substrate_name: dATP (insertion opposite abasic site)

substrate: dATP (insertion opposite abasic site)


enzyme_display_name: DNA-directed DNA polymerase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: dTTP (insertion opposite abasic site)

source_db: uniprot

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

data_origin: experimental

enzyme: DNA-directed DNA polymerase

substrate: dTTP (insertion opposite abasic site)

source: uniprot


substrate_name: dCTP (insertion opposite abasic site)

substrate: dCTP (insertion opposite abasic site)


enzyme_display_name: hexokinase

organism: Brugia malayi

substrate_name: glucose

enzyme: hexokinase

substrate: glucose


substrate_name: fructose

substrate: fructose


substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Toxoplasma gondii

source_db: brenda

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

source: brenda


substrate_name: D-glucose

substrate: D-glucose


source_db: oed

source: oed


organism: Schizosaccharomyces pombe

source_databases_merged: brenda uniprot


substrate_name: D-mannose

substrate: D-mannose


substrate_name: D-fructose

substrate: D-fructose


organism: Macrobrachium nipponense

verification_status: corrected

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

status: corrected


organism: Escherichia coli

substrate_name: sedoheptulose 7-phosphate

kcat_over_km_origin: calculated

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

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

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

proof_lines:
pH 7.0, 55°C
Raw SKiD Env: Temp=55°C, pH=7

source_databases_merged: brenda skid

substrate: sedoheptulose 7-phosphate


assay_conditions_summary: pH 7; 328.15 K; cofactor NADH

column_label: Table 1; row PfkA E.co PFK; cofactor ATP; substrate S7P; Km cell 2.5 mM; kcat cell 0.25 s^-1; kcat/Km cell 0.15 x 10^3 s^-1 M^-1; assay at 55 C and pH 7.0.

raw_value_unit_evidence: Table 1 PfkA E.co PFK S7P cells: Km 2.5 mM; kcat 0.25 s^-1; kcat/Km 0.15 x 10^3 s^-1 M^-1.

row_label: PfkA E.co PFK | sedoheptulose 7-phosphate

table_label: Table 1. Kinetics of the PFKs tested


substrate_name: D-Fructose 6-phosphate

column_label: Table 1; row PfkA E.co PFK; cofactor ATP; substrate F6P; Km cell 0.065 mM; kcat cell 1.2 s^-1; kcat/Km cell 19 x 10^3 s^-1 M^-1; assay at 55 C and pH 7.0.

raw_value_unit_evidence: Table 1 PfkA E.co PFK F6P cells: Km 0.065 mM; kcat 1.2 s^-1; kcat/Km 19 x 10^3 s^-1 M^-1.

row_label: PfkA E.co PFK | F6P

substrate: D-Fructose 6-phosphate


organism: Thermotoga maritima

sequence_source: multiple

assay_conditions_summary: pH 7.8; 323.15 K; cofactor ATP


substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


substrate_name: GTP

substrate: GTP


organism: Homo sapiens


organism: Saccharolobus solfataricus

substrate_name: dATP

substrate: dATP


substrate_name: dTTP

substrate: dTTP


substrate_name: dGTP

substrate: dGTP


organism: Botrytis cinerea


organism: Candida albicans (strain SC5314 / ATCC MYA-2876)

substrate_name: N-acetylglucosamine (GlcNAc)

verification_status: unverified

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

assay_conditions_summary: pH 7.5; cofactor ATP

substrate: N-acetylglucosamine (GlcNAc)

status: unverified


organism: Ogataea angusta

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


organism: Thermus thermophilus


organism: Amycolatopsis methanolica


verification_status: verified

normalized_value_unit_evidence: Km 0.6 mM.

raw_value_unit_evidence: Table 4 row ATP: Kapp 0.6 mM with table uncertainty 0.1 mM; prose identifies this as the apparent Km for ATP.

row_label: ATP; PPi absent; F-6-P fixed at 10 mM

table_label: Table 4. Kinetics of the ATP-PFK enzyme from A. methanolica WVI and effects of PPi on affinities for substrates F-6-P and ATP

status: verified


organism: Bacillus licheniformis


assay_conditions_summary: pH 6.8; 303.15 K; cofactor ATP


organism: Schistosoma mansoni

assay_conditions_summary: pH 8.5; cofactor ATP


organism: Lactococcus lactis subsp. lactis


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: Saccharomyces cerevisiae

substrate_name: D-Glucose

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH

column_label: Table 2; isoenzyme block HXK / Hxk1p; row "HXK | Hxk1p | kcat | 10.2 |  |  | s−1" column Value raw value 10.2 with column Unit s−1; row "HXK | Hxk1p | Kglc | 0.15 |  | 0.08 | mM" column Value raw value 0.15 with column Unit mM. Both cells sit in the same Hxk1p isoenzyme block of Table 2, so the kcat and Km cells are one tuple.

normalized_value_unit_evidence: kcat 10.2 s-1 normalizes to 10.2 s^-1. Kglc 0.15 mM normalizes to 0.15 mM. kcat/Km is not printed in Table 2, so paper kcat/Km = paper kcat / paper Km = 10.2 / 0.15 = 68.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 line "HXK | Hxk1p | kcat | 10.2 |  |  | s−1" gives kcat 10.2 s−1. Table 2 line "HXK | Hxk1p | Kglc | 0.15 |  | 0.08 | mM" gives Kglc 0.15 mM. Table 2 prints no kcat/Km or catalytic-efficiency column.

row_label: HXK / Hxk1p

table_label: Table 2. Enzyme kinetics parameters determined in this project and contrasted with those of Ref. [23]

substrate: D-Glucose


column_label: Table 2; isoenzyme block HXK / Hxk2p; row "HXK | Hxk2p | kcat | 63.1 |  |  | s−1" column Value raw value 63.1 with column Unit s−1; row "HXK | Hxk2p | Kglc | 0.2 |  | 0.08 | mM" column Value raw value 0.2 with column Unit mM. Both cells sit in the same Hxk2p isoenzyme block of Table 2, so the kcat and Km cells are one tuple.

normalized_value_unit_evidence: kcat 63.1 s-1 normalizes to 63.1 s^-1. Kglc 0.2 mM normalizes to 0.2 mM. kcat/Km is not printed in Table 2, so paper kcat/Km = paper kcat / paper Km = 63.1 / 0.2 = 315.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 line "HXK | Hxk2p | kcat | 63.1 |  |  | s−1" gives kcat 63.1 s−1. Table 2 line "HXK | Hxk2p | Kglc | 0.2 |  | 0.08 | mM" gives Kglc 0.2 mM. Table 2 prints no kcat/Km or catalytic-efficiency column.

row_label: HXK / Hxk2p


organism: Lysinibacillus sphaericus


organism: Escherichia coli (strain K12)


assay_conditions_summary: pH 6.9; cofactor ATP


column_label: Results 3.3, journal page 174, and Figure 4/caption on page 175: recombinant Schistosoma mansoni PFK Fru-6-P saturation under 1 mM AMP reports apparent Km 0.8 mM; the figure caption specifies pH 6.9 and 1 mM ATP.

normalized_value_unit_evidence: Apparent Fru-6-P Km is already canonical at 0.8 mM.

raw_value_unit_evidence: Apparent Km for Fru-6-P under 1 mM AMP: raw 0.8 mM.

row_label: recombinant Schistosoma mansoni PFK; Fru-6-P saturation with 1 mM AMP

table_label: Results 3.3 and Figure 4


organism: Leishmania donovani


organism: Spinacia oleracea

assay_conditions_summary: pH 7.8; 303.15 K; cofactor ATP


substrate_name: North-methanocarba-dATP

substrate: North-methanocarba-dATP


substrate_name: South-methanocarba-dATP

substrate: South-methanocarba-dATP


organism: Schizosaccharomyces pombe

assay_conditions_summary: pH 7.2; 298.15 K; cofactor ATP


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


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

substrate_name: fructose 6-phosphate (without effector)

substrate: fructose 6-phosphate (without effector)


organism: Homo sapiens

substrate_name: dTTP (POLG polymerase activity at matched G:C primer-template)


organism: Drosophila melanogaster

substrate_name: deoxythymidine triphosphate

substrate: deoxythymidine triphosphate


organism: Danio rerio


organism: Thermococcus thioreducens

substrate_name: dNTP

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

substrate: dNTP


organism: Trypanosoma cruzi (strain CL Brener)

substrate_name: ATP

substrate: ATP


organism: Dictyostelium discoideum


organism: Thermococcus kodakarensis

substrate_name: ADP

assay_conditions_summary: pH 7.5; 323.15 K; cofactor ADP

substrate: ADP


substrate_name: AMP

assay_conditions_summary: pH 7.5; 323.15 K; cofactor ATP

substrate: AMP


substrate_name: D-fructose 1,6-bisphosphate

substrate: D-fructose 1,6-bisphosphate


substrate_name: D-glucose

substrate: D-glucose


substrate_name: D-Fructose 6-phosphate

substrate: D-Fructose 6-phosphate


organism: Komagataella pastoris

substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


organism: Saccharolobus solfataricus

substrate_name: dCTP

sequence_variant_note: Resolved canonical sequence from uniprot_Q97W02_reconstructed_variant_from_PMID_18984592 and applied mutation signature N188W to reconstruct the assayed variant sequence.

mutation_type: substitution

substrate: dCTP


sequence_variant_note: Resolved canonical sequence from uniprot_Q97W02_reconstructed_variant_from_PMID_18984592 and applied mutation signature T239W to reconstruct the assayed variant sequence.


organism: Lactobacillus delbrueckii subsp. bulgaricus

assay_conditions_summary: pH 8.2; cofactor ATP


assay_conditions_summary: pH 6; cofactor ATP


organism: Trypanosoma brucei

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

proof_lines:
Trypanosoma brucei
phosphofructokinase
ATP


substrate_name: Fructose 6-phosphate

proof_lines:
Trypanosoma brucei
phosphofructokinase
fructose 6-phosphate

substrate: Fructose 6-phosphate


organism: Thermotoga maritima

assay_conditions_summary: pH 7; 348.15 K; cofactor ATP


organism: Geobacillus stearothermophilus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


organism: Escherichia coli

source_db: skid

assay_conditions_summary: pH 8.2; 301.15 K; cofactor ATP

source_databases_merged: skid uniprot

source: skid


assay_conditions_summary: pH 8.2; 298.15 K; cofactor ATP


organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

assay_conditions_summary: cofactor ATP


substrate_name: fructose 6-phosphate


organism: Oceanimonas doudoroffii

assay_conditions_summary: pH 8; 301.15 K; cofactor ATP


substrate_name: dATP

sequence_source: UniProtKB P52026 canonical FASTA retrieved by direct UniProt REST check on 2026-05-25

proof_lines: pH and temperature not specified in the publication

substrate: dATP


substrate_name: dGTP

substrate: dGTP


substrate_name: TTP

substrate: TTP


substrate_name: D-mannose

sequence_source: UniProtKB:P35557 canonical sequence with row-specific substitution reconstruction

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

substrate: D-mannose


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


substrate_name: D-fructose

substrate: D-fructose


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


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


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


substrate_name: fructose 1,6-bisphosphate

km_display: Not reported

substrate: fructose 1,6-bisphosphate


substrate: fructose 6-phosphate


assay_conditions_summary: pH 8.2; 303.15 K; cofactor ATP

proof_lines: pH 8.2, 30°C, at fructose 6-phosphate concentrations that are less than approx. one-third the fixed MgATP concentration


substrate_name: GTP

substrate: GTP


substrate_name: UTP

substrate: UTP


substrate_name: CTP

substrate: CTP


substrate_name: ATP

substrate: ATP


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: pH 8.0, mutant enzyme Q466_H467insHMNLAEQ


sequence_source: UniProt P35557 canonical sequence reconstructed with A208G after direct residue check

sequence_variant_note: Mutation signature A208G matches the mutant residue at offset +0 and the reference residue at offset -7; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

assay_conditions_summary: 303.15 K; cofactor ATP


sequence_source: UniProt P35557 canonical sequence reconstructed with K458R after direct residue check

sequence_variant_note: Mutation signature K458R matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProt P35557 canonical sequence reconstructed with C457V after direct residue check

sequence_variant_note: Mutation signature C457V matches the mutant residue at offset +0 and the reference residue at offset +4; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProt P35557 canonical sequence reconstructed with Y215A after direct residue check

sequence_variant_note: Mutation signature Y215A matches the mutant residue at offset +0 and the reference residue at offset -1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProt P35557 canonical sequence reconstructed with A460R after direct residue check


sequence_source: UniProt P35557 canonical sequence reconstructed with K459L after direct residue check

sequence_variant_note: Mutation signature K459L matches the mutant residue at offset +0 and the reference residue at offset -1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


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

substrate_name: fructose 1,6-bisphosphate (at 75 degrees Celsius)


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from UniProt P08237 canonical sequence plus PMID 22474333 human mutant muscle Pfk evidence and applied mutation signature N341A/R246A/K386A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

proof_lines: mutant enzyme N341A/R246A/K386A, 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 N341A/R246A/K386A, 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 N341A/R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P08237 canonical sequence plus PMID 22474333 human mutant muscle Pfk evidence and applied mutation signature R246A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R246A, 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 R246A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme R246A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P08237 canonical sequence plus PMID 22474333 human mutant muscle Pfk evidence and applied mutation signature K678A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K678A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme K678A, 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 K678A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P08237 canonical sequence plus PMID 22474333 human mutant muscle Pfk evidence and applied mutation signature K386A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K386A, 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 K386A, 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 K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P08237 canonical sequence plus PMID 22474333 human mutant muscle Pfk evidence and applied mutation signature S377A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S377A, 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 S377A, 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 S377A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P08237 canonical sequence plus PMID 22474333 human mutant muscle Pfk evidence and applied mutation signature S377A/K678A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S377A/K678A, 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 S377A/K678A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme S377A/K678A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P08237 canonical sequence plus PMID 22474333 human mutant muscle Pfk evidence and applied mutation signature R246A/K386A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R246A/K386A, 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 R246A/K386A, 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 R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


substrate_name: Unknown

ki_unit: mM

sequence_source: UniProt P08237 canonical sequence plus PMID 22474333 human mutant muscle Pfk evidence

proof_lines: mutant enzyme S377A, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

substrate: Unknown


proof_lines: mutant enzyme N341A/R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme N341A/R246A/K386A, 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 N341A/R246A/K386A, 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 K678A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme K678A, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme K678A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: Ki above 10 mM, mutant enzyme K386A, 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 K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: Ki above 10 mM, mutant enzyme R246A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: Ki above 10 mM, mutant enzyme R246A, 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 R246A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


proof_lines: Ki above 10 mM, mutant enzyme R246A/K386A, in the presence of 0.82 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: Ki above 10 mM, mutant enzyme R246A/K386A, 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: Ki above 10 mM, mutant enzyme R246A/K386A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt P08237 canonical sequence plus PMID 22474333 human mutant muscle Pfk evidence and applied mutation signature N341A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N341A, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme N341A, 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 N341A, 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 S377A/K678A, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme S377A/K678A, 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 S377A/K678A, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


organism: Cucumis sativus

assay_conditions_summary: pH 7.2; 298.15 K; cofactor ATP

proof_lines:
pH 8.0, 25°C, cytosolic PFK
pH 7.2, 25°C, plastid PFK
pH 8.0, 25°C, plastid PFK


substrate_name: ITP

proof_lines: pH 8.0, 25°C, pH 7.2, 25°C, cytosolic PFK

substrate: ITP


proof_lines:
pH 7.2, 25°C, cytosolic PFK
pH 8.0, 25°C, plastid PFK
pH 8.0, 25°C, cytosolic PFK


proof_lines:
pH 8.0, 25°C, cytosolic PFK
pH 7.2, 25°C, cytosolic PFK
pH 8.0, 25°C, plastid PFK


substrate_name: D-fructose 6-phosphate


proof_lines: pH 8.5, 30°C, D127/R252Q double mutant PFK


assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP


substrate_name: D-glucosamine

proof_lines:
hexokinase I, at 37°C, pH 8.1
hexokinases Ib and Ic, at 37°C, pH 7.2
hexokinase Ia, at 37°C, pH 7.2

substrate: D-glucosamine


proof_lines:
hexokinase I, at 37°C, pH 8.1
hexokinase Ib, at 37°C, pH 7.2
hexokinase Ia, at 37°C, pH 7.2


proof_lines: hexokinases Ia, Ib and Ic, at 37°C, pH 7.2


organism: Saccharomyces cerevisiae


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


substrate_name: D-mannosamine

substrate: D-mannosamine


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


smiles: C(C(C(C(C(C=O)F)O)O)O)O


organism: Pyrococcus furiosus

proof_lines: 55°C, pH not specified in the publication, mutant enzyme Y410I


proof_lines: 55°C, pH not specified in the publication, mutant enzyme Y410L


proof_lines: 55°C, pH not specified in the publication, mutant enzyme Y410V


proof_lines: 55°C, pH not specified in the publication, wild-type enzyme


proof_lines: 55°C, pH not specified in the publication, mutant enzyme L409V


proof_lines: 55°C, pH not specified in the publication, mutant enzyme L409M


proof_lines: 55°C, pH not specified in the publication, mutant enzyme L409I


substrate_name: D-glucose

sequence_variant_note: Resolved canonical sequence from uniprot_accession:P19367 and applied mutation signature A464P/E465G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

substrate: D-glucose


assay_conditions_summary: pH 8; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P19367 and applied mutation signature Q466insHMNLAEQ to reconstruct the assayed variant sequence.

mutation_type: insertion

proof_lines: pH 8.0, mutant enzyme Q466_H467insHMNLAEQ


substrate_name: dATP

sequence_source: UniProt P00582 Klenow-fragment region; paper identity from PMID 29036327

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


substrate_name: dCTP

substrate: dCTP


substrate_name: dGTP


substrate_name: dTTP

substrate: dTTP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P28340 plus PMID:20628184 Leu-606 paper context and applied mutation signature L606G to reconstruct the assayed variant sequence.

proof_lines: mutant L606G, pH 7.5, 37°C, misincorporation of dTTP with G at first position


sequence_source: UniProtKB:P28340 plus PMID:20628184 Leu-606 paper context

proof_lines: wild-type enzyme, pH 7.5, 37°C, misincorporation of dTTP with G at first position


sequence_variant_note: Resolved canonical sequence from UniProtKB:P28340 plus PMID:20628184 Leu-606 paper context and applied mutation signature L606K to reconstruct the assayed variant sequence.

proof_lines: mutant L606K, pH 7.5, 37°C, misincorporation of dTTP with G at first position


organism: Musa acuminata

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

assay_conditions_summary: pH 7.3; 298.15 K; cofactor ATP

proof_lines:
pH 7.3, 25°C, PFK II
pH 8.0, 25°C, PFK I


organism: Aspergillus niger


substrate_name: D-fructose


substrate_name: fructose 6-phosphate

proof_lines:
pH 8.0, 8.5°C, wild-type PFK
pH 8.5, 30°C, wild-type PFK


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


organism: Leishmania mexicana


proof_lines:
inhibition with respect to ATP
inhibition with respect to glucose


organism: Oryctolagus cuniculus

proof_lines:
at 37°C, pH 8.1
hexokinase Ib
hexokinase Ia


proof_lines:
MgITP2-, at 37°C, pH 8.1
MgITP2-, erythrocyte enzyme
MgITP2-, hexokinase Ia


assay_conditions_summary: pH 8.1; 310.15 K; cofactor ATP

proof_lines: MgATP2-, bound mitochondrial HK I, at pH 7.5


proof_lines: mutant enzyme N341A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme N341A, 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 N341A, 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 D543A, in the presence of 0.1 mM 5-phospho-alpha-D ribose 1-diphosphate, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme D543A, 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 D543A, without effectors, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


assay_conditions_summary: pH 7; 298.15 K; cofactor ADP

proof_lines: mutant enzyme D543A, in the presence of 1 mM ADP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C

proof_lines: mutant enzyme D543A, 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: wild type enzyme, 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: wild type enzyme, at pH 7.0 in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2 and 25°C

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


substrate_name: ATP; D-Glucose

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

proof_lines: uncomplexed ATP, erythrocyte enzyme, competitive to MgATP2-

proof_lines: erythrocyte enzyme, competitive to glucose

proof_lines: erythrocyte enzyme, mixed inhibitor versus MgATP2-

substrate: ATP; D-Glucose


proof_lines:
hexokinase Ib
at 37°C, pH 8.1
erythrocyte enzyme


substrate_name: D-mannose

proof_lines:
hexokinase Ib
at 37°C, pH 8.1
reticulocyte hexokinase Ib


proof_lines:
hexokinase Ia
at 37°C, pH 8.1
hexokinase Ib


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: wild-type, 37°C, pH not specified in the puclication. Kinetic constants at high and low concentrations of the fixed substrate: 0.5 mM D-glucose


sequence_source: reconstructed_from_uniprot:P35557; L146R applied after direct residue check

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

proof_lines: mutant L146R, 37°C, pH not specified in the puclication


sequence_source: reconstructed_from_uniprot:P35557; T228M applied after direct residue check

proof_lines: mutant T228M, 37°C, pH not specified in the puclication


assay_conditions_summary: 310.15 K; cofactor ATP


organism: Thermococcus litoralis

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: O6-MeG

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


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: N2-MeG


substrate: dATP


substrate: dGTP


organism: Ascaris suum


substrate: D-fructose


organism: Entamoeba histolytica

proof_lines:
recombinant HXK1, at 30°C, pH 8
recombinant HXK2, at 30°C, pH 8


proof_lines:
recombinant HXK2, at 30°C, pH 8
recombinant HXK1, at 30°C, pH 8


assay_conditions_summary: pH 7.8; 303.15 K; cofactor ATP


substrate_name: GTP


proof_lines:
pH 7.8, 30°C, at 0.5 mM ATP
pH 7.8, 30°C, at 0.1 mM ATP
pH 7.8, 30°C


organism: Bos taurus


organism: Crassostrea virginica

substrate_name: ATP

assay_conditions_summary: pH 7.9; 297.15 K; cofactor ATP


substrate: D-fructose 6-phosphate


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: wild type enzyme, at 25°C, in the presence of 0.02 mM activator LY-2121260

proof_lines: wild type enzyme, at 25°C, in the presence of 0.02 mM activator N-[2-amino-4-fluoro-5-[(1-methyl-1H-imidazol-2-yl)sulfanyl]benzyl]-1,3-thiazol-2-amine


proof_lines:
wild-type enzyme
30°C, pH 7.5, wild-type


proof_lines: glucokinase with C-terminal 10 alanine addition

proof_lines: glucokinase with C-terminal 5 alanine addition

proof_lines: recombinant hexokinase I expressed in Escherichia coli


mutation_signature: truncated enzyme with removed helix alpha13 truncated enzyme with removed helix alpha13

mutation_type: truncation


sequence_source: UniProtKB:P35557 canonical sequence with D205A reconstructed during review

proof_lines: mutant enzyme D205A, kcat less than 0.00091 s-1


organism: Solanum tuberosum

substrate: D-mannose


assay_conditions_summary: cofactor ATP


organism: Sus scrofa

substrate_name: D-Fructose 6-phosphate; ATP

assay_conditions_summary: pH 7; cofactor ATP

substrate: D-Fructose 6-phosphate; ATP


assay_conditions_summary: pH 7


organism: Sulfolobus acidocaldarius

proof_lines: pH and temperature not specified in the publication


organism: Thermus aquaticus


organism: Streptococcus pneumoniae

substrate_name: primed M13

proof_lines: exonuclease activity, wild-type, pH 7.6, 37°C

substrate: primed M13


assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines: polymerase activity, D190A mutant, pH 7.6, 37°C


proof_lines: exonuclease activity, D190A mutant, pH 7.6, 37°C


organism: Homo sapiens

mutation_signature: a truncate HK I form lacking the first 11 amino acids named HK-11aa / a truncate HK I form lacking the first 11 amino acids named HK-11aa

sequence_source: UniProt P19367 FASTA reconstructed as HK-11aa using PMID 9879670

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

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines: MgATP2-, recombinant HK I, a truncate HK I form lacking the first 11 amino acids named HK-11aa, and the 50 kDa C-terminal half of HK I, at 37°C, pH 7.2


proof_lines: recombinant HK I, a truncate HK I form lacking the first 11 amino acids named HK-11aa, and the 50 kDa C-terminal half of HK I, at 37°C, pH 7.2


substrate_name: Unknown


organism: Saccharomyces cerevisiae


substrate_name: rCTP

substrate: rCTP


organism: Triticum aestivum

substrate_name: D-fructose 6-phosphate

assay_conditions_summary: pH 7.9; cofactor ATP


substrate: ATP


substrate: Unknown


organism: Anguilla anguilla


organism: Citrus x paradisi

assay_conditions_summary: pH 7.5; cofactor ATP


proof_lines:
pH 7.5, theoretical value
pH 7.5


assay_conditions_summary: pH 6.8; 303.15 K; cofactor ATP


organism: Aquarana catesbeiana


organism: Clostridium pasteurianum


assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


substrate_name: K+

substrate: K+


organism: Cyprinus carpio


organism: Escherichia coli

sequence_source: UniProtKB:P06999 direct lookup

assay_conditions_summary: pH 8.2; 303.15 K; cofactor ATP

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

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


assay_conditions_summary: pH 8.2; cofactor ATP


substrate_name: beta-D-glucose

proof_lines: co-substrate: ATP, mutant W167F/W257F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication

proof_lines: co-substrate: ATP, mutant W167F/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: co-substrate: ATP, mutant W167F/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

substrate: beta-D-glucose


proof_lines: mutant W167F/W257F, pH and temperature not specified in the publication

proof_lines: mutant W167F/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: mutant W167F/W257F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication


organism: Lactococcus lactis

sequence_source: UniProtKB:P0DOB6; direct UniProt JSON check links PMID 6218377 and DOI 10.1016/s0076-6879(82)90109-4 to strain C10 phosphofructokinase function/biophysical evidence

proof_lines:
pH 7.5
ATP in form of MgATP2-


organism: Geobacillus anatolicus

substrate_name: dATP

sequence_source: UniProtKB:Q0PL69 / NCBI Protein ABG80522.1; GF C-terminal 592-aa fragment reconstructed from Q0PL69 residues 287-878 using PMID 22652043 method context

proof_lines:
pH 8.0, 50°C, recombinant enzyme
pH 8.0, 37°C, recombinant enzyme


proof_lines:
pH 8.0, 50°C, recombinant enzyme
pH 8.0, 22°C, recombinant enzyme
pH 8.0, 37°C, recombinant enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9UGP5 and applied mutation signature Y505A to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme Y505A
37°C, pH 7.0, mutant enzyme Y505A


organism: Rattus norvegicus


substrate_name: D-glucosamine

substrate: D-glucosamine


organism: Ricinus communis

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

proof_lines:
pH 7.0, 25°C, chloroplasr PFK
pH 8.0, 25°C, cytosolic PFK
pH 7.0, 25°C, cytosolic PFK


substrate: fructose 6-phosphate


organism: Mus musculus

sequence_source: UniProtKB:P52792 direct follow-up; paper-linked Gck/GK identity from PMID 17353190

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


substrate_name: D-glucose

substrate: D-glucose


assay_conditions_summary: pH 8.4; cofactor ATP

proof_lines: 12 h after isoproterenol administration, PFK-1


organism: Saccharolobus solfataricus

proof_lines:
template base: dA, pH 7.5, 37°C
pH 7.5, 25°C
template base: dX, pH 7.5, 37°C


substrate_name: dCTP

proof_lines: template base: 2-fluoro-2-deoxyinosine, pH 7.5, 37°C

substrate: dCTP


organism: Oryza sativa

sequence_variant_note: Resolved canonical sequence from UniProt REST Q6Z4T5 canonical sequence with D362A substitution applied during review and applied mutation signature D362A to reconstruct the assayed variant sequence.

proof_lines: 37°C, pH 7.5, mutant enzyme D362A, substitution opposite the template G


sequence_source: UniProt REST Q6Z4T5 canonical sequence checked during review

proof_lines: 37°C, pH 7.5, wild-type enzyme, substitution opposite the template G

proof_lines: 37°C, pH 7.5, wild-type enzyme, substitution opposite the template A


substrate_name: dGTP

proof_lines:
pH 7.5, 25°C
template base: dX, pH 7.5, 37°C
template base: dA, pH 7.5, 37°C


substrate_name: dTTP

proof_lines: template base: 2-bromo-2-deoxyinosine, pH 7.5, 37°C

substrate: dTTP


assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP

proof_lines:
pH 7.5, 22°C, immobilized enzyme
pH 7.5, 22°C, soluble enzyme
pH 7.5, 22°C


organism: Thermoplasma acidophilum

substrate: dATP


organism: Trypanosoma cruzi


proof_lines: varied substrate is D-glucose, in the presence of 1 mM ATP and 3 mM MgCl2, Kis

proof_lines: varied substrate is D-glucose, in the presence of 1 mM ATP and 3 mM MgCl2, Kii

proof_lines: varied substrate is ATP, in the presence of 2 mM D-glucose and 3 mM MgCl2, Kis


organism: Vigna mungo


organism: Streptococcus thermophilus

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


organism: Trypanosoma brucei

assay_conditions_summary: pH 7.4; cofactor ATP

proof_lines: pH and temperature not specified in the publication

proof_lines: pH 7.4, temperature not specified in the publication

proof_lines: pH 6.5, temperature not specified in the publication


organism: Sporolactobacillus inulinus

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP


organism: Thermus aquaticus

substrate_name: deoxynucleoside triphosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P19821 canonical sequence with G418K/E507Q reconstructed during review and applied mutation signature G418K/E507Q to reconstruct the assayed variant sequence.

substrate: deoxynucleoside triphosphate


sequence_source: UniProtKB:P19821 canonical sequence


organism: African swine fever virus


organism: Bos taurus

proof_lines:
pH 7.2, 37°C
polymerase delta, pH 7.5, 37°C
pH 7.5, 37°C


substrate_name: 2-Deoxyglucose; ATP

proof_lines: inhibition of fructose phosphorylation, at 37°C, pH 7.4

substrate: 2-Deoxyglucose; ATP


organism: Bacillus subtilis

substrate_name: DNA; Deoxynucleoside triphosphate

substrate: DNA; Deoxynucleoside triphosphate


organism: Dictyostelium discoideum

substrate_name: ATP

proof_lines: wild type enzyme, at pH 7.0 in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2 and 25°C


organism: Eimeria tenella

substrate_name: D-fructose

substrate: D-fructose


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35557 and applied mutation signature V62Q to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ATP

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 V62Q, row mean of two independent expressions; column kcat (s^-1) cell = 14.9; column ATP Km (mM) cell = 0.11. captured primary segment: Table I, mutant row V62Q, row mean of two independent expressions | construct V62Q GST-GCK | substrate ATP | condition kinetic analysis of the purified GST fusion enzyme, no assay pH or temperature printed for Table I | kcat 14.9 s^-1 | ATP Km 0.11 mM

normalized_value_unit_evidence: kcat: printed Table I kcat cell 14.9 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 14.9 s^(-1). Km: printed Table I ATP Km cell 0.11 mM; the printed column is already in millimolar, so no unit conversion applies and the value is 0.11 mM. kcat/Km: the exported efficiency is the quotient of those two printed cells of this one measurement, 14.9 / 0.11 = 135.45454545454547 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 14108, Table I, mutant row V62Q, row mean of two independent expressions: kcat = 14.9 s^-1; ATP Km = 0.11 mM. Table I carries no catalytic-efficiency column.

row_label: Table I, mutant row V62Q, row mean of two independent expressions; the cited cells are the mean of the two independent expressions of this mutant


substrate_name: dTTP; DNA

proof_lines: DNA polymerase lambda, in 50 mM Tris-HCl (pH 7.5), 1 mM dithiothreitol, 50% (v/v) glycerol, and 0.1 mM EDTA, at 37°C

substrate: dTTP; DNA


organism: Escherichia coli

substrate_name: dATP; DNA

proof_lines:
pol I
pol III
pol II

substrate: dATP; DNA


substrate_name: Unknown

assay_conditions_summary: pH 8

proof_lines:
wild type hexokinase II
pH 8.0, wild-type enzyme


sequence_source: UniProtKB:P08237 canonical sequence

proof_lines: wild type enzyme, 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: wild type enzyme, in the presence of 1 mM AMP, in 50 mM HEPES, 100 mM KCl, 5 mM MgCl2, pH 7.0, at 25°C


organism: Drosophila melanogaster

substrate_name: 2'-deoxyguanosine triphosphate

sequence_source: UniProtKB reviewed Q27607 (DPOG1_DROME), direct UniProt REST FASTA lookup on 2026-05-25

assay_conditions_summary: pH 7.6; 303.15 K; buffer matches the PMID 18056280 Pol gamma primer-extension assay

proof_lines: in 50 mM Tris-HCl (pH 7.6), 100 mM KCl, 5 mM MgCl2, 10% (v/v) glycerol, 1 mM dithiothreitol, at 30°C

substrate: 2'-deoxyguanosine triphosphate


substrate_name: D-Glucose; ATP

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines: catalytically active recombinant carboxyl-domain of hexokinase III, at 37°C, pH 7.2

proof_lines: hexokinase III from lymphocytes, at 37°C, pH 7.2

proof_lines: hexokinase Ia, Ib and Ic, at 37°C, pH 7.2

substrate: D-Glucose; ATP


assay_conditions_summary: pH 8.1; 310.15 K; cofactor ATP

proof_lines: hexokinase III from lymphocytes, at 37°C, pH 8.1

proof_lines: MgATP2-, hexokinases Ia, Ib and Ic, at 37°C, pH 7.2

proof_lines: catalytically active recombinant carboxyl-domain of hexokinase III, at 37°C, pH 8.1

substrate: ATP


substrate_name: D-fructose 6-phosphate

proof_lines:
pH 8.0, 25°C, erythrocyte PFK
pH 7.1, 25°C, M-type PFK

substrate: D-fructose 6-phosphate


organism: Kluyveromyces lactis

proof_lines: pH 7.15, 25°C, in the presence of 1 mM AMP

proof_lines: pH 7.15, 25°C, in the presence of 0.1 mM fructose 2,6-bisphosphate


organism: Mus musculus


substrate_name: ATP; D-Fructose 6-phosphate

assay_conditions_summary: pH 7.2; 298.15 K; cofactor ATP

proof_lines: pH 7.2, 25°C, mammary gland and ascites tumor PFK

substrate: ATP; D-Fructose 6-phosphate


substrate_name: ATP; D-Glucose

substrate: ATP; D-Glucose


organism: Oncorhynchus mykiss

assay_conditions_summary: pH 7.2; 295.15 K; cofactor ATP


organism: Rattus norvegicus

proof_lines:
HK I, at 25°C, pH 7.4
HK II, at 25°C, pH 7.4


substrate_name: fructose 6-phosphate

substrate: fructose 6-phosphate


organism: Oryctolagus cuniculus

substrate_name: N-acetyl-D-glucosamine

substrate: N-acetyl-D-glucosamine


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines:
at 30°C, pH 7.5
hexokinase III
hexokinase C


assay_conditions_summary: pH 7.1; cofactor ATP


enzyme_display_name: CDQ83_07225 C.ts A/GTP-PFK

organism: Clostridium thermosuccinogenes

assay_conditions_summary: pH 7; 328.15 K; cofactor ATP

enzyme: CDQ83_07225 C.ts A/GTP-PFK


substrate_name: ATP; Glucose

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: hexokinase C, versus ATP, at 0.2 mM glucose

substrate: ATP; Glucose


proof_lines: DNA polymerase beta, in 50 mM Tris-HCl (pH 7.5), 1 mM dithiothreitol, 50% (v/v) glycerol, and 0.1 mM EDTA, at 37°C


substrate_name: D-mannose

proof_lines:
at 30°C, pH 7.5
hexokinase C
hexokinase II

substrate: D-mannose


proof_lines:
rat brain enzyme, hexokinase I
HKI, at 25°C, pH 7.4
rat liver enzyme, hexokinase IV


organism: Saccharomyces cerevisiae

substrate_name: ATP; 6-Aminoglucose

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines:
glucokinase
hexokinase PI
hexokinase PII

substrate: ATP; 6-Aminoglucose


organism: Saccharolobus solfataricus

substrate_name: North-methanocarba-dATP

substrate: North-methanocarba-dATP


organism: Solanum tuberosum

assay_conditions_summary: pH 7

proof_lines:
pH 7, hexokinase 1
HK1, at pH 7
HK2

substrate: Unknown


organism: Spinacia oleracea

assay_conditions_summary: pH 7.7; 298.15 K; cofactor ATP


organism: Sulfolobus acidocaldarius

substrate_name: dTTP

proof_lines: pH and temperature not specified in the publication

substrate: dTTP


substrate_name: ATP


organism: Sus scrofa

assay_conditions_summary: pH 8.1; 303.15 K; cofactor ATP


organism: Sparus aurata

proof_lines: Ki(slope) Ki(intercept)


assay_conditions_summary: pH 7; cofactor ATP

proof_lines: purified enzyme, at pH 7.0, in the absence of D-fructose 2,6-bisphosphate

proof_lines: purified enzyme, at pH 7.0, in the presence of 0.005 mM D-fructose 2,6-bisphosphate


organism: Thermus thermophilus


organism: Triticum aestivum


organism: Trypanosoma cruzi

substrate_name: D-fructose

substrate: D-fructose


enzyme_display_name: DNA polymerase I

organism: Thermotoga petrophila

sequence_variant_note: Resolved canonical sequence from UniProtKB:E2RWL8 / GenPept:BAJ23222.1 reconstructed as L329A from PMID:23026053 and applied mutation signature L329A to reconstruct the assayed variant sequence.

proof_lines: pH 8.2, 50 C, recombinant enzyme mutant K4polL329A

enzyme: DNA polymerase I


organism: Thermococcus pacificus

substrate_name: deoxynucleoside triphosphate

proof_lines: pH 7.5, 75°C, turnover number of each nucleotide in an equimolar mixture of the four nucleotides, unmodified Tpa DNA polymerase

proof_lines: pH 7.5, 75°C, turnover number of each nucleotide in an equimolar mixture of the four nucleotides, fusion protein of the Sso7d protein to the C-terminus of Tpa DNA polymerase

proof_lines: pH 7.5, 75°C, mol of template, in the presence of an excess of annealed primer, unmodified Tpa DNA polymerase

substrate: deoxynucleoside triphosphate


sequence_source: UniProtKB Q5SJ64, Thermus thermophilus HB8 DNA polymerase beta / PolX / TTHA1150

proof_lines:
pH 9.0, 25°C
in the absence of dNTPs
in the presence of dNTPs


organism: Zea mays

proof_lines:
non-cytosolic hexokinase from root
root, non-cytosolic enzyme
non-cytoslic hexokinase from root


organism: Escherichia coli

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

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant I126A


substrate_name: D-Fructose 6-phosphate; ATP

proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant R72H

substrate: D-Fructose 6-phosphate; ATP


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant Y41A


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant Y41F


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant Y41W


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant Y41L


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant F76A


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant F76Y


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant F76W


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant M169L


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant M169A


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant R252Q


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant D127S:R252Q


organism: Gallus gallus


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant R111A


proof_lines: SABIO-RK modifier species: 6-phosphofructokinase(Enzyme) mutant R111E


substrate_name: ITP; D-Fructose 6-phosphate

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

substrate: ITP; D-Fructose 6-phosphate


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


organism: Lactococcus lactis subsp. lactis


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


organism: Rana catesbeiana


organism: Canis familiaris

substrate_name: Glucose; ATP

substrate: Glucose; ATP


organism: Nicotiana tabacum

sequence_source: UniProtKB Q6Q8A5 direct REST lookup; entry is HXK2_TOBAC/NtHxK2, EC 2.7.1.1, organism Nicotiana tabacum, PubMed ID 15670855.


organism: Salmo salar


organism: Drosophila melanogaster

substrate_name: D-Glucose; ATP

substrate: D-Glucose; ATP


organism: Ustilago maydis


organism: Bos taurus


organism: Chlorocebus sp.


organism: Crassostrea virginica


organism: Lactobacillus casei


organism: Sus scrofa


organism: Mytilus galloprovincialis


organism: Plasmodium falciparum


organism: Musa acuminata


organism: Oncorhynchus mykiss


organism: Mustela vison


organism: Saccharomyces cerevisiae

substrate_name: ATP; beta-D-Fructose 6-phosphate

substrate: ATP; beta-D-Fructose 6-phosphate


organism: Saccharomyces pastorianus

substrate_name: ATP; D-Fructose 6-phosphate

substrate: ATP; D-Fructose 6-phosphate


organism: Ricinus communis


organism: Saccharum officinarum


organism: Enterococcus faecalis

substrate_name: DNA; Deoxynucleoside triphosphate

substrate: DNA; Deoxynucleoside triphosphate


organism: Thermus sp.


enzyme_display_name: exo-alpha-sialidase

organism: Clostridium chauvoei

substrate_name: fetuin

enzyme: exo-alpha-sialidase

substrate: fetuin


organism: Clostridium perfringens


organism: Corynebacterium diphtheriae

substrate_name: alpha-sialyllactose

substrate: alpha-sialyllactose


organism: Corynebacterium ulcerans

substrate_name: sialyllactose

substrate: sialyllactose


organism: Entamoeba histolytica


organism: Actinomyces viscosus


organism: Akkermansia muciniphila

proof_lines:
isoform Am0705, at pH 6.5 and 37°C
isoform Am0707, at pH 6.5 and 37°C
isoform Am2085, at pH 6.5 and 37°C


organism: Arthrobacter sp.

substrate_name: N-acetylneuraminyllactose

substrate: N-acetylneuraminyllactose


organism: Aspergillus fumigatus


organism: Bifidobacterium bifidum


organism: Bos taurus


organism: Staphylococcus aureus

substrate_name: Deoxynucleoside triphosphate; DNA

substrate: Deoxynucleoside triphosphate; DNA


organism: Erysipelothrix rhusiopathiae


organism: Homo sapiens

substrate_name: ganglioside GD1b

proof_lines: 37°C, pH 5.6 or 7.0, without Triton X-100

proof_lines: 37°C, pH 5.6 or 7.0 activated by 0.02% Triton X-100

substrate: ganglioside GD1b


organism: Human respirovirus 1


organism: influenza A virus


organism: influenza A virus H1N1

proof_lines: mutant enzyme D199E, at 37°C, pH not specified in the publication


organism: unidentified influenza virus

proof_lines: mutant enzyme R152K, at 37°C, pH not specified in the publication


proof_lines: mutant enzyme R152K/V94I, at 37°C, pH not specified in the publication


proof_lines: mutant enzyme R368K, at 37°C, pH not specified in the publication


proof_lines:
recombinant head domain, pH 6.5, 37°C
at pH 7.4 and 37°C
predicted Ki value


organism: Vibrio cholerae serotype O1


enzyme_display_name: mandelate racemase

organism: Pseudomonas putida

substrate_name: (R)-mandelate

proof_lines:
25°C, pH 7.5, mutant enzyme N197A
mutant N197A

enzyme: mandelate racemase

substrate: (R)-mandelate


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Sphingobacterium multivorum


organism: Sphingobacterium sp. HMA12


organism: Streptococcus oralis

substrate_name: alpha1-Acid glycoprotein

substrate: alpha1-Acid glycoprotein


organism: Streptococcus pneumoniae


organism: Streptococcus sp.

substrate_name: bovine submaxillary mucin

substrate: bovine submaxillary mucin


organism: Paraclostridium sordellii


organism: Pasteurella multocida


organism: Photobacterium damselae


organism: Porphyromonas gingivalis

sequence_source: UniProt Q7MX62 direct lookup for PG_0352

proof_lines: in the presence of 200 mM NaCl, at pH 7.4 and 20Â°C

proof_lines: in the absence of NaCl, at pH 7.4 and 20Â°C

proof_lines: in the presence of 200 mM NaCl, at pH 5.6 and 20Â°C


organism: Rattus norvegicus

proof_lines:
glomeruli
cortex
intralysosomal sialidase


organism: Respirovirus muris


organism: Sus scrofa


organism: Trichomonas vaginalis


organism: Trypanosoma cruzi


substrate_name: 4-nitrophenyl alpha-sialoside

substrate: 4-nitrophenyl alpha-sialoside


organism: Trypanosoma evansi

proof_lines: pH 6.5, 37°C, versus 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid


organism: Trypanosoma vivax


organism: unidentified influenza virus


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


proof_lines: mutant enzyme V94I, at 37°C, pH not specified in the publication


organism: Pseudomonas putida

substrate_name: (S)-2-Hydroxy-3-butenoic acid

sequence_source: UniProtKB:P11444 direct EC+organism lookup; reviewed mandelate racemase for Pseudomonas putida with BRENDA EC 5.1.2.2 cross-reference

proof_lines:
in presence of 1 mM Mg2+
4-chloro-D-mandelate
L-mandelate

substrate: (S)-2-Hydroxy-3-butenoic acid


sequence_source: UniProtKB:P11444 direct EC+organism lookup; PubMed/UniProt evidence links PMIDs 7893689 and 7893690 to mandelate racemase catalytic activity

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


sequence_source: Reconstructed E317Q from UniProtKB:P11444 canonical sequence after confirming residue 317 is E; PubMed 7893689 describes the E317Q mutant

sequence_variant_note: Mutation signature E317Q 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:
mutant E317Q
E317Q mutant


substrate_name: (S)-Mandelate

sequence_source: Reconstructed K166R from UniProtKB:P11444 canonical sequence after confirming residue 166 is K; PubMed 7893690 describes the K166R mutant

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

substrate: (S)-Mandelate


organism: influenza A virus H1N1

proof_lines: mutant enzyme P458T, at 37°C, pH not specified in the publication


organism: influenza B virus

substrate_name: Unknown

substrate: Unknown


organism: Micromonospora viridifaciens


organism: Oryctolagus cuniculus


organism: Paenarthrobacter ureafaciens

substrate_name: dipalmitoyl phosphatidylethanolamine-ganglioside GM1 conjugate

proof_lines:
at pH 5.5 and 37°C
strain dependent


enzyme_display_name: acetylcholinesterase

organism: Homo sapiens

substrate_name: Acetylthiocholine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical FASTA with row-specific mutation reconstruction using paper-numbered residue offset +31. and applied mutation signature W86A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

smiles: CC(=O)SCC[N+](C)(C)C

enzyme: acetylcholinesterase

substrate: Acetylthiocholine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical FASTA with row-specific mutation reconstruction using paper-numbered residue offset +31. and applied mutation signature Y124A/E285A/W286A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical FASTA with row-specific mutation reconstruction using paper-numbered residue offset +31. and applied mutation signature Y72A/Y124A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical FASTA with row-specific mutation reconstruction using paper-numbered residue offset +31. and applied mutation signature E285A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


substrate_name: Propionylthiocholine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical FASTA with row-specific mutation reconstruction using paper-numbered residue offset +31. and applied mutation signature Y337F with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

smiles: CCCC(=O)SCC[N+](C)(C)C

substrate: Propionylthiocholine


substrate_name: Butyrylthiocholine

sequence_source: UniProtKB:P22303 canonical FASTA checked; row-specific variant sequence not reconstructed.

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

substrate: Butyrylthiocholine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical FASTA with row-specific mutation reconstruction using paper-numbered residue offset +31. and applied mutation signature F295L/F297V with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


substrate_name: S-Propyl thioacetate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical FASTA with row-specific mutation reconstruction using paper-numbered residue offset +31. and applied mutation signature W286A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

smiles: CCCSC(C)=O

substrate: S-Propyl thioacetate


substrate_name: propionylthiocholine

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

substrate: propionylthiocholine


substrate_name: acetylthiocholine, Acetylthiocholine

substrate: acetylthiocholine, Acetylthiocholine


assay_conditions_summary: pH 7.4; 310.15 K; buffer 0.1 M phosphate

column_label: Table 2. Kinetic parameters of BChE, AChE, and CocH1 against 6-MAM Table 2, 6-MAM row, enzyme column AChE; column 'K_M (uM)' = 259; column 'kcat (min^-1)' = 7.078; column 'k_cat/K_M (min^-1 M^-1)' = 2.73 x 10^4.

normalized_value_unit_evidence: Km: printed cell 259 uM converts to 0.259 mM; the exported value is 0.259 mM. kcat: printed cell 7.078 min^-1 converts to 0.11796666666666666 s^(-1); the exported value is 118.0 s^(-1). kcat/Km: printed cell 2.73 x 10^4 min^-1 M^-1 converts to 0.455 s^(-1)*mM^(-1); the exported value is 455.5984555984556 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2. Kinetic parameters of BChE, AChE, and CocH1 against 6-MAM Table 2, 6-MAM row, enzyme column AChE: Km = 259 uM; kcat = 7.078 min^-1; printed kcat/Km = 2.73 x 10^4 min^-1 M^-1.

row_label: Table 2, 6-MAM row, enzyme column AChE


substrate_name: heroin

assay_conditions_summary: pH 7.4; 310.15 K; buffer heroin in 0.1 M phosphate

column_label: Table 1: Kinetic parameters of BChE, AChE, and CocHl against heroin (Chem Biol Interact 2018, 293:107-114); printed column heads Enzyme | kcat (min^-1) | KM (uM) | kcat/KM (min^-1 M^-1) | RCE | R2. Table 1, enzyme row 'AChE' (wild-type human acetylcholinesterase), substrate heroin; column kcat (min^-1) = 2100; column KM (uM) = 2170; column kcat/KM (min^-1 M^-1) = 9.68 x 10^5; column RCE = 0.06; column R2 = 0.997. captured primary segment: AChE | kcat 2100 min^-1 | KM 2170 uM | kcat/KM 9.68 x 10^5 min^-1 M^-1 | RCE 0.06 | R2 0.997

normalized_value_unit_evidence: kcat: printed Table 1 kcat cell 2100 min^-1; 1 min^-1 is 1/60 s^-1, so 2100 / 60 = 35.0 s^(-1); the exported value is 35.0 s^(-1). Km: printed Table 1 KM cell 2170 uM; 1 uM is 1/1000 mM, so 2170 / 1000 = 2.17 mM; the exported value is 2.17 mM. kcat/Km: printed Table 1 kcat/KM cell 9.68 x 10^5 min^-1 M^-1; 1 min^-1 M^-1 is 1/60000 s^-1 mM^-1, so 9.68 x 10^5 / 60000 = 16.133333333333333 s^(-1)*mM^(-1). Quotient disclosure for this row: 35.0 / 2.17 = 16.129032258064516 s^-1 mM^-1, which is the exported kcat_over_km, and the printed efficiency cell is that quotient written to the three significant figures the table uses.

raw_value_unit_evidence: Table 1, enzyme row 'AChE', substrate heroin: kcat = 2100 min^-1; KM = 2170 uM; printed kcat/KM = 9.68 x 10^5 min^-1 M^-1.

substrate: heroin


substrate_name: p-Nitrophenyl acetate

sequence_source: UniProt REST P22303 canonical sequence; direct lookup on 2026-05-27

substrate: p-Nitrophenyl acetate


sequence_variant_note: Resolved canonical sequence from UniProt REST P22303 canonical sequence; direct lookup on 2026-05-27 and applied mutation signature Y337A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P22303 canonical sequence; direct lookup on 2026-05-27 and applied mutation signature F338A to reconstruct the assayed variant sequence.


organism: Mus musculus

substrate_name: Acetylcholine

sequence_variant_note: Resolved canonical sequence from UniProt REST P21836 canonical sequence; direct lookup on 2026-05-27 and applied mutation signature F297I/Y337A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

smiles: CC(=O)OCC[N+](C)(C)C

substrate: Acetylcholine


sequence_variant_note: Resolved canonical sequence from UniProt REST P21836 canonical sequence; direct lookup on 2026-05-27 and applied mutation signature F295A/Y337A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_source: UniProt REST P21836 canonical sequence; direct lookup on 2026-05-27


sequence_variant_note: Resolved canonical sequence from UniProt REST P21836 canonical sequence; direct lookup on 2026-05-27 and applied mutation signature E202Q/F295L/Y337A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P22303 REST record checked directly; signal peptide 1-31, chain 32-614. and applied mutation signature F297V with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P22303 REST record checked directly; signal peptide 1-31, chain 32-614. and applied mutation signature F338A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P22303 REST record checked directly; signal peptide 1-31, chain 32-614. and applied mutation signature W86A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P22303 REST record checked directly; signal peptide 1-31, chain 32-614. and applied mutation signature F295L with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P22303 REST record checked directly; signal peptide 1-31, chain 32-614. and applied mutation signature W286A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P22303 REST record checked directly; signal peptide 1-31, chain 32-614. and applied mutation signature Y337A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P22303 REST record checked directly; signal peptide 1-31, chain 32-614.


sequence_source: UniProtKB:P21836 direct REST FASTA/JSON; mature-chain mutation positions mapped to precursor sequence with UniProt Signal 1-31 and Chain 32-614.

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +31, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature F295L/Y337A matches the mutant residue at offset +31 and the reference residue at offset +35; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB:P21836 direct REST FASTA/JSON canonical sequence; UniProt reviewed mouse acetylcholinesterase EC 3.1.1.7.


sequence_source: UniProtKB:P22303 canonical sequence; row-specific variant unresolved

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical sequence; HuAChE mature-chain mutation numbering applied at offset +31 and applied mutation signature Y72A/E285A/W286A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical sequence; HuAChE mature-chain mutation numbering applied at offset +31 and applied mutation signature Y124A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical sequence; HuAChE mature-chain mutation numbering applied at offset +31 and applied mutation signature Y72A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical sequence; HuAChE mature-chain mutation numbering applied at offset +31 and applied mutation signature E285A/W286A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical sequence; HuAChE mature-chain mutation numbering applied at offset +31 and applied mutation signature Y72A/E285A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical sequence; HuAChE mature-chain mutation numbering applied at offset +31 and applied mutation signature F297A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical sequence; HuAChE mature-chain mutation numbering applied at offset +31 and applied mutation signature F295A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22303 canonical sequence; HuAChE mature-chain mutation numbering applied at offset +31 and applied mutation signature Y72A/W286A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P21836 (ACES_MOUSE); signal peptide 1-31; mature-enzyme numbering offset +31


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21836 (ACES_MOUSE); signal peptide 1-31; mature-enzyme numbering offset +31 and applied mutation signature W286R with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21836 (ACES_MOUSE); signal peptide 1-31; mature-enzyme numbering offset +31 and applied mutation signature Y72N/D74N/Y124Q/W286A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P21836 and applied mutation signature Y72N/Y124Q/W286A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters for Cholinesterase Wild-Type and Mutant Enzymes), enzyme row 'Y72N/Y124Q/W286A'; column 'Km (uM)' = 230; column 'Kss (mM)' = 14; column 'b' = 0.27; column 'kcat (10^5/min)' = 1.5; column 'kcat/Km (10^9/min M)' = 0.67.

normalized_value_unit_evidence: Km: printed Table I cell 230 uM; 230 / 1000 = 0.23 mM; the exported value is 0.23 mM. kcat: printed Table I cell 1.5 x 10^5 min^-1 = 150000 min^-1; 150000 / 60 = 2500.0 s^-1; the exported value is 2500.0 s^(-1). kcat/Km: the paper's own printed efficiency cell 0.67 x 10^9 M^-1 min^-1 converts to 11166.666666666666 s^-1 mM^-1 because 1 M^-1 min^-1 is 1/60000 s^-1 mM^-1. The quotient of the two printed component cells, re-expressed in the printed column's units, is 0.6522 x 10^9 M^-1 min^-1, which falls outside the rounding interval of the printed cell 0.67 x 10^9, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table I, enzyme row 'Y72N/Y124Q/W286A': Km = 230 uM; kcat = 1.5 x 10^5 min^-1; printed kcat/Km = 0.67 x 10^9 M^-1 min^-1.

row_label: Table I, enzyme row 'Y72N/Y124Q/W286A' (substrate acetylthiocholine)

table_label: Table I: Kinetic Parameters for Cholinesterase Wild-Type and Mutant Enzymes (Biochemistry 1993, 32(45):12074-12084)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21836 (ACES_MOUSE); signal peptide 1-31; mature-enzyme numbering offset +31 and applied mutation signature F297Y with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21836 (ACES_MOUSE); signal peptide 1-31; mature-enzyme numbering offset +31 and applied mutation signature F295Y with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P21836 and applied mutation signature Y124Q with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters for Cholinesterase Wild-Type and Mutant Enzymes), enzyme row 'Y124Q'; column 'Km (uM)' = 120; column 'Kss (mM)' = 25; column 'b' = 0.35; column 'kcat (10^5/min)' = 1.1; column 'kcat/Km (10^9/min M)' = 0.94.

normalized_value_unit_evidence: Km: printed Table I cell 120 uM; 120 / 1000 = 0.12 mM; the exported value is 0.12 mM. kcat: printed Table I cell 1.1 x 10^5 min^-1 = 110000 min^-1; 110000 / 60 = 1833.333 s^-1; the exported value is 1833.333 s^(-1). kcat/Km: the paper's own printed efficiency cell 0.94 x 10^9 M^-1 min^-1 converts to 15666.666666666666 s^-1 mM^-1 because 1 M^-1 min^-1 is 1/60000 s^-1 mM^-1. The quotient of the two printed component cells, re-expressed in the printed column's units, is 0.9167 x 10^9 M^-1 min^-1, which falls outside the rounding interval of the printed cell 0.94 x 10^9, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table I, enzyme row 'Y124Q': Km = 120 uM; kcat = 1.1 x 10^5 min^-1; printed kcat/Km = 0.94 x 10^9 M^-1 min^-1.

row_label: Table I, enzyme row 'Y124Q' (substrate acetylthiocholine)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P21836 (ACES_MOUSE); signal peptide 1-31; mature-enzyme numbering offset +31 and applied mutation signature Y72N with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P21836 (ACES_MOUSE), fetched via UniProt REST FASTA on 2026-05-27; variant reconstructed from source mutation_signature using mature-chain numbering offset +31 because UniProt marks residues 1-31 as signal peptide. and applied mutation signature V300G with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P21836 (ACES_MOUSE), fetched via UniProt REST FASTA on 2026-05-27; variant reconstructed from source mutation_signature using mature-chain numbering offset +31 because UniProt marks residues 1-31 as signal peptide. and applied mutation signature Y72N/W286R with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P21836 and applied mutation signature D74N with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters for Cholinesterase Wild-Type and Mutant Enzymes), enzyme row 'D74N'; column 'Km (uM)' = 1300; column 'Kss (mM)' = 530; column 'b' = 0; column 'kcat (10^5/min)' = 0.84; column 'kcat/Km (10^9/min M)' = 0.063.

normalized_value_unit_evidence: Km: printed Table I cell 1300 uM; 1300 / 1000 = 1.3 mM; the exported value is 1.3 mM. kcat: printed Table I cell 0.84 x 10^5 min^-1 = 84000 min^-1; 84000 / 60 = 1400.0 s^-1; the exported value is 1400.0 s^(-1). kcat/Km: the paper's own printed efficiency cell 0.063 x 10^9 M^-1 min^-1 converts to 1050.0 s^-1 mM^-1 because 1 M^-1 min^-1 is 1/60000 s^-1 mM^-1. The quotient of the two printed component cells, re-expressed in the printed column's units, is 0.0646 x 10^9 M^-1 min^-1, which falls outside the rounding interval of the printed cell 0.063 x 10^9, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table I, enzyme row 'D74N': Km = 1300 uM; kcat = 0.84 x 10^5 min^-1; printed kcat/Km = 0.063 x 10^9 M^-1 min^-1.

row_label: Table I, enzyme row 'D74N' (substrate acetylthiocholine)


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P21836 (ACES_MOUSE), fetched via UniProt REST FASTA on 2026-05-27; variant reconstructed from source mutation_signature using mature-chain numbering offset +31 because UniProt marks residues 1-31 as signal peptide. and applied mutation signature Y72N/Y124Q/W286R with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P21836 (ACES_MOUSE), fetched via UniProt REST FASTA on 2026-05-27; variant reconstructed from source mutation_signature using mature-chain numbering offset +31 because UniProt marks residues 1-31 as signal peptide. and applied mutation signature Y72N/D74N/Y124Q/W286R with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P21836 (ACES_MOUSE), fetched via UniProt REST FASTA on 2026-05-27; variant reconstructed from source mutation_signature using mature-chain numbering offset +31 because UniProt marks residues 1-31 as signal peptide. and applied mutation signature Y124Q/W286R with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P21836 (ACES_MOUSE), fetched via UniProt REST FASTA on 2026-05-27; variant reconstructed from source mutation_signature using mature-chain numbering offset +31 because UniProt marks residues 1-31 as signal peptide. and applied mutation signature F297I with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P21836 (ACES_MOUSE), fetched via UniProt REST FASTA on 2026-05-27; variant reconstructed from source mutation_signature using mature-chain numbering offset +31 because UniProt marks residues 1-31 as signal peptide. and applied mutation signature Y337F with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P21836 reviewed canonical precursor sequence; F295L reconstructed on the mature acetylcholinesterase chain by applying UniProt chain start 32 as a +31 precursor offset. and applied mutation signature F295L with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P21836 and applied mutation signature Y337A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters for Cholinesterase Wild-Type and Mutant Enzymes), enzyme row 'Y337A'; column 'Km (uM)' = 110; column 'Kss (mM)' = 29; column 'b' = 0.59; column 'kcat (10^5/min)' = 0.52; column 'kcat/Km (10^9/min M)' = 0.46.

normalized_value_unit_evidence: Km: printed Table I cell 110 uM; 110 / 1000 = 0.11 mM; the exported value is 0.11 mM. kcat: printed Table I cell 0.52 x 10^5 min^-1 = 52000 min^-1; 52000 / 60 = 866.667 s^-1; the exported value is 866.667 s^(-1). kcat/Km: the paper's own printed efficiency cell 0.46 x 10^9 M^-1 min^-1 converts to 7666.666666666667 s^-1 mM^-1 because 1 M^-1 min^-1 is 1/60000 s^-1 mM^-1. The quotient of the two printed component cells, re-expressed in the printed column's units, is 0.4727 x 10^9 M^-1 min^-1, which falls outside the rounding interval of the printed cell 0.46 x 10^9, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table I, enzyme row 'Y337A': Km = 110 uM; kcat = 0.52 x 10^5 min^-1; printed kcat/Km = 0.46 x 10^9 M^-1 min^-1.

row_label: Table I, enzyme row 'Y337A' (substrate acetylthiocholine)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P21836 and applied mutation signature F295L/F297I with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters for Cholinesterase Wild-Type and Mutant Enzymes), enzyme row 'F295L/F297I'; column 'Km (uM)' = 200; column 'Kss (mM)' = 83; column 'b' = 0.67; column 'kcat (10^5/min)' = 0.12; column 'kcat/Km (10^9/min M)' = 0.059.

normalized_value_unit_evidence: Km: printed Table I cell 200 uM; 200 / 1000 = 0.2 mM; the exported value is 0.2 mM. kcat: printed Table I cell 0.12 x 10^5 min^-1 = 12000 min^-1; 12000 / 60 = 200.0 s^-1; the exported value is 200.0 s^(-1). kcat/Km: the paper's own printed efficiency cell 0.059 x 10^9 M^-1 min^-1 converts to 983.3333333333334 s^-1 mM^-1 because 1 M^-1 min^-1 is 1/60000 s^-1 mM^-1. The quotient of the two printed component cells, re-expressed in the printed column's units, is 0.0600 x 10^9 M^-1 min^-1, which falls outside the rounding interval of the printed cell 0.059 x 10^9, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table I, enzyme row 'F295L/F297I': Km = 200 uM; kcat = 0.12 x 10^5 min^-1; printed kcat/Km = 0.059 x 10^9 M^-1 min^-1.

row_label: Table I, enzyme row 'F295L/F297I' (substrate acetylthiocholine)


enzyme_display_name: beta-lactamase

organism: Aeromonas enteropelogenes

substrate_name: ceftriaxone

sequence_source: UniProtKB:B2BSN6 direct REST lookup on 2026-05-27

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

column_label: Table 3. Kinetic parameters of TRU-1, CAV-1, and AmpC beta-lactamases; row Ceftriaxone; TRU-1 columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 0.042, 6, 7.0 × 10^3

raw_value_unit_evidence: TRU-1 / Ceftriaxone: kcat=0.042 s^-1; Km=6 uM; kcat/Km=7.0 × 10^3 M^-1 s^-1

row_label: TRU-1 / Ceftriaxone

enzyme: beta-lactamase

substrate: ceftriaxone


organism: Aeromonas hydrophila

substrate_name: biapenem

sequence_source: UniProtKB:P26918 direct REST lookup on 2026-05-27

column_label: PMID 15588826 DOI 10.1016/j.jmb.2004.10.070 Table 1; row Wild-type; biapenem columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 1 wild-type CphA biapenem: kcat 300 s^-1; Km 166 uM; kcat/Km 1.8 x 10^6 M^-1 s^-1.

row_label: Wild-type / Biapenem

table_label: Table 1. Kinetic parameters of the wild type and selected mutants of CphA

substrate: biapenem


substrate_name: Imipenem

sequence_variant_note: Mutation signature N220G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: Imipenem


substrate_name: Cephaloridine

sequence_variant_note: Mutation signature N116H/R121H/N220G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: Cephaloridine


sequence_variant_note: Mutation signature N116H/N220G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: Penicillin G

substrate: Penicillin G


substrate_name: cefotaxime

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

substrate: cefotaxime


substrate_name: Nitrocefin

substrate: Nitrocefin


substrate_name: Ampicillin

substrate: Ampicillin


substrate_name: cefoxitin

assay_conditions_summary: pH 7; 303.15 K; buffer 50 mM HEPES

column_label: Table label: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f. Row: Cefoxitin. Enzyme column group: TRU-1. Columns read: k cat (s^-1) cell 0.88, K m (uM) cell 0.025, k cat / K m (M^-1 s^-1) cell 3.5 x 10^7. metric: kcat; raw value: 0.88; raw unit: s^-1; normalized value: 0.88 s^(-1); metric: Km; raw value: 0.025; raw unit: uM; normalized value: 0.000025 mM; metric: kcat/Km; raw unit: M^-1 s^-1; normalized value: 35200.0 s^-1 mM^-1; assay condition: Purified TRU-1 beta-lactamase; steady-state kinetic parameters for the hydrolysis of beta-lactam substrates were determined at 30°C with 50 mM HEPES buffer (pH 7.0); the enzyme concentration in the assay mixtures ranged between 0.2 and 450 nM. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: TRU-1 columns of Table 3 row Cefoxitin: kcat 0.88 s^-1 = 0.88 s^(-1); Km 0.025 uM = 0.000025 mM (1 uM = 0.001 mM); kcat/Km 35200.0 s^-1 mM^-1. In the table asset the multiplication sign renders as ×, the superscript minus one as −1, the micro sign as μ, and superscript exponents are flattened, so the printed cell `3.5 × 10 7` is the paper's 3.5 x 10^7 M^-1 s^-1.

raw_value_unit_evidence: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f | column group header row of Table 3: TRU-1 b CAV-1 AmpC TRU-1 CAV-1 AmpC TRU-1 c CAV-1 AmpC; metric header row: Substrate k cat (s −1 ) K m (μM) k cat / K m (M −1 ·s −1 ) | row: Cefoxitin 0.88 0.5 0.2 0.025 a 0.4 0.65 3.5 × 10 7 1.3 × 10 6 3.0 × 10 5 | TRU-1 cells read: k cat = 0.88 s^-1; K m = 0.025 uM; k cat / K m = 3.5 x 10^7 M^-1 s^-1

row_label: TRU-1 | Cefoxitin

substrate: cefoxitin


substrate_name: penicillin G

column_label: Table label: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f. Row: Penicillin G. Enzyme column group: TRU-1. Columns read: k cat (s^-1) cell 27, K m (uM) cell 2, k cat / K m (M^-1 s^-1) cell 1.4 x 10^7. metric: kcat; raw value: 27; raw unit: s^-1; normalized value: 27.0 s^(-1); metric: Km; raw value: 2; raw unit: uM; normalized value: 0.002 mM; metric: kcat/Km; raw unit: M^-1 s^-1; normalized value: 13500.0 s^-1 mM^-1; assay condition: Purified TRU-1 beta-lactamase; steady-state kinetic parameters for the hydrolysis of beta-lactam substrates were determined at 30°C with 50 mM HEPES buffer (pH 7.0); the enzyme concentration in the assay mixtures ranged between 0.2 and 450 nM. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: TRU-1 columns of Table 3 row Penicillin G: kcat 27 s^-1 = 27.0 s^(-1); Km 2 uM = 0.002 mM (1 uM = 0.001 mM); kcat/Km 13500.0 s^-1 mM^-1. In the table asset the multiplication sign renders as ×, the superscript minus one as −1, the micro sign as μ, and superscript exponents are flattened, so the printed cell `1.4 × 10 7` is the paper's 1.4 x 10^7 M^-1 s^-1.

raw_value_unit_evidence: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f | column group header row of Table 3: TRU-1 b CAV-1 AmpC TRU-1 CAV-1 AmpC TRU-1 c CAV-1 AmpC; metric header row: Substrate k cat (s −1 ) K m (μM) k cat / K m (M −1 ·s −1 ) | row: Penicillin G 27 5 45 2 a 8.7 4.4 1.4 × 10 7 5.7 × 10 5 1.0 × 10 7 | TRU-1 cells read: k cat = 27 s^-1; K m = 2 uM; k cat / K m = 1.4 x 10^7 M^-1 s^-1

row_label: TRU-1 | Penicillin G

substrate: penicillin G


column_label: Table label: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f. Row: Cefotaxime. Enzyme column group: TRU-1. Columns read: k cat (s^-1) cell 0.015, K m (uM) cell 0.0009, k cat / K m (M^-1 s^-1) cell 1.7 x 10^7. metric: kcat; raw value: 0.015; raw unit: s^-1; normalized value: 0.015 s^(-1); metric: Km; raw value: 0.0009; raw unit: uM; normalized value: 0.0000009 mM; metric: kcat/Km; raw unit: M^-1 s^-1; normalized value: 16666.666666666668 s^-1 mM^-1; assay condition: Purified TRU-1 beta-lactamase; steady-state kinetic parameters for the hydrolysis of beta-lactam substrates were determined at 30°C with 50 mM HEPES buffer (pH 7.0); the enzyme concentration in the assay mixtures ranged between 0.2 and 450 nM. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: TRU-1 columns of Table 3 row Cefotaxime: kcat 0.015 s^-1 = 0.015 s^(-1); Km 0.0009 uM = 0.0000009 mM (1 uM = 0.001 mM); kcat/Km 16666.666666666668 s^-1 mM^-1. In the table asset the multiplication sign renders as ×, the superscript minus one as −1, the micro sign as μ, and superscript exponents are flattened, so the printed cell `1.7 × 10 7` is the paper's 1.7 x 10^7 M^-1 s^-1.

raw_value_unit_evidence: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f | column group header row of Table 3: TRU-1 b CAV-1 AmpC TRU-1 CAV-1 AmpC TRU-1 c CAV-1 AmpC; metric header row: Substrate k cat (s −1 ) K m (μM) k cat / K m (M −1 ·s −1 ) | row: Cefotaxime 0.015 0.2 0.17 0.0009 a 0.1 1.7 1.7 × 10 7 2.0 × 10 6 1.0 × 10 5 | TRU-1 cells read: k cat = 0.015 s^-1; K m = 0.0009 uM; k cat / K m = 1.7 x 10^7 M^-1 s^-1

row_label: TRU-1 | Cefotaxime


substrate_name: ceftazidime

column_label: Table label: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f. Row: Ceftazidime. Enzyme column group: TRU-1. Columns read: k cat (s^-1) cell 0.11, K m (uM) cell 0.12, k cat / K m (M^-1 s^-1) cell 9.2 x 10^5. metric: kcat; raw value: 0.11; raw unit: s^-1; normalized value: 0.11 s^(-1); metric: Km; raw value: 0.12; raw unit: uM; normalized value: 0.00012 mM; metric: kcat/Km; raw unit: M^-1 s^-1; normalized value: 916.6666666666666 s^-1 mM^-1; assay condition: Purified TRU-1 beta-lactamase; steady-state kinetic parameters for the hydrolysis of beta-lactam substrates were determined at 30°C with 50 mM HEPES buffer (pH 7.0); the enzyme concentration in the assay mixtures ranged between 0.2 and 450 nM. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: TRU-1 columns of Table 3 row Ceftazidime: kcat 0.11 s^-1 = 0.11 s^(-1); Km 0.12 uM = 0.00012 mM (1 uM = 0.001 mM); kcat/Km 916.6666666666666 s^-1 mM^-1. In the table asset the multiplication sign renders as ×, the superscript minus one as −1, the micro sign as μ, and superscript exponents are flattened, so the printed cell `9.2 × 10 5` is the paper's 9.2 x 10^5 M^-1 s^-1.

raw_value_unit_evidence: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f | column group header row of Table 3: TRU-1 b CAV-1 AmpC TRU-1 CAV-1 AmpC TRU-1 c CAV-1 AmpC; metric header row: Substrate k cat (s −1 ) K m (μM) k cat / K m (M −1 ·s −1 ) | row: Ceftazidime 0.11 0.2 0.12 a 0.6 9.2 × 10 5 3.3 × 10 5 | TRU-1 cells read: k cat = 0.11 s^-1; K m = 0.12 uM; k cat / K m = 9.2 x 10^5 M^-1 s^-1

row_label: TRU-1 | Ceftazidime

substrate: ceftazidime


substrate_name: piperacillin

column_label: Table label: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f. Row: Piperacillin. Enzyme column group: TRU-1. Columns read: k cat (s^-1) cell 0.54, K m (uM) cell 0.2, k cat / K m (M^-1 s^-1) cell 2.7 x 10^6. metric: kcat; raw value: 0.54; raw unit: s^-1; normalized value: 0.54 s^(-1); metric: Km; raw value: 0.2; raw unit: uM; normalized value: 0.0002 mM; metric: kcat/Km; raw unit: M^-1 s^-1; normalized value: 2700.0 s^-1 mM^-1; assay condition: Purified TRU-1 beta-lactamase; steady-state kinetic parameters for the hydrolysis of beta-lactam substrates were determined at 30°C with 50 mM HEPES buffer (pH 7.0); the enzyme concentration in the assay mixtures ranged between 0.2 and 450 nM. Export row conditions: pH 7; 303.15 K.

normalized_value_unit_evidence: TRU-1 columns of Table 3 row Piperacillin: kcat 0.54 s^-1 = 0.54 s^(-1); Km 0.2 uM = 0.0002 mM (1 uM = 0.001 mM); kcat/Km 2700.0 s^-1 mM^-1. In the table asset the multiplication sign renders as ×, the superscript minus one as −1, the micro sign as μ, and superscript exponents are flattened, so the printed cell `2.7 × 10 6` is the paper's 2.7 x 10^6 M^-1 s^-1.

raw_value_unit_evidence: TABLE 3. Kinetic parameters of the purified TRU-1 β-lactamase f | column group header row of Table 3: TRU-1 b CAV-1 AmpC TRU-1 CAV-1 AmpC TRU-1 c CAV-1 AmpC; metric header row: Substrate k cat (s −1 ) K m (μM) k cat / K m (M −1 ·s −1 ) | row: Piperacillin 0.54 0.2 a 2.7 × 10 6 | TRU-1 cells read: k cat = 0.54 s^-1; K m = 0.2 uM; k cat / K m = 2.7 x 10^6 M^-1 s^-1

row_label: TRU-1 | Piperacillin

substrate: piperacillin


organism: Achromobacter sp. sallbros1

substrate_name: ampicillin

sequence_source: UniProtKB:E7BCS7 direct lookup

assay_conditions_summary: pH 7.2; 298.15 K; buffer 50 mM HEPES

column_label: Table label: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1. Row: Ampicillin. Enzyme column group: TMB-1. Columns read: k cat (s^-1) cell 3.3, K m (uM) cell 27, k cat / K m (s^-1/uM) cell 0.122. metric: kcat; raw value: 3.3; raw unit: s^-1; normalized value: 3.3 s^(-1); metric: Km; raw value: 27; raw unit: uM; normalized value: 0.027 mM; metric: kcat/Km; raw value: 0.122; raw unit: s^-1/uM; normalized value: 122 s^-1 mM^-1; independently reported primary cell: true; assay condition: Purified TMB-1 metallo-beta-lactamase; steady-state kinetics were performed at 25 degrees C in a spectrophotometer using 96-well plates; all substrates were tested as duplicates using 50 mM HEPES buffer, pH 7.2, 100 uM ZnCl2, 0.02% NaN3, and 0.1 mg/ml bovine serum albumin as a buffer system. Export row conditions: pH 7.2; 298.15 K.

normalized_value_unit_evidence: TMB-1 columns of Table 2 row Ampicillin: kcat 3.3 s^-1 = 3.3 s^(-1); Km 27 uM = 0.027 mM (1 uM = 0.001 mM); kcat/Km primary cell 0.122 s^-1/uM = 122 s^-1 mM^-1 (1 s^-1/uM = 1000 s^-1 mM^-1). In the table asset the micro sign renders as μ, the superscript minus one as −1, and superscript markers are flattened, so the printed header cells read `k cat (s −1 )`, `K m (μM)` and `k cat / K m (s −1 /μM)`.

raw_value_unit_evidence: Table 2. Steady-state kinetic constants of TMB-1, DIM-1, and GIM-1 | enzyme column group header row of Table 2: TMB-1 DIM-1 a GIM-1 b; metric header row: k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) k cat (s −1 ) K m (μM) k cat / K m (s −1 /μM) | row: Ampicillin 3.3 27 0.122 20 110 0.182 3.3 20 0.165 | TMB-1 cells read: k cat = 3.3 s^-1; K m = 27 uM; k cat / K m = 0.122 s^-1/uM

row_label: TMB-1 | Ampicillin

substrate: ampicillin


sequence_source: UniProtKB:E7BCS5 canonical sequence; NCBI FR771847 protein_id CBY88906.1


substrate_name: meropenem

substrate: meropenem


substrate_name: ertapenem

substrate: ertapenem


substrate_name: cefuroxime

substrate: cefuroxime


substrate_name: azlocillin

sequence_source: UniProtKB:P26918 direct FASTA lookup; reviewed Swiss-Prot BLAB_AERHY/cphA

assay_conditions_summary: pH 6.5; 303.15 K; buffer 30 mM sodium cacodylate

column_label: Table label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa. Row: Azlocillin. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 90 ± 5, kcat (s^-1) cell 0.18, kcat/Km (M^-1 s^-1) cell 2.00 x 10^3 M^-1 s^-1. Km 90 ± 5 uM normalizes to 0.09 mM and equals the exported km; kcat 0.18 s^-1 equals the exported kcat; the table's printed kcat/Km cell 2.00 x 10^3 M^-1 s^-1 normalizes to 2.0 s^-1 mM^-1 and decimal-matches the exported kcat_over_km.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 4 row Azlocillin: Km 90 ± 5 uM = 0.09 mM; kcat 0.18 s^-1 = 0.18 s^-1; kcat/Km 2.0 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Azlocillin 90 6 5 0.18 2.00 3 103 170 6 10 205 1.20 3 106 6 6 0.1b 75 1.30 3 107

row_label: A. hydrophila AE036 | Azlocillin

substrate: azlocillin


substrate_name: Sulbenicillin

column_label: Table label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa. Row: Sulbenicillin. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 230 ± 10, kcat (s^-1) cell 0.50, kcat/Km (M^-1 s^-1) cell 2.10 x 10^3 M^-1 s^-1. Km 230 ± 10 uM normalizes to 0.23 mM and equals the exported km; kcat 0.50 s^-1 equals the exported kcat; the exported kcat_over_km 2.1739130434782608 s^-1 mM^-1 is the exact quotient of those same two printed cells, and the table's own printed kcat/Km cell 2.10 x 10^3 M^-1 s^-1 = 2.1 s^-1 mM^-1 is that same quantity at the three-significant-figure precision the table prints.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 4 row Sulbenicillin: Km 230 ± 10 uM = 0.23 mM; kcat 0.50 s^-1 = 0.5 s^-1; kcat/Km 2.1739130434782608 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Sulbenicillin 230 6 10 0.50 2.10 3 103 .2,000 .300 1.93 3 105c 190 6 5 225 1.20 3 106

row_label: A. hydrophila AE036 | Sulbenicillin

substrate: Sulbenicillin


substrate_name: Cefsulodin

column_label: Table label: TABLE 5. Kinetic parameters of metallo-b-lactamases with cephalosporins (D3-cephems)a. Row: Cefsulodin. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 130 ± 10, kcat (s^-1) cell 0.05, kcat/Km (M^-1 s^-1) cell 3.50 x 10^2 M^-1 s^-1. Km 130 ± 10 uM normalizes to 0.13 mM and equals the exported km; kcat 0.05 s^-1 equals the exported kcat; the exported kcat_over_km 0.38461538461538464 s^-1 mM^-1 is the exact quotient of those same two printed cells, and the table's own printed kcat/Km cell 3.50 x 10^2 M^-1 s^-1 = 0.35 s^-1 mM^-1 is that same quantity at the three-significant-figure precision the table prints.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 5 row Cefsulodin: Km 130 ± 10 uM = 0.13 mM; kcat 0.05 s^-1 = 0.05 s^-1; kcat/Km 0.38461538461538464 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 5. Kinetic parameters of metallo-b-lactamases with cephalosporins (D3-cephems)a | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Cefsulodin 130 6 10 0.05 3.50 3 102 230 6 20 12.5 5.40 3 104 5 6 0.3d 7.5 1.50 3 106

row_label: A. hydrophila AE036 | Cefsulodin

substrate: Cefsulodin


column_label: Table label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa. Row: Piperacillin. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 55 ± 2, kcat (s^-1) cell 0.43, kcat/Km (M^-1 s^-1) cell 7.80 x 10^3 M^-1 s^-1. Km 55 ± 2 uM normalizes to 0.055 mM and equals the exported km; kcat 0.43 s^-1 equals the exported kcat; the exported kcat_over_km 7.818181818181818 s^-1 mM^-1 is the exact quotient of those same two printed cells, and the table's own printed kcat/Km cell 7.80 x 10^3 M^-1 s^-1 = 7.8 s^-1 mM^-1 is that same quantity at the three-significant-figure precision the table prints.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 4 row Piperacillin: Km 55 ± 2 uM = 0.055 mM; kcat 0.43 s^-1 = 0.43 s^-1; kcat/Km 7.818181818181818 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Piperacillin 55 6 2 0.43 7.80 3 103 450 6 10 75 1.70 3 105 20 6 1 140 7.00 3 106

row_label: A. hydrophila AE036 | Piperacillin


substrate_name: Imipenem

substrate: Imipenem


substrate_name: Talampicillin

sequence_source: UniProt P26918 FASTA; direct lookup on rest.uniprot.org

column_label: Table label: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa. Row: Talampicillin. Enzyme column group: A. hydrophila AE036. Columns read: Km (uM) cell 90 ± 10, kcat (s^-1) cell 0.04, kcat/Km (M^-1 s^-1) cell 5.00 x 10^2 M^-1 s^-1. Km 90 ± 10 uM normalizes to 0.09 mM and equals the exported km; kcat 0.04 s^-1 equals the exported kcat; the exported kcat_over_km 0.4444444444444445 s^-1 mM^-1 is the exact quotient of those same two printed cells, and the table's own printed kcat/Km cell 5.00 x 10^2 M^-1 s^-1 = 0.5 s^-1 mM^-1 is that same quantity at the three-significant-figure precision the table prints.

normalized_value_unit_evidence: A. hydrophila AE036 columns of Table 4 row Talampicillin: Km 90 ± 10 uM = 0.09 mM; kcat 0.04 s^-1 = 0.04 s^-1; kcat/Km 0.4444444444444445 s^-1 mM^-1. In the PDF text layer the multiplication sign renders as `3`, the plus/minus sign as `6`, superscript -1 as `21`, and the micro sign as `m`, so the printed Km column header `(mM)` is the paper's `(uM)`.

raw_value_unit_evidence: TABLE 4. Kinetic parameters of metallo-b-lactamases with penicillinsa | enzyme column group: A. hydrophila AE036 | column header: Antibiotic Km kcat kcat/Km Km kcat kcat/Km Km kcat kcat/Km / (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) (mM) (s21) (M21 s21) | row: Talampicillin 90 6 10 0.04 5.00 3 102 —d — — 160 6 5 220 6.50 3 105

row_label: A. hydrophila AE036 | Talampicillin

substrate: Talampicillin