column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row msCAR (Mycobacterium smegmatis) / 3-Methoxybenzoic acid (4); kcat column kcat [min^-1] raw 18+/-1*; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 1.4+/-0.2*; Km column Km [mM] raw 12+/-1*

normalized_value_unit_evidence: kcat normalized_value=0.3 normalized_unit=s^-1 from 18+/-1* / 60; kcat/Km normalized_value=0.024999999999999998 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=1.4+/-0.2* min^-1 mM^-1; Km normalized_value=12.0 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=18+/-1* raw_unit=min^-1; kcat/Km raw_value=1.4+/-0.2* raw_unit=min^-1 mM^-1; Km raw_value=12+/-1* raw_unit=mM


enzyme_display_name: carboxylate reductase (NADP+)

organism: Mycolicibacterium smegmatis

source_db: brenda

verification_status: corrected

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

column_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring row msCAR (Mycolicibacterium smegmatis), substrate column trans-2-Phenylcyclopropane-1-carboxylic acid (13), metric row k cat [min^-1], raw cell 2.2+/-0.1, normalized 0.0366666666666666666666666666667 s^-1; Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring row msCAR (Mycolicibacterium smegmatis), substrate column trans-2-Phenylcyclopropane-1-carboxylic acid (13), metric row K_m [mM], raw cell 0.006+/-0.0001, normalized 0.006 mM

normalized_value_unit_evidence: kcat normalized_value=0.0366666666666666666666666666667 normalized_unit=s^-1; Km normalized_value=0.006 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=2.2 raw_unit=min^-1 raw_cell=2.2+/-0.1; Km raw_value=0.006 raw_unit=mM raw_cell=0.006+/-0.0001

row_label: msCAR (Mycolicibacterium smegmatis) / trans-2-Phenylcyclopropane-1-carboxylic acid (13)

enzyme: carboxylate reductase (NADP+)

status: corrected

source: brenda


verification_status: verified

assay_conditions_summary: pH 7.8; cofactor NADPH

column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row msCAR (Mycobacterium smegmatis) / 3-Nitrobenzoic acid (7); kcat column kcat [min^-1] raw 40+/-10; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 100+/-50; Km column Km [mM] raw 0.5+/-0.2

normalized_value_unit_evidence: kcat normalized_value=0.67 normalized_unit=s^-1 from 40+/-10 / 60; kcat/Km normalized_value=1.34 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=100+/-50 min^-1 mM^-1; Km normalized_value=0.5 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=40+/-10 raw_unit=min^-1; kcat/Km raw_value=100+/-50 raw_unit=min^-1 mM^-1; Km raw_value=0.5+/-0.2 raw_unit=mM

data_origin: experimental

status: verified


substrate_name: octadecanoate

kcat_over_km_origin: calculated

smiles: CCCCCCCCCCCCCCCCCC(=O)[O-]

assay_conditions_summary: pH 8; cofactor NADPH

column_label: Table 4. CAR activity against heterocycles and fatty acids.; row msCAR (Mycobacterium smegmatis) / Octadecanoic acid (21); kcat column kcat [min^-1] raw 46+/-4; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 80+/-10; Km column Km [mM] raw 0.6+/-0.09

normalized_value_unit_evidence: kcat normalized_value=0.77 normalized_unit=s^-1 from 46+/-4 / 60; kcat/Km normalized_value=1.2833333333333334 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=80+/-10 min^-1 mM^-1; Km normalized_value=0.6 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=46+/-4 raw_unit=min^-1; kcat/Km raw_value=80+/-10 raw_unit=min^-1 mM^-1; Km raw_value=0.6+/-0.09 raw_unit=mM

substrate: octadecanoate


column_label: Table 4. CAR activity against heterocycles and fatty acids.; row msCAR (Mycobacterium smegmatis) / Furan-2-carboxylic acid (16); kcat column kcat [min^-1] raw 50+/-10; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 4+/-2; Km column Km [mM] raw 13+/-4

normalized_value_unit_evidence: kcat normalized_value=0.83 normalized_unit=s^-1 from 50+/-10 / 60; kcat/Km normalized_value=0.06384615384615384 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=4+/-2 min^-1 mM^-1; Km normalized_value=13.0 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=50+/-10 raw_unit=min^-1; kcat/Km raw_value=4+/-2 raw_unit=min^-1 mM^-1; Km raw_value=13+/-4 raw_unit=mM


column_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring.; row msCAR (Mycobacterium smegmatis) / 3-Oxo-3-phenylpropanoic acid (12); kcat column kcat [min^-1] raw 75+/-2; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 280+/-20; Km column Km [mM] raw 0.27+/-0.02

normalized_value_unit_evidence: kcat normalized_value=1.25 normalized_unit=s^-1 from 75+/-2 / 60; kcat/Km normalized_value=4.62962962962963 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=280+/-20 min^-1 mM^-1; Km normalized_value=0.27 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=75+/-2 raw_unit=min^-1; kcat/Km raw_value=280+/-20 raw_unit=min^-1 mM^-1; Km raw_value=0.27+/-0.02 raw_unit=mM


column_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring.; row msCAR (Mycobacterium smegmatis) / (E)-3-Phenylprop-2-enoic acid (10); kcat column kcat [min^-1] raw 118+/-2; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 1600+/-500; Km column Km [mM] raw 0.075+/-0.004

normalized_value_unit_evidence: kcat normalized_value=1.97 normalized_unit=s^-1 from 118+/-2 / 60; kcat/Km normalized_value=26.266666666666666 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=1600+/-500 min^-1 mM^-1; Km normalized_value=0.075 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=118+/-2 raw_unit=min^-1; kcat/Km raw_value=1600+/-500 raw_unit=min^-1 mM^-1; Km raw_value=0.075+/-0.004 raw_unit=mM


column_label: Table 4. CAR activity against heterocycles and fatty acids.; row msCAR (Mycobacterium smegmatis) / Thiophene-2-carboxylic acid (17); kcat column kcat [min^-1] raw 123+/-4; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 37+/-3; Km column Km [mM] raw 3.3+/-0.3

normalized_value_unit_evidence: kcat normalized_value=2.05 normalized_unit=s^-1 from 123+/-4 / 60; kcat/Km normalized_value=0.6212121212121212 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=37+/-3 min^-1 mM^-1; Km normalized_value=3.3 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=123+/-4 raw_unit=min^-1; kcat/Km raw_value=37+/-3 raw_unit=min^-1 mM^-1; Km raw_value=3.3+/-0.3 raw_unit=mM


substrate_name: Butanoate

smiles: CCCC(=O)[O-]

column_label: Table 4. CAR activity against heterocycles and fatty acids.; row msCAR (Mycobacterium smegmatis) / Butanoic acid (18); kcat column kcat [min^-1] raw 129+/-7*; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 16+/-2*; Km column Km [mM] raw 7.9+/-0.8*

normalized_value_unit_evidence: kcat normalized_value=2.15 normalized_unit=s^-1 from 129+/-7* / 60; kcat/Km normalized_value=0.27215189873417717 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=16+/-2* min^-1 mM^-1; Km normalized_value=7.9 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=129+/-7* raw_unit=min^-1; kcat/Km raw_value=16+/-2* raw_unit=min^-1 mM^-1; Km raw_value=7.9+/-0.8* raw_unit=mM

substrate: Butanoate


substrate_name: dodecanoate

smiles: CCCCCCCCCCCC(=O)[O-]

column_label: Table 4. CAR activity against heterocycles and fatty acids.; row msCAR (Mycobacterium smegmatis) / Dodecanoic acid (20); kcat column kcat [min^-1] raw 131+/-5; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 2700+/-400; Km column Km [mM] raw 0.05+/-0.01

normalized_value_unit_evidence: kcat normalized_value=2.18 normalized_unit=s^-1 from 131+/-5 / 60; kcat/Km normalized_value=43.6 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=2700+/-400 min^-1 mM^-1; Km normalized_value=0.05 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=131+/-5 raw_unit=min^-1; kcat/Km raw_value=2700+/-400 raw_unit=min^-1 mM^-1; Km raw_value=0.05+/-0.01 raw_unit=mM

substrate: dodecanoate


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row msCAR (Mycobacterium smegmatis) / 4-Methylbenzoic acid (2); kcat column kcat [min^-1] raw 154+/-6; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 900+/-100; Km column Km [mM] raw 0.16+/-0.02

normalized_value_unit_evidence: kcat normalized_value=2.57 normalized_unit=s^-1 from 154+/-6 / 60; kcat/Km normalized_value=16.0625 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=900+/-100 min^-1 mM^-1; Km normalized_value=0.16 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=154+/-6 raw_unit=min^-1; kcat/Km raw_value=900+/-100 raw_unit=min^-1 mM^-1; Km raw_value=0.16+/-0.02 raw_unit=mM


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row msCAR (Mycobacterium smegmatis) / 4-Methoxybenzoic acid (3); kcat column kcat [min^-1] raw 179+/-6; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 930+/-80; Km column Km [mM] raw 0.19+/-0.02

normalized_value_unit_evidence: kcat normalized_value=2.98 normalized_unit=s^-1 from 179+/-6 / 60; kcat/Km normalized_value=15.68421052631579 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=930+/-80 min^-1 mM^-1; Km normalized_value=0.19 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=179+/-6 raw_unit=min^-1; kcat/Km raw_value=930+/-80 raw_unit=min^-1 mM^-1; Km raw_value=0.19+/-0.02 raw_unit=mM


enzyme_display_name: branched-chain alpha-keto acid dehydrogenase system

organism: Bacillus subtilis

substrate_name: CoA

verification_status: unverified

kcat_display: Not reported

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

assay_conditions_summary: cofactor CoA

substrate: CoA

status: unverified


substrate_name: L-alpha-keto-beta-methylvalerate

enzyme: branched-chain alpha-keto acid dehydrogenase system

substrate: L-alpha-keto-beta-methylvalerate


organism: Nocardia otitidiscaviarum

assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: Table 4. CAR activity against heterocycles and fatty acids.; row noCAR (Nocardia otitidiscaviarum) / Octadecanoic acid (21); kcat column kcat [min^-1] raw 11+/-1; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 500+/-300; Km column Km [mM] raw 0.02+/-0.01

normalized_value_unit_evidence: kcat normalized_value=0.183 normalized_unit=s^-1 from 11+/-1 / 60; kcat/Km normalized_value=9.15 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=500+/-300 min^-1 mM^-1; Km normalized_value=0.02 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=11+/-1 raw_unit=min^-1; kcat/Km raw_value=500+/-300 raw_unit=min^-1 mM^-1; Km raw_value=0.02+/-0.01 raw_unit=mM


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

column_label: Table 3; enzyme row Nocardia otitidiscaviarum / trans-2-phenylcyclopropane-1-carboxylate; substrate column trans-2-phenylcyclopropane-1-carboxylate; metric rows kcat, Km, kcat/Km

raw_value_unit_evidence: paper Table 3 cells: kcat=48 min^-1; Km=1 mM; kcat/Km=46 min^-1 mM^-1

table_label: Table 3


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row noCAR (Nocardia otitidiscaviarum) / 3-Nitrobenzoic acid (7); kcat column kcat [min^-1] raw 59+/-2; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 24+/-3; Km column Km [mM] raw 2.5+/-0.3

normalized_value_unit_evidence: kcat normalized_value=0.983 normalized_unit=s^-1 from 59+/-2 / 60; kcat/Km normalized_value=0.3932 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=24+/-3 min^-1 mM^-1; Km normalized_value=2.5 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=59+/-2 raw_unit=min^-1; kcat/Km raw_value=24+/-3 raw_unit=min^-1 mM^-1; Km raw_value=2.5+/-0.3 raw_unit=mM


column_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring.; row noCAR (Nocardia otitidiscaviarum) / 3-Oxo-3-phenylpropanoic acid (12); kcat column kcat [min^-1] raw 63+/-2; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 210+/-20; Km column Km [mM] raw 0.29+/-0.03

normalized_value_unit_evidence: kcat normalized_value=1.05 normalized_unit=s^-1 from 63+/-2 / 60; kcat/Km normalized_value=3.620689655172414 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=210+/-20 min^-1 mM^-1; Km normalized_value=0.29 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=63+/-2 raw_unit=min^-1; kcat/Km raw_value=210+/-20 raw_unit=min^-1 mM^-1; Km raw_value=0.29+/-0.03 raw_unit=mM


column_label: Table 4. CAR activity against heterocycles and fatty acids.; row noCAR (Nocardia otitidiscaviarum) / Pyridine-2-carboxylic acid (14); kcat column kcat [min^-1] raw 76+/-4; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 3.9+/-0.4; Km column Km [mM] raw 20+/-2

normalized_value_unit_evidence: kcat normalized_value=1.27 normalized_unit=s^-1 from 76+/-4 / 60; kcat/Km normalized_value=0.0635 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=3.9+/-0.4 min^-1 mM^-1; Km normalized_value=20.0 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=76+/-4 raw_unit=min^-1; kcat/Km raw_value=3.9+/-0.4 raw_unit=min^-1 mM^-1; Km raw_value=20+/-2 raw_unit=mM


column_label: Table 4. CAR activity against heterocycles and fatty acids.; row noCAR (Nocardia otitidiscaviarum) / Dodecanoic acid (20); kcat column kcat [min^-1] raw 99+/-3; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 2500+/-300; Km column Km [mM] raw 0.04+/-0.01

normalized_value_unit_evidence: kcat normalized_value=1.65 normalized_unit=s^-1 from 99+/-3 / 60; kcat/Km normalized_value=41.25 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=2500+/-300 min^-1 mM^-1; Km normalized_value=0.04 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=99+/-3 raw_unit=min^-1; kcat/Km raw_value=2500+/-300 raw_unit=min^-1 mM^-1; Km raw_value=0.04+/-0.01 raw_unit=mM


column_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring.; row noCAR (Nocardia otitidiscaviarum) / (E)-3-Phenylprop-2-enoic acid (10); kcat column kcat [min^-1] raw 105+/-3; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 147+/-15; Km column Km [mM] raw 0.72+/-0.07

normalized_value_unit_evidence: kcat normalized_value=1.75 normalized_unit=s^-1 from 105+/-3 / 60; kcat/Km normalized_value=2.430555555555556 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=147+/-15 min^-1 mM^-1; Km normalized_value=0.72 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=105+/-3 raw_unit=min^-1; kcat/Km raw_value=147+/-15 raw_unit=min^-1 mM^-1; Km raw_value=0.72+/-0.07 raw_unit=mM


column_label: Table 4. CAR activity against heterocycles and fatty acids.; row noCAR (Nocardia otitidiscaviarum) / Thiophene-2-carboxylic acid (17); kcat column kcat [min^-1] raw 135+/-4; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 52+/-4; Km column Km [mM] raw 2.6+/-0.2

normalized_value_unit_evidence: kcat normalized_value=2.25 normalized_unit=s^-1 from 135+/-4 / 60; kcat/Km normalized_value=0.8653846153846153 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=52+/-4 min^-1 mM^-1; Km normalized_value=2.6 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=135+/-4 raw_unit=min^-1; kcat/Km raw_value=52+/-4 raw_unit=min^-1 mM^-1; Km raw_value=2.6+/-0.2 raw_unit=mM


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row noCAR (Nocardia otitidiscaviarum) / 3-Methoxybenzoic acid (4); kcat column kcat [min^-1] raw 136+/-5; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 150+/-10; Km column Km [mM] raw 0.9+/-0.1

normalized_value_unit_evidence: kcat normalized_value=2.27 normalized_unit=s^-1 from 136+/-5 / 60; kcat/Km normalized_value=2.522222222222222 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=150+/-10 min^-1 mM^-1; Km normalized_value=0.9 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=136+/-5 raw_unit=min^-1; kcat/Km raw_value=150+/-10 raw_unit=min^-1 mM^-1; Km raw_value=0.9+/-0.1 raw_unit=mM


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups row noCAR (Nocardia otitidiscaviarum), substrate column 4-Methylbenzoic acid (2), metric row k cat [min^-1], raw cell 135+/-5, normalized 2.25 s^-1; Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups row noCAR (Nocardia otitidiscaviarum), substrate column 4-Methylbenzoic acid (2), metric row k cat/K_m [min^-1 mM^-1], raw cell 110+/-20, normalized 1.83333333333333333333333333333 s^-1*mM^-1; Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups row noCAR (Nocardia otitidiscaviarum), substrate column 4-Methylbenzoic acid (2), metric row K_m [mM], raw cell 1.2+/-0.2, normalized 1.2 mM

normalized_value_unit_evidence: kcat normalized_value=2.25 normalized_unit=s^-1; kcat/Km normalized_value=1.83333333333333333333333333333 normalized_unit=s^-1*mM^-1; Km normalized_value=1.2 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=135 raw_unit=min^-1 raw_cell=135+/-5; kcat/Km raw_value=110 raw_unit=min^-1*mM^-1 raw_cell=110+/-20; Km raw_value=1.2 raw_unit=mM raw_cell=1.2+/-0.2

row_label: noCAR (Nocardia otitidiscaviarum) / 4-Methylbenzoic acid (2)


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row noCAR (Nocardia otitidiscaviarum) / 4-Methoxybenzoic acid (3); kcat column kcat [min^-1] raw 138+/-4; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 130+/-10; Km column Km [mM] raw 1.1+/-0.1

normalized_value_unit_evidence: kcat normalized_value=2.3 normalized_unit=s^-1 from 138+/-4 / 60; kcat/Km normalized_value=2.0909090909090904 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=130+/-10 min^-1 mM^-1; Km normalized_value=1.1 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=138+/-4 raw_unit=min^-1; kcat/Km raw_value=130+/-10 raw_unit=min^-1 mM^-1; Km raw_value=1.1+/-0.1 raw_unit=mM


column_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring.; row noCAR (Nocardia otitidiscaviarum) / 3-Phenylpropionic acid (9); kcat column kcat [min^-1] raw 140+/-4; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 52+/-4; Km column Km [mM] raw 2.7+/-0.2

normalized_value_unit_evidence: kcat normalized_value=2.33 normalized_unit=s^-1 from 140+/-4 / 60; kcat/Km normalized_value=0.8629629629629629 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=52+/-4 min^-1 mM^-1; Km normalized_value=2.7 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=140+/-4 raw_unit=min^-1; kcat/Km raw_value=52+/-4 raw_unit=min^-1 mM^-1; Km raw_value=2.7+/-0.2 raw_unit=mM


enzyme_display_name: benzaldehyde dehydrogenase (NAD+)

organism: Sorbus aucuparia

substrate_name: benzaldehyde

enzyme: benzaldehyde dehydrogenase (NAD+)

substrate: benzaldehyde


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


organism: Felis catus

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


organism: Acinetobacter calcoaceticus

substrate_name: K+

substrate: K+


organism: Pyrus pyrifolia


assay_conditions_summary: pH 9.5; 313.15 K; cofactor NAD+


organism: Mycobacterium marinum

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines: pH and temperature not specified in the publication

substrate: NADPH


substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


substrate_name: benzoic acid

substrate: benzoic acid


organism: Pseudomonas putida

substrate_name: DELTA1-piperidine 6-carboxylate

substrate: DELTA1-piperidine 6-carboxylate


organism: Ectopseudomonas oleovorans


enzyme_display_name: 2,5-dioxovalerate dehydrogenase

organism: Azospirillum brasilense

substrate_name: NADP+

protein_accession_database: UniProt

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1JUP4 and applied mutation signature R334Q/A337R/A442P/P444T to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; buffer A340 in 100 mM phosphate; cofactor NADP+

column_label: Table 2 (Kinetic characterization of KGSADH enzymes at pH 8), clone row '106-QR'; NADP+ column group: column 'kcat (s^-1)' = 4.0(±1.7); column 'Km (mM)' = 0.54(±0.038); column 'kcat/Km (s^-1 mM^-1)' = 7.2(±3.6).

normalized_value_unit_evidence: kcat: printed Table 2 cell 4.0 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 4.0 s^(-1). Km: printed Table 2 cell 0.54 mM; already in mM, no conversion (this paper prints no uM kinetic cell); the exported value is 0.54 mM. kcat/Km: printed Table 2 cell 7.2 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no conversion is applied and the paper-side value is 7.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, clone row '106-QR', NADP+ column group: kcat = 4.0 s^-1; Km = 0.54 mM; printed kcat/Km = 7.2 s^-1 mM^-1.

table_label: Table 2: Kinetic characterization of KGSADH enzymes at pH 8 (Scientific Reports 2017, 7:17155)

enzyme: 2,5-dioxovalerate dehydrogenase

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R334Q/A337R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: pH 8.0, 25°C, recombinant mutant R334Q/A337R


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1JUP4 and applied mutation signature K273A/R334Q/A337R/A442P/T443E/P444A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic characterization of KGSADH enzymes at pH 8), clone row '108-QR'; NADP+ column group: column 'kcat (s^-1)' = 4.5(±1.1); column 'Km (mM)' = 0.66(±0.065); column 'kcat/Km (s^-1 mM^-1)' = 6.9(±2.3).

normalized_value_unit_evidence: kcat: printed Table 2 cell 4.5 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 4.5 s^(-1). Km: printed Table 2 cell 0.66 mM; already in mM, no conversion (this paper prints no uM kinetic cell); the exported value is 0.66 mM. kcat/Km: printed Table 2 cell 6.9 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no conversion is applied and the paper-side value is 6.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, clone row '108-QR', NADP+ column group: kcat = 4.5 s^-1; Km = 0.66 mM; printed kcat/Km = 6.9 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1JUP4 and applied mutation signature A110S/K273A/R334Q/A337R/A442P/P444T to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic characterization of KGSADH enzymes at pH 8), clone row '104-QR'; NADP+ column group: column 'kcat (s^-1)' = 4.7(±0.79); column 'Km (mM)' = 0.70(±0.075); column 'kcat/Km (s^-1 mM^-1)' = 6.8(±1.8).

normalized_value_unit_evidence: kcat: printed Table 2 cell 4.7 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 4.7 s^(-1). Km: printed Table 2 cell 0.70 mM; already in mM, no conversion (this paper prints no uM kinetic cell); the exported value is 0.7 mM. kcat/Km: printed Table 2 cell 6.8 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no conversion is applied and the paper-side value is 6.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, clone row '104-QR', NADP+ column group: kcat = 4.7 s^-1; Km = 0.70 mM; printed kcat/Km = 6.8 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R334Q/A337R/A442P/P444T to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: pH 8.0, 25°C, recombinant mutant R334Q/A337R/A442P/P444T


smiles: C(CO)C=O

assay_conditions_summary: pH 8


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A110S/K273A/R334Q/A337R/A442P/P444T to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant A110S/K273A/R334Q/A337R/A442P/P444T


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K273A/R334Q/A337R/A442P/T443E/P444A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant K273A/R334Q/A337R/A442P/T443E/P444A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K273A/A442P/T443E/P444A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant K273A/A442P/T443E/P444A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A442P/P444T to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant A442P/P444T


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A110S/K273A/A442P/P444T to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant A110S/K273A/A442P/P444T


organism: Antirrhinum majus

substrate_name: phenylacetaldehyde

proof_lines: kcat is 0.31 sec(-1) with benzaldehyde as substrate (PubMed:19292760). kcat is 2.08 sec(-1) with acetaldehyde as substrate (PubMed:19292760). kcat is 0.23 sec(-1) with phenylacetaldehyde as substrate (PubMed:19292760).

source_databases_merged: brenda uniprot

substrate: phenylacetaldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


enzyme_display_name: Aldehyde dehydrogenase 1A1

organism: Bos taurus

substrate_name: all-trans retinal

source_db: uniprot

proof_lines: Has a much higher catalytic efficiency toward all-trans retinal.

enzyme: Aldehyde dehydrogenase 1A1

substrate: all-trans retinal

source: uniprot


substrate_name: propanal

smiles: CCC=O

substrate: propanal


organism: Bacillus subtilis (strain 168)

substrate_name: NAD(+) (at 25 degrees Celsius and pH 7.2)

assay_conditions_summary: pH 7.2; cofactor NAD+

proof_lines: kcat is 2.75 sec(-1) with alpha-ketoglutaric semialdehyde as substrate (in the presence of NAD(+)). kcat is 1.12 sec(-1) with alpha-ketoglutaric semialdehyde as substrate (in the presence of NADP(+)). kcat is 1.29 sec(-1) with propionaldehy


substrate_name: NADP(+) (at 25 degrees Celsius and pH 7.2)


enzyme_display_name: Malonate-semialdehyde dehydrogenase

substrate_name: malonate semialdehyde (at 30 degrees Celsius and pH 8.2)

proof_lines: kcat is 7.4 sec(-1) with malonate semialdehyde as substrate. kcat is 1.1 sec(-1) with methylmalonate semialdehyde as substrate.

enzyme: Malonate-semialdehyde dehydrogenase


substrate_name: methylmalonate semialdehyde (at 30 degrees Celsius and pH 8.2)

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


substrate_name: CoA (with malonate semialdehyde at 30 degrees Celsius and pH 8.2)

assay_conditions_summary: pH 8.2; cofactor CoA


substrate_name: NAD (with malonate semialdehyde at 30 degrees Celsius and pH 8.2)


enzyme_display_name: Alpha-ketoglutaric semialdehyde dehydrogenase 3

proof_lines: kcat is 21.3 sec(-1) with alpha-ketoglutaric semialdehyde as substrate (in the presence of NAD(+)). kcat is 23.0 sec(-1) with alpha-ketoglutaric semialdehyde as substrate (in the presence of NADP(+)).

substrate: NAD(+) (at 25 degrees Celsius and pH 7.2)


enzyme: Alpha-ketoglutaric semialdehyde dehydrogenase 3

substrate: NADP(+) (at 25 degrees Celsius and pH 7.2)


enzyme_display_name: Alpha-ketoglutaric semialdehyde dehydrogenase 2

proof_lines: kcat is 53.9 sec(-1) with alpha-ketoglutaric semialdehyde as substrate (in the presence of NAD(+)). kcat is 15.4 sec(-1) with alpha-ketoglutaric semialdehyde as substrate (in the presence of NADP(+)).


enzyme: Alpha-ketoglutaric semialdehyde dehydrogenase 2


organism: Saccharolobus solfataricus

substrate_name: glycolaldehyde

smiles: C(C=O)O

proof_lines: pH 6.0, 70°C, native enzyme form xylose-grown cells

substrate: glycolaldehyde


enzyme_display_name: Carboxylic acid reductase

organism: Nocardia iowensis

proof_lines: Vmax is 3 times higher than that of the natural enzyme when recombinant apo-Car is incubated with the purified PPTase Npt and CoA.

enzyme: Carboxylic acid reductase


organism: Rattus norvegicus

substrate_name: 9-cis retinal (at pH 7.5 and 25 degrees Celsius)

proof_lines: Has more than 2-fold higher catalytic efficiency for 9-cis retinal compared to all-trans retinal and 11-cis retinal.


substrate_name: NAD+


organism: Rhodococcus ruber

substrate_name: benzaldehyde

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


organism: Macaca fascicularis

substrate_name: all-trans retinal (at pH 7.5 and 25 degrees Celsius)

proof_lines: Has a nearly 2-fold higher catalytic efficiency for 9-cis retinal compared to all-trans and 13-cis retinal.


substrate_name: benzaldehyde (with NAD)

proof_lines: kcat is 8240 min(-1) with benzaldehyde and NAD as substrate. kcat is 2550 min(-1) with benzaldehyde and NADP as substrate.

substrate: benzaldehyde (with NAD)


organism: Oryctolagus cuniculus

smiles: CCCCCC(C=CC=O)O


substrate_name: malonaldehyde

smiles: C(C=O)C=O

substrate: malonaldehyde


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: benzoate

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

sequence_source: multiple

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

source_databases_merged: brenda skid uniprot

substrate: benzoate


enzyme_display_name: L-2-aminoadipate reductase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: NADPH

enzyme: L-2-aminoadipate reductase


organism: Burkholderia cepacia

assay_conditions_summary: pH 8.5; cofactor NAD+

proof_lines: pH 8.5, 25°C, with 2-hydroxy-5-methyl-muconic-6-semialdehyde as substrate

proof_lines: pH 8.5, 25°C, with 2-hydroxymuconate-6-semialdehyde as substrate

proof_lines: pH 8.5, 25°C, with 5-chloro-2-hydroxymuconic-6-semialdehyde as substrate

substrate: NAD+


organism: Mus musculus

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

proof_lines: Activity was measured with total soluble protein.


organism: Neurospora crassa

proof_lines: reduction of the intermediate benzoyladenylate to benzaldehyde

substrate: NADPH


organism: Homo sapiens

substrate_name: 2-aminomuconate 6-semialdehyde

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

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

substrate: 2-aminomuconate 6-semialdehyde


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R109A to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: mutant enzyme R109A, pH and temperature not specified in the publication


substrate_name: dodecanoate

column_label: Table 4. CAR activity against heterocycles and fatty acids.; row niCAR (Nocardia iowensis) / Dodecanoic acid (20); kcat column kcat [min^-1] raw 157+/-9; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 7000+/-2000; Km column Km [mM] raw 0.02+/-0.01

normalized_value_unit_evidence: kcat normalized_value=2.62 normalized_unit=s^-1 from 157+/-9 / 60; kcat/Km normalized_value=131.0 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=7000+/-2000 min^-1 mM^-1; Km normalized_value=0.02 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=157+/-9 raw_unit=min^-1; kcat/Km raw_value=7000+/-2000 raw_unit=min^-1 mM^-1; Km raw_value=0.02+/-0.01 raw_unit=mM

source_databases_merged: brenda skid

substrate: dodecanoate


substrate_name: Octanoate

smiles: CCCCCCCC(=O)[O-]

column_label: Table 4. CAR activity against heterocycles and fatty acids.; row niCAR (Nocardia iowensis) / Octanoic acid (19); kcat column kcat [min^-1] raw 233+/-5; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 1350+/-90; Km column Km [mM] raw 0.2+/-0.01

normalized_value_unit_evidence: kcat normalized_value=3.88 normalized_unit=s^-1 from 233+/-5 / 60; kcat/Km normalized_value=19.4 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=1350+/-90 min^-1 mM^-1; Km normalized_value=0.2 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=233+/-5 raw_unit=min^-1; kcat/Km raw_value=1350+/-90 raw_unit=min^-1 mM^-1; Km raw_value=0.2+/-0.01 raw_unit=mM

substrate: Octanoate


substrate_name: Butanoate

column_label: Table 4. CAR activity against heterocycles and fatty acids.; row niCAR (Nocardia iowensis) / Butanoic acid (18); kcat column kcat [min^-1] raw 260+/-30*; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 8+/-1*; Km column Km [mM] raw 32+/-4*

normalized_value_unit_evidence: kcat normalized_value=4.33 normalized_unit=s^-1 from 260+/-30* / 60; kcat/Km normalized_value=0.1353125 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=8+/-1* min^-1 mM^-1; Km normalized_value=32.0 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=260+/-30* raw_unit=min^-1; kcat/Km raw_value=8+/-1* raw_unit=min^-1 mM^-1; Km raw_value=32+/-4* raw_unit=mM

substrate: Butanoate


enzyme_display_name: carboxylate reductase (NADP(+))

source_db: oed

column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row niCAR (Nocardia iowensis) / 3-Methoxybenzoic acid (4); kcat column kcat [min^-1] raw 93+/-1; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 137+/-6; Km column Km [mM] raw 0.68+/-0.03

normalized_value_unit_evidence: kcat normalized_value=1.55 normalized_unit=s^-1 from 93+/-1 / 60; kcat/Km normalized_value=2.2794117647058822 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=137+/-6 min^-1 mM^-1; Km normalized_value=0.68 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=93+/-1 raw_unit=min^-1; kcat/Km raw_value=137+/-6 raw_unit=min^-1 mM^-1; Km raw_value=0.68+/-0.03 raw_unit=mM

enzyme: carboxylate reductase (NADP(+))

source: oed


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row niCAR (Nocardia iowensis) / 3-Nitrobenzoic acid (7); kcat column kcat [min^-1] raw 18+/-1; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 3.2+/-0.4; Km column Km [mM] raw 5.6+/-0.7

normalized_value_unit_evidence: kcat normalized_value=0.3 normalized_unit=s^-1 from 18+/-1 / 60; kcat/Km normalized_value=0.053571428571428575 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=3.2+/-0.4 min^-1 mM^-1; Km normalized_value=5.6 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=18+/-1 raw_unit=min^-1; kcat/Km raw_value=3.2+/-0.4 raw_unit=min^-1 mM^-1; Km raw_value=5.6+/-0.7 raw_unit=mM


column_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring.; row niCAR (Nocardia iowensis) / 3-Oxo-3-phenylpropanoic acid (12); kcat column kcat [min^-1] raw 37.1+/-0.5; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 94+/-4; Km column Km [mM] raw 0.39+/-0.02

normalized_value_unit_evidence: kcat normalized_value=0.618 normalized_unit=s^-1 from 37.1+/-0.5 / 60; kcat/Km normalized_value=1.5846153846153845 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=94+/-4 min^-1 mM^-1; Km normalized_value=0.39 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=37.1+/-0.5 raw_unit=min^-1; kcat/Km raw_value=94+/-4 raw_unit=min^-1 mM^-1; Km raw_value=0.39+/-0.02 raw_unit=mM


column_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring.; row niCAR (Nocardia iowensis) / Phenylpropynoic acid (11); kcat column kcat [min^-1] raw 7+/-0.4; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 5+/-1; Km column Km [mM] raw 1.3+/-0.2

normalized_value_unit_evidence: kcat normalized_value=0.117 normalized_unit=s^-1 from 7+/-0.4 / 60; kcat/Km normalized_value=0.09 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=5+/-1 min^-1 mM^-1; Km normalized_value=1.3 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=7+/-0.4 raw_unit=min^-1; kcat/Km raw_value=5+/-1 raw_unit=min^-1 mM^-1; Km raw_value=1.3+/-0.2 raw_unit=mM


column_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring.; row niCAR (Nocardia iowensis) / 3-Phenylpropionic acid (9); kcat column kcat [min^-1] raw 85.8+/-0.9; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 88+/-3; Km column Km [mM] raw 0.97+/-0.03

normalized_value_unit_evidence: kcat normalized_value=1.43 normalized_unit=s^-1 from 85.8+/-0.9 / 60; kcat/Km normalized_value=1.4742268041237112 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=88+/-3 min^-1 mM^-1; Km normalized_value=0.97 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=85.8+/-0.9 raw_unit=min^-1; kcat/Km raw_value=88+/-3 raw_unit=min^-1 mM^-1; Km raw_value=0.97+/-0.03 raw_unit=mM


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row niCAR (Nocardia iowensis) / 4-Methoxybenzoic acid (3); kcat column kcat [min^-1] raw 49+/-1; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 200+/-10; Km column Km [mM] raw 0.25+/-0.01

normalized_value_unit_evidence: kcat normalized_value=0.82 normalized_unit=s^-1 from 49+/-1 / 60; kcat/Km normalized_value=3.28 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=200+/-10 min^-1 mM^-1; Km normalized_value=0.25 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=49+/-1 raw_unit=min^-1; kcat/Km raw_value=200+/-10 raw_unit=min^-1 mM^-1; Km raw_value=0.25+/-0.01 raw_unit=mM


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row niCAR (Nocardia iowensis) / 4-Methylbenzoic acid (2); kcat column kcat [min^-1] raw 94+/-2; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 97+/-6; Km column Km [mM] raw 1.0+/-0.1

normalized_value_unit_evidence: kcat normalized_value=1.57 normalized_unit=s^-1 from 94+/-2 / 60; kcat/Km normalized_value=1.57 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=97+/-6 min^-1 mM^-1; Km normalized_value=1.0 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=94+/-2 raw_unit=min^-1; kcat/Km raw_value=97+/-6 raw_unit=min^-1 mM^-1; Km raw_value=1.0+/-0.1 raw_unit=mM


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row niCAR (Nocardia iowensis) / Benzoic acid (1); kcat column kcat [min^-1] raw 98+/-7; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 103+/-9; Km column Km [mM] raw 0.9+/-0.1

normalized_value_unit_evidence: kcat normalized_value=1.63 normalized_unit=s^-1 from 98+/-7 / 60; kcat/Km normalized_value=1.811111111111111 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=103+/-9 min^-1 mM^-1; Km normalized_value=0.9 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=98+/-7 raw_unit=min^-1; kcat/Km raw_value=103+/-9 raw_unit=min^-1 mM^-1; Km raw_value=0.9+/-0.1 raw_unit=mM


smiles: CCCC(=O)O

row_label: niCAR (Nocardia iowensis) / Butanoic acid (18)

table_label: Table 4. CAR activity against heterocycles and fatty acids.


smiles: CCCCCCCCCCCC(=O)O

row_label: niCAR (Nocardia iowensis) / Dodecanoic acid (20)


column_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring.; row niCAR (Nocardia iowensis) / (E)-3-Phenylprop-2-enoic acid (10); kcat column kcat [min^-1] raw 7.7+/-0.7; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 170+/-70; Km column Km [mM] raw 0.05+/-0.02

normalized_value_unit_evidence: kcat normalized_value=0.128 normalized_unit=s^-1 from 7.7+/-0.7 / 60; kcat/Km normalized_value=2.56 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=170+/-70 min^-1 mM^-1; Km normalized_value=0.05 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=7.7+/-0.7 raw_unit=min^-1; kcat/Km raw_value=170+/-70 raw_unit=min^-1 mM^-1; Km raw_value=0.05+/-0.02 raw_unit=mM


substrate_name: octadecanoate

smiles: CCCCCCCCCCCCCCCCCC(=O)O

column_label: Table 4. CAR activity against heterocycles and fatty acids.; row niCAR (Nocardia iowensis) / Octadecanoic acid (21); kcat column kcat [min^-1] raw 68+/-7; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 100+/-20; Km column Km [mM] raw 0.7+/-0.1

normalized_value_unit_evidence: kcat normalized_value=1.13 normalized_unit=s^-1 from 68+/-7 / 60; kcat/Km normalized_value=1.6142857142857143 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=100+/-20 min^-1 mM^-1; Km normalized_value=0.7 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=68+/-7 raw_unit=min^-1; kcat/Km raw_value=100+/-20 raw_unit=min^-1 mM^-1; Km raw_value=0.7+/-0.1 raw_unit=mM

substrate: octadecanoate


row_label: niCAR (Nocardia iowensis) / Octanoic acid (19)


column_label: Table 4. CAR activity against heterocycles and fatty acids.; row niCAR (Nocardia iowensis) / Thiophene-2-carboxylic acid (17); kcat column kcat [min^-1] raw 60.8+/-0.9; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 58+/-3; Km column Km [mM] raw 1.00+/-0.05

normalized_value_unit_evidence: kcat normalized_value=1.01 normalized_unit=s^-1 from 60.8+/-0.9 / 60; kcat/Km normalized_value=1.01 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=58+/-3 min^-1 mM^-1; Km normalized_value=1.0 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=60.8+/-0.9 raw_unit=min^-1; kcat/Km raw_value=58+/-3 raw_unit=min^-1 mM^-1; Km raw_value=1.00+/-0.05 raw_unit=mM


column_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring.; row niCAR (Nocardia iowensis) / trans-2-Phenylcyclopropane-1-carboxylic acid (13); kcat column kcat [min^-1] raw 10.8+/-0.3; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 51+/-5; Km column Km [mM] raw 0.21+/-0.02

normalized_value_unit_evidence: kcat normalized_value=0.18 normalized_unit=s^-1 from 10.8+/-0.3 / 60; kcat/Km normalized_value=0.8571428571428571 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=51+/-5 min^-1 mM^-1; Km normalized_value=0.21 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=10.8+/-0.3 raw_unit=min^-1; kcat/Km raw_value=51+/-5 raw_unit=min^-1 mM^-1; Km raw_value=0.21+/-0.02 raw_unit=mM


enzyme_display_name: benzaldehyde dehydrogenase (NAD(+))

organism: Pseudomonas putida

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NAD+

column_label: Article PDF page 7, Table III, row p-chlorobenzaldehyde, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); cells 1.2 +/- 0.2, 135 +/- 2, and 11 x 10^7.

raw_value_unit_evidence: Table III row p-chlorobenzaldehyde: Km 1.2 +/- 0.2 uM; kcat 135 +/- 2 s^-1; kcat/Km 11 x 10^7 M^-1 s^-1.

row_label: p-chlorobenzaldehyde

table_label: Table III. Reaction of PpBADH with substituted benzaldehydes

enzyme: benzaldehyde dehydrogenase (NAD(+))


column_label: Article PDF page 7, Table III, row p-nitrobenzaldehyde, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); cells 9.3 +/- 0.8, 95 +/- 3, and 1.0 x 10^7.

raw_value_unit_evidence: Table III row p-nitrobenzaldehyde: Km 9.3 +/- 0.8 uM; kcat 95 +/- 3 s^-1; kcat/Km 1.0 x 10^7 M^-1 s^-1.

row_label: p-nitrobenzaldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E215D to reconstruct the assayed variant sequence.

column_label: Article PDF page 7, Table II, PpBADH row E215D, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); cells 28 +/- 3.9, 1.5 +/- 0.2, and 5.4 x 10^4.

normalized_value_unit_evidence: Km 0.028 mM; kcat 1.5 s^-1; printed kcat/Km 54 s^-1 mM^-1.

row_label: PpBADH E215D

table_label: Table II. Comparison of kinetic parameters of PpBADH variants and selected other ALDHs

substrate: benzaldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E337D to reconstruct the assayed variant sequence.

column_label: Article PDF page 7, Table II, PpBADH row E337D, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); cells 6.6 +/- 0.7, 45 +/- 1, and 6.8 x 10^6.

normalized_value_unit_evidence: Km 0.0066 mM; kcat 45 s^-1; printed kcat/Km 6800 s^-1 mM^-1.

row_label: PpBADH E337D


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E337L to reconstruct the assayed variant sequence.

column_label: Article PDF page 7, Table II, PpBADH row E337L, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); cells 20 +/- 1.5, 1.3 +/- 0.1, and 6.5 x 10^4.

normalized_value_unit_evidence: Km 0.02 mM; kcat 1.3 s^-1; printed kcat/Km 65 s^-1 mM^-1.

row_label: PpBADH E337L


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E337Q to reconstruct the assayed variant sequence.

column_label: Article PDF page 7, Table II, PpBADH row E337Q, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); cells 20 +/- 1.6, 0.8 +/- 0.1, and 4.0 x 10^4.

normalized_value_unit_evidence: Km 0.02 mM; kcat 0.8 s^-1; printed kcat/Km 40 s^-1 mM^-1.

row_label: PpBADH E337Q


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

column_label: Article PDF page 7, Table III, row Benzaldehyde, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); cells 4.4 +/- 2.2, 156 +/- 29, and 3.5 x 10^7.

raw_value_unit_evidence: Table III row Benzaldehyde: Km 4.4 +/- 2.2 uM; kcat 156 +/- 29 s^-1; kcat/Km 3.5 x 10^7 M^-1 s^-1.

row_label: Benzaldehyde


column_label: Article PDF page 7, Table III, row p-methoxybenzaldehyde, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); cells 2.0 +/- 0.3, 116 +/- 4, and 5.8 x 10^7.

raw_value_unit_evidence: Table III row p-methoxybenzaldehyde: Km 2.0 +/- 0.3 uM; kcat 116 +/- 4 s^-1; kcat/Km 5.8 x 10^7 M^-1 s^-1.

row_label: p-methoxybenzaldehyde


column_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring.; row niCAR (Nocardia iowensis) / Phenylpropynoic acid (11); kcat column kcat [min^-1] raw 7+/-0.4; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 5+/-1; Km column Km [mM] raw 1.3+/-0.2


row_label: niCAR (Nocardia iowensis) / (E)-3-Phenylprop-2-enoic acid (10)

table_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring.


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row niCAR (Nocardia iowensis) / 3-Nitrobenzoic acid (7); kcat column kcat [min^-1] raw 18+/-1; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 3.2+/-0.4; Km column Km [mM] raw 5.6+/-0.7


column_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring.; row niCAR (Nocardia iowensis) / 3-Oxo-3-phenylpropanoic acid (12); kcat column kcat [min^-1] raw 37.1+/-0.5; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 94+/-4; Km column Km [mM] raw 0.39+/-0.02


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row niCAR (Nocardia iowensis) / 4-Methoxybenzoic acid (3); kcat column kcat [min^-1] raw 49+/-1; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 200+/-10; Km column Km [mM] raw 0.25+/-0.01


row_label: niCAR (Nocardia iowensis) / Thiophene-2-carboxylic acid (17)


smiles: CCCCCCCCCCCCCCCCCC(=O)[O-]

row_label: niCAR (Nocardia iowensis) / Octadecanoic acid (21)


column_label: Table 3. CAR activity against benzoic acid derivatives with the carboxylic acid group extended from the ring.; row niCAR (Nocardia iowensis) / 3-Phenylpropionic acid (9); kcat column kcat [min^-1] raw 85.8+/-0.9; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 88+/-3; Km column Km [mM] raw 0.97+/-0.03


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row niCAR (Nocardia iowensis) / 3-Methoxybenzoic acid (4); kcat column kcat [min^-1] raw 93+/-1; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 137+/-6; Km column Km [mM] raw 0.68+/-0.03


column_label: Table 2. CAR activity against benzoic acid and its derivatives with electron-donating and -withdrawing groups.; row niCAR (Nocardia iowensis) / 4-Methylbenzoic acid (2); kcat column kcat [min^-1] raw 94+/-2; kcat/Km column kcat/Km [min^-1 mM^-1] plus same-row kcat/Km calculation raw 97+/-6; Km column Km [mM] raw 1.0+/-0.1


substrate_name: nonanal

smiles: CCCCCCCCC=O

column_label: Table 1; row Nonanal; Km column

normalized_value_unit_evidence: Km=0.0285 mM converted from 28.5 uM

raw_value_unit_evidence: Table 1 Nonanal Km 28.5 +/- 4.8 uM

row_label: Nonanal

table_label: Table 1

substrate: nonanal


smiles: CCCCCCC=CC=O

column_label: Table 1; row trans-2-Nonenal; Km column

normalized_value_unit_evidence: Km=0.0053 mM converted from 5.3 uM

raw_value_unit_evidence: Table 1 trans-2-Nonenal Km 5.3 +/- 0.7 uM


column_label: Table 1; row Hexanal; Km column

normalized_value_unit_evidence: Km=0.0391 mM converted from 39.1 uM

raw_value_unit_evidence: Table 1 Hexanal Km 39.1 +/- 3.9 uM

row_label: Hexanal


substrate_name: octanal

smiles: CCCCCCCC=O

column_label: Table 1; row Octanal; Km column

normalized_value_unit_evidence: Km=0.0175 mM converted from 17.5 uM

raw_value_unit_evidence: Table 1 Octanal Km 17.5 +/- 2.1 uM

row_label: Octanal

substrate: octanal


substrate_name: betaine aldehyde

column_label: Table 1; row Betaine aldehyde; Km column

normalized_value_unit_evidence: Km=0.0411 mM converted from 41.1 uM

raw_value_unit_evidence: Table 1 Betaine aldehyde Km 41.1 +/- 9.3 uM

row_label: Betaine aldehyde

substrate: betaine aldehyde


substrate_name: L-2-aminoadipate 6-semialdehyde

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

column_label: Table 1; row AASA; Km column

normalized_value_unit_evidence: Km=0.169 mM converted from 169 uM

raw_value_unit_evidence: Table 1 AASA Km 169 +/- 9.5 uM

row_label: AASA

substrate: L-2-aminoadipate 6-semialdehyde


column_label: Table 1; row Benzaldehyde; Km column

normalized_value_unit_evidence: Km=0.5302 mM converted from 530.2 uM

raw_value_unit_evidence: Table 1 Benzaldehyde Km 530.2 +/- 86.3 uM


substrate_name: propanal

column_label: Table 1; row Propanal; Km column

normalized_value_unit_evidence: Km=0.6474 mM converted from 647.4 uM

raw_value_unit_evidence: Table 1 Propanal Km 647.4 +/- 38.5 uM

row_label: Propanal

substrate: propanal


substrate_name: glyceraldehyde

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

column_label: Table 1; row Glyceraldehyde; Km column

normalized_value_unit_evidence: Km=7.3743 mM converted from 7374.3 uM

raw_value_unit_evidence: Table 1 Glyceraldehyde Km 7374.3 +/- 117.2 uM

row_label: Glyceraldehyde

substrate: glyceraldehyde


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

assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADP+

column_label: Table 1. Kinetic parameters of KGSADH-I, KGSADH-II, KGSADH-III, and ycbD protein for alphaKGSA; row KGSADH-III / NADP+; columns Km (mM); kcat (s^-1); kcat/Km (s^-1*mM^-1); raw table cells: Km 0.0075 ± 0.0009 mM | kcat 23.0 ± 1.0 s^-1 | kcat/Km 3090 ± 250 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=23 normalized_unit=s^-1; Km normalized_value=0.008 normalized_unit=mM; kcat/Km normalized_value=2875 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=23.0 ± 1.0 raw_unit=s^-1; Km raw_value=0.0075 ± 0.0009 raw_unit=mM; kcat/Km raw_value=3090 ± 250 raw_unit=s^-1*mM^-1

row_label: KGSADH-III / NADP+


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NAD+

column_label: Table 1. Kinetic parameters of KGSADH-I, KGSADH-II, KGSADH-III, and ycbD protein for alphaKGSA; row KGSADH-II / NAD+; columns Km (mM); kcat (s^-1); kcat/Km (s^-1*mM^-1); raw table cells: Km 0.0246 ± 0.004 mM | kcat 53.9 ± 6.1 s^-1 | kcat/Km 2230 ± 176 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=53.9 normalized_unit=s^-1; Km normalized_value=0.025 normalized_unit=mM; kcat/Km normalized_value=2156 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=53.9 ± 6.1 raw_unit=s^-1; Km raw_value=0.0246 ± 0.004 raw_unit=mM; kcat/Km raw_value=2230 ± 176 raw_unit=s^-1*mM^-1

row_label: KGSADH-II / NAD+


substrate_name: NAD+

column_label: Table 2. Kinetic parameters of KGSADH-I, KGSADH-II, KGSADH-III, and ycbD protein for NAD+ and NADP+; row KGSADH-III / NAD+; columns Km (mM); kcat (s^-1); kcat/Km (s^-1*mM^-1); raw table cells: Km 1.136 ± 0.334 mM | kcat 52.3 ± 12 s^-1 | kcat/Km 47.2 ± 4.3 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=52.3 normalized_unit=s^-1; Km normalized_value=1.136 normalized_unit=mM; kcat/Km normalized_value=46.0387323943662 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=52.3 ± 12 raw_unit=s^-1; Km raw_value=1.136 ± 0.334 raw_unit=mM; kcat/Km raw_value=47.2 ± 4.3 raw_unit=s^-1*mM^-1

row_label: KGSADH-III / NAD+


column_label: Table 2. Kinetic parameters of KGSADH-I, KGSADH-II, KGSADH-III, and ycbD protein for NAD+ and NADP+; row KGSADH-II / NAD+; columns Km (mM); kcat (s^-1); kcat/Km (s^-1*mM^-1); raw table cells: Km 0.1169 ± 0.017 mM | kcat 35.5 ± 3.2 s^-1 | kcat/Km 307 ± 21 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=35.5 normalized_unit=s^-1; Km normalized_value=0.117 normalized_unit=mM; kcat/Km normalized_value=303.4188034188034 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=35.5 ± 3.2 raw_unit=s^-1; Km raw_value=0.1169 ± 0.017 raw_unit=mM; kcat/Km raw_value=307 ± 21 raw_unit=s^-1*mM^-1


substrate_name: NADP+

column_label: Table 2. Kinetic parameters of KGSADH-I, KGSADH-II, KGSADH-III, and ycbD protein for NAD+ and NADP+; row KGSADH-III / NADP+; columns Km (mM); kcat (s^-1); kcat/Km (s^-1*mM^-1); raw table cells: Km 0.0149 ± 0.0008 mM | kcat 15.3 ± 0.2 s^-1 | kcat/Km 1030 ± 46 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=15.3 normalized_unit=s^-1; Km normalized_value=0.015 normalized_unit=mM; kcat/Km normalized_value=1020.0000000000001 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=15.3 ± 0.2 raw_unit=s^-1; Km raw_value=0.0149 ± 0.0008 raw_unit=mM; kcat/Km raw_value=1030 ± 46 raw_unit=s^-1*mM^-1

substrate: NADP+


column_label: Table 2. Kinetic parameters of KGSADH-I, KGSADH-II, KGSADH-III, and ycbD protein for NAD+ and NADP+; row KGSADH-II / NADP+; columns Km (mM); kcat (s^-1); kcat/Km (s^-1*mM^-1); raw table cells: Km 0.0622 ± 0.002 mM | kcat 10.2 ± 0.1 s^-1 | kcat/Km 164 ± 6.6 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=10.2 normalized_unit=s^-1; Km normalized_value=0.062 normalized_unit=mM; kcat/Km normalized_value=164.51612903225805 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=10.2 ± 0.1 raw_unit=s^-1; Km raw_value=0.0622 ± 0.002 raw_unit=mM; kcat/Km raw_value=164 ± 6.6 raw_unit=s^-1*mM^-1

row_label: KGSADH-II / NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A110S/K273A/A442P/P444T to reconstruct the assayed variant sequence.

smiles: O=CCCO

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

column_label: PDF Table 2 row 104; substrate block 3-hydroxypropionaldehyde; columns kcat 15 s^-1, Km 2.2 mM, printed kcat/Km 7 s^-1 mM^-1; export-normalized kcat/Km 6.81818181818182 from same-row values

normalized_value_unit_evidence: kcat normalized_value=15 normalized_unit=s^-1; Km normalized_value=2.2 normalized_unit=mM; kcat/Km normalized_value=6.81818181818182 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=15 raw_unit=s^-1; Km raw_value=2.2 raw_unit=mM for 3-hydroxypropionaldehyde; printed kcat/Km=7 s^-1 mM^-1

table_label: Table 2. Kinetic characterization of KGSADH enzymes at pH 8


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A110S/K273A/R334Q/A337R/A442P/P444T to reconstruct the assayed variant sequence.

column_label: PDF Table 2 row 104-QR; substrate block 3-hydroxypropionaldehyde; columns kcat 6.7 s^-1, Km 0.43 mM, printed kcat/Km 16 s^-1 mM^-1; export-normalized kcat/Km 15.5813953488372 from same-row values

normalized_value_unit_evidence: kcat normalized_value=6.7 normalized_unit=s^-1; Km normalized_value=0.43 normalized_unit=mM; kcat/Km normalized_value=15.5813953488372 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=6.7 raw_unit=s^-1; Km raw_value=0.43 raw_unit=mM for 3-hydroxypropionaldehyde; printed kcat/Km=16 s^-1 mM^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A442P/P444T to reconstruct the assayed variant sequence.

column_label: PDF Table 2 row 106; substrate block 3-hydroxypropionaldehyde; columns kcat 12 s^-1, Km 1.4 mM, printed kcat/Km 9 s^-1 mM^-1; export-normalized kcat/Km 8.57142857142857 from same-row values

normalized_value_unit_evidence: kcat normalized_value=12 normalized_unit=s^-1; Km normalized_value=1.4 normalized_unit=mM; kcat/Km normalized_value=8.57142857142857 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=12 raw_unit=s^-1; Km raw_value=1.4 raw_unit=mM for 3-hydroxypropionaldehyde; printed kcat/Km=9 s^-1 mM^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K273A/A442P/T443E/P444A to reconstruct the assayed variant sequence.

column_label: PDF Table 2 row 108; substrate block 3-hydroxypropionaldehyde; columns kcat 11 s^-1, Km 0.78 mM, printed kcat/Km 14 s^-1 mM^-1; export-normalized kcat/Km 14.1025641025641 from same-row values

normalized_value_unit_evidence: kcat normalized_value=11 normalized_unit=s^-1; Km normalized_value=0.78 normalized_unit=mM; kcat/Km normalized_value=14.1025641025641 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=11 raw_unit=s^-1; Km raw_value=0.78 raw_unit=mM for 3-hydroxypropionaldehyde; printed kcat/Km=14 s^-1 mM^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K273A/R334Q/A337R/A442P/T443E/P444A to reconstruct the assayed variant sequence.

column_label: PDF Table 2 row 108-QR; substrate block 3-hydroxypropionaldehyde; columns kcat 6 s^-1, Km 0.17 mM, printed kcat/Km 35 s^-1 mM^-1; export-normalized kcat/Km 35.2941176470588 from same-row values

normalized_value_unit_evidence: kcat normalized_value=6 normalized_unit=s^-1; Km normalized_value=0.17 normalized_unit=mM; kcat/Km normalized_value=35.2941176470588 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=6 raw_unit=s^-1; Km raw_value=0.17 raw_unit=mM for 3-hydroxypropionaldehyde; printed kcat/Km=35 s^-1 mM^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R334Q/A337R to reconstruct the assayed variant sequence.

column_label: PDF Table 2 row WT-QR; substrate block 3-hydroxypropionaldehyde; columns kcat 6.8 s^-1, Km 0.55 mM, printed kcat/Km 12 s^-1 mM^-1; export-normalized kcat/Km 12.3636363636364 from same-row values

normalized_value_unit_evidence: kcat normalized_value=6.8 normalized_unit=s^-1; Km normalized_value=0.55 normalized_unit=mM; kcat/Km normalized_value=12.3636363636364 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=6.8 raw_unit=s^-1; Km raw_value=0.55 raw_unit=mM for 3-hydroxypropionaldehyde; printed kcat/Km=12 s^-1 mM^-1

row_label: WT-QR


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R334Q/A337R/A442P/P444T to reconstruct the assayed variant sequence.

column_label: PDF Table 2 row 106-QR; substrate block 3-hydroxypropionaldehyde; columns kcat 5 s^-1, Km 0.29 mM, printed kcat/Km 17 s^-1 mM^-1; export-normalized kcat/Km 17.2413793103448 from same-row values

normalized_value_unit_evidence: kcat normalized_value=5 normalized_unit=s^-1; Km normalized_value=0.29 normalized_unit=mM; kcat/Km normalized_value=17.2413793103448 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=5 raw_unit=s^-1; Km raw_value=0.29 raw_unit=mM for 3-hydroxypropionaldehyde; printed kcat/Km=17 s^-1 mM^-1


column_label: PDF Table 2 row KGSADH; substrate block 3-hydroxypropionaldehyde; columns kcat 15 s^-1, Km 1.6 mM, printed kcat/Km 9 s^-1 mM^-1; export-normalized kcat/Km 9.375 from same-row values

normalized_value_unit_evidence: kcat normalized_value=15 normalized_unit=s^-1; Km normalized_value=1.6 normalized_unit=mM; kcat/Km normalized_value=9.375 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=15 raw_unit=s^-1; Km raw_value=1.6 raw_unit=mM for 3-hydroxypropionaldehyde; printed kcat/Km=9 s^-1 mM^-1

row_label: KGSADH


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

column_label: PDF Table 2 row 104; substrate block NAD+; columns kcat 19 s^-1, Km 0.28 mM, printed kcat/Km 68 s^-1 mM^-1; export-normalized kcat/Km 67.8571428571428 from same-row values

normalized_value_unit_evidence: kcat normalized_value=19 normalized_unit=s^-1; Km normalized_value=0.28 normalized_unit=mM; kcat/Km normalized_value=67.8571428571428 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=19 raw_unit=s^-1; Km raw_value=0.28 raw_unit=mM for NAD+; printed kcat/Km=68 s^-1 mM^-1


column_label: PDF Table 2 row 104-QR; substrate block NAD+; columns kcat 5.9 s^-1, Km 0.033 mM, printed kcat/Km 179 s^-1 mM^-1; export-normalized kcat/Km 178.787878787879 from same-row values

normalized_value_unit_evidence: kcat normalized_value=5.9 normalized_unit=s^-1; Km normalized_value=0.033 normalized_unit=mM; kcat/Km normalized_value=178.787878787879 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=5.9 raw_unit=s^-1; Km raw_value=0.033 raw_unit=mM for NAD+; printed kcat/Km=179 s^-1 mM^-1


column_label: PDF Table 2 row 106; substrate block NAD+; columns kcat 20 s^-1, Km 0.27 mM, printed kcat/Km 74 s^-1 mM^-1; export-normalized kcat/Km 74.0740740740741 from same-row values

normalized_value_unit_evidence: kcat normalized_value=20 normalized_unit=s^-1; Km normalized_value=0.27 normalized_unit=mM; kcat/Km normalized_value=74.0740740740741 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=20 raw_unit=s^-1; Km raw_value=0.27 raw_unit=mM for NAD+; printed kcat/Km=74 s^-1 mM^-1


column_label: PDF Table 2 row 108; substrate block NAD+; columns kcat 18 s^-1, Km 0.27 mM, printed kcat/Km 67 s^-1 mM^-1; export-normalized kcat/Km 66.6666666666667 from same-row values

normalized_value_unit_evidence: kcat normalized_value=18 normalized_unit=s^-1; Km normalized_value=0.27 normalized_unit=mM; kcat/Km normalized_value=66.6666666666667 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=18 raw_unit=s^-1; Km raw_value=0.27 raw_unit=mM for NAD+; printed kcat/Km=67 s^-1 mM^-1


column_label: PDF Table 2 row 108-QR; substrate block NAD+; columns kcat 6.1 s^-1, Km 0.037 mM, printed kcat/Km 165 s^-1 mM^-1; export-normalized kcat/Km 164.864864864865 from same-row values

normalized_value_unit_evidence: kcat normalized_value=6.1 normalized_unit=s^-1; Km normalized_value=0.037 normalized_unit=mM; kcat/Km normalized_value=164.864864864865 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=6.1 raw_unit=s^-1; Km raw_value=0.037 raw_unit=mM for NAD+; printed kcat/Km=165 s^-1 mM^-1


column_label: PDF Table 2 row WT-QR; substrate block NAD+; columns kcat 7.9 s^-1, Km 0.044 mM, printed kcat/Km 180 s^-1 mM^-1; export-normalized kcat/Km 179.545454545455 from same-row values

normalized_value_unit_evidence: kcat normalized_value=7.9 normalized_unit=s^-1; Km normalized_value=0.044 normalized_unit=mM; kcat/Km normalized_value=179.545454545455 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=7.9 raw_unit=s^-1; Km raw_value=0.044 raw_unit=mM for NAD+; printed kcat/Km=180 s^-1 mM^-1


column_label: PDF Table 2 row 106-QR; substrate block NAD+; columns kcat 4.8 s^-1, Km 0.025 mM, printed kcat/Km 192 s^-1 mM^-1; export-normalized kcat/Km 192 from same-row values

normalized_value_unit_evidence: kcat normalized_value=4.8 normalized_unit=s^-1; Km normalized_value=0.025 normalized_unit=mM; kcat/Km normalized_value=192 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=4.8 raw_unit=s^-1; Km raw_value=0.025 raw_unit=mM for NAD+; printed kcat/Km=192 s^-1 mM^-1


column_label: PDF Table 2 row 104-QR; substrate block NADP+; columns kcat 4.7 s^-1, Km 0.7 mM, printed kcat/Km 6.8 s^-1 mM^-1; export-normalized kcat/Km 6.71428571428572 from same-row values

normalized_value_unit_evidence: kcat normalized_value=4.7 normalized_unit=s^-1; Km normalized_value=0.7 normalized_unit=mM; kcat/Km normalized_value=6.71428571428572 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=4.7 raw_unit=s^-1; Km raw_value=0.7 raw_unit=mM for NADP+; printed kcat/Km=6.8 s^-1 mM^-1


column_label: PDF Table 2 row 108-QR; substrate block NADP+; columns kcat 4.5 s^-1, Km 0.66 mM, printed kcat/Km 6.9 s^-1 mM^-1; export-normalized kcat/Km 6.81818181818182 from same-row values

normalized_value_unit_evidence: kcat normalized_value=4.5 normalized_unit=s^-1; Km normalized_value=0.66 normalized_unit=mM; kcat/Km normalized_value=6.81818181818182 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=4.5 raw_unit=s^-1; Km raw_value=0.66 raw_unit=mM for NADP+; printed kcat/Km=6.9 s^-1 mM^-1


column_label: PDF Table 2 row WT-QR; substrate block NADP+; columns kcat 4.4 s^-1, Km 0.81 mM, printed kcat/Km 5.4 s^-1 mM^-1; export-normalized kcat/Km 5.4320987654321 from same-row values

normalized_value_unit_evidence: kcat normalized_value=4.4 normalized_unit=s^-1; Km normalized_value=0.81 normalized_unit=mM; kcat/Km normalized_value=5.4320987654321 normalized_unit=s^-1*mM^-1 from same-row values

raw_value_unit_evidence: kcat raw_value=4.4 raw_unit=s^-1; Km raw_value=0.81 raw_unit=mM for NADP+; printed kcat/Km=5.4 s^-1 mM^-1


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1JUP4 and applied mutation signature R334Q/A337R/A442P/P444T to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; buffer A340 in 100 mM phosphate; cofactor NAD+

column_label: Table 2 (Kinetic characterization of KGSADH enzymes at pH 8), clone row '106-QR'; NADP+ column group: column 'kcat (s^-1)' = 4.0(±1.7); column 'Km (mM)' = 0.54(±0.038); column 'kcat/Km (s^-1 mM^-1)' = 7.2(±3.6).

normalized_value_unit_evidence: kcat: printed Table 2 cell 4.0 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 4.0 s^(-1). Km: printed Table 2 cell 0.54 mM; already in mM, no conversion (this paper prints no uM kinetic cell); the exported value is 0.54 mM. kcat/Km: printed Table 2 cell 7.2 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no conversion is applied and the paper-side value is 7.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, clone row '106-QR', NADP+ column group: kcat = 4.0 s^-1; Km = 0.54 mM; printed kcat/Km = 7.2 s^-1 mM^-1.


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

proof_lines: oxidized 2-hydroxymuconate semialdehyde more efficiently


proof_lines: substituted benzaldehydes depended on ring substitution


assay_conditions_summary: cofactor NAD+

proof_lines: benzaldehyde dehydrogenase substrate-specificity paper


proof_lines:
substituted benzaldehydes
benzaldehyde dehydrogenase
row-aligned kinetic value


proof_lines: electron-withdrawing groups at positions 3 and 4


organism: Acinetobacter baylyi

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADP+

proof_lines:
Table 5
NAD+
NADP+


substrate_name: Acetaldehyde

smiles: CC=O

column_label: Table 5: Kinetic parameters of alpha-KGSA dehydrogenase oxidations; row Acetaldehyde (NADP+) row; metric columns Km, kcat, and/or kcat/Km; Acetaldehyde (NADP+) row: Km = 3900 +/- 900 uM, kcat = 0.41 +/- 0.03 s^-1, kcat/Km = 1.0 x 10^2 s^-1 M^-1.

normalized_value_unit_evidence: 3900 uM = 3.9 mM; kcat/Km normalized from components = 0.10512820512820513 s^-1 mM^-1.

row_label: Acetaldehyde (NADP+) row

substrate: Acetaldehyde


substrate_name: Glutaral

smiles: O=CCCCC=O

column_label: Table 5: Kinetic parameters of alpha-KGSA dehydrogenase oxidations; row Glutaraldehyde; NADP+ row; metric columns Km, kcat, and/or kcat/Km; Glutaraldehyde NADP+ row: Km = 310 +/- 30 uM, kcat = 4.13 +/- 0.08 s^-1, kcat/Km = 1.3 x 10^4 s^-1 M^-1.

normalized_value_unit_evidence: 310 uM = 0.31 mM; kcat/Km normalized from components = 13.32258064516129 s^-1 mM^-1.

row_label: Glutaraldehyde; NADP+ row

substrate: Glutaral


substrate_name: Succinate semialdehyde

smiles: O=CCCC(=O)O

proof_lines:
Table 5
succinate semialdehyde
NAD+

substrate: Succinate semialdehyde


smiles: CCC=O

column_label: Table 5: Kinetic parameters of alpha-KGSA dehydrogenase oxidations; row Propanal; NADP+ row; metric columns Km, kcat, and/or kcat/Km; Propanal NADP+ row: Km = 1050 +/- 40 uM, kcat = 2.07 +/- 0.03 s^-1, kcat/Km = 2.0 x 10^3 s^-1 M^-1.

normalized_value_unit_evidence: 1050 uM = 1.05 mM; kcat/Km normalized from components = 1.971428571428571 s^-1 mM^-1.

row_label: Propanal; NADP+ row


enzyme_display_name: Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial

column_label: Table III; Constant section Michaelis constant (Km); substrate row methylmalonate semialdehyde; value 5.3 uM.

raw_value_unit_evidence: Table III Michaelis constant row: methylmalonate semialdehyde 5.3 uM.

row_label: Michaelis constant (Km), methylmalonate semialdehyde

table_label: Table III. Kinetic characterization of methylmalonate-semialdehyde dehydrogenase


column_label: Table III; Maximum velocity row malonate semialdehyde = 9.4 units/mg; Michaelis constant row malonate semialdehyde = 4.5 uM.

normalized_value_unit_evidence: Paper Km 0.0045 mM; current/export Km 0.0094 mM.

raw_value_unit_evidence: Table III separates malonate semialdehyde Vmax 9.4 units/mg from Km 4.5 uM.

row_label: Michaelis constant (Km), malonate semialdehyde

enzyme: Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial


substrate_name: NAD(+)

column_label: Table III; Constant section Michaelis constant (Km); substrate row NAD+; value 150 uM.

raw_value_unit_evidence: Table III Michaelis constant row: NAD+ 150 uM.

row_label: Michaelis constant (Km), NAD+

substrate: NAD(+)


substrate_name: CoA

assay_conditions_summary: cofactor CoA

column_label: Table III; Constant section Michaelis constant (Km); substrate row CoA; value 30 uM.

raw_value_unit_evidence: Table III Michaelis constant row: CoA 30 uM.

row_label: Michaelis constant (Km), CoA

substrate: CoA


organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)

substrate_name: NADP(+)

assay_conditions_summary: pH 7; cofactor NADP+

column_label: Km values (mM) cosubstrate / KGSADH column; KGSADH prose NADP+

normalized_value_unit_evidence: KGSADH prose supports Km 0.03 mM for NADP+.

raw_value_unit_evidence: Table 4 KGSADH cosubstrate row gives (0.03 +/- 0.002) mM; KGSADH prose directly reports NADP+ Km 0.03 +/- 0.002 mM.

row_label: KGSADH/HVO_B0039; NADP+ cosubstrate

table_label: Table 4: Properties of enzymes involved in D-xylose degradation of H. volcanii; KGSADH section prose

substrate: NADP(+)


assay_conditions_summary: pH 7; cofactor NAD+

column_label: Km values (mM) cosubstrate / KGSADH column; KGSADH prose NAD+

normalized_value_unit_evidence: KGSADH prose supports Km 2.6 mM for NAD+.

raw_value_unit_evidence: Table 4 KGSADH cosubstrate row gives (2.6 +/- 0.55) mM; KGSADH prose directly reports NAD+ Km 2.6 +/- 0.55 mM.

row_label: KGSADH/HVO_B0039; NAD+ cosubstrate


substrate_name: glutaraldehyde

smiles: C(CC=O)CC=O

column_label: Km values (mM) substrate / KGSADH column

normalized_value_unit_evidence: Table 4 KGSADH column supports Km 1.16 mM for glutaraldehyde.

raw_value_unit_evidence: Table 4 KGSADH substrate row reports (1.16 +/- 0.21) mM for glutaraldehyde.

table_label: Table 4: Properties of enzymes involved in D-xylose degradation of H. volcanii

substrate: glutaraldehyde


substrate_name: succinate semialdehyde

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

normalized_value_unit_evidence: Table 4 KGSADH column supports Km 6.2 mM for succinate semialdehyde.

raw_value_unit_evidence: Table 4 KGSADH substrate row reports (6.2 +/- 1.8) mM for succinate semialdehyde.

row_label: KGSADH/HVO_B0039; succinate semialdehyde substrate

substrate: succinate semialdehyde


km_display: Not reported

assay_conditions_summary: pH 8.2; cofactor NADP+

column_label: MSDH prose states: PA kcat 0.03 s^-1, MSA kcat 0.02 s^-1, and D,L-MMSA kcat 0.003 s^-1.

raw_value_unit_evidence: D,L-MMSA (kcat 0.003 s^-1) in MSDH prose paragraph

row_label: SSO1218 MSDH; D,L-MMSA / methylmalonate semialdehyde

table_label: Prose: Methylmalonate semialdehyde dehydrogenase (MSDH), p. 209


substrate_name: methylmalonate semialdehyde

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

substrate: methylmalonate semialdehyde


substrate_name: malonate semialdehyde

substrate: malonate semialdehyde


substrate_name: propionaldehyde

substrate: propionaldehyde


column_label: Apparent Km (uM)

normalized_value_unit_evidence: Table 3 row 4-Fluorobenzaldehyde, Km 0.31 mM after uM-to-mM conversion.

raw_value_unit_evidence: Table 3 row 4-Fluorobenzaldehyde, Apparent Km column reports 310 uM.

table_label: Table 3: Kinetic parameters of benzaldehyde dehydrogenase


normalized_value_unit_evidence: Table 3 row 4-Nitrobenzaldehyde, Km 0.31 mM after uM-to-mM conversion.

raw_value_unit_evidence: Table 3 row 4-Nitrobenzaldehyde, Apparent Km column reports 310 uM.


normalized_value_unit_evidence: Table 3 row 2-Nitrobenzaldehyde, Km 0.48 mM after uM-to-mM conversion.

raw_value_unit_evidence: Table 3 row 2-Nitrobenzaldehyde, Apparent Km column reports 480 uM.


normalized_value_unit_evidence: Table 3 row 4-Chlorobenzaldehyde, Km 0.7 mM after uM-to-mM conversion.

raw_value_unit_evidence: Table 3 row 4-Chlorobenzaldehyde, Apparent Km column reports 700 uM.


normalized_value_unit_evidence: Table 3 row 4-Methoxybenzaldehyde, Km 1.1 mM after uM-to-mM conversion.

raw_value_unit_evidence: Table 3 row 4-Methoxybenzaldehyde, Apparent Km column reports 1100 uM.


normalized_value_unit_evidence: Table 3 row 2-Fluorobenzaldehyde, Km 2.0 mM after uM-to-mM conversion.

raw_value_unit_evidence: Table 3 row 2-Fluorobenzaldehyde, Apparent Km column reports 2000 uM.


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

assay_conditions_summary: pH 9.2; cofactor CoA

column_label: Table VI; subgroup With CoA; row Methylmalonate semialdehyde; Km column on 10^-5 M scale; raw 1.9; normalized 0.019 mM

raw_value_unit_evidence: Printed page 1834, Table VI, With CoA, Methylmalonate semialdehyde row: Km entry 1.9 on the 10^-5 M scale

row_label: With CoA / Methylmalonate semialdehyde

table_label: Table VI


column_label: Table VI; subgroup With CoA; row NAD; Km column on 10^-5 M scale; raw 8.2; normalized 0.082 mM

raw_value_unit_evidence: Printed page 1834, Table VI, With CoA, NAD row: Km entry 8.2 on the 10^-5 M scale

row_label: With CoA / NAD


column_label: Table VI; subgroup With CoA; row CoA; Km column on 10^-5 M scale; raw 2.2; normalized 0.022 mM

raw_value_unit_evidence: Printed page 1834, Table VI, With CoA, CoA row: Km entry 2.2 on the 10^-5 M scale

row_label: With CoA / CoA


substrate_name: propanaldehyde

column_label: Table VI; subgroup With CoA; row Propionaldehyde; Km column on 10^-5 M scale; raw 610; normalized 6.10 mM

raw_value_unit_evidence: Printed page 1834, Table VI, With CoA, Propionaldehyde row: Km entry 610 on the 10^-5 M scale

row_label: With CoA / Propionaldehyde

substrate: propanaldehyde


organism: Blastobotrys adeninivorans

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

column_label: PubMed abstract for PMID 1975789 states that Km values were estimated to be 0.23 mM for NADPH.

raw_value_unit_evidence: Km = 0.23 mM for NADPH

row_label: NADPH

table_label: PubMed abstract prose

substrate: NADPH


column_label: PubMed abstract for PMID 1975789 states that Km values were estimated to be 0.77 mM for MgCl2.

raw_value_unit_evidence: Km = 0.77 mM for MgCl2


substrate_name: alpha-aminoadipate

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

column_label: PubMed abstract for PMID 1975789 states that Km values were estimated to be 0.78 mM for alpha-aminoadipate.

raw_value_unit_evidence: Km = 0.78 mM for alpha-aminoadipate

row_label: alpha-aminoadipate

substrate: alpha-aminoadipate


substrate_name: ATP

assay_conditions_summary: cofactor ATP

column_label: PubMed abstract for PMID 1975789 states that Km values were estimated to be 1.0 mM for ATP.

raw_value_unit_evidence: Km = 1.0 mM for ATP

row_label: ATP

substrate: ATP


enzyme_display_name: methylmalonate-semialdehyde dehydrogenase (CoA acylating)

organism: Bacillus subtilis

sequence_variant_note: Mutation signature C49A/C176A/C305A/C369A/C403A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


assay_conditions_summary: pH 8.2; 303.15 K; cofactor NAD+

enzyme: methylmalonate-semialdehyde dehydrogenase (CoA acylating)


smiles: O=CCC(=O)O


substrate_name: Coenzyme A

assay_conditions_summary: pH 8.2; 303.15 K; cofactor CoA

substrate: Coenzyme A


substrate_name: NAD+

substrate: NAD+


substrate_name: NAD (at pH 8.0)

assay_conditions_summary: pH 8; cofactor NAD+

column_label: Table 1, row NAD, column Km (uM).

raw_value_unit_evidence: Table 1 row NAD: Km 59.4 +/- 2.4 uM; assay condition pH 8.0.

row_label: NAD

table_label: Table 1: Kinetic Parameters of Human Lens ALDH1A1 Using Various Substrates

substrate: NAD (at pH 8.0)


substrate_name: (E)-4-hydroxynon-2-enal (at pH 8.0)

smiles: CCCCCC(C=CC=O)O

substrate: (E)-4-hydroxynon-2-enal (at pH 8.0)


substrate_name: acetaldehyde (at pH 8.0)

column_label: Table 1, row Acetaldehyde, column Km (uM).

raw_value_unit_evidence: Table 1 row Acetaldehyde: Km 238.2 +/- 12.9 uM; assay condition pH 8.0.

row_label: Acetaldehyde

substrate: acetaldehyde (at pH 8.0)


substrate_name: propanal (at pH 8.0)

assay_conditions_summary: pH 8

substrate: propanal (at pH 8.0)


substrate_name: trans-2-heptenal (at pH 8.0)

smiles: CCCCC=CC=O

column_label: Table 1, row trans-2-Heptenal, column Km (uM).

raw_value_unit_evidence: Table 1 row trans-2-Heptenal: Km 177.1 +/- 11.7 uM; assay condition pH 8.0.

substrate: trans-2-heptenal (at pH 8.0)


enzyme_display_name: Aspartate-semialdehyde dehydrogenase

substrate_name: L-aspartate 4-semialdehyde

assay_conditions_summary: pH 9

column_label: Official ScienceDirect PDF text, Table 2 row P. aeruginosa, ASA Km (mM) column gives 0.12.

raw_value_unit_evidence: Km raw_value=0.12 raw_unit=mM

row_label: P. aeruginosa

table_label: Table 2. Kinetic Parameters of Purified ASA Dehydrogenases

enzyme: Aspartate-semialdehyde dehydrogenase

substrate: L-aspartate 4-semialdehyde


substrate_name: NADP(+)

assay_conditions_summary: pH 9; cofactor NADP+

column_label: Official ScienceDirect PDF text, Table 2 row P. aeruginosa, NADP Km (mM) column gives 0.13.

raw_value_unit_evidence: Km raw_value=0.13 raw_unit=mM

substrate: NADP(+)


substrate_name: phosphate

column_label: Official ScienceDirect PDF text, Table 2 row P. aeruginosa, Phosphate Km (mM) column gives 1.5.

raw_value_unit_evidence: Km raw_value=1.5 raw_unit=mM

substrate: phosphate


organism: Nitrosomonas europaea

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADP+

column_label: Table 3 NAD+ row under variable NAD+ with saturating and fixed succinate semialdehyde reports 27 +/- 1 min^-1, 1.12 +/- 0.06 mM, and 4.0 x 10^2 M^-1 s^-1.

row_label: NAD+

table_label: Table 3: Kinetic parameters for GabD with different aldehydes


substrate_name: NADP+

column_label: Table 3 NADP+ row under variable NADP+ with saturating and fixed succinate semialdehyde reports 37 +/- 1 min^-1, 0.04 +/- 0.01 mM, and 1.5 x 10^4 M^-1 s^-1.

row_label: NADP+

substrate: NADP+


substrate_name: succinate semialdehyde

substrate: succinate semialdehyde


enzyme_display_name: Aldehyde dehydrogenase family 3 member B1

substrate_name: octanal

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

smiles: CCCCCCCC=O

assay_conditions_summary: pH 8.5; buffer B: 50 mM Tris-HCl pH 8; cofactor NAD+

column_label: Figure 3 kinetic-parameter prose / ALDH3B1-catalyzed oxidation of octanal: Km 25.0 uM; normalized Km 0.025 mM.

raw_value_unit_evidence: Figure 3 kinetic-parameter prose reports Vmax (pmol/min/ng protein) and Km (uM) for 3xFLAG-ALDH3B1-catalyzed oxidation: 9.7 and 45.6 for hexadecanal, 4.8 and 4.9 for trans-2-hexadecenal, and 5.0 and 25.0 for octanal. Matched row substrate: octanal; Km 25.0 uM.

row_label: 3xFLAG-ALDH3B1 oxidation of octanal

table_label: Figure 3 / ALDH3B1 exhibits activity toward C16 aldehydes

substrate: octanal


substrate_name: hexadecanal

smiles: CCCCCCCCCCCCCCCC=O

column_label: Figure 3 kinetic-parameter prose / ALDH3B1-catalyzed oxidation of hexadecanal: Km 45.6 uM; normalized Km 0.0456 mM.

raw_value_unit_evidence: Figure 3 kinetic-parameter prose reports Vmax (pmol/min/ng protein) and Km (uM) for 3xFLAG-ALDH3B1-catalyzed oxidation: 9.7 and 45.6 for hexadecanal, 4.8 and 4.9 for trans-2-hexadecenal, and 5.0 and 25.0 for octanal. Matched row substrate: hexadecanal; Km 45.6 uM.

row_label: 3xFLAG-ALDH3B1 oxidation of hexadecanal

enzyme: Aldehyde dehydrogenase family 3 member B1

substrate: hexadecanal


smiles: CCCCCCCCCCCCCC=CC=O

column_label: Figure 3 kinetic-parameter prose / ALDH3B1-catalyzed oxidation of trans-2-hexadecenal: Km 4.9 uM; normalized Km 0.0049 mM.

raw_value_unit_evidence: Figure 3 kinetic-parameter prose reports Vmax (pmol/min/ng protein) and Km (uM) for 3xFLAG-ALDH3B1-catalyzed oxidation: 9.7 and 45.6 for hexadecanal, 4.8 and 4.9 for trans-2-hexadecenal, and 5.0 and 25.0 for octanal. Matched row substrate: trans-2-hexadecenal; Km 4.9 uM.

row_label: 3xFLAG-ALDH3B1 oxidation of trans-2-hexadecenal


organism: Clostridium acetobutylicum


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


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

column_label: OUP full text Table 1 row L-ASA reports Km (mM)=0.955.

raw_value_unit_evidence: Table 1 row L-ASA reports Km raw_value=0.955 raw_unit=mM.

row_label: L-ASA

table_label: Table 1: Apparent kinetic parameters of purified recombinant ASD of Mycobacterium tuberculosis H37Rv


column_label: OUP full text Table 1 row NADP reports Km (mM)=0.065.

raw_value_unit_evidence: Table 1 row NADP reports Km raw_value=0.065 raw_unit=mM.

row_label: NADP


enzyme_display_name: Bifunctional aldehyde-alcohol dehydrogenase AdhE

organism: Escherichia coli (strain K12)

substrate_name: acetaldehyde (for acetaldehyde dehydrogenase activity)

assay_conditions_summary: pH 10; cofactor NADH

column_label: Table III reports AdhE row, Km acetaldehyde column = 5.4 mM.

raw_value_unit_evidence: Km raw_value=5.4 raw_unit=mM

row_label: AdhE row

table_label: Table III


substrate_name: ethanol (for ethanol dehydrogenase activity)

smiles: CCO

assay_conditions_summary: pH 10; cofactor CoA

column_label: Table III reports AdhE row, Km ethanol column = 240 mM.

raw_value_unit_evidence: Km raw_value=240 raw_unit=mM

enzyme: Bifunctional aldehyde-alcohol dehydrogenase AdhE


organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

column_label: Official ScienceDirect PDF text, Table 2 row Ha. influenzae, ASA Km (mM) column gives 0.24.

raw_value_unit_evidence: Km raw_value=0.24 raw_unit=mM

row_label: Ha. influenzae


column_label: Official ScienceDirect PDF text, Table 2 row Ha. influenzae, NADP Km (mM) column gives 0.15.

raw_value_unit_evidence: Km raw_value=0.15 raw_unit=mM


organism: Geobacillus stearothermophilus

substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


substrate_name: 3-phospho-D-glyceroyl phosphate

substrate: 3-phospho-D-glyceroyl phosphate


organism: Streptococcus mutans

substrate_name: D-Glyceraldehyde 3-phosphate

sequence_variant_note: Mutation signature R459I could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: Tyr-170->Phe has no major effect on kcat and Km for d-G3P

substrate: D-Glyceraldehyde 3-phosphate


organism: Sardina pilchardus

assay_conditions_summary: pH 8.5; 303.15 K; buffer 50 mM tricine-NaOH; cofactor NAD+

column_label: The abstract reports Michaelis constants for NAD+ and D-glyceraldehyde-3-phosphate of 92.0 microM and 73.4 microM, respectively.

raw_value_unit_evidence: Km raw_value=73.4 microM raw_unit=microM

row_label: Prose segment: D-glyceraldehyde-3-phosphate Km

table_label: PubMed PMID 18064387 abstract


substrate_name: NAD+

raw_value_unit_evidence: Km raw_value=92.0 microM raw_unit=microM

row_label: Prose segment: NAD+ Km


organism: Spinacia oleracea

assay_conditions_summary: cofactor NADP+


substrate_name: D-glyceraldehyde 3-phosphate

substrate: D-glyceraldehyde 3-phosphate


organism: Lactococcus lactis

assay_conditions_summary: pH 7.2; cofactor NAD+

substrate: NAD+


organism: Fasciola gigantica


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+


organism: Aspergillus nidulans


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+


organism: Pinus sylvestris

assay_conditions_summary: cofactor NAD+

column_label: Abstract reports apparent Km for NAD+ and glyceraldehyde-3-phosphate as 62 and 344 microM respectively.

raw_value_unit_evidence: Km raw_value=62 microM raw_unit=microM

row_label: Pinus sylvestris chloroplast GapCp / NAD+

table_label: PubMed XML abstract PMID 9583948


raw_value_unit_evidence: Km raw_value=344 microM raw_unit=microM

row_label: Pinus sylvestris chloroplast GapCp / glyceraldehyde-3-phosphate


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

substrate_name: glyceraldehyde-3-phosphate (at pH 8.0 and 40 degrees Celsius)


substrate_name: NAD(+) (at pH 8.0 and 40 degrees Celsius)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: NAD(+)

substrate: NAD(+)


organism: Streptomyces arenae

substrate_name: NAD (at pH 8 and 26 degrees Celsius)

column_label: Scanned page 934, Substrate kinetics paragraph: row/segment PL-insensitive form; substrate NAD+; metric apparent Km; raw value 120 uM; normalized value 0.12 mM.

raw_value_unit_evidence: The apparent Km for NAD+ was 120 uM for the PL-insensitive form.

row_label: PL-insensitive GAPDH isoenzyme; substrate NAD+

table_label: Prose/table-adjacent kinetic section on scanned page 934, after Tables 1-2

substrate: NAD (at pH 8 and 26 degrees Celsius)


column_label: Scanned page 934, Substrate kinetics paragraph: row/segment PL-sensitive form; substrate NAD+; metric apparent Km; raw value 110 uM; normalized value 0.11 mM.

raw_value_unit_evidence: The apparent Km for NAD+ was 110 uM for the PL-sensitive form.

row_label: PL-sensitive GAPDH isoenzyme; substrate NAD+


organism: Streptococcus pyogenes

assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+

column_label: Table 2. Steady-state kinetic parameters of SpSSADH; row Variable ligand NAD+; fixed substrate SSA (0.5 mM)

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

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


column_label: Table 2 columns Km, kcat, and kcat/Km for variable ligand NADP+ with fixed substrate SSA (0.5 mM).

normalized_value_unit_evidence: kcat/Km normalized_value=72.0 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=0.10 +/- 0.01 raw_unit=mM; kcat raw_value=7.20 +/- 0.12 raw_unit=s^-1; kcat/Km raw_value=7.2 +/- 0.3 x 10^4 raw_unit=M^-1 s^-1

row_label: Variable ligand NADP+; fixed substrate SSA (0.5 mM)

table_label: Table 2. Steady-state kinetic parameters of SpSSADH


organism: Saccharomyces cerevisiae

column_label: Sibling PMID 25092794 reports high specificity for succinate semi-aldehyde with Km = 15.48 +/- 0.14 microM.

raw_value_unit_evidence: Km raw_value=15.48 +/- 0.14 microM raw_unit=microM

row_label: Recombinant yeast SSADH / succinate semi-aldehyde

table_label: PubMed XML abstract PMID 25092794


organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 8; 333.15 K; cofactor NAD+


assay_conditions_summary: pH 8; 333.15 K; cofactor NADP+


organism: Saccharolobus solfataricus

substrate_name: DL-glyceraldehyde

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

assay_conditions_summary: pH 7.5; cofactor NADP+

column_label: Official JBC full-table HTML Table 1 reports DopDH substrate specificity, turnover number (s^-1): dl-glyceraldehyde (4.8).

raw_value_unit_evidence: kcat raw_value=4.8 raw_unit=s^-1

row_label: Substrate specificity, turnover number (s^-1) / dl-glyceraldehyde

table_label: Table 1 - Properties of the d-Ara degrading enzymes of S. solfataricus

substrate: DL-glyceraldehyde


column_label: Official JBC full-table HTML Table 1 reports DopDH substrate specificity, turnover number (s^-1): 2,5-Dioxopentanoate (8.6).

raw_value_unit_evidence: kcat raw_value=8.6 raw_unit=s^-1

row_label: Substrate specificity, turnover number (s^-1) / 2,5-Dioxopentanoate


enzyme_display_name: glyceraldehyde-3-phosphate dehydrogenase (NADP(+)) (phosphorylating)

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


substrate_name: NADPH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

enzyme: glyceraldehyde-3-phosphate dehydrogenase (NADP(+)) (phosphorylating)

substrate: NADPH


organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)

substrate_name: cinnamic acid

proof_lines:
cinnamic acid
NcCAR
kinetic parameters

substrate: cinnamic acid


substrate_name: piperonylic acid

proof_lines:
piperonylic acid
NcCAR
kinetic parameters

substrate: piperonylic acid


organism: Thermus thermophilus

substrate_name: Acetaldehyde

smiles: CC=O

column_label: Table 5 (asset `tables[4]`), row `TTHB247 | –`, acetaldehyde column block: Km,app (mM) = 5.5; kcat (s–1) = 7.4; kcat/Km,app(×102 M–1 s–1) = 13.5 (decoded: 13.5 x10^2 M^-1 s^-1 = 1.35 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 7.4 s–1 -> 7.4 s^(-1); the catalog holds 7.4 s^(-1); no unit conversion applied. Km,app: printed cell 5.5 mM -> 5.5 mM; the catalog holds 5.5 mM; no unit conversion applied. kcat/Km,app: The paper PRINTS this row's efficiency cell `13.5` in the `kcat/Km,app(×102 M–1 s–1)` column, i.e. 13.5 x10^2 M^-1 s^-1 = 1.35 s^-1 mM^-1. The catalog stores 1.3454545454545455 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km (7.4 / 5.5) rather than a transcription of the printed cell; the two differ. The nested oed source snapshot for this row already carries the printed value 1.35 s^(-1)*mM^(-1).

row_label: Table 5, decoded transcription, row `TTHB247 | -` (dehydrogenase TTHB247 with no aldolase partner), acetaldehyde column block

table_label: Table 5 'Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde' (asset `tables[4]`)

substrate: Acetaldehyde


enzyme_display_name: carboxylate reductase (NADP+)

organism: Neurospora crassa

substrate_name: ATP

assay_conditions_summary: cofactor ATP

enzyme: carboxylate reductase (NADP+)

substrate: ATP


substrate_name: salicylate

assay_conditions_summary: cofactor NADPH

normalized_value_unit_evidence: Km normalized_value=0.167 normalized_unit=mM from 1.67 x 10^-4 M.

raw_value_unit_evidence: Article prose reports K_M for salicylic acid = 1.67 x 10^-4 M, normalized to 0.167 mM. Raw value 1.67 x 10^-4 M.

row_label: Salicylic acid substrate

table_label: Article abstract/results prose

substrate: salicylate


enzyme_display_name: aspartate-semialdehyde dehydrogenase

substrate_name: NADP+

proof_lines:
aspartic-semialdehyde dehydrogenase
Saccharomyces cerevisiae

enzyme: aspartate-semialdehyde dehydrogenase

substrate: NADP+


organism: Homo sapiens

substrate_name: malonaldehyde (at pH 8.0 and 25 degrees Celsius)

smiles: C(C=O)C=O

assay_conditions_summary: pH 8


substrate_name: hexanal (at pH 8.0 and 25 degrees Celsius)

smiles: CCCCCC=O

assay_conditions_summary: pH 8; buffer pH 8; cofactor NAD+

column_label: PDF Table 4 row Hexanal has recombinant human ALDH1A1 Km=13.4 +/- 2.3 uM; 13.4 uM normalizes to 0.0134 mM.

raw_value_unit_evidence: Km raw_value=13.4 raw_unit=uM; SE=2.3 uM

row_label: Hexanal; recombinant human ALDH1A1

table_label: Table 4. Kinetic properties of recombinant human ALDH1A1


substrate_name: benzaldehyde (at pH 7.1 and 30 degrees Celsius)


substrate_name: 3-deoxyglucosone (at pH 7.1 and 30 degrees Celsius)

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


enzyme_display_name: Acetaldehyde dehydrogenase (acetylating) EutE

organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

substrate_name: acetyl-CoA

assay_conditions_summary: pH 8; buffer pH 8; cofactor CoA

column_label: PMC full text states that purified SeEutE had Km for acetyl-CoA of 23.4 +/- 6.8 uM, with Vmax 69.91 +/- 2.20 umol min^-1 mg^-1.

raw_value_unit_evidence: Km raw_value=23.4 +/- 6.8 uM raw_unit=uM

row_label: purified His6-SeEutE acetyl-CoA reductase reaction / acetyl-CoA

table_label: PMC3187147 Results prose: Cofactor preference and kinetic constants of His6-SeEutE

substrate: acetyl-CoA


substrate_name: phosphate

proof_lines: Semi-aldehyde aspartic dehydrogenase of Saccharomyces cerevisiae: properties and regulation

substrate: phosphate


organism: Geobacillus stearothermophilus

substrate_name: D-glyceraldehyde 3-phosphate


substrate_name: NADP(+)

column_label: Abstract reports the recombinant protein could use both NAD(+) and NADP(+) as co-factors, with Km values of 579.06+/-30.1 microM and 1.017+/-0.46 mM, respectively.

raw_value_unit_evidence: Km raw_value=1.017+/-0.46 mM raw_unit=mM

row_label: recombinant yeast succinic semi-aldehyde dehydrogenase / NADP(+)

substrate: NADP(+)


organism: Arabidopsis thaliana

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

proof_lines: specific activity 26 micromol NADPH oxidized min(-1) mg(-1)


organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40)

substrate_name: glyceraldehyde-3-phosphate (GAP)

column_label: Full text reports GpdA and GpdB Km values for GAP as 0.32 +/- 0.06 mM and 0.28 +/- 0.06 mM, respectively; the GpdB value matches the row.

raw_value_unit_evidence: Km raw_value=0.28 +/- 0.06 mM raw_unit=mM

row_label: GpdB for glyceraldehyde-3-phosphate (GAP)

table_label: Taylor full-text GpdA/GpdB properties prose; Figure 5

substrate: glyceraldehyde-3-phosphate (GAP)


substrate_name: NAD+

assay_conditions_summary: pH 8.5; 338.15 K; cofactor NAD+


enzyme_display_name: 2,5-dioxovalerate dehydrogenase

organism: Pseudomonas putida

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

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADP+

column_label: Results prose: P. putida alpha-KGSA dehydrogenase kinetic parameters; row P. putida alpha-KGSA dehydrogenase with alpha-KGSA / 2,5-dioxopentanoate substrate; metric columns Km, kcat, and/or kcat/Km; Prose reports P. putida alpha-KGSA dehydrogenase with alpha-KGSA substrate: Km = 14.0 +/- 1.5 uM and kcat = 197 +/- 5 s^-1.

normalized_value_unit_evidence: 14.0 uM = 0.014 mM; kcat/Km normalized from components = 14071.42857142857 s^-1 mM^-1.

enzyme: 2,5-dioxovalerate dehydrogenase


substrate_name: NADP(+) (at pH 8.5 and at 30 degrees Celsius)

assay_conditions_summary: pH 8.5; cofactor NADP+


assay_conditions_summary: pH 8; cofactor NAD+

column_label: PMC full-text paragraph P24 states a Km of 119.5 +/- 16.8 uM was determined for 4HNE; method paragraph P16 gives the assay conditions.

raw_value_unit_evidence: Km raw_value=119.5 raw_unit=uM uncertainty=+/-16.8 uM

row_label: Paragraph P24 4HNE metric sentence

table_label: PMC full-text prose section 3.5


substrate_name: salicylic acid

column_label: Article prose reports K_M for salicylic acid = 1.67 x 10^-4 M, normalized to 0.167 mM.

row_label: Salicylic acid / salicylate substrate

substrate: salicylic acid


substrate_name: benzoate

substrate: benzoate


organism: Ctenopharyngodon idella

substrate_name: acetaldehyde

sequence: SALAINQPNYSVLKELGLNED

wild_type_sequence: SALAINQPNYSVLKELGLNED

column_label: Abstract reports at pH 9.5 the Vmax and Km values for acetaldehyde were 1.95 U/mg and 2.00 mM, respectively.

raw_value_unit_evidence: Km raw_value=2.00 mM raw_unit=mM

row_label: Grass carp antiquitin / acetaldehyde

table_label: PubMed XML abstract PMID 14602152

substrate: acetaldehyde