substrate_name: enol-oxaloacetate

substrate: enol-oxaloacetate


enzyme_display_name: lactoylglutathione lyase

organism: Bos taurus

source_db: brenda

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

enzyme: lactoylglutathione lyase

status: unverified

source: brenda


enzyme_display_name: guanylate cyclase

substrate_name: UTP

km_display: Not reported

ki_unit: mM

enzyme: guanylate cyclase

substrate: UTP


substrate_name: GTP

proof_lines: purified recombinant sGC in presence of 3-ethyl-3-(ethylaminoethyl)-1-hydroxy-2-oxo-1-triazene

substrate: GTP


enzyme_display_name: 2-hydroxymuconate tautomerase

organism: Leptothrix cholodnii

substrate_name: (2E)-2-Hydroxypenta-2,4-dienoic acid

source_db: oed

protein_accession_database: UniProt

kcat_over_km_origin: calculated

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

data_origin: experimental

enzyme: 2-hydroxymuconate tautomerase

substrate: (2E)-2-Hydroxypenta-2,4-dienoic acid

source: oed


organism: Pseudomonas putida


smiles: O=C(O)/C(O)=C\C=C/Br


smiles: O=C(O)/C(O)=C\C=C/Cl


substrate_name: Unknown

proof_lines:
at 10°C
at 27°C
37°C, pH 7.4, competitive vs. Mg2+

substrate: Unknown


enzyme_display_name: ribose-5-phosphate isomerase

substrate_name: D-ribose 5-phosphate

proof_lines:
calf spleen
ox muscle
calf liver

enzyme: ribose-5-phosphate isomerase

substrate: D-ribose 5-phosphate


enzyme_display_name: lanosterol synthase

enzyme: lanosterol synthase


enzyme_display_name: aldose 1-epimerase

substrate_name: alpha-D-glucose

proof_lines:
embryo
alpha-D-glucose, newborn calf
adult

enzyme: aldose 1-epimerase

substrate: alpha-D-glucose


enzyme_display_name: adenylate cyclase

substrate_name: ATP

assay_conditions_summary: cofactor ATP

enzyme: adenylate cyclase

substrate: ATP


enzyme_display_name: thromboxane-A synthase

substrate_name: prostaglandin H2

proof_lines:
immobilized enzyme
soluble enzyme

enzyme: thromboxane-A synthase

substrate: prostaglandin H2


enzyme_display_name: isopentenyl-diphosphate Delta-isomerase

organism: Choristoneura fumiferana

substrate_name: isopentenyl diphosphate

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

proof_lines: wild type enzyme, in 25 mM Tris-HCl, pH 7.0, at 37°C

enzyme: isopentenyl-diphosphate Delta-isomerase

substrate: isopentenyl diphosphate


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

mutation_type: substitution

proof_lines: mutant enzyme Y105F, in 25 mM Tris-HCl, pH 7.0, at 37°C


proof_lines: mutant enzyme E169Q, in 25 mM Tris-HCl, pH 7.0, at 37°C


proof_lines: mutant enzyme W216F, in 25 mM Tris-HCl, pH 7.0, at 37°C


proof_lines: mutant enzyme Y159F, in 25 mM Tris-HCl, pH 7.0, at 37°C


organism: Burkholderia lata


organism: Archaeoglobus fulgidus

proof_lines: pH 7.3, 23°C, conversion to (3E)-2-oxohex-3-enedioate


substrate_name: phenylenolpyruvate

substrate: phenylenolpyruvate


organism: Helicobacter pylori


organism: Gammaproteobacteria bacterium


substrate_name: propiolate

substrate: propiolate


organism: Methylibium petroleiphilum

assay_conditions_summary: pH 7.3; 297.15 K; buffer 10 mM potassium phosphate

proof_lines: isoform 4-oxalocrotonate tautomerase II, in 10 mM potassium phosphate buffer, pH 7.3, at 24°C

proof_lines: isoform 4-oxalocrotonate tautomerase I, in 10 mM potassium phosphate buffer, pH 7.3, at 24°C


organism: Chloroflexus aurantiacus

proof_lines: pH 7.3, 24°C, recombinant hh4-OT mutant betaP1A

proof_lines: pH 7.3, 24°C, recombinant hh4-OT mutant alphaR12A

proof_lines: pH 7.3, 24°C, recombinant hh4-OT mutant betaR39A


proof_lines: pH 7.3, 24°C, recombinant wild-type hh4-OT


organism: Cinchona robusta

proof_lines:
isomerase II
isomerase I


substrate_name: dimethylallyl diphosphate

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

substrate: dimethylallyl diphosphate


organism: Narcissus pseudonarcissus


enzyme_display_name: vinylacetyl-CoA Delta-isomerase

substrate_name: vinylacetyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: vinylacetyl-CoA Delta-isomerase

substrate: vinylacetyl-CoA


enzyme_display_name: steroid Delta-isomerase

organism: Nocardia erythropolis

enzyme: steroid Delta-isomerase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R39A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; buffer 10 mM potassium phosphate

proof_lines: mutant enzyme R39A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R11A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R11A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C


organism: Saccharolobus shibatae

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q160N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6

proof_lines: mutant enzyme Q160N, in 50 mM MOPS-NaOH, pH 6.0, at 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q160L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q160L, in 50 mM MOPS-NaOH, pH 6.0, at 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q160H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q160H, in 50 mM MOPS-NaOH, pH 6.0, at 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q160E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q160E, in 50 mM MOPS-NaOH, pH 6.0, at 60°C


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

sequence_source: multiple

assay_conditions_summary: pH 6; 333.15 K; cofactor NADH

proof_lines:
pH 6.0, 60°C
pH 6.0
Raw SKiD Env: Temp=60°C, pH=6

source_databases_merged: brenda skid uniprot


substrate_name: NADH

assay_conditions_summary: cofactor NADH

proof_lines: dehydrogenase reaction without isopentenyl diphosphate

source_databases_merged: brenda skid

substrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E118A/N120A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R72A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y14F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y14F, at pH 7.0, temperature not specified in the publication


organism: Aedes aegypti

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

proof_lines: in 0.4 M Tris, 1 mM dithiothreitol, 10 mM MgCl2, pH 8.0, at 50°C


organism: Methanocaldococcus jannaschii

proof_lines: kcat is 191 sec(-1) for isomerase activity with IPP.

source_databases_merged: brenda uniprot


organism: Homo sapiens

substrate_name: dehydroepiandrosterone

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q240R with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

substrate: dehydroepiandrosterone


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R240Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q105M to reconstruct the assayed variant sequence.

proof_lines:
mutant Q105M, isoform 1, 27°C, pH 7.4
mutant Q105M, isoform 2, 27°C, pH 7.4


organism: Rattus norvegicus

substrate_name: dihydrotestosterone (in the presence of NADPH)

source_db: uniprot

assay_conditions_summary: cofactor NADPH

proof_lines: Vmax for dihydrotestosterone reduction is 15-fold higher in the presence of NADH than in the presence of NADPH.

source: uniprot


organism: Streptomyces sp. (strain SA-COO)

substrate_name: cholesterol

proof_lines: kcat is 44 sec(-1) for the oxidation of cholesterol. kcat is 64 sec(-1) for the isomerization of cholest-5-en-3-one.

substrate: cholesterol


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D265N to reconstruct the assayed variant sequence.


organism: Pseudomonas putida

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y30F/Y55F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W92A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W92A/L125A/V127A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L125F/V127F with inferred residue-numbering offset -26 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L125A/V127A with inferred residue-numbering offset -26 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y115F with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y115F, at pH 7.0, temperature not specified in the publication


organism: Bacillus subtilis (strain 168)

substrate_name: (p-hydroxyphenyl)-enolpyruvate

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

proof_lines: kcat is 3 sec(-1) for 2-hydroxy-2,4-heptadiene-1,7-dioate, 4.1 sec(-1) for (p-hydroxyphenyl)-enolpyruvate, 10 sec(-1) for 2-hydroxymuconate, 26 sec(-1) for 2-hydroxymuconate, 112 sec(-1) for 2-hydroxy-2,4-pentadienoate, 125 sec(-1) for phen

substrate: (p-hydroxyphenyl)-enolpyruvate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R11A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R39A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R39Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Comamonas testosteroni


source_db: skid

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7
Raw SKiD Env: Temp=°C, pH=7

source: skid


proof_lines: mutant enzyme Y30F/Y55F, at pH 7.0, temperature not specified in the publication


organism: Escherichia coli (strain K12)


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q105M with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines:
mutant Q105M, isoform 2, 27°C, pH 7.4
mutant Q105M, isoform 1, 27°C, pH 7.4


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M187T with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


proof_lines: wild type enzyme, in 50 mM MOPS-NaOH, pH 6.0, at 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q160K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q160K, in 50 mM MOPS-NaOH, pH 6.0, at 60°C


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y14F/Y30F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature Y14F/Y55F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y14F/Y30F/Y55F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: 25°C, pH 7.0, mutant enzyme Y14F/Y30F/Y55F


substrate_name: 2-hydroxymuconate (with 2-oxo-4-hexenedioate as product)

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


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A9W9U6 and applied mutation signature R12A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 297.15 K; buffer this pass. Assay condition: 10 mM potassium phosphate

column_label: Table 3: Kinetic Parameters for 4-Oxalocrotonate Tautomerases using Phenylenolpyruvate (3) (Biochemistry 2010, 49(24):5016-5027), enzyme row 'αR12A'; column 'kcat (s−1)' = 0.6; column 'Km (μM)' = 143; column 'kcat/Km (M−1 s−1)' = 4.2 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.6 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 0.6 s^(-1). Km: printed Table 3 cell 143 uM; 143 / 1000 = 0.143 mM; the exported value is 0.143 mM. kcat/Km: printed Table 3 cell 4.2 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.2 x 10^3 / 1000 = 4.2 s^-1 mM^-1, which is the paper's two-significant-figure printing of the exact quotient 0.6 / 0.143 = 4.195804195804196 s^-1 mM^-1 that the catalog carries.

raw_value_unit_evidence: Table 3, enzyme row αR12A: column kcat (s−1) = 0.6; column Km (μM) = 143; column kcat/Km (M−1 s−1) = 4.2 x 10^3.

row_label: Table 3, enzyme row αR12A

status: verified


column_label: Table 3: Kinetic Parameters for 4-Oxalocrotonate Tautomerases using Phenylenolpyruvate (3) (Biochemistry 2010, 49(24):5016-5027), enzyme row 'hh4-OT (wild type)'; column 'kcat (s−1)' = 13; column 'Km (μM)' = 121; column 'kcat/Km (M−1 s−1)' = 1.1 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 13 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 13.0 s^(-1). Km: printed Table 3 cell 121 uM; 121 / 1000 = 0.121 mM; the exported value is 0.121 mM. kcat/Km: printed Table 3 cell 1.1 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^5 / 1000 = 110.0 s^-1 mM^-1, which is the paper's two-significant-figure printing of the exact quotient 13.0 / 0.121 = 107.43801652892563 s^-1 mM^-1 that the catalog carries.

raw_value_unit_evidence: Table 3, enzyme row hh4-OT (wild type): column kcat (s−1) = 13; column Km (μM) = 121; column kcat/Km (M−1 s−1) = 1.1 x 10^5.

row_label: Table 3, enzyme row hh4-OT (wild type)


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61615 and applied mutation signature Q160E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 333.15 K; buffer 50 mM MOPS-NaOH

column_label: Table 2 (Kinetic parameters for Q160 mutants of S. shibatae IDI-2), Enzymes column row 'Q160E'; column 'kcat (x10^3 s^-1)' = 3.28 ± 0.31; column 'Km, uM' = 8.26 ± 1.41; column 'kcat/Km, M^-1 s^-1' = 397.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 3.28 under the column head kcat (x10^3 s^-1), so kcat is 3.28 / 10^3 = 0.00328 s^(-1). Km: the printed cell is 8.26 uM; 8.26 / 1000 = 0.00826 mM. kcat/Km: the printed cell is 397 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 397 / 1000 = 0.397 s^-1 mM^-1. Closure of the paper's own three printed cells: 0.00328 / 0.00826 = 0.397094 s^-1 mM^-1, which rounds to the printed efficiency cell 397 M^-1 s^-1 at the precision the paper prints.

raw_value_unit_evidence: Table 2 (Kinetic parameters for Q160 mutants of S. shibatae IDI-2), Enzymes row 'Q160E': the kcat column, whose printed head is kcat (x10^3 s^-1), prints 3.28 ± 0.31; the Km column, printed head Km, uM, prints 8.26 ± 1.41; the catalytic-efficiency column, printed head kcat/Km, M^-1 s^-1, prints 397.

row_label: Table 2, Enzymes row 'Q160E' (Gln160 replaced, S. shibatae IDI-2)

table_label: Table 2: Kinetic parameters for Q160 mutants of S. shibatae IDI-2 (PNAS 2011, 108(51):20461-20466, page 20464)

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61615 and applied mutation signature Q160H to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for Q160 mutants of S. shibatae IDI-2), Enzymes column row 'Q160H'; column 'kcat (x10^3 s^-1)' = 1.21 ± 0.11; column 'Km, uM' = 7.13 ± 1.22; column 'kcat/Km, M^-1 s^-1' = 170.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 1.21 under the column head kcat (x10^3 s^-1), so kcat is 1.21 / 10^3 = 0.00121 s^(-1). Km: the printed cell is 7.13 uM; 7.13 / 1000 = 0.00713 mM. kcat/Km: the printed cell is 170 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 170 / 1000 = 0.17 s^-1 mM^-1. Closure of the paper's own three printed cells: 0.00121 / 0.00713 = 0.169705 s^-1 mM^-1, which rounds to the printed efficiency cell 170 M^-1 s^-1 at the precision the paper prints.

raw_value_unit_evidence: Table 2 (Kinetic parameters for Q160 mutants of S. shibatae IDI-2), Enzymes row 'Q160H': the kcat column, whose printed head is kcat (x10^3 s^-1), prints 1.21 ± 0.11; the Km column, printed head Km, uM, prints 7.13 ± 1.22; the catalytic-efficiency column, printed head kcat/Km, M^-1 s^-1, prints 170.

row_label: Table 2, Enzymes row 'Q160H' (Gln160 replaced, S. shibatae IDI-2)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61615 and applied mutation signature Q160L to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for Q160 mutants of S. shibatae IDI-2), Enzymes column row 'Q160L'; column 'kcat (x10^3 s^-1)' = 0.221 ± 0.014; column 'Km, uM' = 1.52 ± 0.3; column 'kcat/Km, M^-1 s^-1' = 145.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 0.221 under the column head kcat (x10^3 s^-1), so kcat is 0.221 / 10^3 = 0.000221 s^(-1). Km: the printed cell is 1.52 uM; 1.52 / 1000 = 0.00152 mM. kcat/Km: the printed cell is 145 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 145 / 1000 = 0.145 s^-1 mM^-1. Closure of the paper's own three printed cells: 0.000221 / 0.00152 = 0.145395 s^-1 mM^-1, which rounds to the printed efficiency cell 145 M^-1 s^-1 at the precision the paper prints.

raw_value_unit_evidence: Table 2 (Kinetic parameters for Q160 mutants of S. shibatae IDI-2), Enzymes row 'Q160L': the kcat column, whose printed head is kcat (x10^3 s^-1), prints 0.221 ± 0.014; the Km column, printed head Km, uM, prints 1.52 ± 0.3; the catalytic-efficiency column, printed head kcat/Km, M^-1 s^-1, prints 145.

row_label: Table 2, Enzymes row 'Q160L' (Gln160 replaced, S. shibatae IDI-2)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61615 and applied mutation signature Q160N to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for Q160 mutants of S. shibatae IDI-2), Enzymes column row 'Q160N'; column 'kcat (x10^3 s^-1)' = 0.197 ± 0.019; column 'Km, uM' = 3.23 ± 0.75; column 'kcat/Km, M^-1 s^-1' = 61.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 0.197 under the column head kcat (x10^3 s^-1), so kcat is 0.197 / 10^3 = 0.000197 s^(-1). Km: the printed cell is 3.23 uM; 3.23 / 1000 = 0.00323 mM. kcat/Km: the printed cell is 61 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 61 / 1000 = 0.061 s^-1 mM^-1. Closure of the paper's own three printed cells: 0.000197 / 0.00323 = 0.060991 s^-1 mM^-1, which rounds to the printed efficiency cell 61 M^-1 s^-1 at the precision the paper prints.

raw_value_unit_evidence: Table 2 (Kinetic parameters for Q160 mutants of S. shibatae IDI-2), Enzymes row 'Q160N': the kcat column, whose printed head is kcat (x10^3 s^-1), prints 0.197 ± 0.019; the Km column, printed head Km, uM, prints 3.23 ± 0.75; the catalytic-efficiency column, printed head kcat/Km, M^-1 s^-1, prints 61.

row_label: Table 2, Enzymes row 'Q160N' (Gln160 replaced, S. shibatae IDI-2)


substrate_name: isopentenyl

assay_conditions_summary: pH 8

column_label: Abstract reports K(IPP)(m) value of 22.8 microm IPP.

raw_value_unit_evidence: Km raw_value=22.8 microM raw_unit=microM

row_label: human IDI2 / IPP

table_label: PubMed XML abstract PMID 17202134

substrate: isopentenyl


organism: Saccharomyces cerevisiae


sequence_variant_note: Mutation signature L141H/Y195F/W256C could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme L141H/Y195F/W256C, at pH 7.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R39A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A9W9U6 and applied mutation signature R40A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters for 4-Oxalocrotonate Tautomerases using Phenylenolpyruvate (3) (Biochemistry 2010, 49(24):5016-5027), enzyme row 'αR40A'; column 'kcat (s−1)' = 44; column 'Km (μM)' = 152; column 'kcat/Km (M−1 s−1)' = 2.9 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 44 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 44.0 s^(-1). Km: printed Table 3 cell 152 uM; 152 / 1000 = 0.152 mM; the exported value is 0.152 mM. kcat/Km: printed Table 3 cell 2.9 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.9 x 10^5 / 1000 = 290.0 s^-1 mM^-1, which is the paper's two-significant-figure printing of the exact quotient 44.0 / 0.152 = 289.4736842105263 s^-1 mM^-1 that the catalog carries.

raw_value_unit_evidence: Table 3, enzyme row αR40A: column kcat (s−1) = 44; column Km (μM) = 152; column kcat/Km (M−1 s−1) = 2.9 x 10^5.

row_label: Table 3, enzyme row αR40A


sequence_variant_note: Mutation signature P1A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature R11A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


column_label: Table 2: Kinetic Parameters for 4-Oxalocrotonate Tautomerases using 2-Hydroxymuconate (1) (Biochemistry 2010, 49(24):5016-5027), enzyme row 'αR12A'; column 'kcat (s−1)' = 43; column 'Km (μM)' = 1033; column 'kcat/Km (M−1 s−1)' = 4.2 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 43 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 43.0 s^(-1). Km: printed Table 2 cell 1033 uM; 1033 / 1000 = 1.033 mM; the exported value is 1.033 mM. kcat/Km: printed Table 2 cell 4.2 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.2 x 10^4 / 1000 = 42.0 s^-1 mM^-1, which is the paper's two-significant-figure printing of the exact quotient 43.0 / 1.033 = 41.626331074540175 s^-1 mM^-1 that the catalog carries.

raw_value_unit_evidence: Table 2, enzyme row αR12A: column kcat (s−1) = 43; column Km (μM) = 1033; column kcat/Km (M−1 s−1) = 4.2 x 10^4.

row_label: Table 2, enzyme row αR12A


column_label: Table 2: Kinetic Parameters for 4-Oxalocrotonate Tautomerases using 2-Hydroxymuconate (1) (Biochemistry 2010, 49(24):5016-5027), enzyme row 'αR40A'; column 'kcat (s−1)' = 65; column 'Km (μM)' = 345; column 'kcat/Km (M−1 s−1)' = 1.9 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 65 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 65.0 s^(-1). Km: printed Table 2 cell 345 uM; 345 / 1000 = 0.345 mM; the exported value is 0.345 mM. kcat/Km: printed Table 2 cell 1.9 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.9 x 10^5 / 1000 = 190.0 s^-1 mM^-1, which is the paper's two-significant-figure printing of the exact quotient 65.0 / 0.345 = 188.40579710144928 s^-1 mM^-1 that the catalog carries.

raw_value_unit_evidence: Table 2, enzyme row αR40A: column kcat (s−1) = 65; column Km (μM) = 345; column kcat/Km (M−1 s−1) = 1.9 x 10^5.

row_label: Table 2, enzyme row αR40A


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

column_label: Table 2: Kinetic Parameters for 4-Oxalocrotonate Tautomerases using 2-Hydroxymuconate (1) (Biochemistry 2010, 49(24):5016-5027), enzyme row 'hh4-OT (wild type)'; column 'kcat (s−1)' = 3000; column 'Km (μM)' = 70; column 'kcat/Km (M−1 s−1)' = 4.3 x 10^7.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3000 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 3000.0 s^(-1). Km: printed Table 2 cell 70 uM; 70 / 1000 = 0.07 mM; the exported value is 0.07 mM. kcat/Km: printed Table 2 cell 4.3 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.3 x 10^7 / 1000 = 43000.0 s^-1 mM^-1, which is the paper's two-significant-figure printing of the exact quotient 3000.0 / 0.07 = 42857.142857142855 s^-1 mM^-1 that the catalog carries.

raw_value_unit_evidence: Table 2, enzyme row hh4-OT (wild type): column kcat (s−1) = 3000; column Km (μM) = 70; column kcat/Km (M−1 s−1) = 4.3 x 10^7.

row_label: Table 2, enzyme row hh4-OT (wild type)


organism: Archaeoglobus fulgidus

assay_conditions_summary: pH 7.3; 296.15 K; buffer 20 mM NaH2PO4

column_label: Table 4 AfDmpI reaction 1 -> 5 reports kcat 0.2, Km 170 uM, and kcat/Km 1.2 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized 0.2 s^-1; Km normalized 0.17 mM; kcat/Km normalized 1.2 s^-1 mM^-1.

row_label: AfDmpI reaction 1 -> 5

table_label: PMC2963697 Table 4, kinetic parameters for AfDmpI using 1, 3, and 7


normalized_value_unit_evidence: kcat 2.4 s^-1; Km 0.09 mM; independently printed kcat/Km 27 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row 7 -> 8: kcat 2.4 +/- 0.3 s^-1; Km 90 +/- 20 uM; independently printed kcat/Km 2.7 x 10^4 M^-1 s^-1.

table_label: Table 4. Kinetic parameters for AfDmpI using 1, 3, and 7


column_label: Table 4 AfDmpI reaction 3 -> 6 reports kcat 0.1, Km 90 uM, and kcat/Km 1.1 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized 0.1 s^-1; Km normalized 0.09 mM; kcat/Km normalized 1.1 s^-1 mM^-1.

row_label: AfDmpI reaction 3 -> 6


organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

substrate_name: IPP (at pH 7.6 and 37 degrees Celsius)

proof_lines: kcat is 17.9 sec(-1) for isomerase activity with IPP (at pH 7.6 and 37 degrees Celsius).

substrate: IPP (at pH 7.6 and 37 degrees Celsius)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E13R/R235E with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M187T with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Escherichia coli

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

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

source_databases_merged: skid uniprot


organism: Microcystis aeruginosa

substrate_name: 2,3-diketo-5-methylthiopentyl-1-phosphate (at pH 8 and 37 degrees Celsius)

smiles: CSCCC(=O)C(=O)COP(=O)(O)O


organism: Methylibium petroleiphilum


organism: Streptomyces sp.

substrate_name: Isopentenyl diphosphate

assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH

substrate: Isopentenyl diphosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P39A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P39G with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


organism: Staphylococcus aureus

assay_conditions_summary: pH 7; 310.15 K; cofactor FMN


column_label: Results paragraph tied to Figure 3 reports DMAPP Km=14.3 +/- 0.8 microM.

raw_value_unit_evidence: Kms for DMAPP and IPP were 14.3 +/- 0.8 and 9.5 +/- 0.5 microM, respectively.

row_label: Recombinant E. coli IPP isomerase / DMAPP

table_label: Official PMC result text / Figure 3 product inhibition kinetics


organism: Clostridium aminobutyricum


assay_conditions_summary: pH 7.5; 303.15 K; buffer 50 mM MOPS

column_label: Table 1 row IDI lists Km 41.5 +/- 0.39 uM, Kcat 8.27 +/- 0.06 s^-1, and Kcat/Km 0.20 s^-1 uM^-1. The results prose states the Km decreased from 41.5 +/- 0.39 to 37.6 +/- 0.17 uM, kcat increased from 8.27 +/- 0.06 to 10.57 +/- 0.13 s^-1, and catalytic efficiency from 0.20 to 0.28 s^-1 uM^-1.

normalized_value_unit_evidence: Km normalized_value=0.0415 normalized_unit=mM; kcat normalized_value=8.27 normalized_unit=s^-1; kcat/Km CatLog computed normalized_value=199.27710843373492 normalized_unit=s^-1 mM^-1 from 8.27/0.0415; paper printed rounded normalized ratio=200 s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=41.5 +/- 0.39 raw_unit=uM; kcat raw_value=8.27 +/- 0.06 raw_unit=s^-1; kcat/Km printed raw_value=0.20 raw_unit=s^-1 uM^-1

row_label: IDI

table_label: Table 1, kinetic parameters of IDI and IDI (L141H/Y195F/W256C)


organism: Thermococcus kodakarensis


organism: Homo sapiens

substrate_name: dehydroepiandrosterone (in the presence of NAD(+))


substrate_name: pregnenolone (in the presence of NAD(+))


substrate_name: dihydrotestosterone (in the presence of NADH)


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P1A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


column_label: PMC Table 1 row for compound 5 reports kcat 112 +/- 14 s^-1, Km 243 +/- 42 uM, kcat/Km 4.6 +/- 0.8 x 10^5 M^-1 s^-1; Table 2 identifies YwhB wt conversion of 5 to 4 with the same values.

normalized_value_unit_evidence: kcat/Km normalized_value=460.0 s^-1*mM^-1; same row kcat=112 s^-1 and Km=0.243 mM gives 460.905 s^-1*mM^-1

raw_value_unit_evidence: kcat/Km raw_value=4.6 x 10^5 raw_unit=M^-1 s^-1

row_label: compound 5 / YwhB wt conversion of 5 to 4

table_label: Table 1; Table 2


assay_conditions_summary: pH 7.3; 296.15 K; buffer Assay condition: 20 mM NaH2PO4

column_label: Table 1 compound 11 row reports kcat = 3.0 +/- 0.4 s^-1, Km = 335 +/- 55 uM, and kcat/Km = 9.0 +/- 1.5 x 10^3 M^-1 s^-1; article text identifies compound 11 as 2-hydroxy-2,4-heptadiene-1,7-dioate.

normalized_value_unit_evidence: kcat 3.0 s^-1 from explicit paper cell; kcat_over_km 9.0 s^-1 mM^-1 from explicit paper cell; km 0.335 mM from explicit paper cell

raw_value_unit_evidence: kcat raw_value=3.0 raw_unit=s^-1; Km raw_value=335 raw_unit=uM; kcat/Km raw_value=9.0e3 raw_unit=M^-1 s^-1

row_label: compound 11 / 2-hydroxy-2,4-heptadiene-1,7-dioate

table_label: Table 1 - Kinetic Parameters for YwhB Using Enol and Dienol Substrates


column_label: PMC Table 1 row for compound 8 reports kcat 4.1 +/- 0.4 s^-1, Km 160 +/- 22 uM, kcat/Km 2.6 +/- 0.4 x 10^4 M^-1 s^-1.

normalized_value_unit_evidence: kcat/Km normalized_value=26.0 s^-1*mM^-1; same row kcat=4.1 s^-1 and Km=0.160 mM gives 25.625 s^-1*mM^-1

raw_value_unit_evidence: kcat/Km raw_value=2.6 x 10^4 raw_unit=M^-1 s^-1

row_label: compound 8 / p-hydroxyphenyl(enol)pyruvate

table_label: Table 1


substrate_name: Enol-Phenylpyruvate

substrate: Enol-Phenylpyruvate


column_label: PMC Table 1 row for compound 7 reports kcat 125 +/- 18 s^-1, Km 300 +/- 60 uM, kcat/Km 4.2 +/- 0.8 x 10^5 M^-1 s^-1; Table 3 identifies YwhB wt conversion of 7 to 9 with the same values.

normalized_value_unit_evidence: kcat/Km normalized_value=420.0 s^-1*mM^-1; same row kcat=125 s^-1 and Km=0.300 mM gives 416.667 s^-1*mM^-1

raw_value_unit_evidence: kcat/Km raw_value=4.2 x 10^5 raw_unit=M^-1 s^-1

row_label: compound 7 / YwhB wt conversion of 7 to 9

table_label: Table 1; Table 3


organism: Pseudomonas putida

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.


substrate_name: isopentenyl diphosphate


proof_lines:
wild-type enzyme
wild-type, pH 7.4, 37°C


substrate_name: pregnenolone

substrate: pregnenolone


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D241N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D265N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D36A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.4; 300.15 K; cofactor NADH


substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D36A/K37R to reconstruct the assayed variant sequence.

substrate: NADPH


proof_lines:
below, pH 7.3, 23°C, mutant R11A/R39A
pH 7.3, 23°C, mutant R11A/R39A


assay_conditions_summary: pH 7.3; 295.15 K; buffer 10 mM potassium phosphate

proof_lines: mutant enzyme P1A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C


proof_lines: wild type enzyme, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C


proof_lines: mutant enzyme R61A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C


organism: Streptococcus pneumoniae

proof_lines: wild type enzyme, at anaerobic conditions, at pH 7.0 and 37°C

proof_lines: wild type enzyme, at aerobic conditions, at pH 7.0 and 37°C


proof_lines: mutant enzyme N37A, at aerobic conditions, at pH 7.0 and 37°C


substrate_name: Unknown

substrate: Unknown


organism: Comamonas testosteroni


proof_lines: mutant enzyme K122R, in 50 mM Tris-HCl (pH 8.2), 1 mM MgCl2, at 25°C


proof_lines: wild type enzyme, in 50 mM Tris-HCl (pH 8.2), 1 mM MgCl2, at 25°C


enzyme_display_name: muconolactone Delta-isomerase

organism: Cupriavidus necator

enzyme: muconolactone Delta-isomerase


proof_lines: pH and temperature not specified in the publication


proof_lines: in 50 mM HEPES (pH 7.2) containing 10 mM MgCl2, 200 mM KCl, 1 mg/ml bovine serum albumin, 0.5 mM dithiothreitol, at 37°C


proof_lines: 25°C, pH 7.0, mutant enzyme Y14F/Y30F/Y55F/D99L


proof_lines: 25°C, pH 7.0, mutant enzyme Y14F/Y30F/Y55F/D99N


sequence_source: UniProtKB/Swiss-Prot P07445

sequence_variant_note: Resolved canonical sequence from UniProtKB/Swiss-Prot P07445 and applied mutation signature Y55F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y55F, at pH 7.0, temperature not specified in the publication


sequence_variant_note: Mutation signature Y30F/Y55F/Y115F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme Y30F/Y55F/Y115F, at pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +12, so it is treated as a source-provided variant sequence.

proof_lines: mutant enzyme Y30F, at pH 7.0, temperature not specified in the publication


proof_lines: wild type enzyme, at pH 7.0, temperature not specified in the publication


enzyme_display_name: pancreatic ribonuclease

organism: Bos taurus

substrate_name: RNA

proof_lines:
pH 7.0, 37°C
pH 5.5, 25°C, comercial enzyme
pH 5.5, 25°C, type I enzyme

enzyme: pancreatic ribonuclease

substrate: RNA


organism: Bombyx mori

substrate: isopentenyl diphosphate


substrate_name: 2',3'-cyclic UMP

substrate: 2',3'-cyclic UMP


substrate_name: uronic acid residues

substrate: uronic acid residues


enzyme_display_name: ribulose-phosphate 3-epimerase

substrate_name: D-ribulose 5-phosphate

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

enzyme: ribulose-phosphate 3-epimerase

substrate: D-ribulose 5-phosphate


enzyme_display_name: UDP-glucose 4-epimerase

substrate_name: UDPgalactose

proof_lines:
mammary enzyme
liver enzyme

enzyme: UDP-glucose 4-epimerase

substrate: UDPgalactose


enzyme_display_name: mandelate racemase

substrate_name: 2-hydroxy-3-butenoic acid

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

enzyme: mandelate racemase

substrate: 2-hydroxy-3-butenoic acid


substrate_name: muconolactone

substrate: muconolactone


enzyme_display_name: protein disulfide-isomerase

substrate_name: scrambled ribonuclease

proof_lines: scrambled, with dithiothreitol as substrate

enzyme: protein disulfide-isomerase

substrate: scrambled ribonuclease


enzyme_display_name: methionine gamma-lyase

organism: Brevibacterium linens

substrate_name: L-methionine

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

enzyme: methionine gamma-lyase

substrate: L-methionine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N120A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


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


enzyme_display_name: 4-hydroxyproline epimerase

organism: Brucella abortus

enzyme: 4-hydroxyproline epimerase


organism: Brucella suis


organism: Brucella anthropi

substrate_name: L-rhamnose

substrate: L-rhamnose


organism: Brucella melitensis


organism: Brugia malayi


substrate_name: D-allose

substrate: D-allose


enzyme_display_name: mannose-6-phosphate isomerase

organism: Burkholderia cepacia

substrate_name: D-mannose 6-phosphate

proof_lines: pH 7.6, 5 mM Mg2+, temperature not specified in the publication

enzyme: mannose-6-phosphate isomerase

substrate: D-mannose 6-phosphate


enzyme_display_name: phosphoenolpyruvate mutase

organism: Burkholderia gladioli

substrate_name: Phosphonopyruvate

enzyme: phosphoenolpyruvate mutase

substrate: Phosphonopyruvate


enzyme_display_name: glutamate racemase

organism: Burkholderia cenocepacia

substrate_name: D-glutamate

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

assay_conditions_summary: pH 8; 310.15 K; buffer HEPES

enzyme: glutamate racemase

substrate: D-glutamate


enzyme_display_name: UniProt Q2PS28

organism: Paraburkholderia acidicola

substrate_name: D-glucose

enzyme: UniProt Q2PS28

substrate: D-glucose


substrate_name: isomaltulose

substrate: isomaltulose


substrate_name: Trehalulose

substrate: Trehalulose


enzyme_display_name: UniProt D9MPF2

organism: Erwinia rhapontici

substrate_name: sucrose

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

proof_lines:
Raw SKiD Env: Temp=30°C, pH=-----
Raw SKiD Env: Temp=30°C, pH=6

enzyme: UniProt D9MPF2

substrate: sucrose


enzyme_display_name: UniProt Q8KR84

organism: Klebsiella sp. LX3

enzyme: UniProt Q8KR84


organism: Saccharolobus solfataricus

substrate_name: maltoheptaose

substrate: maltoheptaose


substrate_name: maltohexaose

substrate: maltohexaose


substrate_name: maltopentaose

substrate: maltopentaose


substrate_name: maltotetraose

substrate: maltotetraose


substrate_name: maltotriose

substrate: maltotriose


enzyme_display_name: maltose alpha-D-glucosyltransferase

organism: Deinococcus geothermalis

substrate_name: maltose

enzyme: maltose alpha-D-glucosyltransferase

substrate: maltose


enzyme_display_name: alanine racemase

organism: Caldanaerobacter subterraneus subsp. tengcongensis

substrate_name: D-alanine

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

enzyme: alanine racemase

substrate: D-alanine


proof_lines: pH 10.0, 65°C, recombinant wild-type enzyme


organism: Campylobacter jejuni subsp. jejuni

substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


organism: Burkholderia pseudomallei


organism: Brevibacillus brevis

substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


enzyme_display_name: isomaltulose synthase

enzyme: isomaltulose synthase


organism: Erwinia sp. Ejp617


organism: Enterobacter hormaechei

assay_conditions_summary: pH 6; 310.15 K; buffer 50 mM phosphate

proof_lines: in 50 mM phosphate buffer (pH 6) at 37°C


substrate_name: alpha,alpha-trehalose

substrate: alpha,alpha-trehalose


organism: Rhodococcus rhodochrous


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

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

proof_lines: immobilized recombinant enzyme, pH 6.0, 30°C


enzyme_display_name: serine racemase

organism: Caenorhabditis elegans

substrate_name: L-serine

sequence_source: UniProtKB Q93968

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

enzyme: serine racemase

substrate: L-serine


organism: Erwinia sp. D12

proof_lines: pH not specified in the publication, 40°C, native enzyme


proof_lines: pH 6.0, temperature not specified in the publication, enzyme immobilized on graphene oxide with addition of surfactant NP40

proof_lines: pH 6.0, temperature not specified in the publication, soluble enzyme


organism: Picrophilus oshimae

proof_lines:
45°C, pH 6.0
45°C, pH 6.0, presence of 10 mM glucose


substrate_name: trehalose

substrate: trehalose


enzyme_display_name: isobutyryl-CoA mutase

organism: Xanthobacter autotrophicus

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

enzyme: isobutyryl-CoA mutase


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

assay_conditions_summary: cofactor CoA


organism: Pantoea dispersa

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

proof_lines: pH and temperature not specified in the publication


organism: Paraburkholderia acidicola

substrate_name: Unknown

substrate: Unknown


organism: Raoultella terrigena


proof_lines: pH not specified in the publication, 20°C, native enzyme

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


organism: Nostoc flagelliforme

assay_conditions_summary: pH 7; 323.15 K; buffer 50 mM phosphate-citric acid

proof_lines: recombinant enzyme, in 50 mM phosphate-citric acid buffer (0.2 M Na3PO4, 0.1 M citric acid, pH 7.0) at 50°C


organism: Saccharolobus solfataricus

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P95869 and applied mutation signature Y290F to reconstruct the assayed variant sequence.

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 Y290F, transglycosylation column G6; printed row label kcat (s-1) = 26.5; printed row label KM (mM) = 6.00; printed row label kcat/KM (s-1 mM-1) = 4.45. captured primary segment: Y290F MTSase | maltohexaose G6 | kcat 26.5 s^-1 | KM 6.00 mM | kcat/KM 4.45 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 6.00 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 6.0 mM. kcat: printed Table 3 kcat cell 26.5 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 26.5 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 4.45 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 4.45 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 26.5 / 6.00 = 4.416666666666667 s^-1 mM^-1, against the printed catalytic-efficiency cell 4.45 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, MTSase form block Y290F, transglycosylation column G6: kcat = 26.5 s^-1; KM = 6.00 mM; printed kcat/KM = 4.45 s^-1 mM^-1.

row_label: Table 3, MTSase form block Y290F, transglycosylation column G6 (maltohexaose)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P95869 and applied mutation signature Y409F 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 Y409F, transglycosylation column G4; printed row label kcat (s-1) = 114; printed row label KM (mM) = 16.1; printed row label kcat/KM (s-1 mM-1) = 7.07. captured primary segment: Y409F MTSase | maltotetraose G4 | kcat 114 s^-1 | KM 16.1 mM | kcat/KM 7.07 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 16.1 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 16.1 mM. kcat: printed Table 3 kcat cell 114 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 114.0 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 7.07 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 7.07 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 114 / 16.1 = 7.080745341614906 s^-1 mM^-1, against the printed catalytic-efficiency cell 7.07 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, MTSase form block Y409F, transglycosylation column G4: kcat = 114 s^-1; KM = 16.1 mM; printed kcat/KM = 7.07 s^-1 mM^-1.

row_label: Table 3, MTSase form block Y409F, transglycosylation column G4 (maltotetraose)


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 G4; printed row label kcat (s-1) = 138; printed row label KM (mM) = 13.2; printed row label kcat/KM (s-1 mM-1) = 10.4. captured primary segment: wild-type MTSase | maltotetraose G4 | kcat 138 s^-1 | KM 13.2 mM | kcat/KM 10.4 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 13.2 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 13.2 mM. kcat: printed Table 3 kcat cell 138 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 138.0 s^(-1). kcat/Km: printed Table 3 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: 138 / 13.2 = 10.454545454545455 s^-1 mM^-1, against the printed catalytic-efficiency cell 10.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, MTSase form block wild-type, transglycosylation column G4: kcat = 138 s^-1; KM = 13.2 mM; printed kcat/KM = 10.4 s^-1 mM^-1.

row_label: Table 3, MTSase form block wild-type, transglycosylation column G4 (maltotetraose)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P95869 and applied mutation signature Y367F 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 Y367F, transglycosylation column G6; printed row label kcat (s-1) = 139; printed row label KM (mM) = 3.78; printed row label kcat/KM (s-1 mM-1) = 36.9. captured primary segment: Y367F MTSase | maltohexaose G6 | kcat 139 s^-1 | KM 3.78 mM | kcat/KM 36.9 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 3.78 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 3.78 mM. kcat: printed Table 3 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 3 kcat/KM cell 36.9 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 36.9 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 139 / 3.78 = 36.77248677248677 s^-1 mM^-1, against the printed catalytic-efficiency cell 36.9 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, MTSase form block Y367F, transglycosylation column G6: kcat = 139 s^-1; KM = 3.78 mM; printed kcat/KM = 36.9 s^-1 mM^-1.

row_label: Table 3, MTSase form block Y367F, transglycosylation column G6 (maltohexaose)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique 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 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)


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)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y409F 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 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)


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)


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)


organism: Serratia plymuthica

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


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).


organism: Geobacillus kaustophilus (strain HTA426)

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

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

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


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


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.


organism: Thermus aquaticus

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


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)


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.


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)


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


organism: Escherichia coli

substrate_name: CO2; Aminoimidazole ribotide

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)

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

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.

substrate_name: sucrose

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

substrate: sucrose


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


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


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


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


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

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

substrate_name: maltose


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


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)


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

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

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