05-24)


sequence_source: UniProtKB:P0C1Y0 canonical sequence retained as context only (2026-05-24)

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0C1Y0 direct lookup plus L317F reconstruction (2026-05-24) and applied mutation signature L317F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant L317F


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant P429S


km_display: Not reported


sequence_source: UniProtKB:P00722 canonical sequence from REST lookup; context only, not a row-specific variant sequence

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant W999F


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant W999Y


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant G794A


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant D201E-


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant D201N-


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant D201F-


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

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant epg ab

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant epg_b

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant epg_a


substrate_name: p-Nitrophenyl-beta-D-galactoside; H2O

substrate: p-Nitrophenyl-beta-D-galactoside; H2O


organism: Bifidobacterium bifidum


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H391K


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H391E


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant H391F


substrate_name: H2O; p-Nitrophenyl-beta-D-galactoside

sequence_source: UniProtKB P00722 FASTA direct lookup on 2026-05-24; reviewed E. coli K-12 lacZ beta-galactosidase canonical sequence.

substrate: H2O; p-Nitrophenyl-beta-D-galactoside


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant W999G


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant W999L


enzyme_display_name: Beta-galactosidase

organism: Trichoderma reesei

sequence_source: UniProtKB Q70SY0 FASTA

unit: lgwedgeoneswedgeone

enzyme: Beta-galactosidase


sequence_source: UniProtKB A2QAN3 canonical sequence with UniProt mutagenesis feature Y304A applied; direct lookup 2026-05-24.

sequence_variant_note: Mutation signature Y304A matches the mutant residue at offset +0 and the reference residue at offset -10; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant Y304A His6-tagged


organism: Aspergillus oryzae

sequence_source: UniProtKB Q2UCU3 canonical sequence; direct lookup 2026-05-24.


organism: Bacillus coagulans

sequence_source: UniProtKB A0A1L1XWG1 canonical sequence; direct lookup 2026-05-24.


organism: Bacillus subtilis

sequence_source: UniProtKB O31529 canonical sequence with UniProt mutagenesis feature E145A applied; direct lookup 2026-05-24.

proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant E145A


sequence_source: UniProtKB O31529 canonical sequence; direct lookup 2026-05-24.


organism: Bacteroides ovatus

sequence_source: UniProtKB A7LXS9 canonical sequence; direct lookup 2026-05-24.


substrate_name: H2O; Lactose

substrate: H2O; Lactose


organism: Lactococcus lactis subsp. lactis


organism: Mus musculus


organism: Pantoea agglomerans

column_label: PMID 17336932 characterization paragraph, Bga/oNPGal segment, Km = 0.06 mM and Vmax = 0.43 mM/min.

raw_value_unit_evidence: The Km and Vmax values for oNPGal were calculated as 0.06 mM and 0.43 mM/min, respectively.

row_label: Bga beta-galactosidase with oNPGal substrate

table_label: Characterization of the enzyme paragraph


organism: Pediococcus pentosaceus


organism: Raphanus sativus


organism: Streptococcus thermophilus


organism: Sulfolobus solfataricus

verification_status: verified

column_label: Table label: Table 3. Kinetic constuntsfor S. solfataricus 8-galactosiduse (Wiley ePDF text layer; caption OCR-mangled from 'Kinetic constants for S. solfataricus beta-galactosidase'). Row: P-NpCal. Columns read: K m (mM) cell 0.225, k cat (min^-1) cell 5700, k cat / K m (min^-1 mM^-1) cell 25333. metric: Km; raw value: 0.225; raw unit: mM; normalized value: 0.225 mM; metric: kcat; raw value: 5700; raw unit: min^-1; normalized value: 95.0 s^(-1); assay condition: Purified Sulfolobus solfataricus beta-galactosidase; Km values determined by Lineweaver-Burk plots of data from assays carried out at 75 deg C for p-NpGal (this row's substrate), as described in Experimental Procedures.

normalized_value_unit_evidence: Table 3 row P-NpCal: Km 0.225 mM = 0.225 mM (already in export units); kcat 5700 min^-1 = 5700/60 = 95.0 s^(-1) (1 min^-1 = 1/60 s^-1), an exact conversion. In the ePDF text layer the Greek beta renders variously as '8', 'P' or 'B', the substrate o-nitrophenyl-beta-D-galactoside row is rendered 'P-NpCal' (paper's p-NpGal), the kcat column header renders as 'k,,,' with unit 'min-l', and the kcat/Km column header renders as 'k C a t i K ,' with unit 'min-' x mM-'.

raw_value_unit_evidence: Table 3. Kinetic constuntsfor S. solfataricus 8-galactosiduse (Wiley ePDF text layer; caption OCR-mangled from 'Kinetic constants for S. solfataricus beta-galactosidase') | metric header row: Substrate K , k,,, k C a t i K , | units row: mM min-l min-' x mM-' | row: P-NpCal 0.225 5700 25333 | cells read: K m = 0.225 mM; k cat = 5700 min^-1; k cat / K m = 25333 min^-1 mM^-1. In the ePDF text layer the Greek beta renders variously as '8', 'P' or 'B', the substrate o-nitrophenyl-beta-D-galactoside row is rendered 'P-NpCal' (paper's p-NpGal), the kcat column header renders as 'k,,,' with unit 'min-l', and the kcat/Km column header renders as 'k C a t i K ,' with unit 'min-' x mM-'.

row_label: P-NpCal

status: verified


organism: Rattus norvegicus


organism: Escherichia coli


organism: Homo sapiens


proof_lines: SABIO-RK modifier species: beta-galactosidase(Enzyme) mutant Lac- Gal d


organism: Oryctolagus cuniculus


organism: Pseudarthrobacter oxydans


enzyme_display_name: beta-lactamase

organism: Aeromonas hydrophila

substrate_name: H2O; Imipenem

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N116H/N220G

enzyme: beta-lactamase

substrate: H2O; Imipenem


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant N220G


organism: Enterobacter cloacae

substrate_name: H2O; Cefotaxime

sequence_source: UniProtKB:P05364 direct REST lookup on 2026-05-24

substrate: H2O; Cefotaxime


substrate_name: Nitrocefin; H2O

ki_unit: mM

sequence_source: UniProt REST exact accession lookup on 2026-05-24 for P13661

substrate: Nitrocefin; H2O


substrate_name: H2O; Cephaloridine

sequence_source: UniProt REST exact accession lookup on 2026-05-24 for P00811

substrate: H2O; Cephaloridine


substrate_name: H2O; Ampicillin

sequence_source: UniProtKB:P62593 direct accession lookup on 2026-05-24

substrate: H2O; Ampicillin


organism: Klebsiella pneumoniae

sequence_source: UniProtKB:C7C422 canonical sequence


organism: Serratia marcescens

substrate_name: Ampicillin; H2O

sequence_source: UniProtKB:P52699 canonical FASTA checked 2026-05-24

substrate: Ampicillin; H2O


organism: Shewanella algae

substrate_name: H2O; Penicillin G

sequence_source: UniProtKB:Q6VCW0 canonical FASTA checked 2026-05-24

substrate: H2O; Penicillin G


organism: Shewanella frigidimarina

substrate_name: H2O; Amoxicillin

sequence_source: UniProtKB:Q53BU0 canonical FASTA checked 2026-05-24

substrate: H2O; Amoxicillin


organism: Shewanella livingstonensis

substrate_name: Amoxicillin; H2O

sequence_source: UniProtKB:Q53BU1 canonical FASTA checked 2026-05-24

substrate: Amoxicillin; H2O


organism: Pseudomonas putida

sequence_source: UniProtKB direct lookup: https://rest.uniprot.org/uniprotkb/Q8GCU7.json (2026-05-24)


organism: Mycobacterium tuberculosis

substrate_name: H2O; Nitrocefin

substrate: H2O; Nitrocefin


organism: Pseudomonas aeruginosa

substrate_name: H2O; Carbenicillin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant R234K

substrate: H2O; Carbenicillin


substrate_name: Penicillin G; H2O

sequence_source: UniProtKB Q3SAW3 direct accession lookup, active entry accessed 2026-05-24

substrate: Penicillin G; H2O


organism: Stenotrophomonas maltophilia

sequence_source: UniProtKB:P52700 direct REST FASTA/JSON lookup


substrate_name: H2O; Biapenem

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120N

substrate: H2O; Biapenem


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120C


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant D120S


organism: Aeromonas sobria

substrate_name: Imipenem; H2O

substrate: Imipenem; H2O


substrate_name: Cefdinir; H2O

substrate: Cefdinir; H2O


substrate_name: H2O; Cefdinir

substrate: H2O; Cefdinir


enzyme_display_name: carboxylesterase

substrate_name: p-Nitrophenyl acetate; H2O

verification_status: corrected

column_label: Table 5. Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates. Enzyme block 'hCE-1'; substrate row 'pNPA'; column 'Km(uM)' = 27; column 'kcat(min-1)' = 1020; column 'kcat/Km(uM-1 min1)' = 38.

normalized_value_unit_evidence: Km: printed Table 5 cell 27 uM; 27 / 1000 = 0.027 mM; the exported value is 0.00000001105833 mM. kcat: printed Table 5 cell 1020 min^-1; 1020 / 60 = 17.0 s^(-1); the exported value is 17.0 s^(-1). kcat/Km: printed Table 5 cell 38 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 38 x 1000 / 60 = 633.3333333333334 s^-1 mM^-1; the catalog carries no catalytic-efficiency value for this row, so the printed cell is kept as paper evidence only.

raw_value_unit_evidence: Table 5, enzyme block 'hCE-1', substrate row 'pNPA': Km = 27 uM; kcat = 1020 min^-1; printed kcat/Km = 38 uM^-1 min^-1.

table_label: Table 5: Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates (Arch Biochem Biophys 2006;445(1):115-123)

enzyme: carboxylesterase

substrate: p-Nitrophenyl acetate; H2O

status: corrected


proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant p.Asp260fs


sequence_source: UniProtKB:P23141 with direct G143E substitution reconstruction

proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant p.Gly143Glu


organism: Lactobacillus casei

substrate_name: H2O; p-Nitrophenyl acetate

substrate: H2O; p-Nitrophenyl acetate


organism: Lactococcus lactis subsp. cremoris


substrate_name: Tripropionin; H2O

substrate: Tripropionin; H2O


substrate_name: H2O; 1-R,S-cis-Permethrin

substrate: H2O; 1-R,S-cis-Permethrin


substrate_name: p-Nitrophenyl butyrate; H2O

substrate: p-Nitrophenyl butyrate; H2O


organism: Actinidia eriantha

substrate_name: H2O; 4-Methylumbelliferyl acetate

sequence_source: UniProtKB:Q0ZPV7 direct accession lookup

substrate: H2O; 4-Methylumbelliferyl acetate


organism: Alicyclobacillus acidocaldarius

substrate_name: p-Nitrophenyl dodecanoate; H2O

sequence_source: UniProtKB:Q7M0L6 checked; 19-residue accession cannot validate residue-numbered variant

proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant M211S/R215L

substrate: p-Nitrophenyl dodecanoate; H2O


substrate_name: H2O; p-Nitrophenyl dodecanoate

proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant M211S

substrate: H2O; p-Nitrophenyl dodecanoate


proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant R215L


sequence_source: UniProtKB:Q7M0L6 checked; 19-residue accession not accepted as full enzyme sequence


substrate_name: Triacetin; H2O

sequence_source: UniProtKB:Q7SIG1 direct accession lookup

substrate: Triacetin; H2O


organism: Arabidopsis thaliana

substrate_name: H2O; Methyl indole-3-acetate

sequence_source: UniProtKB:Q9SG92 direct accession lookup

substrate: H2O; Methyl indole-3-acetate


organism: Archaeoglobus fulgidus

sequence_source: UniProtKB:O28558 direct accession lookup


substrate_name: H2O; p-Nitrophenyl butyrate

proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant chimer EstA-EstP

substrate: H2O; p-Nitrophenyl butyrate


proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant chimer EstP-EstA


organism: Rattus norvegicus

substrate_name: H2O; All-trans-Retinyl palmitate

substrate: H2O; All-trans-Retinyl palmitate


organism: Rhizomucor miehei


organism: Sus scrofa

substrate_name: H2O; 5'-L-Phenylalanyl-floxuridine

substrate: H2O; 5'-L-Phenylalanyl-floxuridine


organism: Thermomyces lanuginosus


organism: Aspergillus niger

sequence_source: UniProtKB accession Q6ED33 direct REST lookup


organism: Bacillus sp.

sequence_source: UniProtKB accession Q6DV85 direct REST lookup


sequence_source: UniProtKB accession Q6DV84 direct REST lookup


organism: Bacillus subtilis


organism: Cavia porcellus


organism: Escherichia coli


organism: Felis silvestris catus

sequence_source: UniProtKB accession Q8I034 direct REST lookup


organism: Geobacillus stearothermophilus

substrate_name: H2O; p-Nitrophenyl caproate

sequence_source: UniProtKB accession Q06174 direct REST lookup

substrate: H2O; p-Nitrophenyl caproate


substrate_name: p-Nitrophenyl caproate; H2O

proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant M211V

substrate: p-Nitrophenyl caproate; H2O


substrate_name: p-Nitrophenyl octanoate; H2O

substrate: p-Nitrophenyl octanoate; H2O


proof_lines: SABIO-RK modifier species: carboxylesterase(Enzyme) mutant M211T


substrate_name: H2O; p-Nitrophenyl octanoate

substrate: H2O; p-Nitrophenyl octanoate


organism: Geobacillus thermoleovorans

substrate_name: p-Nitrophenyl laurate; H2O

unit: moldivs

substrate: p-Nitrophenyl laurate; H2O


organism: Homo sapiens

substrate_name: Irinotecan; H2O

substrate: Irinotecan; H2O


substrate_name: H2O; Irinotecan

substrate: H2O; Irinotecan


substrate_name: Capecitabine; H2O

substrate: Capecitabine; H2O


substrate_name: H2O; Tripropionin

substrate: H2O; Tripropionin


substrate_name: p-Nitrophenyl acetate; H2O

substrate: p-Nitrophenyl acetate; H2O


organism: Salmo salar

substrate_name: H2O; Trioleoylglycerol

substrate: H2O; Trioleoylglycerol


organism: Fusarium solani


substrate_name: cis-Permethrin; H2O

substrate: cis-Permethrin; H2O


organism: Mus musculus

substrate_name: H2O; cis-Permethrin

substrate: H2O; cis-Permethrin


organism: Oncorhynchus mykiss


organism: Rattus norvegicus

substrate_name: H2O; trans-Permethrin

substrate: H2O; trans-Permethrin


organism: Vibrio vulnificus

sequence_source: UniProtKB reviewed accession Q8DF91


organism: Bacillus sp. (in: firmicutes)

substrate_name: D-fructose 6-phosphate

source_db: brenda

source_license: CC BY 4.0

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

data_origin: experimental

substrate: D-fructose 6-phosphate

source: brenda


enzyme_display_name: UniProt Q2FXM8

organism: Staphylococcus aureus

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q2FXM8

source: skid


organism: Saccharomyces cerevisiae

substrate_name: ATP

source_db: oed

kcat_over_km_origin: calculated

substrate: ATP

source: oed


substrate_name: D-Fructose 6-phosphate

substrate: D-Fructose 6-phosphate


enzyme_display_name: ATP-dependent 6-phosphofructokinase

organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)

source_db: uniprot

enzyme: ATP-dependent 6-phosphofructokinase

source: uniprot


substrate_name: GTP

substrate: GTP


substrate_name: ITP

substrate: ITP


substrate_name: UTP

substrate: UTP


substrate_name: CTP

substrate: CTP


substrate_name: fructose 6-phosphate

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

substrate: fructose 6-phosphate


organism: Bombus atratus

substrate_name: ATP; D-Fructose 6-phosphate

assay_conditions_summary: cofactor ATP

substrate: ATP; D-Fructose 6-phosphate


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP


organism: Dunaliella marina

substrate_name: D-Fructose 6-phosphate; ATP

substrate: D-Fructose 6-phosphate; ATP


assay_conditions_summary: pH 7; cofactor ATP


organism: Desulfurococcus amylolyticus


assay_conditions_summary: pH 6; 323.15 K; cofactor ATP


substrate_name: ADP

assay_conditions_summary: pH 6; 358.15 K; cofactor ADP

substrate: ADP


substrate_name: D-fructose 1,6-bisphosphate

substrate: D-fructose 1,6-bisphosphate


organism: Auxenochlorella pyrenoidosa


assay_conditions_summary: pH 7.7; cofactor ATP


organism: Trachemys scripta


assay_conditions_summary: pH 7; 279.15 K; cofactor ATP

proof_lines: pH 7.0, 20°C, normoxic and anoxic animals


proof_lines:
pH 7.0, 6°C, anoxic animals
pH 7.0, 20°C, normoxic animals
pH 7.0, 6°C, normoxic animals


organism: Kluyveromyces lactis


organism: Pichia pastoris


organism: Haloferax volcanii

assay_conditions_summary: pH 8; 315.15 K; cofactor ATP


organism: Austromegabalanus psittacus


organism: Pseudomonas doudoroffii

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant M-1


organism: Blastocladiella emersonii


organism: Monoraphidium minutum

assay_conditions_summary: pH 7.25; 298.15 K; cofactor ATP


organism: Zapus hudsonius


organism: Selenastrum minutum


enzyme_display_name: DNA-directed DNA polymerase

organism: [Bacillus] caldotenax

substrate_name: dNTP

enzyme: DNA-directed DNA polymerase

substrate: dNTP


enzyme_display_name: UniProt P19821

organism: Thermus aquaticus

substrate_name: dATP

enzyme: UniProt P19821

substrate: dATP


enzyme_display_name: UniProt P96022

organism: Saccharolobus solfataricus

substrate_name: dTTP

enzyme: UniProt P96022

substrate: dTTP


organism: Thermococcus kodakarensis

substrate_name: D-glucose

substrate: D-glucose


substrate_name: AMP

substrate: AMP


assay_conditions_summary: pH 7.5; 323.15 K; cofactor ADP


organism: Geobacillus stearothermophilus

sequence_source: multiple

assay_conditions_summary: pH 8.2; 303.15 K; cofactor ATP

source_databases_merged: brenda uniprot


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature G212V to reconstruct the assayed variant sequence.


substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


substrate_name: ATP

substrate: ATP


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

proof_lines:
pH 8.2, 30°C, native PFK
Raw SKiD Env: Temp=25°C, pH=8

source_databases_merged: brenda skid


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E190Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.2; cofactor ATP

proof_lines: mutant enzyme E190Q, in the presence of Mn2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication

proof_lines: mutant enzyme E190Q, in the presence of Mg2+, in 0.05 M Tris-HCl, pH 8.2, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession_plus_mutation_signature_reconstruction and applied mutation signature I153V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_plus_mutation_signature_reconstruction and applied mutation signature I150V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_plus_mutation_signature_reconstruction and applied mutation signature I234V 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.


substrate_name: dGTP

substrate: dGTP


substrate_name: dCTP

substrate: dCTP


organism: Saccharomyces cerevisiae

substrate_name: DNA; dGTP

substrate: DNA; dGTP


organism: Bacillus methanolicus

assay_conditions_summary: pH 9; 303.15 K; cofactor ATP

proof_lines:
strain PB1, Pfk2, pH 9.0, 30°C
strain MGA3, Pfk1, pH 9.0, 30°C
strain MGA3, Pfk2, pH 9.0, 30°C


proof_lines:
strain PB1, Pfk2, pH 9.0, 30°C
strain MGA3, Pfk2, pH 9.0, 30°C
strain MGA3, Pfk1, pH 9.0, 30°C


organism: Abax parallelepipedus


organism: Tequatrovirus T4

substrate_name: Unknown

substrate: Unknown


assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP

proof_lines: pH 7.2, 30°C, cosubstrate gamma-thio-ATP


proof_lines:
pH 7.2, 30°C, cosubstrate ATP
pH 7.2, 30°C, at 2mM ATP
Raw SKiD Env: Temp=30°C, pH=7.2


organism: Homo sapiens

assay_conditions_summary: pH 7.1; 298.15 K; cofactor ATP

proof_lines: wild-type, presence of 5 mM AMP, pH 7.1, 25°C


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

proof_lines: N-terminal truncation mutant, presence of 5 mM AMP, pH 7.1, 25°C


organism: Staphylococcus aureus


sequence_variant_note: Resolved canonical sequence from canonical_uniprot_q2fxm8_plus_g150d_l151a_reconstruction and applied mutation signature G150D/L151A to reconstruct the assayed variant sequence.


organism: Aeropyrum pernix

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

assay_conditions_summary: pH 6.5; 368.15 K; cofactor ATP

proof_lines:
pH 6.5, 95°C, discontinuous assay
pH 6.7, 85°C


assay_conditions_summary: pH 7.2; 298.15 K; cofactor ATP

proof_lines: pH 7.2, 25°C, red blood cell lysate from diabetic subjects as source of enzyme


proof_lines: pH 7.2, 25°C, red blood cell lysate as source of enzyme


proof_lines: pH 7.2, 30°C, cosubstrate fructose 1-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D127S with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 6.7; 358.15 K; cofactor ATP

proof_lines:
pH 6.7, 85°C
pH 6.5, 95°C, discontinuous assay


proof_lines: in the presence of 0.5 mM MgATP2-, at pH 8.2 and 25°C

proof_lines: in the presence of 0.1 mM MgATP2-, at pH 8.2 and 25°C


organism: Fasciola hepatica

assay_conditions_summary: pH 8

proof_lines:
pH 8.0, native PFK
pH 8.0, phosphorylated PFK


proof_lines: pH 7.5, 37°C, dNTP incorporation opposite DNA lesions, template base: G

proof_lines: pH 7.5, 37°C, dNTP incorporation opposite DNA lesions, template base: O6-BzG


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 = Dpo3; dNTP column = C (dCTP); column 'Km (uM)' = 75 +/- 13; column 'kcat (min^-1)' = 0.00053 +/- 0.00006; column 'kcat/Km (min^-1 uM^-1)' = 7.1 x 10^-6; column 'fins' = 1.

normalized_value_unit_evidence: Km: printed TABLE 2 cell 75 uM; 75 / 1000 = 0.075 mM. kcat: printed TABLE 2 cell 0.00053 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 0.00053 / 60 = 0.000008833333333333332 s^-1. kcat/Km: printed TABLE 2 cell 7.1 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 0.000007099999999999999 x 1000 / 60 = 0.00011833333333333333 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 2, Polymerase Dpo3, dNTP row C (dCTP): Km = 75 uM; kcat = 0.00053 min^-1; printed kcat/Km = 7.1 x 10^-6 min^-1 uM^-1.

row_label: TABLE 2, Polymerase block 'Dpo3', dNTP row 'C' (incoming nucleotide dCTP), 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)


column_label: TABLE 2 (Steady-state kinetics of dNTP incorporation opposite G by Dpo 1, Dpo2, Dpo3, and Dpo4); Polymerase column = Dpo1; dNTP column = A (dATP); column 'Km (uM)' = 2100 +/- 1300; column 'kcat (min^-1)' = 0.0018 +/- 0.0004; column 'kcat/Km (min^-1 uM^-1)' = 8.6 x 10^-7; column 'fins' = 3.2 x 10^-5.

normalized_value_unit_evidence: Km: printed TABLE 2 cell 2100 uM; 2100 / 1000 = 2.1 mM. kcat: printed TABLE 2 cell 0.0018 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 0.0018 / 60 = 0.000029999999999999997 s^-1. kcat/Km: printed TABLE 2 cell 8.6 x 10^-7 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 0.0000008599999999999999 x 1000 / 60 = 0.000014333333333333332 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 2, Polymerase Dpo1, dNTP row A (dATP): Km = 2100 uM; kcat = 0.0018 min^-1; printed kcat/Km = 8.6 x 10^-7 min^-1 uM^-1.

row_label: TABLE 2, Polymerase block 'Dpo1', dNTP row 'A' (incoming nucleotide dATP), insertion opposite template G


column_label: TABLE 2 (Steady-state kinetics of dNTP incorporation opposite G by Dpo 1, Dpo2, Dpo3, and Dpo4); Polymerase column = Dpo1; dNTP column = C (dCTP); column 'Km (uM)' = 8.4 +/- 0.7; column 'kcat (min^-1)' = 0.23 +/- 0.004; column 'kcat/Km (min^-1 uM^-1)' = 2.7 x 10^-2; column 'fins' = 1.

normalized_value_unit_evidence: Km: printed TABLE 2 cell 8.4 uM; 8.4 / 1000 = 0.0084 mM. kcat: printed TABLE 2 cell 0.23 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 0.23 / 60 = 0.0038333333333333336 s^-1. kcat/Km: printed TABLE 2 cell 2.7 x 10^-2 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 0.027000000000000003 x 1000 / 60 = 0.45000000000000007 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 2, Polymerase Dpo1, dNTP row C (dCTP): Km = 8.4 uM; kcat = 0.23 min^-1; printed kcat/Km = 2.7 x 10^-2 min^-1 uM^-1.

row_label: TABLE 2, Polymerase block 'Dpo1', dNTP row 'C' (incoming nucleotide dCTP), insertion opposite template G


column_label: TABLE 2 (Steady-state kinetics of dNTP incorporation opposite G by Dpo 1, Dpo2, Dpo3, and Dpo4); Polymerase column = Dpo1; dNTP column = G (dGTP); column 'Km (uM)' = 2500 +/- 900; column 'kcat (min^-1)' = 0.0068 +/- 0.0011; column 'kcat/Km (min^-1 uM^-1)' = 2.7 x 10^-6; column 'fins' = 1.0 x 10^-4.

normalized_value_unit_evidence: Km: printed TABLE 2 cell 2500 uM; 2500 / 1000 = 2.5 mM. kcat: printed TABLE 2 cell 0.0068 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 0.0068 / 60 = 0.00011333333333333333 s^-1. kcat/Km: printed TABLE 2 cell 2.7 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 0.0000027 x 1000 / 60 = 0.000045 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 2, Polymerase Dpo1, dNTP row G (dGTP): Km = 2500 uM; kcat = 0.0068 min^-1; printed kcat/Km = 2.7 x 10^-6 min^-1 uM^-1.

row_label: TABLE 2, Polymerase block 'Dpo1', dNTP row 'G' (incoming nucleotide dGTP), insertion opposite template G


column_label: TABLE 2 (Steady-state kinetics of dNTP incorporation opposite G by Dpo 1, Dpo2, Dpo3, and Dpo4); Polymerase column = Dpo3; dNTP column = T (dTTP); column 'Km (uM)' = 930 +/- 160; column 'kcat (min^-1)' = 0.00011 +/- 0.00001; column 'kcat/Km (min^-1 uM^-1)' = 1.2 x 10^-7; column 'fins' = 1.7 x 10^-2.

normalized_value_unit_evidence: Km: printed TABLE 2 cell 930 uM; 930 / 1000 = 0.93 mM. kcat: printed TABLE 2 cell 0.00011 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 0.00011 / 60 = 0.0000018333333333333333 s^-1. kcat/Km: printed TABLE 2 cell 1.2 x 10^-7 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 0.00000012 x 1000 / 60 = 0.000002 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 2, Polymerase Dpo3, dNTP row T (dTTP): Km = 930 uM; kcat = 0.00011 min^-1; printed kcat/Km = 1.2 x 10^-7 min^-1 uM^-1.

row_label: TABLE 2, Polymerase block 'Dpo3', dNTP row 'T' (incoming nucleotide dTTP), insertion opposite template G


column_label: TABLE 2 (Steady-state kinetics of dNTP incorporation opposite G by Dpo 1, Dpo2, Dpo3, and Dpo4); Polymerase column = Dpo1; dNTP column = T (dTTP); column 'Km (uM)' = 3100 +/- 600; column 'kcat (min^-1)' = 0.096 +/- 0.008; column 'kcat/Km (min^-1 uM^-1)' = 3.1 x 10^-5; column 'fins' = 1.1 x 10^-3.

normalized_value_unit_evidence: Km: printed TABLE 2 cell 3100 uM; 3100 / 1000 = 3.1 mM. kcat: printed TABLE 2 cell 0.096 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 0.096 / 60 = 0.0016 s^-1. kcat/Km: printed TABLE 2 cell 3.1 x 10^-5 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 0.000031 x 1000 / 60 = 0.0005166666666666667 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 2, Polymerase Dpo1, dNTP row T (dTTP): Km = 3100 uM; kcat = 0.096 min^-1; printed kcat/Km = 3.1 x 10^-5 min^-1 uM^-1.

row_label: TABLE 2, Polymerase block 'Dpo1', dNTP row 'T' (incoming nucleotide dTTP), insertion opposite template G


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: 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: 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


mutation_type: insertion

proof_lines: pH 7.5, 37°C, dTTP insertion opposite the N6dA-butanetriol in 5-TCTC-N6dA-butanetriol-GTTTATGGACCACC-3


proof_lines: pH 7.5, 37°C, dTTP insertion opposite the N6dA-(OH)2butyl-GSH in 5-TCTC-N6dA-(OH)2butyl-GSH-GTTTATGGACCACC-3


proof_lines: pH 7.5, 37°C, dTTP insertion opposite an unmodified deoxyadenosine in 5-TCTCAGTTTATGGACCACC-3


proof_lines: pH 7.5, 37°C, dCTP insertion opposite the N6dA-(OH)2butyl-GSH in 5-TCTC-N6dA-(OH)2butyl-GSH-GTTTATGGACCACC-3


proof_lines: pH 7.5, 37°C, dCTP insertion opposite the N6dA-butanetriol in 5-TCTC-N6dA-butanetriol-GTTTATGGACCACC-3


proof_lines: pH 7.5, 37°C, dCTP insertion opposite an unmodified deoxyadenosine in 5-TCTCAGTTTATGGACCACC-3


organism: Klebsiella aerogenes

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: pH 8.0, 25, at a Mg2+/ATP ratio of 1.4/1

proof_lines: pH 8.0, 25, at a Mg2+/ATP ratio of 0.7/1


mutation_signature: PMCID:PMC2754150. The full-text sidecar places these Dpo4 rows in steady-state individual-dNTP insertion assays opposite MeFapy-dGuo lesions or unmodified dGuo

proof_lines: pH 7.8, 37°C, dATP insertion opposite N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine in 5-TCAT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimi

proof_lines: pH 7.8, 37°C, dATP insertion opposite N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine in 5-TCGT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimi


proof_lines: pH 7.8, 37°C, dCTP insertion opposite an unmodified deoxyguanosine in 5-TCAT-G-GAATCCTTACGAGCATCGCCCCC-3


proof_lines: pH 7.8, 37°C, dATP insertion opposite an unmodified deoxyguanosine in 5-TCAT-G-GAATCCTTACGAGCATCGCCCCC-3


proof_lines: pH 7.8, 37°C, dCTP insertion opposite N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine in 5-TCAT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimi

proof_lines: pH 7.8, 37°C, dCTP insertion opposite N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine in 5-TCGT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimi


proof_lines: pH 7.8, 37°C, dTTP insertion opposite N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine in 5-TCAT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimi


proof_lines: pH 7.8, 37°C, dCTP insertion opposite an unmodified deoxyguanosine in 5-TCGT-G-TCAATCCTTACGAGCATCGCCCCC-3


proof_lines: pH 7.8, 37°C, dGTP insertion opposite an unmodified deoxyguanosine in 5-TCAT-G-GAATCCTTACGAGCATCGCCCCC-3


proof_lines: pH 7.8, 37°C, dATP insertion opposite an unmodified deoxyguanosine in 5-TCGT-G-TCAATCCTTACGAGCATCGCCCCC-3


proof_lines: pH 7.8, 37°C, dTTP insertion opposite an unmodified deoxyguanosine in 5-TCAT-G-GAATCCTTACGAGCATCGCCCCC-3


proof_lines: pH 7.8, 37°C, dGTP insertion opposite N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine in 5-TCAT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimi


proof_lines: pH 7.8, 37°C, dGTP insertion opposite the N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine lesion in 5-TCAT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylform


proof_lines: pH 7.8, 37°C, dGCTP insertion opposite an unmodified deoxyguanosine in 5-TCAT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine)-GAATCCTTACGAGCATCGCCCCC-3


proof_lines: pH 7.8, 37°C, dTTP insertion opposite an unmodified deoxyguanosine in 5-TCAT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine)-GAATCCTTACGAGCATCGCCCCC-3


proof_lines: pH 7.8, 37°C, dATP insertion opposite the N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine lesion in 5-TCAT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylform

proof_lines: pH 7.8, 37°C, dATP insertion opposite the N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine lesion in 5-TCGT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylform


proof_lines: pH 7.8, 37°C, dTTP insertion opposite the N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine lesion in 5-TCAT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylform


proof_lines: pH 7.8, 37°C, dCTP insertion opposite the N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine lesion in 5-TCGT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylform

proof_lines: pH 7.8, 37°C, dCTP insertion opposite the N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine lesion in 5-TCAT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylform


proof_lines: pH 7.8, 37°C, dCTP insertion opposite an unmodified deoxyguanosine in 5-TCAT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine)-GAATCCTTACGAGCATCGCCCCC-3


proof_lines: pH 7.8, 37°C, dATP insertion opposite an unmodified deoxyguanosine in 5-TCAT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine)-GAATCCTTACGAGCATCGCCCCC-3


proof_lines: pH 7.8, 37°C, dGTP insertion opposite an unmodified deoxyguanosine in 5-TCAT-(N6-(2-deoxy-D-erythro-pentofuranosyl)-2,6-diamino-3,4-dihydro-4-oxo-5-N-methylformamidopyrimidine)-GAATCCTTACGAGCATCGCCCCC-3


organism: Arabidopsis thaliana

substrate_name: dATP (with cytosine as template)

proof_lines: With cytosine as template, kcat is 0.024 min(-1) with dATP as substrate, kcat is 0.125 min(-1) with dGTP as substrate, kcat is 0.057 min(-1) with dATTP as substrate and kcat is 0.0038 min(-1) with dCTP as substrate. With thymine as template

substrate: dATP (with cytosine as template)


substrate_name: dGTP (with cytosine as template)

substrate: dGTP (with cytosine as template)


substrate_name: dTTP (with cytosine as template)

substrate: dTTP (with cytosine as template)


substrate_name: dCTP (with cytosine as template)

substrate: dCTP (with cytosine as template)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T239W to reconstruct the assayed variant sequence.

proof_lines: PMID 18984592 Table 1: Dpo4 T239W, dCTP opposite template G, pH 7.4 at 37 C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N188W to reconstruct the assayed variant sequence.

proof_lines: PMID 18984592 Table 1: Dpo4 N188W, dCTP opposite template G, pH 7.4 at 37 C


organism: Trypanosoma brucei

assay_conditions_summary: pH 6.7; 310.15 K; cofactor ATP

proof_lines: pH 6.7, 37°C, at 2.0 mM fructose 6-phosphate

proof_lines: pH 6.7, 37°C, at 0.4 mM fructose 6-phosphate

proof_lines: pH 6.7, 37°C, at 0.25 mM fructose 6-phosphate


substrate_name: dATP (for Pol-zeta2)

proof_lines: kcat is 0.31 min(-1) for DNA synthesis by Pol-zeta4. kcat is 0.05 min(-1) for DNA synthesis by Pol-zeta2.

substrate: dATP (for Pol-zeta2)


substrate_name: D-Fructose 6-phosphate; ATP

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

substrate: D-Fructose 6-phosphate; ATP


organism: Amycolatopsis methanolica

assay_conditions_summary: cofactor ATP


organism: Bacillus licheniformis

assay_conditions_summary: pH 6.8; 303.15 K; cofactor ATP


organism: Bacillus macquariensis


organism: Dictyostelium discoideum


substrate_name: ATP; D-Fructose 6-phosphate

substrate: ATP; D-Fructose 6-phosphate


organism: Thermus aquaticus

substrate_name: dADP

proof_lines: pH and temperature not specified in the publication

substrate: dADP


organism: Escherichia coli


organism: Geobacillus stearothermophilus


organism: Lactobacillus delbrueckii subsp. bulgaricus


organism: Pyrococcus furiosus

substrate_name: dATP

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A408S to reconstruct the assayed variant sequence.

proof_lines: 55°C, pH not specified in the publication, mutant enzyme A408S

substrate: dATP


organism: Danio rerio

substrate_name: dTTP

proof_lines: pH 8.8, 30°C, recombinant enzyme, in presence of Mn2+

proof_lines: pH 8.8, 30°C, recombinant enzyme, in presence of Mg2+

substrate: dTTP


organism: Saccharolobus solfataricus

proof_lines: pH 7.5, 37°C, dNTP incorporation opposite DNA lesions, template base: N2-MeG

proof_lines: pH 7.5, 37°C, dNTP incorporation opposite DNA lesions, template: abasic site

proof_lines: pH 7.5, 37°C, dNTP incorporation opposite DNA lesions, template base: G


proof_lines: pH 7.4, 37°C, steady-state kinetics for single nucleotide primer extension with O6-methylguanine as template

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


proof_lines: pH 7.8, 37°C, incorporation of dCTP opposite (8oxoG) in the double stranded oligonucleotide: 5-GGGGGAAGGATTC-3/3-CCCCCTTCCTAAG(8oxoG)CACT-5


proof_lines: pH 7.5, 60°C, incorporation opposite the 3-thymine of an nondamaged template

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

proof_lines: pH 7.5, 60°C, incorporation opposite the 3-thymine of a cis-syn thymine dimer of the template


organism: Lactobacillus plantarum


organism: Lactococcus lactis subsp. lactis


organism: Leishmania donovani


organism: Mus musculus


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Oryctolagus cuniculus


organism: Rattus norvegicus


organism: Saccharomyces cerevisiae


organism: Thermus thermophilus

proof_lines: Full-text M1polWT dTTP kinetic extract: Km 230 +/- 70 uM, kcat 1.0 +/- 0.2 s-1; buffer B pH 8.2 at 50 C.


enzyme_display_name: hexokinase

organism: Bos taurus

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

enzyme: hexokinase


enzyme_display_name: UniProt P19367

organism: Homo sapiens

substrate_name: D-glucose

enzyme: UniProt P19367

substrate: D-glucose


proof_lines:
Raw SKiD Env: Temp=25°C, pH=-----
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=7.5


organism: Schistosoma mansoni


organism: Schizosaccharomyces pombe


organism: Spinacia oleracea


organism: Streptococcus thermophilus


organism: Streptomyces coelicolor


organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)


organism: Thermococcus thioreducens

substrate_name: DNAn

substrate: DNAn


organism: Xenotropic MuLV-related virus (isolate VP62)

substrate_name: RNA/DNA duplex

substrate: RNA/DNA duplex


organism: Thermotoga maritima


organism: Trypanosoma brucei brucei


organism: Trypanosoma cruzi


organism: Ustilago maydis


organism: Bacillus subtilis


organism: Bacteriophage T4

substrate_name: Deoxynucleoside triphosphate; DNA

substrate: Deoxynucleoside triphosphate; DNA


organism: Enterobacteria phage PRD1

substrate_name: deoxynucleoside triphosphate

substrate: deoxynucleoside triphosphate


organism: Escherichia coli

substrate_name: H2O; DNA

substrate: H2O; DNA


organism: Homo sapiens

substrate_name: DNA; dATP

substrate: DNA; dATP


organism: Aspergillus niger

assay_conditions_summary: pH 7.8; cofactor ATP

proof_lines: pH 7.8, in presence of 5 mM Mg2+, native enzyme form


organism: Dictyostelium discoideum

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R82E with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant R82E


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R77A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant R77A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R77D with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant R77D


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R77L with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant R77L


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R77E with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant R77E


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R82A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant R82A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Δ311 to reconstruct the assayed variant sequence.

mutation_type: deletion

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) wildtype delta311-319


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant D127S


sequence_variant_note: Mutation signature T125S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant Thr125Ser


organism: Fasciola hepatica

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

proof_lines:
pH 8.0, native PFK
pH 8.0, phosphorylated PFK


organism: Brugia malayi

substrate_name: D-Glucose; ATP

sequence_source: UniProtKB direct lookup of Q56VN6 on 2026-05-25; active primary accession A0A0K0JFP3 / HXK_BRUMA.

substrate: D-Glucose; ATP


substrate_name: ATP

substrate: ATP


substrate_name: D-fructose

substrate: D-fructose


organism: Mus musculus

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


organism: Rattus norvegicus


substrate_name: alpha-D-Glucose 6-phosphate; ADP

assay_conditions_summary: cofactor ADP

substrate: alpha-D-Glucose 6-phosphate; ADP


substrate_name: alpha-D-Glucose; ATP

substrate: alpha-D-Glucose; ATP


substrate_name: ATP; alpha-D-Glucose

substrate: ATP; alpha-D-Glucose


organism: Saccharomyces cerevisiae


substrate_name: D-Hexose; ATP

substrate: D-Hexose; ATP


organism: Bubalus bubalis


assay_conditions_summary: pH 8.1; 303.15 K; cofactor ATP


substrate_name: D-glucosamine

substrate: D-glucosamine


substrate_name: Unknown

proof_lines:
versus MgATP2-, at 30°C, pH 8.1
versus glucose, at 30°C, pH 8.1
at 30°C, pH 8.1

substrate: Unknown


organism: Mammalia

proof_lines:
type I isozyme
type III isozyme
type II isozyme


proof_lines:
type III isozyme
type II isozyme
type I isozyme


proof_lines:
type I and type II isozymes
type III isozyme


organism: Catharanthus roseus


substrate_name: UTP

substrate: UTP


organism: Aeropyrum pernix

substrate_name: D-mannose

assay_conditions_summary: pH 6.2; 363.15 K; cofactor ATP

substrate: D-mannose


organism: Brassica rapa subsp. oleifera

proof_lines:
isozyme HKI
isozyme HKII


substrate_name: D-glucose

substrate: D-glucose


organism: Lithobates sylvaticus

assay_conditions_summary: pH 8.2; 278.15 K; cofactor ATP

proof_lines:
control, pH 8.2, 5°C, no glucose
frozen, pH 8.2, 25°C
frozen, pH 8.2, 25°C, no glucose


proof_lines:
frozen, pH 8.2, 5°C, no glucose
control, pH 8.2, 25°C
control, pH 8.2, 25°C, no glucose


organism: Littorina littorea

proof_lines: enzyme from hepatopancreas, 24 h anoxic conditions, pH 7.5, 22°C

proof_lines: enzyme from hepatopancreas, pH 7.5, 22°C

proof_lines: enzyme from foot muscle, 24 h anoxic conditions, pH 7.5, 22°C


assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP


organism: Ogataea angusta

assay_conditions_summary: pH 7.5; cofactor ATP


organism: Thermus thermophilus


organism: Asterias amurensis


organism: Urocitellus undulatus

proof_lines: enzyme from hibernating animals, S0.5 value, Hill coefficient 1.2, pH 7.8, 2°C

proof_lines: enzyme from active animals, S0.5 value, Hill coefficient 1.16, pH 7.8, 2°C

proof_lines: enzyme from hibernating animals, S0.5 value, Hill coefficient 1.6, pH 7.8, 25°C


organism: Homo sapiens

mutation_signature: deletion mutant lacking residues 70-71

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

proof_lines: deletion mutant lacking residues 70-71, pH 7.6, 25 °C

proof_lines: deletion mutant lacking residues 70-71, K0.5 value, Hill coefficient 1.3, pH 7.6, 25 °C


mutation_signature: deletion mutant lacking residue 71

proof_lines: deletion mutant lacking residue 71, pH 7.6, 25 °C

proof_lines: deletion mutant lacking residue 71, K0.5 value, Hill coefficient 1.5, pH 7.6, 25 °C


mutation_signature: deletion mutant lacking residues 66-71

proof_lines: deletion mutant lacking residues 66-71, pH 7.6, 25 °C

proof_lines: deletion mutant lacking residues 66-71, K0.5 value, Hill coefficient 1.2, pH 7.6, 25 °C


mutation_signature: deletion mutant lacking residues 68-71

proof_lines: deletion mutant lacking residues 68-71, pH 7.6, 25 °C

proof_lines: deletion mutant lacking residues 68-71, K0.5 value, Hill coefficient 1.2, pH 7.6, 25 °C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S64R/E67D/S69T to reconstruct the assayed variant sequence.

proof_lines: mutant S64R/E67D/S69T, K0.5 value, Hill coefficient 1.7, pH 7.6, 25 °C


mutation_signature: deletion mutant lacking residues 67-71

proof_lines: deletion mutant lacking residues 67-71, pH 7.6, 25 °C

proof_lines: deletion mutant lacking residues 67-71, K0.5 value, Hill coefficient 1.1, pH 7.6, 25 °C


assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35557 and applied mutation signature V62E to reconstruct the assayed variant sequence.

column_label: Table I: Mutational Analysis of the V62 GKA binding site (J. Biol. Chem. 2005, volume 280, number 14, pages 14105-14113; journal page 14108, PDF page 4), printed parameter column heads Yield (mg/liter), Protein concentration (mg/ml), kcat (s^-1), Glucose S0.5 (mM), ATP Km (mM), nH, GIa and EC50 for RO0274377 (uM); the article prints no catalytic-efficiency column in this table. Journal page 14108 (PDF page 4). Table I, mutant row V62E, row mean of two independent expressions; column kcat (s^-1) cell = 4.92; column ATP Km (mM) cell = 0.07. captured primary segment: Table I, mutant row V62E, row mean of two independent expressions | construct V62E GST-GCK | substrate ATP | condition kinetic analysis of the purified GST fusion enzyme, no assay pH or temperature printed for Table I | kcat 4.92 s^-1 | ATP Km 0.07 mM

normalized_value_unit_evidence: kcat: printed Table I kcat cell 4.92 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 4.92 s^(-1). Km: printed Table I ATP Km cell 0.07 mM; the printed column is already in millimolar, so no unit conversion applies and the value is 0.07 mM. kcat/Km: the exported efficiency is the quotient of those two printed cells of this one measurement, 4.92 / 0.07 = 70.28571428571428 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 14108, Table I, mutant row V62E, row mean of two independent expressions: kcat = 4.92 s^-1; ATP Km = 0.07 mM. Table I carries no catalytic-efficiency column.

row_label: Table I, mutant row V62E, row mean of two independent expressions; the cited cells are the mean of the two independent expressions of this mutant


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35557 and applied mutation signature V62T to reconstruct the assayed variant sequence.

column_label: Table I: Mutational Analysis of the V62 GKA binding site (J. Biol. Chem. 2005, volume 280, number 14, pages 14105-14113; journal page 14108, PDF page 4), printed parameter column heads Yield (mg/liter), Protein concentration (mg/ml), kcat (s^-1), Glucose S0.5 (mM), ATP Km (mM), nH, GIa and EC50 for RO0274377 (uM); the article prints no catalytic-efficiency column in this table. Journal page 14108 (PDF page 4). Table I, mutant row V62T, row mean of two independent expressions; column kcat (s^-1) cell = 25.7; column ATP Km (mM) cell = 0.22. captured primary segment: Table I, mutant row V62T, row mean of two independent expressions | construct V62T GST-GCK | substrate ATP | condition kinetic analysis of the purified GST fusion enzyme, no assay pH or temperature printed for Table I | kcat 25.7 s^-1 | ATP Km 0.22 mM

normalized_value_unit_evidence: kcat: printed Table I kcat cell 25.7 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 25.7 s^(-1). Km: printed Table I ATP Km cell 0.22 mM; the printed column is already in millimolar, so no unit conversion applies and the value is 0.22 mM. kcat/Km: the exported efficiency is the quotient of those two printed cells of this one measurement, 25.7 / 0.22 = 116.81818181818181 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 14108, Table I, mutant row V62T, row mean of two independent expressions: kcat = 25.7 s^-1; ATP Km = 0.22 mM. Table I carries no catalytic-efficiency column.

row_label: Table I, mutant row V62T, row mean of two independent expressions; the cited cells are the mean of the two independent expressions of this mutant


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V62M with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35557 and applied mutation signature V62L to reconstruct the assayed variant sequence.

column_label: Table I: Mutational Analysis of the V62 GKA binding site (J. Biol. Chem. 2005, volume 280, number 14, pages 14105-14113; journal page 14108, PDF page 4), printed parameter column heads Yield (mg/liter), Protein concentration (mg/ml), kcat (s^-1), Glucose S0.5 (mM), ATP Km (mM), nH, GIa and EC50 for RO0274377 (uM); the article prints no catalytic-efficiency column in this table. Journal page 14108 (PDF page 4). Table I, mutant row V62L, row mean of two independent expressions; column kcat (s^-1) cell = 59.9; column ATP Km (mM) cell = 0.61. captured primary segment: Table I, mutant row V62L, row mean of two independent expressions | construct V62L GST-GCK | substrate ATP | condition kinetic analysis of the purified GST fusion enzyme, no assay pH or temperature printed for Table I | kcat 59.9 s^-1 | ATP Km 0.61 mM

normalized_value_unit_evidence: kcat: printed Table I kcat cell 59.9 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 59.9 s^(-1). Km: printed Table I ATP Km cell 0.61 mM; the printed column is already in millimolar, so no unit conversion applies and the value is 0.61 mM. kcat/Km: the exported efficiency is the quotient of those two printed cells of this one measurement, 59.9 / 0.61 = 98.19672131147541 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 14108, Table I, mutant row V62L, row mean of two independent expressions: kcat = 59.9 s^-1; ATP Km = 0.61 mM. Table I carries no catalytic-efficiency column.

row_label: Table I, mutant row V62L, row mean of two independent expressions; the cited cells are the mean of the two independent expressions of this mutant


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V62A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V62F with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V62K with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 7.5; 323.15 K; cofactor ATP

proof_lines: pH 7.5, 50°C, D-glucose as phosphoryl acceptor


proof_lines:
pH 7.5, 50°C, ATP as phosphoryl donor
pH 7.5, 50°C
Raw SKiD Env: Temp=50°C, pH=7.5


substrate_name: N-acetyl-D-glucosamine

substrate: N-acetyl-D-glucosamine


substrate_name: CTP

substrate: CTP


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature Y214A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.1; cofactor ATP

column_label: Table 1; row label: Y214A; column label: kcat (sec^-1); raw value: 117.0; raw unit: sec^-1; normalized value: 117.0; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 117.0; normalized unit: s^-1

raw_value_unit_evidence: raw value: 117 (123, 111); raw unit: sec^-1

table_label: Table 1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature C213R to reconstruct the assayed variant sequence.

column_label: Table 1; row label: C213R; column label: kcat (sec^-1); raw value: 50.0; raw unit: sec^-1; normalized value: 50.0; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 50.0; normalized unit: s^-1

raw_value_unit_evidence: raw value: 50.0; raw unit: sec^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature M197E to reconstruct the assayed variant sequence.

column_label: Table 1; row label: M197E; column label: kcat (sec^-1); raw value: 17.7; raw unit: sec^-1; normalized value: 17.7; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 17.7; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature K414E to reconstruct the assayed variant sequence.

column_label: Table 1; row label: K414E; column label: kcat (sec^-1); raw value: 19.9; raw unit: sec^-1; normalized value: 19.9; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 19.9; normalized unit: s^-1

raw_value_unit_evidence: raw value: 19.9; raw unit: sec^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature Y215A to reconstruct the assayed variant sequence.

column_label: Table 1; row label: Y215A; column label: kcat (sec^-1); raw value: 44.7; raw unit: sec^-1; normalized value: 44.7; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 44.7; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature K140E to reconstruct the assayed variant sequence.

column_label: Table 1; row label: K140E; column label: kcat (sec^-1); raw value: 40.0; raw unit: sec^-1; normalized value: 40.0; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 40.0; normalized unit: s^-1

raw_value_unit_evidence: raw value: 40.0±1.36; raw unit: sec^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature C252Y to reconstruct the assayed variant sequence.

column_label: Table 1; row label: C252Y; column label: kcat (sec^-1); raw value: 29.3; raw unit: sec^-1; normalized value: 29.3; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 29.3; normalized unit: s^-1

raw_value_unit_evidence: raw value: 29.3; raw unit: sec^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature V452L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: V452L; column label: kcat (sec^-1); raw value: 122.0; raw unit: sec^-1; normalized value: 122.0; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 122.0; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature P417R to reconstruct the assayed variant sequence.

column_label: Table 1; row label: P417R; column label: kcat (sec^-1); raw value: 48.3; raw unit: sec^-1; normalized value: 48.3; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 48.3; normalized unit: s^-1

raw_value_unit_evidence: raw value: 48.3±7.40; raw unit: sec^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature T65I to reconstruct the assayed variant sequence.

column_label: Table 1; row label: T65I; column label: kcat (sec^-1); raw value: 22.6; raw unit: sec^-1; normalized value: 22.6; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 22.6; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature S263P to reconstruct the assayed variant sequence.

column_label: Table 1; row label: S263P; column label: kcat (sec^-1); raw value: 44.6; raw unit: sec^-1; normalized value: 44.6; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 44.6; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature S64Y to reconstruct the assayed variant sequence.

column_label: Table 1; row label: S64Y; column label: kcat (sec^-1); raw value: 114.0; raw unit: sec^-1; normalized value: 114.0; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 114.0; normalized unit: s^-1

raw_value_unit_evidence: raw value: 114 (111, 116); raw unit: sec^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature M298K to reconstruct the assayed variant sequence.

column_label: Table 1; row label: M298K; column label: kcat (sec^-1); raw value: 37.7; raw unit: sec^-1; normalized value: 37.7; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 37.7; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature S64P to reconstruct the assayed variant sequence.

column_label: Table 1; row label: S64P; column label: kcat (sec^-1); raw value: 83.3; raw unit: sec^-1; normalized value: 83.3; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 83.3; normalized unit: s^-1


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

column_label: Table 1; row label: A456V; column label: kcat (sec^-1); raw value: 65.6; raw unit: sec^-1; normalized value: 65.6; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 65.6; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature G68V to reconstruct the assayed variant sequence.

column_label: Table 1; row label: G68V; column label: kcat (sec^-1); raw value: 62.7; raw unit: sec^-1; normalized value: 62.7; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 62.7; normalized unit: s^-1


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

proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant 454-Ala


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature Y214A/V452A to reconstruct the assayed variant sequence.

column_label: Table 1; row label: Y214A/V452A; column label: kcat (sec^-1); raw value: 23.1; raw unit: sec^-1; normalized value: 23.1; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 23.1; normalized unit: s^-1

raw_value_unit_evidence: raw value: 23.1±2.38; raw unit: sec^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M197I/A379T to reconstruct the assayed variant sequence.

proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197I/A379T


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature G68K to reconstruct the assayed variant sequence.

column_label: Table 1; row label: G68K; column label: kcat (sec^-1); raw value: 43.2; raw unit: sec^-1; normalized value: 43.2; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 43.2; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature M197I to reconstruct the assayed variant sequence.

column_label: Table 1; row label: M197I; column label: kcat (sec^-1); raw value: 58.1; raw unit: sec^-1; normalized value: 58.1; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 58.1; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature V91L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: V91L; column label: kcat (sec^-1); raw value: 60.6; raw unit: sec^-1; normalized value: 60.6; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 60.6; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature A379T to reconstruct the assayed variant sequence.

column_label: Table 1; row label: A379T; column label: kcat (sec^-1); raw value: 61.2; raw unit: sec^-1; normalized value: 61.2; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 61.2; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature S336L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: S336L; column label: kcat (sec^-1); raw value: 2.46; raw unit: sec^-1; normalized value: 2.46; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 2.46; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature M197L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: M197L; column label: kcat (sec^-1); raw value: 62.6; raw unit: sec^-1; normalized value: 62.6; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 62.6; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature Y214C to reconstruct the assayed variant sequence.

column_label: Table 1; row label: Y214C; column label: kcat (sec^-1); raw value: 65.3; raw unit: sec^-1; normalized value: 65.3; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 65.3; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature V389L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: V389L; column label: kcat (sec^-1); raw value: 67.1; raw unit: sec^-1; normalized value: 67.1; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 67.1; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature E442K to reconstruct the assayed variant sequence.

column_label: Table 1; row label: E442K; column label: kcat (sec^-1); raw value: 52.6; raw unit: sec^-1; normalized value: 52.6; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 52.6; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature V455M to reconstruct the assayed variant sequence.

column_label: Table 1; row label: V455M; column label: kcat (sec^-1); raw value: 61.8; raw unit: sec^-1; normalized value: 61.8; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 61.8; normalized unit: s^-1


column_label: Table 1; row label: G68K; column label: ATP Km (mM); raw value: 0.39; raw unit: mM; normalized value: 0.39; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.39; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature S263P to reconstruct the assayed variant sequence.

column_label: Table 1; row label: S263P; column label: ATP Km (mM); raw value: 0.63; raw unit: mM; normalized value: 0.63; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.63; normalized unit: mM


sequence_variant_note: Mutation signature V62M matches the mutant residue at offset -5 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

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 V62M

proof_lines: mutant enzyme V62M, at 30°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol

proof_lines: mutant enzyme V62M, at 37°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature M197E to reconstruct the assayed variant sequence.

column_label: Table 1; row label: M197E; column label: ATP Km (mM); raw value: 0.4; raw unit: mM; normalized value: 0.4; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.4; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature G68V to reconstruct the assayed variant sequence.

column_label: Table 1; row label: G68V; column label: ATP Km (mM); raw value: 0.31; raw unit: mM; normalized value: 0.31; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.31; normalized unit: mM


column_label: Table 1; row label: A379T; column label: ATP Km (mM); raw value: 0.87; raw unit: mM; normalized value: 0.87; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.87; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature S64P to reconstruct the assayed variant sequence.

column_label: Table 1; row label: S64P; column label: ATP Km (mM); raw value: 0.32; raw unit: mM; normalized value: 0.32; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.32; normalized unit: mM


column_label: Table 1; row label: E442K; column label: ATP Km (mM); raw value: 1.5; raw unit: mM; normalized value: 1.5; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 1.5; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature K140E to reconstruct the assayed variant sequence.

column_label: Table 1; row label: K140E; column label: ATP Km (mM); raw value: 0.35; raw unit: mM; normalized value: 0.35; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.35; normalized unit: mM

raw_value_unit_evidence: raw value: 0.35±0.08; raw unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature C213R to reconstruct the assayed variant sequence.

column_label: Table 1; row label: C213R; column label: ATP Km (mM); raw value: 0.89; raw unit: mM; normalized value: 0.89; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.89; normalized unit: mM

raw_value_unit_evidence: raw value: 0.89; raw unit: mM


column_label: Table 1; row label: V455M; column label: ATP Km (mM); raw value: 0.38; raw unit: mM; normalized value: 0.38; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.38; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature Y215A to reconstruct the assayed variant sequence.

column_label: Table 1; row label: Y215A; column label: ATP Km (mM); raw value: 0.58; raw unit: mM; normalized value: 0.58; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.58; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature S64Y to reconstruct the assayed variant sequence.

column_label: Table 1; row label: S64Y; column label: ATP Km (mM); raw value: 1.59; raw unit: mM; normalized value: 1.59; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 1.59; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature C252Y to reconstruct the assayed variant sequence.

column_label: Table 1; row label: C252Y; column label: ATP Km (mM); raw value: 0.75; raw unit: mM; normalized value: 0.75; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.75; normalized unit: mM

raw_value_unit_evidence: raw value: 0.75; raw unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature V452L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: V452L; column label: ATP Km (mM); raw value: 0.53; raw unit: mM; normalized value: 0.53; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.53; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature V91L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: V91L; column label: ATP Km (mM); raw value: 0.48; raw unit: mM; normalized value: 0.48; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.48; normalized unit: mM


column_label: Table 1; row label: V389L; column label: ATP Km (mM); raw value: 0.76; raw unit: mM; normalized value: 0.76; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.76; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature T65I to reconstruct the assayed variant sequence.

column_label: Table 1; row label: T65I; column label: ATP Km (mM); raw value: 0.57; raw unit: mM; normalized value: 0.57; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.57; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature Y214A to reconstruct the assayed variant sequence.

column_label: Table 1; row label: Y214A; column label: ATP Km (mM); raw value: 0.92; raw unit: mM; normalized value: 0.92; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.92; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature Y214C to reconstruct the assayed variant sequence.

column_label: Table 1; row label: Y214C; column label: ATP Km (mM); raw value: 1.08; raw unit: mM; normalized value: 1.08; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 1.08; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature S336L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: S336L; column label: ATP Km (mM); raw value: 12.6; raw unit: mM; normalized value: 12.6; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 12.6; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature M197I to reconstruct the assayed variant sequence.

column_label: Table 1; row label: M197I; column label: ATP Km (mM); raw value: 1.39; raw unit: mM; normalized value: 1.39; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 1.39; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature Y214A/V452A to reconstruct the assayed variant sequence.

column_label: Table 1; row label: Y214A/V452A; column label: ATP Km (mM); raw value: 1.42; raw unit: mM; normalized value: 1.42; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 1.42; normalized unit: mM

raw_value_unit_evidence: raw value: 1.42±0.29; raw unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature P417R to reconstruct the assayed variant sequence.

column_label: Table 1; row label: P417R; column label: ATP Km (mM); raw value: 2.08; raw unit: mM; normalized value: 2.08; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 2.08; normalized unit: mM

raw_value_unit_evidence: raw value: 2.08±0.15; raw unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature K414E to reconstruct the assayed variant sequence.

column_label: Table 1; row label: K414E; column label: ATP Km (mM); raw value: 1.53; raw unit: mM; normalized value: 1.53; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 1.53; normalized unit: mM

raw_value_unit_evidence: raw value: 1.53; raw unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature M197L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: M197L; column label: ATP Km (mM); raw value: 1.31; raw unit: mM; normalized value: 1.31; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 1.31; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature M298K to reconstruct the assayed variant sequence.

column_label: Table 1; row label: M298K; column label: ATP Km (mM); raw value: 3.32; raw unit: mM; normalized value: 3.32; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 3.32; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M197I/A379T to reconstruct the assayed variant sequence.


organism: Sus scrofa

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

proof_lines:
hexokinase II, at 30°C, pH 8.1
hexokinase III, at 30°C, pH 8.1
hexokinase IV


substrate_name: ITP

substrate: ITP


substrate_name: beta-D-glucose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W99R/W167F to reconstruct the assayed variant sequence.

proof_lines: co-substrate: ATP, mutant W99R/W167F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication

proof_lines: co-substrate: ATP, mutant W99R/W167F in the presence of 20-30% glycerol and in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication

proof_lines: co-substrate: ATP, mutant W99R/W167F, pH and temperature not specified in the publication

substrate: beta-D-glucose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W99R/W257F to reconstruct the assayed variant sequence.

proof_lines: co-substrate: ATP, mutant W99R/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: co-substrate: ATP, mutant W99R/W257F in the presence of 20-30% glycerol and in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication

proof_lines: co-substrate: ATP, mutant W99R/W257F, pH and temperature not specified in the publication


proof_lines: mutant W99R/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: mutant W99R/W257F, pH and temperature not specified in the publication

proof_lines: mutant W99R/W257F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication


proof_lines: mutant W99R/W167F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: mutant W99R/W167F in the presence of 20-30% glycerol and in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication

proof_lines: mutant W99R/W167F, pH and temperature not specified in the publication


organism: Eimeria tenella


substrate_name: D-mannose; D-glucose

substrate: D-mannose; D-glucose


sequence_variant_note: Mutation signature N216K matches the mutant residue at offset +13 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D217H to reconstruct the assayed variant sequence.


proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=7.1

source_databases_merged: skid uniprot


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines:
Raw SKiD Env: Temp=°C, pH=7.6
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=30°C, pH=7.4


substrate_name: 2-deoxyglucose (at 30 degrees Celsius and pH 7.5)

proof_lines: kcat is 66.4 sec(-1) with glucose as substrate (at 30 degrees Celsius and pH 7.5) (PubMed:7742312). kcat is 56.4 sec(-1) with mannose as substrate (at 30 degrees Celsius and pH 7.5) (PubMed:7742312). kcat is 56.4 sec(-1) with 2-deoxyglucose


substrate_name: fructose (at 30 degrees Celsius and pH 7.5)


substrate_name: glucosamine (at 30 degrees Celsius and pH 9)

assay_conditions_summary: pH 9


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G72R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines: mutant enzyme G72R, at 37°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol

proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant G72R

proof_lines: mutant enzyme G72R, at 30°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol


sequence_variant_note: Mutation signature V62M matches the mutant residue at offset -5 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines: mutant enzyme V62M, at 30°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol

proof_lines: mutant enzyme V62M, at 37°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol

proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant V62M


proof_lines: wild type enzyme, at 30°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol

proof_lines: wild type enzyme, at 37°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol


substrate_name: ATP

proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, wild-type


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


organism: Mus musculus

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K414E to reconstruct the assayed variant sequence.


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

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S151C/N166R to reconstruct the assayed variant sequence.


substrate_name: D-fructose


sequence_variant_note: Resolved canonical sequence from selected_batch_variant_sequence_check and applied mutation signature V182L to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ATP

proof_lines: mutant enzyme V182L, glutathione S-transferase glucokinase B fusion protein


sequence_variant_note: Resolved canonical sequence from selected_batch_variant_sequence_check and applied mutation signature K420E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K420E, glutathione S-transferase glucokinase B fusion protein


sequence_variant_note: Resolved canonical sequence from selected_batch_variant_sequence_check and applied mutation signature E265K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E265K, glutathione S-transferase glucokinase B fusion protein


sequence_variant_note: Resolved canonical sequence from selected_batch_variant_sequence_check and applied mutation signature Y61S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y61S, glutathione S-transferase glucokinase B fusion protein


sequence_variant_note: Resolved canonical sequence from selected_batch_variant_sequence_check and applied mutation signature A379V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A379V, glutathione S-transferase glucokinase B fusion protein


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W167F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W167F, in 25 mM HEPES (pH 7.4), at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W99F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W99F, in 25 mM HEPES (pH 7.4), at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W257F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W257F, in 25 mM HEPES (pH 7.4), at 37°C