column_label: Table 3. Kinetics data for cyclic imine substrates 1-7; row 7a (R = Me); columns kcat, Km, kcat/Km.

raw_value_unit_evidence: Table 3 row 7a (R = Me) reports Vmax 0.340; kcat 0.189 s^-1; Km 0.155 mM; kcat/Km 1.22 s^-1 mM^-1.

row_label: Table 3 row 7a (R = Me); 1-methyl-3,4-dihydroisoquinoline


enzyme_display_name: 2-methyl-1-pyrroline reductase

organism: Streptomyces sp. GF3587

source_db: brenda

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

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.

assay_conditions_summary: cofactor NADPH

column_label: Table 3. Kinetics data for cyclic imine substrates 1-7; row 5c (R = p-MeOPh); columns kcat, Km, kcat/Km.

raw_value_unit_evidence: Table 3 row 5c (R = p-MeOPh) reports Vmax 0.474; kcat 0.263 s^-1; Km 1.05 mM; kcat/Km 0.250 s^-1 mM^-1.

row_label: Table 3 row 5c (R = p-MeOPh); 6-(4-methoxyphenyl)-2,3,4,5-tetrahydropyridine

data_origin: experimental

enzyme: 2-methyl-1-pyrroline reductase

status: verified

source: brenda


column_label: Table 3. Kinetics data for cyclic imine substrates 1-7; row 1a (R = Me); columns kcat, Km, kcat/Km.

raw_value_unit_evidence: Table 3 row 1a (R = Me) reports Vmax 0.633; kcat 0.351 s^-1; Km 1.88 mM; kcat/Km 0.187 s^-1 mM^-1.

row_label: Table 3 row 1a (R = Me); 2-methyl-1-pyrroline


column_label: Table 3. Kinetics data for cyclic imine substrates 1-7; row 9 (R = H); columns kcat, Km, kcat/Km.

raw_value_unit_evidence: Table 3 row 9 (R = H) reports Vmax 1.905; kcat 1.057 s^-1; Km 0.481 mM; kcat/Km 2.195 s^-1 mM^-1.

row_label: Table 3 row 9 (R = H); 2-methyl-3,4-dihydroisoquinolin-2-ium


verification_status: unverified

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

status: unverified


column_label: Table 3. Kinetics data for cyclic imine substrates 1-7; row 5a (R = Me); columns kcat, Km, kcat/Km.

raw_value_unit_evidence: Table 3 row 5a (R = Me) reports Vmax 7.60; kcat 4.21 s^-1; Km 0.371 mM; kcat/Km 11.4 s^-1 mM^-1.

row_label: Table 3 row 5a (R = Me); 6-methyl-2,3,4,5-tetrahydropyridine


column_label: Table 3. Kinetics data for cyclic imine substrates 1-7; row 5i (R = n-propyl); columns kcat, Km, kcat/Km.

raw_value_unit_evidence: Table 3 row 5i (R = n-propyl) reports Vmax 8.35; kcat 4.63 s^-1; Km 0.804 mM; kcat/Km 5.76 s^-1 mM^-1.

row_label: Table 3 row 5i (R = n-propyl); 6-propyl-2,3,4,5-tetrahydropyridine


organism: Saccharomyces cerevisiae

kcat_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

assay_conditions_summary: pH 7.2; cofactor NADPH

proof_lines: wild-type, cosubstrate NADPH, pH 7.2, temperature not specified in the publication


substrate_name: NADPH

proof_lines: wild-type, pH 7.2, temperature not specified in the publication

substrate: NADPH


proof_lines: Chimera-1, cosubstrate NADPH, pH 7.2, temperature not specified in the publication

proof_lines: Chimera-1, cosubstrate NADH, pH 7.2, temperature not specified in the publication


enzyme_display_name: staphylopine dehydrogenase

organism: Staphylococcus aureus

substrate_name: glyoxylate

verification_status: corrected

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

sequence_source: multiple

assay_conditions_summary: pH 8; 295.15 K; buffer 50 mM Tris pH 8; cofactor NADPH

column_label: Table 1 row SaODH Glyoxylate NADPH d-HisNA; columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 1 row SaODH Glyoxylate NADPH d-HisNA: kcat=0.074 +/- 0.003 s^-1; Km=3000 +/- 200 uM; kcat/Km=24 +/- 2 M^-1 s^-1.

row_label: SaODH / Glyoxylate / NADPH / d-HisNA

table_label: Table 1

source_databases_merged: brenda skid uniprot

enzyme: staphylopine dehydrogenase

substrate: glyoxylate

status: corrected


substrate_name: pyruvate

column_label: Table 1 row SaODH Pyruvate NADPH d-HisNA; columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 1 row SaODH Pyruvate NADPH d-HisNA: kcat=0.26 +/- 0.01 s^-1; Km=29 +/- 2 uM; kcat/Km=8900 +/- 700 M^-1 s^-1.

row_label: SaODH / Pyruvate / NADPH / d-HisNA

substrate: pyruvate


substrate_name: oxaloacetate

column_label: Table 1 row SaODH Oxaloacetate NADPH d-HisNA; columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 1 row SaODH Oxaloacetate NADPH d-HisNA: kcat=0.26 +/- 0.01 s^-1; Km=1400 +/- 100 uM; kcat/Km=180 +/- 10 M^-1 s^-1.

row_label: SaODH / Oxaloacetate / NADPH / d-HisNA

substrate: oxaloacetate


organism: Homo sapiens

source_db: uniprot

source: uniprot


substrate_name: NADH

substrate: NADH


organism: Colwellia psychrerythraea

substrate_name: L-proline

assay_conditions_summary: pH 10.5; cofactor NADP+

proof_lines:
pH 10.5, 30°C, cosubstrate: NAD+
pH 10.5, 30°C, cosubstrate: NADP+

substrate: L-proline


assay_conditions_summary: pH 6.5; cofactor NADPH

proof_lines:
pH 6.5, 30°C, cosubstrate: NADH
pH 6.5, 30°C, cosubstrate: NADPH


organism: Ancylobacter novellus (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIMB 10456)

proof_lines: kcat is 26 sec(-1) for Pyr2C reduction using NADPH.


organism: Shewanella loihica

substrate_name: 1-Pyrroline-2-carboxylate; H+; NADPH

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

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

substrate: 1-Pyrroline-2-carboxylate; H+; NADPH


organism: Silicibacter pomeroyi

substrate_name: H+; NADPH; 1-Pyrroline-2-carboxylate

substrate: H+; NADPH; 1-Pyrroline-2-carboxylate


substrate_name: D-Histidine nicotianamine; H+; NADPH; Pyruvate


organism: Burkholderia pseudomallei


organism: Burkholderia thailandensis

substrate_name: H+; 1-Pyrroline-2-carboxylate; NADPH

substrate: H+; 1-Pyrroline-2-carboxylate; NADPH


substrate_name: NADPH; 1-Pyrroline-2-carboxylate; H+

substrate: NADPH; 1-Pyrroline-2-carboxylate; H+


organism: Pseudomonas aeruginosa


organism: Rhodobacter sphaeroides


organism: Roseobacter denitrificans


organism: Methylorubrum extorquens

assay_conditions_summary: pH 5.3; cofactor NADPH

column_label: Article Table 2 row M. extorquens AM1 DmrA-H4 columns KM(app)=193 +/- 71 uM and kcat(s^-1)=1.5; kcat/Km is calculated from those same-row cells.

raw_value_unit_evidence: Table 2 row reports KM(app) 193 +/- 71 uM and kcat 1.5 s^-1 for M. extorquens AM1 DmrA-H4; prose identifies 193 uM H2SPT.

row_label: M. extorquens AM1 DmrA-H4

table_label: Table 2


substrate_name: dihydrosarcinapterin

proof_lines: pH 5.3, temperature not specified in the publication

substrate: dihydrosarcinapterin


organism: Agrobacterium tumefaciens

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

proof_lines: kcat is 32 sec(-1) for Pyr2C reduction using NADPH.


organism: Bacillus cereus

proof_lines: kcat is 5.8 sec(-1) for Pyr2C reduction using NADPH. kcat is 0.87 sec(-1) for Pyr2C reduction using NADH.


proof_lines: kcat is 15 sec(-1) for Pyr2C reduction using NADPH. kcat is 19 sec(-1) for Pyr2C reduction using NADH.


substrate_name: NADPH; H+; 1-Pyrroline-2-carboxylate

proof_lines: kcat is 15 sec(-1) for Pyr2C reduction using NADPH. kcat is 2.1 sec(-1) for Pyr2C reduction using NADH.

substrate: NADPH; H+; 1-Pyrroline-2-carboxylate


organism: Bacillus thuringiensis

proof_lines: kcat is 11 sec(-1) for Pyr2C reduction using NADPH. kcat is 2.1 sec(-1) for Pyr2C reduction using NADH.


organism: Pseudomonas fluorescens

km_display: Not reported


proof_lines: kcat is 20 sec(-1) for Pyr2C reduction using NADPH.


enzyme_display_name: Dihydromonapterin reductase

organism: Escherichia coli (strain K12)

substrate_name: Unknown

enzyme: Dihydromonapterin reductase

substrate: Unknown


organism: Staphylococcus aureus

assay_conditions_summary: pH 8; 295.15 K; cofactor NADPH

column_label: Table 1 row SaODH NADPH; alpha-keto acid Pyruvate; HisNA substrate d-HisNA; column kcat (s^-1).

raw_value_unit_evidence: Table 1 row SaODH NADPH with Pyruvate and d-HisNA: kcat=0.26 +/- 0.01 s^-1.

row_label: SaODH / NADPH / Pyruvate / d-HisNA

source_databases_merged: brenda skid


source_db: oed

smiles: O=CC(=O)O

source: oed


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


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


organism: Burkholderia ambifaria

proof_lines: kcat is 106 sec(-1) for Pyr2C reduction using NADPH. kcat is 41 sec(-1) for Pyr2C reduction using NADH.


substrate_name: 1-Pyrroline-2-carboxylate; NADPH; H+

proof_lines: kcat is 54 sec(-1) for Pyr2C reduction using NADPH.

substrate: 1-Pyrroline-2-carboxylate; NADPH; H+


organism: Burkholderia multivorans

proof_lines: kcat is 33 sec(-1) for Pyr2C reduction using NADPH.


proof_lines: kcat is 25 sec(-1) for Pyr2C reduction using NADPH.


organism: Colwellia psychrerythraea (strain 34H / ATCC BAA-681)

substrate_name: Delta(1)-pyrroline-2-carboxylate (using NADPH, at pH 6.5)

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature H2C with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: kcat is 7470 min(-1) for Pyr2C reduction using NADPH. kcat is 621 min(-1) for Pyr2C reduction using NADH. kcat is 82.0 min(-1) for Pip2C reduction using NADPH. kcat is 5.27 min(-1) for Pip2C reduction using NADH. kcat is 61.3 min(-1) for De


organism: Paracoccus denitrificans

proof_lines: kcat is 260 sec(-1) for Pyr2C reduction using NADPH. kcat is 81 sec(-1) for Pyr2C reduction using NADH.


assay_conditions_summary: pH 7.6; 298.15 K; cofactor NADPH

column_label: Table 7 (PDF page 17 of 32); OCD_PRS_navy (5); row group `Q63FA5 | BCE33L0803`; Cofactor sub-row `NADH`; columns kcat [s-1] = `0.87`, KM [mM] = `4.9`, kcat/KM[M-1s-1] = `180`.

normalized_value_unit_evidence: kcat: printed cell 0.87 s^-1 -> 0.87 s^(-1); the export holds 0.87 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 4.9 mM -> 4.9 mM; the export holds 4.9 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 180 M^-1 s^-1 converted as 180 / 1000 = 0.18 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 0.17755102040816326 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 7, row group `Q63FA5 | BCE33L0803`, sub-row `NADH`: kcat = 0.87 s^-1; KM = 4.9 mM; kcat/KM = 180 M^-1 s^-1.

row_label: Q63FA5 | BCE33L0803 / NADH (Table 7 OCD_PRS_navy (5))

table_label: Table 7. Kinetic constants for the proline ketimine reductases (members of the malate/Llactate dehydrogenase 2 [MLD2] and ornithine cyclodeaminase [OCD] superfamilies) that are in the genome neighborhoods of members of the PRS


proof_lines:
PRS family
Bacillus cereus
1-Pyrroline-2-carboxylate


organism: Colwellia psychrerythraea

assay_conditions_summary: pH 6.5; 303.15 K; buffer 50 mM potassium phosphate; cofactor NADPH

column_label: Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction. Row CpLhpI (Colwellia psychrerythraea) | Pyr2C | NADPH; pH cell 6.5; column 'K m (mM)' = 5.90 ± 0.36; column 'k cat (min^-1)' = 7470 ± 470; column 'k cat / K m (min^-1 mM^-1)' = 1270 ± 2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 7470 ± 470 min^-1; 7470 / 60 = 124.5 s^(-1) exactly; the exported value is 124.5 s^(-1) and already agrees. Km: printed Table 1 cell 5.90 ± 0.36 mM; the paper prints Km in mM already, so the value stands at 5.9 mM; the exported value is 1.8 mM. kcat/Km: printed Table 1 cell 1270 ± 2 min^-1 mM^-1; 1270 / 60 = 21.166666666666668 s^-1 mM^-1; the exported value is 69.16666666666667 s^(-1)*mM^(-1), which is the bare quotient 124.5 / 1.8 of the export's own two stored numbers.

raw_value_unit_evidence: Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction. | metric header row of the table: Enzymes Substrates pH a Coenzymes Specific activity (units/mg protein) K m (mM) k cat (min −1 ) k cat / K m b (min −1 mM −1 ) | row CpLhpI (Colwellia psychrerythraea) | Pyr2C | NADPH cells read: specific activity 30.2 units/mg protein, K m = 5.90 ± 0.36 mM, k cat = 7470 ± 470 min^-1, k cat / K m = 1270 ± 2 min^-1 mM^-1.

row_label: Table 1, row CpLhpI (Colwellia psychrerythraea) | Pyr2C | NADPH


column_label: Table label: Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction. Row: CpLhpI | Pip2C. Coenzyme: NADPH. Columns read: K m (mM) cell 7.26 ± 1.22, k cat (min^-1) cell 82.9 ± 13.7, k cat / K m (min^-1 mM^-1) cell 11.4 ± 0.2. metric: kcat; raw value: 82.9 ± 13.7; raw unit: min^-1; normalized value: 1.382 s^(-1); metric: Km; raw value: 7.26 ± 1.22; raw unit: mM; normalized value: 7.26 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 0.19035812672176308 s^-1 mM^-1; assay condition: All enzyme assays were performed at 30 C. Pyr2C/Pip2C reductase was assayed routinely in the direction of Pyr2C reduction by measuring the oxidization of NAD(P)H at 340 nm; the standard assay mixture contained 10 mM Pyr2C (or Pip2C) in 50 mM potassium phosphate buffer, pH 6.5 for AbLhpI and CpLhpI; the reactions were started by the addition of 100 uL of a 1.5 mM NAD(P)H solution to a final volume of 1 mL; K m and k cat values were calculated by a Lineweaver-Burk plot. Export row conditions: pH 6.5.

normalized_value_unit_evidence: CpLhpI | Pip2C | NADPH row of Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction. K m 7.26 ± 1.22 mM = 7.26 mM (the paper already prints K m in mM, so no conversion is needed); k cat 82.9 ± 13.7 min^-1 = 82.9 / 60 = 1.3816666666666668 s^-1 (1 min^-1 = 1/60 s^-1), which is 1.382 s^-1 at the export's stored precision; k cat / K m 1.382 s^-1 / 7.26 mM = 0.19035812672176308 s^-1 mM^-1. The paper's own printed k cat / K m cell 11.4 ± 0.2 min^-1 mM^-1 = 11.4 / 60 s^-1 mM^-1 agrees with that quotient at the printed cell's own precision. In the table asset the superscript minus one renders as the U+2212 sign in the headers `k cat (min −1 )` and `k cat / K m b (min −1 mM −1 )`, subscripts are flattened so K m and k cat print with a space, the substrate names print as `Pyr4 S H2C`, `Pip2C` and `l -Pipecolate`, and each cell carries its standard deviation after the ± sign.

raw_value_unit_evidence: Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction. | metric header row of the table: Enzymes Substrates pH a Coenzymes Specific activity (units/mg protein) K m (mM) k cat (min −1 ) k cat / K m b (min −1 mM −1 ) | row: Pip2C NADPH 0.291 7.26 ± 1.22 82.9 ± 13.7 11.4 ± 0.2 | CpLhpI | Pip2C | NADPH cells read: specific activity, then K m = 7.26 ± 1.22 mM, k cat = 82.9 ± 13.7 min^-1, k cat / K m = 11.4 ± 0.2 min^-1 mM^-1.

row_label: CpLhpI | Pip2C


mutation_signature: Δ1

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Δ1 to reconstruct the assayed variant sequence.

mutation_type: deletion

assay_conditions_summary: pH 6.5; 303.15 K; buffer 10 mM Pyr2C or Pip2C in 50 mM potassium phosphate; cofactor NADPH

column_label: Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction; row CpLhpI / Pyr2C / NADPH; columns Km (mM); kcat (min^-1); kcat/Km (min^-1*mM^-1); raw table cells: Km 5.90 ± 0.36 mM | kcat 7470 ± 470 min^-1 | kcat/Km 1270 ± 2 min^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=124.5 normalized_unit=s^-1; Km normalized_value=5.9 normalized_unit=mM; kcat/Km normalized_value=21.101694915254235 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=7470 ± 470 raw_unit=min^-1; Km raw_value=5.90 ± 0.36 raw_unit=mM; kcat/Km raw_value=1270 ± 2 raw_unit=min^-1*mM^-1

row_label: CpLhpI / Pyr2C / NADPH


substrate_name: L-Pipecolate

column_label: Table label: Table 2. Kinetic parameters of AbLhpI, CpLhpI and PaLhpD in the reverse direction. Row: CpLhpI | l -Pipecolate. Coenzyme: NADP +. Columns read: K m (mM) cell 80.1 ± 2.8, k cat (min^-1) cell 1.28 ± 0.04, k cat / K m (min^-1 mM^-1) cell 0.016 ± 0.001. metric: kcat; raw value: 1.28 ± 0.04; raw unit: min^-1; normalized value: 0.021 s^(-1); metric: Km; raw value: 80.1 ± 2.8; raw unit: mM; normalized value: 80.1 mM; metric: kcat/Km; raw value: 0.016 ± 0.001; raw unit: min^-1 mM^-1; normalized value: 0.0002666666666666667 s^-1 mM^-1; explicit printed primary cell; assay condition: All enzyme assays were performed at 30 C. To assay the reverse reaction, the reaction mixture consisted of 50 mM Glycine-NaOH buffer, pH 10.5 for AbLhpI and CpLhpI, and 10 mM l -proline (or l -pipecolate); the reaction was started by the addition of 15 mM NAD(P) + (100 uL) with a final reaction volume of 1 mL; K m and k cat values were calculated by a Lineweaver-Burk plot. Export row conditions: pH 10.5.

normalized_value_unit_evidence: kcat raw 1.28 ± 0.04 min^-1 -> 0.021 s^(-1); Km raw 80.1 ± 2.8 mM -> 80.1 mM; explicit printed kcat/Km raw 0.016 ± 0.001 min^-1 mM^-1 -> 0.0002666666666666667 s^-1 mM^-1. Conversion: 0.016 min^-1 mM^-1 / 60 = 1/3750 s^-1 mM^-1. The normalized ratio is taken directly from the printed primary cell, not recomputed from kcat and Km.

raw_value_unit_evidence: Table 2. Kinetic parameters of AbLhpI, CpLhpI and PaLhpD in the reverse direction. | metric header row of the table: Enzymes Substrates pH a Coenzymes Specific activity (units/mg protein) K m (mM) k cat (min −1 ) k cat / K m b (min −1 mM −1 ) | row: l -Pipecolate NADP + 0.00435 80.1 ± 2.8 1.28 ± 0.04 0.016 ± 0.001 | CpLhpI | l -Pipecolate | NADP + cells read: specific activity, then K m = 80.1 ± 2.8 mM, k cat = 1.28 ± 0.04 min^-1, k cat / K m = 0.016 ± 0.001 min^-1 mM^-1.

row_label: CpLhpI | l -Pipecolate

substrate: L-Pipecolate


substrate_name: L-Proline

substrate: L-Proline


enzyme_display_name: dihydromonapterin reductase

assay_conditions_summary: pH 6; 298.15 K; cofactor NADPH

column_label: Table 1. Summary of kinetic parameters and substrate specificities for PruA from A. tumefaciens compared to homologs from B. abortus and P. aeruginosa; row P. aeruginosa PA3437 / H2BPt; columns kcat s^-1 raw 0.8, Km uM raw 75.7 +/- 13.5, kcat/Km M^-1*s^-1 raw 1.1 x 10^4; normalized paper kcat 0.8 s^-1, Km 0.0757 mM, same-row kcat/Km 10.568031704095114 s^-1*mM^-1; export values kcat 0.8 s^-1, Km 0.757 mM, kcat/Km 1.0568031704095113 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.8 normalized_unit=s^-1; Km normalized_value=0.0757 normalized_unit=mM from 75.7 +/- 13.5 uM / 1000; kcat/Km normalized_value=10.568031704095114 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=1.1 x 10^4 M^-1*s^-1

raw_value_unit_evidence: kcat raw_value=0.8 raw_unit=s^-1; Km raw_value=75.7 +/- 13.5 raw_unit=uM; kcat/Km raw_value=1.1 x 10^4 raw_unit=M^-1*s^-1

row_label: P. aeruginosa PA3437 / H2BPt

enzyme: dihydromonapterin reductase


column_label: Table 1. Summary of kinetic parameters and substrate specificities for PruA from A. tumefaciens compared to homologs from B. abortus and P. aeruginosa; row P. aeruginosa PA3437 / H2MPt; columns kcat s^-1 raw 1.9, Km uM raw 170.0 +/- 31.2, kcat/Km M^-1*s^-1 raw 1.1 x 10^4; normalized paper kcat 1.9 s^-1, Km 0.17 mM, same-row kcat/Km 11.176470588235293 s^-1*mM^-1; export values kcat 1.9 s^-1, Km 0.17 mM, kcat/Km 11.176470588235293 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=1.9 normalized_unit=s^-1; Km normalized_value=0.17 normalized_unit=mM from 170.0 +/- 31.2 uM / 1000; kcat/Km normalized_value=11.176470588235293 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=1.1 x 10^4 M^-1*s^-1

raw_value_unit_evidence: kcat raw_value=1.9 raw_unit=s^-1; Km raw_value=170.0 +/- 31.2 raw_unit=uM; kcat/Km raw_value=1.1 x 10^4 raw_unit=M^-1*s^-1

row_label: P. aeruginosa PA3437 / H2MPt


column_label: Table 1. Summary of kinetic parameters and substrate specificities for PruA from A. tumefaciens compared to homologs from B. abortus and P. aeruginosa; row P. aeruginosa PA3437 / H2NPt; columns kcat s^-1 raw 0.7, Km uM raw 90.0 +/- 20.3, kcat/Km M^-1*s^-1 raw 7.8 x 10^3; normalized paper kcat 0.7 s^-1, Km 0.09 mM, same-row kcat/Km 7.777777777777778 s^-1*mM^-1; export values kcat 0.7 s^-1, Km 0.9 mM, kcat/Km 0.7777777777777777 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.7 normalized_unit=s^-1; Km normalized_value=0.09 normalized_unit=mM from 90.0 +/- 20.3 uM / 1000; kcat/Km normalized_value=7.777777777777778 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=7.8 x 10^3 M^-1*s^-1

raw_value_unit_evidence: kcat raw_value=0.7 raw_unit=s^-1; Km raw_value=90.0 +/- 20.3 raw_unit=uM; kcat/Km raw_value=7.8 x 10^3 raw_unit=M^-1*s^-1

row_label: P. aeruginosa PA3437 / H2NPt


column_label: Official eLife HTML Table 7 row Q0B9S2 / Bamb_3547 / NADPH; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.015

normalized_value_unit_evidence: kcat normalized_value=54 normalized_unit=s^-1; Km normalized_value=9.4 normalized_unit=mM; kcat/KM normalized_value=5.7 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=54 +/- 13 raw_unit=s^-1; Km raw_value=9.4 +/- 4 raw_unit=mM; kcat/KM raw_value=5700 raw_unit=M^-1 s^-1

row_label: Q0B9S2 / Bamb_3547 / NADPH

table_label: Table 7. Kinetic constants for the proline ketimine reductases


column_label: Official eLife HTML Table 7 row A9AKH1 / Bmul_4263 / NADPH; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.015

normalized_value_unit_evidence: kcat normalized_value=25 normalized_unit=s^-1; Km normalized_value=4 normalized_unit=mM; kcat/KM normalized_value=6.4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=25 +/- 6 raw_unit=s^-1; Km raw_value=4 +/- 2 raw_unit=mM; kcat/KM raw_value=6400 raw_unit=M^-1 s^-1

row_label: A9AKH1 / Bmul_4263 / NADPH


column_label: Official eLife HTML Table 7 row A9ALD3 / Bmul_4451 / NADPH; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.015

normalized_value_unit_evidence: kcat normalized_value=33 normalized_unit=s^-1; Km normalized_value=7.4 normalized_unit=mM; kcat/KM normalized_value=4.4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=33 +/- 2 raw_unit=s^-1; Km raw_value=7.4 +/- 1 raw_unit=mM; kcat/KM raw_value=4400 raw_unit=M^-1 s^-1

row_label: A9ALD3 / Bmul_4451 / NADPH


substrate_name: 7,8-dihydrofolate (at pH 6.0)

assay_conditions_summary: pH 6

proof_lines: FolM, A New Chromosomally Encoded Dihydrofolate Reductase in Escherichia coli

substrate: 7,8-dihydrofolate (at pH 6.0)


substrate_name: NADPH (at pH 6.0)

assay_conditions_summary: pH 6; cofactor NADPH

substrate: NADPH (at pH 6.0)


enzyme_display_name: FMN reductase [NAD(P)H]

substrate_name: NADPH

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

assay_conditions_summary: pH 7.5; cofactor NADPH

enzyme: FMN reductase [NAD(P)H]

substrate: NADPH


column_label: Official eLife HTML Table 7 row Q7CVK1 / Atu4676 / NADPH; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.015

normalized_value_unit_evidence: kcat normalized_value=32 normalized_unit=s^-1; Km normalized_value=0.33 normalized_unit=mM; kcat/KM normalized_value=99 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=32 +/- 1 raw_unit=s^-1; Km raw_value=0.33 +/- 0.04 raw_unit=mM; kcat/KM raw_value=99000 raw_unit=M^-1 s^-1

row_label: Q7CVK1 / Atu4676 / NADPH


assay_conditions_summary: pH 5.3; 296.15 K; cofactor NADPH


organism: Burkholderia pseudomallei

proof_lines:
PRS family
Bacillus cereus


column_label: Table 7 (PDF page 17 of 32); MLD2_PRS_light skyblue (3); row group `Q9I492 | PA1252`; Cofactor sub-row `NADPH`; columns kcat [s-1] = `1.6`, KM [mM] = `0.41`, kcat/KM[M-1s-1] = `3900`.

normalized_value_unit_evidence: kcat: printed cell 1.6 s^-1 -> 1.6 s^(-1); the export holds 1.6 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 0.41 mM -> 0.41 mM; the export holds 0.41 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 3900 M^-1 s^-1 converted as 3900 / 1000 = 3.9 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 3.9024390243902443 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 7, row group `Q9I492 | PA1252`, sub-row `NADPH`: kcat = 1.6 s^-1; KM = 0.41 mM; kcat/KM = 3900 M^-1 s^-1.

row_label: Q9I492 | PA1252 / NADPH (Table 7 MLD2_PRS_light skyblue (3))


organism: Burkholderia thailandensis


column_label: Official eLife HTML Table 7 row Q3IZJ8 / RSP_0854 / NADPH; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.015

normalized_value_unit_evidence: kcat normalized_value=66 normalized_unit=s^-1; Km normalized_value=0.43 normalized_unit=mM; kcat/KM normalized_value=150 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=66 +/- 4 raw_unit=s^-1; Km raw_value=0.43 +/- 0.09 raw_unit=mM; kcat/KM raw_value=150000 raw_unit=M^-1 s^-1

row_label: Q3IZJ8 / RSP_0854 / NADPH


column_label: Official eLife HTML Table 7 row Q4KGT8 / PFL_1416 / NADPH; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.015

normalized_value_unit_evidence: kcat normalized_value=20 normalized_unit=s^-1; Km normalized_value=1.1 normalized_unit=mM; kcat/KM normalized_value=18 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=20 +/- 0.8 raw_unit=s^-1; Km raw_value=1.1 +/- 0.2 raw_unit=mM; kcat/KM raw_value=18000 raw_unit=M^-1 s^-1

row_label: Q4KGT8 / PFL_1416 / NADPH


organism: Shewanella loihica


substrate_name: 7,8-dihydromonapterin (at pH 6.0)

substrate: 7,8-dihydromonapterin (at pH 6.0)


organism: Silicibacter pomeroyi

column_label: Official eLife HTML Table 7 row Q5LLV0 / SPO3821 / NADPH; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.015

normalized_value_unit_evidence: kcat normalized_value=130 normalized_unit=s^-1; Km normalized_value=3.0 normalized_unit=mM; kcat/KM normalized_value=43 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=130 +/- 20 raw_unit=s^-1; Km raw_value=3.0 +/- 0.9 raw_unit=mM; kcat/KM raw_value=43000 raw_unit=M^-1 s^-1

row_label: Q5LLV0 / SPO3821 / NADPH


enzyme_display_name: FMN reductase (NADPH)

organism: Escherichia coli

substrate_name: FMN

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

assay_conditions_summary: pH 7.9; 303.15 K; cofactor FMN

enzyme: FMN reductase (NADPH)

substrate: FMN


substrate_name: FAD

assay_conditions_summary: pH 7.9; 303.15 K; cofactor FAD

substrate: FAD


assay_conditions_summary: pH 7.9; 303.15 K; cofactor NADPH


substrate_name: NADH

assay_conditions_summary: pH 7.9; 303.15 K; cofactor NADH

substrate: NADH


organism: Homo sapiens

proof_lines: wild-type, pH 6.6, temperature not specified in the publication


mutation_signature: truncated protein

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

mutation_type: truncation

proof_lines: truncated protein, residues 38-644, pH 6.6, temperature not specified in the publication


assay_conditions_summary: pH 6.6; cofactor NADPH


assay_conditions_summary: pH 6.6; cofactor NADH


ki_unit: mM


enzyme_display_name: FMN reductase (NADH)

organism: Pseudomonas putida

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

enzyme: FMN reductase (NADH)


enzyme_display_name: glutamate dehydrogenase (NADP+)

substrate_name: NADP+

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

proof_lines: chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 80.8 micromol/min/mg, pH 8.0, 25°C

enzyme: glutamate dehydrogenase (NADP+)

substrate: NADP+


proof_lines: chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 1960 micromol/min/mg, pH 8.0, 25°C


substrate_name: L-glutamate

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

proof_lines: chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 121.9 micromol/min/mg, pH 8.0, 25°C

substrate: L-glutamate


enzyme_display_name: UniProt B9L163

organism: Thermomicrobium roseum

substrate_name: N-Methyl-L-alanine

source_db: skid

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt B9L163

substrate: N-Methyl-L-alanine

source: skid


substrate_name: N-methyl-L-phenylalanine

substrate: N-methyl-L-phenylalanine


substrate_name: N-methyl-L-tryptophan

substrate: N-methyl-L-tryptophan


substrate_name: L-proline

substrate: L-proline


substrate_name: N-methyl-D-proline

substrate: N-methyl-D-proline


substrate_name: N-methyl-L-aspartate

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

substrate: N-methyl-L-aspartate


substrate_name: N-Methyl-L-leucine

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

substrate: N-Methyl-L-leucine


enzyme_display_name: UniProt P40859

organism: Bacillus sp. (in: Bacteria)

substrate_name: sarcosine

smiles: CNCC(=O)O

enzyme: UniProt P40859

substrate: sarcosine


enzyme_display_name: alanine dehydrogenase

organism: Halobacterium salinarum

assay_conditions_summary: cofactor NADH

enzyme: alanine dehydrogenase


substrate_name: L-Ala

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

substrate: L-Ala


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

assay_conditions_summary: pH 8; buffer 50 mM triethanolamine; cofactor NADP+

proof_lines: mutant enzyme R443S/G456A, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP

enzyme: glutamate dehydrogenase [NAD(P)+]


smiles: N


organism: Paenarthrobacter ureafaciens

substrate_name: N-Methyl-DL-alanine

substrate: N-Methyl-DL-alanine


enzyme_display_name: N6-methyl-lysine oxidase

organism: Rattus norvegicus

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

enzyme: N6-methyl-lysine oxidase


organism: Mycolicibacterium smegmatis


assay_conditions_summary: pH 7.2; 296.15 K; cofactor NADH


organism: Achromobacter denitrificans


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

proof_lines:
crude extract
partially purified enzyme


enzyme_display_name: N-methyl-L-amino-acid oxidase

organism: Oryctolagus cuniculus

substrate_name: alpha-N-methyl-L-tryptophan

enzyme: N-methyl-L-amino-acid oxidase

substrate: alpha-N-methyl-L-tryptophan


organism: Bacillus sp. (in: firmicutes)

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K265Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8


sequence_variant_note: Mutation signature K265A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature K265M could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature K265R could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Synechocystis sp. PCC 6803

smiles: C(CN)CN

assay_conditions_summary: pH 7.4; cofactor NADPH

proof_lines: at pH 7.4, temperature not specified in the publication

proof_lines: kcat is 2.57 sec(-1) with agmatine as substrate. kcat is 0.32 sec(-1) with putrescine as substrate. kcat is 0.07 sec(-1) with 1,3-diaminopropane as substrate. kcat is 2.43 sec(-1) with NADPH as substrate.

source_databases_merged: brenda uniprot


substrate_name: putrescine

smiles: C(CCN)CN

substrate: putrescine


substrate_name: agmatine

smiles: C(CCN=C(N)N)CN

proof_lines: with NADPH as cosubstrate, at pH 7.4, temperature not specified in the publication

substrate: agmatine


substrate_name: NADPH

substrate: NADPH


substrate_name: NADH

substrate: NADH


organism: Arthrobacter sp.

proof_lines: immobilized enzyme on alkylamine glass beads, pH 7.8, 37°C

proof_lines: immobilized enzyme on arylamine glass beads, pH 7.8, 37°C


enzyme_display_name: 18-hydroxynorfluorocurarine reductase

organism: Strychnos nux-vomica

substrate_name: norfluorocurarine

proof_lines: kcat is 1.754 min(-1) with norfluorocurarine as substrate (PubMed:35794473). kcat is 0.337 min(-1) with 18-OH norfluorocurarine as substrate (PubMed:35794473).

enzyme: 18-hydroxynorfluorocurarine reductase

substrate: norfluorocurarine


substrate_name: 18-OH norfluorocurarine

substrate: 18-OH norfluorocurarine


organism: Escherichia coli (strain K12)

substrate_name: NADH (at pH 7.2 and 15 degrees Celsius)

assay_conditions_summary: pH 7.2; cofactor NADH

proof_lines: kcat is 1800 min(-1) for the NADH-dependent reduction of 5,10-methylenetetrahydrofolate (at pH 7.2 and 15 degrees Celsius) (PubMed:9922232). kcat is 1410 min(-1) for the oxidation of NADH by enzyme-bound FAD (at pH 7.2 and 15 degrees Celsiu

substrate: NADH (at pH 7.2 and 15 degrees Celsius)


substrate_name: (6R)-5,10-methylenetetrahydrofolate (at pH 7.2 and 15 degrees Celsius)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F235V/F339L with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines: mutant F235V/F339L, pH not specified in the publication, 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R49K to reconstruct the assayed variant sequence.


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: D-arginine dehydrogenase

organism: Pseudomonas aeruginosa

substrate_name: D-arginine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y249F to reconstruct the assayed variant sequence.

enzyme: D-arginine dehydrogenase

substrate: D-arginine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y53F to reconstruct the assayed variant sequence.


organism: Corynebacterium sp. U-96


substrate_name: oxygen

smiles: O=O

substrate: oxygen


organism: Corynebacterium sp.

substrate_name: N-ethylglycine

smiles: CCNCC(=O)O

substrate: N-ethylglycine


substrate_name: N-Methyl-L-alanine

substrate: N-Methyl-L-alanine


substrate_name: sarcosine


substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


substrate_name: potassium ferricyanide

substrate: potassium ferricyanide


organism: Escherichia coli

assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADH

proof_lines: mutant E28Q, cosubstrate menadione, pH 7.2, 25°C


substrate_name: menadione

substrate: menadione


proof_lines:
wild-type, pH 7.2, 25°C
wild-type, pH 7.2, 4°C
wild-type, pH 7.2, 15°C


proof_lines: mutant D120N, cosubstrate menadione, pH 7.2, 25°C


proof_lines: mutant D120N, cosubstrate NADH, pH 7.2, 25°C


proof_lines: wild-type, cosubstrate menadione, pH 7.2, 25°C


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7.2; cofactor NADPH

proof_lines: Chimera-1, cosubstrate NADPH, pH 7.2, temperature not specified in the publication

proof_lines: Chimera-1, cosubstrate NADH, pH 7.2, temperature not specified in the publication


proof_lines: wild-type, cosubstrate NADH, pH 7.2, temperature not specified in the publication


proof_lines: wild-type, pH 7.2, temperature not specified in the publication


assay_conditions_summary: pH 7.2; 277.15 K; cofactor NADH


proof_lines: wild-type, cosubstrate NADH, pH 7.2, 25°C


organism: Homo sapiens

substrate_name: S-(2-aminoethyl)-L-cysteine ketimine

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

proof_lines:
pH 7.2, 37°C
pH 7.2, temperature 37°C

substrate: S-(2-aminoethyl)-L-cysteine ketimine


proof_lines:
pH 7.2, 37°C
pH 7.2, 37°C, recombinant enzyme


substrate_name: 1-piperideine 2-carboxylate

substrate: 1-piperideine 2-carboxylate


enzyme_display_name: UniProt Q93NH4

organism: Paenarthrobacter nicotinovorans

substrate_name: (S)-nicotine

enzyme: UniProt Q93NH4

substrate: (S)-nicotine


enzyme_display_name: UniProt F8G0P2

organism: Pseudomonas putida

enzyme: UniProt F8G0P2


substrate_name: NADH

assay_conditions_summary: pH 7.2; 288.15 K; cofactor NADH

proof_lines: presence of 0.05 mM genistein, pH 7.2, 37°C


assay_conditions_summary: cofactor NADP+

proof_lines: deuterated, NADP+-dependent bifunctional dehydrogenase-cyclohydrolase domain of the cytoplasmic trifunctional enzyme

proof_lines: NAD+-M2+-phopsphate-dependent mitochondrial dehydrogenase-cyclohydrolase enzyme


substrate_name: NADP+

proof_lines: substrate constant: methylenetetrahydrofolate, deuterated, NADP+-dependent bifunctional dehydrogenase-cyclohydrolase domain of the cytoplasmic trifunctional enzyme

substrate: NADP+


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


enzyme_display_name: dihydrobenzophenanthridine oxidase

organism: Eschscholzia californica

substrate_name: Dihydromacarpine

enzyme: dihydrobenzophenanthridine oxidase

substrate: Dihydromacarpine


substrate_name: dihydrochelirubine

substrate: dihydrochelirubine


substrate_name: Dihydrosanguinarine

substrate: Dihydrosanguinarine


enzyme_display_name: L-pipecolate oxidase

organism: Macaca mulatta

substrate_name: L-pipecolic acid

enzyme: L-pipecolate oxidase

substrate: L-pipecolic acid


substrate_name: (S)-1,3-thiazane-4-carboxylic acid

proof_lines: competitive inhibitor that completely inactivates the enzyme

substrate: (S)-1,3-thiazane-4-carboxylic acid


organism: Sanguinaria canadensis


substrate_name: Dihydrochelerythrine

substrate: Dihydrochelerythrine


organism: Papaver somniferum

substrate_name: (S)-scoulerine

substrate: (S)-scoulerine


enzyme_display_name: dimethylglycine oxidase

organism: Cylindrocarpon didymum

substrate_name: N,N-dimethylglycine

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

enzyme: dimethylglycine oxidase

substrate: N,N-dimethylglycine


organism: Rhodotorula glutinis


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: (S)-6-hydroxynicotine oxidase

organism: Ochrobactrum sp. SJY1

enzyme: (S)-6-hydroxynicotine oxidase


organism: Macacine alphaherpesvirus 1


organism: Arthrobacter globiformis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y259F to reconstruct the assayed variant sequence.

proof_lines:
mutant Y259F
mutant Y259F, pH 8.5, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H225Q to reconstruct the assayed variant sequence.

proof_lines:
mutant H225Q
mutant H225Q, pH 8.5, 25°C


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

proof_lines:
wild-type enzyme
wild-type, pH 8.5, 25°C

source_databases_merged: brenda oed


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K287M to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N166A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y311F to reconstruct the assayed variant sequence.


column_label: Table 1; row Wild-type; substrate section (S)-6-hydroxynornicotine; column kcat (s^-1) raw value 16; column kcat/Kamine (mM^-1 s^-1) raw value 370; column Kamine (mM) raw value 0.064

normalized_value_unit_evidence: kcat normalized_value=16 normalized_unit=s^-1; kcat/Kamine normalized_value=370 normalized_unit=s^-1*mM^-1; Kamine normalized_value=0.064 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=16 raw_unit=s^-1; kcat/Kamine raw_value=370 raw_unit=mM^-1*s^-1; Kamine raw_value=0.064 raw_unit=mM

row_label: Wild-type / (S)-6-hydroxynornicotine

table_label: Table 1. Steady-state kinetic parameters for wild-type and variant L-6-hydroxynicotine oxidase


column_label: Table 1; row Y311F; substrate section (S)-6-hydroxynicotine; column K_O2 (mM); raw value 0.19 mM.

raw_value_unit_evidence: Table 1 row Y311F with (S)-6-hydroxynicotine; K_O2 = 0.19 mM.


column_label: Table 1; row N166A; substrate section (S)-6-hydroxynicotine; column K_O2 (mM); raw value 0.20 mM.

raw_value_unit_evidence: Table 1 row N166A with (S)-6-hydroxynicotine; K_O2 = 0.20 mM.


column_label: Table 1; row Wild-type; substrate section (S)-6-hydroxynicotine; column K_O2 (mM); raw value 0.29 mM.

raw_value_unit_evidence: Table 1 row Wild-type with (S)-6-hydroxynicotine; K_O2 = 0.29 mM.

row_label: Wild-type / O2


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R274A/Y311W/C417W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y311W with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


proof_lines:
wild-type, pH 7.4, 22°C
pH 7.0, 25°C, wild-type enzyme


enzyme_display_name: (R)-6-hydroxynicotine oxidase

substrate_name: (R)-nicotine

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

enzyme: (R)-6-hydroxynicotine oxidase

substrate: (R)-nicotine


column_label: Table 1 (Steady-State Kinetic Parameters for Wild-Type and Mutant D-6-Hydroxynicotine oxidase), substrate section '(R)-6-Hydroxynornicotine', enzyme row 'wild-type'; column 'kcat (s^-1)' = 8.1 ± 0.5; column 'kcat/Kamine (mM^-1 s^-1)' = 24 ± 3; column 'Kamine (mM)' = 0.34 ± 0.06. The 'kcat/K(O2) (mM^-1 s^-1)' and 'K(O2) (mM)' columns are empty for this section.

normalized_value_unit_evidence: kcat: printed Table 1 cell 8.1 s^-1; the printed unit is already s^-1, so no unit conversion applies, giving 8.1 s^(-1). Km: printed Table 1 cell 0.34 mM; the printed unit is already mM, so no unit conversion applies, giving 0.34 mM. kcat/Km: 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell 24 mM^-1 s^-1 converts to 24.0 s^-1 mM^-1; the catalog carries the exact quotient of the same two printed cells, 8.1 / 0.34 = 23.823529411764703 s^(-1)*mM^(-1), and 24 is that quotient rounded to the whole-unit precision the paper printed.

raw_value_unit_evidence: Table 1, substrate section '(R)-6-Hydroxynornicotine', enzyme row 'wild-type': column kcat (s^-1) prints 8.1 ± 0.5; column Kamine (mM) prints 0.34 ± 0.06; column kcat/Kamine (mM^-1 s^-1) prints 24 ± 3.

row_label: Table 1, wild-type row in the (R)-6-Hydroxynornicotine section

table_label: Table 1: Steady-State Kinetic Parameters for Wild-Type and Mutant D-6-Hydroxynicotine oxidase (Biochemistry 2019, 58(21):2534-2541)


column_label: Table 1 (Steady-State Kinetic Parameters for Wild-Type and Mutant D-6-Hydroxynicotine oxidase), substrate section '(R)-6-Hydroxynicotine', enzyme row 'wild-type'; column 'kcat (s^-1)' = 77 ± 24 (footnote b); column 'kcat/Kamine (mM^-1 s^-1)' = 380 ± 52 (footnote c); column 'Kamine (mM)' = 0.20 ± 0.03; column 'kcat/K(O2) (mM^-1 s^-1)' = 16 ± 1 (footnote b); column 'K(O2) (mM)' = 4.7 ± 1.7 (footnote b); the second sub-row of the same enzyme row prints the apparent kcat 8.7 ± 0.6 s^-1 and the apparent Kamine 0.023 ± 0.004 mM measured at 250 microM O2 (footnote c).

normalized_value_unit_evidence: kcat: printed Table 1 cell 77 s^-1; the printed unit is already s^-1, so no unit conversion applies, giving 77.0 s^(-1). Km: printed Table 1 cell 0.20 mM; the printed unit is already mM, so no unit conversion applies, giving 0.20 mM. kcat/Km: printed Table 1 cell 380 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so 380 mM^-1 s^-1 converts to 380.0 s^(-1)*mM^(-1), the paper's own fitted catalytic-efficiency value for this row.

raw_value_unit_evidence: Table 1, substrate section '(R)-6-Hydroxynicotine', enzyme row 'wild-type': column kcat (s^-1) prints 77 ± 24; column Kamine (mM) prints 0.20 ± 0.03; column kcat/Kamine (mM^-1 s^-1) prints 380 ± 52.

row_label: Table 1, wild-type row in the (R)-6-Hydroxynicotine section


organism: Shinella sp.

proof_lines: kcat is 7.3 sec(-1) with (S)-6-hydroxynicotine as substrate. kcat is 0.396 sec(-1) with nicotine as substrate (PubMed:25002425). kcat is 5.9 sec(-1) with 6-hydroxynornicotine as substrate (PubMed:27568381).


assay_conditions_summary: pH 9

proof_lines: DMGO1, pH 9.0, temperature not specified in the publication

proof_lines: DMGO2, pH 9.0, temperature not specified in the publication


organism: Schizosaccharomyces pombe

substrate_name: L-proline

substrate: L-proline


substrate_name: L-pipecolate

substrate: L-pipecolate


proof_lines: kcat is 30 sec(-1) with (S)-6-hydroxynicotine as substrate. kcat is 16 sec(-1) with (S)-6-hydroxynornicotine as substrate.


organism: Shinella sp. (strain HZN7)


proof_lines: pH and temperature not specified in the publication


substrate_name: N,N-Dimethylglycine; H2O; O2

substrate: N,N-Dimethylglycine; H2O; O2


substrate_name: O2; L-Pipecolate

substrate: O2; L-Pipecolate


proof_lines: pH 7.0, 25°C, mutant enzyme K287M, cosubstrate: (S)-6-hydroxynicotine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E352Q with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


organism: Oryctolagus cuniculus


substrate_name: (S)-nicotine

substrate: (S)-nicotine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R274A/Y311W/C417W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y311W with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


organism: Zea mays

smiles: CC(=O)NCCCNCCCCNCCCN


smiles: CC(=O)NCCCNCCCCN


enzyme_display_name: Polyamine oxidase 1

substrate_name: dioxygen

enzyme: Polyamine oxidase 1

substrate: dioxygen


substrate_name: spermine

smiles: C(CCNCCCN)CNCCCN

substrate: spermine


substrate_name: spermidine

smiles: C(CCNCCCN)CN

substrate: spermidine


enzyme_display_name: UniProt P50264

organism: Saccharomyces cerevisiae

enzyme: UniProt P50264


organism: Paenarthrobacter nicotinovorans

substrate_name: FAD

assay_conditions_summary: cofactor FAD

proof_lines:
D- and L-6-Hydroxynicotine Oxidase
Arthrobacter oxidans
coenzyme binding

substrate: FAD


proof_lines:
D- and L-6-hydroxynicotine oxidase
Arthrobacter oxidans
6-hydroxynicotine


column_label: Abstract reports rabbit activity was maximal when FAD, phenazine ethosulfate, and glycerol were included in the assay; Kmapp was 0.74+/-0.16 mM.

raw_value_unit_evidence: Km raw_value=0.74+/-0.16 mM raw_unit=mM

row_label: rabbit kidney cortex L-pipecolic acid oxidation

table_label: PubMed XML abstract PMID 2914918


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E350A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E350Q with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +5, so it is treated as a source-provided variant sequence.


enzyme_display_name: non-specific polyamine oxidase

organism: Branchiostoma japonicum

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

enzyme: non-specific polyamine oxidase


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


organism: Mus musculus

proof_lines: pH 10.0, 30°C, recombinant wild-type enzyme, with spermine

proof_lines: pH 8.6, 30°C, recombinant wild-type enzyme, with N,N'-dibenzyl-1,4-diaminobutane

proof_lines: pH 10.0, 30°C, recombinant wild-type enzyme and recombinant mutants H64A and H64N, with N1-acetylspermine


proof_lines: pH 8.6, 30°C, recombinant mutants H64A and H64Q, with N,N'-dibenzyl-1,4-diaminobutane


proof_lines: pH 8.6, 30°C, recombinant mutant H64N, with N,N'-dibenzyl-1,4-diaminobutane

proof_lines: pH 10.0, 30°C, recombinant mutant H64N, with N1-acetylspermine

proof_lines: pH 10.0, 30°C, recombinant mutant H64N, with spermine


proof_lines: pH 10.0, 30°C, recombinant mutants H64A and H64Q


proof_lines: pH 10.0, 30°C, recombinant mutants H64A and H64N, with spermine


proof_lines: pH 10.0, 30°C, recombinant mutant H64Q, with spermine

proof_lines: pH 10.0, 30°C, recombinant mutant H64Q, with N1-acetylspermine

proof_lines: pH 8.6, 30°C, recombinant mutant H64Q, with N,N'-dibenzyl-1,4-diaminobutane


proof_lines: pH 10.0, 30°C, recombinant mutant H64A, with N1-acetylspermine

proof_lines: pH 8.6, 30°C, recombinant mutant H64A, with N,N'-dibenzyl-1,4-diaminobutane


proof_lines: pH 8.6, 30°C, recombinant mutants H64A and H64N


proof_lines: pH 8.6, 30°C, recombinant wild-type enzyme


proof_lines: pH 10.0, 30°C, recombinant wild-type enzyme


organism: Oryza sativa

substrate_name: norspermidine

smiles: C(CN)CNCCCN

substrate: norspermidine


substrate_name: thermospermine

smiles: C(CCNCCCNCCCN)CN

substrate: thermospermine


substrate_name: norspermine

smiles: C(CN)CNCCCNCCCN

substrate: norspermine


enzyme_display_name: N1-acetylpolyamine oxidase

enzyme: N1-acetylpolyamine oxidase


enzyme_display_name: spermine oxidase

organism: Ascaris suum

substrate_name: O2; Spermine; H2O

enzyme: spermine oxidase

substrate: O2; Spermine; H2O


substrate_name: tryptamine

substrate: tryptamine


organism: Bos taurus


smiles: C(CN)CNCCNCCCN


proof_lines: pH 7.2, 37°C, with spermine as substrate


substrate_name: O2; H2O; Tryptamine

substrate: O2; H2O; Tryptamine


smiles: CC(=O)NCCCCNCCCN


enzyme_display_name: N-alkylglycine oxidase

organism: Cladosporium sp.

substrate_name: N-ethylglycine

enzyme: N-alkylglycine oxidase

substrate: N-ethylglycine


substrate_name: sarcosine

smiles: CNCC(=O)O

substrate: sarcosine


substrate_name: Nepsilon-carboxymethyllysine

substrate: Nepsilon-carboxymethyllysine


organism: Arabidopsis thaliana


organism: Synechocystis sp. PCC 6803


organism: Acanthamoeba culbertsoni


organism: Mammalia

substrate_name: N1-Acetylspermidine; O2; H2O

substrate: N1-Acetylspermidine; O2; H2O


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N313D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N313L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


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

assay_conditions_summary: pH 9; 303.15 K; buffer of 0

column_label: Table 2 (Kinetic Parameters for Wild-Type and Mutant Murine Polyamine Oxidases), spermine block, wild-type PAO column: parameter row 'Ks,app (mM)' = 8; parameter row 'kcat,app (s^-1)' = 8; parameter row 'kcat/Ks (mM^-1 s^-1)' = 1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 8 s^-1 (row kcat,app); the column head prints s^-1, so no unit conversion applies and the paper value is 8 s^(-1); the exported value is 8.0 s^(-1). Km: printed Table 2 cell 8 mM (row Ks,app, the apparent Michaelis constant); the column head prints mM, so no unit conversion applies and the paper value is 8 mM; the exported value is 8.0 mM. kcat/Km: printed Table 2 cell 1 mM^-1 s^-1 (row kcat/Ks); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell is 1 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 8 / 8 = 1.0 s^-1 mM^-1, identical to the printed efficiency cell and to the exported kcat_over_km.

raw_value_unit_evidence: Table 2, spermine block, wild-type PAO column: kcat,app = 8 s^-1; Ks,app = 8 mM; printed kcat/Ks = 1 mM^-1 s^-1.

table_label: Table 2: Kinetic Parameters for Wild-Type and Mutant Murine Polyamine Oxidases (Biochemistry 2017, volume 56, number 3, pages 458-467); printed columns wild-type PAO, N313D, N313A, N313L and N313T, each carrying an N1-acetylspermine block and a spermine block of three parameter rows Ks,app (mM), kcat,app (s^-1) and kcat/Ks (mM^-1 s^-1)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N313T with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N313A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8C0L6 and applied mutation signature N313T to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Wild-Type and Mutant Murine Polyamine Oxidases), N1-acetylspermine block, N313T column: parameter row 'Ks,app (mM)' = 0.12; parameter row 'kcat,app (s^-1)' = 22; parameter row 'kcat/Ks (mM^-1 s^-1)' = 175.

normalized_value_unit_evidence: kcat: printed Table 2 cell 22 s^-1 (row kcat,app); the column head prints s^-1, so no unit conversion applies and the paper value is 22 s^(-1); the exported value is 22.0 s^(-1). Km: printed Table 2 cell 0.12 mM (row Ks,app, the apparent Michaelis constant); the column head prints mM, so no unit conversion applies and the paper value is 0.12 mM; the exported value is 0.12 mM. kcat/Km: printed Table 2 cell 175 mM^-1 s^-1 (row kcat/Ks); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell is 175 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 22 / 0.12 = 183.33333333333334 s^-1 mM^-1, which is the exported kcat_over_km 183.33333333333334; the printed efficiency cell 175 is the paper's own fitted value and is the value proposed for the catalog.

raw_value_unit_evidence: Table 2, N1-acetylspermine block, N313T column: kcat,app = 22 s^-1; Ks,app = 0.12 mM; printed kcat/Ks = 175 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8C0L6 and applied mutation signature N313A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Wild-Type and Mutant Murine Polyamine Oxidases), N1-acetylspermine block, N313A column: parameter row 'Ks,app (mM)' = 0.1; parameter row 'kcat,app (s^-1)' = 25; parameter row 'kcat/Ks (mM^-1 s^-1)' = 277.

normalized_value_unit_evidence: kcat: printed Table 2 cell 25 s^-1 (row kcat,app); the column head prints s^-1, so no unit conversion applies and the paper value is 25 s^(-1); the exported value is 25.0 s^(-1). Km: printed Table 2 cell 0.1 mM (row Ks,app, the apparent Michaelis constant); the column head prints mM, so no unit conversion applies and the paper value is 0.1 mM; the exported value is 0.1 mM. kcat/Km: printed Table 2 cell 277 mM^-1 s^-1 (row kcat/Ks); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell is 277 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 25 / 0.1 = 250.0 s^-1 mM^-1, which is the exported kcat_over_km 250.0; the printed efficiency cell 277 is the paper's own fitted value and is the value proposed for the catalog.

raw_value_unit_evidence: Table 2, N1-acetylspermine block, N313A column: kcat,app = 25 s^-1; Ks,app = 0.1 mM; printed kcat/Ks = 277 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8C0L6 and applied mutation signature N313L to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Wild-Type and Mutant Murine Polyamine Oxidases), N1-acetylspermine block, N313L column: parameter row 'Ks,app (mM)' = 0.2; parameter row 'kcat,app (s^-1)' = 25; parameter row 'kcat/Ks (mM^-1 s^-1)' = 144.

normalized_value_unit_evidence: kcat: printed Table 2 cell 25 s^-1 (row kcat,app); the column head prints s^-1, so no unit conversion applies and the paper value is 25 s^(-1); the exported value is 25.0 s^(-1). Km: printed Table 2 cell 0.2 mM (row Ks,app, the apparent Michaelis constant); the column head prints mM, so no unit conversion applies and the paper value is 0.2 mM; the exported value is 0.2 mM. kcat/Km: printed Table 2 cell 144 mM^-1 s^-1 (row kcat/Ks); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell is 144 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 25 / 0.2 = 125.0 s^-1 mM^-1, which is the exported kcat_over_km 125.0; the printed efficiency cell 144 is the paper's own fitted value and is the value proposed for the catalog.

raw_value_unit_evidence: Table 2, N1-acetylspermine block, N313L column: kcat,app = 25 s^-1; Ks,app = 0.2 mM; printed kcat/Ks = 144 mM^-1 s^-1.


column_label: Table 2 (Kinetic Parameters for Wild-Type and Mutant Murine Polyamine Oxidases), N1-acetylspermine block, wild-type PAO column: parameter row 'Ks,app (mM)' = 0.003; parameter row 'kcat,app (s^-1)' = 27; parameter row 'kcat/Ks (mM^-1 s^-1)' = 9600.

normalized_value_unit_evidence: kcat: printed Table 2 cell 27 s^-1 (row kcat,app); the column head prints s^-1, so no unit conversion applies and the paper value is 27 s^(-1); the exported value is 27.0 s^(-1). Km: printed Table 2 cell 0.003 mM (row Ks,app, the apparent Michaelis constant); the column head prints mM, so no unit conversion applies and the paper value is 0.003 mM; the exported value is 0.003 mM. kcat/Km: printed Table 2 cell 9600 mM^-1 s^-1 (row kcat/Ks); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell is 9600 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 27 / 0.003 = 9000.0 s^-1 mM^-1, which is the exported kcat_over_km 9000.0; the printed efficiency cell 9600 is the paper's own fitted value and is the value proposed for the catalog.

raw_value_unit_evidence: Table 2, N1-acetylspermine block, wild-type PAO column: kcat,app = 27 s^-1; Ks,app = 0.003 mM; printed kcat/Ks = 9600 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8C0L6 and applied mutation signature N313D to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Wild-Type and Mutant Murine Polyamine Oxidases), N1-acetylspermine block, N313D column: parameter row 'Ks,app (mM)' = 0.2; parameter row 'kcat,app (s^-1)' = 27; parameter row 'kcat/Ks (mM^-1 s^-1)' = 137.

normalized_value_unit_evidence: kcat: printed Table 2 cell 27 s^-1 (row kcat,app); the column head prints s^-1, so no unit conversion applies and the paper value is 27 s^(-1); the exported value is 27.0 s^(-1). Km: printed Table 2 cell 0.2 mM (row Ks,app, the apparent Michaelis constant); the column head prints mM, so no unit conversion applies and the paper value is 0.2 mM; the exported value is 0.2 mM. kcat/Km: printed Table 2 cell 137 mM^-1 s^-1 (row kcat/Ks); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell is 137 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 27 / 0.2 = 135.0 s^-1 mM^-1, which is the exported kcat_over_km 135.0; the printed efficiency cell 137 is the paper's own fitted value and is the value proposed for the catalog.

raw_value_unit_evidence: Table 2, N1-acetylspermine block, N313D column: kcat,app = 27 s^-1; Ks,app = 0.2 mM; printed kcat/Ks = 137 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P50264 and applied mutation signature D94N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9.35; 298.15 K; buffer containing 10 percent glycerol

column_label: Table 2 (Steady-State Kinetic Parameters), spermine substrate block, value column under the printed head D94N: printed row Kamine (uM) = 320; printed row kcat (s-1) = 2.0; printed row kcat/Kamine (mM-1 s-1) = 4.1. The value printed after the plus/minus sign in each of those cells is the printed uncertainty and is not an exported metric; the same column also prints kcat/KO2 (mM-1 s-1) = 104 and KO2 (uM) = 192, which are the oxygen parameters of the same table line.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.0 in a row headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 2.0 s^(-1). Km: printed Table 2 cell 320 in a row headed Kamine (uM); 1 uM is 0.001 mM, so 320 / 1000 = 0.32 mM. kcat/Km: printed Table 2 cell 4.1 in a row headed kcat/Kamine (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 4.1 s^(-1)*mM^(-1). The catalog carries kcat 2.0 s^(-1), Km 0.32 mM and kcat_over_km 6.25 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, spermine block, value column under the printed head D94N: Kamine = 320 uM; kcat = 2.0 s-1; printed kcat/Kamine = 4.1 in a row headed kcat/Kamine (mM-1 s-1).

row_label: Table 2, spermine block, D94N column

table_label: Table 2: Steady-State Kinetic Parameters for Wild-type Fmsl and the N195A and D94N Enzymes (Biochemistry 2012, 51(43):8690-8697). Printed parameter rows in each substrate block: kcat (s-1); kcat/Kamine (mM-1 s-1); Kamine (uM); kcat/KO2 (mM-1 s-1); KO2 (uM). Printed value columns, left to right: Fms1 (footnote d, from ref. (13)), N195A, D94N.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P50264 and applied mutation signature N195A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Kinetic Parameters), spermine substrate block, value column under the printed head N195A: printed row Kamine (uM) = 127; printed row kcat (s-1) = 4.9; printed row kcat/Kamine (mM-1 s-1) = 38.5. The value printed after the plus/minus sign in each of those cells is the printed uncertainty and is not an exported metric; the same column also prints kcat/KO2 (mM-1 s-1) = 327 and KO2 (uM) = 15, which are the oxygen parameters of the same table line.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4.9 in a row headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 4.9 s^(-1). Km: printed Table 2 cell 127 in a row headed Kamine (uM); 1 uM is 0.001 mM, so 127 / 1000 = 0.127 mM. kcat/Km: printed Table 2 cell 38.5 in a row headed kcat/Kamine (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 38.5 s^(-1)*mM^(-1). The catalog carries kcat 4.9 s^(-1), Km 0.127 mM and kcat_over_km 38.58267716535433 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, spermine block, value column under the printed head N195A: Kamine = 127 uM; kcat = 4.9 s-1; printed kcat/Kamine = 38.5 in a row headed kcat/Kamine (mM-1 s-1).

row_label: Table 2, spermine block, N195A column


assay_conditions_summary: pH 9; 298.15 K; buffer containing 10 percent glycerol

column_label: Table 2 (Steady-State Kinetic Parameters), N1-acetylspermine substrate block, value column under the printed head N195A: printed row Kamine (uM) = 104; printed row kcat (s-1) = 8.1; printed row kcat/Kamine (mM-1 s-1) = 78. The value printed after the plus/minus sign in each of those cells is the printed uncertainty and is not an exported metric; the same column also prints kcat/KO2 (mM-1 s-1) = 405 and KO2 (uM) = 20, which are the oxygen parameters of the same table line.

normalized_value_unit_evidence: kcat: printed Table 2 cell 8.1 in a row headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 8.1 s^(-1). Km: printed Table 2 cell 104 in a row headed Kamine (uM); 1 uM is 0.001 mM, so 104 / 1000 = 0.104 mM. kcat/Km: printed Table 2 cell 78 in a row headed kcat/Kamine (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 78.0 s^(-1)*mM^(-1). The catalog carries kcat 8.1 s^(-1), Km 0.104 mM and kcat_over_km 77.88461538461539 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, N1-acetylspermine block, value column under the printed head N195A: Kamine = 104 uM; kcat = 8.1 s-1; printed kcat/Kamine = 78 in a row headed kcat/Kamine (mM-1 s-1).

row_label: Table 2, N1-acetylspermine block, N195A column


column_label: Table 2 (Steady-State Kinetic Parameters), N1-acetylspermine substrate block, value column under the printed head D94N: printed row Kamine (uM) = 30; printed row kcat (s-1) = 9.7; printed row kcat/Kamine (mM-1 s-1) = 320. The value printed after the plus/minus sign in each of those cells is the printed uncertainty and is not an exported metric; the same column also prints kcat/KO2 (mM-1 s-1) = 100 and KO2 (uM) = 97, which are the oxygen parameters of the same table line.

normalized_value_unit_evidence: kcat: printed Table 2 cell 9.7 in a row headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 9.7 s^(-1). Km: printed Table 2 cell 30 in a row headed Kamine (uM); 1 uM is 0.001 mM, so 30 / 1000 = 0.03 mM. kcat/Km: printed Table 2 cell 320 in a row headed kcat/Kamine (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 320.0 s^(-1)*mM^(-1). The catalog carries kcat 9.7 s^(-1), Km 0.03 mM and kcat_over_km 323.3333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, N1-acetylspermine block, value column under the printed head D94N: Kamine = 30 uM; kcat = 9.7 s-1; printed kcat/Kamine = 320 in a row headed kcat/Kamine (mM-1 s-1).

row_label: Table 2, N1-acetylspermine block, D94N column


column_label: Table 2 (Steady-State Kinetic Parameters), N1-acetylspermine substrate block, value column under the printed head Fms1: printed row Kamine (uM) = 10.9; printed row kcat (s-1) = 15.1; printed row kcat/Kamine (mM-1 s-1) = 1400. The value printed after the plus/minus sign in each of those cells is the printed uncertainty and is not an exported metric; the same column also prints kcat/KO2 (mM-1 s-1) = 358 and KO2 (uM) = 43.6, which are the oxygen parameters of the same table line.

normalized_value_unit_evidence: kcat: printed Table 2 cell 15.1 in a row headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 15.1 s^(-1). Km: printed Table 2 cell 10.9 in a row headed Kamine (uM); 1 uM is 0.001 mM, so 10.9 / 1000 = 0.0109 mM. kcat/Km: printed Table 2 cell 1400 in a row headed kcat/Kamine (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 1400.0 s^(-1)*mM^(-1). The catalog carries kcat 15.1 s^(-1), Km 0.011 mM and kcat_over_km 1372.7272727272727 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, N1-acetylspermine block, value column under the printed head Fms1: Kamine = 10.9 uM; kcat = 15.1 s-1; printed kcat/Kamine = 1400 in a row headed kcat/Kamine (mM-1 s-1).

row_label: Table 2, N1-acetylspermine block, Fms1 wild type column


column_label: Table 2 (Steady-State Kinetic Parameters), spermine substrate block, value column under the printed head Fms1: printed row Kamine (uM) = 118; printed row kcat (s-1) = 39.0; printed row kcat/Kamine (mM-1 s-1) = 330. The value printed after the plus/minus sign in each of those cells is the printed uncertainty and is not an exported metric; the same column also prints kcat/KO2 (mM-1 s-1) = 428 and KO2 (uM) = 91, which are the oxygen parameters of the same table line.

normalized_value_unit_evidence: kcat: printed Table 2 cell 39.0 in a row headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 39.0 s^(-1). Km: printed Table 2 cell 118 in a row headed Kamine (uM); 1 uM is 0.001 mM, so 118 / 1000 = 0.118 mM. kcat/Km: printed Table 2 cell 330 in a row headed kcat/Kamine (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 330.0 s^(-1)*mM^(-1). The catalog carries kcat 39.0 s^(-1), Km 0.118 mM and kcat_over_km 330.5084745762712 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, spermine block, value column under the printed head Fms1: Kamine = 118 uM; kcat = 39.0 s-1; printed kcat/Kamine = 330 in a row headed kcat/Kamine (mM-1 s-1).

row_label: Table 2, spermine block, Fms1 wild type column


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N195A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 25°C, recombinant mutant N195A, with spermine

proof_lines: pH 9.0, 25°C, recombinant mutant N195A, with N1-acetylspermine


proof_lines: pH 9.0, 25°C, recombinant wild-type Fms1, with N1-acetylspermine

proof_lines: pH 9.0, 25°C, recombinant wild-type Fms1, with spermine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D94N to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 25°C, recombinant mutant D94N, with N1-acetylspermine

proof_lines: pH 9.0, 25°C, recombinant mutant D94N, with spermine


organism: Homo sapiens


substrate_name: alpha-methylspermidine

smiles: CC(CCNCCCCN)N

substrate: alpha-methylspermidine


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -9, so it is treated as a source-provided variant sequence.

assay_conditions_summary: pH 6


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O64411 and applied mutation signature E62Q with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 298.15 K; buffer Pichia pastoris | 0.2 M sodium phosphate

column_label: Table 1: Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris (Biochemistry 2005, 44(49): 16108-16120; journal page 16112, PDF page 5); printed column heads MPAO | kcat (spd) (s^-1) | kcat (spm) (s^-1) | kcat (spd)/kcat (spm) | Km (spd) (uM) | Km (spm) (uM) | kcat/Km (spd) (s^-1 uM^-1). Table 1, MPAO row Glu62Gln; columns kcat (spm) (s^-1) and Km (spm) (uM); kcat (spm) cell = 2.8; Km (spm) cell = 14.7; Table 1 has no kcat/Km (spm) column. captured primary segment: Table 1 (Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris), journal page 16112 (PDF page 5) | spermine (spm) | Glu62Gln MPAO, the site-directed Glu62Gln mutant of recombinant Zea mays polyamine oxidase expressed in Pichia pastoris | 0.2 M sodium phosphate buffer at pH 6.0, 25 °C, O2 at the air-saturated level | Table 1, row Glu62Gln, kcat (spm) = 2.8 s^-1 | Table 1, row Glu62Gln, Km (spm) = 14.7 uM | kcat/Km (spm): Table 1 prints no kcat/Km (spm) column and this article prints no kcat/Km value for spm oxidation by this enzyme form

normalized_value_unit_evidence: Km: printed Table 1 Km (spm) cell 14.7 uM; 1 uM is 1/1000 mM, so 14.7 / 1000 = 0.0147 mM; the export stores 0.0147 mM. kcat: printed Table 1 kcat (spm) cell 2.8 s^-1; already in s^-1, no unit conversion applies; the export stores 2.8 s^(-1). kcat/Km: Table 1 prints no kcat/Km (spm) cell; the quotient of the two printed cells is 2.8 / 0.0147 = 190.47619047619048 s^-1 mM^-1, which is the exported 190.47619047619048 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 16112, Table 1, MPAO row Glu62Gln: kcat (spm) = 2.8 s^-1; Km (spm) = 14.7 uM; Table 1 prints no kcat/Km (spm) column.

row_label: Table 1, MPAO row Glu62Gln


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O64411 and applied mutation signature E170Q with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris (Biochemistry 2005, 44(49): 16108-16120; journal page 16112, PDF page 5); printed column heads MPAO | kcat (spd) (s^-1) | kcat (spm) (s^-1) | kcat (spd)/kcat (spm) | Km (spd) (uM) | Km (spm) (uM) | kcat/Km (spd) (s^-1 uM^-1). Table 1, MPAO row Glu170Gln; columns kcat (spm) (s^-1) and Km (spm) (uM); kcat (spm) cell = 4.6; Km (spm) cell = 12.5; Table 1 has no kcat/Km (spm) column. captured primary segment: Table 1 (Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris), journal page 16112 (PDF page 5) | spermine (spm) | Glu170Gln MPAO, the site-directed Glu170Gln mutant of recombinant Zea mays polyamine oxidase expressed in Pichia pastoris | 0.2 M sodium phosphate buffer at pH 6.0, 25 °C, O2 at the air-saturated level | Table 1, row Glu170Gln, kcat (spm) = 4.6 s^-1 | Table 1, row Glu170Gln, Km (spm) = 12.5 uM | kcat/Km (spm): Table 1 prints no kcat/Km (spm) column and this article prints no kcat/Km value for spm oxidation by this enzyme form

normalized_value_unit_evidence: Km: printed Table 1 Km (spm) cell 12.5 uM; 1 uM is 1/1000 mM, so 12.5 / 1000 = 0.0125 mM; the export stores 0.0125 mM. kcat: printed Table 1 kcat (spm) cell 4.6 s^-1; already in s^-1, no unit conversion applies; the export stores 4.6 s^(-1). kcat/Km: Table 1 prints no kcat/Km (spm) cell; the quotient of the two printed cells is 4.6 / 0.0125 = 367.99999999999994 s^-1 mM^-1, which is the exported 367.99999999999994 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 16112, Table 1, MPAO row Glu170Gln: kcat (spm) = 4.6 s^-1; Km (spm) = 12.5 uM; Table 1 prints no kcat/Km (spm) column.

row_label: Table 1, MPAO row Glu170Gln


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O64411 and applied mutation signature Y298F with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris (Biochemistry 2005, 44(49): 16108-16120; journal page 16112, PDF page 5); printed column heads MPAO | kcat (spd) (s^-1) | kcat (spm) (s^-1) | kcat (spd)/kcat (spm) | Km (spd) (uM) | Km (spm) (uM) | kcat/Km (spd) (s^-1 uM^-1). Table 1, MPAO row Tyr298Phe; columns kcat (spm) (s^-1) and Km (spm) (uM); kcat (spm) cell = 7.7; Km (spm) cell = 1.2; Table 1 has no kcat/Km (spm) column. captured primary segment: Table 1 (Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris), journal page 16112 (PDF page 5) | spermine (spm) | Tyr298Phe MPAO, the site-directed Tyr298Phe mutant of recombinant Zea mays polyamine oxidase expressed in Pichia pastoris | 0.2 M sodium phosphate buffer at pH 6.0, 25 °C, O2 at the air-saturated level | Table 1, row Tyr298Phe, kcat (spm) = 7.7 s^-1 | Table 1, row Tyr298Phe, Km (spm) = 1.2 uM | kcat/Km (spm): Table 1 prints no kcat/Km (spm) column and this article prints no kcat/Km value for spm oxidation by this enzyme form

normalized_value_unit_evidence: Km: printed Table 1 Km (spm) cell 1.2 uM; 1 uM is 1/1000 mM, so 1.2 / 1000 = 0.0012 mM; the export stores 0.0012 mM. kcat: printed Table 1 kcat (spm) cell 7.7 s^-1; already in s^-1, no unit conversion applies; the export stores 7.7 s^(-1). kcat/Km: Table 1 prints no kcat/Km (spm) cell; the quotient of the two printed cells is 7.7 / 0.0012 = 6416.666666666667 s^-1 mM^-1, which is the exported 6416.666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 16112, Table 1, MPAO row Tyr298Phe: kcat (spm) = 7.7 s^-1; Km (spm) = 1.2 uM; Table 1 prints no kcat/Km (spm) column.

row_label: Table 1, MPAO row Tyr298Phe


column_label: Table 1: Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris (Biochemistry 2005, 44(49): 16108-16120; journal page 16112, PDF page 5); printed column heads MPAO | kcat (spd) (s^-1) | kcat (spm) (s^-1) | kcat (spd)/kcat (spm) | Km (spd) (uM) | Km (spm) (uM) | kcat/Km (spd) (s^-1 uM^-1). Table 1, MPAO row Glu62Gln; columns kcat (spd) (s^-1), Km (spd) (uM) and kcat/Km (spd) (s^-1 uM^-1); kcat (spd) cell = 8.3; Km (spd) cell = 24.6; kcat/Km (spd) cell = 0.3. captured primary segment: Table 1 (Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris), journal page 16112 (PDF page 5) | spermidine (spd) | Glu62Gln MPAO, the site-directed Glu62Gln mutant of recombinant Zea mays polyamine oxidase expressed in Pichia pastoris | 0.2 M sodium phosphate buffer at pH 6.0, 25 °C, O2 at the air-saturated level | Table 1, row Glu62Gln, kcat (spd) = 8.3 s^-1 | Table 1, row Glu62Gln, Km (spd) = 24.6 uM | Table 1, row Glu62Gln, kcat/Km (spd) = 0.3 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 Km (spd) cell 24.6 uM; 1 uM is 1/1000 mM, so 24.6 / 1000 = 0.0246 mM; the export stores 0.0246 mM. kcat: printed Table 1 kcat (spd) cell 8.3 s^-1; already in s^-1, no unit conversion applies; the export stores 8.3 s^(-1). kcat/Km: printed Table 1 kcat/Km (spd) cell 0.3 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.3 x 1000 = 300.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 8.3 / 0.0246 = 337.3983739837399 s^-1 mM^-1, against the printed catalytic-efficiency cell 300.0 s^-1 mM^-1, which is that quotient rounded to the one decimal the column prints; the export stores 337.3983739837399 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 16112, Table 1, MPAO row Glu62Gln: kcat (spd) = 8.3 s^-1; Km (spd) = 24.6 uM; printed kcat/Km (spd) = 0.3 s^-1 uM^-1.


column_label: Table 1: Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris (Biochemistry 2005, 44(49): 16108-16120; journal page 16112, PDF page 5); printed column heads MPAO | kcat (spd) (s^-1) | kcat (spm) (s^-1) | kcat (spd)/kcat (spm) | Km (spd) (uM) | Km (spm) (uM) | kcat/Km (spd) (s^-1 uM^-1). Table 1, MPAO row Tyr298Phe; columns kcat (spd) (s^-1), Km (spd) (uM) and kcat/Km (spd) (s^-1 uM^-1); kcat (spd) cell = 16.5; Km (spd) cell = 0.7; kcat/Km (spd) cell = 23.6. captured primary segment: Table 1 (Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris), journal page 16112 (PDF page 5) | spermidine (spd) | Tyr298Phe MPAO, the site-directed Tyr298Phe mutant of recombinant Zea mays polyamine oxidase expressed in Pichia pastoris | 0.2 M sodium phosphate buffer at pH 6.0, 25 °C, O2 at the air-saturated level | Table 1, row Tyr298Phe, kcat (spd) = 16.5 s^-1 | Table 1, row Tyr298Phe, Km (spd) = 0.7 uM | Table 1, row Tyr298Phe, kcat/Km (spd) = 23.6 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 Km (spd) cell 0.7 uM; 1 uM is 1/1000 mM, so 0.7 / 1000 = 0.0007 mM; the export stores 0.0007 mM. kcat: printed Table 1 kcat (spd) cell 16.5 s^-1; already in s^-1, no unit conversion applies; the export stores 16.5 s^(-1). kcat/Km: printed Table 1 kcat/Km (spd) cell 23.6 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 23.6 x 1000 = 23600.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 16.5 / 0.0007 = 23571.428571428572 s^-1 mM^-1, against the printed catalytic-efficiency cell 23600.0 s^-1 mM^-1, which is that quotient rounded to the one decimal the column prints; the export stores 23571.428571428572 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 16112, Table 1, MPAO row Tyr298Phe: kcat (spd) = 16.5 s^-1; Km (spd) = 0.7 uM; printed kcat/Km (spd) = 23.6 s^-1 uM^-1.


column_label: Table 1: Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris (Biochemistry 2005, 44(49): 16108-16120; journal page 16112, PDF page 5); printed column heads MPAO | kcat (spd) (s^-1) | kcat (spm) (s^-1) | kcat (spd)/kcat (spm) | Km (spd) (uM) | Km (spm) (uM) | kcat/Km (spd) (s^-1 uM^-1). Table 1, MPAO row Glu170Gln; columns kcat (spd) (s^-1), Km (spd) (uM) and kcat/Km (spd) (s^-1 uM^-1); kcat (spd) cell = 17.3; Km (spd) cell = 16.7; kcat/Km (spd) cell = 1.0. captured primary segment: Table 1 (Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris), journal page 16112 (PDF page 5) | spermidine (spd) | Glu170Gln MPAO, the site-directed Glu170Gln mutant of recombinant Zea mays polyamine oxidase expressed in Pichia pastoris | 0.2 M sodium phosphate buffer at pH 6.0, 25 °C, O2 at the air-saturated level | Table 1, row Glu170Gln, kcat (spd) = 17.3 s^-1 | Table 1, row Glu170Gln, Km (spd) = 16.7 uM | Table 1, row Glu170Gln, kcat/Km (spd) = 1.0 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 Km (spd) cell 16.7 uM; 1 uM is 1/1000 mM, so 16.7 / 1000 = 0.0167 mM; the export stores 0.0167 mM. kcat: printed Table 1 kcat (spd) cell 17.3 s^-1; already in s^-1, no unit conversion applies; the export stores 17.3 s^(-1). kcat/Km: printed Table 1 kcat/Km (spd) cell 1.0 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.0 x 1000 = 1000.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 17.3 / 0.0167 = 1035.9281437125749 s^-1 mM^-1, against the printed catalytic-efficiency cell 1000.0 s^-1 mM^-1, which is that quotient rounded to the one decimal the column prints; the export stores 1035.9281437125749 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 16112, Table 1, MPAO row Glu170Gln: kcat (spd) = 17.3 s^-1; Km (spd) = 16.7 uM; printed kcat/Km (spd) = 1.0 s^-1 uM^-1.


column_label: Table 1: Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris (Biochemistry 2005, 44(49): 16108-16120; journal page 16112, PDF page 5); printed column heads MPAO | kcat (spd) (s^-1) | kcat (spm) (s^-1) | kcat (spd)/kcat (spm) | Km (spd) (uM) | Km (spm) (uM) | kcat/Km (spd) (s^-1 uM^-1). Table 1, MPAO row wild-type; columns kcat (spm) (s^-1) and Km (spm) (uM); kcat (spm) cell = 32.9; Km (spm) cell = 1.6; Table 1 has no kcat/Km (spm) column. captured primary segment: Table 1 (Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris), journal page 16112 (PDF page 5) | spermine (spm) | wild-type MPAO, recombinant wild-type Zea mays polyamine oxidase expressed in Pichia pastoris | 0.2 M sodium phosphate buffer at pH 6.0, 25 °C, O2 at the air-saturated level | Table 1, row wild-type, kcat (spm) = 32.9 s^-1 | Table 1, row wild-type, Km (spm) = 1.6 uM | kcat/Km (spm): Table 1 prints no kcat/Km (spm) column and this article prints no kcat/Km value for spm oxidation by this enzyme form

normalized_value_unit_evidence: Km: printed Table 1 Km (spm) cell 1.6 uM; 1 uM is 1/1000 mM, so 1.6 / 1000 = 0.0016 mM; the export stores 0.0016 mM. kcat: printed Table 1 kcat (spm) cell 32.9 s^-1; already in s^-1, no unit conversion applies; the export stores 32.9 s^(-1). kcat/Km: Table 1 prints no kcat/Km (spm) cell; the quotient of the two printed cells is 32.9 / 0.0016 = 20562.499999999996 s^-1 mM^-1, which is the exported 20562.499999999996 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 16112, Table 1, MPAO row wild-type: kcat (spm) = 32.9 s^-1; Km (spm) = 1.6 uM; Table 1 prints no kcat/Km (spm) column.

row_label: Table 1, MPAO row wild-type


column_label: Table 1: Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris (Biochemistry 2005, 44(49): 16108-16120; journal page 16112, PDF page 5); printed column heads MPAO | kcat (spd) (s^-1) | kcat (spm) (s^-1) | kcat (spd)/kcat (spm) | Km (spd) (uM) | Km (spm) (uM) | kcat/Km (spd) (s^-1 uM^-1). Table 1, MPAO row wild-type; columns kcat (spd) (s^-1), Km (spd) (uM) and kcat/Km (spd) (s^-1 uM^-1); kcat (spd) cell = 50.2; Km (spd) cell = 2.1; kcat/Km (spd) cell = 23.9. captured primary segment: Table 1 (Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris), journal page 16112 (PDF page 5) | spermidine (spd) | wild-type MPAO, recombinant wild-type Zea mays polyamine oxidase expressed in Pichia pastoris | 0.2 M sodium phosphate buffer at pH 6.0, 25 °C, O2 at the air-saturated level | Table 1, row wild-type, kcat (spd) = 50.2 s^-1 | Table 1, row wild-type, Km (spd) = 2.1 uM | Table 1, row wild-type, kcat/Km (spd) = 23.9 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 Km (spd) cell 2.1 uM; 1 uM is 1/1000 mM, so 2.1 / 1000 = 0.0021 mM; the export stores 0.0021 mM. kcat: printed Table 1 kcat (spd) cell 50.2 s^-1; already in s^-1, no unit conversion applies; the export stores 50.2 s^(-1). kcat/Km: printed Table 1 kcat/Km (spd) cell 23.9 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 23.9 x 1000 = 23900.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 50.2 / 0.0021 = 23904.76190476191 s^-1 mM^-1, against the printed catalytic-efficiency cell 23900.0 s^-1 mM^-1, which is that quotient rounded to the one decimal the column prints; the export stores 23904.76190476191 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 16112, Table 1, MPAO row wild-type: kcat (spd) = 50.2 s^-1; Km (spd) = 2.1 uM; printed kcat/Km (spd) = 23.9 s^-1 uM^-1.


proof_lines:
pH 7.5, 25°C, recombinant ZmPAO
pH 6.0, 25°C, native enzyme
pH 6.5, 30°C


proof_lines:
pH 7.5, 25°C, recombinant AtPAO2
pH 6.0, 25°C, native enzyme
Raw SKiD Env: Temp=25°C, pH=6


assay_conditions_summary: pH 8

proof_lines:
SMO/PAOh1
37°C, pH 8.0
pH 8.3, 25°C


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature H82Q with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

proof_lines:
mutant H82Q, pH 8.5, 25°C
pH 8.5, 25°C, recombinant mutant H82Q


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K367M to reconstruct the assayed variant sequence.

proof_lines:
mutant K367M, pH 8.5, 25°C
pH 8.5, 25°C, recombinant mutant K367M


proof_lines: mutant enzyme deprived of all but two cysteine residues (C263/C429), pH 8.3, 25°C


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

proof_lines: pH 8.5, 25°C, recombinant wild-type enzyme


proof_lines:
pH 9, 25°C
pH 8.0
without benzyladehyde, hPAO


proof_lines:
addition of 5 mM benzyldehyde, hPAO
without benzyladehyde, hPAO


proof_lines: kcat is 800 sec(-1) with 4-methylaminobutanoate as substrate. kcat is 4 sec(-1) with sarcosine as substrate.


proof_lines: isozyme SMO1, pH 8.0, temperature not specified in the publication


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

proof_lines: pH 8.0, 37°C, purified recombinant-tagged form enzyme

proof_lines: isozyme SMOalpha, pH 8.0, temperature not specified in the publication


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

proof_lines: pH 8.5, mutant mSMOmuDELTA (with a deletion of the nuclear domain A)


proof_lines: pH 8.0, temperature not specified in the publication


substrate_name: O2; N1-Acetylspermine; H2O

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

source_databases_merged: sabio_rk brenda skid

substrate: O2; N1-Acetylspermine; H2O


substrate_name: N1-Acetylspermidine; H2O; O2

substrate: N1-Acetylspermidine; H2O; O2


organism: Hordeum vulgare

substrate_name: Spermine; H2O; O2

substrate: Spermine; H2O; O2


substrate_name: H2O; Spermine; O2

substrate: H2O; Spermine; O2


substrate_name: O2; H2O; Bis(3-aminopropyl)amine

substrate: O2; H2O; Bis(3-aminopropyl)amine


enzyme_display_name: L-saccharopine oxidase

organism: Schizosaccharomyces pombe

enzyme: L-saccharopine oxidase


smiles: CC(O)=NCCCNCCCCN


smiles: CC(O)=NCCCNCCCCNCCCN


smiles: NCCCNCCCN


smiles: NCCCNCCCNCCCN


substrate_name: spermidine

smiles: NCCCCNCCCN

substrate: spermidine


substrate_name: spermine

smiles: NCCCNCCCCNCCCN

substrate: spermine


substrate_name: thermospermine

smiles: NCCCCNCCCNCCCN

substrate: thermospermine


proof_lines: without benzyladehyde, kinetic value for the methylated end, hPAO

proof_lines: without benzyladehyde, kinetic value for the unmethylated end, hPAO


enzyme_display_name: N(1)-acetylpolyamine oxidase

enzyme: N(1)-acetylpolyamine oxidase


substrate_name: H2O; O2; Spermine

proof_lines:
pH 6.5, 25°C
pH 6.0, 25°C
N1-acetyl-3-aminopropyl-4-aminobutanal

source_databases_merged: sabio_rk brenda skid uniprot

substrate: H2O; O2; Spermine


substrate_name: Unknown

substrate: Unknown


proof_lines: pH 7.2, 37°C, with spermine as substrate


substrate_name: alpha-methylspermine

proof_lines: without benzyladehyde, kinetic value for the unmethylated end, hSMO

substrate: alpha-methylspermine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D94N to reconstruct the assayed variant sequence.


column_label: Table I row N1-AcSpm, pH 7.5 columns kcat, Km, and kcat/Km

table_label: Table I. Kinetic parameters of recombinant AtPAO5


substrate_name: norspermine

column_label: Table I row NorSpm, pH 6.5 columns kcat, Km, and kcat/Km

row_label: NorSpm

substrate: norspermine


column_label: Table I row NorSpm, pH 7.5 columns kcat, Km, and kcat/Km


column_label: Table I row Spd, pH 7.5 columns kcat, Km, and kcat/Km

row_label: Spd


column_label: Table I row Spm, pH 7.5 columns kcat, Km, and kcat/Km

row_label: Spm


column_label: Table I row T-Spm, pH 7.5 columns kcat, Km, and kcat/Km

row_label: T-Spm


proof_lines:
pH 7.6, 30°C
Raw SKiD Env: Temp=30°C, pH=9
Raw SKiD Env: Temp=30°C, pH=7.6


smiles: CC(=O)NCCCNCCCCNCCCN

proof_lines:
pH 7.6, 30°C
pH 7.5, 37°C
Raw SKiD Env: Temp=30°C, pH=7.6


smiles: CC(=O)NCCCNCCCCN

proof_lines:
pH 7.6, 30°C
Raw SKiD Env: Temp=30°C, pH=7.6


smiles: CCNCCCNCCCNCCCNCC


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


smiles: C(CCNCCCN)CNCCCN

column_label: Table I row Spm, Km column.

normalized_value_unit_evidence: Spm normalized paper Km=0.11 mM.

raw_value_unit_evidence: PMC HTML pmid_16778015_pmc_html_text.txt lines 313-337 report Table I kinetic constants: Spm Km 0.11 +/- 0.02 mM.

row_label: Spm / spermine

table_label: Table I


smiles: C(CN)CNCCCNCCCN

column_label: Table I row Nor-Spm, Km column.

normalized_value_unit_evidence: Nor-Spm normalized paper Km=0.09 mM.

raw_value_unit_evidence: PMC HTML pmid_16778015_pmc_html_text.txt lines 313-337 report Table I kinetic constants: Nor-Spm Km 0.09 +/- 0.01 mM.

row_label: Nor-Spm / norspermine


column_label: Table I row N1-acetyl-Spm, Km column.

normalized_value_unit_evidence: N1-acetyl-Spm normalized paper Km=0.47 mM.

raw_value_unit_evidence: PMC HTML pmid_16778015_pmc_html_text.txt lines 313-337 report Table I kinetic constants: N1-acetyl-Spm Km 0.47 +/- 0.02 mM.


enzyme_display_name: Polyamine oxidase 3

column_label: Table 2 row Nor-Spm / AtPAO3, Km column: 45 +/- 12 uM

raw_value_unit_evidence: Km raw_value=45 +/- 12 raw_unit=uM

row_label: Nor-Spm / AtPAO3

enzyme: Polyamine oxidase 3


column_label: Table 2 row Therm-Spm / AtPAO3, Km column: 50 +/- 10 uM

raw_value_unit_evidence: Km raw_value=50 +/- 10 raw_unit=uM

row_label: Therm-Spm / AtPAO3


column_label: Table 2 row Therm-Spm / AtPAO1, Km column: 20 +/- 3.0 uM

raw_value_unit_evidence: Km raw_value=20 +/- 3.0 raw_unit=uM

row_label: Therm-Spm / AtPAO1


smiles: C(CN)CNCCNCCCN

proof_lines:
spermine
spermidine
acetylated polyamines


smiles: C(CCNCCCN)CN


proof_lines: AtPAO3 spermidine Spd


proof_lines: AtPAO3 spermine Spm


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N313T with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature N313L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature N313A 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_rest_accession:Q8C0L6 and applied mutation signature N313D to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Wild-Type and Mutant Murine Polyamine Oxidases), N1-acetylspermine block, N313D column: parameter row 'Ks,app (mM)' = 0.2; parameter row 'kcat,app (s^-1)' = 27; parameter row 'kcat/Ks (mM^-1 s^-1)' = 137.

normalized_value_unit_evidence: kcat: printed Table 2 cell 27 s^-1 (row kcat,app); the column head prints s^-1, so no unit conversion applies and the paper value is 27 s^(-1); the exported value is 27.0 s^(-1). Km: printed Table 2 cell 0.2 mM (row Ks,app, the apparent Michaelis constant); the column head prints mM, so no unit conversion applies and the paper value is 0.2 mM; the exported value is 0.2 mM. kcat/Km: printed Table 2 cell 137 mM^-1 s^-1 (row kcat/Ks); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell is 137 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 27 / 0.2 = 135.0 s^-1 mM^-1, which is the exported kcat_over_km 135.0; the printed efficiency cell 137 is the paper's own fitted value and is the value proposed for the catalog.

raw_value_unit_evidence: Table 2, N1-acetylspermine block, N313D column: kcat,app = 27 s^-1; Ks,app = 0.2 mM; printed kcat/Ks = 137 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8C0L6 and applied mutation signature N313T to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Wild-Type and Mutant Murine Polyamine Oxidases), N1-acetylspermine block, N313T column: parameter row 'Ks,app (mM)' = 0.12; parameter row 'kcat,app (s^-1)' = 22; parameter row 'kcat/Ks (mM^-1 s^-1)' = 175.

normalized_value_unit_evidence: kcat: printed Table 2 cell 22 s^-1 (row kcat,app); the column head prints s^-1, so no unit conversion applies and the paper value is 22 s^(-1); the exported value is 22.0 s^(-1). Km: printed Table 2 cell 0.12 mM (row Ks,app, the apparent Michaelis constant); the column head prints mM, so no unit conversion applies and the paper value is 0.12 mM; the exported value is 0.12 mM. kcat/Km: printed Table 2 cell 175 mM^-1 s^-1 (row kcat/Ks); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell is 175 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 22 / 0.12 = 183.33333333333334 s^-1 mM^-1, which is the exported kcat_over_km 183.33333333333334; the printed efficiency cell 175 is the paper's own fitted value and is the value proposed for the catalog.

raw_value_unit_evidence: Table 2, N1-acetylspermine block, N313T column: kcat,app = 22 s^-1; Ks,app = 0.12 mM; printed kcat/Ks = 175 mM^-1 s^-1.


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


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


smiles: C(CCNCCCNCCCN)CN


enzyme_display_name: Probable polyamine oxidase 4

column_label: Table 2 row Spd / AtPAO4, Km column: 139 +/- 18 uM

raw_value_unit_evidence: Km raw_value=139 +/- 18 raw_unit=uM

row_label: Spd / AtPAO4

enzyme: Probable polyamine oxidase 4


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H82Q with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K367M with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8; cofactor FAD


proof_lines:
spermine oxidase
SMOX
thermal denaturation


proof_lines:
pH 7.4, 25°C
Raw SKiD Env: Temp=25°C, pH=9.35


organism: Lathyrus oleraceus

substrate_name: tetrahydropteroylmonoglutamate

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

proof_lines: varying concentration of tetrahydropteroylmonoglutamate

substrate: tetrahydropteroylmonoglutamate


substrate_name: Tetrahydropteroylpentaglutamate

substrate: Tetrahydropteroylpentaglutamate


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


enzyme_display_name: UniProt O42629

organism: Aspergillus fumigatus

substrate_name: fructosyl propylamine

enzyme: UniProt O42629

substrate: fructosyl propylamine


enzyme_display_name: UniProt P78573

substrate_name: fructosyl adamantanamine

enzyme: UniProt P78573

substrate: fructosyl adamantanamine


substrate_name: fructosyl glycine

substrate: fructosyl glycine


enzyme_display_name: fructosyl amine oxidase (glucosone-forming)

organism: Arthrobacter sp. 2-4-1

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T60A/A188G/M244L/N257S/L261M to reconstruct the assayed variant sequence.


enzyme: fructosyl amine oxidase (glucosone-forming)


substrate_name: fructosyl L-valine

substrate: fructosyl L-valine


enzyme_display_name: alanine dehydrogenase

organism: Lysinibacillus sphaericus

substrate_name: NAD+

enzyme: alanine dehydrogenase

substrate: NAD+


substrate_name: pyruvate

substrate: pyruvate


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


smiles: N


organism: Aspergillus sp.


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


proof_lines: amadoriase II mutant R112E/R114E, pH 8, 37°C


proof_lines: mutant R114S, 30°C, pH not specified in the publication


proof_lines: mutant E71S, 30°C, pH not specified in the publication


proof_lines: mutant E71R, 30°C, pH not specified in the publication


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


proof_lines: mutant Y60F, 30°C, pH not specified in the publication


proof_lines: mutant K368M, 30°C, pH not specified in the publication


proof_lines: mutant E71R/R114E, 30°C, pH not specified in the publication


proof_lines: mutant R112E, 30°C, pH not specified in the publication


proof_lines: mutant R114E, 30°C, pH not specified in the publication


substrate_name: L-saccharopine

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

proof_lines:
Fap2
L-saccharopine oxidase
Schizosaccharomyces pombe

substrate: L-saccharopine


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

enzyme: glutamate dehydrogenase [NAD(P)+]


substrate_name: alpha-ketoglutarate

substrate: alpha-ketoglutarate


proof_lines: mutant R112W, pH 8, temperature not specified in the publication


substrate_name: fructosyl poly-L-lysine

proof_lines: wild-type, pH 8, temperature not specified in the publication

substrate: fructosyl poly-L-lysine


proof_lines: mutant R112Y, pH 8, temperature not specified in the publication


proof_lines: mutant R112Y/V113F/R114S, pH 8, temperature not specified in the publication


proof_lines: mutant N63D/K64Q/R112W/V113F/R114S, pH 8, temperature not specified in the publication