column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2006, volume 54, number 10, pages 3585-3590); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 3, MTSase form block Y409F, transglycosylation column G5; printed row label kcat (s-1) = 267; printed row label KM (mM) = 5.85; printed row label kcat/KM (s-1 mM-1) = 45.5. captured primary segment: Y409F MTSase | maltopentaose G5 | kcat 267 s^-1 | KM 5.85 mM | kcat/KM 45.5 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 5.85 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 5.85 mM. kcat: printed Table 3 kcat cell 267 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 267.0 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 45.5 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 45.5 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 267 / 5.85 = 45.64102564102564 s^-1 mM^-1, against the printed catalytic-efficiency cell 45.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, MTSase form block Y409F, transglycosylation column G5: kcat = 267 s^-1; KM = 5.85 mM; printed kcat/KM = 45.5 s^-1 mM^-1.

row_label: Table 3, MTSase form block Y409F, transglycosylation column G5 (maltopentaose)


organism: Saccharolobus solfataricus

substrate_name: maltoheptaose

source_db: brenda

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P95869 and applied mutation signature Y409F to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 5; 333.15 K; buffer 50 mM citrate phosphate

column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2006, volume 54, number 10, pages 3585-3590); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 3, MTSase form block Y409F, transglycosylation column G7; printed row label kcat (s-1) = 282; printed row label KM (mM) = 3.8; printed row label kcat/KM (s-1 mM-1) = 74.5. captured primary segment: Y409F MTSase | maltoheptaose G7 | kcat 282 s^-1 | KM 3.8 mM | kcat/KM 74.5 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 3.8 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 3.8 mM. kcat: printed Table 3 kcat cell 282 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 282.0 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 74.5 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 74.5 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 282 / 3.8 = 74.21052631578948 s^-1 mM^-1, against the printed catalytic-efficiency cell 74.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, MTSase form block Y409F, transglycosylation column G7: kcat = 282 s^-1; KM = 3.8 mM; printed kcat/KM = 74.5 s^-1 mM^-1.

row_label: Table 3, MTSase form block Y409F, transglycosylation column G7 (maltoheptaose)

data_origin: experimental

substrate: maltoheptaose

status: corrected

source: brenda


substrate_name: maltohexaose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y409F to reconstruct the assayed variant sequence.

substrate: maltohexaose


substrate_name: maltopentaose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F405Y to reconstruct the assayed variant sequence.

substrate: maltopentaose


verification_status: verified

mutation_signature: Unknown

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 Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2006, volume 54, number 10, pages 3585-3590); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 3, MTSase form block wild-type, transglycosylation column G6; printed row label kcat (s-1) = 359; printed row label KM (mM) = 4.53; printed row label kcat/KM (s-1 mM-1) = 79.2. captured primary segment: wild-type MTSase | maltohexaose G6 | kcat 359 s^-1 | KM 4.53 mM | kcat/KM 79.2 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 4.53 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 4.53 mM. kcat: printed Table 3 kcat cell 359 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 359.0 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 79.2 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 79.2 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 359 / 4.53 = 79.24944812362031 s^-1 mM^-1, against the printed catalytic-efficiency cell 79.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, MTSase form block wild-type, transglycosylation column G6: kcat = 359 s^-1; KM = 4.53 mM; printed kcat/KM = 79.2 s^-1 mM^-1.

row_label: Table 3, MTSase form block wild-type, transglycosylation column G6 (maltohexaose)

status: verified


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P95869 and applied mutation signature F405Y to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2006, volume 54, number 10, pages 3585-3590); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 3, MTSase form block F405Y, transglycosylation column G6; printed row label kcat (s-1) = 362; printed row label KM (mM) = 4.90; printed row label kcat/KM (s-1 mM-1) = 74.0. captured primary segment: F405Y MTSase | maltohexaose G6 | kcat 362 s^-1 | KM 4.90 mM | kcat/KM 74.0 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 4.90 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 4.9 mM. kcat: printed Table 3 kcat cell 362 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 362.0 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 74.0 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 74.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 362 / 4.90 = 73.87755102040816 s^-1 mM^-1, against the printed catalytic-efficiency cell 74.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, MTSase form block F405Y, transglycosylation column G6: kcat = 362 s^-1; KM = 4.90 mM; printed kcat/KM = 74.0 s^-1 mM^-1.

row_label: Table 3, MTSase form block F405Y, transglycosylation column G6 (maltohexaose)


column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2006, volume 54, number 10, pages 3585-3590); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 3, MTSase form block F405Y, transglycosylation column G7; printed row label kcat (s-1) = 363; printed row label KM (mM) = 3.80; printed row label kcat/KM (s-1 mM-1) = 95.6. captured primary segment: F405Y MTSase | maltoheptaose G7 | kcat 363 s^-1 | KM 3.80 mM | kcat/KM 95.6 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 3.80 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 3.8 mM. kcat: printed Table 3 kcat cell 363 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 363.0 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 95.6 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 95.6 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 363 / 3.80 = 95.52631578947368 s^-1 mM^-1, against the printed catalytic-efficiency cell 95.6 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, MTSase form block F405Y, transglycosylation column G7: kcat = 363 s^-1; KM = 3.80 mM; printed kcat/KM = 95.6 s^-1 mM^-1.

row_label: Table 3, MTSase form block F405Y, transglycosylation column G7 (maltoheptaose)


kcat_over_km_origin: calculated

proof_lines:
wild-type, pH 5.0, 60°C
pH 5, 60°C, wild-type enzyme
pH 5.0, 60°C, wild-type enzyme


column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2006, volume 54, number 10, pages 3585-3590); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 3, MTSase form block wild-type, transglycosylation column G7; printed row label kcat (s-1) = 383; printed row label KM (mM) = 3.88; printed row label kcat/KM (s-1 mM-1) = 98.8. captured primary segment: wild-type MTSase | maltoheptaose G7 | kcat 383 s^-1 | KM 3.88 mM | kcat/KM 98.8 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 3.88 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 3.88 mM. kcat: printed Table 3 kcat cell 383 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 383.0 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 98.8 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 98.8 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 383 / 3.88 = 98.71134020618557 s^-1 mM^-1, against the printed catalytic-efficiency cell 98.8 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, MTSase form block wild-type, transglycosylation column G7: kcat = 383 s^-1; KM = 3.88 mM; printed kcat/KM = 98.8 s^-1 mM^-1.

row_label: Table 3, MTSase form block wild-type, transglycosylation column G7 (maltoheptaose)


enzyme_display_name: isomaltulose synthase

organism: Serratia plymuthica

substrate_name: sucrose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q181P/D398G/F453Y with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

proof_lines: pH 5.5, 20°C, mutant enzyme Q181P/D398G/F453Y

enzyme: isomaltulose synthase

substrate: sucrose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y219L/T369F/D398G/F453Y with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

proof_lines: pH 5.5, 20°C, mutant enzyme Y219L/T369F/D398G/F453Y


sequence_variant_note: Mutation signature Y219L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y219L/D398G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature V465E could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R614A to reconstruct the assayed variant sequence.

proof_lines:
pH 5, 60°C, mutant enzyme R614A
pH 5.0, 60°C, mutant enzyme R614A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D411A to reconstruct the assayed variant sequence.

proof_lines:
pH 5, 60°C, mutant enzyme D411A
pH 5.0, 60°C, mutant enzyme D411A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D610A to reconstruct the assayed variant sequence.

proof_lines:
pH 5, 60°C, mutant enzyme D610A
pH 5.0, 60°C, mutant enzyme D610A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P402Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V426T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A406S to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature K576D references residue 576, which is outside the resolved sequence length.

assay_conditions_summary: pH 6


sequence_variant_note: Mutation signature E175N/K576D references residue 576, which is outside the resolved sequence length.

proof_lines: recombinant mutant E175N/K576D, pH 6.0, 30°C


sequence_variant_note: Mutation signature E175N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: isobutyryl-CoA mutase

organism: Geobacillus kaustophilus (strain HTA426)

substrate_name: isobutyryl-CoA (in the absence of nucleotides, at pH 7.5 and 37 degrees Celsius)

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: kcat is 3.1 sec(-1) for ICM activity in the absence of nucleotides, at pH 7.5 and 37 degrees Celsius. Activity might be 4-fold higher at 60 degrees Celsius, the optimal growth temperature for this organism. kcat is 1.96 sec(-1) for ICM acti

enzyme: isobutyryl-CoA mutase

source: uniprot


substrate_name: GTP (at 37 degrees Celsius)

substrate: GTP (at 37 degrees Celsius)


organism: Klebsiella pneumoniae

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

proof_lines: recombinant enzyme, pH not specified in the publication, 35°C

proof_lines: pH and temperature not specified in the publication


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

sequence_source: multiple

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

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

proof_lines: native enzyme, pH not specified in the publication, 30°C

source_databases_merged: brenda skid


organism: Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)

proof_lines: kcat is 18 min(-1) for GTPase activity (at 37 degrees Celsius).


organism: Arthrobacter ramosus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G415P to reconstruct the assayed variant sequence.


enzyme_display_name: maltose alpha-D-glucosyltransferase

organism: Thermus aquaticus

substrate_name: maltose

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

enzyme: maltose alpha-D-glucosyltransferase

substrate: maltose


substrate_name: trehalose

substrate: trehalose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S44P to reconstruct the assayed variant sequence.


organism: Sulfolobus acidocaldarius


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P95869 and applied mutation signature F206Y to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2007, volume 55, number 14, pages 5588-5594); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 2, MTSase form block F206Y, transglycosylation column G6; printed row label kcat (s-1) = 6.11; printed row label KM (mM) = 2.48; printed row label kcat/KM (s-1 mM-1) = 2.47. captured primary segment: F206Y MTSase | maltohexaose G6 | kcat 6.11 s^-1 | KM 2.48 mM | kcat/KM 2.47 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 2.48 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 2.48 mM. kcat: printed Table 2 kcat cell 6.11 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 6.11 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 2.47 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 2.47 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 6.11 / 2.48 = 2.463709677419355 s^-1 mM^-1, against the printed catalytic-efficiency cell 2.47 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MTSase form block F206Y, transglycosylation column G6: kcat = 6.11 s^-1; KM = 2.48 mM; printed kcat/KM = 2.47 s^-1 mM^-1.

row_label: Table 2, MTSase form block F206Y, transglycosylation column G6 (maltohexaose)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P95869 and applied mutation signature F206W to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2007, volume 55, number 14, pages 5588-5594); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 2, MTSase form block F206W, transglycosylation column G6; printed row label kcat (s-1) = 11.1; printed row label KM (mM) = 1.93; printed row label kcat/KM (s-1 mM-1) = 5.78. captured primary segment: F206W MTSase | maltohexaose G6 | kcat 11.1 s^-1 | KM 1.93 mM | kcat/KM 5.78 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 1.93 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 1.93 mM. kcat: printed Table 2 kcat cell 11.1 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 11.1 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 5.78 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 5.78 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 11.1 / 1.93 = 5.751295336787565 s^-1 mM^-1, against the printed catalytic-efficiency cell 5.78 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MTSase form block F206W, transglycosylation column G6: kcat = 11.1 s^-1; KM = 1.93 mM; printed kcat/KM = 5.78 s^-1 mM^-1.

row_label: Table 2, MTSase form block F206W, transglycosylation column G6 (maltohexaose)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P95869 and applied mutation signature F207Y to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2007, volume 55, number 14, pages 5588-5594); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 2, MTSase form block F207Y, transglycosylation column G6; printed row label kcat (s-1) = 14.0; printed row label KM (mM) = 2.92; printed row label kcat/KM (s-1 mM-1) = 4.80. captured primary segment: F207Y MTSase | maltohexaose G6 | kcat 14.0 s^-1 | KM 2.92 mM | kcat/KM 4.80 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 2.92 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 2.92 mM. kcat: printed Table 2 kcat cell 14.0 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 14.0 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 4.80 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 4.8 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 14.0 / 2.92 = 4.794520547945205 s^-1 mM^-1, against the printed catalytic-efficiency cell 4.80 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MTSase form block F207Y, transglycosylation column G6: kcat = 14.0 s^-1; KM = 2.92 mM; printed kcat/KM = 4.80 s^-1 mM^-1.

row_label: Table 2, MTSase form block F207Y, transglycosylation column G6 (maltohexaose)


substrate_name: maltotetraose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F405S with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

substrate: maltotetraose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P95869 and applied mutation signature F405W to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2007, volume 55, number 14, pages 5588-5594); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 2, MTSase form block F405W, transglycosylation column G4; printed row label kcat (s-1) = 139; printed row label KM (mM) = 20.6; printed row label kcat/KM (s-1 mM-1) = 6.73. captured primary segment: F405W MTSase | maltotetraose G4 | kcat 139 s^-1 | KM 20.6 mM | kcat/KM 6.73 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 20.6 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 20.6 mM. kcat: printed Table 2 kcat cell 139 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 139.0 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 6.73 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 6.73 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 139 / 20.6 = 6.747572815533981 s^-1 mM^-1, against the printed catalytic-efficiency cell 6.73 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MTSase form block F405W, transglycosylation column G4: kcat = 139 s^-1; KM = 20.6 mM; printed kcat/KM = 6.73 s^-1 mM^-1.

row_label: Table 2, MTSase form block F405W, transglycosylation column G4 (maltotetraose)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P95869 and applied mutation signature F405S to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2007, volume 55, number 14, pages 5588-5594); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 2, MTSase form block F405S, transglycosylation column G7; printed row label kcat (s-1) = 147; printed row label KM (mM) = 2.84; printed row label kcat/KM (s-1 mM-1) = 51.9. captured primary segment: F405S MTSase | maltoheptaose G7 | kcat 147 s^-1 | KM 2.84 mM | kcat/KM 51.9 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 2.84 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 2.84 mM. kcat: printed Table 2 kcat cell 147 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 147.0 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 51.9 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 51.9 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 147 / 2.84 = 51.76056338028169 s^-1 mM^-1, against the printed catalytic-efficiency cell 51.9 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MTSase form block F405S, transglycosylation column G7: kcat = 147 s^-1; KM = 2.84 mM; printed kcat/KM = 51.9 s^-1 mM^-1.

row_label: Table 2, MTSase form block F405S, transglycosylation column G7 (maltoheptaose)


column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2007, volume 55, number 14, pages 5588-5594); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 2, MTSase form block F405S, transglycosylation column G6; printed row label kcat (s-1) = 169; printed row label KM (mM) = 3.75; printed row label kcat/KM (s-1 mM-1) = 45.2. captured primary segment: F405S MTSase | maltohexaose G6 | kcat 169 s^-1 | KM 3.75 mM | kcat/KM 45.2 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 3.75 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 3.75 mM. kcat: printed Table 2 kcat cell 169 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 169.0 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 45.2 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 45.2 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 169 / 3.75 = 45.06666666666667 s^-1 mM^-1, against the printed catalytic-efficiency cell 45.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MTSase form block F405S, transglycosylation column G6: kcat = 169 s^-1; KM = 3.75 mM; printed kcat/KM = 45.2 s^-1 mM^-1.

row_label: Table 2, MTSase form block F405S, transglycosylation column G6 (maltohexaose)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P95869 and applied mutation signature F405M to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2007, volume 55, number 14, pages 5588-5594); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 2, MTSase form block F405M, transglycosylation column G4; printed row label kcat (s-1) = 196; printed row label KM (mM) = 19.0; printed row label kcat/KM (s-1 mM-1) = 10.4. captured primary segment: F405M MTSase | maltotetraose G4 | kcat 196 s^-1 | KM 19.0 mM | kcat/KM 10.4 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 19.0 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 19.0 mM. kcat: printed Table 2 kcat cell 196 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 196.0 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 10.4 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 10.4 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 196 / 19.0 = 10.31578947368421 s^-1 mM^-1, against the printed catalytic-efficiency cell 10.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MTSase form block F405M, transglycosylation column G4: kcat = 196 s^-1; KM = 19.0 mM; printed kcat/KM = 10.4 s^-1 mM^-1.

row_label: Table 2, MTSase form block F405M, transglycosylation column G4 (maltotetraose)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F405M with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F405W with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2007, volume 55, number 14, pages 5588-5594); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 2, MTSase form block F405W, transglycosylation column G7; printed row label kcat (s-1) = 429; printed row label KM (mM) = 5.71; printed row label kcat/KM (s-1 mM-1) = 83.0. captured primary segment: F405W MTSase | maltoheptaose G7 | kcat 429 s^-1 | KM 5.71 mM | kcat/KM 83.0 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 5.71 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 5.71 mM. kcat: printed Table 2 kcat cell 429 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 429.0 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 83.0 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 83.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 429 / 5.71 = 75.13134851138354 s^-1 mM^-1, against the printed catalytic-efficiency cell 83.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MTSase form block F405W, transglycosylation column G7: kcat = 429 s^-1; KM = 5.71 mM; printed kcat/KM = 83.0 s^-1 mM^-1.

row_label: Table 2, MTSase form block F405W, transglycosylation column G7 (maltoheptaose)


column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2007, volume 55, number 14, pages 5588-5594); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 2, MTSase form block F405W, transglycosylation column G6; printed row label kcat (s-1) = 445; printed row label KM (mM) = 5.90; printed row label kcat/KM (s-1 mM-1) = 75.6. captured primary segment: F405W MTSase | maltohexaose G6 | kcat 445 s^-1 | KM 5.90 mM | kcat/KM 75.6 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 5.90 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 5.9 mM. kcat: printed Table 2 kcat cell 445 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 445.0 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 75.6 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 75.6 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 445 / 5.90 = 75.42372881355932 s^-1 mM^-1, against the printed catalytic-efficiency cell 75.6 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MTSase form block F405W, transglycosylation column G6: kcat = 445 s^-1; KM = 5.90 mM; printed kcat/KM = 75.6 s^-1 mM^-1.

row_label: Table 2, MTSase form block F405W, transglycosylation column G6 (maltohexaose)


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197)


substrate_name: maltodextrin

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature T439A/Q585R to reconstruct the assayed variant sequence.

substrate: maltodextrin


substrate_name: short chain amylose

substrate: short chain amylose


organism: Mycolicibacterium smegmatis

substrate_name: 2,4-dinitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)

assay_conditions_summary: pH 6.8; 310.15 K; buffer 40 mM potassium phosphate

proof_lines: in 40 mM potassium phosphate buffer (pH 6.8), at 37°C

source_databases_merged: brenda uniprot


organism: Escherichia coli

substrate_name: CO2; Aminoimidazole ribotide

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

substrate: CO2; Aminoimidazole ribotide


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E263G/F284V/F583L/I611T/S615G to reconstruct the assayed variant sequence.

proof_lines: pH 6.0, 60°C, mutant enzyme E263G/F284V/F583L/I611T/S615G


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature G81S/F284V/S615G to reconstruct the assayed variant sequence.

proof_lines: pH 6.0, 60°C, mutant enzyme G81S/F284V/S615G


enzyme_display_name: squalene--hopene cyclase

organism: Alicyclobacillus acidocaldarius

substrate_name: H2O; Squalene

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

enzyme: squalene--hopene cyclase

substrate: H2O; Squalene


substrate_name: Squalene

proof_lines:
pH 6.0, 60°C
kcat is 72 min(-1).

source_databases_merged: sabio_rk brenda uniprot

substrate: Squalene


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


organism: Klebsiella sp.

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D327R to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature D327N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D329L with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R325D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R325L to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature R329N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Pseudomonas reinekei

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y39F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; buffer phosphate

proof_lines: mutant enzyme Y39F, in phosphate buffer, 50 mM, pH 7.3


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C67S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C67S, in phosphate buffer, 50 mM, pH 7.3


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

proof_lines: wild type enzyme, in phosphate buffer, 50 mM, pH 7.3


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H52A with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H52A, in phosphate buffer, 50 mM, pH 7.3


source_db: skid

proof_lines: kcat is 24.2 sec(-1) with 4-methylmuconolactone as substrate.

source_databases_merged: skid uniprot

source: skid


substrate_name: squalene

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F365Y to reconstruct the assayed variant sequence.

proof_lines: mutant F365Y changed to O-methyltyrosine, pH 6.0, 50°C

substrate: squalene


proof_lines:
wild-type, pH 6.0, 40°C
pH 6.0, 45°C, wild-type enzyme
wild-type, pH 6.0, 50°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F605Y to reconstruct the assayed variant sequence.

proof_lines: mutant F605Y changed to O-methyltyrosine, pH 6.0, 50°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F605W to reconstruct the assayed variant sequence.

proof_lines:
mutant F605W, pH 6.0, 40°C
mutant F605W, pH 6.0, 50°C


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

proof_lines: mutant F605 changed to O-methyltyrosine, pH 6.0, 40°C

proof_lines: mutant F6365 changed to trifluorophenylalanine, pH 6.0, 50°C

proof_lines: mutant F365 changed to difluorophenylalanine, pH 6.0, 50°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y606A to reconstruct the assayed variant sequence.

proof_lines: mutant F605 changed to difluorophenylalanine plus mutation Y606A, pH 6.0, 50°C

proof_lines: mutant F605 changed to fluorophenylalanine plus mutation Y606A, pH 6.0, 50°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F297A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, purified recombinant mutant F297A+P


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +15, so it is treated as a source-provided variant sequence.

proof_lines: pH 7.0, 30°C, purified recombinant mutant R333K


proof_lines: pH 7.0, 30°C, recombinant wild-type enzyme

proof_lines: recombinant wild-type enzyme, pH 6.0, 30°C


organism: Thermomonospora curvata


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V289L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G322A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G78D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I323L to reconstruct the assayed variant sequence.


substrate_name: isovaleryl-CoA (at 37 degrees Celsius)

proof_lines: kcat is 3.1 sec(-1) for ICM activity in the absence of nucleotides, at pH 7.5 and 37 degrees Celsius. Activity might be 4-fold higher at 60 degrees Celsius, the optimal growth temperature for this organism. kcat is 1.96 sec(-1) for ICM acti

substrate: isovaleryl-CoA (at 37 degrees Celsius)


substrate_name: ATP (at 37 degrees Celsius)

assay_conditions_summary: pH 7.5; cofactor ATP

substrate: ATP (at 37 degrees Celsius)


proof_lines:
quintuple mutant, 50°C, pH 6.0
sextuple mutant, 50°C, pH 6.0


source_db: oed

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature E45A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 323.15 K; buffer 60 mM sodium citrate

column_label: Table 3 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B), SHC row 'E45A', product row '2+3'; column 'Km (uM)' = 2.13 x 10; column 'kcat (min^-1)' = 34.0; column 'kcat/Km' = 1.60.

raw_value_unit_evidence: Table 3, SHC row E45A, product row 2+3: Km = 2.13 x 10 uM; kcat = 34.0 min^-1; printed kcat/Km = 1.60 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 3, SHC row E45A, product row 2+3

table_label: Table 3: Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B (Bioscience, Biotechnology, and Biochemistry 2004, 68(3):728-738)

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature E93A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 328.15 K; buffer 60 mM sodium citrate

column_label: Table 3 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B), SHC row 'E93A', product row '2+3'; column 'Km (uM)' = 1.89 x 10; column 'kcat (min^-1)' = 31.6; column 'kcat/Km' = 1.67.

raw_value_unit_evidence: Table 3, SHC row E93A, product row 2+3: Km = 1.89 x 10 uM; kcat = 31.6 min^-1; printed kcat/Km = 1.67 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 3, SHC row E93A, product row 2+3


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature F434A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 333.15 K; buffer 60 mM sodium citrate

column_label: Table 4 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutant SHCs in Category C), SHC row 'F434A', product row '2+3'; column 'Km (uM)' = 8.16 x 10; column 'kcat (min^-1)' = 41.5; column 'kcat/Km' = 5.09 x 10^-1.

raw_value_unit_evidence: Table 4, SHC row F434A, product row 2+3: Km = 8.16 x 10 uM; kcat = 41.5 min^-1; printed kcat/Km = 5.09 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 4, SHC row F434A, product row 2+3

table_label: Table 4: Kinetic Data and Optimal Temperatures for the Wild-type and Mutant SHCs in Category C (Bioscience, Biotechnology, and Biochemistry 2004, 68(3):728-738)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature F437A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 318.15 K; buffer 60 mM sodium citrate

column_label: Table 4 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutant SHCs in Category C), SHC row 'F437A', product row '2+3'; column 'Km (uM)' = 9.55 x 10; column 'kcat (min^-1)' = 91.1; column 'kcat/Km' = 9.54 x 10^-1.

raw_value_unit_evidence: Table 4, SHC row F437A, product row 2+3: Km = 9.55 x 10 uM; kcat = 91.1 min^-1; printed kcat/Km = 9.54 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 4, SHC row F437A, product row 2+3


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature P263A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category A), SHC row 'P263A', product row '2+3+5'; column 'Km (uM)' = 1.85 x 10^2; column 'kcat (min^-1)' = 310.9; column 'kcat/Km' = 1.68.

raw_value_unit_evidence: Table 2, SHC row P263A, product row 2+3+5: Km = 1.85 x 10^2 uM; kcat = 310.9 min^-1; printed kcat/Km = 1.68 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

table_label: Table 2: Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category A (Bioscience, Biotechnology, and Biochemistry 2004, 68(3):728-738)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature P263G to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category A), SHC row 'P263G', product row '2+3+5'; column 'Km (uM)' = 2.37 x 10^2; column 'kcat (min^-1)' = 315.4; column 'kcat/Km' = 1.33.

raw_value_unit_evidence: Table 2, SHC row P263G, product row 2+3+5: Km = 2.37 x 10^2 uM; kcat = 315.4 min^-1; printed kcat/Km = 1.33 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature Q262A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category A), SHC row 'Q262A', product row '2+3+5'; column 'Km (uM)' = 1.02 x 10^2; column 'kcat (min^-1)' = 202.8; column 'kcat/Km' = 1.99.

raw_value_unit_evidence: Table 2, SHC row Q262A, product row 2+3+5: Km = 1.02 x 10^2 uM; kcat = 202.8 min^-1; printed kcat/Km = 1.99 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature Q262G to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category A), SHC row 'Q262G', product row '2+3+5'; column 'Km (uM)' = 1.56 x 10^2; column 'kcat (min^-1)' = 366.5; column 'kcat/Km' = 2.35.

raw_value_unit_evidence: Table 2, SHC row Q262G, product row 2+3+5: Km = 1.56 x 10^2 uM; kcat = 366.5 min^-1; printed kcat/Km = 2.35 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature R127Q to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B), SHC row 'R127Q', product row '2+3'; column 'Km (uM)' = 2.55 x 10; column 'kcat (min^-1)' = 39.7; column 'kcat/Km' = 1.56.

normalized_value_unit_evidence: Km: printed Table 3 cell 2.55 x 10 uM, that is 25.5 uM; 25.5 / 1000 = 0.0255 mM; the exported value is 0.025 mM. kcat: printed Table 3 cell 39.7 min^-1; 39.7 / 60 = 0.6616666667 s^-1; the exported value is 0.662 s^(-1). kcat/Km: printed Table 3 cell 1.56 uM^-1 min^-1, that is 1.56 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 1.56 x 1000 / 60 = 26 s^-1 mM^-1; the exported value is 26.48 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, SHC row R127Q, product row 2+3: Km = 2.55 x 10 uM; kcat = 39.7 min^-1; printed kcat/Km = 1.56 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 3, SHC row R127Q, product row 2+3


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature T41A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B), SHC row 'T41A', product row '2+3'; column 'Km (uM)' = 1.67 x 10; column 'kcat (min^-1)' = 53.9; column 'kcat/Km' = 3.23.

raw_value_unit_evidence: Table 3, SHC row T41A, product row 2+3: Km = 1.67 x 10 uM; kcat = 53.9 min^-1; printed kcat/Km = 3.23 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 3, SHC row T41A, product row 2+3


organism: Enterobacter sp. FMB-1

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

proof_lines: pH not specified in the publication, 50°C, recombinant enzyme


organism: Raoultella planticola

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

proof_lines: recombinant enzyme, pH not specified in the publication, 35°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature W133A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B), SHC row 'W133A', product row '2+3'; column 'Km (uM)' = 1.69 x 10; column 'kcat (min^-1)' = 48.8; column 'kcat/Km' = 2.89.

raw_value_unit_evidence: Table 3, SHC row W133A, product row 2+3: Km = 1.69 x 10 uM; kcat = 48.8 min^-1; printed kcat/Km = 2.89 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 3, SHC row W133A, product row 2+3


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W133A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature Y267A to reconstruct the assayed variant sequence.

column_label: Table 4 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutant SHCs in Category C), SHC row 'Y267A', product row '2+3'; column 'Km (uM)' = 1.97 x 10^2; column 'kcat (min^-1)' = 51.1; column 'kcat/Km' = 2.59 x 10^-1.

raw_value_unit_evidence: Table 4, SHC row Y267A, product row 2+3: Km = 1.97 x 10^2 uM; kcat = 51.1 min^-1; printed kcat/Km = 2.59 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 4, SHC row Y267A, product row 2+3


organism: Cupriavidus metallidurans

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1LRY0 and applied mutation signature F598A to reconstruct the assayed variant sequence.

column_label: Table 1: Comparison of the kinetic parameters for the isovaleryl-CoA mutase and isobutyryl-CoA mutase activities of wild-type and mutant IcmFs, PCM, and PCM-F (J. Biol. Chem. 2015, 290(33):20466-20476); enzyme row 'F598A' of the first column, which the caption sentence "Wild-type and the mutants in the first column refer to IcmF" resolves to F598A IcmF; isobutyryl-CoA column block: column 'kcat (min^-1)' = 4.8; column 'Km (mM)' = 0.45; column 'kcat/Km (mM^-1 min^-1)' = 11. The other three cells of the same printed row belong to the isovaleryl-CoA reaction (kcat 22 min^-1, Km 0.51 mM, kcat/Km 43 mM^-1 min^-1).

normalized_value_unit_evidence: Km: printed Table 1 cell 0.45 mM; the printed column unit is already the canonical mM, so the value carries over as 0.45 mM. kcat: printed Table 1 cell 4.8 min^-1; 4.8 / 60 = 0.08 s^(-1). kcat/Km: printed Table 1 cell 11 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so the printed cell becomes 0.18333333333333332 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed component cells is 0.08 / 0.45 = 0.17777777777777778 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row 'F598A', isobutyryl-CoA column block: kcat = 4.8 min^-1; Km = 0.45 mM; kcat/Km = 11 mM^-1 min^-1.

row_label: Table 1, enzyme row 'F598A', the three isobutyryl-CoA cells (kcat, Km, kcat/Km)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1LRY0 and applied mutation signature F598V to reconstruct the assayed variant sequence.

column_label: Table 1: Comparison of the kinetic parameters for the isovaleryl-CoA mutase and isobutyryl-CoA mutase activities of wild-type and mutant IcmFs, PCM, and PCM-F (J. Biol. Chem. 2015, 290(33):20466-20476); enzyme row 'F598V' of the first column, which the caption sentence "Wild-type and the mutants in the first column refer to IcmF" resolves to F598V IcmF; isobutyryl-CoA column block: column 'kcat (min^-1)' = 12; column 'Km (mM)' = 0.67; column 'kcat/Km (mM^-1 min^-1)' = 18. The other three cells of the same printed row belong to the isovaleryl-CoA reaction (kcat 15 min^-1, Km 0.62 mM, kcat/Km 24 mM^-1 min^-1).

normalized_value_unit_evidence: Km: printed Table 1 cell 0.67 mM; the printed column unit is already the canonical mM, so the value carries over as 0.67 mM. kcat: printed Table 1 cell 12 min^-1; 12 / 60 = 0.2 s^(-1). kcat/Km: printed Table 1 cell 18 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so the printed cell becomes 0.3 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed component cells is 0.2 / 0.67 = 0.29850746268656714 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row 'F598V', isobutyryl-CoA column block: kcat = 12 min^-1; Km = 0.67 mM; kcat/Km = 18 mM^-1 min^-1.

row_label: Table 1, enzyme row 'F598V', the three isobutyryl-CoA cells (kcat, Km, kcat/Km)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1LRY0 and applied mutation signature Q742A to reconstruct the assayed variant sequence.

column_label: Table 1: Comparison of the kinetic parameters for the isovaleryl-CoA mutase and isobutyryl-CoA mutase activities of wild-type and mutant IcmFs, PCM, and PCM-F (J. Biol. Chem. 2015, 290(33):20466-20476); enzyme row 'Q742A' of the first column, which the caption sentence "Wild-type and the mutants in the first column refer to IcmF" resolves to Q742A IcmF; isobutyryl-CoA column block: column 'kcat (min^-1)' = 18; column 'Km (mM)' = 0.79; column 'kcat/Km (mM^-1 min^-1)' = 23. The other three cells of the same printed row belong to the isovaleryl-CoA reaction (ND in all three cells).

normalized_value_unit_evidence: Km: printed Table 1 cell 0.79 mM; the printed column unit is already the canonical mM, so the value carries over as 0.79 mM. kcat: printed Table 1 cell 18 min^-1; 18 / 60 = 0.3 s^(-1). kcat/Km: printed Table 1 cell 23 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so the printed cell becomes 0.3833333333333333 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed component cells is 0.3 / 0.79 = 0.37974683544303794 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row 'Q742A', isobutyryl-CoA column block: kcat = 18 min^-1; Km = 0.79 mM; kcat/Km = 23 mM^-1 min^-1.

row_label: Table 1, enzyme row 'Q742A', the three isobutyryl-CoA cells (kcat, Km, kcat/Km)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q742N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F598A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1LRY0 and applied mutation signature F598I to reconstruct the assayed variant sequence.

column_label: Table 1: Comparison of the kinetic parameters for the isovaleryl-CoA mutase and isobutyryl-CoA mutase activities of wild-type and mutant IcmFs, PCM, and PCM-F (J. Biol. Chem. 2015, 290(33):20466-20476); enzyme row 'F598I' of the first column, which the caption sentence "Wild-type and the mutants in the first column refer to IcmF" resolves to F598I IcmF; isovaleryl-CoA column block: column 'kcat (min^-1)' = 3.6; column 'Km (mM)' = 0.58; column 'kcat/Km (mM^-1 min^-1)' = 6.2. The other three cells of the same printed row belong to the isobutyryl-CoA reaction (kcat 8.4 min^-1, Km 0.36 mM, kcat/Km 23 mM^-1 min^-1).

normalized_value_unit_evidence: Km: printed Table 1 cell 0.58 mM; the printed column unit is already the canonical mM, so the value carries over as 0.58 mM. kcat: printed Table 1 cell 3.6 min^-1; 3.6 / 60 = 0.06 s^(-1). kcat/Km: printed Table 1 cell 6.2 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so the printed cell becomes 0.10333333333333333 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed component cells is 0.06 / 0.58 = 0.10344827586206896 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row 'F598I', isovaleryl-CoA column block: kcat = 3.6 min^-1; Km = 0.58 mM; kcat/Km = 6.2 mM^-1 min^-1.

row_label: Table 1, enzyme row 'F598I', the three isovaleryl-CoA cells (kcat, Km, kcat/Km)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1LRY0 and applied mutation signature F598L to reconstruct the assayed variant sequence.

column_label: Table 1: Comparison of the kinetic parameters for the isovaleryl-CoA mutase and isobutyryl-CoA mutase activities of wild-type and mutant IcmFs, PCM, and PCM-F (J. Biol. Chem. 2015, 290(33):20466-20476); enzyme row 'F598L' of the first column, which the caption sentence "Wild-type and the mutants in the first column refer to IcmF" resolves to F598L IcmF; isovaleryl-CoA column block: column 'kcat (min^-1)' = 8.4; column 'Km (mM)' = 0.56; column 'kcat/Km (mM^-1 min^-1)' = 15. The other three cells of the same printed row belong to the isobutyryl-CoA reaction (kcat 76 min^-1, Km 0.89 mM, kcat/Km 85 mM^-1 min^-1).

normalized_value_unit_evidence: Km: printed Table 1 cell 0.56 mM; the printed column unit is already the canonical mM, so the value carries over as 0.56 mM. kcat: printed Table 1 cell 8.4 min^-1; 8.4 / 60 = 0.14 s^(-1). kcat/Km: printed Table 1 cell 15 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so the printed cell becomes 0.25 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed component cells is 0.14 / 0.56 = 0.25 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row 'F598L', isovaleryl-CoA column block: kcat = 8.4 min^-1; Km = 0.56 mM; kcat/Km = 15 mM^-1 min^-1.

row_label: Table 1, enzyme row 'F598L', the three isovaleryl-CoA cells (kcat, Km, kcat/Km)


column_label: Table 1: Comparison of the kinetic parameters for the isovaleryl-CoA mutase and isobutyryl-CoA mutase activities of wild-type and mutant IcmFs, PCM, and PCM-F (J. Biol. Chem. 2015, 290(33):20466-20476); enzyme row 'F598V' of the first column, which the caption sentence "Wild-type and the mutants in the first column refer to IcmF" resolves to F598V IcmF; isovaleryl-CoA column block: column 'kcat (min^-1)' = 15; column 'Km (mM)' = 0.62; column 'kcat/Km (mM^-1 min^-1)' = 24. The other three cells of the same printed row belong to the isobutyryl-CoA reaction (kcat 12 min^-1, Km 0.67 mM, kcat/Km 18 mM^-1 min^-1).

normalized_value_unit_evidence: Km: printed Table 1 cell 0.62 mM; the printed column unit is already the canonical mM, so the value carries over as 0.62 mM. kcat: printed Table 1 cell 15 min^-1; 15 / 60 = 0.25 s^(-1). kcat/Km: printed Table 1 cell 24 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so the printed cell becomes 0.4 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed component cells is 0.25 / 0.62 = 0.40322580645161293 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row 'F598V', isovaleryl-CoA column block: kcat = 15 min^-1; Km = 0.62 mM; kcat/Km = 24 mM^-1 min^-1.

row_label: Table 1, enzyme row 'F598V', the three isovaleryl-CoA cells (kcat, Km, kcat/Km)


organism: Cupriavidus necator


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature E45A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B), SHC row 'E45A', product row '2'; column 'Km (uM)' = 2.13 x 10; column 'kcat (min^-1)' = 20.7; column 'kcat/Km' = 9.72 x 10^-1.

raw_value_unit_evidence: Table 3, SHC row E45A, product row 2: Km = 2.13 x 10 uM; kcat = 20.7 min^-1; printed kcat/Km = 9.72 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 3, SHC row E45A, product row 2


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature E93A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B), SHC row 'E93A', product row '2'; column 'Km (uM)' = 1.89 x 10; column 'kcat (min^-1)' = 21.2; column 'kcat/Km' = 1.12.

raw_value_unit_evidence: Table 3, SHC row E93A, product row 2: Km = 1.89 x 10 uM; kcat = 21.2 min^-1; printed kcat/Km = 1.12 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 3, SHC row E93A, product row 2


column_label: Table 3 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B), SHC row 'R127Q', product row '2'; column 'Km (uM)' = 2.55 x 10; column 'kcat (min^-1)' = 26.9; column 'kcat/Km' = 1.05.

raw_value_unit_evidence: Table 3, SHC row R127Q, product row 2: Km = 2.55 x 10 uM; kcat = 26.9 min^-1; printed kcat/Km = 1.05 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 3, SHC row R127Q, product row 2


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature F434A to reconstruct the assayed variant sequence.

column_label: Table 4 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutant SHCs in Category C), SHC row 'F434A', product row '2'; column 'Km (uM)' = 8.16 x 10; column 'kcat (min^-1)' = 32.3; column 'kcat/Km' = 3.96 x 10^-1.

raw_value_unit_evidence: Table 4, SHC row F434A, product row 2: Km = 8.16 x 10 uM; kcat = 32.3 min^-1; printed kcat/Km = 3.96 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 4, SHC row F434A, product row 2


column_label: Table 3 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B), SHC row 'W133A', product row '2'; column 'Km (uM)' = 1.69 x 10; column 'kcat (min^-1)' = 37.3; column 'kcat/Km' = 2.21.

raw_value_unit_evidence: Table 3, SHC row W133A, product row 2: Km = 1.69 x 10 uM; kcat = 37.3 min^-1; printed kcat/Km = 2.21 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 3, SHC row W133A, product row 2


column_label: Table 4 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutant SHCs in Category C), SHC row 'Y267A', product row '2'; column 'Km (uM)' = 1.97 x 10^2; column 'kcat (min^-1)' = 38.5; column 'kcat/Km' = 1.95 x 10^-1.

raw_value_unit_evidence: Table 4, SHC row Y267A, product row 2: Km = 1.97 x 10^2 uM; kcat = 38.5 min^-1; printed kcat/Km = 1.95 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 4, SHC row Y267A, product row 2


column_label: Table 3 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B), SHC row 'T41A', product row '2'; column 'Km (uM)' = 1.67 x 10; column 'kcat (min^-1)' = 44.1; column 'kcat/Km' = 2.64.

normalized_value_unit_evidence: Km: printed Table 3 cell 1.67 x 10 uM, that is 16.7 uM; 16.7 / 1000 = 0.0167 mM; the exported value is 0.0167 mM. kcat: printed Table 3 cell 44.1 min^-1; 44.1 / 60 = 0.735 s^-1; the exported value is 0.735 s^(-1). kcat/Km: printed Table 3 cell 2.64 uM^-1 min^-1, that is 2.64 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 2.64 x 1000 / 60 = 44 s^-1 mM^-1; the exported value is 44.0119760479 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, SHC row T41A, product row 2: Km = 1.67 x 10 uM; kcat = 44.1 min^-1; printed kcat/Km = 2.64 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 3, SHC row T41A, product row 2


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature F437A to reconstruct the assayed variant sequence.

column_label: Table 4 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutant SHCs in Category C), SHC row 'F437A', product row '2'; column 'Km (uM)' = 9.55 x 10; column 'kcat (min^-1)' = 61.5; column 'kcat/Km' = 6.44 x 10^-1.

raw_value_unit_evidence: Table 4, SHC row F437A, product row 2: Km = 9.55 x 10 uM; kcat = 61.5 min^-1; printed kcat/Km = 6.44 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 4, SHC row F437A, product row 2


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature P263G to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category A), SHC row 'P263G', product row '2'; column 'Km (uM)' = 2.37 x 10^2; column 'kcat (min^-1)' = 63.4; column 'kcat/Km' = 2.68 x 10^-1.

raw_value_unit_evidence: Table 2, SHC row P263G, product row 2: Km = 2.37 x 10^2 uM; kcat = 63.4 min^-1; printed kcat/Km = 2.68 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 2, SHC row P263G, product row 2


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature P263A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category A), SHC row 'P263A', product row '2'; column 'Km (uM)' = 1.85 x 10^2; column 'kcat (min^-1)' = 65.6; column 'kcat/Km' = 3.55 x 10^-1.

raw_value_unit_evidence: Table 2, SHC row P263A, product row 2: Km = 1.85 x 10^2 uM; kcat = 65.6 min^-1; printed kcat/Km = 3.55 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 2, SHC row P263A, product row 2


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q262A to reconstruct the assayed variant sequence.

proof_lines:
pH 6.0, 45°C, mutant Q262A
mutant Q262A, 45°C, pH 6.0


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature Q262G to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category A), SHC row 'Q262G', product row '2'; column 'Km (uM)' = 1.56 x 10^2; column 'kcat (min^-1)' = 82.1; column 'kcat/Km' = 5.26 x 10^-1.

raw_value_unit_evidence: Table 2, SHC row Q262G, product row 2: Km = 1.56 x 10^2 uM; kcat = 82.1 min^-1; printed kcat/Km = 5.26 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 2, SHC row Q262G, product row 2


organism: Serratia plymuthica

verification_status: unverified

sequence_variant_note: Mutation signature E175N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

status: unverified


sequence_variant_note: Mutation signature E175N/K576D references residue 576, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature K576D references residue 576, which is outside the resolved sequence length.


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


organism: Pseudomonas putida

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K490L with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


substrate_name: maltopentaose

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

column_label: Abstract reports Kms for maltotetraose, maltopentaose, maltohexaose, maltoheptaose, and short chain amylose as 41.5, 7.1, 5.7, 1.4, and 0.6 mM respectively.

raw_value_unit_evidence: Km raw_value=7.1 mM raw_unit=mM

row_label: Sulfolobus acidocaldarius maltooligosyl trehalose synthase / maltopentaose

table_label: PubMed XML abstract PMID 9063973


raw_value_unit_evidence: Km raw_value=41.5 mM raw_unit=mM

row_label: Sulfolobus acidocaldarius maltooligosyl trehalose synthase / maltotetraose


organism: Thermus antranikianii

substrate_name: alpha,alpha-trehalose

assay_conditions_summary: pH 7

substrate: alpha,alpha-trehalose


protein_accession_database: NCBI Protein


organism: Meiothermus ruber


organism: Saccharolobus solfataricus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A406S with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D411A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D610A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P402Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R614A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V426T to reconstruct the assayed variant sequence.


column_label: Table 3; Wild-type row; kcat/KM column; raw kcat/KM cell=62.3 +/- 2.7 s^-1 mM^-1; kcat cell=411 +/- 9 s^-1; KM cell=6.60 +/- 0.41 mM.

row_label: Wild-type row; kcat/KM column

table_label: PMID 24564903, Table 3: kinetic parameters for MTSase transglycosylation of maltopentaose at 60 C in 50 mM citrate phosphate buffer, pH 5


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate_name: 4-nitrophenyl alpha-D-glucoside (at pH 6.8 and 37 degrees Celsius)


substrate_name: alpha-glucosyl fluoride (at pH 6.8 and 37 degrees Celsius)


organism: Thermus thermophilus

substrate_name: maltose


organism: Mycolicibacterium smegmatis

proof_lines: in 40 mM potassium phosphate buffer (pH 6.8), at 37°C


organism: Acetobacter aceti

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


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


organism: Streptomyces virginiae

substrate_name: butanoyl-CoA

assay_conditions_summary: pH 7.4; cofactor CoA

substrate: butanoyl-CoA


column_label: Abstract assigns 57 microM to isobutyryl-CoA and 54 microM to n-butyryl-CoA.

normalized_value_unit_evidence: Expected substrate 2-methylpropanoyl-CoA/isobutyryl-CoA maps to 0.057 mM; exported 0.054 mM belongs to n-butyryl-CoA.

raw_value_unit_evidence: Km values for isobutyryl-CoA, n-butyryl-CoA, and coenzyme B12 were 57 +/- 13, 54 +/- 12, and 12 +/- 2 microM, respectively.

row_label: Isobutyryl-CoA mutase / isobutyryl-CoA and n-butyryl-CoA

table_label: PubMed XML abstract PMID 10531377


substrate_name: isovaleryl-CoA

substrate: isovaleryl-CoA


proof_lines: recombinant engineered PCM mutant, pH 7.5, 37°C

proof_lines: recombinant engineered PCM-F mutant, pH 7.5, 37°C


proof_lines: recombinant wild-type enzyme, pH 7.5, 37°C


organism: Escherichia coli (strain K12)


organism: Klebsiella sp.

substrate_name: sucrose

proof_lines: mutant enzyme R325D and R325L, pH 6.0, 35°C

substrate: sucrose


proof_lines:
pH 6.5, 30°C, recombinant mutant TSTtMr
pH 6.5, 30°C, recombinant mutant TSMrTt


proof_lines:
pH 6.5, 30°C, recombinant mutant TSMrTt
pH 6.5, 30°C, recombinant mutant TSTtMr


proof_lines: pH 6.5, 30°C, recombinant wild-type enzyme


organism: Arthrobacter ramosus

substrate: maltopentaose


proof_lines: pH 7.0, 45°C, mutant enzyme S316R/S444E/G415P


organism: Escherichia coli


organism: Arthrobacter sp.

substrate_name: maltoheptaose

column_label: Abstract states the Km of the enzyme for maltotetraose, maltopentaose, maltohexaose, and maltoheptaose were 22.9 mM, 8.7 mM, 1.4 mM, and 0.9 mM, respectively.

raw_value_unit_evidence: Km raw_value=0.9 raw_unit=mM for maltoheptaose

row_label: maltoheptaose in ordered Km prose list

table_label: J-STAGE article abstract / PubMed abstract PMID 8611744

substrate: maltoheptaose


substrate_name: maltohexaose

raw_value_unit_evidence: Km raw_value=1.4 raw_unit=mM for maltohexaose

row_label: maltohexaose in ordered Km prose list

substrate: maltohexaose


raw_value_unit_evidence: Km raw_value=8.7 raw_unit=mM for maltopentaose

row_label: maltopentaose in ordered Km prose list


substrate_name: maltotetraose

raw_value_unit_evidence: Km raw_value=22.9 raw_unit=mM for maltotetraose

row_label: maltotetraose in ordered Km prose list

substrate: maltotetraose


substrate: maltose


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: tRNA pseudouridine(38-40) synthase

substrate_name: tRNA uridine39

proof_lines:
pH 8.0, 30?, wild-type enzyme
wild-type, pH 8.0, 30°C
pH 8.0, wild-type enzyme

enzyme: tRNA pseudouridine(38-40) synthase

substrate: tRNA uridine39


proof_lines: pH 8.0, 30°C, mutant enzyme C55A/C154A/C169A


organism: Pseudarthrobacter chlorophenolicus


organism: Pseudomonas sp.


substrate_name: trehalose

substrate: trehalose


proof_lines: recombinant His6-tagged mutant DM2, pH 6.5, 50°C


proof_lines: recombinant His6-tagged wild-type enzyme, pH 6.5, 50°C


enzyme_display_name: aldose 1-epimerase

organism: Canis lupus familiaris

substrate_name: alpha-D-glucose

enzyme: aldose 1-epimerase

substrate: alpha-D-glucose


enzyme_display_name: isopentenyl-diphosphate Delta-isomerase

organism: Capsicum annuum

substrate_name: isopentenyl diphosphate

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

enzyme: isopentenyl-diphosphate Delta-isomerase

substrate: isopentenyl diphosphate


enzyme_display_name: adenylate cyclase

proof_lines: VC1-IIC2 in the presence of 0.1 mM forskolin and GTPgammaS-activated Galphas

enzyme: adenylate cyclase


substrate_name: ATP

assay_conditions_summary: cofactor ATP

proof_lines: recombinant cytosolic domain of type V adenylyl cyclase

substrate: ATP


enzyme_display_name: UDP-arabinopyranose mutase

organism: Oryza sativa

substrate_name: UDP-beta-L-arabinopyranose

enzyme: UDP-arabinopyranose mutase

substrate: UDP-beta-L-arabinopyranose


substrate_name: UDP-beta-L-arabinofuranose

substrate: UDP-beta-L-arabinofuranose


organism: Chlamydomonas reinhardtii

proof_lines:
pH 6, 25°C, recombinant enzyme
pH 6, 25°C, native enzyme


organism: Oryza sativa subsp. japonica


enzyme_display_name: tRNA pseudouridine(32) synthase

substrate_name: tRNA uridine32

proof_lines: pH 7.5, 37°C, Escherichia coli tRNAPhe, mutant enzyme P29L

enzyme: tRNA pseudouridine(32) synthase

substrate: tRNA uridine32


proof_lines: pH 7.5, 37°C, Escherichia coli tRNAPhe, mutant enzyme P29G


proof_lines: pH 7.5, 37°C, Escherichia coli tRNAPhe, wild-type enzyme

proof_lines: pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe. wild-type enzyme


proof_lines: pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe, mutant enzyme C117A


proof_lines: pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe, mutant enzyme C117A/C128A


proof_lines: pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe, mutant enzyme C128A


enzyme_display_name: beta-amyrin synthase

organism: Euphorbia tirucalli

enzyme: beta-amyrin synthase


enzyme_display_name: glucose-6-phosphate isomerase

organism: Carassius auratus

substrate_name: D-fructose 6-phosphate

assay_conditions_summary: pH 8

enzyme: glucose-6-phosphate isomerase

substrate: D-fructose 6-phosphate


enzyme_display_name: UniProt P21638

organism: Pseudomonas denitrificans (nom. rej.)

substrate_name: Hydrogenobyrinate

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P21638

substrate: Hydrogenobyrinate


enzyme_display_name: alpha-amyrin synthase

organism: Malus domestica

enzyme: alpha-amyrin synthase


enzyme_display_name: protostadienol synthase

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

enzyme: protostadienol synthase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C564A to reconstruct the assayed variant sequence.


substrate_name: UDP-L-arabinofuranose

column_label: Table 1 reports rUAM3 UDP-Araf Km as 84.8 mM.

raw_value_unit_evidence: Km = 84.8 mM for rUAM3 with UDP-Araf

row_label: rUAM3 / UDP-Araf

table_label: Table 1

substrate: UDP-L-arabinofuranose


substrate_name: UDP-L-arabinopyranose

column_label: Table 1 reports rUAM3 UDP-Arap Km as 210 mM.

raw_value_unit_evidence: Km = 210 mM for rUAM3 with UDP-Arap

row_label: rUAM3 / UDP-Arap

substrate: UDP-L-arabinopyranose


column_label: Table 1 reports rUAM1 UDP-Araf Km as 22.8 mM.

raw_value_unit_evidence: Km = 22.8 mM for rUAM1 with UDP-Araf

row_label: rUAM1 / UDP-Araf


column_label: Table 1 reports rUAM1 UDP-Arap Km as 45.4 mM.

raw_value_unit_evidence: Km = 45.4 mM for rUAM1 with UDP-Arap

row_label: rUAM1 / UDP-Arap


organism: Eriobotrya japonica


enzyme_display_name: 2-hydroxyisobutanoyl-CoA mutase

organism: Kyrpidia tusciae DSM 2912

assay_conditions_summary: pH 7.8; 328.15 K; cofactor CoA

enzyme: 2-hydroxyisobutanoyl-CoA mutase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C486A to reconstruct the assayed variant sequence.


column_label: Browser-verified Wiley Table 3, Wild row: Km 33.8 +/- 0.53; kcat 46.4 +/- 0.68; kcat/Km 1.37 +/- 0.21.

raw_value_unit_evidence: Table 3 Wild row: Km 33.8 +/- 0.53 uM; kcat 46.4 +/- 0.68 min^-1; independently printed kcat/Km 1.37 +/- 0.21 uM^-1 min^-1.

row_label: Wild

table_label: Table 3. The enzymatic activities of the D485, C486 and C564 variants


enzyme_display_name: dTDP-fucopyranose mutase

substrate_name: dTDP-alpha-D-fucopyranose

enzyme: dTDP-fucopyranose mutase

substrate: dTDP-alpha-D-fucopyranose


enzyme_display_name: precorrin-8X methylmutase

enzyme: precorrin-8X methylmutase


organism: Sinorhizobium sp


enzyme_display_name: ethylmalonyl-CoA mutase

organism: Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.)

enzyme: ethylmalonyl-CoA mutase


organism: Aquincola tertiaricarbonis

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 12 min(-1) with (S)-3-hydroxybutyryl-CoA as substrate. kcat is 3.0 min(-1) with 2-hydroxyisobutyryl-CoA as substrate. kcat is 0.20 min(-1) with (R)-3-hydroxybutyryl-CoA as substrate. kcat is 0.20 min(-1) with butyryl-CoA as substrat


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature D117V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.6; 303.15 K; cofactor CoA


substrate_name: isovaleryl-CoA

proof_lines: pH 6.6, 30°C, mutant enzyme D117V (mutation in subunit HcmA)

substrate: isovaleryl-CoA


enzyme_display_name: cucurbitadienol synthase

organism: Siraitia grosvenorii

proof_lines:
pH 7.0, 30°C, wild-type variant 50C573L
pH 7.0, 30°C, wild-type variant 50R573L

enzyme: cucurbitadienol synthase


substrate_name: isobutanoyl-CoA

assay_conditions_summary: pH 6.6; 303.15 K; buffer 1-2 ml of 50 mM potassium phosphate; cofactor CoA

column_label: Table 1: Kinetic parameters of reconstituted HCM subunits incubated with various acyl-CoA substrates (J. Biol. Chem. 2012, 287(19):15502-15511), wild-type HcmA subunit block, substrate row 'Isobutyryl-CoA'; column 'Vmax (nmol min^-1 mg^-1)' = 0.67 (0.5); column 'Km (uM)' = 550; column 'kcat (min^-1)' = 0.06; column 'kcat/Km (mM^-1 min^-1)' = 0.10; column 'Vmax/Km (liters min^-1 mg^-1)' = 1.2.

raw_value_unit_evidence: Table 1, wild-type HcmA subunit block, substrate row 'Isobutyryl-CoA': Km = 550 uM; kcat = 0.06 min^-1; printed kcat/Km = 0.10 mM^-1 min^-1.

substrate: isobutanoyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


column_label: Table 3 reports Wild-type HcmA Isovaleryl-CoA Vmax 8.20 +/- 0.34 nmol min^-1 mg^-1, Km 288 +/- 18 uM, kcat 0.68 +/- 0.03 min^-1, and kcat/Km 2.4 +/- 0.2 mM^-1 min^-1

normalized_value_unit_evidence: KM normalized_value=0.288 normalized_unit=mM; kcat normalized_value=0.011333333333333334 normalized_unit=s^-1; kcat_over_km normalized_value=0.04 normalized_unit=s^-1*mM^-1; current_export_kcat=0.011; current_export_kcat_over_km=0.03819444444444445

raw_value_unit_evidence: KM raw_value=288 raw_unit=uM; kcat raw_value=0.68 raw_unit=min^-1; kcat_over_km raw_value=2.4 raw_unit=mM^-1*min^-1 for isovaleryl-CoA

row_label: Wild-type HcmA Isovaleryl-CoA row; KM, kcat, and kcat/Km columns

table_label: PMID 25720495 PMC HTML Table 3


column_label: Table 3 reports Wild-type HcmA Pivalyl-CoA Vmax 11.8 +/- 0.73 nmol min^-1 mg^-1, Km 374 +/- 46 uM, kcat 0.98 +/- 0.06 min^-1, and kcat/Km 2.6 +/- 0.4 mM^-1 min^-1

normalized_value_unit_evidence: KM normalized_value=0.374 normalized_unit=mM; kcat normalized_value=0.016333333333333333 normalized_unit=s^-1; kcat_over_km normalized_value=0.043333333333333335 normalized_unit=s^-1*mM^-1; current_export_kcat=0.016; current_export_kcat_over_km=0.04278074866310161

raw_value_unit_evidence: KM raw_value=374 raw_unit=uM; kcat raw_value=0.98 raw_unit=min^-1; kcat_over_km raw_value=2.6 raw_unit=mM^-1*min^-1 for pivalyl-CoA

row_label: Wild-type HcmA Pivalyl-CoA row; KM, kcat, and kcat/Km columns


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:I3VE77 and applied mutation signature I90V to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of reconstituted HCM subunits incubated with various acyl-CoA substrates (J. Biol. Chem. 2012, 287(19):15502-15511), HcmA I90V subunit block, substrate row '2-Hydroxyisobutyryl-CoA'; column 'Vmax (nmol min^-1 mg^-1)' = 15 (11); column 'Km (uM)' = 1,840; column 'kcat (min^-1)' = 1.2; column 'kcat/Km (mM^-1 min^-1)' = 0.7; column 'Vmax/Km (liters min^-1 mg^-1)' = 8.1.

raw_value_unit_evidence: Table 1, HcmA I90V subunit block, substrate row '2-Hydroxyisobutyryl-CoA': Km = 1,840 uM; kcat = 1.2 min^-1; printed kcat/Km = 0.7 mM^-1 min^-1.


column_label: Table 1: Kinetic parameters of reconstituted HCM subunits incubated with various acyl-CoA substrates (J. Biol. Chem. 2012, 287(19):15502-15511), HcmA I90V subunit block, substrate row '(S)-3-Hydroxybutyryl-CoA'; column 'Vmax (nmol min^-1 mg^-1)' = 24 (17); column 'Km (uM)' = 1,760; column 'kcat (min^-1)' = 2.0; column 'kcat/Km (mM^-1 min^-1)' = 1.1; column 'Vmax/Km (liters min^-1 mg^-1)' = 14.

raw_value_unit_evidence: Table 1, HcmA I90V subunit block, substrate row '(S)-3-Hydroxybutyryl-CoA': Km = 1,760 uM; kcat = 2.0 min^-1; printed kcat/Km = 1.1 mM^-1 min^-1.


column_label: Table 1: Kinetic parameters of reconstituted HCM subunits incubated with various acyl-CoA substrates (J. Biol. Chem. 2012, 287(19):15502-15511), wild-type HcmA subunit block, substrate row '2-Hydroxyisobutyryl-CoA'; column 'Vmax (nmol min^-1 mg^-1)' = 36 (26); column 'Km (uM)' = 104; column 'kcat (min^-1)' = 3.0; column 'kcat/Km (mM^-1 min^-1)' = 29; column 'Vmax/Km (liters min^-1 mg^-1)' = 350.

raw_value_unit_evidence: Table 1, wild-type HcmA subunit block, substrate row '2-Hydroxyisobutyryl-CoA': Km = 104 uM; kcat = 3.0 min^-1; printed kcat/Km = 29 mM^-1 min^-1.


substrate_name: butyryl-CoA

column_label: Table 1: Kinetic parameters of reconstituted HCM subunits incubated with various acyl-CoA substrates (J. Biol. Chem. 2012, 287(19):15502-15511), wild-type HcmA subunit block, substrate row 'Butyryl-CoA'; column 'Vmax (nmol min^-1 mg^-1)' = 2.4 (2); column 'Km (uM)' = 3,340; column 'kcat (min^-1)' = 0.20; column 'kcat/Km (mM^-1 min^-1)' = 0.06; column 'Vmax/Km (liters min^-1 mg^-1)' = 0.7.

raw_value_unit_evidence: Table 1, wild-type HcmA subunit block, substrate row 'Butyryl-CoA': Km = 3,340 uM; kcat = 0.20 min^-1; printed kcat/Km = 0.06 mM^-1 min^-1.

substrate: butyryl-CoA


substrate_name: isobutyryl-CoA

row_label: Table 1, wild-type HcmA subunit block, substrate row 'Isobutyryl-CoA'

table_label: Table 1: Kinetic parameters of reconstituted HCM subunits incubated with various acyl-CoA substrates (J. Biol. Chem. 2012, 287(19):15502-15511)

substrate: isobutyryl-CoA


row_label: Table 1, wild-type HcmA subunit block, substrate row '2-Hydroxyisobutyryl-CoA'


row_label: Table 1, wild-type HcmA subunit block, substrate row 'Butyryl-CoA'


column_label: PMC article prose metric sentence gives Km for CobH/precorrin-8x as 0.91 +/- 0.04 microM at pH 7.7

normalized_value_unit_evidence: PMC article prose Km normalized_value=0.00091 normalized_unit=mM

raw_value_unit_evidence: PMC article prose: This enzyme had a Km of 0.91 +/- 0.04 microM and a Vmax of 230 nmol h-1 mg-1 at pH 7.7

row_label: CobH precorrin-8x kinetic sentence

table_label: PMC article prose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:I3VE77 and applied mutation signature I90A to reconstruct the assayed variant sequence.

column_label: Table 2 | HcmA I90A | substrate (R)-3-Hydroxybutyryl-CoA | condition pH 6.6, 30 °C | Vmax 2.6 ± 0.1 nmol min^-1 mg^-1 | Km 298 ± 24 µM | kcat 0.21 ± 0.01 min^-1 | kcat/Km 0.72 ± 0.06 mM^-1 min^-1

row_label: HcmA I90A / (R)-3-Hydroxybutyryl-CoA

table_label: Table 2: kinetic parameters of reconstituted HCM subunits HcmA variants and wild-type HcmB


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:I3VE77 and applied mutation signature D117A to reconstruct the assayed variant sequence.

column_label: Table 2 | HcmA D117A | substrate (S)-3-Hydroxybutyryl-CoA | condition pH 6.6, 30 °C | Vmax 18.4 ± 0.6 nmol min^-1 mg^-1 | Km 14.6 ± 3.8 µM | kcat 1.53 ± 0.05 min^-1 | kcat/Km 105 ± 27 mM^-1 min^-1

row_label: HcmA D117A / (S)-3-Hydroxybutyryl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:I3VE77 and applied mutation signature D117V to reconstruct the assayed variant sequence.

column_label: Table 2 | HcmA D117V | substrate (S)-3-Hydroxybutyryl-CoA | condition pH 6.6, 30 °C | Vmax 44.4 ± 3.6 nmol min^-1 mg^-1 | Km 117 ± 32 µM | kcat 3.69 ± 0.30 min^-1 | kcat/Km 31.5 ± 8.9 mM^-1 min^-1

row_label: HcmA D117V / (S)-3-Hydroxybutyryl-CoA


column_label: Table 2 | HcmA I90A | substrate (S)-3-Hydroxybutyryl-CoA | condition pH 6.6, 30 °C | Vmax 1.5 ± 0.1 nmol min^-1 mg^-1 | Km 433 ± 56 µM | kcat 0.12 ± 0.01 min^-1 | kcat/Km 0.28 ± 0.04 mM^-1 min^-1

row_label: HcmA I90A / (S)-3-Hydroxybutyryl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:I3VE77 and applied mutation signature I90L to reconstruct the assayed variant sequence.

column_label: Table 2 | HcmA I90L | substrate (S)-3-Hydroxybutyryl-CoA | condition pH 6.6, 30 °C | Vmax 2.48 ± 0.02 nmol min^-1 mg^-1 | Km 663 ± 12 µM | kcat 0.21 ± 0.002 min^-1 | kcat/Km 0.31 ± 0.01 mM^-1 min^-1

row_label: HcmA I90L / (S)-3-Hydroxybutyryl-CoA


organism: Cereibacter sphaeroides

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

assay_conditions_summary: pH 7.8; cofactor CoA


row_label: Table 1, HcmA I90V subunit block, substrate row '2-Hydroxyisobutyryl-CoA'


row_label: Table 1, HcmA I90V subunit block, substrate row '(S)-3-Hydroxybutyryl-CoA'


organism: Escherichia coli


organism: Catfish


organism: Oryza sativa


substrate_name: Unknown

substrate: Unknown


proof_lines:
pH 6.6, 30°C, wild-type enzyme
wild-type, pH 6.6, 30°C


column_label: Table 3 | HcmA D117V | substrate Pivalyl-CoA | condition pH 6.6, 30 °C | Vmax 101 ± 3.9 nmol min^-1 mg^-1 | Km 43.5 ± 6.3 µM | kcat 8.37 ± 0.32 min^-1 | kcat/Km 192 ± 29 mM^-1 min^-1

row_label: HcmA D117V / Pivalyl-CoA

table_label: Table 3: kinetic parameters for pivalyl- and isovaleryl-CoA with reconstituted HCM


column_label: Table 3 | HcmA I90A | substrate Pivalyl-CoA | condition pH 6.6, 30 °C | Vmax 9.4 ± 0.1 nmol min^-1 mg^-1 | Km 235 ± 4 µM | kcat 0.79 ± 0.01 min^-1 | kcat/Km 3.4 ± 0.1 mM^-1 min^-1

row_label: HcmA I90A / Pivalyl-CoA


column_label: Table 3 | HcmA I90V | substrate Pivalyl-CoA | condition pH 6.6, 30 °C | Vmax 12.3 ± 0.96 nmol min^-1 mg^-1 | Km 977 ± 122 µM | kcat 1.02 ± 0.08 min^-1 | kcat/Km 1.0 ± 0.2 mM^-1 min^-1

row_label: HcmA I90V / Pivalyl-CoA


column_label: Table 2 | HcmA D117A | substrate 2-Hydroxyisobutyryl-CoA | condition pH 6.6, 30 °C | Vmax 32.0 ± 1.5 nmol min^-1 mg^-1 | Km 42.0 ± 8.1 µM | kcat 2.66 ± 0.12 min^-1 | kcat/Km 63.2 ± 12.5 mM^-1 min^-1

row_label: HcmA D117A / 2-Hydroxyisobutyryl-CoA


column_label: Table 2 | HcmA D117V | substrate 2-Hydroxyisobutyryl-CoA | condition pH 6.6, 30 °C | Vmax 32.2 ± 1.1 nmol min^-1 mg^-1 | Km 61.4 ± 8.3 µM | kcat 2.68 ± 0.09 min^-1 | kcat/Km 43.6 ± 6.1 mM^-1 min^-1

row_label: HcmA D117V / 2-Hydroxyisobutyryl-CoA


column_label: Table 2 | HcmA I90A | substrate 2-Hydroxyisobutyryl-CoA | condition pH 6.6, 30 °C | Vmax 17.7 ± 0.5 nmol min^-1 mg^-1 | Km 304 ± 22 µM | kcat 1.47 ± 0.04 min^-1 | kcat/Km 4.9 ± 0.4 mM^-1 min^-1

row_label: HcmA I90A / 2-Hydroxyisobutyryl-CoA


column_label: Table 2 | HcmA I90L | substrate 2-Hydroxyisobutyryl-CoA | condition pH 6.6, 30 °C | Vmax 4.81 ± 0.18 nmol min^-1 mg^-1 | Km 517 ± 43 µM | kcat 0.40 ± 0.02 min^-1 | kcat/Km 0.78 ± 0.07 mM^-1 min^-1

row_label: HcmA I90L / 2-Hydroxyisobutyryl-CoA


column_label: Table 3 | HcmA I90V | substrate Isovaleryl-CoA | condition pH 6.6, 30 °C | Vmax 6.74 ± 0.54 nmol min^-1 mg^-1 | Km 329 ± 69 µM | kcat 0.56 ± 0.05 min^-1 | kcat/Km 1.7 ± 0.4 mM^-1 min^-1

row_label: HcmA I90V / Isovaleryl-CoA


column_label: Table 2 | HcmA D117A | substrate (R)-3-Hydroxybutyryl-CoA | condition pH 6.6, 30 °C | Vmax 19.7 ± 0.5 nmol min^-1 mg^-1 | Km 7.5 ± 1.7 µM | kcat 1.64 ± 0.04 min^-1 | kcat/Km 220 ± 49 mM^-1 min^-1

row_label: HcmA D117A / (R)-3-Hydroxybutyryl-CoA


column_label: Table 2 | HcmA D117V | substrate (R)-3-Hydroxybutyryl-CoA | condition pH 6.6, 30 °C | Vmax 125 ± 4.8 nmol min^-1 mg^-1 | Km 67.0 ± 10.2 µM | kcat 10.4 ± 0.4 min^-1 | kcat/Km 155 ± 24 mM^-1 min^-1

row_label: HcmA D117V / (R)-3-Hydroxybutyryl-CoA


enzyme_display_name: leukotriene-C4 synthase

organism: Cavia porcellus

substrate_name: leukotriene A4 methyl ester

enzyme: leukotriene-C4 synthase

substrate: leukotriene A4 methyl ester


enzyme_display_name: protoporphyrin ferrochelatase

substrate_name: 2,4-disulfonic deuteroporphyrin

enzyme: protoporphyrin ferrochelatase

substrate: 2,4-disulfonic deuteroporphyrin


enzyme_display_name: cysteine-S-conjugate beta-lyase

enzyme: cysteine-S-conjugate beta-lyase


enzyme_display_name: methionine gamma-lyase

organism: Citrobacter freundii

substrate_name: DL-homocysteine

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

proof_lines:
30°C, pH 8.0
pH 8.0, 30°C
recombinant enzyme

enzyme: methionine gamma-lyase

substrate: DL-homocysteine


enzyme_display_name: alanine racemase

organism: Clostridioides difficile

substrate_name: L-alanine

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

enzyme: alanine racemase

substrate: L-alanine


enzyme_display_name: isopentenyl-diphosphate Delta-isomerase

organism: Claviceps sp.

substrate_name: isopentenyl diphosphate

enzyme: isopentenyl-diphosphate Delta-isomerase

substrate: isopentenyl diphosphate


enzyme_display_name: methylaspartate mutase

organism: Clostridium cochlearium

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

enzyme: methylaspartate mutase


enzyme_display_name: adenylate cyclase

substrate_name: ATP

enzyme: adenylate cyclase

substrate: ATP


organism: Clostridium perfringens


enzyme_display_name: D-psicose 3-epimerase

organism: [Clostridium] scindens

substrate_name: D-fructose

enzyme: D-psicose 3-epimerase

substrate: D-fructose


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature I90A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.6; cofactor CoA

proof_lines: pH 6.6, 30°C, mutant enzyme I90A (mutation in subunit HcmA)

proof_lines: pH 6.6, 30°C, mutant enzyme, I90A (mutation in subunit HcmA)


assay_conditions_summary: pH 6.6; 303.15 K; buffer 50 mM potassium phosphate; cofactor CoA

column_label: Table 2: Kinetic parameters Vmax, Km, and kcat and deduced catalytic efficiency kcat/Km of reconstituted HCM subunits HcmA and wild-type HcmB incubated with 2-hydroxyisobutyryl-CoA and both 3-hydroxybutyryl-CoA enantiomers at pH 6.6 and 30 C (J. Biol. Chem. 2015, 290(15):9727-9737); variant block 'HcmA I90L', substrate row '(S)-3-Hydroxybutyryl-CoA'; column 'Km' in uM = 663; column 'kcat' in min^-1 = 0.21; column 'kcat/Km' in mM^-1 min^-1 = 0.31; column 'Vmax' in nmol min^-1 mg^-1 is printed for the same row.

raw_value_unit_evidence: Table 2, variant block 'HcmA I90L', substrate row '(S)-3-Hydroxybutyryl-CoA': Km = 663 uM; kcat = 0.21 min^-1; printed kcat/Km = 0.31 mM^-1 min^-1.


column_label: Table 2: Kinetic parameters Vmax, Km, and kcat and deduced catalytic efficiency kcat/Km of reconstituted HCM subunits HcmA and wild-type HcmB incubated with 2-hydroxyisobutyryl-CoA and both 3-hydroxybutyryl-CoA enantiomers at pH 6.6 and 30 C (J. Biol. Chem. 2015, 290(15):9727-9737); variant block 'HcmA I90L', substrate row '2-Hydroxyisobutyryl-CoA'; column 'Km' in uM = 517; column 'kcat' in min^-1 = 0.40; column 'kcat/Km' in mM^-1 min^-1 = 0.78; column 'Vmax' in nmol min^-1 mg^-1 is printed for the same row.

raw_value_unit_evidence: Table 2, variant block 'HcmA I90L', substrate row '2-Hydroxyisobutyryl-CoA': Km = 517 uM; kcat = 0.40 min^-1; printed kcat/Km = 0.78 mM^-1 min^-1.


column_label: Table 3: Kinetic parameters Vmax, Km, and kcat and deduced catalytic efficiency kcat/Km of reconstituted HCM subunits HcmA and wild-type HcmB incubated with pivalyl- and isovaleryl-CoA at pH 6.6 and 30 C (J. Biol. Chem. 2015, 290(15):9727-9737); variant block 'HcmA I90A', substrate row 'Isovaleryl-CoA'; column 'Km' in uM = 147; column 'kcat' in min^-1 = 0.54; column 'kcat/Km' in mM^-1 min^-1 = 3.7; column 'Vmax' in nmol min^-1 mg^-1 is printed for the same row.

raw_value_unit_evidence: Table 3, variant block 'HcmA I90A', substrate row 'Isovaleryl-CoA': Km = 147 uM; kcat = 0.54 min^-1; printed kcat/Km = 3.7 mM^-1 min^-1.


column_label: Table 3: Kinetic parameters Vmax, Km, and kcat and deduced catalytic efficiency kcat/Km of reconstituted HCM subunits HcmA and wild-type HcmB incubated with pivalyl- and isovaleryl-CoA at pH 6.6 and 30 C (J. Biol. Chem. 2015, 290(15):9727-9737); variant block 'HcmA I90V', substrate row 'Isovaleryl-CoA'; column 'Km' in uM = 329; column 'kcat' in min^-1 = 0.56; column 'kcat/Km' in mM^-1 min^-1 = 1.7; column 'Vmax' in nmol min^-1 mg^-1 is printed for the same row.

raw_value_unit_evidence: Table 3, variant block 'HcmA I90V', substrate row 'Isovaleryl-CoA': Km = 329 uM; kcat = 0.56 min^-1; printed kcat/Km = 1.7 mM^-1 min^-1.


column_label: Table 3: Kinetic parameters Vmax, Km, and kcat and deduced catalytic efficiency kcat/Km of reconstituted HCM subunits HcmA and wild-type HcmB incubated with pivalyl- and isovaleryl-CoA at pH 6.6 and 30 C (J. Biol. Chem. 2015, 290(15):9727-9737); variant block 'HcmA I90A', substrate row 'Pivalyl-CoA'; column 'Km' in uM = 235; column 'kcat' in min^-1 = 0.79; column 'kcat/Km' in mM^-1 min^-1 = 3.4; column 'Vmax' in nmol min^-1 mg^-1 is printed for the same row.

raw_value_unit_evidence: Table 3, variant block 'HcmA I90A', substrate row 'Pivalyl-CoA': Km = 235 uM; kcat = 0.79 min^-1; printed kcat/Km = 3.4 mM^-1 min^-1.


column_label: Table 3: Kinetic parameters Vmax, Km, and kcat and deduced catalytic efficiency kcat/Km of reconstituted HCM subunits HcmA and wild-type HcmB incubated with pivalyl- and isovaleryl-CoA at pH 6.6 and 30 C (J. Biol. Chem. 2015, 290(15):9727-9737); variant block 'HcmA I90V', substrate row 'Pivalyl-CoA'; column 'Km' in uM = 977; column 'kcat' in min^-1 = 1.02; column 'kcat/Km' in mM^-1 min^-1 = 1.0; column 'Vmax' in nmol min^-1 mg^-1 is printed for the same row.

raw_value_unit_evidence: Table 3, variant block 'HcmA I90V', substrate row 'Pivalyl-CoA': Km = 977 uM; kcat = 1.02 min^-1; printed kcat/Km = 1.0 mM^-1 min^-1.


column_label: Table 2: Kinetic parameters Vmax, Km, and kcat and deduced catalytic efficiency kcat/Km of reconstituted HCM subunits HcmA and wild-type HcmB incubated with 2-hydroxyisobutyryl-CoA and both 3-hydroxybutyryl-CoA enantiomers at pH 6.6 and 30 C (J. Biol. Chem. 2015, 290(15):9727-9737); variant block 'HcmA I90A', substrate row '2-Hydroxyisobutyryl-CoA'; column 'Km' in uM = 304; column 'kcat' in min^-1 = 1.47; column 'kcat/Km' in mM^-1 min^-1 = 4.9; column 'Vmax' in nmol min^-1 mg^-1 is printed for the same row.

raw_value_unit_evidence: Table 2, variant block 'HcmA I90A', substrate row '2-Hydroxyisobutyryl-CoA': Km = 304 uM; kcat = 1.47 min^-1; printed kcat/Km = 4.9 mM^-1 min^-1.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature D117A to reconstruct the assayed variant sequence.

proof_lines: pH 6.6, 30°C, mutant enzyme D117A (mutation in subunit HcmA)


column_label: Table 2: Kinetic parameters Vmax, Km, and kcat and deduced catalytic efficiency kcat/Km of reconstituted HCM subunits HcmA and wild-type HcmB incubated with 2-hydroxyisobutyryl-CoA and both 3-hydroxybutyryl-CoA enantiomers at pH 6.6 and 30 C (J. Biol. Chem. 2015, 290(15):9727-9737); variant block 'HcmA D117A', substrate row '2-Hydroxyisobutyryl-CoA'; column 'Km' in uM = 42.0; column 'kcat' in min^-1 = 2.66; column 'kcat/Km' in mM^-1 min^-1 = 63.2; column 'Vmax' in nmol min^-1 mg^-1 is printed for the same row.

raw_value_unit_evidence: Table 2, variant block 'HcmA D117A', substrate row '2-Hydroxyisobutyryl-CoA': Km = 42.0 uM; kcat = 2.66 min^-1; printed kcat/Km = 63.2 mM^-1 min^-1.