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

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

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

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

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


enzyme_display_name: isobutyryl-CoA mutase

organism: Cupriavidus metallidurans

source_db: oed

verification_status: verified

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

mutation_type: substitution

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

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

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

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

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

data_origin: experimental

enzyme: isobutyryl-CoA mutase

status: verified

source: oed


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

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

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

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

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


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


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


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

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

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

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

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


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

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

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

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

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


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

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

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

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


organism: Cupriavidus necator

source_db: brenda

mutation_signature: Unknown

sequence_source: multiple

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

source_databases_merged: brenda uniprot

source: brenda


enzyme_display_name: squalene--hopene cyclase

organism: Alicyclobacillus acidocaldarius

substrate_name: squalene

verification_status: corrected

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; 318.15 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'; column 'Km (uM)' = 2.13 x 10; column 'kcat (min^-1)' = 20.7; column 'kcat/Km' = 9.72 x 10^-1.

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

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

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)

enzyme: squalene--hopene cyclase

substrate: squalene

status: corrected


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

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

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

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


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'; column 'Km (uM)' = 2.55 x 10; column 'kcat (min^-1)' = 26.9; column 'kcat/Km' = 1.05.

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

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


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

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

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

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

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 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'; column 'Km (uM)' = 1.69 x 10; column 'kcat (min^-1)' = 37.3; column 'kcat/Km' = 2.21.

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

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


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'; column 'Km (uM)' = 1.97 x 10^2; column 'kcat (min^-1)' = 38.5; column 'kcat/Km' = 1.95 x 10^-1.

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

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


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'; column 'Km (uM)' = 1.67 x 10; column 'kcat (min^-1)' = 44.1; column 'kcat/Km' = 2.64.

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

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

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


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

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

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

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


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

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

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

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

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 P263A to reconstruct the assayed variant sequence.

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

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

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


kcat_over_km_origin: calculated

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

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


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

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

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

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


enzyme_display_name: isomaltulose synthase

organism: Serratia plymuthica

substrate_name: sucrose

verification_status: unverified

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

enzyme: isomaltulose synthase

substrate: sucrose

status: unverified


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


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


enzyme_display_name: maltose alpha-D-glucosyltransferase

organism: Pseudomonas putida

substrate_name: maltose

kcat_display: Not reported

kcat_over_km_display: Not reported

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

enzyme: maltose alpha-D-glucosyltransferase

substrate: maltose


organism: Sulfolobus acidocaldarius

substrate_name: maltopentaose

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

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

raw_value_unit_evidence: Km raw_value=7.1 mM raw_unit=mM

row_label: Sulfolobus acidocaldarius maltooligosyl trehalose synthase / maltopentaose

table_label: PubMed XML abstract PMID 9063973

substrate: maltopentaose


substrate_name: maltotetraose

raw_value_unit_evidence: Km raw_value=41.5 mM raw_unit=mM

row_label: Sulfolobus acidocaldarius maltooligosyl trehalose synthase / maltotetraose

substrate: maltotetraose


organism: Thermus antranikianii

substrate_name: alpha,alpha-trehalose

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

assay_conditions_summary: pH 7

substrate: alpha,alpha-trehalose


protein_accession_database: NCBI Protein


organism: Meiothermus ruber


organism: Saccharolobus solfataricus

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


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


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


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


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


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


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

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

row_label: Wild-type row; kcat/KM column

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


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

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

source_db: uniprot

source: uniprot


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


organism: Thermus thermophilus


organism: Mycolicibacterium smegmatis

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: Acetobacter aceti

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


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


organism: Streptomyces virginiae

substrate_name: butanoyl-CoA

assay_conditions_summary: pH 7.4; cofactor CoA

substrate: butanoyl-CoA


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

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

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

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

table_label: PubMed XML abstract PMID 10531377


substrate_name: isovaleryl-CoA

substrate: isovaleryl-CoA


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

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


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


organism: Escherichia coli (strain K12)


organism: Klebsiella sp.

km_display: Not reported

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


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


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


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


organism: Arthrobacter ramosus


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


organism: Escherichia coli

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


organism: Arthrobacter sp.

substrate_name: maltoheptaose

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

raw_value_unit_evidence: Km raw_value=0.9 raw_unit=mM for maltoheptaose

row_label: maltoheptaose in ordered Km prose list

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

substrate: maltoheptaose


substrate_name: maltohexaose

raw_value_unit_evidence: Km raw_value=1.4 raw_unit=mM for maltohexaose

row_label: maltohexaose in ordered Km prose list

substrate: maltohexaose


raw_value_unit_evidence: Km raw_value=8.7 raw_unit=mM for maltopentaose

row_label: maltopentaose in ordered Km prose list


raw_value_unit_evidence: Km raw_value=22.9 raw_unit=mM for maltotetraose

row_label: maltotetraose in ordered Km prose list


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


enzyme_display_name: tRNA pseudouridine(38-40) synthase

substrate_name: tRNA uridine39

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

enzyme: tRNA pseudouridine(38-40) synthase

substrate: tRNA uridine39


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


organism: Pseudarthrobacter chlorophenolicus


organism: Pseudomonas sp.


substrate_name: trehalose

substrate: trehalose


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


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


enzyme_display_name: aldose 1-epimerase

organism: Canis lupus familiaris

substrate_name: alpha-D-glucose

enzyme: aldose 1-epimerase

substrate: alpha-D-glucose


enzyme_display_name: isopentenyl-diphosphate Delta-isomerase

organism: Capsicum annuum

substrate_name: isopentenyl diphosphate

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

enzyme: isopentenyl-diphosphate Delta-isomerase

substrate: isopentenyl diphosphate


enzyme_display_name: adenylate cyclase

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

enzyme: adenylate cyclase


substrate_name: ATP

assay_conditions_summary: cofactor ATP

proof_lines: recombinant cytosolic domain of type V adenylyl cyclase

substrate: ATP


enzyme_display_name: UDP-arabinopyranose mutase

organism: Oryza sativa

substrate_name: UDP-beta-L-arabinopyranose

enzyme: UDP-arabinopyranose mutase

substrate: UDP-beta-L-arabinopyranose


substrate_name: UDP-beta-L-arabinofuranose

substrate: UDP-beta-L-arabinofuranose


organism: Chlamydomonas reinhardtii

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


organism: Oryza sativa subsp. japonica


enzyme_display_name: tRNA pseudouridine(32) synthase

substrate_name: tRNA uridine32

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

enzyme: tRNA pseudouridine(32) synthase

substrate: tRNA uridine32


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


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

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


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


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


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


enzyme_display_name: beta-amyrin synthase

organism: Euphorbia tirucalli

enzyme: beta-amyrin synthase


enzyme_display_name: glucose-6-phosphate isomerase

organism: Carassius auratus

substrate_name: D-fructose 6-phosphate

assay_conditions_summary: pH 8

enzyme: glucose-6-phosphate isomerase

substrate: D-fructose 6-phosphate


enzyme_display_name: UniProt P21638

organism: Pseudomonas denitrificans (nom. rej.)

substrate_name: Hydrogenobyrinate

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P21638

substrate: Hydrogenobyrinate

source: skid


enzyme_display_name: alpha-amyrin synthase

organism: Malus domestica

enzyme: alpha-amyrin synthase


enzyme_display_name: protostadienol synthase

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

enzyme: protostadienol synthase


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


substrate_name: UDP-L-arabinofuranose

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

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

row_label: rUAM3 / UDP-Araf

table_label: Table 1

substrate: UDP-L-arabinofuranose


substrate_name: UDP-L-arabinopyranose

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

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

row_label: rUAM3 / UDP-Arap

substrate: UDP-L-arabinopyranose


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

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

row_label: rUAM1 / UDP-Araf


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

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

row_label: rUAM1 / UDP-Arap


organism: Eriobotrya japonica


enzyme_display_name: 2-hydroxyisobutanoyl-CoA mutase

organism: Kyrpidia tusciae DSM 2912

assay_conditions_summary: pH 7.8; 328.15 K; cofactor CoA

enzyme: 2-hydroxyisobutanoyl-CoA mutase


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


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

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

row_label: Wild

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


enzyme_display_name: dTDP-fucopyranose mutase

substrate_name: dTDP-alpha-D-fucopyranose

enzyme: dTDP-fucopyranose mutase

substrate: dTDP-alpha-D-fucopyranose


enzyme_display_name: precorrin-8X methylmutase

enzyme: precorrin-8X methylmutase


organism: Sinorhizobium sp


enzyme_display_name: ethylmalonyl-CoA mutase

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

enzyme: ethylmalonyl-CoA mutase


organism: Aquincola tertiaricarbonis

assay_conditions_summary: cofactor CoA

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


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

assay_conditions_summary: pH 6.6; 303.15 K; cofactor CoA


substrate_name: isovaleryl-CoA

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

substrate: isovaleryl-CoA


enzyme_display_name: cucurbitadienol synthase

organism: Siraitia grosvenorii

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

enzyme: cucurbitadienol synthase


substrate_name: isobutanoyl-CoA

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

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

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

substrate: isobutanoyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


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

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

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

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

table_label: PMID 25720495 PMC HTML Table 3


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

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

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

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


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

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

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


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

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


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

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


substrate_name: butyryl-CoA

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

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

substrate: butyryl-CoA


substrate_name: isobutyryl-CoA

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

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

substrate: isobutyryl-CoA


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


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


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

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

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

row_label: CobH precorrin-8x kinetic sentence

table_label: PMC article prose


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

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

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

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


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

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

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


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

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

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


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

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


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

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

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


organism: Cereibacter sphaeroides

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

assay_conditions_summary: pH 7.8; cofactor CoA


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


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


organism: Escherichia coli


organism: Catfish


organism: Oryza sativa


substrate_name: Unknown

substrate: Unknown


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


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

row_label: HcmA D117V / Pivalyl-CoA

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


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

row_label: HcmA I90A / Pivalyl-CoA


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

row_label: HcmA I90V / Pivalyl-CoA


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

row_label: HcmA D117A / 2-Hydroxyisobutyryl-CoA


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

row_label: HcmA D117V / 2-Hydroxyisobutyryl-CoA


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

row_label: HcmA I90A / 2-Hydroxyisobutyryl-CoA


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

row_label: HcmA I90L / 2-Hydroxyisobutyryl-CoA


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

row_label: HcmA I90V / Isovaleryl-CoA


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

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


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

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


enzyme_display_name: leukotriene-C4 synthase

organism: Cavia porcellus

substrate_name: leukotriene A4 methyl ester

enzyme: leukotriene-C4 synthase

substrate: leukotriene A4 methyl ester


enzyme_display_name: protoporphyrin ferrochelatase

substrate_name: 2,4-disulfonic deuteroporphyrin

enzyme: protoporphyrin ferrochelatase

substrate: 2,4-disulfonic deuteroporphyrin


enzyme_display_name: cysteine-S-conjugate beta-lyase

enzyme: cysteine-S-conjugate beta-lyase


enzyme_display_name: methionine gamma-lyase

organism: Citrobacter freundii

substrate_name: DL-homocysteine

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

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

enzyme: methionine gamma-lyase

substrate: DL-homocysteine


enzyme_display_name: alanine racemase

organism: Clostridioides difficile

substrate_name: L-alanine

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

enzyme: alanine racemase

substrate: L-alanine


enzyme_display_name: isopentenyl-diphosphate Delta-isomerase

organism: Claviceps sp.

substrate_name: isopentenyl diphosphate

enzyme: isopentenyl-diphosphate Delta-isomerase

substrate: isopentenyl diphosphate


enzyme_display_name: methylaspartate mutase

organism: Clostridium cochlearium

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

enzyme: methylaspartate mutase


enzyme_display_name: adenylate cyclase

substrate_name: ATP

enzyme: adenylate cyclase

substrate: ATP


organism: Clostridium perfringens


enzyme_display_name: D-psicose 3-epimerase

organism: [Clostridium] scindens

substrate_name: D-fructose

enzyme: D-psicose 3-epimerase

substrate: D-fructose


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

assay_conditions_summary: pH 6.6; cofactor CoA

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

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


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

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

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


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

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


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

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


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

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


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

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


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

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


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

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


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

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


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

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


column_label: Table 2: Kinetic parameters Vmax, Km, and kcat and deduced catalytic efficiency kcat/Km of reconstituted HCM subunits HcmA and wild-type HcmB incubated with 2-hydroxyisobutyryl-CoA and both 3-hydroxybutyryl-CoA enantiomers at pH 6.6 and 30 C (J. Biol. Chem. 2015, 290(15):9727-9737); variant block 'HcmA D117V', substrate row '2-Hydroxyisobutyryl-CoA'; column 'Km' in uM = 61.4; column 'kcat' in min^-1 = 2.68; column 'kcat/Km' in mM^-1 min^-1 = 43.6; column 'Vmax' in nmol min^-1 mg^-1 is printed for the same row.

raw_value_unit_evidence: Table 2, variant block 'HcmA D117V', substrate row '2-Hydroxyisobutyryl-CoA': Km = 61.4 uM; kcat = 2.68 min^-1; printed kcat/Km = 43.6 mM^-1 min^-1.


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


column_label: Table 3: Kinetic parameters Vmax, Km, and kcat and deduced catalytic efficiency kcat/Km of reconstituted HCM subunits HcmA and wild-type HcmB incubated with pivalyl- and isovaleryl-CoA at pH 6.6 and 30 C (J. Biol. Chem. 2015, 290(15):9727-9737); variant block 'HcmA D117V', substrate row 'Pivalyl-CoA'; column 'Km' in uM = 43.5; column 'kcat' in min^-1 = 8.37; column 'kcat/Km' in mM^-1 min^-1 = 192; column 'Vmax' in nmol min^-1 mg^-1 is printed for the same row.

raw_value_unit_evidence: Table 3, variant block 'HcmA D117V', substrate row 'Pivalyl-CoA': Km = 43.5 uM; kcat = 8.37 min^-1; printed kcat/Km = 192 mM^-1 min^-1.


substrate_name: pivalyl-CoA

column_label: Table 3 | Wild-type HcmA | substrate Pivalyl-CoA | condition pH 6.6, 30 °C | Vmax 11.8 ± 0.73 nmol min^-1 mg^-1 | Km 374 ± 46 µM | kcat 0.98 ± 0.06 min^-1 | kcat/Km 2.6 ± 0.4 mM^-1 min^-1

row_label: Wild-type HcmA / Pivalyl-CoA

substrate: pivalyl-CoA


column_label: Table 3 | Wild-type HcmA | substrate Isovaleryl-CoA | condition pH 6.6, 30 °C | Vmax 8.20 ± 0.34 nmol min^-1 mg^-1 | Km 288 ± 18 µM | kcat 0.68 ± 0.03 min^-1 | kcat/Km 2.4 ± 0.2 mM^-1 min^-1

row_label: Wild-type HcmA / Isovaleryl-CoA


raw_value_unit_evidence: Table 3 | Wild-type HcmA | substrate Pivalyl-CoA | condition pH 6.6, 30 °C | Vmax 11.8 ± 0.73 nmol min^-1 mg^-1 | Km 374 ± 46 µM | kcat 0.98 ± 0.06 min^-1 | kcat/Km 2.6 ± 0.4 mM^-1 min^-1


raw_value_unit_evidence: Table 3 | Wild-type HcmA | substrate Isovaleryl-CoA | condition pH 6.6, 30 °C | Vmax 8.20 ± 0.34 nmol min^-1 mg^-1 | Km 288 ± 18 µM | kcat 0.68 ± 0.03 min^-1 | kcat/Km 2.4 ± 0.2 mM^-1 min^-1


organism: Clostridium sp.

proof_lines: pH 8.0, 65°C, in presence of 0.2 mM Co2+


proof_lines: pH and temperature not specified in the publication


enzyme_display_name: lysine 2,3-aminomutase

substrate_name: L-Lys

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

enzyme: lysine 2,3-aminomutase

substrate: L-Lys


organism: Clostridium subterminale

assay_conditions_summary: pH 8; 310.15 K; buffer 0.2 M Na-EPPS

proof_lines: at pH 8.0, 37°C, in 0.2 M Na-EPPS buffer


organism: Clostridium tetanomorphum

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


enzyme_display_name: steroid Delta-isomerase

organism: Comamonas testosteroni

proof_lines: 25°C, pH 6.5, solvent D2O, mutant enzyme D38A

proof_lines: 25°C, pH 8.5, solvent D2O, mutant enzyme D38A

proof_lines: 25°C, pH 6.5, solvent H2O, mutant enzyme D38A

enzyme: steroid Delta-isomerase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D38E to reconstruct the assayed variant sequence.

proof_lines:
mutant D38E, pH 7.0, 5.4°C
mutant D38E, pH 7.0, 10.3°C
mutant D38E, pH 7.0, 15.3°C


enzyme_display_name: UDP-galactopyranose mutase

organism: Corynebacterium diphtheriae

proof_lines: pH 7.0, temperature not specified in the publication

enzyme: UDP-galactopyranose mutase


enzyme_display_name: 2-hydroxyisobutanoyl-CoA mutase

organism: Aquincola tertiaricarbonis

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

enzyme: 2-hydroxyisobutanoyl-CoA mutase


enzyme_display_name: (-)-kolavenyl diphosphate synthase

organism: Salvia divinorum

substrate_name: geranylgeranyl diphosphate

enzyme: (-)-kolavenyl diphosphate synthase

substrate: geranylgeranyl diphosphate


enzyme_display_name: UniProt P23971

organism: Bacillus subtilis

enzyme: UniProt P23971


substrate_name: CoA

substrate: CoA


enzyme_display_name: UniProt B4EL89

organism: Burkholderia cenocepacia

enzyme: UniProt B4EL89


substrate_name: phenylacetate

substrate: phenylacetate


organism: Cucurbita pepo

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Cucurbita maxima


enzyme_display_name: Delta(3)-Delta(2)-enoyl-CoA isomerase

organism: Cucumis sativus

enzyme: Delta(3)-Delta(2)-enoyl-CoA isomerase


enzyme_display_name: peptidylprolyl isomerase

organism: Corynebacterium glutamicum

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: peptidylprolyl isomerase


enzyme_display_name: muconolactone Delta-isomerase

organism: Cupriavidus necator

enzyme: muconolactone Delta-isomerase


enzyme_display_name: benzoate--CoA ligase

organism: Anaerobic bacterium

substrate_name: benzoate

enzyme: benzoate--CoA ligase

substrate: benzoate


substrate_name: CoASH

substrate: CoASH


enzyme_display_name: dicarboxylate--CoA ligase

organism: Rattus norvegicus

enzyme: dicarboxylate--CoA ligase


substrate_name: dodecanedioic acid

smiles: C(CCCCCC(=O)O)CCCCC(=O)O

substrate: dodecanedioic acid


enzyme_display_name: phenylacetate--CoA ligase

organism: Penicillium chrysogenum

assay_conditions_summary: pH 8.5; 303.15 K; cofactor CoA

proof_lines: pH 8.5, 30°C, recombinant enzyme, with phenylacetic acid

proof_lines: pH 8.5, 30°C, recombinant enzyme, with trans-cinnamic acid

enzyme: phenylacetate--CoA ligase


assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP


substrate_name: Butyric acid

smiles: CCCC(=O)O

substrate: Butyric acid


substrate_name: trans-cinnamic acid

substrate: trans-cinnamic acid


substrate_name: myristic acid

smiles: CCCCCCCCCCCCCC(=O)O

substrate: myristic acid


substrate_name: propionic acid

smiles: CCC(=O)O

substrate: propionic acid


organism: Clarkia breweri


assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP


assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA


substrate_name: palmitate

smiles: CCCCCCCCCCCCCCCC(=O)O

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

substrate: palmitate


substrate_name: stearate

smiles: CCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: stearate


substrate_name: Phenoxyacetate

proof_lines:
recombinant enzyme, pH 7.5, 30°C
pH 8.5, 30°C, recombinant enzyme

substrate: Phenoxyacetate


substrate_name: caprylate

smiles: CCCCCCCC(=O)[O-]

substrate: caprylate


substrate_name: caproate

smiles: CCCCCC(=O)[O-]

substrate: caproate


proof_lines:
recombinant enzyme, pH 7.5, 30°C
pH 8.5, 30°C, recombinant enzyme
pH 6.8, 37°C


substrate_name: caprate

smiles: CCCCCCCCCC(=O)[O-]

substrate: caprate


organism: Petunia hybrida

assay_conditions_summary: pH 8.5; buffer 50 mM Tris/K phosphate/Na citrate; cofactor CoA

column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-4CL1', substrate (acid) row 't-Cinnamic'; column 'Km (uM)' prints 149.4; column 'Vmax (pkat mg^-1)' prints 14680; column 'kcat (s^-1)' prints 0.847; column 'kcat/Km (mM^-1 s^-1)' prints 6.43; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.847 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.847 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 149.4 uM; 149.4 / 1000 = 0.1494 mM; the exported value is 0.1494 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 6.43 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 6.43 s^-1 mM^-1. The exported ratio 5.669344042838018 s^(-1)*mM^(-1) is the quotient 0.847 / 0.1494 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 6.43 and kcat and Km are unchanged.


substrate_name: 4-coumaric acid

column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-4CL1', substrate (acid) row '4-Coumaric'; column 'Km (uM)' prints 16.4; column 'Vmax (pkat mg^-1)' prints 25797; column 'kcat (s^-1)' prints 1.488; column 'kcat/Km (mM^-1 s^-1)' prints 84.32; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.488 s^-1; already in s^-1, no unit conversion applies; the exported value is 1.488 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 16.4 uM; 16.4 / 1000 = 0.0164 mM; the exported value is 0.016399999999999998 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 84.32 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 84.32 s^-1 mM^-1. The exported ratio 90.73170731707319 s^(-1)*mM^(-1) is the quotient 1.488 / 0.016399999999999998 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 84.32 and kcat and Km are unchanged.

substrate: 4-coumaric acid


substrate_name: caffeic acid

column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-4CL1', substrate (acid) row 'Caffeic'; column 'Km (uM)' prints 47.8; column 'Vmax (pkat mg^-1)' prints 63200; column 'kcat (s^-1)' prints 3.645; column 'kcat/Km (mM^-1 s^-1)' prints 70.14; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.645 s^-1; already in s^-1, no unit conversion applies; the exported value is 3.645 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 47.8 uM; 47.8 / 1000 = 0.0478 mM; the exported value is 0.047799999999999995 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 70.14 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 70.14 s^-1 mM^-1. The exported ratio 76.25523012552301 s^(-1)*mM^(-1) is the quotient 3.645 / 0.047799999999999995 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 70.14 and kcat and Km are unchanged.

substrate: caffeic acid


substrate_name: ferulic acid

column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-4CL1', substrate (acid) row 'Ferulic'; column 'Km (uM)' prints 15.2; column 'Vmax (pkat mg^-1)' prints 41377; column 'kcat (s^-1)' prints 2.39; column 'kcat/Km (mM^-1 s^-1)' prints 145.37; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.39 s^-1; already in s^-1, no unit conversion applies; the exported value is 2.39 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 15.2 uM; 15.2 / 1000 = 0.0152 mM; the exported value is 0.0152 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 145.37 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 145.37 s^-1 mM^-1. The exported ratio 157.23684210526318 s^(-1)*mM^(-1) is the quotient 2.39 / 0.0152 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 145.37 and kcat and Km are unchanged.

substrate: ferulic acid


substrate_name: benzoic acid

proof_lines: kcat is 0.847 sec(-1) with trans-cinnamic acid as substrate (PubMed:22649270). kcat is 1.488 sec(-1) with 4-coumaric acid as substrate (PubMed:22649270). kcat is 3.645 sec(-1) with caffeic acid as substrate (PubMed:22649270). kcat is 2.39 s

substrate: benzoic acid


substrate_name: CoA

column_label: Table 1: Kinetic Parameters of Ph-4CL1 and Ph-CNL Proteins (The Plant Cell 2012, 24(5):2015-2030); Table 1, enzyme 'Ph-4CL1', substrate (acid) row 'CoA'; column 'Km (uM)' prints 9.9; column 'Vmax (pkat mg^-1)' prints 8451; column 'kcat (s^-1)' prints 0.487; column 'kcat/Km (mM^-1 s^-1)' prints 49.46; each cell is printed as mean +/- SE of n = 3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.487 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.487 s^(-1) and the printed cell reproduces it. Km: printed Table 1 cell 9.9 uM; 9.9 / 1000 = 0.0099 mM; the exported value is 0.0099 mM and the printed cell reproduces it. kcat/Km: printed Table 1 cell 49.46 mM^-1 s^-1; mM^-1 s^-1 is the same unit as s^-1 mM^-1, so no unit conversion applies and the cell is 49.46 s^-1 mM^-1. The exported ratio 49.19191919191918 s^(-1)*mM^(-1) is the quotient 0.487 / 0.0099 of the row's own kcat and Km rather than the printed efficiency cell, so the ratio is corrected to the printed value 49.46 and kcat and Km are unchanged.

substrate: CoA


substrate_name: geranylgeranyl diphosphate

assay_conditions_summary: pH 7

proof_lines: kcat is 0.88 sec(-1) with geranylgeranyl diphosphate as substrate.

substrate: geranylgeranyl diphosphate


organism: Geobacter metallireducens

substrate_name: benzoate

sequence_source: NCBI RefSeq protein WP_004513062.1

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

substrate: benzoate


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: phytanate--CoA ligase

organism: Homo sapiens

enzyme: phytanate--CoA ligase


organism: Thauera aromatica


enzyme_display_name: 4-hydroxybenzoate--CoA ligase

organism: Pseudomonas sp.

enzyme: 4-hydroxybenzoate--CoA ligase


organism: Bos taurus

substrate_name: ATP (with (R)-lipoate as substrate)

assay_conditions_summary: cofactor ATP

substrate: ATP (with (R)-lipoate as substrate)


organism: Rhodopseudomonas palustris

substrate_name: Coenzyme A; ATP; Benzoate

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

substrate: Coenzyme A; ATP; Benzoate


substrate_name: ATP; Coenzyme A; 4-Hydroxybenzoate

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

substrate: ATP; Coenzyme A; 4-Hydroxybenzoate


organism: Azoarcus evansii

substrate_name: ATP; Coenzyme A; Phenylacetic acid

substrate: ATP; Coenzyme A; Phenylacetic acid


assay_conditions_summary: pH 8; 304.15 K; cofactor CoA

column_label: Figure S11 caption gives row substrate BadA with 3-chlorobenzoate (3-Cl-BzO) with metric cells KM = 289 ± 23 µM and kcat = 0.33 ± 0.011 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 289 µM normalizes to 0.29 mM; kcat 0.33 s-1 normalizes to 0.33 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 0.33 / 0.29 = 1.1379310344827587 s^-1*mM^-1. Caption KM 289 uM = 0.289 mM is carried in the export rounded to 0.29 mM; caption kcat 0.33 s-1 is carried unrounded.

raw_value_unit_evidence: Figure S11 caption, row BadA with 3-chlorobenzoate (3-Cl-BzO): KM = 289 ± 23 µM and kcat = 0.33 ± 0.011 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 3-chlorobenzoate (3-Cl-BzO)

table_label: Supporting Information Figure S11


column_label: Figure S6 caption gives row substrate BadA with 3-cyclohexen-1-carboxylate (3-Cyc) with metric cells KM = 56.2 ± 9.1 µM and kcat = 16 ± 1.03 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 56.2 µM normalizes to 0.056 mM; kcat 16.0 s-1 normalizes to 16.0 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 16.0 / 0.056 = 285.7142857142857 s^-1*mM^-1. Caption KM 56.2 uM = 0.0562 mM is carried in the export rounded to 0.056 mM; caption kcat 16 s-1 is carried unrounded.

raw_value_unit_evidence: Figure S6 caption, row BadA with 3-cyclohexen-1-carboxylate (3-Cyc): KM = 56.2 ± 9.1 µM and kcat = 16 ± 1.03 s-1. The caption prints no kcat/KM cell.

table_label: Supporting Information Figure S6


column_label: Figure S8 caption gives row substrate BadA with 3-fluorobenzoate (3-F-BzO) with metric cells KM = 73 ± 11 µM and kcat = 35 ± 1.45 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 73 µM normalizes to 0.073 mM; kcat 35.0 s-1 normalizes to 35.0 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 35.0 / 0.073 = 479.45205479452056 s^-1*mM^-1. Caption KM 73 uM = 0.073 mM and caption kcat 35 s-1 are carried in the export unrounded.

raw_value_unit_evidence: Figure S8 caption, row BadA with 3-fluorobenzoate (3-F-BzO): KM = 73 ± 11 µM and kcat = 35 ± 1.45 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 3-fluorobenzoate (3-F-BzO)

table_label: Supporting Information Figure S8


column_label: Figure S3 caption gives row substrate BadA with 3-Furoate (3-Fur) with metric cells KM = 70.8 ± 12.3 µM and kcat = 6.74 ± 0.48 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 70.8 µM normalizes to 0.071 mM; kcat 6.7 s-1 normalizes to 6.7 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 6.7 / 0.071 = 94.3661971830986 s^-1*mM^-1. Caption KM 70.8 uM = 0.0708 mM and caption kcat 6.74 s-1 are carried in the export rounded to 0.071 mM and 6.7 s^-1.

raw_value_unit_evidence: Figure S3 caption, row BadA with 3-Furoate (3-Fur): KM = 70.8 ± 12.3 µM and kcat = 6.74 ± 0.48 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 3-Furoate (3-Fur)

table_label: Supporting Information Figure S3


column_label: Figure S20 caption gives row substrate BadA with 3-methylbenzoate (3-Me-BzO) with metric cells KM = 215 ± 25.6 µM and kcat = 0.54 ± 0.018 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 215 µM normalizes to 0.215 mM; kcat 0.54 s-1 normalizes to 0.54 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 0.54 / 0.215 = 2.511627906976744 s^-1*mM^-1. Caption KM 215 uM = 0.215 mM and caption kcat 0.54 s-1 are carried in the export unrounded.

raw_value_unit_evidence: Figure S20 caption, row BadA with 3-methylbenzoate (3-Me-BzO): KM = 215 ± 25.6 µM and kcat = 0.54 ± 0.018 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 3-methylbenzoate (3-Me-BzO)

table_label: Supporting Information Figure S20


column_label: Figure S15 caption gives row substrate BadA with 4-aminobenzoate (4-NH2-BzO) with metric cells KM = 25.3 ± 3.01 µM and kcat = 0.18 ± 0.0043 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 25.3 µM normalizes to 0.025 mM; kcat 0.18 s-1 normalizes to 0.18 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 0.18 / 0.025 = 7.199999999999999 s^-1*mM^-1. Caption KM 25.3 uM = 0.0253 mM is carried in the export rounded to 0.025 mM; caption kcat 0.18 s-1 is carried unrounded.

raw_value_unit_evidence: Figure S15 caption, row BadA with 4-aminobenzoate (4-NH2-BzO): KM = 25.3 ± 3.01 µM and kcat = 0.18 ± 0.0043 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 4-aminobenzoate (4-NH2-BzO)

table_label: Supporting Information Figure S15


column_label: Figure S12 caption gives row substrate BadA with 4-chlorobenzoate (4-Cl-BzO) with metric cells KM = 83.2 ± 11.1 µM and kcat = 0.29 ± 0.012 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 83.2 µM normalizes to 0.083 mM; kcat 0.29 s-1 normalizes to 0.29 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 0.29 / 0.083 = 3.4939759036144573 s^-1*mM^-1. Caption KM 83.2 uM = 0.0832 mM is carried in the export rounded to 0.083 mM; caption kcat 0.29 s-1 is carried unrounded.

raw_value_unit_evidence: Figure S12 caption, row BadA with 4-chlorobenzoate (4-Cl-BzO): KM = 83.2 ± 11.1 µM and kcat = 0.29 ± 0.012 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 4-chlorobenzoate (4-Cl-BzO)

table_label: Supporting Information Figure S12


column_label: Figure S9 caption gives row substrate BadA with 4-fluorobenzoate (4-F-BzO) with metric cells KM = 6.6 ± 0.9 µM and kcat = 22 ± 0.66 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 6.6 µM normalizes to 0.0066 mM; kcat 22.0 s-1 normalizes to 22.0 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 22.0 / 0.0066 = 3333.3333333333335 s^-1*mM^-1. Caption KM 6.6 uM = 0.0066 mM and caption kcat 22 s-1 are carried in the export unrounded.

raw_value_unit_evidence: Figure S9 caption, row BadA with 4-fluorobenzoate (4-F-BzO): KM = 6.6 ± 0.9 µM and kcat = 22 ± 0.66 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 4-fluorobenzoate (4-F-BzO)

table_label: Supporting Information Figure S9


column_label: Figure S21 caption gives row substrate BadA with 4-methylbenzoate (4-Me-BzO) with metric cells KM = 590 ± 73 µM and kcat = 0.7 ± 0.035 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 590 µM normalizes to 0.59 mM; kcat 0.7 s-1 normalizes to 0.7 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 0.7 / 0.59 = 1.1864406779661016 s^-1*mM^-1. Caption KM 590 uM = 0.59 mM and caption kcat 0.7 s-1 are carried in the export unrounded.

raw_value_unit_evidence: Figure S21 caption, row BadA with 4-methylbenzoate (4-Me-BzO): KM = 590 ± 73 µM and kcat = 0.7 ± 0.035 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 4-methylbenzoate (4-Me-BzO)

table_label: Supporting Information Figure S21


substrate_name: butyrate

smiles: CCCC(=O)[O-]

substrate: butyrate


substrate_name: decanoate

substrate: decanoate


substrate_name: hexanoate

substrate: hexanoate


substrate_name: laurate

smiles: CCCCCCCCCCCC(=O)[O-]

substrate: laurate


substrate_name: phenylacetate

substrate: phenylacetate


substrate_name: salicylate

substrate: salicylate


column_label: Figure S1 caption gives wild-type benzoate row KM=4.40 +/- 0.65 uM and kcat=27.5 +/- 0.87 s^-1; Figure S27 is Lys427Ala mutant and has kcat=0.05 s^-1, also not this no-mutation row

raw_value_unit_evidence: Figure S1 reports KM=4.40 +/- 0.65 uM and kcat=27.5 +/- 0.87 s^-1 for wild-type BadA

row_label: wild-type BadA with benzoate (BzO)

table_label: Supporting Information Figure S1


substrate_name: cyclohexane carboxylate

column_label: Figure S4 caption gives row substrate cyclohexane carboxylate and metric cells KM=1466 +/- 213 uM and kcat=13.5 +/- 1.07 s^-1

normalized_value_unit_evidence: KM=1.466 mM from 1466 uM; export rounded KM=1.47 mM; kcat=13.5 s^-1; export kcat/KM=9.183673469387756 s^-1*mM^-1 from rounded KM

row_label: BadA with cyclohexane carboxylate (Cyc)

table_label: Supporting Information Figure S4

substrate: cyclohexane carboxylate


column_label: Figure S2 caption gives row substrate thiophene-2-carboxylate and metric cells KM=37 +/- 5.7 uM and kcat=4.8 +/- 0.23 s^-1

raw_value_unit_evidence: Figure S2 reports KM=37 +/- 5.7 uM and kcat=4.8 +/- 0.23 s^-1

row_label: BadA with thiophene-2-carboxylate (Thio-2-C)

table_label: Supporting Information Figure S2


column_label: Figure S17 caption gives row substrate 3-hydroxybenzoate and metric cells KM=229 +/- 18 uM and kcat=1.8 +/- 0.04 s^-1

raw_value_unit_evidence: Figure S17 reports KM=229 +/- 18 uM and kcat=1.8 +/- 0.04 s^-1

row_label: BadA with 3-hydroxybenzoate (3-OH-BzO)

table_label: Supporting Information Figure S17


substrate_name: caprate

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

column_label: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Capric acid (C10)'; column 'Km mmol/L' = 0.070; column 'kcat s−1' = 0.102; column 'kcat/Km L mmol−1 s−1' = 1.455.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.070 mmol/L; 1 mmol/L is 1 mM, so the normalized value is 0.07 mM, which is the value the catalog carries. kcat: printed Table 3 cell 0.102 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 0.102 s^(-1), which is the value the catalog carries. kcat/Km: printed Table 3 cell 1.455 L mmol^-1 s^-1; L mmol^-1 s^-1 is the reciprocal of mmol/L per second, so it is already s^-1 mM^-1 and no unit conversion applies, giving 1.455 s^(-1)*mM^(-1). The catalog carries 1.4571428571428569 s^(-1)*mM^(-1), which is the plain quotient 0.102 / 0.070 = 1.4571428571428569 of the two component cells; the paper's own efficiency cell for this substrate is 1.455, an independently fitted primary value printed to three decimals, and it is proposed in place of the quotient.

raw_value_unit_evidence: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Capric acid (C10)': column 'Km mmol/L' prints 0.070; column 'kcat s−1' prints 0.102; column 'kcat/Km L mmol−1 s−1' prints 1.455.

row_label: Table 3, PhlC block, substrate row 'Capric acid (C10)'

table_label: Table 3: Apparent kinetic parameters of Phl, PhlB, and PhlC (Folia Microbiologica 2011, 56:246-252)

substrate: caprate


substrate_name: caproate

column_label: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Caproic acid (C6)'; column 'Km mmol/L' = 0.026; column 'kcat s−1' = 0.076; column 'kcat/Km L mmol−1 s−1' = 2.917.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.026 mmol/L; 1 mmol/L is 1 mM, so the normalized value is 0.026 mM, which is the value the catalog carries. kcat: printed Table 3 cell 0.076 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 0.076 s^(-1), which is the value the catalog carries. kcat/Km: printed Table 3 cell 2.917 L mmol^-1 s^-1; L mmol^-1 s^-1 is the reciprocal of mmol/L per second, so it is already s^-1 mM^-1 and no unit conversion applies, giving 2.917 s^(-1)*mM^(-1). The catalog carries 2.9230769230769234 s^(-1)*mM^(-1), which is the plain quotient 0.076 / 0.026 = 2.9230769230769234 of the two component cells; the paper's own efficiency cell for this substrate is 2.917, an independently fitted primary value printed to three decimals, and it is proposed in place of the quotient.

raw_value_unit_evidence: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Caproic acid (C6)': column 'Km mmol/L' prints 0.026; column 'kcat s−1' prints 0.076; column 'kcat/Km L mmol−1 s−1' prints 2.917.

row_label: Table 3, PhlC block, substrate row 'Caproic acid (C6)'

substrate: caproate


substrate_name: caprylate

column_label: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Caprylic acid (C8)'; column 'Km mmol/L' = 0.046; column 'kcat s−1' = 0.073; column 'kcat/Km L mmol−1 s−1' = 1.575.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.046 mmol/L; 1 mmol/L is 1 mM, so the normalized value is 0.046 mM, which is the value the catalog carries. kcat: printed Table 3 cell 0.073 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 0.073 s^(-1), which is the value the catalog carries. kcat/Km: printed Table 3 cell 1.575 L mmol^-1 s^-1; L mmol^-1 s^-1 is the reciprocal of mmol/L per second, so it is already s^-1 mM^-1 and no unit conversion applies, giving 1.575 s^(-1)*mM^(-1). The catalog carries 1.5869565217391304 s^(-1)*mM^(-1), which is the plain quotient 0.073 / 0.046 = 1.5869565217391304 of the two component cells; the paper's own efficiency cell for this substrate is 1.575, an independently fitted primary value printed to three decimals, and it is proposed in place of the quotient.

raw_value_unit_evidence: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Caprylic acid (C8)': column 'Km mmol/L' prints 0.046; column 'kcat s−1' prints 0.073; column 'kcat/Km L mmol−1 s−1' prints 1.575.

row_label: Table 3, PhlC block, substrate row 'Caprylic acid (C8)'

substrate: caprylate


substrate_name: palmitate

column_label: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Palmitic acid (C16)'; column 'Km mmol/L' = 0.092; column 'kcat s−1' = 0.026; column 'kcat/Km L mmol−1 s−1' = 0.283.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.092 mmol/L; 1 mmol/L is 1 mM, so the normalized value is 0.092 mM, which is the value the catalog carries. kcat: printed Table 3 cell 0.026 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 0.026 s^(-1), which is the value the catalog carries. kcat/Km: printed Table 3 cell 0.283 L mmol^-1 s^-1; L mmol^-1 s^-1 is the reciprocal of mmol/L per second, so it is already s^-1 mM^-1 and no unit conversion applies, giving 0.283 s^(-1)*mM^(-1) as the printed efficiency. The plain quotient of the two printed component cells is 0.026 / 0.092 = 0.2826086956521739 s^-1 mM^-1, which is the value the catalog carries, and the printed efficiency cell 0.283 is that same quotient written to the three decimals Table 3 prints.

raw_value_unit_evidence: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Palmitic acid (C16)': column 'Km mmol/L' prints 0.092; column 'kcat s−1' prints 0.026; column 'kcat/Km L mmol−1 s−1' prints 0.283.

row_label: Table 3, PhlC block, substrate row 'Palmitic acid (C16)'

substrate: palmitate


substrate_name: Phenoxyacetate

column_label: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Phenoxyacetic acid'; column 'Km mmol/L' = 0.257; column 'kcat s−1' = 0.063; column 'kcat/Km L mmol−1 s−1' = 0.247.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.257 mmol/L; 1 mmol/L is 1 mM, so the normalized value is 0.257 mM, which is the value the catalog carries. kcat: printed Table 3 cell 0.063 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 0.063 s^(-1), which is the value the catalog carries. kcat/Km: printed Table 3 cell 0.247 L mmol^-1 s^-1; L mmol^-1 s^-1 is the reciprocal of mmol/L per second, so it is already s^-1 mM^-1 and no unit conversion applies, giving 0.247 s^(-1)*mM^(-1). The catalog carries 0.245136186770428 s^(-1)*mM^(-1), which is the plain quotient 0.063 / 0.257 = 0.245136186770428 of the two component cells; the paper's own efficiency cell for this substrate is 0.247, an independently fitted primary value printed to three decimals, and it is proposed in place of the quotient.

raw_value_unit_evidence: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Phenoxyacetic acid': column 'Km mmol/L' prints 0.257; column 'kcat s−1' prints 0.063; column 'kcat/Km L mmol−1 s−1' prints 0.247.

row_label: Table 3, PhlC block, substrate row 'Phenoxyacetic acid'

substrate: Phenoxyacetate


column_label: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Phenylacetic acid'; column 'Km mmol/L' = 0.809; column 'kcat s−1' = 0.099; column 'kcat/Km L mmol−1 s−1' = 0.124.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.809 mmol/L; 1 mmol/L is 1 mM, so the normalized value is 0.809 mM, which is the value the catalog carries. kcat: printed Table 3 cell 0.099 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 0.099 s^(-1), which is the value the catalog carries. kcat/Km: printed Table 3 cell 0.124 L mmol^-1 s^-1; L mmol^-1 s^-1 is the reciprocal of mmol/L per second, so it is already s^-1 mM^-1 and no unit conversion applies, giving 0.124 s^(-1)*mM^(-1). The catalog carries 0.12237330037082818 s^(-1)*mM^(-1), which is the plain quotient 0.099 / 0.809 = 0.12237330037082818 of the two component cells; the paper's own efficiency cell for this substrate is 0.124, an independently fitted primary value printed to three decimals, and it is proposed in place of the quotient.

raw_value_unit_evidence: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Phenylacetic acid': column 'Km mmol/L' prints 0.809; column 'kcat s−1' prints 0.099; column 'kcat/Km L mmol−1 s−1' prints 0.124.

row_label: Table 3, PhlC block, substrate row 'Phenylacetic acid'


substrate_name: stearate

column_label: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Stearic acid (C18)'; column 'Km mmol/L' = 0.841; column 'kcat s−1' = 0.062; column 'kcat/Km L mmol−1 s−1' = 0.074.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.841 mmol/L; 1 mmol/L is 1 mM, so the normalized value is 0.841 mM, which is the value the catalog carries. kcat: printed Table 3 cell 0.062 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 0.062 s^(-1), which is the value the catalog carries. kcat/Km: printed Table 3 cell 0.074 L mmol^-1 s^-1; L mmol^-1 s^-1 is the reciprocal of mmol/L per second, so it is already s^-1 mM^-1 and no unit conversion applies, giving 0.074 s^(-1)*mM^(-1) as the printed efficiency. The plain quotient of the two printed component cells is 0.062 / 0.841 = 0.0737217598097503 s^-1 mM^-1, which is the value the catalog carries, and the printed efficiency cell 0.074 is that same quotient written to the three decimals Table 3 prints.

raw_value_unit_evidence: Table 3 (Apparent kinetic parameters of Phl, PhlB, and PhlC), PhlC block, substrate row 'Stearic acid (C18)': column 'Km mmol/L' prints 0.841; column 'kcat s−1' prints 0.062; column 'kcat/Km L mmol−1 s−1' prints 0.074.

row_label: Table 3, PhlC block, substrate row 'Stearic acid (C18)'

substrate: stearate


column_label: Figure S5 caption gives row substrate BadA with 1-cyclohexen-1-carboxylate (1-Cyc) with metric cells KM = 52 ± 7.1 µM and kcat = 5.6 ± 0.24 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 52 uM normalizes to 0.052 mM, carried in the export at its stored precision as 0.05 mM; kcat 5.6 s-1 normalizes to 5.6 s^-1, carried unrounded; kcat/KM is not printed by the paper, so it is the export-normalized quotient 5.6 / 0.05 = 111.99999999999999 s^-1*mM^-1.

raw_value_unit_evidence: Figure S5 caption, row BadA with 1-cyclohexen-1-carboxylate (1-Cyc): KM = 52 ± 7.1 µM and kcat = 5.6 ± 0.24 s-1. The caption prints no kcat/KM cell.

table_label: Supporting Information Figure S5


column_label: Figure S13 caption gives row substrate BadA with 2-aminobenzoate (2-NH2-BzO) with metric cells KM = 21 ± 2.3 µM and kcat = 3.9 ± 0.1 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 21 uM normalizes to 0.021 mM, carried in the export unrounded as 0.021 mM; kcat 3.9 s-1 normalizes to 3.9 s^-1, carried unrounded; kcat/KM is not printed by the paper, so it is the export-normalized quotient 3.9 / 0.021 = 185.7142857142857 s^-1*mM^-1.

raw_value_unit_evidence: Figure S13 caption, row BadA with 2-aminobenzoate (2-NH2-BzO): KM = 21 ± 2.3 µM and kcat = 3.9 ± 0.1 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 2-aminobenzoate (2-NH2-BzO)

table_label: Supporting Information Figure S13


column_label: Figure S10 caption gives row substrate BadA with 2-chlorobenzoate (2-Cl-BzO) with metric cells KM = 126 ± 12.3 µM and kcat = 2.21 ± 0.068 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 126 uM normalizes to 0.126 mM, carried in the export at its stored precision as 0.13 mM; kcat 2.21 s-1 normalizes to 2.21 s^-1, carried in the export at its stored precision as 2.2 s^-1; kcat/KM is not printed by the paper, so it is the export-normalized quotient 2.2 / 0.13 = 16.923076923076923 s^-1*mM^-1.

raw_value_unit_evidence: Figure S10 caption, row BadA with 2-chlorobenzoate (2-Cl-BzO): KM = 126 ± 12.3 µM and kcat = 2.21 ± 0.068 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 2-chlorobenzoate (2-Cl-BzO)

table_label: Supporting Information Figure S10


column_label: Figure S22 caption gives row substrate BadA with 2-cyanobenzoate (2-CN-BzO) with metric cells KM = 213 ± 22 µM and kcat = 0.11 ± 0.0034 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 213 uM normalizes to 0.213 mM, carried in the export unrounded as 0.213 mM; kcat 0.11 s-1 normalizes to 0.11 s^-1, carried unrounded; kcat/KM is not printed by the paper, so it is the export-normalized quotient 0.11 / 0.213 = 0.5164319248826291 s^-1*mM^-1.

raw_value_unit_evidence: Figure S22 caption, row BadA with 2-cyanobenzoate (2-CN-BzO): KM = 213 ± 22 µM and kcat = 0.11 ± 0.0034 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 2-cyanobenzoate (2-CN-BzO)

table_label: Supporting Information Figure S22


column_label: Figure S7 caption gives row substrate BadA with 2-fluorobenzoate (2-F-BzO) with metric cells KM = 8.1 ± 0.91 µM and kcat = 34 ± 0.7 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 8.1 uM normalizes to 0.0081 mM, carried in the export unrounded as 0.0081 mM; kcat 34 s-1 normalizes to 34.0 s^-1, carried unrounded; kcat/KM is not printed by the paper, so it is the export-normalized quotient 34.0 / 0.0081 = 4197.530864197531 s^-1*mM^-1.

raw_value_unit_evidence: Figure S7 caption, row BadA with 2-fluorobenzoate (2-F-BzO): KM = 8.1 ± 0.91 µM and kcat = 34 ± 0.7 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 2-fluorobenzoate (2-F-BzO)

table_label: Supporting Information Figure S7


column_label: Figure S23 caption gives row substrate BadA with 2-methoxybenzoate (2-MeO-BzO) with metric cells KM = 789 ± 82 µM and kcat = 0.011 ± 0.00052 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 789 uM normalizes to 0.789 mM, carried in the export unrounded as 0.789 mM; kcat 0.011 s-1 normalizes to 0.011 s^-1, carried unrounded; kcat/KM is not printed by the paper, so it is the export-normalized quotient 0.011 / 0.789 = 0.013941698352344739 s^-1*mM^-1.

raw_value_unit_evidence: Figure S23 caption, row BadA with 2-methoxybenzoate (2-MeO-BzO): KM = 789 ± 82 µM and kcat = 0.011 ± 0.00052 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 2-methoxybenzoate (2-MeO-BzO)

table_label: Supporting Information Figure S23


column_label: Figure S19 caption gives row substrate BadA with 2-methylbenzoate (2-Me-BzO) with metric cells KM = 44 ± 6 µM and kcat = 1.2 ± 0.042 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 44 uM normalizes to 0.044 mM, carried in the export unrounded as 0.044 mM; kcat 1.2 s-1 normalizes to 1.2 s^-1, carried unrounded; kcat/KM is not printed by the paper, so it is the export-normalized quotient 1.2 / 0.044 = 27.272727272727273 s^-1*mM^-1.

raw_value_unit_evidence: Figure S19 caption, row BadA with 2-methylbenzoate (2-Me-BzO): KM = 44 ± 6 µM and kcat = 1.2 ± 0.042 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 2-methylbenzoate (2-Me-BzO)

table_label: Supporting Information Figure S19


column_label: Figure S24 caption gives row substrate BadA with 2-nitrobenzoate (2-NO2-BzO) with metric cells KM = 2015 ± 167 µM and kcat = 0.27 ± 0.011 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 2015 uM normalizes to 2.015 mM, carried in the export unrounded as 2.015 mM; kcat 0.27 s-1 normalizes to 0.27 s^-1, carried unrounded; kcat/KM is not printed by the paper, so it is the export-normalized quotient 0.27 / 2.015 = 0.13399503722084366 s^-1*mM^-1.

raw_value_unit_evidence: Figure S24 caption, row BadA with 2-nitrobenzoate (2-NO2-BzO): KM = 2015 ± 167 µM and kcat = 0.27 ± 0.011 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 2-nitrobenzoate (2-NO2-BzO)

table_label: Supporting Information Figure S24


column_label: Figure S14 caption gives row substrate BadA with 3-aminobenzoate (3-NH2-BzO) with metric cells KM = 174 ± 32 µM and kcat = 1.8 ± 0.1 s-1; both cells sit in that one caption, so the tuple does not span two rows, columns or cofactor blocks.

normalized_value_unit_evidence: KM 174 uM normalizes to 0.174 mM, carried in the export unrounded as 0.174 mM; kcat 1.8 s-1 normalizes to 1.8 s^-1, carried unrounded; kcat/KM is not printed by the paper, so it is the export-normalized quotient 1.8 / 0.174 = 10.344827586206897 s^-1*mM^-1.

raw_value_unit_evidence: Figure S14 caption, row BadA with 3-aminobenzoate (3-NH2-BzO): KM = 174 ± 32 µM and kcat = 1.8 ± 0.1 s-1. The caption prints no kcat/KM cell.

row_label: BadA with 3-aminobenzoate (3-NH2-BzO)

table_label: Supporting Information Figure S14


substrate_name: stearate (when expressed in bacteria)

substrate: stearate (when expressed in bacteria)


substrate_name: oleate (when expressed in bacteria)

smiles: CCCCCCCCC=CCCCCCCCC(=O)[O-]

substrate: oleate (when expressed in bacteria)


substrate_name: linoleate (when expressed in bacteria)

smiles: CCCCCC=CCC=CCCCCCCCC(=O)[O-]

substrate: linoleate (when expressed in bacteria)


substrate_name: arachidonate (when expressed in bacteria)

smiles: CCCCCC=CCC=CCC=CCC=CCCCC(=O)[O-]


organism: Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)

substrate_name: benzoate

substrate: benzoate


substrate_name: ATP

substrate: ATP


substrate_name: CoA

assay_conditions_summary: cofactor CoA

substrate: CoA


organism: Arabidopsis thaliana

substrate_name: trans-cinnamate

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

column_label: Table 2 (Kinetic Properties of Recombinant At4g19010), printed substrate row 't-Cinnamate': column 'K_m (uM)' = 112; column 'k_cat (s^-1)' = 0.7; column 'k_cat/K_m (s^-1 mM^-1)' = 6.

normalized_value_unit_evidence: K_m: printed Table 2 cell 112 uM; 1 uM is 0.001 mM, so 112 / 1000 = 0.112 mM, and the exported value is 0.112 mM. k_cat: printed Table 2 cell 0.7 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 0.7 s^(-1). k_cat/K_m: printed Table 2 cell 6 s^-1 mM^-1; the column head is already the export's own unit, so no unit conversion applies and the printed cell reads 6.0 s^-1 mM^-1. Quotient disclosure for this row: 0.7 / 0.112 = 6.249999999999999 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 2 uses.

raw_value_unit_evidence: Table 2, printed substrate row 't-Cinnamate': K_m = 112 uM; k_cat = 0.7 s^-1; printed k_cat/K_m = 6 s^-1 mM^-1.

table_label: Table 2: Kinetic Properties of Recombinant At4g19010 (The Plant Cell 2014, volume 26, number 5, pages 1938-1948); printed column heads K_m (uM), k_cat (s^-1) and k_cat/K_m (s^-1 mM^-1)

substrate: trans-cinnamate


substrate_name: p-coumarate

column_label: Table 2 (Kinetic Properties of Recombinant At4g19010), printed substrate row 'p-Coumarate': column 'K_m (uM)' = 125; column 'k_cat (s^-1)' = 2.1; column 'k_cat/K_m (s^-1 mM^-1)' = 17.

normalized_value_unit_evidence: K_m: printed Table 2 cell 125 uM; 1 uM is 0.001 mM, so 125 / 1000 = 0.125 mM, and the exported value is 0.125 mM. k_cat: printed Table 2 cell 2.1 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 2.1 s^(-1). k_cat/K_m: printed Table 2 cell 17 s^-1 mM^-1; the column head is already the export's own unit, so no unit conversion applies and the printed cell reads 17.0 s^-1 mM^-1. Quotient disclosure for this row: 2.1 / 0.125 = 16.8 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 2 uses.

raw_value_unit_evidence: Table 2, printed substrate row 'p-Coumarate': K_m = 125 uM; k_cat = 2.1 s^-1; printed k_cat/K_m = 17 s^-1 mM^-1.

substrate: p-coumarate


substrate_name: ferulate

column_label: Table 2 (Kinetic Properties of Recombinant At4g19010), printed substrate row 'Ferulate': column 'K_m (uM)' = 113; column 'k_cat (s^-1)' = 3.6; column 'k_cat/K_m (s^-1 mM^-1)' = 32.

normalized_value_unit_evidence: K_m: printed Table 2 cell 113 uM; 1 uM is 0.001 mM, so 113 / 1000 = 0.113 mM, and the exported value is 0.113 mM. k_cat: printed Table 2 cell 3.6 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 3.6 s^(-1). k_cat/K_m: printed Table 2 cell 32 s^-1 mM^-1; the column head is already the export's own unit, so no unit conversion applies and the printed cell reads 32.0 s^-1 mM^-1. Quotient disclosure for this row: 3.6 / 0.113 = 31.858407079646017 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 2 uses.

raw_value_unit_evidence: Table 2, printed substrate row 'Ferulate': K_m = 113 uM; k_cat = 3.6 s^-1; printed k_cat/K_m = 32 s^-1 mM^-1.

substrate: ferulate


substrate_name: caffeate

column_label: Table 2 (Kinetic Properties of Recombinant At4g19010), printed substrate row 'Caffeate': column 'K_m (uM)' = 85; column 'k_cat (s^-1)' = 2.4; column 'k_cat/K_m (s^-1 mM^-1)' = 28.

normalized_value_unit_evidence: K_m: printed Table 2 cell 85 uM; 1 uM is 0.001 mM, so 85 / 1000 = 0.085 mM, and the exported value is 0.085 mM. k_cat: printed Table 2 cell 2.4 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 2.4 s^(-1). k_cat/K_m: printed Table 2 cell 28 s^-1 mM^-1; the column head is already the export's own unit, so no unit conversion applies and the printed cell reads 28.0 s^-1 mM^-1. Quotient disclosure for this row: 2.4 / 0.085 = 28.235294117647054 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 2 uses.

raw_value_unit_evidence: Table 2, printed substrate row 'Caffeate': K_m = 85 uM; k_cat = 2.4 s^-1; printed k_cat/K_m = 28 s^-1 mM^-1.

substrate: caffeate