sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_candidate and applied mutation signature I107N with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


enzyme_display_name: methylamine dehydrogenase (amicyanin)

organism: Paracoccus denitrificans

substrate_name: Butylamine

source_db: brenda

verification_status: unverified

ki_display: Not reported

source_license: CC BY 4.0

km_unit: mM

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

smiles: CCCCN

mutation_type: substitution

data_origin: experimental

enzyme: methylamine dehydrogenase (amicyanin)

substrate: Butylamine

status: unverified

source: brenda


substrate_name: methylamine

smiles: CN

substrate: methylamine


enzyme_display_name: galactokinase

organism: Rattus norvegicus

substrate_name: alpha-D-galactose / D-talose

protein_accession_database: UniProt

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R37A to reconstruct the assayed variant sequence.

enzyme: galactokinase

substrate: alpha-D-galactose / D-talose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y109F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y109H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y236F to reconstruct the assayed variant sequence.


mutation_signature: Unknown

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


kcat_display: Not reported

kcat_over_km_display: Not reported

assay_conditions_summary: cofactor ATP


km_display: Not reported

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


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


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


enzyme_display_name: hydroxymethylglutaryl-CoA synthase

organism: Brassica juncea

substrate_name: acetoacetyl-CoA

ki_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R157A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor CoA

enzyme: hydroxymethylglutaryl-CoA synthase

substrate: acetoacetyl-CoA


substrate_name: acetyl-CoA

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9M6U3 and applied mutation signature R157A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

column_label: Table 3: Kinetic properties of wild-type and mutant His6-BjHMGS1 (Biochem. J. 2004, 383:517-527), enzyme row 'R157A'; column 'V max (umol . min^-1 . mg^-1)' = 0.032; column 'K m-acetyl-CoA (uM)' = 52; column 'K i-AcAc-CoA (uM)' = 242 uM; column 'K cat (min^-1) (V max /[E])' = 1.7; column 'acetyl-CoA hydrolysis (t 1/2)' = 24.1 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 52 uM; 52 / 1000 = 0.052 mM. kcat: printed Table 3 cell 1.7 min^-1 under the column head 'K cat (min^-1)'; 1.7 / 60 = 0.028333333333333332 s^-1. kcat/Km: this paper prints no catalytic-efficiency cell in any table, so the ratio here is the full-precision quotient of the two printed cells of this same Table 3 row, 0.028333333333333332 / 0.052 = 0.5448717948717948 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'R157A': V max = 0.032 umol min^-1 mg^-1; K m-acetyl-CoA = 52 uM; K i-AcAc-CoA = 242 uM; K cat = 1.7 min^-1; acetyl-CoA hydrolysis t1/2 = 24.1 min.

row_label: Table 3, enzyme row 'R157A'

substrate: acetyl-CoA

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9M6U3 and applied mutation signature H188N to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic properties of wild-type and mutant His6-BjHMGS1 (Biochem. J. 2004, 383:517-527), enzyme row 'H188N'; column 'V max (umol . min^-1 . mg^-1)' = 0.056; column 'K m-acetyl-CoA (uM)' = 55; column 'K i-AcAc-CoA (uM)' = n.i. (no inhibition); column 'K cat (min^-1) (V max /[E])' = 2.9; column 'acetyl-CoA hydrolysis (t 1/2)' = 61.7 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 55 uM; 55 / 1000 = 0.055 mM. kcat: printed Table 3 cell 2.9 min^-1 under the column head 'K cat (min^-1)'; 2.9 / 60 = 0.04833333333333333 s^-1. kcat/Km: this paper prints no catalytic-efficiency cell in any table, so the ratio here is the full-precision quotient of the two printed cells of this same Table 3 row, 0.04833333333333333 / 0.055 = 0.8787878787878788 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'H188N': V max = 0.056 umol min^-1 mg^-1; K m-acetyl-CoA = 55 uM; K i-AcAc-CoA = n.i. (no inhibition); K cat = 2.9 min^-1; acetyl-CoA hydrolysis t1/2 = 61.7 min.

row_label: Table 3, enzyme row 'H188N'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9M6U3 and applied mutation signature C212S to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic properties of wild-type and mutant His6-BjHMGS1 (Biochem. J. 2004, 383:517-527), enzyme row 'C212S'; column 'V max (umol . min^-1 . mg^-1)' = 0.078; column 'K m-acetyl-CoA (uM)' = 29; column 'K i-AcAc-CoA (uM)' = 39 uM; column 'K cat (min^-1) (V max /[E])' = 4.1; column 'acetyl-CoA hydrolysis (t 1/2)' = 14.7 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 29 uM; 29 / 1000 = 0.029 mM. kcat: printed Table 3 cell 4.1 min^-1 under the column head 'K cat (min^-1)'; 4.1 / 60 = 0.06833333333333333 s^-1. kcat/Km: this paper prints no catalytic-efficiency cell in any table, so the ratio here is the full-precision quotient of the two printed cells of this same Table 3 row, 0.06833333333333333 / 0.029 = 2.3563218390804597 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'C212S': V max = 0.078 umol min^-1 mg^-1; K m-acetyl-CoA = 29 uM; K i-AcAc-CoA = 39 uM; K cat = 4.1 min^-1; acetyl-CoA hydrolysis t1/2 = 14.7 min.

row_label: Table 3, enzyme row 'C212S'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9M6U3 and applied mutation signature S89A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic properties of wild-type and mutant His6-BjHMGS1 (Biochem. J. 2004, 383:517-527), enzyme row 'S89A'; column 'V max (umol . min^-1 . mg^-1)' = 0.14; column 'K m-acetyl-CoA (uM)' = 18; column 'K i-AcAc-CoA (uM)' = 46 uM; column 'K cat (min^-1) (V max /[E])' = 7.6; column 'acetyl-CoA hydrolysis (t 1/2)' = 18.8 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 18 uM; 18 / 1000 = 0.018 mM. kcat: printed Table 3 cell 7.6 min^-1 under the column head 'K cat (min^-1)'; 7.6 / 60 = 0.12666666666666665 s^-1. kcat/Km: this paper prints no catalytic-efficiency cell in any table, so the ratio here is the full-precision quotient of the two printed cells of this same Table 3 row, 0.12666666666666665 / 0.018 = 7.037037037037036 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'S89A': V max = 0.14 umol min^-1 mg^-1; K m-acetyl-CoA = 18 uM; K i-AcAc-CoA = 46 uM; K cat = 7.6 min^-1; acetyl-CoA hydrolysis t1/2 = 18.8 min.

row_label: Table 3, enzyme row 'S89A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9M6U3 and applied mutation signature S356A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic properties of wild-type and mutant His6-BjHMGS1 (Biochem. J. 2004, 383:517-527), enzyme row 'S356A'; column 'V max (umol . min^-1 . mg^-1)' = 0.30; column 'K m-acetyl-CoA (uM)' = 26; column 'K i-AcAc-CoA (uM)' = 199 uM; column 'K cat (min^-1) (V max /[E])' = 16.1; column 'acetyl-CoA hydrolysis (t 1/2)' = 25 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 26 uM; 26 / 1000 = 0.026 mM. kcat: printed Table 3 cell 16.1 min^-1 under the column head 'K cat (min^-1)'; 16.1 / 60 = 0.26833333333333337 s^-1. kcat/Km: this paper prints no catalytic-efficiency cell in any table, so the ratio here is the full-precision quotient of the two printed cells of this same Table 3 row, 0.26833333333333337 / 0.026 = 10.320512820512823 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'S356A': V max = 0.30 umol min^-1 mg^-1; K m-acetyl-CoA = 26 uM; K i-AcAc-CoA = 199 uM; K cat = 16.1 min^-1; acetyl-CoA hydrolysis t1/2 = 25 min.

row_label: Table 3, enzyme row 'S356A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9M6U3 and applied mutation signature N115A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic properties of wild-type and mutant His6-BjHMGS1 (Biochem. J. 2004, 383:517-527), enzyme row 'N115A'; column 'V max (umol . min^-1 . mg^-1)' = 0.44; column 'K m-acetyl-CoA (uM)' = 27; column 'K i-AcAc-CoA (uM)' = 91 uM; column 'K cat (min^-1) (V max /[E])' = 23.4; column 'acetyl-CoA hydrolysis (t 1/2)' = 8.8 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 27 uM; 27 / 1000 = 0.027 mM. kcat: printed Table 3 cell 23.4 min^-1 under the column head 'K cat (min^-1)'; 23.4 / 60 = 0.38999999999999996 s^-1. kcat/Km: this paper prints no catalytic-efficiency cell in any table, so the ratio here is the full-precision quotient of the two printed cells of this same Table 3 row, 0.38999999999999996 / 0.027 = 14.444444444444443 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'N115A': V max = 0.44 umol min^-1 mg^-1; K m-acetyl-CoA = 27 uM; K i-AcAc-CoA = 91 uM; K cat = 23.4 min^-1; acetyl-CoA hydrolysis t1/2 = 8.8 min.

row_label: Table 3, enzyme row 'N115A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9M6U3 and applied mutation signature S359A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic properties of wild-type and mutant His6-BjHMGS1 (Biochem. J. 2004, 383:517-527), enzyme row 'S359A'; column 'V max (umol . min^-1 . mg^-1)' = 4.04; column 'K m-acetyl-CoA (uM)' = 24; column 'K i-AcAc-CoA (uM)' = 28 uM; column 'K cat (min^-1) (V max /[E])' = 214.1; column 'acetyl-CoA hydrolysis (t 1/2)' = 4.7 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 24 uM; 24 / 1000 = 0.024 mM. kcat: printed Table 3 cell 214.1 min^-1 under the column head 'K cat (min^-1)'; 214.1 / 60 = 3.5683333333333334 s^-1. kcat/Km: this paper prints no catalytic-efficiency cell in any table, so the ratio here is the full-precision quotient of the two printed cells of this same Table 3 row, 3.5683333333333334 / 0.024 = 148.68055555555554 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'S359A': V max = 4.04 umol min^-1 mg^-1; K m-acetyl-CoA = 24 uM; K i-AcAc-CoA = 28 uM; K cat = 214.1 min^-1; acetyl-CoA hydrolysis t1/2 = 4.7 min.

row_label: Table 3, enzyme row 'S359A'


verification_status: verified

column_label: Table 3: Kinetic properties of wild-type and mutant His6-BjHMGS1 (Biochem. J. 2004, 383:517-527), enzyme row 'Wild-Type'; column 'V max (umol . min^-1 . mg^-1)' = 0.47; column 'K m-acetyl-CoA (uM)' = 43; column 'K i-AcAc-CoA (uM)' = 38 uM; column 'K cat (min^-1) (V max /[E])' = 24.9; column 'acetyl-CoA hydrolysis (t 1/2)' = 11.1 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 43 uM; 43 / 1000 = 0.043 mM. kcat: printed Table 3 cell 24.9 min^-1 under the column head 'K cat (min^-1)'; 24.9 / 60 = 0.415 s^-1. kcat/Km: this paper prints no catalytic-efficiency cell in any table, so the ratio here is the full-precision quotient of the two printed cells of this same Table 3 row, 0.415 / 0.043 = 9.651162790697676 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'Wild-Type': V max = 0.47 umol min^-1 mg^-1; K m-acetyl-CoA = 43 uM; K i-AcAc-CoA = 38 uM; K cat = 24.9 min^-1; acetyl-CoA hydrolysis t1/2 = 11.1 min.

row_label: Table 3, enzyme row 'Wild-Type'

status: verified


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H188N/S359A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H188N to reconstruct the assayed variant sequence.


substrate_name: Unknown

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S359A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C212S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S89A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N115A to reconstruct the assayed variant sequence.


enzyme_display_name: leucine dehydrogenase

organism: Geobacillus stearothermophilus

substrate_name: L-Leu

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

enzyme: leucine dehydrogenase

substrate: L-Leu


substrate_name: alpha-keto-isocaproate

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

substrate: alpha-keto-isocaproate


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


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


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A113A/V291L to reconstruct the assayed variant sequence.


substrate_name: alpha-keto-beta-methylvalerate

substrate: alpha-keto-beta-methylvalerate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A113A to reconstruct the assayed variant sequence.


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


substrate_name: L-norvaline

substrate: L-norvaline


substrate_name: L-norleucine

substrate: L-norleucine


substrate_name: L-Phe

substrate: L-Phe


substrate_name: L-Ile

substrate: L-Ile


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P29894 and applied mutation signature F55I with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the alpha-F55I MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row Methylamine, alpha-F55I MADH enzyme column; column Km (uM) cell = 60; column kcat (s-1) cell = 2.0. captured primary segment: Methylamine | alpha-F55I MADH | Table I | pH 7.5 | 30 C | Km 60 uM | kcat 2.0 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 60 uM; 1 uM is 1/1000 mM, so 60 / 1000 = 0.06 mM. kcat: printed Table I kcat cell 2.0 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 2.0 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 2.0 / 0.06 = 33.333333333333336 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row Methylamine, alpha-F55I MADH enzyme column: Km = 60 uM; kcat = 2.0 s^-1. Table I carries no catalytic-efficiency column.


substrate_name: Propylamine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P22619 and applied mutation signature I107V with inferred residue-numbering offset +57 to reconstruct the assayed variant sequence.

smiles: CCCN

column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the beta-I107V MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row Propylamine, beta-I107V MADH enzyme column; column Km (uM) cell = 6; column kcat (s-1) cell = 3.1. captured primary segment: Propylamine | beta-I107V MADH | Table I | pH 7.5 | 30 C | Km 6 uM | kcat 3.1 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 6 uM; 1 uM is 1/1000 mM, so 6 / 1000 = 0.006 mM. kcat: printed Table I kcat cell 3.1 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 3.1 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 3.1 / 0.006 = 516.6666666666666 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row Propylamine, beta-I107V MADH enzyme column: Km = 6 uM; kcat = 3.1 s^-1. Table I carries no catalytic-efficiency column.

substrate: Propylamine


smiles: CCCCCN

column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the beta-I107V MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row 1-Aminopentane, beta-I107V MADH enzyme column; column Km (uM) cell = 130; column kcat (s-1) cell = 3.4. captured primary segment: 1-Aminopentane | beta-I107V MADH | Table I | pH 7.5 | 30 C | Km 130 uM | kcat 3.4 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 130 uM; 1 uM is 1/1000 mM, so 130 / 1000 = 0.13 mM. kcat: printed Table I kcat cell 3.4 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 3.4 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 3.4 / 0.13 = 26.153846153846153 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row 1-Aminopentane, beta-I107V MADH enzyme column: Km = 130 uM; kcat = 3.4 s^-1. Table I carries no catalytic-efficiency column.


column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the alpha-F55I MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row 1,6-Diaminohexane, alpha-F55I MADH enzyme column; column Km (uM) cell = 99; column kcat (s-1) cell = 3.4. captured primary segment: 1,6-Diaminohexane | alpha-F55I MADH | Table I | pH 7.5 | 30 C | Km 99 uM | kcat 3.4 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 99 uM; 1 uM is 1/1000 mM, so 99 / 1000 = 0.099 mM. kcat: printed Table I kcat cell 3.4 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 3.4 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 3.4 / 0.099 = 34.34343434343434 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row 1,6-Diaminohexane, alpha-F55I MADH enzyme column: Km = 99 uM; kcat = 3.4 s^-1. Table I carries no catalytic-efficiency column.


smiles: C(CCCN)CCCN

column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the alpha-F55I MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row 1,7-Diaminoheptane, alpha-F55I MADH enzyme column; column Km (uM) cell = 57; column kcat (s-1) cell = 3.4. captured primary segment: 1,7-Diaminoheptane | alpha-F55I MADH | Table I | pH 7.5 | 30 C | Km 57 uM | kcat 3.4 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 57 uM; 1 uM is 1/1000 mM, so 57 / 1000 = 0.057 mM. kcat: printed Table I kcat cell 3.4 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 3.4 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 3.4 / 0.057 = 59.64912280701754 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row 1,7-Diaminoheptane, alpha-F55I MADH enzyme column: Km = 57 uM; kcat = 3.4 s^-1. Table I carries no catalytic-efficiency column.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P22619 and applied mutation signature I107N with inferred residue-numbering offset +57 to reconstruct the assayed variant sequence.

column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the beta-I107N MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row Propylamine, beta-I107N MADH enzyme column; column Km (uM) cell = 8; column kcat (s-1) cell = 4.1. captured primary segment: Propylamine | beta-I107N MADH | Table I | pH 7.5 | 30 C | Km 8 uM | kcat 4.1 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 8 uM; 1 uM is 1/1000 mM, so 8 / 1000 = 0.008 mM. kcat: printed Table I kcat cell 4.1 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 4.1 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 4.1 / 0.008 = 512.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row Propylamine, beta-I107N MADH enzyme column: Km = 8 uM; kcat = 4.1 s^-1. Table I carries no catalytic-efficiency column.


column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the beta-I107N MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row Butylamine, beta-I107N MADH enzyme column; column Km (uM) cell = 7; column kcat (s-1) cell = 4.2. captured primary segment: Butylamine | beta-I107N MADH | Table I | pH 7.5 | 30 C | Km 7 uM | kcat 4.2 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 7 uM; 1 uM is 1/1000 mM, so 7 / 1000 = 0.007 mM. kcat: printed Table I kcat cell 4.2 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 4.2 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 4.2 / 0.007 = 600.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row Butylamine, beta-I107N MADH enzyme column: Km = 7 uM; kcat = 4.2 s^-1. Table I carries no catalytic-efficiency column.


column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the beta-I107N MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row 1-Aminopentane, beta-I107N MADH enzyme column; column Km (uM) cell = 4; column kcat (s-1) cell = 4.2. captured primary segment: 1-Aminopentane | beta-I107N MADH | Table I | pH 7.5 | 30 C | Km 4 uM | kcat 4.2 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 4 uM; 1 uM is 1/1000 mM, so 4 / 1000 = 0.004 mM. kcat: printed Table I kcat cell 4.2 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 4.2 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 4.2 / 0.004 = 1050.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row 1-Aminopentane, beta-I107N MADH enzyme column: Km = 4 uM; kcat = 4.2 s^-1. Table I carries no catalytic-efficiency column.


substrate_name: ethylamine

smiles: CCN

column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the beta-I107N MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row Ethylamine, beta-I107N MADH enzyme column; column Km (uM) cell = 840; column kcat (s-1) cell = 4.5. captured primary segment: Ethylamine | beta-I107N MADH | Table I | pH 7.5 | 30 C | Km 840 uM | kcat 4.5 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 840 uM; 1 uM is 1/1000 mM, so 840 / 1000 = 0.84 mM. kcat: printed Table I kcat cell 4.5 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 4.5 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 4.5 / 0.84 = 5.357142857142858 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row Ethylamine, beta-I107N MADH enzyme column: Km = 840 uM; kcat = 4.5 s^-1. Table I carries no catalytic-efficiency column.

substrate: ethylamine


column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the alpha-F55I MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row Propylamine, alpha-F55I MADH enzyme column; column Km (uM) cell = 200; column kcat (s-1) cell = 5.2. captured primary segment: Propylamine | alpha-F55I MADH | Table I | pH 7.5 | 30 C | Km 200 uM | kcat 5.2 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 200 uM; 1 uM is 1/1000 mM, so 200 / 1000 = 0.2 mM. kcat: printed Table I kcat cell 5.2 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 5.2 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 5.2 / 0.2 = 26.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row Propylamine, alpha-F55I MADH enzyme column: Km = 200 uM; kcat = 5.2 s^-1. Table I carries no catalytic-efficiency column.


substrate_name: Butylamine

column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the alpha-F55I MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row Butylamine, alpha-F55I MADH enzyme column; column Km (uM) cell = 370; column kcat (s-1) cell = 5.4. captured primary segment: Butylamine | alpha-F55I MADH | Table I | pH 7.5 | 30 C | Km 370 uM | kcat 5.4 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 370 uM; 1 uM is 1/1000 mM, so 370 / 1000 = 0.37 mM. kcat: printed Table I kcat cell 5.4 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 5.4 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 5.4 / 0.37 = 14.594594594594597 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row Butylamine, alpha-F55I MADH enzyme column: Km = 370 uM; kcat = 5.4 s^-1. Table I carries no catalytic-efficiency column.

substrate: Butylamine


column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the alpha-F55I MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row 1-Aminopentane, alpha-F55I MADH enzyme column; column Km (uM) cell = 250; column kcat (s-1) cell = 5.4. captured primary segment: 1-Aminopentane | alpha-F55I MADH | Table I | pH 7.5 | 30 C | Km 250 uM | kcat 5.4 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 250 uM; 1 uM is 1/1000 mM, so 250 / 1000 = 0.25 mM. kcat: printed Table I kcat cell 5.4 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 5.4 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 5.4 / 0.25 = 21.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row 1-Aminopentane, alpha-F55I MADH enzyme column: Km = 250 uM; kcat = 5.4 s^-1. Table I carries no catalytic-efficiency column.


column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the beta-I107V MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row Ethylamine, beta-I107V MADH enzyme column; column Km (uM) cell = 340; column kcat (s-1) cell = 6.2. captured primary segment: Ethylamine | beta-I107V MADH | Table I | pH 7.5 | 30 C | Km 340 uM | kcat 6.2 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 340 uM; 1 uM is 1/1000 mM, so 340 / 1000 = 0.34 mM. kcat: printed Table I kcat cell 6.2 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 6.2 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 6.2 / 0.34 = 18.235294117647058 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row Ethylamine, beta-I107V MADH enzyme column: Km = 340 uM; kcat = 6.2 s^-1. Table I carries no catalytic-efficiency column.


column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the beta-I107V MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row Butylamine, beta-I107V MADH enzyme column; column Km (uM) cell = 88; column kcat (s-1) cell = 14. captured primary segment: Butylamine | beta-I107V MADH | Table I | pH 7.5 | 30 C | Km 88 uM | kcat 14 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 88 uM; 1 uM is 1/1000 mM, so 88 / 1000 = 0.088 mM. kcat: printed Table I kcat cell 14 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 14.0 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 14.0 / 0.088 = 159.0909090909091 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row Butylamine, beta-I107V MADH enzyme column: Km = 88 uM; kcat = 14 s^-1. Table I carries no catalytic-efficiency column.


column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the beta-I107N MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row 1,7-Diaminoheptane, beta-I107N MADH enzyme column; column Km (uM) cell = 68; column kcat (s-1) cell = 15. captured primary segment: 1,7-Diaminoheptane | beta-I107N MADH | Table I | pH 7.5 | 30 C | Km 68 uM | kcat 15 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 68 uM; 1 uM is 1/1000 mM, so 68 / 1000 = 0.068 mM. kcat: printed Table I kcat cell 15 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 15.0 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 15.0 / 0.068 = 220.58823529411762 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row 1,7-Diaminoheptane, beta-I107N MADH enzyme column: Km = 68 uM; kcat = 15 s^-1. Table I carries no catalytic-efficiency column.


column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the alpha-F55I MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row Ethylamine, alpha-F55I MADH enzyme column; column Km (uM) cell = 360; column kcat (s-1) cell = 15. captured primary segment: Ethylamine | alpha-F55I MADH | Table I | pH 7.5 | 30 C | Km 360 uM | kcat 15 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 360 uM; 1 uM is 1/1000 mM, so 360 / 1000 = 0.36 mM. kcat: printed Table I kcat cell 15 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 15.0 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 15.0 / 0.36 = 41.66666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row Ethylamine, alpha-F55I MADH enzyme column: Km = 360 uM; kcat = 15 s^-1. Table I carries no catalytic-efficiency column.


column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the beta-I107N MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row 1,6-Diaminohexane, beta-I107N MADH enzyme column; column Km (uM) cell = 31; column kcat (s-1) cell = 16. captured primary segment: 1,6-Diaminohexane | beta-I107N MADH | Table I | pH 7.5 | 30 C | Km 31 uM | kcat 16 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 31 uM; 1 uM is 1/1000 mM, so 31 / 1000 = 0.031 mM. kcat: printed Table I kcat cell 16 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 16.0 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 16.0 / 0.031 = 516.1290322580645 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row 1,6-Diaminohexane, beta-I107N MADH enzyme column: Km = 31 uM; kcat = 16 s^-1. Table I carries no catalytic-efficiency column.


column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the native MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row 1-Aminopentane, native MADH enzyme column; column Km (uM) cell = 2500; column kcat (s-1) cell = 17. captured primary segment: 1-Aminopentane | native MADH | Table I | pH 7.5 | 30 C | Km 2500 uM | kcat 17 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 2500 uM; 1 uM is 1/1000 mM, so 2500 / 1000 = 2.5 mM. kcat: printed Table I kcat cell 17 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 17.0 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 17.0 / 2.5 = 6.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row 1-Aminopentane, native MADH enzyme column: Km = 2500 uM; kcat = 17 s^-1. Table I carries no catalytic-efficiency column.


column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the native MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row 1,6-Diaminohexane, native MADH enzyme column; column Km (uM) cell = 720; column kcat (s-1) cell = 17. captured primary segment: 1,6-Diaminohexane | native MADH | Table I | pH 7.5 | 30 C | Km 720 uM | kcat 17 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 720 uM; 1 uM is 1/1000 mM, so 720 / 1000 = 0.72 mM. kcat: printed Table I kcat cell 17 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 17.0 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 17.0 / 0.72 = 23.61111111111111 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row 1,6-Diaminohexane, native MADH enzyme column: Km = 720 uM; kcat = 17 s^-1. Table I carries no catalytic-efficiency column.


column_label: Table I: Substrate specificities of native and mutant MADHs (journal page 4120), printed metric column heads Km (uM) and kcat (s-1) under each enzyme column head; the article prints no catalytic-efficiency column in this table; the record cites the beta-I107V MADH enzyme column. Journal page 4120 (PDF page 2). Table I, substrate row 1,7-Diaminoheptane, beta-I107V MADH enzyme column; column Km (uM) cell = 290; column kcat (s-1) cell = 19. captured primary segment: 1,7-Diaminoheptane | beta-I107V MADH | Table I | pH 7.5 | 30 C | Km 290 uM | kcat 19 s^-1

normalized_value_unit_evidence: Km: printed Table I Km cell 290 uM; 1 uM is 1/1000 mM, so 290 / 1000 = 0.29 mM. kcat: printed Table I kcat cell 19 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 19.0 s^(-1). kcat/Km: the exported efficiency is the quotient of the two printed cells of this same row, 19.0 / 0.29 = 65.51724137931035 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 4120, Table I, substrate row 1,7-Diaminoheptane, beta-I107V MADH enzyme column: Km = 290 uM; kcat = 19 s^-1. Table I carries no catalytic-efficiency column.


enzyme_display_name: aryldialkylphosphatase

organism: Homo sapiens

proof_lines: wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C

proof_lines: pH 8.0, 25°C, recombinant wild-type enzyme

enzyme: aryldialkylphosphatase


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -8, so it is treated as a source-provided variant sequence.

proof_lines: mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C


sequence_variant_note: Mutation signature H254G/H257W/L303T could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C


sequence_variant_note: Mutation signature H275Y/L303T could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +3, so it is treated as a source-provided variant sequence.

proof_lines: mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C


substrate_name: soman

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

assay_conditions_summary: pH 9

substrate: soman


proof_lines: wild type enzyme, in 20 mM Tris-HCl with 1 mM CaCl2 (pH 7.4), at 25°C


substrate_name: sarin

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

substrate: sarin


enzyme_display_name: alpha-tubulin N-acetyltransferase

substrate_name: alpha-tubulin L-lysine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L164A to reconstruct the assayed variant sequence.

enzyme: alpha-tubulin N-acetyltransferase

substrate: alpha-tubulin L-lysine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F186A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P159A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L173A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P178A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R69A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K103A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q131A to reconstruct the assayed variant sequence.


mutation_signature: truncation variant 1-193

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

mutation_type: truncation


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K169A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S160A to reconstruct the assayed variant sequence.


mutation_signature: truncation variant 1-236


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N182A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R158A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N73A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V184A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F190A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K162A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S66A to reconstruct the assayed variant sequence.


enzyme_display_name: L-amino-acid oxidase

organism: Rhodococcus opacus

substrate_name: L-lysine

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

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

enzyme: L-amino-acid oxidase

substrate: L-lysine


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


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


substrate_name: L-citrulline

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

substrate: L-citrulline


substrate_name: L-leucine

substrate: L-leucine


substrate_name: L-asparagine

substrate: L-asparagine


substrate_name: L-ornithine

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

substrate: L-ornithine


substrate_name: L-methionine

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

substrate: L-methionine


substrate_name: L-arginine

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

substrate: L-arginine


substrate_name: L-glutamine

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

substrate: L-glutamine


substrate_name: L-Glutamic acid

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

substrate: L-Glutamic acid


substrate_name: L-serine

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

substrate: L-serine


substrate_name: L-valine

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

substrate: L-valine


substrate_name: L-isoleucine

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

substrate: L-isoleucine


substrate_name: L-Orn

substrate: L-Orn


enzyme_display_name: hydrogen dehydrogenase

substrate_name: methyl viologen

sequence: MKHSEKNEIASHELPTTPLDPVLAAGRES

proof_lines:
at pH 9.4
at pH 8.0

enzyme: hydrogen dehydrogenase

substrate: methyl viologen


substrate_name: FAD

assay_conditions_summary: cofactor FAD

substrate: FAD


substrate_name: methylene blue

substrate: methylene blue


substrate_name: ferricyanide

substrate: ferricyanide


enzyme_display_name: D-amino-acid oxidase

organism: Rhodotorula toruloides

substrate_name: cephalosporin C

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q339E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

enzyme: D-amino-acid oxidase

substrate: cephalosporin C


substrate_name: D-Aspartate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y238R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y238R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

substrate: D-Aspartate


substrate_name: D-alanine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M213E to reconstruct the assayed variant sequence.

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

proof_lines: mutant enzyme M213E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

substrate: D-alanine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S335R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S335R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


substrate_name: D-arginine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y223F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y223F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

substrate: D-arginine


sequence_variant_note: Mutation signature Y228F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme Y228F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S335G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S335G, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M213R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M213R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

proof_lines: mutant enzyme M213R, apparent value, at 25°C and pH 8.5


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y238S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y238S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


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

proof_lines: wild type enzyme, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S335H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S335H, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


enzyme_display_name: alcohol dehydrogenase (azurin)

organism: Comamonas testosteroni

smiles: CCCCCC(C)O

proof_lines: soluble enzyme, pH 7.7, presence of CaCl2

proof_lines: enzyme electrode, pH 7.7, presence of CaCl2

enzyme: alcohol dehydrogenase (azurin)


smiles: CCCCCCC(C)O


smiles: CCCCC(C)O


smiles: CC(C)CCC(C)O


smiles: CCCCCCC(CCC)O


smiles: CCCC(C)O


smiles: CCCC(CCC)O


smiles: CC(C)CC(C)O


smiles: CCCCCCC(CC)O


substrate_name: Cyclohexanol

substrate: Cyclohexanol


smiles: CCCCCC(CC)O


smiles: CCC(C)C(C)O


smiles: CCCCC(CC)O


substrate_name: (S)-glycidol

substrate: (S)-glycidol


smiles: CCC(C)O


smiles: CCCC(CC)O


smiles: CC(C)O


smiles: CCC(CC)O


enzyme_display_name: acetoacetate decarboxylase

organism: Streptomyces bingchenggensis

proof_lines: pH 6.5, 25°C, aldolase-dehydratase reaction, with pyruvate

enzyme: acetoacetate decarboxylase


substrate_name: trans-cinnamaldehyde

sequence_variant_note: Mutation signature Q118N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 6.5, 25°C, mutant Q118N, aldolase-dehydratase reaction, with pyruvate

substrate: trans-cinnamaldehyde


proof_lines: pH 6.5, 25°C, mutant Q118N, hydratase-retroaldolase reaction


sequence_variant_note: Mutation signature Y82F/Y252F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 6.5, 25°C, mutant Y82F/Y252F, hydratase-retroaldolase reaction


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +6, so it is treated as a source-provided variant sequence.

proof_lines: pH 6.5, 25°C, mutant E84Q, hydratase-retroaldolase reaction


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_candidate and applied mutation signature Y252F with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

proof_lines: pH 6.5, 25°C, mutant Y252F, hydratase-retroaldolase reaction


proof_lines: pH 6.5, 25°C, wild-type enzyme, hydratase-retroaldolase reaction

proof_lines: pH 6.5, 4°C, wild-type enzyme, aldolase-dehydratase reaction, with pyruvate

proof_lines: pH 6.5, 25°C, wild-type enzyme, dehydration


proof_lines: pH 6.5, 25°C, mutant Y82F/Y252F, aldolase-dehydratase reaction, with pyruvate


proof_lines: pH 6.5, 25°C, mutant Y252F, aldolase-dehydratase reaction, with pyruvate


sequence_variant_note: Mutation signature Y82F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 6.5, 4°C, mutant Y82F, aldolase-dehydratase reaction, with pyruvate

proof_lines: pH 6.5, 25°C, mutant Y82F, hydratase-retroaldolase reaction


proof_lines: pH 6.5, 25°C, mutant E84Q, aldolase-dehydratase reaction, with pyruvate


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


substrate_name: pyruvate

substrate: pyruvate


proof_lines: pH 6.5, 25°C, wild-type enzyme, aldolase-dehydratase reaction, with pyruvate


enzyme_display_name: thiopurine S-methyltransferase

enzyme: thiopurine S-methyltransferase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R226H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R226E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R152H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R226A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R152A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R152E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R152A/R226A to reconstruct the assayed variant sequence.


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y238S to reconstruct the assayed variant sequence.

smiles: O=O


substrate_name: D-Ala

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y238F to reconstruct the assayed variant sequence.

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

substrate: D-Ala


substrate_name: D-Phe

substrate: D-Phe


substrate_name: D-Trp

substrate: D-Trp


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


assay_conditions_summary: pH 8.5; 298.15 K; buffer 75 mM sodium diphosphate

proof_lines: wild type enzyme, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C


substrate_name: D-Ser

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

substrate: D-Ser


substrate_name: D-Val

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

substrate: D-Val


substrate_name: D-Pro

substrate: D-Pro


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K119T with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

proof_lines: mutant K119T, cytosolic fraction of yeast cells is incubated with 0-350 microM of 6-TG and 1mM of SAM


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G144R with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A80P with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K122T with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R163H with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G36S with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C132Y with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


enzyme_display_name: NADPH--hemoprotein reductase

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines:
wild type, cosubstrate FAD, Km below
wild type, cosubstrate cytochrome c

enzyme: NADPH--hemoprotein reductase

substrate: NADPH


proof_lines:
T491V mutant, cosubstrate FAD
T491V mutant, cosubstrate cytochrome c


substrate_name: cytochrome c

proof_lines:
T491V mutant, cosubstrate FAD
T491V mutant, cosubstrate NADPH

substrate: cytochrome c


proof_lines:
G488L mutant, cosubstrate FAD
G488L mutant, cosubstrate cytochrome c


proof_lines:
G488L mutant, cosubstrate FAD
G488L mutant, cosubstrate NADPH


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

proof_lines:
W677X mutant, cosubstrate NADPH
S678X mutant, cosubstrate NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R454E with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

proof_lines:
R454E mutant, cosubstrate NADPH
R454E mutant, cosubstrate FAD


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y456S with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines:
Y456S mutant, cosubstrate NADPH
Y456S mutant, cosubstrate FAD


proof_lines:
Y456S mutant, cosubstrate FAD
Y456S mutant, cosubstrate cytochrome c


proof_lines:
W677X mutant, cosubstrate cytochrome c
S678X mutant, cosubstrate cytochrome c


proof_lines:
R454E mutant, cosubstrate cytochrome c
R454E mutant, cosubstrate FAD


enzyme_display_name: tryptophan dehydrogenase

organism: Nostoc punctiforme

substrate_name: L-tryptophan

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L288M to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L288M, at pH 11.0 and 25°C

enzyme: tryptophan dehydrogenase

substrate: L-tryptophan


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M65A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature A69M to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 11; 298.15 K; cofactor NAD+

column_label: Table 2 | A69M NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.82 +/- 0.071 mM | kcat 1.2 +/- 0.058 s^-1 | kcat/Km 1.5 mM^-1 s^-1

normalized_value_unit_evidence: kcat=1.2 s^(-1); km=0.82 mM; kcat_over_km=1.5 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row A69M, non-parenthetical L-tryptophan cells

table_label: Table 2: kinetic constants of NpTrpDH mutants


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature A69L to reconstruct the assayed variant sequence.

column_label: Table 2 | A69L NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 1.1 +/- 0.047 mM | kcat 1.2 +/- 0.090 s^-1 | kcat/Km 1.1 mM^-1 s^-1

normalized_value_unit_evidence: kcat=1.2 s^(-1); km=1.1 mM; kcat_over_km=1.1 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row A69L, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature V133A to reconstruct the assayed variant sequence.

column_label: Table 2 | V133A NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.019 +/- 0.0019 mM | kcat 2.6 +/- 0.18 s^-1 | kcat/Km 140 mM^-1 s^-1

normalized_value_unit_evidence: kcat=2.6 s^(-1); km=0.019 mM; kcat_over_km=140 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row V133A, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature V291A to reconstruct the assayed variant sequence.

column_label: Table 2 | V291A NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.047 +/- 0.0030 mM | kcat 2.9 +/- 0.12 s^-1 | kcat/Km 62 mM^-1 s^-1

normalized_value_unit_evidence: kcat=2.9 s^(-1); km=0.047 mM; kcat_over_km=62 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row V291A, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature Y292H to reconstruct the assayed variant sequence.

column_label: Table 2 | Y292H NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.021 +/- 0.0030 mM | kcat 3.5 +/- 0.41 s^-1 | kcat/Km 170 mM^-1 s^-1

normalized_value_unit_evidence: kcat=3.5 s^(-1); km=0.021 mM; kcat_over_km=170 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row Y292H, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature V132A to reconstruct the assayed variant sequence.

column_label: Table 2 | V132A NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.017 +/- 0.0010 mM | kcat 4.6 +/- 0.20 s^-1 | kcat/Km 270 mM^-1 s^-1

normalized_value_unit_evidence: kcat=4.6 s^(-1); km=0.017 mM; kcat_over_km=270 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row V132A, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature M295A to reconstruct the assayed variant sequence.

column_label: Table 2 | M295A NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.047 +/- 0.0025 mM | kcat 8.0 +/- 0.58 s^-1 | kcat/Km 170 mM^-1 s^-1

normalized_value_unit_evidence: kcat=8 s^(-1); km=0.047 mM; kcat_over_km=170 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row M295A, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature Y292W to reconstruct the assayed variant sequence.

column_label: Table 2 | Y292W NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.030 +/- 0.0050 mM | kcat 8.5 +/- 0.58 s^-1 | kcat/Km 280 mM^-1 s^-1

normalized_value_unit_evidence: kcat=8.5 s^(-1); km=0.03 mM; kcat_over_km=280 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row Y292W, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature I296A to reconstruct the assayed variant sequence.

column_label: Table 2 | I296A NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.059 +/- 0.0070 mM | kcat 10 +/- 1.0 s^-1 | kcat/Km 170 mM^-1 s^-1

normalized_value_unit_evidence: kcat=10 s^(-1); km=0.059 mM; kcat_over_km=170 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row I296A, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature M40L to reconstruct the assayed variant sequence.

column_label: Table 2 | M40L NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.047 +/- 0.0036 mM | kcat 12 +/- 0.63 s^-1 | kcat/Km 260 mM^-1 s^-1

normalized_value_unit_evidence: kcat=12 s^(-1); km=0.047 mM; kcat_over_km=260 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row M40L, non-parenthetical L-tryptophan cells


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

column_label: Table 2 | None (wild type) NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.045 +/- 0.0015 mM | kcat 20 +/- 1.3 s^-1 | kcat/Km 440 mM^-1 s^-1

normalized_value_unit_evidence: kcat=20 s^(-1); km=0.045 mM; kcat_over_km=440 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row None (wild type), non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature Y292F to reconstruct the assayed variant sequence.

column_label: Table 2 | Y292F NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.039 +/- 0.0030 mM | kcat 21 +/- 1.5 s^-1 | kcat/Km 540 mM^-1 s^-1

normalized_value_unit_evidence: kcat=21 s^(-1); km=0.039 mM; kcat_over_km=540 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row Y292F, non-parenthetical L-tryptophan cells


organism: Roseovarius nubinhibens

substrate_name: FAD

assay_conditions_summary: pH 9; cofactor FAD

column_label: Table 5. Km values of wild type DmdC and its mutants to different substrates; row Wild type DmdC / To FAD; column Km to FAD (uM); raw cell 6.3 +/- 0.5 uM; normalized Km 0.0063 mM

raw_value_unit_evidence: Wild type DmdC / To FAD: Km to FAD (uM)=6.3 +/- 0.5 uM

row_label: Wild type DmdC / To FAD

substrate: FAD


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


assay_conditions_summary: pH 9; cofactor CoA

column_label: Table 5. Km values of wild type DmdC and its mutants to different substrates; row Wild type DmdC / To MMPA-CoA; column Km to MMPA-CoA (mM); raw cell 1.4 +/- 0.2 mM; normalized Km 1.4 mM

normalized_value_unit_evidence: Km=1.4 mM

raw_value_unit_evidence: Wild type DmdC / To MMPA-CoA: Km to MMPA-CoA (mM)=1.4 +/- 0.2 mM

row_label: Wild type DmdC / To MMPA-CoA


proof_lines: Km above 100 mM, mutant enzyme R448A, at pH 9.0 and 40°C


enzyme_display_name: valine dehydrogenase (NAD(+))

organism: Streptomyces fradiae

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

assay_conditions_summary: pH 10.4; cofactor NADH

column_label: PubMed XML abstract for PMID 3269392 reports 2-oxoisovalerate Km = 0.80 mM, which does not equal the current row value 0.31 mM.

raw_value_unit_evidence: Km raw_value=0.80 raw_unit=mM for 2-oxoisovalerate.

row_label: Streptomyces fradiae valine dehydrogenase / 2-oxoisovalerate

table_label: PubMed XML abstract PMID 3269392

enzyme: valine dehydrogenase (NAD(+))


substrate_name: L-valine

assay_conditions_summary: pH 10.4; cofactor NAD+

column_label: PubMed XML abstract for PMID 3269392 reports L-valine Km = 1 mM, which does not equal the current row value 0.43 mM.

raw_value_unit_evidence: Km raw_value=1 raw_unit=mM for L-valine.

row_label: Streptomyces fradiae valine dehydrogenase / L-valine

substrate: L-valine


substrate_name: L-leucine

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

column_label: Table 2 lists row L-Leucine under column Km (mM) with central value 0.67 mM and parenthetical SD 0.02 mM.

normalized_value_unit_evidence: Km 0.67 mM; exported Km 0.67 mM.

raw_value_unit_evidence: Table 2 row L-Leucine; column Km (mM); value 0.67 mM with parenthetical SD 0.02 mM.

row_label: L-Leucine

table_label: Table 2

substrate: L-leucine


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

column_label: Table 3 lists row 2-Oxoisocaproate (source synonym for 2-Oxoisohexanoate) under column Km (mM) with central value 0.82 mM and parenthetical SD 0.02 mM.

normalized_value_unit_evidence: Km 0.82 mM; exported Km 0.82 mM.

raw_value_unit_evidence: Table 3 row 2-Oxoisocaproate (source synonym for 2-Oxoisohexanoate); column Km (mM); value 0.82 mM with parenthetical SD 0.02 mM.

table_label: Table 3


smiles: CCC(=O)C(=O)O

column_label: Table 3 lists row 2-Oxobutyrate (source synonym for 2-oxobutanoate) under column Km (mM) with central value 1.00 mM and parenthetical SD 0.03 mM.

normalized_value_unit_evidence: Km 1.00 mM; exported Km 1 mM.

raw_value_unit_evidence: Table 3 row 2-Oxobutyrate (source synonym for 2-oxobutanoate); column Km (mM); value 1.00 mM with parenthetical SD 0.03 mM.


substrate_name: L-isoleucine

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

column_label: Table 2 lists row L-Isoleucine under column Km (mM) with central value 1.18 mM and parenthetical SD 0.03 mM.

normalized_value_unit_evidence: Km 1.18 mM; exported Km 1.18 mM.

raw_value_unit_evidence: Table 2 row L-Isoleucine; column Km (mM); value 1.18 mM with parenthetical SD 0.03 mM.

row_label: L-Isoleucine

substrate: L-isoleucine


substrate_name: L-norvaline

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

column_label: Table 2 lists row L-Norvaline under column Km (mM) with central value 1.33 mM and parenthetical SD 0.03 mM.

normalized_value_unit_evidence: Km 1.33 mM; exported Km 1.33 mM.

raw_value_unit_evidence: Table 2 row L-Norvaline; column Km (mM); value 1.33 mM with parenthetical SD 0.03 mM.

row_label: L-Norvaline

substrate: L-norvaline


smiles: CCCC(=O)C(=O)O

column_label: Table 3 lists row 2-Oxovalerate under column Km (mM) with central value 1.94 mM and parenthetical SD 0.05 mM.

normalized_value_unit_evidence: Km 1.94 mM; exported Km 1.94 mM.

raw_value_unit_evidence: Table 3 row 2-Oxovalerate; column Km (mM); value 1.94 mM with parenthetical SD 0.05 mM.


smiles: CCCCC(=O)C(=O)[O-]

column_label: Table 3 lists row 2-Oxocaproate (source synonym for 2-Oxohexanoate) under column Km (mM) with central value 2.23 mM and parenthetical SD 0.06 mM.

normalized_value_unit_evidence: Km 2.23 mM; exported Km 2.23 mM.

raw_value_unit_evidence: Table 3 row 2-Oxocaproate (source synonym for 2-Oxohexanoate); column Km (mM); value 2.23 mM with parenthetical SD 0.06 mM.


column_label: Table 2 lists row L-alpha-Aminobutyrate (source synonym for L-2-aminobutanoate) under column Km (mM) with central value 3.07 mM and parenthetical SD 0.07 mM.

normalized_value_unit_evidence: Km 3.07 mM; exported Km 3.07 mM.

raw_value_unit_evidence: Table 2 row L-alpha-Aminobutyrate (source synonym for L-2-aminobutanoate); column Km (mM); value 3.07 mM with parenthetical SD 0.07 mM.


column_label: Table 3 lists row 2-Oxo-alpha-methyl-n-valerate (source synonym for 3-methyl-2-oxopentanoate) under column Km (mM) with central value 3.33 mM and parenthetical SD 0.07 mM.

normalized_value_unit_evidence: Km 3.33 mM; exported Km 3.33 mM.

raw_value_unit_evidence: Table 3 row 2-Oxo-alpha-methyl-n-valerate (source synonym for 3-methyl-2-oxopentanoate); column Km (mM); value 3.33 mM with parenthetical SD 0.07 mM.


substrate_name: L-norleucine

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

column_label: Table 2 lists row L-Norleucine under column Km (mM) with central value 6.68 mM and parenthetical SD 0.16 mM.

normalized_value_unit_evidence: Km 6.68 mM; exported Km 6.68 mM.

raw_value_unit_evidence: Table 2 row L-Norleucine; column Km (mM); value 6.68 mM with parenthetical SD 0.16 mM.

row_label: L-Norleucine

substrate: L-norleucine


substrate_name: pyruvate

column_label: Table 3 lists row Pyruvate line in split '2-Oxocaproate / pyruvate' row group under column Km (mM) with central value 25.00 mM and parenthetical SD 0.60 mM.

normalized_value_unit_evidence: Km 25.00 mM; exported Km 25 mM.

raw_value_unit_evidence: Table 3 row Pyruvate line in split '2-Oxocaproate / pyruvate' row group; column Km (mM); value 25.00 mM with parenthetical SD 0.60 mM.

substrate: pyruvate


substrate_name: L-alanine

column_label: Table 2 lists row L-Alanine under column Km (mM) with central value 28.20 mM and parenthetical SD 0.75 mM.

normalized_value_unit_evidence: Km 28.20 mM; exported Km 28.2 mM.

raw_value_unit_evidence: Table 2 row L-Alanine; column Km (mM); value 28.20 mM with parenthetical SD 0.75 mM.

row_label: L-Alanine

substrate: L-alanine


enzyme_display_name: diaminopimelate dehydrogenase

organism: Symbiobacterium thermophilum

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V156D to reconstruct the assayed variant sequence.

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

proof_lines: mutant V156D, pH not specified in the publication, temperature not specified in the publication

enzyme: diaminopimelate dehydrogenase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V14L to reconstruct the assayed variant sequence.

proof_lines: mutant V14L, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P69G to reconstruct the assayed variant sequence.

proof_lines: mutant P69G, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V68M to reconstruct the assayed variant sequence.

proof_lines: mutant V68M, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K159R to reconstruct the assayed variant sequence.

proof_lines: mutant K159R, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q67PI3 and applied mutation signature T70S to reconstruct the assayed variant sequence.

column_label: Table 1 (Determination of Kinetic Parameters of StDAPDH and Its Variants), pyruvic acid block, protein row T70S; column KM (mM) = 10.71 ± 0.64; column kcat (s-1) = 8.30 ± 0.21; column kcat/KM (mM-1 s-1) = 0.78; column relative kcat/KM = 0.90.

normalized_value_unit_evidence: kcat: printed Table 1 cell 8.30 under the pyruvic acid column head kcat (s-1); the printed unit is already the export unit, so no unit conversion applies and the value is 8.3 s^(-1). Km: printed Table 1 cell 10.71 under the pyruvic acid column head KM (mM); the printed unit is already the export unit, so no unit conversion applies and the value is 10.71 mM. kcat/KM: printed Table 1 cell 0.78 under the pyruvic acid column head kcat/KM (mM-1 s-1); the printed unit is already the export unit, so no unit conversion applies and the value is 0.78 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, pyruvic acid block, protein row T70S: KM = 10.71 ± 0.64 mM; kcat = 8.30 ± 0.21 s-1; printed kcat/KM = 0.78 mM-1 s-1.

table_label: Table 1: Determination of Kinetic Parameters of StDAPDH and Its Variants (J. Chem. Inf. Model. 2019, volume 59, number 5, pages 2331-2338); pyruvic acid block, printed column heads protein | KM (mM) | kcat (s-1) | kcat/KM (mM-1 s-1) | relative kcat/KM


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q67PI3 and applied mutation signature S90T to reconstruct the assayed variant sequence.

column_label: Table 1 (Determination of Kinetic Parameters of StDAPDH and Its Variants), meso-DAP block, protein row S90T; column KM (mM) = 0.27 ± 0.02; column kcat (s-1) = 8.81 ± 0.29; column kcat/KM (mM-1 s-1) = 32.38; column relative kcat/KM = 0.22.

normalized_value_unit_evidence: kcat: printed Table 1 cell 8.81 under the meso-DAP column head kcat (s-1); the printed unit is already the export unit, so no unit conversion applies and the value is 8.81 s^(-1). Km: printed Table 1 cell 0.27 under the meso-DAP column head KM (mM); the printed unit is already the export unit, so no unit conversion applies and the value is 0.27 mM. kcat/KM: printed Table 1 cell 32.38 under the meso-DAP column head kcat/KM (mM-1 s-1); the printed unit is already the export unit, so no unit conversion applies and the value is 32.38 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, meso-DAP block, protein row S90T: KM = 0.27 ± 0.02 mM; kcat = 8.81 ± 0.29 s-1; printed kcat/KM = 32.38 mM-1 s-1.

table_label: Table 1: Determination of Kinetic Parameters of StDAPDH and Its Variants (J. Chem. Inf. Model. 2019, volume 59, number 5, pages 2331-2338); meso-DAP block, printed column heads protein | KM (mM) | kcat (s-1) | kcat/KM (mM-1 s-1) | relative kcat/KM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S90T to reconstruct the assayed variant sequence.

proof_lines: mutant S90T, pH not specified in the publication, temperature not specified in the publication


column_label: Table 1 (Determination of Kinetic Parameters of StDAPDH and Its Variants), meso-DAP block, protein row T70S; column KM (mM) = 0.18 ± 0.02; column kcat (s-1) = 23.86 ± 0.76; column kcat/KM (mM-1 s-1) = 130.0; column relative kcat/KM = 0.87.

normalized_value_unit_evidence: kcat: printed Table 1 cell 23.86 under the meso-DAP column head kcat (s-1); the printed unit is already the export unit, so no unit conversion applies and the value is 23.86 s^(-1). Km: printed Table 1 cell 0.18 under the meso-DAP column head KM (mM); the printed unit is already the export unit, so no unit conversion applies and the value is 0.18 mM. kcat/KM: printed Table 1 cell 130.0 under the meso-DAP column head kcat/KM (mM-1 s-1); the printed unit is already the export unit, so no unit conversion applies and the value is 130.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, meso-DAP block, protein row T70S: KM = 0.18 ± 0.02 mM; kcat = 23.86 ± 0.76 s-1; printed kcat/KM = 130.0 mM-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q67PI3 and applied mutation signature K159R to reconstruct the assayed variant sequence.

column_label: Table 1 (Determination of Kinetic Parameters of StDAPDH and Its Variants), meso-DAP block, protein row K159R; column KM (mM) = 0.21 ± 0.05; column kcat (s-1) = 24.50 ± 1.97; column kcat/KM (mM-1 s-1) = 117.15; column relative kcat/KM = 0.79.

normalized_value_unit_evidence: kcat: printed Table 1 cell 24.50 under the meso-DAP column head kcat (s-1); the printed unit is already the export unit, so no unit conversion applies and the value is 24.5 s^(-1). Km: printed Table 1 cell 0.21 under the meso-DAP column head KM (mM); the printed unit is already the export unit, so no unit conversion applies and the value is 0.21 mM. kcat/KM: printed Table 1 cell 117.15 under the meso-DAP column head kcat/KM (mM-1 s-1); the printed unit is already the export unit, so no unit conversion applies and the value is 117.15 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, meso-DAP block, protein row K159R: KM = 0.21 ± 0.05 mM; kcat = 24.50 ± 1.97 s-1; printed kcat/KM = 117.15 mM-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q67PI3 and applied mutation signature V68M to reconstruct the assayed variant sequence.

column_label: Table 1 (Determination of Kinetic Parameters of StDAPDH and Its Variants), meso-DAP block, protein row V68M; column KM (mM) = 0.52 ± 0.08; column kcat (s-1) = 36.05 ± 2.80; column kcat/KM (mM-1 s-1) = 69.70; column relative kcat/KM = 0.47.

normalized_value_unit_evidence: kcat: printed Table 1 cell 36.05 under the meso-DAP column head kcat (s-1); the printed unit is already the export unit, so no unit conversion applies and the value is 36.05 s^(-1). Km: printed Table 1 cell 0.52 under the meso-DAP column head KM (mM); the printed unit is already the export unit, so no unit conversion applies and the value is 0.52 mM. kcat/KM: printed Table 1 cell 69.70 under the meso-DAP column head kcat/KM (mM-1 s-1); the printed unit is already the export unit, so no unit conversion applies and the value is 69.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, meso-DAP block, protein row V68M: KM = 0.52 ± 0.08 mM; kcat = 36.05 ± 2.80 s-1; printed kcat/KM = 69.70 mM-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q67PI3 and applied mutation signature V14L to reconstruct the assayed variant sequence.

column_label: Table 1 (Determination of Kinetic Parameters of StDAPDH and Its Variants), meso-DAP block, protein row V14L; column KM (mM) = 1.02 ± 0.09; column kcat (s-1) = 36.27 ± 1.81; column kcat/KM (mM-1 s-1) = 35.49; column relative kcat/KM = 0.24.

normalized_value_unit_evidence: kcat: printed Table 1 cell 36.27 under the meso-DAP column head kcat (s-1); the printed unit is already the export unit, so no unit conversion applies and the value is 36.27 s^(-1). Km: printed Table 1 cell 1.02 under the meso-DAP column head KM (mM); the printed unit is already the export unit, so no unit conversion applies and the value is 1.02 mM. kcat/KM: printed Table 1 cell 35.49 under the meso-DAP column head kcat/KM (mM-1 s-1); the printed unit is already the export unit, so no unit conversion applies and the value is 35.49 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, meso-DAP block, protein row V14L: KM = 1.02 ± 0.09 mM; kcat = 36.27 ± 1.81 s-1; printed kcat/KM = 35.49 mM-1 s-1.


proof_lines: wild-type, pH not specified in the publication, temperature not specified in the publication

proof_lines: pH 8.5, 30°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q67PI3 and applied mutation signature P69G to reconstruct the assayed variant sequence.

column_label: Table 1 (Determination of Kinetic Parameters of StDAPDH and Its Variants), meso-DAP block, protein row P69G; column KM (mM) = 0.43 ± 0.08; column kcat (s-1) = 48.79 ± 3.54; column kcat/KM (mM-1 s-1) = 113.31; column relative kcat/KM = 0.76.

normalized_value_unit_evidence: kcat: printed Table 1 cell 48.79 under the meso-DAP column head kcat (s-1); the printed unit is already the export unit, so no unit conversion applies and the value is 48.79 s^(-1). Km: printed Table 1 cell 0.43 under the meso-DAP column head KM (mM); the printed unit is already the export unit, so no unit conversion applies and the value is 0.43 mM. kcat/KM: printed Table 1 cell 113.31 under the meso-DAP column head kcat/KM (mM-1 s-1); the printed unit is already the export unit, so no unit conversion applies and the value is 113.31 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, meso-DAP block, protein row P69G: KM = 0.43 ± 0.08 mM; kcat = 48.79 ± 3.54 s-1; printed kcat/KM = 113.31 mM-1 s-1.


enzyme_display_name: cutinase

organism: Thermobifida cellulosilytica

substrate_name: 4-nitrophenyl acetate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R19S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7

enzyme: cutinase

substrate: 4-nitrophenyl acetate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q65E to reconstruct the assayed variant sequence.


substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R187K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R19S/R29N/A30V to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 25°C, recombinant mutant R19S/R29N/A30V


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R29N/A30V to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 25°C, recombinant mutant R29N/A30V


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A30V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R29N to reconstruct the assayed variant sequence.


enzyme_display_name: monoamine oxidase

organism: Danio rerio

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

assay_conditions_summary: pH 7.4; buffer containing 0

column_label: table label: Table 1 (Comparison of steady-state kinetic values for zMAO-catalyzed oxidation of amine substrate analogues with those published for hMAO A and hMAO B.); row label: p-Carboxybenzylamine; column label: kcat (min^-1); Km (uM); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; assay condition: 25 C steady-state assays in 50 mM potassium phosphate, pH 7.4 buffer containing 0.5% (w/v) reduced Triton X-100; buffers equilibrated 30 min at 25 C. Benzylamine analogues used the Amplex-red peroxidase coupled assay; phenolic substrates serotonin, dopamine, and tyramine were assayed by polarographic O2 uptake.; captured paper segment: Table 1 p-Carboxybenzylamine; kcat 0.088 s^-1, kcat_over_km 1.1578947368421053 s^-1 mM^-1, km 0.076 mM.

normalized_value_unit_evidence: kcat normalized value: 0.088; normalized unit: s^-1; kcat_over_km normalized value: 1.1578947368421053; normalized unit: s^-1 mM^-1; km normalized value: 0.076; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 5.3 +/- 0.2; raw unit: min^-1; km raw value: 76 +/- 8; raw unit: uM; kcat_over_km raw value: 0.088 / 0.076; raw unit: s^-1 per mM

row_label: p-Carboxybenzylamine

enzyme: monoamine oxidase


column_label: table label: Table 4 (Effect of para-substituents on the steady state kinetic properties and deuterium kinetic isotope effects of zMAO oxidation of benzylamine analogues.); row label: p-Me; column label: kcat (H) (min^-1); Km(H) (uM); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; assay condition: 25 C steady-state assays in 50 mM potassium phosphate, pH 7.4 buffer containing 0.5% (w/v) reduced Triton X-100; buffers equilibrated 30 min at 25 C. Benzylamine analogues used the Amplex-red peroxidase coupled assay; phenolic substrates serotonin, dopamine, and tyramine were assayed by polarographic O2 uptake.; captured paper segment: Table 4 p-Me; kcat 0.12 s^-1, kcat_over_km 1.7699115044247786 s^-1 mM^-1, km 0.0678 mM.

normalized_value_unit_evidence: kcat normalized value: 0.12; normalized unit: s^-1; kcat_over_km normalized value: 1.7699115044247786; normalized unit: s^-1 mM^-1; km normalized value: 0.0678; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 6.9 +/- 0.1; raw unit: min^-1; km raw value: 67.8 +/- 4.1; raw unit: uM; kcat_over_km raw value: 0.12 / 0.0678; raw unit: s^-1 per mM

row_label: p-Me


column_label: table label: Table 4 (Effect of para-substituents on the steady state kinetic properties and deuterium kinetic isotope effects of zMAO oxidation of benzylamine analogues.); row label: p-MeO; column label: kcat (H) (min^-1); Km(H) (uM); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; assay condition: 25 C steady-state assays in 50 mM potassium phosphate, pH 7.4 buffer containing 0.5% (w/v) reduced Triton X-100; buffers equilibrated 30 min at 25 C. Benzylamine analogues used the Amplex-red peroxidase coupled assay; phenolic substrates serotonin, dopamine, and tyramine were assayed by polarographic O2 uptake.; captured paper segment: Table 4 p-MeO; kcat 0.14 s^-1, kcat_over_km 2.5225225225225225 s^-1 mM^-1, km 0.0555 mM.

normalized_value_unit_evidence: kcat normalized value: 0.14; normalized unit: s^-1; kcat_over_km normalized value: 2.5225225225225225; normalized unit: s^-1 mM^-1; km normalized value: 0.0555; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 8.3 +/- 0.7; raw unit: min^-1; km raw value: 55.5 +/- 4.1; raw unit: uM; kcat_over_km raw value: 0.14 / 0.0555; raw unit: s^-1 per mM

row_label: p-MeO


column_label: table label: Table 4 (Effect of para-substituents on the steady state kinetic properties and deuterium kinetic isotope effects of zMAO oxidation of benzylamine analogues.); row label: p-F; column label: kcat (H) (min^-1); Km(H) (uM); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; assay condition: 25 C steady-state assays in 50 mM potassium phosphate, pH 7.4 buffer containing 0.5% (w/v) reduced Triton X-100; buffers equilibrated 30 min at 25 C. Benzylamine analogues used the Amplex-red peroxidase coupled assay; phenolic substrates serotonin, dopamine, and tyramine were assayed by polarographic O2 uptake.; captured paper segment: Table 4 p-F; kcat 0.25 s^-1, kcat_over_km 1.5527950310559007 s^-1 mM^-1, km 0.161 mM.

normalized_value_unit_evidence: kcat normalized value: 0.25; normalized unit: s^-1; kcat_over_km normalized value: 1.5527950310559007; normalized unit: s^-1 mM^-1; km normalized value: 0.161; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 14.9 +/- 0.3; raw unit: min^-1; km raw value: 161 +/- 8; raw unit: uM; kcat_over_km raw value: 0.25 / 0.161; raw unit: s^-1 per mM

row_label: p-F


column_label: table label: Table 4 (Effect of para-substituents on the steady state kinetic properties and deuterium kinetic isotope effects of zMAO oxidation of benzylamine analogues.); row label: p-CI; column label: kcat (H) (min^-1); Km(H) (uM); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; assay condition: 25 C steady-state assays in 50 mM potassium phosphate, pH 7.4 buffer containing 0.5% (w/v) reduced Triton X-100; buffers equilibrated 30 min at 25 C. Benzylamine analogues used the Amplex-red peroxidase coupled assay; phenolic substrates serotonin, dopamine, and tyramine were assayed by polarographic O2 uptake.; captured paper segment: Table 4 p-CI; kcat 0.58 s^-1, kcat_over_km 6.170212765957446 s^-1 mM^-1, km 0.094 mM. XML text reads p-CI; context is para-chloro benzylamine.

normalized_value_unit_evidence: kcat normalized value: 0.58; normalized unit: s^-1; kcat_over_km normalized value: 6.170212765957446; normalized unit: s^-1 mM^-1; km normalized value: 0.094; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 35 +/- 1; raw unit: min^-1; km raw value: 94 +/- 10; raw unit: uM; kcat_over_km raw value: 0.58 / 0.094; raw unit: s^-1 per mM

row_label: p-CI


column_label: table label: Table 4 (Effect of para-substituents on the steady state kinetic properties and deuterium kinetic isotope effects of zMAO oxidation of benzylamine analogues.); row label: p-Br; column label: kcat (H) (min^-1); Km(H) (uM); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; assay condition: 25 C steady-state assays in 50 mM potassium phosphate, pH 7.4 buffer containing 0.5% (w/v) reduced Triton X-100; buffers equilibrated 30 min at 25 C. Benzylamine analogues used the Amplex-red peroxidase coupled assay; phenolic substrates serotonin, dopamine, and tyramine were assayed by polarographic O2 uptake.; captured paper segment: Table 4 p-Br; kcat 0.67 s^-1, kcat_over_km 6.5048543689320395 s^-1 mM^-1, km 0.103 mM.

normalized_value_unit_evidence: kcat normalized value: 0.67; normalized unit: s^-1; kcat_over_km normalized value: 6.5048543689320395; normalized unit: s^-1 mM^-1; km normalized value: 0.103; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 40 +/- 3; raw unit: min^-1; km raw value: 103 +/- 20; raw unit: uM; kcat_over_km raw value: 0.67 / 0.103; raw unit: s^-1 per mM

row_label: p-Br


substrate_name: kynuramine

column_label: table label: Table 1 (Comparison of steady-state kinetic values for zMAO-catalyzed oxidation of amine substrate analogues with those published for hMAO A and hMAO B.); row label: Kynuramine; column label: kcat (min^-1); Km (uM); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; assay condition: 25 C steady-state assays in 50 mM potassium phosphate, pH 7.4 buffer containing 0.5% (w/v) reduced Triton X-100; buffers equilibrated 30 min at 25 C. Benzylamine analogues used the Amplex-red peroxidase coupled assay; phenolic substrates serotonin, dopamine, and tyramine were assayed by polarographic O2 uptake.; captured paper segment: Table 1 Kynuramine; kcat 1.25 s^-1, kcat_over_km 21.551724137931032 s^-1 mM^-1, km 0.058 mM.

normalized_value_unit_evidence: kcat normalized value: 1.25; normalized unit: s^-1; kcat_over_km normalized value: 21.551724137931032; normalized unit: s^-1 mM^-1; km normalized value: 0.058; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 75 +/- 2; raw unit: min^-1; km raw value: 58 +/- 5; raw unit: uM; kcat_over_km raw value: 1.25 / 0.058; raw unit: s^-1 per mM

row_label: Kynuramine

substrate: kynuramine


column_label: table label: Table 4 (Effect of para-substituents on the steady state kinetic properties and deuterium kinetic isotope effects of zMAO oxidation of benzylamine analogues.); row label: p-CF3; column label: kcat (H) (min^-1); Km(H) (uM); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; assay condition: 25 C steady-state assays in 50 mM potassium phosphate, pH 7.4 buffer containing 0.5% (w/v) reduced Triton X-100; buffers equilibrated 30 min at 25 C. Benzylamine analogues used the Amplex-red peroxidase coupled assay; phenolic substrates serotonin, dopamine, and tyramine were assayed by polarographic O2 uptake.; captured paper segment: Table 4 p-CF3; kcat 1.57 s^-1, kcat_over_km 13.652173913043478 s^-1 mM^-1, km 0.115 mM.

normalized_value_unit_evidence: kcat normalized value: 1.57; normalized unit: s^-1; kcat_over_km normalized value: 13.652173913043478; normalized unit: s^-1 mM^-1; km normalized value: 0.115; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 94 +/- 7; raw unit: min^-1; km raw value: 115 +/- 36; raw unit: uM; kcat_over_km raw value: 1.57 / 0.115; raw unit: s^-1 per mM


column_label: table label: Table 1 (Comparison of steady-state kinetic values for zMAO-catalyzed oxidation of amine substrate analogues with those published for hMAO A and hMAO B.); row label: 4-Phenylbutylamine; column label: kcat (min^-1); Km (uM); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; assay condition: 25 C steady-state assays in 50 mM potassium phosphate, pH 7.4 buffer containing 0.5% (w/v) reduced Triton X-100; buffers equilibrated 30 min at 25 C. Benzylamine analogues used the Amplex-red peroxidase coupled assay; phenolic substrates serotonin, dopamine, and tyramine were assayed by polarographic O2 uptake.; captured paper segment: Table 1 4-Phenylbutylamine; kcat 2.07 s^-1, kcat_over_km 11.189189189189188 s^-1 mM^-1, km 0.185 mM.

normalized_value_unit_evidence: kcat normalized value: 2.07; normalized unit: s^-1; kcat_over_km normalized value: 11.189189189189188; normalized unit: s^-1 mM^-1; km normalized value: 0.185; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 124 +/- 4; raw unit: min^-1; km raw value: 185 +/- 17; raw unit: uM; kcat_over_km raw value: 2.07 / 0.185; raw unit: s^-1 per mM


substrate_name: serotonin

column_label: table label: Table 1 (Comparison of steady-state kinetic values for zMAO-catalyzed oxidation of amine substrate analogues with those published for hMAO A and hMAO B.); row label: Serotonin; column label: kcat (min^-1); Km (uM); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; assay condition: 25 C steady-state assays in 50 mM potassium phosphate, pH 7.4 buffer containing 0.5% (w/v) reduced Triton X-100; buffers equilibrated 30 min at 25 C. Benzylamine analogues used the Amplex-red peroxidase coupled assay; phenolic substrates serotonin, dopamine, and tyramine were assayed by polarographic O2 uptake.; captured paper segment: Table 1 Serotonin; kcat 3.12 s^-1, kcat_over_km 45.21739130434782 s^-1 mM^-1, km 0.069 mM.

normalized_value_unit_evidence: kcat normalized value: 3.12; normalized unit: s^-1; kcat_over_km normalized value: 45.21739130434782; normalized unit: s^-1 mM^-1; km normalized value: 0.069; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 187 +/- 9; raw unit: min^-1; km raw value: 69 +/- 11; raw unit: uM; kcat_over_km raw value: 3.12 / 0.069; raw unit: s^-1 per mM

row_label: Serotonin

substrate: serotonin


substrate_name: dopamine

column_label: table label: Table 1 (Comparison of steady-state kinetic values for zMAO-catalyzed oxidation of amine substrate analogues with those published for hMAO A and hMAO B.); row label: Dopamine; column label: kcat (min^-1); Km (uM); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; assay condition: 25 C steady-state assays in 50 mM potassium phosphate, pH 7.4 buffer containing 0.5% (w/v) reduced Triton X-100; buffers equilibrated 30 min at 25 C. Benzylamine analogues used the Amplex-red peroxidase coupled assay; phenolic substrates serotonin, dopamine, and tyramine were assayed by polarographic O2 uptake.; captured paper segment: Table 1 Dopamine; kcat 4.03 s^-1, kcat_over_km 45.795454545454554 s^-1 mM^-1, km 0.088 mM.

normalized_value_unit_evidence: kcat normalized value: 4.03; normalized unit: s^-1; kcat_over_km normalized value: 45.795454545454554; normalized unit: s^-1 mM^-1; km normalized value: 0.088; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 242 +/- 17; raw unit: min^-1; km raw value: 88 +/- 14; raw unit: uM; kcat_over_km raw value: 4.03 / 0.088; raw unit: s^-1 per mM

row_label: Dopamine

substrate: dopamine