organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)


enzyme_display_name: D-aspartate oxidase

organism: Homo sapiens

substrate_name: D-histidine

source_db: oed

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

data_origin: experimental

enzyme: D-aspartate oxidase

substrate: D-histidine

status: unverified

source: oed


substrate_name: D-proline

substrate: D-proline


substrate_name: N-Methyl-D-aspartate

substrate: N-Methyl-D-aspartate


substrate_name: D-Asparagine

substrate: D-Asparagine


enzyme_display_name: L-glutamate oxidase precursor

organism: Streptomyces sp

substrate_name: L-aspartate (mature LGOX)

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

enzyme: L-glutamate oxidase precursor

substrate: L-aspartate (mature LGOX)

source: uniprot


enzyme_display_name: L-lysine oxidase

organism: Trichoderma viride

substrate_name: L-lysine

source_db: brenda

verification_status: verified

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

sequence_source: multiple

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

assay_conditions_summary: pH 4; 313.15 K; buffer pH 8

column_label: Table 1 columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1); row mature LysOX.

normalized_value_unit_evidence: Km 0.013 mM and kcat 65.5 s^-1 match the export; same-row central-value ratio 65.5/0.013 = 5038.461538461539 s^-1*mM^-1, while the table rounds kcat/Km to 5.0 x 10^3.

raw_value_unit_evidence: Table 1 row mature LysOX reports Km 1.3 x 10^-2 mM, kcat 65.5 s^-1, and kcat/Km 5.0 x 10^3 s^-1 mM^-1.

row_label: mature LysOX

table_label: Table 1: Kinetic parameters of prLysOX and mature LysOX

source_databases_merged: brenda skid

enzyme: L-lysine oxidase

substrate: L-lysine

status: verified

source: brenda


enzyme_display_name: cyclohexylamine oxidase

organism: Microbacterium oxydans

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

enzyme: cyclohexylamine oxidase


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

mutation_type: substitution


proof_lines: mutant enzyme T198F/L199S/M226F, at pH 6.5 and 30°C


proof_lines: mutant enzyme T198F/L199S, at pH 6.5 and 30°C


substrate_name: L-valine ethyl ester

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

proof_lines: pH and temperature not specified in the publication, mutant enzyme M226T

substrate: L-valine ethyl ester


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


organism: Arthrobacter sp. TYUT010-15


enzyme_display_name: L-glutamate oxidase

organism: Streptomyces sp. X-119-6

substrate_name: L-glutamate

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

assay_conditions_summary: pH 6; buffer phosphate

proof_lines: pH 6.0, 30°C, recombinant enzyme before proteolysis by metalloendopeptidase from Streptomyces griseus

proof_lines: pH 7.4, 30°C, recombinant enzyme before proteolysis by metalloendopeptidase from Streptomyces griseus

proof_lines: pH 6.0, 30°C, recombinant enzyme treated with metalloendopeptidase from Streptomyces griseus

source_databases_merged: brenda skid uniprot

enzyme: L-glutamate oxidase

substrate: L-glutamate


organism: Streptomyces mobaraensis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H533L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S280T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S280T/H533L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0J9X1X3 and applied mutation signature D212A to reconstruct the assayed variant sequence.

column_label: Table 2 columns read for the row 'LysOX D212A'; column 'Specific activity (U/mg)' = 18.5; column 'Km (mM)' = 0.56; column 'kcat (s-1)' = 26.4; column 'kcat/Km' = 47.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.56 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 0.56 mM. kcat: printed Table 2 cell 26.4 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 26.4 s^(-1). kcat/Km: the printed Table 2 cell 47 s^-1 mM^-1 is the paper's rounded rendering of the same row's own quotient 26.4 / 0.56 = 47.14285714285714 s^-1 mM^-1, and that full-precision quotient is the exported value; the printed cell is carried as its rounded corroboration.

raw_value_unit_evidence: Table 2, row 'LysOX D212A': Km = 0.56 mM; kcat = 26.4 s^-1; printed kcat/Km = 47 s^-1 mM^-1.

row_label: Table 2, row LysOX D212A

table_label: Table 2: Kinetic parameters of LysOX and LysOX mutant variants for L-lysine (Protein Science 2020, 29:2213-2225)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0J9X1X3 and applied mutation signature D212A/D315A to reconstruct the assayed variant sequence.

column_label: Table 2 columns read for the row 'LysOX D212A/D315A'; column 'Specific activity (U/mg)' = 6.4; column 'Km (mM)' = 7.6; column 'kcat (s-1)' = 17.0; column 'kcat/Km' = 2.2.

normalized_value_unit_evidence: Km: printed Table 2 cell 7.6 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 7.6 mM. kcat: printed Table 2 cell 17.0 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 17.0 s^(-1). kcat/Km: the printed Table 2 cell 2.2 s^-1 mM^-1 is the paper's rounded rendering of the same row's own quotient 17.0 / 7.6 = 2.236842105263158 s^-1 mM^-1, and that full-precision quotient is the exported value; the printed cell is carried as its rounded corroboration.

raw_value_unit_evidence: Table 2, row 'LysOX D212A/D315A': Km = 7.6 mM; kcat = 17.0 s^-1; printed kcat/Km = 2.2 s^-1 mM^-1.

row_label: Table 2, row LysOX D212A/D315A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0J9X1X3 and applied mutation signature D315A to reconstruct the assayed variant sequence.

column_label: Table 2 columns read for the row 'LysOX D315A'; column 'Specific activity (U/mg)' = 22.2; column 'Km (mM)' = 0.28; column 'kcat (s-1)' = 24.3; column 'kcat/Km' = 87.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.28 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 0.28 mM. kcat: printed Table 2 cell 24.3 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 24.3 s^(-1). kcat/Km: the printed Table 2 cell 87 s^-1 mM^-1 is the paper's rounded rendering of the same row's own quotient 24.3 / 0.28 = 86.78571428571428 s^-1 mM^-1, and that full-precision quotient is the exported value; the printed cell is carried as its rounded corroboration.

raw_value_unit_evidence: Table 2, row 'LysOX D315A': Km = 0.28 mM; kcat = 24.3 s^-1; printed kcat/Km = 87 s^-1 mM^-1.

row_label: Table 2, row LysOX D315A


column_label: Table 2 columns read for the row 'Recombinant LysOX, From Escherichia coli'; column 'Specific activity (U/mg)' = 66.1; column 'Km (mM)' = 1.3 x 10^-2; column 'kcat (s-1)' = 62.8; column 'kcat/Km' = 4.8 x 10^3.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.3 x 10^-2 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 0.013 mM. kcat: printed Table 2 cell 62.8 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 62.8 s^(-1). kcat/Km: the printed Table 2 cell 4.8 x 10^3 s^-1 mM^-1 is the paper's rounded rendering of the same row's own quotient 62.8 / 0.013 = 4830.7692307692305 s^-1 mM^-1, and that full-precision quotient is the exported value; the printed cell is carried as its rounded corroboration.

raw_value_unit_evidence: Table 2, row 'Recombinant LysOX, From Escherichia coli': Km = 1.3 x 10^-2 mM; kcat = 62.8 s^-1; printed kcat/Km = 4.8 x 10^3 s^-1 mM^-1.

row_label: Table 2, row Recombinant LysOX, From Escherichia coli


enzyme_display_name: putrescine oxidase

organism: Paenarthrobacter aurescens

substrate_name: spermidine

smiles: C(CCNCCCN)CN

assay_conditions_summary: pH 8

enzyme: putrescine oxidase

substrate: spermidine


substrate_name: cadaverine

smiles: C(CCN)CCN

substrate: cadaverine


substrate_name: putrescine

smiles: C(CCN)CN

assay_conditions_summary: pH 7

substrate: putrescine


organism: Caenorhabditis elegans

substrate_name: D-Aspartate

proof_lines:
D-aspartate oxidase
D-aspartate
D-glutamate

substrate: D-Aspartate


substrate_name: D-Glutamate

proof_lines:
D-aspartate oxidase
D-glutamate
D-aspartate

substrate: D-Glutamate


substrate_name: N-Methyl-D-aspartic acid

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

substrate: N-Methyl-D-aspartic acid


enzyme_display_name: phenylalanine dehydrogenase

organism: Lysinibacillus sphaericus

substrate_name: L-Methionine

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

proof_lines:
Bacillus sphaericus
Lysinibacillus sphaericus
phenylalanine dehydrogenase

enzyme: phenylalanine dehydrogenase

substrate: L-Methionine


assay_conditions_summary: pH 10.4; 298.15 K; cofactor NAD+

column_label: Table label: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs. Row: L-methionine | wt. Enzyme column: wt. Columns read: Km (mM) cell 2.7, kcat (s-1) cell 1.2, kcat/Km (s-1 mM-1) cell 0.44. metric: kcat; raw value: 1.2; raw unit: s^-1; normalized value: 1.2 s^(-1); metric: Km; raw value: 2.7; raw unit: mM; normalized value: 2.7 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 0.4444444444444444 s^-1 mM^-1; assay condition: Oxidative deamination was assayed at 25 °C by measuring the reduction of NAD+ at 340 nm in a 1-cm cuvette; the reaction mixture contained 50 µmol of glycine-KOH buffer, pH 10.4, 100 µmol of KCl and the appropriate amount of enzyme in a total volume of 1 mL, and for amino acid substrates the NAD+ concentration was fixed at 2.5 mM while the amino acid concentration was varied. Steady-state kinetic parameters Km and kcat were obtained by fitting data from duplicate activity readings to the Michaelis-Menten equation. Export row conditions: pH 10.4; 298.15 K.

normalized_value_unit_evidence: Table 4, row L-methionine | wt: Km 2.7 mM = 2.7 mM (already the export unit, no conversion); kcat 1.2 s^-1 = 1.2 s^(-1) (already the export unit, no conversion); kcat/Km = kcat divided by Km = 0.4444444444444444 s^-1 mM^-1. In the PDF text extraction the plus/minus sign renders as `(`, so the printed cell `1.3 ( 0.10` is the paper's 1.3 +/- 0.10, and superscripts are flattened, so the column headers read `kcat (s-1)` and `(s-1 mM-1)` for kcat (s^-1) and kcat/Km (s^-1 mM^-1). The two-column page layout places Table 4 and Table 5 rows on the same physical line; only the left-hand Table 4 columns are quoted for Table 4 rows.

raw_value_unit_evidence: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs | header row: substrates    enzyme     Km (mM)          kcat (s-1)    (s-1 mM-1) | row: L-methionine wt           2.7 ( 0.19      1.2 ( 0.034        0.44 | the wt cells read: Km = 2.7 mM; kcat = 1.2 s^-1; kcat/Km = 0.44 s^-1 mM^-1

row_label: L-methionine | wt


substrate_name: L-Norleucine

substrate: L-Norleucine


verification_status: corrected

assay_conditions_summary: pH 10.4; 298.15 K; buffer pH 10; cofactor NAD+

column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs (Biochemistry 2002, 41(38):11390-11397); printed column heads substrates | enzyme | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 4, substrate block 'L-norleucine', enzyme row 'wt'; column Km (mM) = 0.79; column kcat (s-1) = 3.2; column kcat/Km (s-1 mM-1) = 4.0. captured primary segment: L-norleucine | wt | Km 0.79 mM | kcat 3.2 s^-1 | kcat/Km 4.0 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 4 Km cell 0.79 mM; the printed column is already in mM, so no unit conversion applies and the value is 0.79 mM. kcat: printed Table 4 kcat cell 3.2 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 3.2 s^(-1). kcat/Km: printed Table 4 kcat/Km cell 4.0 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 4.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.2 / 0.79 = 4.050632911392405 s^-1 mM^-1, against the printed efficiency cell 4.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, substrate block 'L-norleucine', enzyme row 'wt': Km = 0.79 mM; kcat = 3.2 s^-1; kcat/Km = 4.0 s^-1 mM^-1.

status: corrected


substrate_name: L-Norvaline

substrate: L-Norvaline


substrate_name: L-ornithine

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

substrate: L-ornithine


smiles: O=O


substrate_name: L-phenylalanine

substrate: L-phenylalanine


organism: Rhodococcus erythropolis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A394C to reconstruct the assayed variant sequence.

smiles: NCCCCN


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A394C/A396T/Q431G to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature P15I/A394C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: L-amino-acid oxidase 4

organism: Hebeloma cylindrosporum

substrate_name: L-methionine (untreated)

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

assay_conditions_summary: pH 7; buffer TEA

column_label: Table 2; row l-methionine; untreated columns Km (mM) and vmax (U/mg).

normalized_value_unit_evidence: Untreated l-methionine Km is already reported as 0.16 mM, matching the export.

raw_value_unit_evidence: Table 2 row l-methionine reports untreated Km 0.16 +/- 0.10 mM and vmax 5.98 +/- 0.38 U/mg; activated Km is separate at 0.41 +/- 0.17 mM.

row_label: l-methionine, untreated 9His-hcLAAO4

table_label: Table 2: Kinetic properties of untreated and acid-activated 9His-hcLAAO4

enzyme: L-amino-acid oxidase 4

substrate: L-methionine (untreated)


substrate_name: L-phenylalanine methyl ester (untreated)


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


proof_lines: pH and temperature not specified in the publication, mutant enzyme L199F


sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature T198I with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme T198I


proof_lines: pH and temperature not specified in the publication, mutant enzyme Y321I


sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature T198F with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


proof_lines: pH and temperature not specified in the publication, mutant enzyme Y321I/T198I


proof_lines: pH and temperature not specified in the publication, mutant enzyme Y321I/ M226T


proof_lines: pH and temperature not specified in the publication, mutant enzyme Y321I/M226T/T198I


proof_lines: pH and temperature not specified in the publication, mutant enzyme Y321I/M226T/T198I/F199F


organism: Streptomyces viridosporus

proof_lines:
L-glutamate oxidase
Streptomyces ghanaensis
alpha-ketoglutaric acid production


substrate_name: D-Asp

substrate: D-Asp


organism: Kocuria rosea


substrate_name: L-glutamine (untreated)

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

column_label: Columns Substrate, vmax [U mg^-1], Km [mM], kcat [s^-1], kcat/Km; untreated top block row L-Glutamine.

raw_value_unit_evidence: Untreated Table 2 row L-Glutamine: vmax 2.22 +/- 0.65 U mg^-1; Km 0.46 +/- 0.07 mM; kcat 2.56 s^-1; kcat/Km 5.58.

row_label: L-Glutamine

table_label: Table 2, kinetic properties of untreated and acid-activated 6His-hcLAAO4

substrate: L-glutamine (untreated)


substrate_name: L-leucine (untreated)

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

substrate: L-leucine (untreated)


substrate_name: L-phenylalanine (untreated)

column_label: Columns Substrate, vmax [U mg^-1], Km [mM], kcat [s^-1], kcat/Km; untreated top block row L-Phenylalanine.

raw_value_unit_evidence: Untreated Table 2 row L-Phenylalanine: vmax 0.72 +/- 0.21 U mg^-1; Km 0.26 +/- 0.11 mM; kcat 0.83 s^-1; kcat/Km 3.14.

row_label: L-Phenylalanine

substrate: L-phenylalanine (untreated)


substrate_name: L-leucine methyl ester (untreated)

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

substrate: L-leucine methyl ester (untreated)


substrate_name: L-Tyrosine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23307 and applied mutation signature N145V to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates (Biochemistry 2002, 41(38):11390-11397); printed column heads substrate | enzyme | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 2, substrate block 'L-tyrosine', enzyme row 'N145V'; column Km (mM) = 1.2; column kcat (s-1) = 23; column kcat/Km (s-1 mM-1) = 19. captured primary segment: L-tyrosine | N145V | Km 1.2 mM | kcat 23 s^-1 | kcat/Km 19 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 1.2 mM; the printed column is already in mM, so no unit conversion applies and the value is 1.2 mM. kcat: printed Table 2 kcat cell 23 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 23.0 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 19 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 19.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 23.0 / 1.2 = 19.166666666666668 s^-1 mM^-1, against the printed efficiency cell 19.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate block 'L-tyrosine', enzyme row 'N145V': Km = 1.2 mM; kcat = 23 s^-1; kcat/Km = 19 s^-1 mM^-1.

substrate: L-Tyrosine


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

column_label: Table label: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates. Row: L-tyrosine | wt. Enzyme column: wt. Columns read: Km (mM) cell 1.3, kcat (s-1) cell 68, kcat/Km (s-1 mM-1) cell 52. metric: kcat; raw value: 68; raw unit: s^-1; normalized value: 68.0 s^(-1); metric: Km; raw value: 1.3; raw unit: mM; normalized value: 1.3 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 52.30769230769231 s^-1 mM^-1; assay condition: Oxidative deamination was assayed at 25 °C by measuring the reduction of NAD+ at 340 nm in a 1-cm cuvette; the reaction mixture contained 50 µmol of glycine-KOH buffer, pH 10.4, 100 µmol of KCl and the appropriate amount of enzyme in a total volume of 1 mL, and for amino acid substrates the NAD+ concentration was fixed at 2.5 mM while the amino acid concentration was varied. Steady-state kinetic parameters Km and kcat were obtained by fitting data from duplicate activity readings to the Michaelis-Menten equation. Export row conditions: pH 10.4; 298.15 K.

normalized_value_unit_evidence: Table 2, row L-tyrosine | wt: Km 1.3 mM = 1.3 mM (already the export unit, no conversion); kcat 68 s^-1 = 68.0 s^(-1) (already the export unit, no conversion); kcat/Km = kcat divided by Km = 52.30769230769231 s^-1 mM^-1. In the PDF text extraction the plus/minus sign renders as `(`, so the printed cell `1.3 ( 0.10` is the paper's 1.3 +/- 0.10, and superscripts are flattened, so the column headers read `kcat (s-1)` and `(s-1 mM-1)` for kcat (s^-1) and kcat/Km (s^-1 mM^-1). The two-column page layout places Table 4 and Table 5 rows on the same physical line; only the left-hand Table 4 columns are quoted for Table 4 rows.

raw_value_unit_evidence: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates | header row: substrate     enzyme        Km (mM)           kcat (s-1) (s-1 mM-1) | row: L-tyrosine      wt             1.3 ( 0.10        68 ( 2.1       52 | the wt cells read: Km = 1.3 mM; kcat = 68 s^-1; kcat/Km = 52 s^-1 mM^-1

row_label: L-tyrosine | wt


substrate_name: L-Valine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23307 and applied mutation signature N145A to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs (Biochemistry 2002, 41(38):11390-11397); printed column heads substrates | enzyme | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 4, substrate block 'L-valine', enzyme row 'N145A'; column Km (mM) = 0.14; column kcat (s-1) = 0.85; column kcat/Km (s-1 mM-1) = 6.1. captured primary segment: L-valine | N145A | Km 0.14 mM | kcat 0.85 s^-1 | kcat/Km 6.1 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 4 Km cell 0.14 mM; the printed column is already in mM, so no unit conversion applies and the value is 0.14 mM. kcat: printed Table 4 kcat cell 0.85 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.85 s^(-1). kcat/Km: printed Table 4 kcat/Km cell 6.1 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 6.1 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.85 / 0.14 = 6.07142857142857 s^-1 mM^-1, against the printed efficiency cell 6.1 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, substrate block 'L-valine', enzyme row 'N145A': Km = 0.14 mM; kcat = 0.85 s^-1; kcat/Km = 6.1 s^-1 mM^-1.

substrate: L-Valine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23307 and applied mutation signature N145I to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs (Biochemistry 2002, 41(38):11390-11397); printed column heads substrates | enzyme | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 4, substrate block 'L-valine', enzyme row 'N145I'; column Km (mM) = 0.23; column kcat (s-1) = 1.6; column kcat/Km (s-1 mM-1) = 7.0. captured primary segment: L-valine | N145I | Km 0.23 mM | kcat 1.6 s^-1 | kcat/Km 7.0 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 4 Km cell 0.23 mM; the printed column is already in mM, so no unit conversion applies and the value is 0.23 mM. kcat: printed Table 4 kcat cell 1.6 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 1.6 s^(-1). kcat/Km: printed Table 4 kcat/Km cell 7.0 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 7.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.6 / 0.23 = 6.956521739130435 s^-1 mM^-1, against the printed efficiency cell 7.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, substrate block 'L-valine', enzyme row 'N145I': Km = 0.23 mM; kcat = 1.6 s^-1; kcat/Km = 7.0 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23307 and applied mutation signature N145L to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs (Biochemistry 2002, 41(38):11390-11397); printed column heads substrates | enzyme | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 4, substrate block 'L-valine', enzyme row 'N145L'; column Km (mM) = 0.27; column kcat (s-1) = 0.62; column kcat/Km (s-1 mM-1) = 2.3. captured primary segment: L-valine | N145L | Km 0.27 mM | kcat 0.62 s^-1 | kcat/Km 2.3 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 4 Km cell 0.27 mM; the printed column is already in mM, so no unit conversion applies and the value is 0.27 mM. kcat: printed Table 4 kcat cell 0.62 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.62 s^(-1). kcat/Km: printed Table 4 kcat/Km cell 2.3 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 2.3 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.62 / 0.27 = 2.2962962962962963 s^-1 mM^-1, against the printed efficiency cell 2.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, substrate block 'L-valine', enzyme row 'N145L': Km = 0.27 mM; kcat = 0.62 s^-1; kcat/Km = 2.3 s^-1 mM^-1.


column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs (Biochemistry 2002, 41(38):11390-11397); printed column heads substrates | enzyme | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 4, substrate block 'L-valine', enzyme row 'N145V'; column Km (mM) = 0.27; column kcat (s-1) = 1.4; column kcat/Km (s-1 mM-1) = 5.2. captured primary segment: L-valine | N145V | Km 0.27 mM | kcat 1.4 s^-1 | kcat/Km 5.2 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 4 Km cell 0.27 mM; the printed column is already in mM, so no unit conversion applies and the value is 0.27 mM. kcat: printed Table 4 kcat cell 1.4 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 1.4 s^(-1). kcat/Km: printed Table 4 kcat/Km cell 5.2 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 5.2 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.4 / 0.27 = 5.185185185185184 s^-1 mM^-1, against the printed efficiency cell 5.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, substrate block 'L-valine', enzyme row 'N145V': Km = 0.27 mM; kcat = 1.4 s^-1; kcat/Km = 5.2 s^-1 mM^-1.


column_label: Table label: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs. Row: L-valine | wt. Enzyme column: wt. Columns read: Km (mM) cell 2.0, kcat (s-1) cell 0.91, kcat/Km (s-1 mM-1) cell 0.46. metric: kcat; raw value: 0.91; raw unit: s^-1; normalized value: 0.91 s^(-1); metric: Km; raw value: 2.0; raw unit: mM; normalized value: 2.0 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 0.455 s^-1 mM^-1; assay condition: Oxidative deamination was assayed at 25 °C by measuring the reduction of NAD+ at 340 nm in a 1-cm cuvette; the reaction mixture contained 50 µmol of glycine-KOH buffer, pH 10.4, 100 µmol of KCl and the appropriate amount of enzyme in a total volume of 1 mL, and for amino acid substrates the NAD+ concentration was fixed at 2.5 mM while the amino acid concentration was varied. Steady-state kinetic parameters Km and kcat were obtained by fitting data from duplicate activity readings to the Michaelis-Menten equation. Export row conditions: pH 10.4; 298.15 K.

normalized_value_unit_evidence: Table 4, row L-valine | wt: Km 2.0 mM = 2.0 mM (already the export unit, no conversion); kcat 0.91 s^-1 = 0.91 s^(-1) (already the export unit, no conversion); kcat/Km = kcat divided by Km = 0.455 s^-1 mM^-1. In the PDF text extraction the plus/minus sign renders as `(`, so the printed cell `1.3 ( 0.10` is the paper's 1.3 +/- 0.10, and superscripts are flattened, so the column headers read `kcat (s-1)` and `(s-1 mM-1)` for kcat (s^-1) and kcat/Km (s^-1 mM^-1). The two-column page layout places Table 4 and Table 5 rows on the same physical line; only the left-hand Table 4 columns are quoted for Table 4 rows.

raw_value_unit_evidence: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs | header row: substrates    enzyme     Km (mM)          kcat (s-1)    (s-1 mM-1) | row: L-valine       wt         2.0 ( 0.10     0.91 ( 0.020         0.46 | the wt cells read: Km = 2.0 mM; kcat = 0.91 s^-1; kcat/Km = 0.46 s^-1 mM^-1

row_label: L-valine | wt


substrate_name: phenylpyruvate

assay_conditions_summary: pH 8.6; 298.15 K; cofactor NADH

column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates (Biochemistry 2002, 41(38):11390-11397); printed column heads substrate | enzyme | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 2, substrate block 'phenylpyruvate', enzyme row 'N145A'; column Km (mM) = 0.030; column kcat (s-1) = 71; column kcat/Km (s-1 mM-1) = 2367. captured primary segment: phenylpyruvate | N145A | Km 0.030 mM | kcat 71 s^-1 | kcat/Km 2367 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 0.030 mM; the printed column is already in mM, so no unit conversion applies and the value is 0.03 mM. kcat: printed Table 2 kcat cell 71 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 71.0 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 2367 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 2367.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 71.0 / 0.03 = 2366.666666666667 s^-1 mM^-1, against the printed efficiency cell 2367.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate block 'phenylpyruvate', enzyme row 'N145A': Km = 0.030 mM; kcat = 71 s^-1; kcat/Km = 2367 s^-1 mM^-1.

substrate: phenylpyruvate


column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates (Biochemistry 2002, 41(38):11390-11397); printed column heads substrate | enzyme | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 2, substrate block 'phenylpyruvate', enzyme row 'N145I'; column Km (mM) = 0.012; column kcat (s-1) = 43; column kcat/Km (s-1 mM-1) = 3583. captured primary segment: phenylpyruvate | N145I | Km 0.012 mM | kcat 43 s^-1 | kcat/Km 3583 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 0.012 mM; the printed column is already in mM, so no unit conversion applies and the value is 0.012 mM. kcat: printed Table 2 kcat cell 43 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 43.0 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 3583 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 3583.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 43.0 / 0.012 = 3583.3333333333335 s^-1 mM^-1, against the printed efficiency cell 3583.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate block 'phenylpyruvate', enzyme row 'N145I': Km = 0.012 mM; kcat = 43 s^-1; kcat/Km = 3583 s^-1 mM^-1.


column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates (Biochemistry 2002, 41(38):11390-11397); printed column heads substrate | enzyme | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 2, substrate block 'phenylpyruvate', enzyme row 'N145L'; column Km (mM) = 0.0095; column kcat (s-1) = 23; column kcat/Km (s-1 mM-1) = 2421. captured primary segment: phenylpyruvate | N145L | Km 0.0095 mM | kcat 23 s^-1 | kcat/Km 2421 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 0.0095 mM; the printed column is already in mM, so no unit conversion applies and the value is 0.0095 mM. kcat: printed Table 2 kcat cell 23 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 23.0 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 2421 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 2421.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 23.0 / 0.0095 = 2421.0526315789475 s^-1 mM^-1, against the printed efficiency cell 2421.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate block 'phenylpyruvate', enzyme row 'N145L': Km = 0.0095 mM; kcat = 23 s^-1; kcat/Km = 2421 s^-1 mM^-1.


substrate_name: putrescine

substrate: putrescine


substrate: L-phenylalanine methyl ester (untreated)


substrate_name: L-Aspartate

proof_lines:
D-aspartate-oxidizing activity
human DDO
pig DAO

substrate: L-Aspartate


substrate_name: L-lysine

column_label: Table 1 columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1); row mature LysOX.

normalized_value_unit_evidence: Km 0.013 mM and kcat 65.5 s^-1 match the export; same-row central-value ratio 65.5/0.013 = 5038.461538461539 s^-1*mM^-1, while the table rounds kcat/Km to 5.0 x 10^3.

raw_value_unit_evidence: Table 1 row mature LysOX reports Km 1.3 x 10^-2 mM, kcat 65.5 s^-1, and kcat/Km 5.0 x 10^3 s^-1 mM^-1.

substrate: L-lysine


substrate_name: L-glutamate

assay_conditions_summary: pH 6

column_label: Abstract reports the apparent Km and Vmax values of SmlGOX were 9.3+/-0.5 mM and 159+/-3 U mg-1.

raw_value_unit_evidence: Km raw_value=9.3+/-0.5 mM raw_unit=mM

row_label: recombinant Streptomyces mobaraensis SmlGOX / L-glutamate

table_label: PubMed XML abstract PMID 28251390

substrate: L-glutamate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N145V with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.6; 298.15 K; buffer pH 10; cofactor NAD+

column_label: Table 2; row phenylpyruvate / N145V; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1); PDF page 4/8, article page 11393.

normalized_value_unit_evidence: Paper normalized required metrics: kcat=60.0 s^-1; Km=0.025 mM; kcat/Km=2400.0 s^-1 mM^-1. Exported required metrics: kcat=60.0 s^-1; Km=0.025 mM; kcat/Km=2400.0 s^-1 mM^-1.

row_label: phenylpyruvate / N145V

table_label: Table 2


column_label: Table 2; substrate row phenylpyruvate; enzyme row wt; metric columns Km, kcat, kcat/Km

normalized_value_unit_evidence: normalized: Km=0.37 mM; kcat=113 s^-1; kcat/Km=305 s^-1 mM^-1

row_label: Lysinibacillus sphaericus / wt / phenylpyruvate


enzyme_display_name: UniProt A0A161XU12

organism: Pseudoalteromonas luteoviolacea

substrate_name: glycine

source_db: skid

km_display: Not reported

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt A0A161XU12

substrate: glycine

source: skid


enzyme_display_name: UniProt O31616

organism: Bacillus subtilis

substrate_name: cyclopropylglycine

enzyme: UniProt O31616

substrate: cyclopropylglycine


enzyme_display_name: UniProt Q81HQ7

organism: Bacillus cereus

substrate_name: D-alanine

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

enzyme: UniProt Q81HQ7

substrate: D-alanine


substrate_name: D-proline

substrate: D-proline


proof_lines:
Raw SKiD Env: Temp=25°C, pH=9.5
Raw SKiD Env: Temp=25°C, pH=7
Raw SKiD Env: Temp=25°C, pH=7.5


substrate_name: glycine-ethyl-ester

smiles: CCOC(=O)CN

substrate: glycine-ethyl-ester


substrate_name: D-pipecolate

substrate: D-pipecolate


enzyme_display_name: UniProt P46883

organism: Escherichia coli

enzyme: UniProt P46883


enzyme_display_name: UniProt Q16853

organism: Homo sapiens

substrate_name: Isobutylamine

smiles: CC(C)CN

enzyme: UniProt Q16853

substrate: Isobutylamine


substrate_name: aminoacetone

smiles: CC(=O)CN

substrate: aminoacetone


substrate_name: Propylamine

smiles: CCCN

substrate: Propylamine


substrate_name: amylamine

smiles: CCCCCN

substrate: amylamine


substrate_name: Butylamine

smiles: CCCCN

substrate: Butylamine


substrate_name: ethylamine

smiles: CCN

substrate: ethylamine


substrate_name: dopamine

substrate: dopamine


substrate_name: cysteamine

smiles: C(CS)N

substrate: cysteamine


substrate_name: benzylamine

substrate: benzylamine


substrate_name: Isoamylamine

smiles: CC(C)CCN

substrate: Isoamylamine


substrate_name: cyclohexanemethylamine

substrate: cyclohexanemethylamine


enzyme_display_name: UniProt P12807

organism: Ogataea angusta

enzyme: UniProt P12807


enzyme_display_name: UniProt P46881

organism: Arthrobacter globiformis

enzyme: UniProt P46881


enzyme_display_name: UniProt Q43077

organism: Pisum sativum

smiles: C(C#CCN)N

enzyme: UniProt Q43077


organism: Rattus norvegicus

substrate_name: D-Asp

substrate: D-Asp


enzyme_display_name: L-aspartate oxidase

substrate_name: N-formyl-L-aspartate

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

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

enzyme: L-aspartate oxidase

substrate: N-formyl-L-aspartate


substrate_name: N-acetyl-L-aspartate

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

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

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

substrate: N-acetyl-L-aspartate


substrate_name: L-aspartate

substrate: L-aspartate


organism: Bacillus badius

substrate_name: L-Phenylalanine

column_label: Table 2; substrate row L-Phenylalanine; enzyme row B. badius; metric columns Km, kcat, kcat/Km

normalized_value_unit_evidence: normalized: Km=0.087 mM; kcat=39 s^-1; kcat/Km=448 s^-1 mM^-1

row_label: Bacillus badius / B. badius / L-Phenylalanine

substrate: L-Phenylalanine


organism: Sulfurisphaera tokodaii

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

smiles: O=O


organism: Thermococcus litoralis

substrate_name: L-Aspartate

substrate: L-Aspartate


enzyme_display_name: primary-amine oxidase

organism: Huperzia serrata

substrate_name: cadaverine

smiles: C(CCN)CCN

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tris-HCl

proof_lines: in 50 mM Tris-HCl buffer, pH 8.0, at 25°C

enzyme: primary-amine oxidase

substrate: cadaverine


substrate_name: histamine

substrate: histamine


substrate_name: putrescine

smiles: C(CCN)CN

substrate: putrescine


substrate_name: spermidine

smiles: C(CCNCCCN)CN

substrate: spermidine


enzyme_display_name: D-aspartate oxidase

substrate_name: D-Glutamate

assay_conditions_summary: pH 8.3; 310.15 K; cofactor FAD

column_label: PMID 31914658; PDF page 30; Supplementary Table 2; row D-Glu; columns kcat/app (s^-1); Km/app (mM); and kcat/app/Km/app (mM^-1 s^-1).

normalized_value_unit_evidence: kcat 11.3 s^-1; Km 31.5 mM; kcat/Km 0.36 s^-1 mM^-1; no unit conversion required.

raw_value_unit_evidence: Supplementary Table 2; D-Glu row: kcat/app 11.3 +/- 0.3 s^-1; Km/app 31.5 +/- 2.0 mM; kcat/app/Km/app 0.36 +/- 0.02 mM^-1 s^-1.

row_label: D-Glu

table_label: Supplementary Table 2. Comparison of apparent steady state parameters of hDASPO on different substrates

enzyme: D-aspartate oxidase

substrate: D-Glutamate


substrate_name: N-Methyl-D-aspartic acid

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

column_label: PMID 31914658; PDF page 30; Supplementary Table 2; row NMDA; columns kcat/app (s^-1); Km/app (mM); and kcat/app/Km/app (mM^-1 s^-1).

normalized_value_unit_evidence: kcat 73.6 s^-1; Km 2.76 mM; kcat/Km 26.7 s^-1 mM^-1; no unit conversion required.

raw_value_unit_evidence: Supplementary Table 2; NMDA row: kcat/app 73.6 +/- 1.3 s^-1; Km/app 2.76 +/- 0.12 mM; kcat/app/Km/app 26.7 +/- 0.8 mM^-1 s^-1.

row_label: NMDA

substrate: N-Methyl-D-aspartic acid


enzyme_display_name: glycine oxidase

organism: Marinomonas mediterranea

proof_lines: mutant enzyme F237A, at 30°C, pH not specified in the publication

enzyme: glycine oxidase


proof_lines: mutant enzyme F237Y, at 30°C, pH not specified in the publication


substrate_name: glycine

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

proof_lines: wild type enzyme, at 30°C, pH not specified in the publication

substrate: glycine


enzyme_display_name: diamine oxidase

organism: Lathyrus oleraceus

substrate_name: tyramine

enzyme: diamine oxidase

substrate: tyramine


substrate_name: O2; H2O; Benzylamine

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

substrate: O2; H2O; Benzylamine


organism: Nicotiana tabacum

substrate_name: O2; H2O; N-Methylputrescine

substrate: O2; H2O; N-Methylputrescine


organism: Paenarthrobacter aurescens


substrate_name: ethylamine

substrate: ethylamine


proof_lines: isoform HPAO-1, using benzylamine as cosubstrate, at 25°C, in 100 mM potassium phosphate, pH 7.2

proof_lines: isoform HPAO-2, using methylamine as cosubstrate, at 25°C, in 100 mM potassium phosphate, pH 7.2


substrate_name: benzylamine

proof_lines: in 100 mM potassium phosphate, pH 7.2, temperature not specified in the publication

proof_lines: isoform HPAO-1, at 25°C, in 100 mM potassium phosphate, pH 7.2

proof_lines: isoform HPAO-2, at 25°C, in 100 mM potassium phosphate, pH 7.2

substrate: benzylamine


organism: Pseudoalteromonas luteoviolacea


substrate_name: methylamine

smiles: CN

substrate: methylamine


organism: Onobrychis viciifolia

ki_unit: mM

smiles: C(CN)C#CCN


enzyme_display_name: L-lysine 6-oxidase

organism: Pseudoalteromonas tunicata

substrate_name: L-lysine

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

enzyme: L-lysine 6-oxidase

substrate: L-lysine


organism: Hyoscyamus niger

substrate_name: H2O; O2; N-Methylputrescine

substrate: H2O; O2; N-Methylputrescine


organism: Lathyrus cicera

substrate_name: H2O; O2; Tyramine

substrate: H2O; O2; Tyramine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:F2JXJ3 and applied mutation signature Y211F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM potassium phosphate

column_label: Table 2 (Steady-state kinetic parameters for LodA variants), enzyme row 'Y211F LodA'; column 'Normalized value of A400/A280' = 0.8; column 'kcat (s-1)' = 0.19 ± 0.02 (0.23); column 'Km lysine (uM)' = 129 ± 22; column 'Km O2 (uM)' = 522 ± 162; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.19 s-1; already in s^-1, no conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.19 s^(-1). Km: printed Table 2 cell 129 uM; 129 / 1000 = 0.129 mM; the paper value is 0.129 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 1.4728682170542635 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.19 / 0.129 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'Y211F LodA': kcat = 0.19 ± 0.02 (0.23) s-1; Km lysine = 129 ± 22 uM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'Y211F LodA'

table_label: Table 2: Steady-state kinetic parameters for LodA variants (Arch Biochem Biophys 2015, 579:26-32)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:F2JXJ3 and applied mutation signature C448D to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters for LodA variants), enzyme row 'C448D LodA'; column 'Normalized value of A400/A280' = 1.5; column 'kcat (s-1)' = 0.29 ± 0.03 (0.19); column 'Km lysine (uM)' = 142 ± 33; column 'Km O2 (uM)' = 386 ± 70; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.29 s-1; already in s^-1, no conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.29 s^(-1). Km: printed Table 2 cell 142 uM; 142 / 1000 = 0.142 mM; the paper value is 0.142 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 2.0422535211267605 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.29 / 0.142 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'C448D LodA': kcat = 0.29 ± 0.03 (0.19) s-1; Km lysine = 142 ± 33 uM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'C448D LodA'


column_label: Table 2 (Steady-state kinetic parameters for LodA variants), enzyme row 'WT LodA'; column 'Normalized value of A400/A280' = 1.0; column 'kcat (s-1)' = 0.34 ± 0.01; column 'Km lysine (uM)' = 3.9 ± 0.2; column 'Km O2 (uM)' = 199 ± 20; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.34 s-1; already in s^-1, no conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.34 s^(-1). Km: printed Table 2 cell 3.9 uM; 3.9 / 1000 = 0.0039 mM; the paper value is 0.0039 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 87.1794871794872 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.34 / 0.0039 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'WT LodA': kcat = 0.34 ± 0.01 s-1; Km lysine = 3.9 ± 0.2 uM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'WT LodA'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:F2JXJ3 and applied mutation signature C448A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters for LodA variants), enzyme row 'C448A LodA'; column 'Normalized value of A400/A280' = 1.0; column 'kcat (s-1)' = 0.39 ± 0.02; column 'Km lysine (uM)' = 48 ± 4; column 'Km O2 (uM)' = 543 ± 94; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.39 s-1; already in s^-1, no conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.39 s^(-1). Km: printed Table 2 cell 48 uM; 48 / 1000 = 0.048 mM; the paper value is 0.048 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 8.125 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.39 / 0.048 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'C448A LodA': kcat = 0.39 ± 0.02 s-1; Km lysine = 48 ± 4 uM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'C448A LodA'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:F2JXJ3 and applied mutation signature K530R to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters for LodA variants), enzyme row 'K530R LodA'; column 'Normalized value of A400/A280' = 0.3; column 'kcat (s-1)' = 0.68 ± 0.04 (2.3); column 'Km lysine (uM)' = 113 ± 13; column 'Km O2 (uM)' = 706 ± 95; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.68 s-1; already in s^-1, no conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.68 s^(-1). Km: printed Table 2 cell 113 uM; 113 / 1000 = 0.113 mM; the paper value is 0.113 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 6.017699115044248 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.68 / 0.113 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'K530R LodA': kcat = 0.68 ± 0.04 (2.3) s-1; Km lysine = 113 ± 13 uM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'K530R LodA'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:F2JXJ3 and applied mutation signature K530A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters for LodA variants), enzyme row 'K530A LodA'; column 'Normalized value of A400/A280' = 0.7; column 'kcat (s-1)' = 1.2 ± 0.1 (1.7); column 'Km lysine (uM)' = 52 ± 5; column 'Km O2 (uM)' = 1043 ± 102; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.2 s-1; already in s^-1, no conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 1.2 s^(-1). Km: printed Table 2 cell 52 uM; 52 / 1000 = 0.052 mM; the paper value is 0.052 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 23.076923076923077 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.2 / 0.052 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'K530A LodA': kcat = 1.2 ± 0.1 (1.7) s-1; Km lysine = 52 ± 5 uM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'K530A LodA'


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C448D with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y211F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C448A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K530R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K530A to reconstruct the assayed variant sequence.


proof_lines: pH and temperature not specified in the publication


enzyme_display_name: L-arginine oxidase

organism: Synechococcus elongatus

substrate_name: L-arginine

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

assay_conditions_summary: cofactor FAD

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

enzyme: L-arginine oxidase

substrate: L-arginine


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M211V/Y394N/L469G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; buffer Krebs Ringer phosphate glucose

proof_lines: mutant enzyme M211V/Y394N/L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T212A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T212A, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C


organism: Bacillus subtilis

substrate_name: D-Ala

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

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

assay_conditions_summary: pH 8; 310.15 K; buffer the corresponding kinetic values) at 50 mM potassium phosphate

proof_lines: kcat is 1.3 sec(-1) with glycine as substrate. kcat is 1.6 sec(-1) with sarcosine as substrate. kcat is 1.4 sec(-1) with N-ethylglycine as substrate. kcat is 1.3 sec(-1) with D-proline as substrate. kcat is 1.1 sec(-1) with D-alanine as sub

source_databases_merged: skid uniprot

substrate: D-Ala


assay_conditions_summary: pH 8; 298.15 K; buffer the corresponding kinetic values) at 50 mM potassium phosphate

proof_lines:
Raw SKiD Env: Temp=25°C, pH=6.5
Raw SKiD Env: Temp=25°C, pH=9.5
Raw SKiD Env: Temp=25°C, pH=7


substrate_name: sarcosine

smiles: CNCC(=O)O

proof_lines:
Raw SKiD Env: Temp=-----, pH=8.5
Raw SKiD Env: Temp=25°C, pH=8.5
Raw SKiD Env: Temp=37°C, pH=8.5

substrate: sarcosine


substrate_name: N-ethylglycine

smiles: CCNCC(=O)O

substrate: N-ethylglycine


substrate_name: D-proline

substrate: D-proline


enzyme_display_name: Glycine oxidase

organism: Bacillus licheniformis

proof_lines: kcat is 0.31 sec(-1) with glycine as substrate. kcat is 0.08 sec(-1) with glyphosate as substrate.

enzyme: Glycine oxidase


substrate_name: glyphosate

smiles: C(C(=O)O)NCP(=O)(O)O

substrate: glyphosate


organism: Bacillus cereus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D103Y/D121G/S122P/R238K/K367R/T368R to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7; 298.15 K; buffer 15 mM potassium phosphate

proof_lines: in 15 mM potassium phosphate buffer (pH 7.0), at 25°C


organism: Geobacillus kaustophilus (strain HTA426)

substrate_name: glycine (at pH 8.5 and 37 degrees Celsius)

proof_lines: Vmax with D-proline as substrate is 1.4-, 2.75-, 3.5- and 4.3-fold higher than with glycine, sarcosine, D-alanine, and N-ethylglycine, respectively.


substrate_name: sarcosine (at pH 8.5 and 37 degrees Celsius)


substrate_name: N-ethylglycine (at pH 8.5 and 37 degrees Celsius)


substrate_name: D-proline (at pH 8.5 and 37 degrees Celsius)


substrate_name: D-alanine (at pH 8.5 and 37 degrees Celsius)


substrate_name: glycine-ethyl ester (at pH 8.5 and 37 degrees Celsius)

smiles: CCOC(=O)CN


organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: Amine oxidase [copper-containing] zeta, peroxisomal

organism: Arabidopsis thaliana


organism: Bos taurus

substrate_name: Benzylamine; O2; H2O

substrate: Benzylamine; O2; H2O


enzyme_display_name: Amine oxidase [flavin-containing] A

enzyme: Amine oxidase [flavin-containing] A


organism: Lens culinaris


enzyme_display_name: N-methylputrescine oxidase 1, peroxisomal

organism: Nicotiana tabacum


substrate_name: O2; Glycine; H2O

column_label: Table 2. Comparison of the apparent kinetic parameters of wild-type and mutants of GO on different substrates; row Wild-type / Glycine; columns kcat,app (s^-1), Km,app (mM), kcat,app/Km,app (mM^-1 s^-1) under substrate column Glycine; cells Km,app 0.7+/-0.1 mM; kcat,app 0.60+/-0.03 s^-1; kcat,app/Km,app 0.86 mM^-1 s^-1.

normalized_value_unit_evidence: km normalized_value=0.7 normalized_unit=mM; kcat normalized_value=0.60 normalized_unit=s^-1; kcat_over_km normalized_value=0.86 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Wild-type / Glycine: Km,app 0.7+/-0.1 mM; kcat,app 0.60+/-0.03 s^-1; kcat,app/Km,app 0.86 mM^-1 s^-1.

row_label: Wild-type / Glycine

substrate: O2; Glycine; H2O


substrate_name: H2O; Glycine; O2

table_label: Table 2. Comparison of the apparent kinetic parameters of wild-type and mutants of GO on different substrates

substrate: H2O; Glycine; O2


enzyme_display_name: Amine oxidase [flavin-containing] B

enzyme: Amine oxidase [flavin-containing] B


substrate_name: H2O; O2; Methylamine

substrate: H2O; O2; Methylamine


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


organism: Pisum sativum

substrate_name: N-Methylputrescine; H2O; O2

smiles: CNCCCCN

substrate: N-Methylputrescine; H2O; O2


enzyme_display_name: Diamine oxidase [copper-containing] 1, peroxisomal


organism: Rattus norvegicus


substrate_name: D-Alanine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H244F with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

substrate: D-Alanine


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -13, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature H244Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M261H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M261Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H242F/H244F to reconstruct the assayed variant sequence.

column_label: Table 2. Comparison of the apparent kinetic parameters of wild-type and mutants of GO on different substrates; row Wild-type / D-Alanine; columns kcat,app (s^-1), Km,app (mM), kcat,app/Km,app (mM^-1 s^-1) under substrate column D-Alanine; cells Km,app 490+/-70 mM; kcat,app 0.92+/-0.08 s^-1; kcat,app/Km,app 0.002 mM^-1 s^-1.

normalized_value_unit_evidence: km normalized_value=490 normalized_unit=mM; kcat normalized_value=0.92 normalized_unit=s^-1; kcat_over_km normalized_value=0.002 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Wild-type / D-Alanine: Km,app 490+/-70 mM; kcat,app 0.92+/-0.08 s^-1; kcat,app/Km,app 0.002 mM^-1 s^-1.

row_label: Wild-type / D-Alanine


substrate_name: D-Proline

substrate: D-Proline


substrate_name: glycine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature A54E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 298.15 K; buffer 50 mM disodium pyrophosphate

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row A54E; under the Glycine group head: column 'kcat,app (s^-1)' = 0.35; column 'Km,app (mM)' = 10.0; column 'kcat,app/Km,app' = 0.04 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 0.35 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 0.35 s^(-1). Km: printed Table 2 glycine cell 10.0 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the catalog carries 10 mM. kcat/Km: printed Table 2 glycine cell 0.04 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 0.04 s^(-1)*mM^(-1), while the catalog carries 0.035 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row A54E: kcat,app = 0.35 s^-1; Km,app = 10.0 mM; printed kcat,app/Km,app = 0.04 mM^-1*s^-1.

row_label: Table 2, body row A54E, glycine cell group

table_label: Table 2: Comparison of the apparent kinetic parameters (determined at 21% oxygen saturation) on glycine or sarcosine as substrates for wild-type and variants of GO obtained by site-directed and site-saturation mutagenesis experiments (FEBS Journal 281 (2014) 3460-3472)

substrate: glycine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature A54R/H244K to reconstruct the assayed variant sequence.

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row A54R/H244K; under the Glycine group head: column 'kcat,app (s^-1)' = 3.20; column 'Km,app (mM)' = 40.1; column 'kcat,app/Km,app' = 0.11 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 3.20 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 3.2 s^(-1). Km: printed Table 2 glycine cell 40.1 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the catalog carries 40.1 mM. kcat/Km: printed Table 2 glycine cell 0.11 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 0.11 s^(-1)*mM^(-1), while the catalog carries 0.0798004988 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row A54R/H244K: kcat,app = 3.20 s^-1; Km,app = 40.1 mM; printed kcat,app/Km,app = 0.11 mM^-1*s^-1.

row_label: Table 2, body row A54R/H244K, glycine cell group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature A54R/H244K/M261R to reconstruct the assayed variant sequence.

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row A54R/H244K/M261R; under the Glycine group head: column 'kcat,app (s^-1)' = 1.61; column 'Km,app (mM)' = 45.9; column 'kcat,app/Km,app' = 0.04 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 1.61 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 1.61 s^(-1). Km: printed Table 2 glycine cell 45.9 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the catalog carries 45.9 mM. kcat/Km: printed Table 2 glycine cell 0.04 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 0.04 s^(-1)*mM^(-1), while the catalog carries 0.0350762527 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row A54R/H244K/M261R: kcat,app = 1.61 s^-1; Km,app = 45.9 mM; printed kcat,app/Km,app = 0.04 mM^-1*s^-1.

row_label: Table 2, body row A54R/H244K/M261R, glycine cell group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature G51H to reconstruct the assayed variant sequence.

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row G51H; under the Glycine group head: column 'kcat,app (s^-1)' = 0.77; column 'Km,app (mM)' = 35.7; column 'kcat,app/Km,app' = 0.02 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 0.77 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 0.77 s^(-1). Km: printed Table 2 glycine cell 35.7 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the catalog carries 35.7 mM. kcat/Km: printed Table 2 glycine cell 0.02 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 0.02 s^(-1)*mM^(-1), while the catalog carries 0.0215686275 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row G51H: kcat,app = 0.77 s^-1; Km,app = 35.7 mM; printed kcat,app/Km,app = 0.02 mM^-1*s^-1.

row_label: Table 2, body row G51H, glycine cell group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature G51Q to reconstruct the assayed variant sequence.

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row G51Q; under the Glycine group head: column 'kcat,app (s^-1)' = 0.74; column 'Km,app (mM)' = 14.6; column 'kcat,app/Km,app' = 0.05 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 0.74 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 0.74 s^(-1). Km: printed Table 2 glycine cell 14.6 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the catalog carries 14.6 mM. kcat/Km: printed Table 2 glycine cell 0.05 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 0.05 s^(-1)*mM^(-1), while the catalog carries 0.0506849315 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row G51Q: kcat,app = 0.74 s^-1; Km,app = 14.6 mM; printed kcat,app/Km,app = 0.05 mM^-1*s^-1.

row_label: Table 2, body row G51Q, glycine cell group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature H244K to reconstruct the assayed variant sequence.

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row H244K; under the Glycine group head: column 'kcat,app (s^-1)' = 1.35; column 'Km,app (mM)' = 0.14; column 'kcat,app/Km,app' = 9.65 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 1.35 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 1.35 s^(-1). Km: printed Table 2 glycine cell 0.14 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the catalog carries 0.14 mM. kcat/Km: printed Table 2 glycine cell 9.65 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 9.65 s^(-1)*mM^(-1), while the catalog carries 9.6428571429 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row H244K: kcat,app = 1.35 s^-1; Km,app = 0.14 mM; printed kcat,app/Km,app = 9.65 mM^-1*s^-1.

row_label: Table 2, body row H244K, glycine cell group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature H244K/M261R to reconstruct the assayed variant sequence.

column_label: Table 2 row H244K/M261R; glycine; glycine/sarcosine columns give kcat,app 1.20 s^-1, Km,app 0.30 mM, and kcat,app/Km,app 4.00 mM^-1*s^-1.

normalized_value_unit_evidence: kcat normalized_value=1.20 normalized_unit=s^-1; Km normalized_value=0.30 normalized_unit=mM; kcat/Km normalized_value=4.00 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat,app raw_value=1.20 raw_unit=s^-1; Km,app raw_value=0.30 raw_unit=mM; kcat,app/Km,app raw_value=4.00 raw_unit=mM^-1*s^-1

row_label: H244K/M261R; glycine

table_label: Table 2. Apparent kinetic parameters on glycine or sarcosine for wild-type and variants of GO


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature H244N to reconstruct the assayed variant sequence.

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row H244N; under the Glycine group head: column 'kcat,app (s^-1)' = 1.30; column 'Km,app (mM)' = 1.90; column 'kcat,app/Km,app' = 0.68 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 1.30 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 1.3 s^(-1). Km: printed Table 2 glycine cell 1.90 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the catalog carries 1.9 mM. kcat/Km: printed Table 2 glycine cell 0.68 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 0.68 s^(-1)*mM^(-1), while the catalog carries 0.6842105263 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row H244N: kcat,app = 1.30 s^-1; Km,app = 1.90 mM; printed kcat,app/Km,app = 0.68 mM^-1*s^-1.

row_label: Table 2, body row H244N, glycine cell group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature H244Q to reconstruct the assayed variant sequence.

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row H244Q; under the Glycine group head: column 'kcat,app (s^-1)' = 1.21; column 'Km,app (mM)' = 0.90; column 'kcat,app/Km,app' = 1.34 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 1.21 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 1.21 s^(-1). Km: printed Table 2 glycine cell 0.90 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the printed cell stands at 0.9 mM, while the catalog carries 0.8 mM for this metric. kcat/Km: printed Table 2 glycine cell 1.34 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 1.34 s^(-1)*mM^(-1), while the catalog carries 1.5125 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row H244Q: kcat,app = 1.21 s^-1; Km,app = 0.90 mM; printed kcat,app/Km,app = 1.34 mM^-1*s^-1.

row_label: Table 2, body row H244Q, glycine cell group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature H244R to reconstruct the assayed variant sequence.

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row H244R; under the Glycine group head: column 'kcat,app (s^-1)' = 1.49; column 'Km,app (mM)' = 0.24; column 'kcat,app/Km,app' = 6.22 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 1.49 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 1.49 s^(-1). Km: printed Table 2 glycine cell 0.24 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the catalog carries 0.24 mM. kcat/Km: printed Table 2 glycine cell 6.22 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 6.22 s^(-1)*mM^(-1), while the catalog carries 6.2083333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row H244R: kcat,app = 1.49 s^-1; Km,app = 0.24 mM; printed kcat,app/Km,app = 6.22 mM^-1*s^-1.

row_label: Table 2, body row H244R, glycine cell group


organism: Huperzia serrata

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

column_label: Table 1 row 8 substrate 2-aminoethylpyridine, columns KM (mM)=1.7, Kcat (s^-1)=2.9, Kcat/KM (s^-1 mM^-1)=1.7

normalized_value_unit_evidence: KM normalized_value=1.7 normalized_unit=mM; Kcat normalized_value=2.9 normalized_unit=s^(-1); Kcat/KM normalized_value=1.7 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Table 1 row 2-aminoethylpyridine: KM 1.7 mM; Kcat 2.9 s^-1; Kcat/KM 1.7 s^-1 mM^-1

row_label: 2-aminoethylpyridine (official substrate-label image pmid22901898_table1_fx9.jpg)

table_label: Table 1. Steady-state kinetic parameters of recombinant HsCAO


column_label: Table 1 row 7 substrate 3-aminomethylpyridine, columns KM (mM)=1.2, Kcat (s^-1)=1.9, Kcat/KM (s^-1 mM^-1)=1.6

normalized_value_unit_evidence: KM normalized_value=1.2 normalized_unit=mM; Kcat normalized_value=1.9 normalized_unit=s^(-1); Kcat/KM normalized_value=1.6 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Table 1 row 3-aminomethylpyridine: KM 1.2 mM; Kcat 1.9 s^-1; Kcat/KM 1.6 s^-1 mM^-1

row_label: 3-aminomethylpyridine (official substrate-label image pmid22901898_table1_fx8.jpg)


column_label: Table 1 row 6 substrate 4-aminomethylpyridine, columns KM (mM)=1.9, Kcat (s^-1)=3.1, Kcat/KM (s^-1 mM^-1)=1.6

normalized_value_unit_evidence: KM normalized_value=1.9 normalized_unit=mM; Kcat normalized_value=3.1 normalized_unit=s^(-1); Kcat/KM normalized_value=1.6 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Table 1 row 4-aminomethylpyridine: KM 1.9 mM; Kcat 3.1 s^-1; Kcat/KM 1.6 s^-1 mM^-1

row_label: 4-aminomethylpyridine (official substrate-label image pmid22901898_table1_fx7.jpg)


substrate_name: benzylamine

column_label: Table 1 row 5 substrate benzylamine, columns KM (mM)=0.5, Kcat (s^-1)=1.4, Kcat/KM (s^-1 mM^-1)=2.8

normalized_value_unit_evidence: KM normalized_value=0.5 normalized_unit=mM; Kcat normalized_value=1.4 normalized_unit=s^(-1); Kcat/KM normalized_value=2.8 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Table 1 row benzylamine: KM 0.5 mM; Kcat 1.4 s^-1; Kcat/KM 2.8 s^-1 mM^-1

row_label: benzylamine (official substrate-label image pmid22901898_table1_fx6.jpg)

substrate: benzylamine


substrate_name: cadaverine

smiles: NCCCCCN

column_label: Table 1 row 1 substrate cadaverine, columns KM (mM)=0.3, Kcat (s^-1)=1.0, Kcat/KM (s^-1 mM^-1)=3.3

normalized_value_unit_evidence: KM normalized_value=0.3 normalized_unit=mM; Kcat normalized_value=1.0 normalized_unit=s^(-1); Kcat/KM normalized_value=3.3 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Table 1 row cadaverine: KM 0.3 mM; Kcat 1.0 s^-1; Kcat/KM 3.3 s^-1 mM^-1

row_label: cadaverine (official substrate-label image pmid22901898_table1_fx2.jpg)

substrate: cadaverine


substrate_name: histamine

column_label: Table 1 row 4 substrate histamine, columns KM (mM)=0.7, Kcat (s^-1)=1.8, Kcat/KM (s^-1 mM^-1)=2.6

normalized_value_unit_evidence: KM normalized_value=0.7 normalized_unit=mM; Kcat normalized_value=1.8 normalized_unit=s^(-1); Kcat/KM normalized_value=2.6 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Table 1 row histamine: KM 0.7 mM; Kcat 1.8 s^-1; Kcat/KM 2.6 s^-1 mM^-1

row_label: histamine (official substrate-label image pmid22901898_table1_fx5.jpg)

substrate: histamine


substrate_name: putrescine

smiles: NCCCCN

column_label: Table 1 row 2 substrate putrescine, columns KM (mM)=1.2, Kcat (s^-1)=1.9, Kcat/KM (s^-1 mM^-1)=1.6

raw_value_unit_evidence: Table 1 row putrescine: KM 1.2 mM; Kcat 1.9 s^-1; Kcat/KM 1.6 s^-1 mM^-1

row_label: putrescine (official substrate-label image pmid22901898_table1_fx3.jpg)

substrate: putrescine


substrate_name: spermidine

smiles: NCCCCNCCCN

column_label: Table 1 row 3 substrate spermidine, columns KM (mM)=0.8, Kcat (s^-1)=2.3, Kcat/KM (s^-1 mM^-1)=2.9

normalized_value_unit_evidence: KM normalized_value=0.8 normalized_unit=mM; Kcat normalized_value=2.3 normalized_unit=s^(-1); Kcat/KM normalized_value=2.9 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: Table 1 row spermidine: KM 0.8 mM; Kcat 2.3 s^-1; Kcat/KM 2.9 s^-1 mM^-1

row_label: spermidine (official substrate-label image pmid22901898_table1_fx4.jpg)

substrate: spermidine


organism: Aspergillus niger

substrate_name: propylamine

smiles: CCCN

substrate: propylamine


substrate_name: butylamine

smiles: CCCCN

substrate: butylamine


substrate_name: aminoacetone

smiles: CC(=O)CN

column_label: Table 2. Human AOC3 substrate kinetic profile; row Aminoacetone; columns kcat(s^-1), Km(uM), kcat/Km(M^-1 s^-1); kcat 1.46 +/- 0.10 s^-1; Km 66 +/- 18 uM; kcat/Km 2.23 +/- 0.28 x 10^4 M^-1 s^-1; normalized kcat 1.46 s^-1; Km 0.066 mM; kcat/Km 22.3 s^-1*mM^-1

row_label: Aminoacetone

substrate: aminoacetone


substrate_name: amylamine

smiles: CCCCCN

column_label: Table 2. Human AOC3 substrate kinetic profile; row Amylamine; columns kcat(s^-1), Km(uM), kcat/Km(M^-1 s^-1); kcat 4.33 +/- 0.19 s^-1; Km 5710 +/- 760 uM; kcat/Km 7.57 +/- 0.14 x 10^2 M^-1 s^-1; normalized kcat 4.33 s^-1; Km 5.71 mM; kcat/Km 0.757 s^-1*mM^-1

row_label: Amylamine

substrate: amylamine


column_label: Table 2. Human AOC3 substrate kinetic profile; row Benzylamine; columns kcat(s^-1), Km(uM), kcat/Km(M^-1 s^-1); kcat 3.42 +/- 0.10 s^-1; Km 84.5 +/- 9.8 uM; kcat/Km 4.05 +/- 0.12 x 10^4 M^-1 s^-1; normalized kcat 3.42 s^-1; Km 0.0845 mM; kcat/Km 40.5 s^-1*mM^-1

row_label: Benzylamine


substrate_name: Butylamine

column_label: Table 2. Human AOC3 substrate kinetic profile; row Butylamine

normalized_value_unit_evidence: Per-metric normalized values and units are preserved in paper_metric_evidence.

raw_value_unit_evidence: Per-metric raw values and units are preserved in paper_metric_evidence; captured_primary_segment preserves the exact source transcription.

row_label: Butylamine

substrate: Butylamine


substrate_name: cyclohexanemethylamine

column_label: Table 2. Human AOC3 substrate kinetic profile; row Cyclohexanemethylamine; columns kcat(s^-1), Km(uM), kcat/Km(M^-1 s^-1); kcat 5.36 +/- 0.77 s^-1; Km 16500 +/- 5200 uM; kcat/Km 3.25 +/- 0.35 x 10^2 M^-1 s^-1; normalized kcat 5.36 s^-1; Km 16.5 mM; kcat/Km 0.325 s^-1*mM^-1

row_label: Cyclohexanemethylamine

substrate: cyclohexanemethylamine


substrate_name: cysteamine

smiles: NCCS

column_label: Table 2. Human AOC3 substrate kinetic profile; row Cysteamine; columns kcat(s^-1), Km(uM), kcat/Km(M^-1 s^-1); kcat 1.11 +/- 0.14 s^-1; Km 31 +/- 15 uM; kcat/Km 3.55 +/- 0.50 x 10^4 M^-1 s^-1; normalized kcat 1.11 s^-1; Km 0.031 mM; kcat/Km 35.5 s^-1*mM^-1

row_label: Cysteamine

substrate: cysteamine


substrate_name: dopamine

column_label: Table 2. Human AOC3 substrate kinetic profile; row Dopamine

row_label: Dopamine

substrate: dopamine


substrate_name: ethylamine

smiles: CCN

column_label: Table 2. Human AOC3 substrate kinetic profile; row Ethylamine; columns kcat(s^-1), Km(uM), kcat/Km(M^-1 s^-1); kcat 6.12 +/- 0.40 s^-1; Km 12800 +/- 1960 uM; kcat/Km 4.78 +/- 0.17 x 10^2 M^-1 s^-1; normalized kcat 6.12 s^-1; Km 12.8 mM; kcat/Km 0.478 s^-1*mM^-1

row_label: Ethylamine

substrate: ethylamine


substrate_name: Isoamylamine

smiles: CC(C)CCN

column_label: Table 2. Human AOC3 substrate kinetic profile; row Isoamylamine

row_label: Isoamylamine

substrate: Isoamylamine


substrate_name: Isobutylamine

smiles: CC(C)CN

column_label: Table 2. Human AOC3 substrate kinetic profile; row Isobutylamine

row_label: Isobutylamine

substrate: Isobutylamine


substrate_name: (R)-adrenaline

column_label: Km

normalized_value_unit_evidence: normalized: km=0.84 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-B Adrenaline Km=840 uM; Vmax=531 pmol/mg protein/min

row_label: MAO-B / Adrenaline

table_label: Table 3

substrate: (R)-adrenaline


normalized_value_unit_evidence: normalized: km=0.29 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-B Dopamine Km=290 uM; Vmax=396 pmol/mg protein/min

row_label: MAO-B / Dopamine


substrate_name: serotonin

normalized_value_unit_evidence: normalized: km=0.533 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-B 5-hydroxytryptamine Km=533 uM; Vmax=125 pmol/mg protein/min

row_label: MAO-B / 5-hydroxytryptamine

substrate: serotonin


substrate_name: (R)-noradrenaline

normalized_value_unit_evidence: normalized: km=1.954 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-B Noradrenaline Km=1954 uM; Vmax=383 pmol/mg protein/min

row_label: MAO-B / Noradrenaline

substrate: (R)-noradrenaline


normalized_value_unit_evidence: normalized: km=0.005 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-B 2-phenethylamine Km=5 uM; Vmax=489 pmol/mg protein/min

row_label: MAO-B / 2-phenethylamine


substrate_name: tyramine

normalized_value_unit_evidence: normalized: km=0.328 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-B Tyramine Km=328 uM; Vmax=687 pmol/mg protein/min

row_label: MAO-B / Tyramine

substrate: tyramine


normalized_value_unit_evidence: normalized: km=0.61 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-A Adrenaline Km=610 uM; Vmax=558 pmol/mg protein/min

row_label: MAO-A / Adrenaline


normalized_value_unit_evidence: normalized: km=0.15 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-A Dopamine Km=150 uM; Vmax=889 pmol/mg protein/min

row_label: MAO-A / Dopamine


column_label: Table 3. Kinetic parameters of the two forms of MAO; row 5-Hydroxytryptamine; rat brain MAO-A; Km column 340 uM normalized to 0.34 mM; Vmax column 997 pmol mg protein^-1 min^-1

normalized_value_unit_evidence: km 0.34 mM

raw_value_unit_evidence: Km 340 uM; Vmax 997 pmol mg protein^-1 min^-1

row_label: rat brain MAO-A / 5-Hydroxytryptamine


normalized_value_unit_evidence: normalized: km=0.582 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-A Noradrenaline Km=582 uM; Vmax=1213 pmol/mg protein/min

row_label: MAO-A / Noradrenaline


substrate_name: D-Proline

substrate: D-Proline


substrate_name: sarcosine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature H244F to reconstruct the assayed variant sequence.

column_label: Table 4: Specific rate constants obtained in stopped-flow experiments for the reductive half-reaction and steady-state parameters of wild-type and mutants of GO with glycine and sarcosine as substrate; printed steady-state column heads Lineweaver-Burk pattern, kcat (s^-1), KM,S (mM^-1) and KM,O2 (mM); journal page 1379; enzyme block H244F, substrate row Sarcosine; column kcat (s^-1) = 5.5; column KM,S (mM^-1) = 8.4; Table 4 prints no catalytic-efficiency column. captured primary segment: H244F GO mutant | sarcosine | Table 4, journal page 1379, PDF page 8 | 75 mM disodium pyrophosphate buffer, pH 8.5, at 25 C | Table 4 kcat cell 5.5 s^-1 | Table 4 KM,S cell 8.4 mM, printed under the column head KM,S (mM^-1) | Table 4 prints no kcat/Km column for this row

normalized_value_unit_evidence: kcat: printed Table 4 cell 5.5 s^-1; the printed turnover column is already per second, so no unit conversion applies and the canonical value is 5.5 s^(-1). Km: printed Table 4 cell 8.4; the printed column head KM,S carries a reciprocal exponent, while a Michaelis constant is a concentration, the neighbouring Table 4 column KM,O2 prints (mM) and Table 2 prints the substrate Michaelis constant as Km,app (mM), so the cell is read as 8.4 mM and no unit conversion applies. kcat/Km: Table 4 prints no catalytic-efficiency column, so the ratio is the arithmetic quotient of the two printed cells of this one measurement: 5.5 / 8.4 = 0.6547619047619048 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, journal page 1379, enzyme block H244F, substrate row Sarcosine, steady-state parameters: kcat = 5.5 s^-1 under the printed column head kcat (s^-1); KM,S = 8.4 under the printed column head KM,S (mM^-1); Table 4 prints no catalytic-efficiency column.

row_label: Table 4, enzyme block H244F, substrate row Sarcosine, steady-state parameters

substrate: sarcosine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H244N with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H244Q with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M261H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M261Y to reconstruct the assayed variant sequence.


substrate_name: glycine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H244F with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

substrate: glycine


enzyme_display_name: UniProt Q16853

substrate_name: methylamine

smiles: CN

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

substrate: methylamine


substrate_name: phenethylamine

substrate: phenethylamine


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

column_label: Table 2, row CHO transfectants / AOC3 / 2-Phenylethylamine; Km column cell 1,940 +/- 260 uM, normalized 1.94 mM.

normalized_value_unit_evidence: Km 1.94 mM

table_label: Table 2. Kinetic constants for AOC2, AOC3 and the AOC3 triple mutant M211V-Y394N-L469G


row_label: CHO transfectants / AOC3 / 2-Phenylethylamine


enzyme_display_name: Amine oxidase [copper-containing] 2

substrate_name: tryptamine

column_label: Table 2, row CHO transfectants / AOC2 / Tryptamine; Km column cell 56 +/- 34 uM, normalized 0.056 mM.

raw_value_unit_evidence: Km raw 56 +/- 34 uM

row_label: CHO transfectants / AOC2 / Tryptamine

enzyme: Amine oxidase [copper-containing] 2

substrate: tryptamine


column_label: Table 2, row CHO transfectants / AOC2 / 2-Phenylethylamine; Km column cell 77 +/- 15 uM, normalized 0.077 mM.

raw_value_unit_evidence: Km raw 77 +/- 15 uM


substrate_name: benzylamine

column_label: Table 2, row CHO transfectants / AOC2 / Benzylamine; Km column cell 167 +/- 132 uM, normalized 0.167 mM.

row_label: CHO transfectants / AOC2 / Benzylamine

substrate: benzylamine


substrate_name: p-tyramine

column_label: Table 2, row CHO transfectants / AOC2 / p-Tyramine; Km column cell 178 +/- 51 uM, normalized 0.178 mM.

row_label: CHO transfectants / AOC2 / p-Tyramine

substrate: p-tyramine


column_label: Table 2, row CHO transfectants / AOC2 / Methylamine; Km column cell 1,700 +/- 710 uM, normalized 1.7 mM.

normalized_value_unit_evidence: Km 1.7 mM

row_label: CHO transfectants / AOC2 / Methylamine


substrate_name: putrescine

smiles: C(CCN)CN

enzyme: Diamine oxidase [copper-containing] 1, peroxisomal

substrate: putrescine


substrate_name: N-methylputrescine

substrate: N-methylputrescine


substrate_name: cadaverine

smiles: C(CCN)CCN

substrate: cadaverine


proof_lines:
MPO1
N-methylputrescine
symmetrical diamines

enzyme: N-methylputrescine oxidase 1, peroxisomal


column_label: Table 2. Human AOC3 substrate kinetic profile; row Phenethylamine; columns kcat(s^-1), Km(uM), kcat/Km(M^-1 s^-1); kcat 1.12 +/- 0.08 s^-1; Km 2050 +/- 620 uM; kcat/Km 5.45 +/- 0.31 x 10^2 M^-1 s^-1; normalized kcat 1.12 s^-1; Km 2.05 mM; kcat/Km 0.545 s^-1*mM^-1

row_label: Phenethylamine


substrate_name: Propylamine

column_label: Table 2. Human AOC3 substrate kinetic profile; row Propylamine

row_label: Propylamine

substrate: Propylamine


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

column_label: Table 1 Kinetic parameters of Pseudomonas putida ThiO (GOPP) for various substrates; row Glycine; Km (mM) column.

raw_value_unit_evidence: Table 1 row Glycine: Km 2.43 mM.

row_label: Glycine

table_label: Table 1. Kinetic parameters of Pseudomonas putida ThiO (GOPP) for various substrates


smiles: CNCC(=O)O

column_label: Table 1 Kinetic parameters of Pseudomonas putida ThiO (GOPP) for various substrates; row Sarcosine; Km (mM) column.

raw_value_unit_evidence: Table 1 row Sarcosine: Km 4.86 mM.

row_label: Sarcosine


substrate_name: D-proline

column_label: Table 1 Kinetic parameters of Pseudomonas putida ThiO (GOPP) for various substrates; row d-Proline; Km (mM) column.

raw_value_unit_evidence: Table 1 row d-Proline: Km 31.7 mM.

row_label: d-Proline

substrate: D-proline


substrate_name: N-ethylglycine

smiles: CCNCC(=O)O

column_label: Table 1 Kinetic parameters of Pseudomonas putida ThiO (GOPP) for various substrates; row N-Ethylglycine; Km (mM) column.

raw_value_unit_evidence: Table 1 row N-Ethylglycine: Km 7.68 mM.

row_label: N-Ethylglycine

substrate: N-ethylglycine


smiles: O=O


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature M261I to reconstruct the assayed variant sequence.

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row M261I; under the Glycine group head: column 'kcat,app (s^-1)' = 0.64; column 'Km,app (mM)' = 1.50; column 'kcat,app/Km,app' = 0.43 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 0.64 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 0.64 s^(-1). Km: printed Table 2 glycine cell 1.50 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the catalog carries 1.5 mM. kcat/Km: printed Table 2 glycine cell 0.43 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 0.43 s^(-1)*mM^(-1), while the catalog carries 0.4266666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row M261I: kcat,app = 0.64 s^-1; Km,app = 1.50 mM; printed kcat,app/Km,app = 0.43 mM^-1*s^-1.

row_label: Table 2, body row M261I, glycine cell group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature M261R to reconstruct the assayed variant sequence.

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row M261R; under the Glycine group head: column 'kcat,app (s^-1)' = 1.00; column 'Km,app (mM)' = 3.50; column 'kcat,app/Km,app' = 0.30 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 1.00 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 1 s^(-1). Km: printed Table 2 glycine cell 3.50 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the catalog carries 3.5 mM. kcat/Km: printed Table 2 glycine cell 0.30 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 0.3 s^(-1)*mM^(-1), while the catalog carries 0.2857142857 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row M261R: kcat,app = 1.00 s^-1; Km,app = 3.50 mM; printed kcat,app/Km,app = 0.30 mM^-1*s^-1.

row_label: Table 2, body row M261R, glycine cell group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature M49I to reconstruct the assayed variant sequence.

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row M49I; under the Glycine group head: column 'kcat,app (s^-1)' = 0.36; column 'Km,app (mM)' = 0.31; column 'kcat,app/Km,app' = 1.17 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 0.36 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 0.36 s^(-1). Km: printed Table 2 glycine cell 0.31 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the catalog carries 0.31 mM. kcat/Km: printed Table 2 glycine cell 1.17 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 1.17 s^(-1)*mM^(-1), while the catalog carries 1.1612903226 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row M49I: kcat,app = 0.36 s^-1; Km,app = 0.31 mM; printed kcat,app/Km,app = 1.17 mM^-1*s^-1.

row_label: Table 2, body row M49I, glycine cell group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature M49L to reconstruct the assayed variant sequence.

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row M49L; under the Glycine group head: column 'kcat,app (s^-1)' = 0.43; column 'Km,app (mM)' = 1.35; column 'kcat,app/Km,app' = 0.32 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 0.43 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 0.43 s^(-1). Km: printed Table 2 glycine cell 1.35 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the catalog carries 1.35 mM. kcat/Km: printed Table 2 glycine cell 0.32 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 0.32 s^(-1)*mM^(-1), while the catalog carries 0.3185185185 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row M49L: kcat,app = 0.43 s^-1; Km,app = 1.35 mM; printed kcat,app/Km,app = 0.32 mM^-1*s^-1.

row_label: Table 2, body row M49L, glycine cell group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature M49L/A54R/H244K to reconstruct the assayed variant sequence.

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row M49L/A54R/H244K; under the Glycine group head: column 'kcat,app (s^-1)' = 0.6; column 'Km,app (mM)' = 18.8; column 'kcat,app/Km,app' = 0.03 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 0.6 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 0.6 s^(-1). Km: printed Table 2 glycine cell 18.8 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the catalog carries 18.8 mM. kcat/Km: printed Table 2 glycine cell 0.03 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 0.03 s^(-1)*mM^(-1), while the catalog carries 0.0319148936 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row M49L/A54R/H244K: kcat,app = 0.6 s^-1; Km,app = 18.8 mM; printed kcat,app/Km,app = 0.03 mM^-1*s^-1.

row_label: Table 2, body row M49L/A54R/H244K, glycine cell group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature M49T to reconstruct the assayed variant sequence.

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row M49T; under the Glycine group head: column 'kcat,app (s^-1)' = 0.04; column 'Km,app (mM)' = 1.47; column 'kcat,app/Km,app' = 0.03 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 0.04 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 0.04 s^(-1). Km: printed Table 2 glycine cell 1.47 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the catalog carries 1.47 mM. kcat/Km: printed Table 2 glycine cell 0.03 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 0.03 s^(-1)*mM^(-1), while the catalog carries 0.0272108844 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row M49T: kcat,app = 0.04 s^-1; Km,app = 1.47 mM; printed kcat,app/Km,app = 0.03 mM^-1*s^-1.

row_label: Table 2, body row M49T, glycine cell group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature Y246W to reconstruct the assayed variant sequence.

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row Y246W; under the Glycine group head: column 'kcat,app (s^-1)' = 1.21; column 'Km,app (mM)' = 17.2; column 'kcat,app/Km,app' = 0.07 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 1.21 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 1.21 s^(-1). Km: printed Table 2 glycine cell 17.2 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the catalog carries 17.2 mM. kcat/Km: printed Table 2 glycine cell 0.07 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 0.07 s^(-1)*mM^(-1), while the catalog carries 0.0703488372 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row Y246W: kcat,app = 1.21 s^-1; Km,app = 17.2 mM; printed kcat,app/Km,app = 0.07 mM^-1*s^-1.

row_label: Table 2, body row Y246W, glycine cell group


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A54R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H244A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


substrate_name: (R)-adrenaline

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

column_label: Km

normalized_value_unit_evidence: normalized: km=0.208 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 2 cells: MAO-A Adrenaline Km=208 uM; Vmax=379 pmol/mg protein/min

row_label: MAO-A / Adrenaline

substrate: (R)-adrenaline


substrate_name: dopamine

normalized_value_unit_evidence: normalized: km=0.212 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 2 cells: MAO-A Dopamine Km=212 uM; Vmax=680 pmol/mg protein/min

row_label: MAO-A / Dopamine

substrate: dopamine


substrate_name: serotonin

column_label: Table 2. Kinetic parameters of the two forms of MAO; row 5-Hydroxytryptamine; human cerebral cortex MAO-A; Km column 137 uM normalized to 0.137 mM; Vmax column 228 pmol mg protein^-1 min^-1

raw_value_unit_evidence: Km 137 uM; Vmax 228 pmol mg protein^-1 min^-1

row_label: human cerebral cortex MAO-A / 5-Hydroxytryptamine

substrate: serotonin


substrate_name: (R)-noradrenaline

normalized_value_unit_evidence: normalized: km=0.284 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 2 cells: MAO-A Noradrenaline Km=284 uM; Vmax=561 pmol/mg protein/min

row_label: MAO-A / Noradrenaline

substrate: (R)-noradrenaline


normalized_value_unit_evidence: normalized: km=0.14 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 2 cells: MAO-A 2-phenethylamine Km=140 uM; Vmax=20 pmol/mg protein/min

row_label: MAO-A / 2-phenethylamine