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.


organism: Zea mays

substrate_name: spermidine

source_db: brenda

verification_status: verified

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

smiles: C(CCNCCCN)CN

mutation_type: substitution

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 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.

row_label: Table 1, MPAO row Glu170Gln

data_origin: experimental

substrate: spermidine

status: verified

source: brenda


substrate_name: spermine

mutation_signature: Unknown

kcat_over_km_origin: calculated

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

smiles: C(CCNCCCN)CNCCCN

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

substrate: spermine


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.


verification_status: unverified

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

sequence_source: multiple

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

source_databases_merged: brenda skid uniprot

status: unverified


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


enzyme_display_name: spermine oxidase

organism: Homo sapiens

smiles: CC(=O)NCCCNCCCCNCCCN

assay_conditions_summary: pH 8

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

source_databases_merged: brenda uniprot

enzyme: spermine oxidase


km_display: Not reported

kcat_over_km_display: Not reported

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


organism: Mus musculus

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


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


enzyme_display_name: N1-acetylpolyamine oxidase

smiles: CC(=O)NCCCNCCCCN

assay_conditions_summary: pH 9

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

enzyme: N1-acetylpolyamine oxidase


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


organism: Paenarthrobacter nicotinovorans

source_db: uniprot

kcat_display: Not reported

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

source: uniprot


substrate_name: sarcosine

smiles: CNCC(=O)O

substrate: sarcosine


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.

mutation_type: deletion

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

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

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: non-specific polyamine oxidase

organism: Saccharomyces cerevisiae

enzyme: non-specific polyamine oxidase


enzyme_display_name: L-saccharopine oxidase

organism: Schizosaccharomyces pombe

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

enzyme: L-saccharopine oxidase


organism: Oryza sativa

source_db: oed

smiles: CC(O)=NCCCNCCCCN

source: oed


smiles: CC(O)=NCCCNCCCCNCCCN


substrate_name: norspermidine

smiles: NCCCNCCCN

substrate: norspermidine


substrate_name: norspermine

smiles: NCCCNCCCNCCCN

substrate: norspermine


smiles: NCCCCNCCCN


smiles: NCCCNCCCCNCCCN


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


enzyme_display_name: Polyamine oxidase 1

substrate_name: Unknown

enzyme: Polyamine oxidase 1

substrate: Unknown


organism: Bos taurus

ki_unit: mM

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


verification_status: corrected

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; 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 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

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.

status: corrected


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), 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 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


sequence_variant_note: Resolved canonical sequence from uniprot_accession 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 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


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


organism: Arabidopsis thaliana

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


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

row_label: NorSpm


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


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


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


smiles: CCNCCCNCCCNCCCNCC


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


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

table_label: Table 2

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


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.

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), 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.

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_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

smiles: C(CCNCCCN)CN

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


smiles: C(CCNCCCN)CNCCCN


smiles: CC(=O)NCCCNCCCCNCCCN


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.


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

assay_conditions_summary: pH 8; cofactor FAD


organism: Synechocystis sp. PCC 6803


proof_lines:
spermine oxidase
SMOX
thermal denaturation


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

source_databases_merged: brenda skid


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

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt O42629

substrate: fructosyl propylamine

source: skid


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+

assay_conditions_summary: cofactor 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


substrate_name: fructosyl L-phenylalanine

substrate: fructosyl L-phenylalanine


organism: Ulocladium sp. JS-103

proof_lines: mutant R94W, pH 8.0, temperature not specified in the publication


proof_lines: mutant R94F, pH 8.0, temperature not specified in the publication


proof_lines: mutant R94L, pH 8.0, temperature not specified in the publication


proof_lines: wild-type, pH 7.5, temperature not specified in the publication


substrate_name: fructosyl-L-lysine

substrate: fructosyl-L-lysine


organism: Fusarium oxysporum f. sp. raphani

proof_lines: mutant K373W, pH 8.0, temperature not specified in the publication

proof_lines: mutant K373W, presence of 20 mM MgCl2, pH 8.0, temperature not specified in the publication


proof_lines: mutant K373M, pH 8.0, temperature not specified in the publication


proof_lines: mutant K373T, pH 8.0, temperature not specified in the publication


proof_lines: mutant K373V, pH 8.0, temperature not specified in the publication


proof_lines: mutant K373R, pH 8.0, temperature not specified in the publication


substrate_name: gamma-fructosyl-aminobutanoate

proof_lines: wild-type, pH 8.0, temperature not specified in the publication

proof_lines: wild-type, presence of 20 mM MgCl2, pH 8.0, temperature not specified in the publication

substrate: gamma-fructosyl-aminobutanoate


organism: Agrobacterium tumefaciens


proof_lines:
wild-type, pH 7.4, 37°C
amadoriase II wild-type, pH 8, 37°C


proof_lines:
amadoriase I, pH 7.4, 37°C
amadoriase II, pH 7.4, 37°C


organism: Pichia sp. N1-1

proof_lines:
mutant N47A, pH 7, 23°C
mutant N47A, pH 7, 25°C


proof_lines:
wild-type, pH 7, 23°C
wild-type, pH 7, 25°C


enzyme_display_name: fructosyl amine oxidase (fructosamine-forming)

organism: Pseudomonas sp.


substrate_name: deoxy-D-fructosyl-Lys-Ser

substrate: deoxy-D-fructosyl-Lys-Ser


organism: Aspergillus oryzae

substrate_name: Nalpha-benzyloxycarbonyl-L-lysine

proof_lines: isoform FAOD-Ao1, pH 8.5, temperature not specified in the publication

substrate: Nalpha-benzyloxycarbonyl-L-lysine


proof_lines: pH 8.5, temperature not specified in the publication


enzyme_display_name: Sarcosine oxidase subunit alpha

organism: Corynebacterium sp. (strain U-96)

substrate_name: sarcosine (at pH 8.3)

smiles: CNCC(=O)O

proof_lines: kcat is 5.8 sec(-1) with sarcosine as substrate (at pH 8.3). kcat is 3.0 sec(-1) with sarcosine as substrate (at pH 7.0). kcat is 2.1 sec(-1) with N-methyl-L-alanine as substrate (at pH 8.3). kcat is 1.8 sec(-1) with N-methyl-L-alanine as s

enzyme: Sarcosine oxidase subunit alpha

substrate: sarcosine (at pH 8.3)


substrate_name: N-methyl-L-alanine (at pH 8.3)

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

substrate: N-methyl-L-alanine (at pH 8.3)


substrate_name: oxygen

smiles: O=O

substrate: oxygen


enzyme_display_name: Sarcosine oxidase subunit gamma

enzyme: Sarcosine oxidase subunit gamma


enzyme_display_name: Sarcosine oxidase subunit delta

enzyme: Sarcosine oxidase subunit delta


enzyme_display_name: Sarcosine oxidase subunit beta

enzyme: Sarcosine oxidase subunit beta


substrate_name: N-ethyl-L-glycine (at pH 7.0)

assay_conditions_summary: pH 7

substrate: N-ethyl-L-glycine (at pH 7.0)


organism: Paenarthrobacter nicotinovorans

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

proof_lines: kcat is 1230 sec(-1) with 4-methylaminobutanoate as substrate. kcat is 878 sec(-1) with 4-aminobutanoate as substrate.


enzyme_display_name: coenzyme F420H2 oxidase

organism: Methanobrevibacter arboriphilus

column_label: The abstract reports the apparent Km for O2 was 2 microM.

raw_value_unit_evidence: Km raw_value=2 microM raw_unit=microM

row_label: Prose segment: O2 Km

table_label: PubMed PMID 15340796 abstract

enzyme: coenzyme F420H2 oxidase


substrate_name: reduced coenzyme F420

column_label: Table 2 reports apparent Km=30 microM in the F420H2 (40 microM O2) row and FprA M. arboriphilus column.

raw_value_unit_evidence: Km raw_value=30 microM raw_unit=microM

row_label: Apparent Km (microM): F420H2 (40 microM O2)

table_label: Table 2, journal page 133 (PDF page 8)

substrate: reduced coenzyme F420


organism: Methanothermobacter marburgensis

column_label: Table 2 reports apparent Km=2 microM in the O2 (30 microM F420H2) row and the FprA M. marburgensis column.

row_label: Apparent Km (microM): O2 (30 microM F420H2)


column_label: Table 2 reports apparent Km=30 microM in the F420H2 (40 microM O2) row and the FprA M. marburgensis column.


substrate_name: fructosyl propylamine

substrate: fructosyl propylamine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D295C/K303C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H106S/G150S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S67C/P121C to reconstruct the assayed variant sequence.


organism: Corynebacterium sp. U-96

substrate_name: sarcosine

substrate: sarcosine


enzyme_display_name: leucine dehydrogenase

substrate_name: NAD+

enzyme: leucine dehydrogenase

substrate: NAD+


substrate_name: L-Leu

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

substrate: L-Leu


substrate_name: L-Val

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

substrate: L-Val


substrate_name: N-Methyl-L-alanine

proof_lines:
at pH 7.0 and 37°C
at pH 8.3 and 37°C

substrate: N-Methyl-L-alanine


substrate_name: N-ethyl-glycine

proof_lines:
at pH 7.0 and 37°C
at pH 8.0 and 25°C

substrate: N-ethyl-glycine


proof_lines:
at pH 8.3 and 37°C
at pH 7.0 and 37°C


substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


substrate_name: ferricyanide

substrate: ferricyanide


enzyme_display_name: glutamate synthase (NADH)

organism: Oryza sativa

substrate_name: L-glutamine

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

enzyme: glutamate synthase (NADH)

substrate: L-glutamine


substrate_name: NADH

substrate: NADH


enzyme_display_name: dihydrofolate reductase

organism: Neisseria gonorrhoeae

enzyme: dihydrofolate reductase


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: Coenzyme F420H(2) oxidase

substrate_name: F420H(2) (at an O(2) concentration of 40 uM)

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

enzyme: Coenzyme F420H(2) oxidase


organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)

substrate: F420H(2) (at an O(2) concentration of 40 uM)


organism: Aspergillus fumigatus

substrate_name: fructosyl-L-lysine

substrate: fructosyl-L-lysine


substrate_name: fructosyl L-valine

substrate: fructosyl L-valine


enzyme_display_name: glutamate synthase (ferredoxin)

enzyme: glutamate synthase (ferredoxin)


substrate_name: reduced ferredoxin

proof_lines:
in etiolated leaf tissue
in green leaf tissue
in root tissue

substrate: reduced ferredoxin


organism: Parvimonas micra

substrate_name: pyridoxal 5'-phosphate

substrate: pyridoxal 5'-phosphate


substrate_name: bicarbonate

substrate: bicarbonate


substrate_name: glycine

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

substrate: glycine


organism: Pneumocystis carinii

proof_lines:
pH 7.4, 37°C, mutant K37Q
recombinant mutant K37Q, pH 7.4, 37°C


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


proof_lines:
pH 7.4, 37°C, mutant K37Q
mutant K37Q enzyme, pH 7.4, 37°C


enzyme_display_name: pyrroline-5-carboxylate reductase

organism: Pseudomonas aeruginosa

enzyme: pyrroline-5-carboxylate reductase


proof_lines:
with NADH
with NADPH


proof_lines: recombinant enzyme, pH 7.0, 0.1 M imidazole


assay_conditions_summary: pH 7; cofactor NADPH


proof_lines:
recombinant enzyme
recombinant enzyme derived from E. coli


organism: Plasmodium knowlesi

assay_conditions_summary: pH 6

proof_lines: pH 6, temperature not specified in the publication, isolate PKNY146CSP


assay_conditions_summary: pH 6; cofactor NADPH


organism: Mus musculus

substrate_name: NADP+

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

substrate: NADP+


proof_lines: pH 8.0, 30°C, monoglutamylated substrate, with NADP+

proof_lines: pH 8.0, 30°C, monoglutamylated substrate, with NAD+

proof_lines: pH 8.0, 30°C, polyglutamylated substrate, with NADP+


substrate_name: NAD+

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

substrate: NAD+


substrate_name: pyruvate

substrate: pyruvate


organism: Saccharomyces cerevisiae


organism: Streptococcus pyogenes

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

proof_lines:
at pH 7.5 and 37°C
apparent value, at pH 7.5 and 37°C


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH


proof_lines: apparent value, with NADPH as cosubstrate, at pH 7.5 and 37°C

proof_lines: apparent value, with NADH as cosubstrate, at pH 7.5 and 37°C


organism: Sus scrofa

substrate_name: dihydrobiopterin

assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADPH

substrate: dihydrobiopterin


substrate_name: dihydrofolate

proof_lines:
cosubstrate NADPH, pH 7.2, 25°C
pH 6.7, 25°C

substrate: dihydrofolate


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADH

proof_lines: cosubstrate 5,10-methylenetetrahydrofolate, pH 7.2, 25°C


organism: Stenotrophomonas maltophilia


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH


organism: Bacillus cereus

substrate_name: L-Ala

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

proof_lines:
Sepharose-bound enzyme
soluble enzyme

substrate: L-Ala


enzyme_display_name: L-aspartate oxidase

organism: Bacillus subtilis

substrate_name: L-aspartate

enzyme: L-aspartate oxidase

substrate: L-aspartate


substrate_name: fumarate

substrate: fumarate


enzyme_display_name: glycine oxidase

enzyme: glycine oxidase


substrate_name: D-Ala

substrate: D-Ala


substrate_name: cyclopropylglycine

substrate: cyclopropylglycine


enzyme_display_name: primary-amine oxidase

substrate_name: 4-aminomethylpyridine dihydrochloride

enzyme: primary-amine oxidase

substrate: 4-aminomethylpyridine dihydrochloride


enzyme_display_name: diamine oxidase

enzyme: diamine oxidase


substrate_name: benzylamine

substrate: benzylamine


enzyme_display_name: D-aspartate oxidase

organism: Bos taurus

substrate_name: N-Methyl-D-aspartate

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

enzyme: D-aspartate oxidase

substrate: N-Methyl-D-aspartate


substrate_name: D-proline

substrate: D-proline


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

substrate_name: L-glutamate

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

assay_conditions_summary: pH 8.5; cofactor NADP+

proof_lines:
cofactor NAD+
at pH 8.5
1 mM, NAD+

enzyme: glutamate dehydrogenase [NAD(P)+]

substrate: L-glutamate


proof_lines:
substrate inhibition vs. NADPH
substrate inhibition vs. NH4+


substrate_name: NADPH

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: Unknown

substrate: Unknown


substrate_name: NADH

assay_conditions_summary: pH 9; 298.15 K; cofactor NADH

proof_lines: enzyme coupled to dockerin from Clostridium thermocellum, pH 9.0, 25°C

substrate: NADH


enzyme_display_name: 6,7-dihydropteridine reductase

proof_lines: reduction of quinonoid 7,8-dihydro-6-methylpterin

proof_lines: reduction of quinonoid 7,8-dihydrobiopterin

proof_lines: NADH-specific liver enzyme, substrate tetrahydrobiopterin

enzyme: 6,7-dihydropteridine reductase


substrate_name: quinonoid 7,8-dihydrobiopterin

proof_lines: NADPH-specific liver enzyme, cofactor NADPH

substrate: quinonoid 7,8-dihydrobiopterin


proof_lines:
1 mM NAD+ or 80 mM NADH
0.08 mM NADH
0.016 mM NADH


assay_conditions_summary: cofactor NAD+


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


organism: Clostridium perfringens

assay_conditions_summary: pH 7.6; cofactor NADP+

proof_lines: pH 7.6, temperature not specified in the publication


proof_lines:
cosubstrate glutamate
cosubstrate norvaline


substrate_name: norvaline

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

substrate: norvaline


organism: Corynebacterium sp. U-96


substrate_name: sarcosine

substrate: sarcosine


organism: Enterococcus faecium


enzyme_display_name: flavin reductase (NADH)

organism: Escherichia coli

substrate_name: FMN

assay_conditions_summary: cofactor NADH

proof_lines: pH and temperature not specified in the publication

enzyme: flavin reductase (NADH)

substrate: FMN


substrate_name: riboflavin

substrate: riboflavin


enzyme_display_name: glutamate dehydrogenase (NADP+)

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines: chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 2180 micromol/min/mg, pH 8.0, 25°C

enzyme: glutamate dehydrogenase (NADP+)


substrate_name: D-Aspartate

proof_lines: 50 mM potassium phosphate buffer, 0.3 mM EDTA, pH 7.4, 4°C

proof_lines: 50 mM potassium phosphate buffer, 0.3 mM EDTA, pH 7.4, 25°C

substrate: D-Aspartate


proof_lines:
at 4°C
at 25°C


substrate_name: D-asparagine

substrate: D-asparagine


substrate_name: D-glutamine

substrate: D-glutamine


substrate_name: beta-phenylethylamine

assay_conditions_summary: pH 8

proof_lines:
pH 8.0, mutant enzyme D383E
pH 7.0, mutant enzyme D383E
pH 5.5, mutant enzyme D383E

substrate: beta-phenylethylamine


assay_conditions_summary: pH 5.5; 298.15 K; buffer 100 mM sodium phosphate

proof_lines: wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

proof_lines: in the presence of 100 mM NH4Cl, at 25°C and pH 8

proof_lines: in the presence of 200 mM NH4Cl, at 25°C and pH 8

proof_lines: in the presence of 400 mM NH4Cl, at 25°C and pH 8


proof_lines: in the presence of 20 mM 2-oxoglutarate, at 25°C and pH 8

proof_lines: in the presence of 5 mM 2-oxoglutarate, at 25°C and pH 8


substrate_name: FAD

assay_conditions_summary: pH 7; 310.15 K; cofactor FAD

substrate: FAD


assay_conditions_summary: pH 7; 310.15 K; cofactor NADH


enzyme_display_name: glutamate synthase (NADPH)

assay_conditions_summary: cofactor NADPH

proof_lines: in the presence of 1 mM alpha-ketoglutarate and 5 mM L-glutamine

proof_lines: NH3-dependent glutamate synthase and apoglutamate synthase

enzyme: glutamate synthase (NADPH)


substrate_name: alpha-ketoglutarate

proof_lines: in the presence of 0.04 mM NADPH and 5 mM L-glutamine

substrate: alpha-ketoglutarate


enzyme_display_name: FMN reductase (NADPH)

assay_conditions_summary: pH 7.5; 298.15 K; cofactor FMN

proof_lines: pH 7.5, 25°C, recombinant wild-type enzyme

enzyme: FMN reductase (NADPH)


proof_lines:
with NADH
with NADPH


enzyme_display_name: L-amino-acid oxidase

organism: Rattus norvegicus

substrate_name: L-leucine

enzyme: L-amino-acid oxidase

substrate: L-leucine


substrate_name: L-lactic acid

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

substrate: L-lactic acid


organism: Aspergillus fumigatus

substrate_name: DL-Ala

substrate: DL-Ala


enzyme_display_name: UniProt Q8VPD4

organism: Rhodococcus opacus

substrate_name: L-lysine

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

source_databases_merged: skid uniprot

enzyme: UniProt Q8VPD4

substrate: L-lysine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: L-arginine

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

substrate: L-arginine


substrate_name: L-asparagine

substrate: L-asparagine


substrate_name: L-ornithine

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

substrate: L-ornithine


substrate_name: L-glutamine

substrate: L-glutamine


substrate_name: L-norleucine

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

substrate: L-norleucine


substrate_name: L-citrulline

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

substrate: L-citrulline


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-methionine

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

substrate: L-methionine


substrate_name: L-serine

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

substrate: L-serine


substrate_name: L-alanine

substrate: L-alanine


substrate_name: L-Glutamic acid

substrate: L-Glutamic acid


substrate_name: L-isoleucine

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

substrate: L-isoleucine


substrate_name: L-valine

substrate: L-valine


organism: Aplysia dactylomela

substrate_name: L-Lys

sequence: DGVCSNRRQCNKEVCGSSYDVAIVGA

wild_type_sequence: DGVCSNRRQCNKEVCGSSYDVAIVGA

substrate: L-Lys


substrate_name: L-Arg

substrate: L-Arg


enzyme_display_name: D-amino-acid oxidase

organism: Trigonopsis variabilis

substrate_name: D-phenylglycine

enzyme: D-amino-acid oxidase

substrate: D-phenylglycine


enzyme_display_name: UniProt P00371

enzyme: UniProt P00371


proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=25°C., pH=10


enzyme_display_name: UniProt P80324

organism: Rhodotorula toruloides

substrate_name: N-Methyl-D-aspartate

enzyme: UniProt P80324

substrate: N-Methyl-D-aspartate


enzyme_display_name: UniProt P14920

organism: Homo sapiens

smiles: O=O

enzyme: UniProt P14920


substrate_name: D-Phe

substrate: D-Phe


substrate_name: D-Trp

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=25°C, pH=8.5

substrate: D-Trp


substrate_name: D-Val

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

substrate: D-Val


substrate_name: D-Ser

substrate: D-Ser


substrate_name: D-Lysine

proof_lines:
Raw SKiD Env: Temp=-----, pH=8.5
Raw SKiD Env: Temp=25°C, pH=8

substrate: D-Lysine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y228L/R283G to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt P21396

substrate_name: benzylamine

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

enzyme: UniProt P21396

substrate: benzylamine


enzyme_display_name: UniProt P21397

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.2
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=20°C, pH=8.5

enzyme: UniProt P21397


enzyme_display_name: UniProt P27338

substrate_name: p-nitrophenylethylamine

enzyme: UniProt P27338

substrate: p-nitrophenylethylamine


substrate_name: p-nitrobenzylamine

substrate: p-nitrobenzylamine


enzyme_display_name: UniProt P46882

organism: Aspergillus niger

enzyme: UniProt P46882


substrate_name: p-tyramine

substrate: p-tyramine


substrate_name: kynuramine

substrate: kynuramine


substrate_name: NADH

assay_conditions_summary: pH 7.2; 288.15 K; cofactor NADH

substrate: NADH


organism: Giardia duodenalis

substrate_name: NADPH

substrate: NADPH


enzyme_display_name: glutamate synthase (ferredoxin)

organism: Glycine max

substrate_name: reduced ferredoxin

enzyme: glutamate synthase (ferredoxin)

substrate: reduced ferredoxin


substrate_name: methyl viologen

substrate: methyl viologen


enzyme_display_name: pyrroline-5-carboxylate reductase

enzyme: pyrroline-5-carboxylate reductase


enzyme_display_name: dihydrofolate reductase

organism: Haloarcula japonica

proof_lines:
pH 8.0, 25°C
pH 8.0, 25°C, presence of 1000 mM NaCl
pH 6.0, 25°C

enzyme: dihydrofolate reductase


proof_lines:
pH 8.0, 25°C
pH 8.0, 25°C, presence of 500 mM NaCl
pH 8.0, 25°C, presence of 200 mM NaCl


organism: Providencia rettgeri

substrate_name: L-arginine

substrate: L-arginine


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-histidine

substrate: L-histidine


substrate_name: L-leucine

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

substrate: L-leucine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: L-tryptophan

substrate: L-tryptophan


substrate_name: L-methionine

substrate: L-methionine


substrate_name: S-adenosylhomocysteine

substrate: S-adenosylhomocysteine


substrate_name: L-ornithine

substrate: L-ornithine


substrate_name: L-citrulline

substrate: L-citrulline


substrate_name: L-lysine

substrate: L-lysine


substrate_name: L-isoleucine

substrate: L-isoleucine


organism: Gloydius ussuriensis


substrate_name: L-valine

substrate: L-valine


substrate_name: L-asparagine

substrate: L-asparagine


proof_lines: pH and temperature not specified in the publication


substrate_name: L-alanine

substrate: L-alanine


organism: Crotalus terrificus terrificus


substrate_name: L-homocystine

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

substrate: L-homocystine


substrate_name: L-homocysteine

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

substrate: L-homocysteine


substrate_name: S-adenosyl-L-homocysteine

substrate: S-adenosyl-L-homocysteine


substrate_name: S-ribosyl-L-homocysteine

substrate: S-ribosyl-L-homocysteine


substrate_name: djenkolic acid

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

substrate: djenkolic acid


substrate_name: L-cysteine

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

substrate: L-cysteine


substrate_name: L-cystine

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

substrate: L-cystine


enzyme_display_name: monoamine oxidase

organism: Katsuwonus pelamis

enzyme: monoamine oxidase


substrate_name: serotonin

substrate: serotonin


substrate_name: dopamine

substrate: dopamine


substrate_name: tryptamine

substrate: tryptamine


substrate_name: N-methylhistamine

substrate: N-methylhistamine


substrate_name: benzylamine

substrate: benzylamine


organism: Narcissus tazetta

substrate_name: n-Propylamine

substrate: n-Propylamine


substrate_name: n-butylamine

smiles: CCCCN

substrate: n-butylamine


substrate_name: methylamine

smiles: CN

substrate: methylamine


substrate_name: ethylamine

smiles: CCN

substrate: ethylamine


substrate_name: n-Pentylamine

smiles: CCCCCN

substrate: n-Pentylamine


substrate_name: ethanolamine

smiles: C(CO)N

substrate: ethanolamine


organism: Oncorhynchus keta


substrate_name: L-homocysteine

substrate: L-homocysteine


substrate_name: L-homocystine

substrate: L-homocystine


substrate_name: S-ribosyl-L-homocysteine

substrate: S-ribosyl-L-homocysteine


substrate_name: S-adenosylmethionine

substrate: S-adenosylmethionine


substrate_name: methionine sulfoxide

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

substrate: methionine sulfoxide


substrate_name: djenkolic acid

substrate: djenkolic acid


substrate_name: S-adenosyl-L-homocysteine sulfoxide

substrate: S-adenosyl-L-homocysteine sulfoxide


substrate_name: O2; Tyramine; H2O

substrate: O2; Tyramine; H2O


organism: Rattus norvegicus

substrate_name: H2O; O2; Serotonin

substrate: H2O; O2; Serotonin


substrate_name: O2; H2O; Benzylamine

substrate: O2; H2O; Benzylamine


substrate_name: O2; Serotonin; H2O

substrate: O2; Serotonin; H2O


substrate_name: H2O; Serotonin; O2

substrate: H2O; Serotonin; O2


substrate_name: 2-Phenylethylamine; O2; H2O

substrate: 2-Phenylethylamine; O2; H2O


substrate_name: H2O; 2-Phenylethylamine; O2

substrate: H2O; 2-Phenylethylamine; O2


organism: Penicillium steckii

substrate_name: fish collagen peptide II

proof_lines: at pH 8.0 and 20°C, measured at the rate of H2O2 production

substrate: fish collagen peptide II


substrate_name: Nepsilon-benzyloxycarbonyl-L-lysine

substrate: Nepsilon-benzyloxycarbonyl-L-lysine


substrate_name: L-Lys

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

substrate: L-Lys


substrate_name: Gly-L-Lys

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

substrate: Gly-L-Lys


substrate_name: Nalpha-benzyloxycarbonyl-L-lysine

substrate: Nalpha-benzyloxycarbonyl-L-lysine


substrate_name: L-Ala-L-Lys

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

substrate: L-Ala-L-Lys


organism: Rhizoctonia solani

substrate_name: L-Met

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

substrate: L-Met


substrate_name: L-Orn

substrate: L-Orn


substrate_name: L-Arg

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

substrate: L-Arg


substrate_name: L-Leu

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

substrate: L-Leu


substrate_name: L-Phe

substrate: L-Phe


substrate_name: L-phenylalanine methyl ester

substrate: L-phenylalanine methyl ester


organism: Acipenser gueldenstaedtii


substrate_name: serotonin

substrate: serotonin


substrate_name: benzylamine

substrate: benzylamine


substrate_name: N-methylhistamine

substrate: N-methylhistamine


organism: Acipenser stellatus


organism: Proteus mirabilis

substrate_name: L-phenylalanine

assay_conditions_summary: pH 7

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

substrate: L-phenylalanine


proof_lines: mutant D165K, pH 7.0, temperature not specified in the publication


proof_lines: mutant L336M, pH 7.0, temperature not specified in the publication


proof_lines: mutant D165K/L336M, pH 7.0, temperature not specified in the publication


proof_lines: mutant D165K/S179L/F263V/L336V, pH 7.0, temperature not specified in the publication


proof_lines: mutant F263M, pH 7.0, temperature not specified in the publication


proof_lines: mutant D165K/F263M, pH 7.0, temperature not specified in the publication


proof_lines: mutant F263M/L336M, pH 7.0, temperature not specified in the publication


proof_lines: mutant D165K/F263M/L336M, pH 7.0, temperature not specified in the publication


organism: Acipenser persicus


organism: Aspergillus oryzae

substrate_name: L-Tyr

substrate: L-Tyr


organism: Bacillus carotarum

substrate_name: L-arginine

substrate: L-arginine


substrate_name: L-asparagine

substrate: L-asparagine


substrate_name: L-glutamine

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

substrate: L-glutamine


organism: Coregonus lavaretus ludoga

substrate_name: tryptamine

assay_conditions_summary: pH 7.4; 296.15 K; buffer 0.01 M phosphate

proof_lines: in 0.01 M phosphate buffer, pH 7.4, at 23°C

substrate: tryptamine


substrate_name: histamine

substrate: histamine


substrate_name: tyramine

substrate: tyramine


organism: Todarodes pacificus

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


substrate_name: Phenylethylamine

substrate: Phenylethylamine


enzyme_display_name: D-glutamate oxidase

organism: Octopus vulgaris

substrate_name: D-Aspartate

enzyme: D-glutamate oxidase

substrate: D-Aspartate


substrate_name: D-glutamate

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

substrate: D-glutamate


organism: Corynebacterium sp.


substrate_name: L-lysine

substrate: L-lysine


substrate_name: cysteine

substrate: cysteine


organism: Cerastes vipera

substrate_name: L-leucine

substrate: L-leucine


organism: Avena sativa


substrate_name: Unknown

substrate: Unknown


organism: Platichthys stellatus

proof_lines:
pH 7, 37°C, EDTA-treated protein
pH 7, 37°C, untreated protein


organism: Myoxocephalus polyacanthocephalus

substrate_name: L-Lys

proof_lines:
37°C, isozyme MPLAO1
37°C, isozyme MPLAO3
37°C, isozymes MPLAO1 and MPLAO3

substrate: L-Lys


organism: Faxonius limosus


enzyme_display_name: pyridoxal 5'-phosphate synthase

organism: Triticum aestivum

substrate_name: pyridoxamine 5'-phosphate

enzyme: pyridoxal 5'-phosphate synthase

substrate: pyridoxamine 5'-phosphate


substrate_name: pyridoxine 5'-phosphate

proof_lines:
isozyme E-II, pH 8.0, 37°C
isozyme E-I, pH 8.0, 37°C

substrate: pyridoxine 5'-phosphate


substrate_name: L-Phe

substrate: L-Phe


organism: Synechococcus cedrorum PCC 6908

substrate_name: L-arginine

substrate: L-arginine


organism: Synechococcus elongatus PCC 7942 = FACHB-805

assay_conditions_summary: cofactor FAD


substrate_name: L-phenylalanine

proof_lines: 37°C, pH not specified in the publication

substrate: L-phenylalanine


organism: Trichoderma harzianum

proof_lines:
at pH 7.0 and 20°C
at pH 7.0 and 30°C
at pH 7.0 and 50°C


organism: Candida tropicalis

substrate_name: D-alanine

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

substrate: D-alanine


organism: Papio hamadryas

substrate_name: benzylamine

substrate: benzylamine


organism: uncultured bacterium

substrate_name: D-Met

substrate: D-Met


proof_lines: with 1-methyl-4-(1-methylpyrrol-2-yl)1,2,3,6-tetrahydropyridine as substrate


organism: Macaca fuscata


enzyme_display_name: ethanolamine oxidase

organism: Phormia regina

substrate_name: ethanolamine

enzyme: ethanolamine oxidase

substrate: ethanolamine


enzyme_display_name: L-amino-acid oxidase

organism: Sebastes schlegelii

enzyme: L-amino-acid oxidase


organism: Synechococcus elongatus PCC 6301

column_label: Public DNB PDF text, Table II, column S. elongatus PCC 6301, row KM value for l-arginine [mM], reports 5. Local text refs: dnb_public_pdf_pmid_17542496_text.txt lines 170-181.

normalized_value_unit_evidence: Paper Table II gives KM value for l-arginine as 5 mM for Synechococcus elongatus PCC 6301, matching the export Km 5.0 mM.

raw_value_unit_evidence: Table II row KM value for l-arginine [mM] reports 5 under S. elongatus PCC 6301.

row_label: KM value for l-arginine [mM]

table_label: Table II. Comparison of the l-amino acid oxidase in Synechococcus elongatus PCC 6301, Synechococcus elongatus PCC 7942, and Synechococcus cedrorum PCC 6908


organism: Trigonopsis variabilis

substrate_name: D-Asn

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F258S with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; buffer 50 mM potassium phosphate

proof_lines: Km less than 0.7 s-1, mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

proof_lines: Km above 50 mM, mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

proof_lines: Km less than 14.8 mM-1 s-1, mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

substrate: D-Asn


substrate_name: D-Thr

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

proof_lines: wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

substrate: D-Thr


substrate_name: D-Lys

substrate: D-Lys


substrate_name: D-Trp

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F258A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F258A, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

substrate: D-Trp


substrate_name: D-Val

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

proof_lines: mutant enzyme F258S, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

substrate: D-Val


substrate_name: D-Tyr

substrate: D-Tyr


substrate_name: D-Ser

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

substrate: D-Ser


substrate_name: D-Phe

substrate: D-Phe


substrate_name: D-Leu

substrate: D-Leu


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F258Y with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F258Y, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C


organism: Sus scrofa

proof_lines:
Raw SKiD Env: Temp=25°C, pH=-----
Raw SKiD Env: Temp=25°C, pH=8.3
Raw SKiD Env: Temp=-----, pH=-----


substrate_name: D-phenylalanine

proof_lines: kcat is 3.5 sec(-1) with D-arginine as substrate (at 25 degrees Celsius and at pH 8.3) (PubMed:16751595). kcat is 0.8 sec(-1) with D-lysine as substrate (at 25 degrees Celsius and at pH 8.3) (PubMed:16751595). kcat is 6.8 sec(-1) with D-met

substrate: D-phenylalanine


substrate_name: D-arginine (at 25 degrees Celsius and at pH 8.3)


substrate_name: D-lysine (at 25 degrees Celsius and at pH 8.3)


substrate_name: D-methionine (at 25 degrees Celsius and at pH 8.3)


substrate_name: D-proline (at 25 degrees Celsius and at pH 8.3)


substrate_name: D-valine (at 25 degrees Celsius and at pH 8.3)


substrate_name: D-serine (at 25 degrees Celsius and at pH 8.3)


organism: Pseudomonas sp.

substrate_name: ethanolamine


enzyme_display_name: UniProt A0A499UB99

organism: Rasamsonia emersonii

substrate_name: D-methionine

proof_lines: kcat is 120 sec(-1) with D-methionine as substrate (at 55 degrees Celsius and at pH 8.0) (PubMed:31420577). kcat is 225 sec(-1) with D-valine as substrate (at 55 degrees Celsius and at pH 8.0) (PubMed:31420577). kcat is 189 sec(-1) with D-a

enzyme: UniProt A0A499UB99

substrate: D-methionine


substrate_name: D-arginine

substrate: D-arginine


substrate_name: D-valine

substrate: D-valine


substrate_name: D-alanine

substrate: D-alanine


substrate_name: D-glutamate

substrate: D-glutamate


substrate_name: L-arginine

sequence_variant_note: Resolved canonical sequence from uniprotkb:W6JQJ6 and applied mutation signature D238A to reconstruct the assayed variant sequence.

column_label: PMID 29511608 Table 2; row D238A / L-arginine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1822-1831.

normalized_value_unit_evidence: Oxidase kcat 0.10 s^-1; Oxidase Km 0.41 mM; Oxidase kcat/Km 0.24 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 0.10 ± 0.02 s^-1; Oxidase Km 0.41 ± 0.01 mM; Oxidase kcat/Km 0.24 ± 0.06 s^-1 mM^-1

row_label: D238A / L-arginine / Oxidase

table_label: PMID 29511608 Table 2. Kinetic parameters of wild-type and mutant enzymes of l-AAO/MOG

substrate: L-arginine


sequence_variant_note: Resolved canonical sequence from uniprotkb:W6JQJ6 and applied mutation signature D238F to reconstruct the assayed variant sequence.

column_label: PMID 29511608 Table 2; row D238F / L-arginine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1868-1877.

normalized_value_unit_evidence: Oxidase kcat 0.10 s^-1; Oxidase Km 0.080 mM; Oxidase kcat/Km 1.3 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 0.10 ± 0.01 s^-1; Oxidase Km 0.080 ± 0.018 mM; Oxidase kcat/Km 1.3 ± 0.1 s^-1 mM^-1

row_label: D238F / L-arginine / Oxidase


substrate_name: L-lysine

column_label: PMID 29511608 Table 2; row D238F / L-lysine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1856-1866.

normalized_value_unit_evidence: Oxidase kcat 0.17 s^-1; Oxidase Km 0.049 mM; Oxidase kcat/Km 3.5 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 0.17 ± 0.01 s^-1; Oxidase Km 0.049 ± 0.009 mM; Oxidase kcat/Km 3.5 ± 0.2 s^-1 mM^-1

row_label: D238F / L-lysine / Oxidase

substrate: L-lysine


substrate_name: L-ornithine

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

column_label: PMID 29511608 Table 2; row D238A / L-ornithine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1811-1820.

normalized_value_unit_evidence: Oxidase kcat 0.37 s^-1; Oxidase Km 0.45 mM; Oxidase kcat/Km 0.82 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 0.37 ± 0.05 s^-1; Oxidase Km 0.45 ± 0.02 mM; Oxidase kcat/Km 0.82 ± 0.10 s^-1 mM^-1

row_label: D238A / L-ornithine / Oxidase

substrate: L-ornithine


column_label: PMID 29511608 Table 2; row WT / L-arginine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1788-1797.

normalized_value_unit_evidence: Oxidase kcat 0.41 s^-1; Oxidase Km 0.048 mM; Oxidase kcat/Km 8.5 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 0.41 ± 0.02 s^-1; Oxidase Km 0.048 ± 0.001 mM; Oxidase kcat/Km 8.5 ± 0.65 s^-1 mM^-1

row_label: WT / L-arginine / Oxidase


column_label: PMID 29511608 Table 2; row D238A / L-lysine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1799-1809.

normalized_value_unit_evidence: Oxidase kcat 0.50 s^-1; Oxidase Km 0.61 mM; Oxidase kcat/Km 0.82 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 0.50 ± 0.03 s^-1; Oxidase Km 0.61 ± 0.05 mM; Oxidase kcat/Km 0.82 ± 0.09 s^-1 mM^-1

row_label: D238A / L-lysine / Oxidase


sequence_variant_note: Resolved canonical sequence from uniprotkb:W6JQJ6 and applied mutation signature D238E to reconstruct the assayed variant sequence.

column_label: PMID 29511608 Table 2; row D238E / L-ornithine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1845-1854.

normalized_value_unit_evidence: Oxidase kcat 0.58 s^-1; Oxidase Km 0.041 mM; Oxidase kcat/Km 14 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 0.58 ± 0.03 s^-1; Oxidase Km 0.041 ± 0.004 mM; Oxidase kcat/Km 14 ± 0.3 s^-1 mM^-1

row_label: D238E / L-ornithine / Oxidase


column_label: PMID 29511608 Table 2; row WT / L-lysine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1766-1775.

normalized_value_unit_evidence: Oxidase kcat 0.80 s^-1; Oxidase Km 0.027 mM; Oxidase kcat/Km 30 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 0.80 ± 0.09 s^-1; Oxidase Km 0.027 ± 0.003 mM; Oxidase kcat/Km 30 ± 1 s^-1 mM^-1

row_label: WT / L-lysine / Oxidase


column_label: PMID 29511608 Table 2; row WT / L-ornithine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1777-1786.

normalized_value_unit_evidence: Oxidase kcat 1.5 s^-1; Oxidase Km 0.022 mM; Oxidase kcat/Km 68 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 1.5 ± 0.2 s^-1; Oxidase Km 0.022 ± 0.004 mM; Oxidase kcat/Km 68 ± 1.8 s^-1 mM^-1

row_label: WT / L-ornithine / Oxidase


column_label: PMID 29511608 Table 2; row D238E / L-lysine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1833-1843.

normalized_value_unit_evidence: Oxidase kcat 2.3 s^-1; Oxidase Km 0.018 mM; Oxidase kcat/Km 130 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 2.3 ± 0.3 s^-1; Oxidase Km 0.018 ± 0.006 mM; Oxidase kcat/Km 130 ± 10 s^-1 mM^-1

row_label: D238E / L-lysine / Oxidase


organism: Crotalus durissus terrificus

substrate_name: L-isoleucine

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

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

substrate: L-isoleucine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: L-tryptophan

substrate: L-tryptophan


substrate_name: L-leucine

substrate: L-leucine


substrate_name: L-methionine

substrate: L-methionine


enzyme_display_name: D-amino-acid oxidase

substrate_name: D-Tyr

enzyme: D-amino-acid oxidase

substrate: D-Tyr


substrate_name: D-Val

substrate: D-Val


substrate_name: D-Met

substrate: D-Met


substrate_name: D-tyrosine (at 30 degrees Celsius and at pH 8.0)

proof_lines: kcat is 80.5 sec(-1) with D-methionine as substrate (at 30 degrees Celsius and at pH 8.0) (PubMed:23157298). kcat is 1.5 sec(-1) with D-methionine as substrate (PubMed:20193780). kcat is 108.6 sec(-1) with D-alanine as substrate (at 30 degr


substrate_name: D-asparagine (at 30 degrees Celsius and at pH 8.0)


substrate_name: D-threonine (at 30 degrees Celsius and at pH 8.0)


substrate_name: D-lysine (at 30 degrees Celsius and at pH 8.0)


organism: Rhodotorula toruloides

substrate_name: D-alanine

proof_lines:
Raw SKiD Env: Temp=25°C, pH=-----
Raw SKiD Env: Temp=15°C, pH=8.5
Raw SKiD Env: Temp=25°C, pH=8.3


substrate_name: D-Asn

proof_lines: kcat is 52.4 sec(-1) with D-alanine as substrate and with free enzyme (at 25 degrees Celsius and at pH 8) (PubMed:18343336). kcat is 23.3 sec(-1) with D-alanine as substrate and with immobilized enzyme (at 25 degrees Celsius and at pH 8) (P

substrate: D-Asn


substrate_name: D-Asp

substrate: D-Asp


substrate_name: D-Glu

substrate: D-Glu


substrate_name: D-Pro

substrate: D-Pro


substrate_name: D-Gln

substrate: D-Gln


substrate_name: D-phenylalanine

substrate: D-phenylalanine


substrate_name: D-leucine

substrate: D-leucine


substrate_name: D-tryptophan

substrate: D-tryptophan


substrate_name: D-methionine

substrate: D-methionine


substrate_name: D-serine

substrate: D-serine


substrate_name: D-valine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T317A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

substrate: D-valine


substrate: D-alanine


substrate_name: D-proline

substrate: D-proline


organism: Rattus norvegicus

substrate_name: tryptamine

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

substrate: tryptamine


substrate_name: tyramine

substrate: tyramine


substrate_name: serotonin

substrate: serotonin


organism: Bungarus fasciatus

substrate_name: L-Trp

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

proof_lines: pH and temperature not specified in the publication

substrate: L-Trp


substrate_name: L-Phe

substrate: L-Phe


substrate_name: L-Met

substrate: L-Met


substrate_name: L-Leu

substrate: L-Leu


substrate_name: D-alanine (at 25 degrees Celsius and at pH 8.3)

column_label: Table 1 rDAAO row D-Ala column Km, app (mM)=140 +/- 20

normalized_value_unit_evidence: Km, app=140 mM

raw_value_unit_evidence: Table 1 rDAAO row D-Ala: kcat, app=27 +/- 1 s^-1; Km, app=140 +/- 20 mM; kcat/Km=0.20 mM^-1*s^-1

row_label: D-Ala

table_label: Table 1. Comparison of substrate specificity of rDAAO and hDAAO


substrate_name: D-serine (at 25 degrees Celsius and at pH 8.3)

column_label: Table 1 rDAAO row D-Ser column Km, app (mM)=310 +/- 60

normalized_value_unit_evidence: Km, app=310 mM

row_label: D-Ser


substrate_name: D-proline (at 25 degrees Celsius and at pH 8.3)

column_label: Table 1 rDAAO row D-Pro column Km, app (mM)=86 +/- 22

normalized_value_unit_evidence: Km, app=86 mM

raw_value_unit_evidence: Table 1 rDAAO row D-Pro: kcat, app=47 +/- 1 s^-1; Km, app=86 +/- 22 mM; kcat/Km=0.55 mM^-1*s^-1

row_label: D-Pro


substrate_name: D-tryptophan (at 25 degrees Celsius and at pH 8.3)

column_label: Table 1 rDAAO row D-Trp column Km, app (mM)=15 +/- 1

normalized_value_unit_evidence: Km, app=15 mM

raw_value_unit_evidence: Table 1 rDAAO row D-Trp: kcat, app=3.7 +/- 0.2 s^-1; Km, app=15 +/- 1 mM; kcat/Km=0.25 mM^-1*s^-1

row_label: D-Trp


substrate_name: D-phenylalanine (at 25 degrees Celsius and at pH 8.3)

column_label: Table 1 rDAAO row D-Phe column Km, app (mM)=35 +/- 9

normalized_value_unit_evidence: Km, app=35 mM

raw_value_unit_evidence: Table 1 rDAAO row D-Phe: kcat, app=8.5 +/- 0.2 s^-1; Km, app=35 +/- 9 mM; kcat/Km=0.24 mM^-1*s^-1

row_label: D-Phe


organism: Hebeloma cylindrosporum

substrate_name: L-phenylalanine

proof_lines: untreated recombinant protein, pH 7, 30°C

proof_lines: acid-activited recombinant protein, pH 7, 30°C

substrate: L-phenylalanine


substrate_name: L-leucine

substrate: L-leucine


substrate_name: L-glutamine

substrate: L-glutamine


substrate_name: L-leucine methyl ester

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

substrate: L-leucine methyl ester


organism: Rubrobacter xylanophilus (strain DSM 9941 / JCM 11954 / NBRC 16129 / PRD-1)

substrate_name: D-tyrosine (at 60 degrees Celsius and at pH 8.0)

column_label: Table 2. Kinetic parameters of RxDAO, row D-Tyr; Km column cell 0.197 +/- 0.043 mM.

row_label: RxDAO / D-Tyr

table_label: Table 2. Kinetic parameters of RxDAO


substrate_name: D-valine (at 60 degrees Celsius and at pH 8.0)

column_label: Table 2. Kinetic parameters of RxDAO, row D-Val; Km column cell 0.094 +/- 0.011 mM.

row_label: RxDAO / D-Val


substrate_name: D-leucine (at 60 degrees Celsius and at pH 8.0)

column_label: Table 2. Kinetic parameters of RxDAO, row D-Leu; Km column cell 0.049 +/- 0.004 mM.

row_label: RxDAO / D-Leu


substrate_name: D-isoleucine (at 60 degrees Celsius and at pH 8.0)

column_label: Table 2. Kinetic parameters of RxDAO, row D-Ile; Km column cell 0.052 +/- 0.005 mM.

row_label: RxDAO / D-Ile


substrate_name: D-threonine (at 60 degrees Celsius and at pH 8.0)

column_label: Table 2. Kinetic parameters of RxDAO, row D-Thr; Km column cell 8.16 +/- 0.93 mM.

normalized_value_unit_evidence: Km 8.16 mM

row_label: RxDAO / D-Thr


substrate_name: cephalosporin C

proof_lines: recombinant wild-type enzyme, pH 7.5, 22°C

substrate: cephalosporin C


sequence_variant_note: Mutation signature F54S could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


substrate_name: D-alanine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y228F with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


substrate_name: D-phenylalanine

substrate: D-phenylalanine


substrate_name: D-proline


substrate_name: D-methionine

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

substrate: D-methionine


organism: Macrovipera lebetinus

substrate_name: L-methionine

substrate: L-methionine


substrate_name: L-tryptophan

substrate: L-tryptophan


organism: Calloselasma rhodostoma

substrate_name: L-Phe

assay_conditions_summary: buffer for its rows

column_label: Table 2: Kinetic parameters of L-amino acid oxidase from snake venom on specific substrates (BioMed Research International 2014, volume 2014, Article ID 196754); Table 2, row Calloselasma rhodostoma, Phe column pair; the kcat value 0.72 s-1 comes from the K cat (s-1) column of the Phe column pair and the Michaelis constant 0.05 mM comes from the Km (mM) column of the same Phe column pair. There is no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.72 s-1; already in s^-1, no unit conversion applies (this review prints no min^-1 kinetic cell); the paper value is 0.72 s^(-1). Km: printed Table 2 cell 0.05 mM; already in mM, no unit conversion applies; the paper value is 0.05 mM. kcat/Km: this review prints no kcat/Km cell for this measurement, so the catalog value 14.399999999999999 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.72 / 0.05 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, row Calloselasma rhodostoma, Phe column pair: kcat = 0.72 s-1 (printed column the K cat (s-1) column of the Phe column pair); Km = 0.05 mM (printed column the Km (mM) column of the Phe column pair). No kcat/Km value is printed for this measurement.


substrate_name: L-Trp

column_label: Table 2: Kinetic parameters of L-amino acid oxidase from snake venom on specific substrates (BioMed Research International 2014, volume 2014, Article ID 196754); Table 2, row Calloselasma rhodostoma, Trp column pair; the kcat value 0.88 s-1 comes from the K cat (s-1) column of the Trp column pair and the Michaelis constant 0.08 mM comes from the Km (mM) column of the same Trp column pair. There is no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.88 s-1; already in s^-1, no unit conversion applies (this review prints no min^-1 kinetic cell); the paper value is 0.88 s^(-1). Km: printed Table 2 cell 0.08 mM; already in mM, no unit conversion applies; the paper value is 0.08 mM. kcat/Km: this review prints no kcat/Km cell for this measurement, so the catalog value 11.0 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.88 / 0.08 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, row Calloselasma rhodostoma, Trp column pair: kcat = 0.88 s-1 (printed column the K cat (s-1) column of the Trp column pair); Km = 0.08 mM (printed column the Km (mM) column of the Trp column pair). No kcat/Km value is printed for this measurement.


substrate_name: L-Met

column_label: Table 2: Kinetic parameters of L-amino acid oxidase from snake venom on specific substrates (BioMed Research International 2014, volume 2014, Article ID 196754); Table 2, row Calloselasma rhodostoma, Met column pair; the kcat value 1.65 s-1 comes from the K cat (s-1) column of the Met column pair and the Michaelis constant 0.24 mM comes from the Km (mM) column of the same Met column pair. There is no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.65 s-1; already in s^-1, no unit conversion applies (this review prints no min^-1 kinetic cell); the paper value is 1.65 s^(-1). Km: printed Table 2 cell 0.24 mM; already in mM, no unit conversion applies; the paper value is 0.24 mM. kcat/Km: this review prints no kcat/Km cell for this measurement, so the catalog value 6.875 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.65 / 0.24 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, row Calloselasma rhodostoma, Met column pair: kcat = 1.65 s-1 (printed column the K cat (s-1) column of the Met column pair); Km = 0.24 mM (printed column the Km (mM) column of the Met column pair). No kcat/Km value is printed for this measurement.


substrate_name: L-Leu


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D206A to reconstruct the assayed variant sequence.

substrate: D-alanine


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -12, 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 -1, so it is treated as a source-provided variant sequence.


organism: Aspergillus niger

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W230I/T354S/W430R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W230I/T354S/W430R, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W230I/T354S/W430R/M242R/Y365V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W230I/T354S/W430R/M242R/Y365V, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W230R/W430C/C214L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W230R/W430C/C214L, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C108S to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant C108S, pH 7.5, 37°C, with 6-dichloroindophenolate

proof_lines: recombinant mutant C108S, pH 7.5, 37°C, with O2


assay_conditions_summary: pH 7.5; buffer 50 mM potassium phosphate

proof_lines: recombinant wild-type enzyme, pH 7.5, 37°C, with 6-dichloroindophenolate

proof_lines: wild type enzyme, in 50 mM potassium phosphate buffer, pH 8.0, at 30°C

proof_lines: recombinant wild-type enzyme, pH 7.5, 37°C, with O2


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C108D to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant C108D, pH 7.5, 37°C, with 6-dichloroindophenolate

proof_lines: recombinant mutant C108D, pH 7.5, 37°C, with O2


organism: Homo sapiens

substrate_name: kynuramine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I199A/Y326A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; buffer 50 mM phosphate

proof_lines: mutant enzyme I199A/Y326A, at 25°C in 50 mM phosphate buffer (pH 7.5)

substrate: kynuramine


substrate_name: Phenylethylamine

substrate: Phenylethylamine


substrate_name: phenylbutylamine

substrate: phenylbutylamine


organism: Crotalus atrox

substrate_name: L-phenylalanine


substrate_name: L-propargylglycine

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

substrate: L-propargylglycine


substrate_name: O-methyl-L-tyrosine

proof_lines: pH 7.5, temperature not specified in the publication

substrate: O-methyl-L-tyrosine


substrate_name: L-tyrosine

proof_lines: presence of 1 mM O-methyl-L-tyrosine, pH 7.5, temperature not specified in the publication

substrate: L-tyrosine


proof_lines: acid-activated recombinant protein, pH 7, 30°C


substrate_name: L-phenylalanine methyl ester

proof_lines: untreated recombinant protein, pH 7, 30°C

substrate: L-phenylalanine methyl ester


organism: Vipera berus berus

column_label: Table 2: Kinetic parameters of L-amino acid oxidase from snake venom on specific substrates (BioMed Research International 2014, volume 2014, Article ID 196754); Table 2, row Vipera berus berus, Phe column pair; the kcat value 28.50 s-1 comes from the K cat (s-1) column of the Phe column pair and the Michaelis constant 0.058 mM comes from the Km (mM) column of the same Phe column pair. There is no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 28.50 s-1; already in s^-1, no unit conversion applies (this review prints no min^-1 kinetic cell); the paper value is 28.5 s^(-1). Km: printed Table 2 cell 0.058 mM; already in mM, no unit conversion applies; the paper value is 0.058 mM. kcat/Km: this review prints no kcat/Km cell for this measurement, so the catalog value 491.37931034482756 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 28.50 / 0.058 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, row Vipera berus berus, Phe column pair: kcat = 28.50 s-1 (printed column the K cat (s-1) column of the Phe column pair); Km = 0.058 mM (printed column the Km (mM) column of the Phe column pair). No kcat/Km value is printed for this measurement.

substrate: L-Phe


column_label: Table 2: Kinetic parameters of L-amino acid oxidase from snake venom on specific substrates (BioMed Research International 2014, volume 2014, Article ID 196754); Table 2, row Vipera berus berus, Met column pair; the kcat value 74.20 s-1 comes from the K cat (s-1) column of the Met column pair and the Michaelis constant 0.286 mM comes from the Km (mM) column of the same Met column pair. There is no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 74.20 s-1; already in s^-1, no unit conversion applies (this review prints no min^-1 kinetic cell); the paper value is 74.2 s^(-1). Km: printed Table 2 cell 0.286 mM; already in mM, no unit conversion applies; the paper value is 0.286 mM. kcat/Km: this review prints no kcat/Km cell for this measurement, so the catalog value 259.44055944055947 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 74.20 / 0.286 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, row Vipera berus berus, Met column pair: kcat = 74.20 s-1 (printed column the K cat (s-1) column of the Met column pair); Km = 0.286 mM (printed column the Km (mM) column of the Met column pair). No kcat/Km value is printed for this measurement.

substrate: L-Met


column_label: Table 2: Kinetic parameters of L-amino acid oxidase from snake venom on specific substrates (BioMed Research International 2014, volume 2014, Article ID 196754); Table 2, row Vipera berus berus, Leu column pair; the kcat value 75.16 s-1 comes from the K cat (s-1) column of the Leu column pair and the Michaelis constant 0.361 mM comes from the Km (mM) column of the same Leu column pair. There is no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 75.16 s-1; already in s^-1, no unit conversion applies (this review prints no min^-1 kinetic cell); the paper value is 75.16 s^(-1). Km: printed Table 2 cell 0.361 mM; already in mM, no unit conversion applies; the paper value is 0.361 mM. kcat/Km: this review prints no kcat/Km cell for this measurement, so the catalog value 208.1994459833795 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 75.16 / 0.361 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, row Vipera berus berus, Leu column pair: kcat = 75.16 s-1 (printed column the K cat (s-1) column of the Leu column pair); Km = 0.361 mM (printed column the Km (mM) column of the Leu column pair). No kcat/Km value is printed for this measurement.

substrate: L-Leu


organism: Dictyostelium discoideum

substrate_name: D-alanine (at pH 8.5)

proof_lines: kcat is 0.53 sec(-1) with D-alanine as substrate (at pH 8.5) (PubMed:29740415). kcat is 0.05 sec(-1) with D-serine as substrate (at pH 8.5) (PubMed:29740415).

substrate: D-alanine (at pH 8.5)


substrate_name: D-serine (at pH 8.5)

substrate: D-serine (at pH 8.5)


organism: Naja oxiana

proof_lines: pH and temperature not specified in the publication

substrate: L-phenylalanine


substrate_name: L-leucine

substrate: L-leucine


substrate_name: L-methionine

substrate: L-methionine


substrate_name: D-serine

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8.3
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=25°C, pH=7

substrate: D-serine


substrate_name: D-phenylalanine

proof_lines: kcat is 3 sec(-1) with D-serine as substrate (at 25 degrees Celsius and at pH 8.5) (PubMed:16616139, PubMed:23219954, PubMed:31799256). kcat is 2.3 sec(-1) with D-serine as substrate (at 25 degrees Celsius and at pH 8.5) (PubMed:18544534).

substrate: D-phenylalanine


substrate_name: D-alanine

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8.3
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=-----, pH=-----

substrate: D-alanine


substrate_name: D-Dopa

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8.5
Raw SKiD Env: Temp=25°C, pH=8.3
Raw SKiD Env: Temp=25°C, pH=7

substrate: D-Dopa


substrate_name: D-tyrosine

substrate: D-tyrosine


substrate_name: D-proline

substrate: D-proline


substrate_name: 3-(2-Naphthyl)-D-alanine (at 25 degrees Celsius and at pH 8.5)

proof_lines: kcat is 52.4 sec(-1) with D-alanine as substrate and with free enzyme (at 25 degrees Celsius and at pH 8) (PubMed:18343336). kcat is 23.3 sec(-1) with D-alanine as substrate and with immobilized enzyme (at 25 degrees Celsius and at pH 8) (P


substrate_name: 3-(1-Naphthyl)-D-alanine (at 25 degrees Celsius and at pH 8.5)


organism: Mus musculus

substrate_name: D-phenylalanine (at 37 degrees Celsius and at pH 8.3)

proof_lines: kcat is 5.42 sec(-1) with D-phenylalanine as substrate (at 37 degrees Celsius and at pH 8.3) (PubMed:20567862). kcat is 0.46 sec(-1) with D-histidine as substrate (at 37 degrees Celsius and at pH 8.3) (PubMed:20567862).


substrate_name: D-histidine (at 37 degrees Celsius and at pH 8.3)


organism: Crotalus durissus cumanensis

assay_conditions_summary: pH 8; buffer 50 mM Tris-HCl

proof_lines: in 50 mM Tris-HCl buffer pH 8.0, at 37°C


organism: Caenorhabditis elegans

substrate_name: D-Met

proof_lines: The values given here are for the recombinant protein.

substrate: D-Met


substrate_name: L-Glu

substrate: L-Glu


organism: Trigonopsis variabilis

assay_conditions_summary: pH 8; buffer 100 mM potassium phosphate

proof_lines: immobilized enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C


substrate_name: D-valine

assay_conditions_summary: pH 8

proof_lines: kcat is 80.5 sec(-1) with D-methionine as substrate (at 30 degrees Celsius and at pH 8.0) (PubMed:23157298). kcat is 1.5 sec(-1) with D-methionine as substrate (PubMed:20193780). kcat is 108.6 sec(-1) with D-alanine as substrate (at 30 degr

substrate: D-valine


organism: [Candida] boidinii


organism: Lachesis muta

proof_lines: at pH 8.0, temperature not specified in the publication


substrate_name: L-Trp

substrate: L-Trp


organism: Rhodotorula toruloides

substrate_name: D-arginine

substrate: D-arginine


organism: Glutamicibacter protophormiae

substrate_name: oxygen (at 30 degrees Celsius and at pH 7.6)

smiles: O=O

proof_lines: kcat is 17.92 sec(-1) with D-methionine as substrate in strain DSM 15035 (at 30 degrees Celsius and at pH 9) (PubMed:36889103). kcat is 23.23 sec(-1) with D-methionine as substrate in strain DSM 20168 (at 30 degrees Celsius and at pH 9) (Pu


substrate_name: cephalosporin C

proof_lines:
Raw SKiD Env: Temp=25°C, pH=-----
Raw SKiD Env: Temp=37°C, pH=-----
Raw SKiD Env: Temp=25°C, pH=8

substrate: cephalosporin C


organism: Sus scrofa

substrate_name: cephalosporin C (CPC) (at 25 degrees Celsius and at pH 8.5)

proof_lines: kcat is 3.5 sec(-1) with D-arginine as substrate (at 25 degrees Celsius and at pH 8.3) (PubMed:16751595). kcat is 0.8 sec(-1) with D-lysine as substrate (at 25 degrees Celsius and at pH 8.3) (PubMed:16751595). kcat is 6.8 sec(-1) with D-met


substrate_name: D-kynurenine

substrate: D-kynurenine


substrate_name: L-aspartate (at 37 degrees Celsius and at pH 8)


enzyme_display_name: UniProt P00371

enzyme: UniProt P00371


proof_lines: free enzyme, in 100 mM potassium phosphate buffer, pH 8.0, at 25°C


substrate_name: D-cycloserine

substrate: D-cycloserine


substrate_name: D-cysteine

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

substrate: D-cysteine


organism: Unknown prokaryotic organism

substrate_name: D-methionine (at 37 degrees Celsius and at pH 8.0)

proof_lines: kcat is 10.9 sec(-1) with D-methionine as substrate (at 37 degrees Celsius and at pH 8.0).


substrate_name: Phenylethylamine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y398F to reconstruct the assayed variant sequence.

substrate: Phenylethylamine


substrate_name: D-phenylalanine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y228L with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


organism: Escherichia coli (strain K12)

substrate_name: pyridoxamine 5'-phosphate

proof_lines: kcat is 0.3 sec(-1) for oxidase activity with pyridoxine 5'-phosphate as substrate (at pH 7.6 and 37 degrees Celsius).

substrate: pyridoxamine 5'-phosphate


enzyme_display_name: UniProt P0AFI7

organism: Escherichia coli

substrate_name: pyridoxine 5'-phosphate

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.6
Raw SKiD Env: Temp=37°C, pH=8.5
Raw SKiD Env: Temp=37°C, pH=8

enzyme: UniProt P0AFI7

substrate: pyridoxine 5'-phosphate


proof_lines:
at pH 8.3 and 25°C
cephalosporin C
D-alanine


enzyme_display_name: Pyridoxine 5'-phosphate oxidase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

enzyme: Pyridoxine 5'-phosphate oxidase


organism: Agkistrodon rhodostoma

substrate_name: L-Alanine; H2O; O2

substrate: L-Alanine; H2O; O2


organism: Bothriechis schlegelii

substrate_name: O2; L-Leucine; H2O

substrate: O2; L-Leucine; H2O


organism: Bungarus fasciatus

assay_conditions_summary: pH 8.5; buffer 0.1 M Tris

column_label: Table 1: The Km, kcat and kcat/Km values for BF-LAAO against different L-amino acid substrates, row L-Leu, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1): Table 1 row L-Leu: Km 60.69 mM; kcat 1025.05 s^-1; kcat/Km 16.89 s^-1 mM^-1.

row_label: L-Leu / BF-LAAO


substrate_name: L-Aspartate; O2; H2O

column_label: Table 1: The Km, kcat and kcat/Km values for BF-LAAO against different L-amino acid substrates, row L-Asp, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1): Table 1 row L-Asp: Km 0.04 mM; kcat 47.49 s^-1; kcat/Km 1187.25 s^-1 mM^-1.

normalized_value_unit_evidence: Km 0.04 mM

row_label: L-Asp / BF-LAAO

substrate: L-Aspartate; O2; H2O


organism: Cerastes cerastes

substrate_name: L-Leucine; O2; H2O

substrate: L-Leucine; O2; H2O


substrate_name: O2; H2O; L-Leucine

substrate: O2; H2O; L-Leucine


organism: Daboia russelii

substrate_name: O2; H2O; L-Phenylalanine

sequence: ADDKNPLEECFCEDDDYCEG

wild_type_sequence: ADDKNPLEECFCEDDDYCEG

substrate: O2; H2O; L-Phenylalanine


substrate_name: D-Ser

substrate: D-Ser


substrate_name: D-His

substrate: D-His


substrate_name: D-Arg

substrate: D-Arg


substrate_name: D-Ala

substrate: D-Ala


substrate_name: D-Phe

substrate: D-Phe


organism: Rattus norvegicus

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

proof_lines: enzyme activity in liver homogenate in the presence of 0.005 mM pyridoxal 5'-phosphate


enzyme_display_name: UniProt P80324

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8.5
Raw SKiD Env: Temp=15°C, pH=8.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P80324


organism: Aplysia californica

substrate_name: Unknown

substrate: Unknown


organism: Crotalus atrox

proof_lines: pH 7.5, temperature not specified in the publication


enzyme_display_name: L-amino-acid oxidase 4

organism: Hebeloma cylindrosporum

enzyme: L-amino-acid oxidase 4


enzyme_display_name: L-amino acid oxidase Lm29

organism: Lachesis muta

enzyme: L-amino acid oxidase Lm29


organism: Mus musculus


organism: Naja atra


substrate_name: S-Adenosyl-L-homocysteine; H2O; O2

substrate: S-Adenosyl-L-homocysteine; H2O; O2


organism: Trimeresurus purpureomaculatus

substrate_name: L-Leucine; H2O; O2

substrate: L-Leucine; H2O; O2


organism: Vipera berus berus


organism: Cyprinus carpio

substrate_name: O2; H2O; D-Alanine

substrate: O2; H2O; D-Alanine


substrate_name: H2O; D-Proline; O2

substrate: H2O; D-Proline; O2


organism: Sus scrofa

substrate_name: D-Alanine; O2; H2O

substrate: D-Alanine; O2; H2O


enzyme_display_name: UniProt P21397

organism: Homo sapiens

enzyme: UniProt P21397


substrate_name: Benzylamine; O2; H2O

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=37°C, pH=7

source_databases_merged: sabio_rk skid uniprot

substrate: Benzylamine; O2; H2O


substrate_name: O2; Serotonin; H2O

substrate: O2; Serotonin; H2O


organism: Escherichia coli

substrate_name: Pyridoxamine phosphate; O2; H2O

substrate: Pyridoxamine phosphate; O2; H2O


substrate_name: Pyridoxamine phosphate; H2O; O2

substrate: Pyridoxamine phosphate; H2O; O2


substrate_name: N-Phosphopyridoxyl tryptamine

substrate: N-Phosphopyridoxyl tryptamine


organism: Ophiophagus hannah

assay_conditions_summary: pH 8.5; 298.15 K; buffer the substrate in 1 ml of 0.1 M Tris-HCl

column_label: Table 2, substrate row '3,4-Dehydro-r-Pro', columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 M^-1): Km cell 4.2, kcat cell 5.0, kcat/Km cell 1203; the explicit kcat/Km cell normalizes to 1.203 s^-1 mM^-1 rather than the current 1.1904761904761905 s^-1 mM^-1. kcat and Km are read from the same single printed row of the same table.

raw_value_unit_evidence: Table 2 substrate row 3,4-Dehydro-r-Pro: Km 4.2 mM; kcat 5.0 s^-1; kcat/Km 1203 s^-1 M^-1.

row_label: Table 2 substrate row 3,4-Dehydro-r-Pro

table_label: Table 2. Kinetic parameters of king cobra venom L-amino acid oxidae*


column_label: Table 2, substrate row '2,4-r.-Diamino-butyric acid', columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 M^-1): Km cell 2.4, kcat cell 5.9, kcat/Km cell 2441; the explicit kcat/Km cell normalizes to 2.441 s^-1 mM^-1 rather than the current 2.4583333333333335 s^-1 mM^-1. kcat and Km are read from the same single printed row of the same table.

raw_value_unit_evidence: Table 2 substrate row 2,4-r.-Diamino-butyric acid: Km 2.4 mM; kcat 5.9 s^-1; kcat/Km 2441 s^-1 M^-1.


substrate_name: L-Alanine

column_label: Table 2, substrate row 'L-Ala', columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 M^-1): Km cell 12.5, kcat cell 16.0, kcat/Km cell 1280. kcat and Km are read from the same single printed row of the same table.

raw_value_unit_evidence: Table 2 substrate row L-Ala: Km 12.5 mM; kcat 16.0 s^-1; kcat/Km 1280 s^-1 M^-1.

row_label: Table 2 substrate row L-Ala

substrate: L-Alanine


substrate_name: L-alpha-Aminobutyrate

column_label: Table 2, substrate row 'L-Aminobutyric acid', columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 M^-1): Km cell 4.0, kcat cell 56.0, kcat/Km cell 14,000. kcat and Km are read from the same single printed row of the same table.

raw_value_unit_evidence: Table 2 substrate row L-Aminobutyric acid: Km 4.0 mM; kcat 56.0 s^-1; kcat/Km 14,000 s^-1 M^-1.

substrate: L-alpha-Aminobutyrate


substrate_name: L-Arginine

column_label: Table 2, substrate row 'L-Arg', columns Km (mM), kcat (s^-1) and kcat/Km (s^-1 M^-1): Km cell 0.15, kcat cell 39.4, kcat/Km cell 255,805; the explicit kcat/Km cell normalizes to 255.805 s^-1 mM^-1 rather than the current 262.6666666666667 s^-1 mM^-1. kcat and Km are read from the same single printed row of the same table.

raw_value_unit_evidence: Table 2 substrate row L-Arg: Km 0.15 mM; kcat 39.4 s^-1; kcat/Km 255,805 s^-1 M^-1.

row_label: Table 2 substrate row L-Arg

substrate: L-Arginine