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


enzyme_display_name: 2,5-dioxovalerate dehydrogenase

organism: Azospirillum brasilense

source_db: oed

verification_status: verified

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_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

data_origin: experimental

enzyme: 2,5-dioxovalerate dehydrogenase

status: verified

source: oed


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


mutation_signature: Unknown

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

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


substrate_name: NAD+

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

substrate: NAD+


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


substrate_name: NADP+

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

substrate: NADP+


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


verification_status: corrected

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.

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

status: corrected


organism: Pseudomonas putida

source_db: brenda

verification_status: unverified

kcat_display: Not reported

kcat_over_km_display: Not reported

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

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

proof_lines: oxidized 2-hydroxymuconate semialdehyde more efficiently

status: unverified

source: brenda


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

kcat_over_km_origin: calculated

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

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


substrate_name: propanal

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

substrate: propanal


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

organism: Rattus norvegicus

source_db: uniprot

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

source: uniprot


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


organism: Saccharolobus solfataricus

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+


enzyme_display_name: Aldehyde dehydrogenase 1A1

organism: Homo sapiens

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

enzyme: Aldehyde dehydrogenase 1A1

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

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).

mutation_type: substitution

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

source_databases_merged: brenda uniprot


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


enzyme_display_name: Carboxylic acid reductase

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

enzyme: Carboxylic acid reductase

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

sequence_source: multiple

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

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

source_databases_merged: brenda skid


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+


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.


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


organism: Paraburkholderia xenovorans

substrate_name: pentaldehyde

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

assay_conditions_summary: pH 8; 298.15 K; buffer 100 mM HEPES

proof_lines: wild type enzyme, at 25°C in 100 mM HEPES buffer (pH 8.0)

substrate: pentaldehyde


substrate_name: benzaldehyde

assay_conditions_summary: cofactor NAD+

column_label: Abstract reports the apparent K(m) value of benzaldehyde dehydrogenase for benzaldehyde was 460 microM.

raw_value_unit_evidence: Km raw_value=460 microM raw_unit=microM

row_label: Pseudomonas putida TOL plasmid benzaldehyde dehydrogenase / benzaldehyde

table_label: PubMed XML abstract PMID 2202600

substrate: benzaldehyde


substrate_name: picolinaldehyde

substrate: picolinaldehyde


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

proof_lines: mutant enzyme I195A, at 25°C in 100 mM HEPES buffer (pH 8.0)


substrate_name: propionaldehyde

smiles: CCC=O

proof_lines: mutant enzyme I195W, at 25°C in 100 mM HEPES buffer (pH 8.0)

substrate: propionaldehyde


proof_lines: mutant enzyme D208A, at 25°C in 100 mM HEPES buffer (pH 8.0)


proof_lines: mutant enzyme I195F, at 25°C in 100 mM HEPES buffer (pH 8.0)


substrate_name: Butyraldehyde

smiles: CCCC=O

substrate: Butyraldehyde


organism: Oryza sativa

substrate_name: 3-phospho-D-glyceroyl phosphate

proof_lines: mutant enzyme F37L, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C

substrate: 3-phospho-D-glyceroyl phosphate


proof_lines: mutant enzyme F37T, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C


proof_lines: mutant enzyme F37L, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C

substrate: D-glyceraldehyde 3-phosphate


proof_lines: mutant enzyme F37T, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C


proof_lines: mutant enzyme F37G, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C


proof_lines: mutant enzyme F37G, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C


proof_lines: wild type enzyme, in 80 mM triethanolamine, 3.3 mM L-cysteine HCl, 1.7 mM MgSO4, 0.5 mM EDTA, pH 7.6, at 25°C


proof_lines: wild type enzyme, in 50 mM triethanolamine, 50 mM Na2HPO4, 0.2 mM EDTA, at pH 8.8 and 25°C


assay_conditions_summary: pH 8.8; 298.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NADH

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NADH

substrate: NADH


organism: Haemophilus influenzae

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


proof_lines: recombinant mutant R103K and mutant K246L


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


substrate_name: phosphate


organism: Oryza sativa Japonica Group

assay_conditions_summary: pH 8.8; 298.15 K; cofactor NADH


substrate_name: D-glyceraldehyde 3-phosphate


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: succinate semialdehyde

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

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

proof_lines: mutant enzyme D426A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C

substrate: succinate semialdehyde


proof_lines: mutant enzyme R428A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C


assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+

proof_lines: mutant enzyme K160E, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: mutant enzyme K160A, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: mutant enzyme N193A, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: wild type enzyme, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: mutant enzyme R145A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: wild type enzyme, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C

proof_lines: wild type enzyme, with NADP+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: mutant enzyme W141A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: mutant enzyme S425A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: mutant enzyme K92A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C


proof_lines: mutant enzyme E442A, with NAD+ as cosubstrate, in 50 mM HEPES (pH 8.0), at 37°C


organism: Bacillus subtilis

assay_conditions_summary: pH 8.2; 303.15 K; cofactor NAD+

proof_lines: V229G/H226P/G225 insertion, pH 8.2 and 30°C


proof_lines: V229G/Y252L/V253I/G225 insertion, pH 8.2 and 30°C


proof_lines:
V229G/G225 insertion, pH 8.2 and 30°C
V229G, pH 8.2 and 30°C


mutation_signature: G225 insertion

mutation_type: insertion


proof_lines: wild type MSDH, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C

proof_lines: wild type MSDH, steady-state conditions with propionaldehyde, pH 8.2 and 30°C


substrate_name: methylmalonate semialdehyde

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

substrate: methylmalonate semialdehyde


proof_lines: wild type MSDH, steady-state conditions, pH 8.2 and 30°C


substrate_name: CoA

assay_conditions_summary: pH 8.2; 303.15 K; cofactor CoA

substrate: CoA


organism: Triticum aestivum

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


substrate_name: NAD+

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NAD+


proof_lines: R124L mutant enzyme, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C

proof_lines: R124L mutant enzyme, steady-state conditions with propionaldehyde, pH 8.2 and 30°C


proof_lines: R301L mutant enzyme, steady-state conditions with methylmalonate semialdehyde, pH 8.2 and 30°C


proof_lines: R124L mutant enzyme, steady-state conditions, pH 8.2 and 30°C


proof_lines: R301L mutant enzyme, steady-state conditions, pH 8.2 and 30°C


proof_lines: R301L mutant enzyme, steady-state conditions with propionaldehyde, pH 8.2 and 30°C


substrate: phosphate


assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+


proof_lines: recombinant wild-type enzyme, pH 9.0, 30°C

proof_lines: recombinant wild-type enzyme and mutant E243D


substrate_name: cacodylate

substrate: cacodylate


enzyme_display_name: UniProt P00352

substrate_name: decanal

source_db: skid

source_license: CC BY-NC-ND 4.0

smiles: CCCCCCCCCC=O

enzyme: UniProt P00352

substrate: decanal

source: skid


substrate_name: all-trans-retinal

substrate: all-trans-retinal


enzyme_display_name: UniProt P47895

substrate_name: hexanal

enzyme: UniProt P47895

substrate: hexanal


proof_lines: glyceraldehyde-3-phosphate dehydrogenase, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25°C

proof_lines: pH 7.3, enzyme isolated of sarcoma tissue


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NAD+


mutation_signature: highly soluble form of sperm-specific glyceraldehyde-3-phosphate dehydrogenase truncated at the N-terminus / highly soluble form of sperm-specific glyceraldehyd

mutation_type: truncation

proof_lines: recombinant, highly soluble form of sperm-specific glyceraldehyde-3-phosphate dehydrogenase truncated at the N-terminus, in 10 mM sodium diphosphate, 20 mM sodium phosphate (pH 8.5), 0.003 mM dithiothreitol and 10 mM sodium arsenate, at 25?


mutation_signature: N-terminally truncated mutant

proof_lines: N-terminally truncated mutant, pH 8.5, 25°C


proof_lines: recombinant wild-type enzyme, pH 8.9, 20°C


organism: Escherichia coli

assay_conditions_summary: pH 9; 303.15 K; cofactor NAD+


proof_lines: recombinant mutant Q350N/H171A, pH 9.0, 30°C


proof_lines:
mutant N313T/Y317G
mutant N313T and Y317G


enzyme_display_name: retinal dehydrogenase

enzyme: retinal dehydrogenase


assay_conditions_summary: pH 8.5; 303.15 K; buffer TAPS; cofactor NADP+

proof_lines: native wild type enzyme, in TAPS buffer, at pH 8.5, at 30°C

proof_lines: recombinant wild type enzyme, in TAPS buffer, at pH 8.5, at 30°C


proof_lines: His-tagged BADH, cosubstrate benzaldehyde


assay_conditions_summary: pH 8.5; 303.15 K; buffer TAPS; cofactor NAD+


assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+


substrate_name: benzaldehyde

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADP+

proof_lines: recombinant wild type enzyme, in the presence of NADP+, TAPS buffer, at pH 8.5, at 30°C

proof_lines: native wild type enzyme, in the presence of NADP+, TAPS buffer, at pH 8.5, at 30°C

substrate: benzaldehyde


proof_lines:
His-tagged BADH, cosubstrate NADP+
His-tagged BADH, cosubstrate NAD+


enzyme_display_name: (R)-dehydropantoate dehydrogenase

organism: Pseudomonas sp.

assay_conditions_summary: cofactor NAD+

enzyme: (R)-dehydropantoate dehydrogenase


enzyme_display_name: phenylacetaldehyde dehydrogenase

organism: Rhodococcus opacus

substrate_name: phenylacetaldehyde

assay_conditions_summary: pH 7.7; cofactor NAD+

proof_lines: with NAD+ as cosubstrate, at pH 7.7, temperature not specified in the publication

enzyme: phenylacetaldehyde dehydrogenase

substrate: phenylacetaldehyde


proof_lines: with phenylacetaldehyde as cosubstrate, at pH 7.7, temperature not specified in the publication


organism: Mus musculus

assay_conditions_summary: pH 9; 298.15 K; buffer 100 mM HEPES

proof_lines: recombinant isozyme type-2, pH 9.0, 25°C

proof_lines: isoform RALDH4, in 100 mM HEPES buffer, pH 8.5, at 37°C

proof_lines: recombinant isozyme type-1, pH 7.5, 25°C


organism: Gordonia rubripertincta


organism: Achromobacter eurydice


substrate_name: Unknown

ki_unit: mM

assay_conditions_summary: pH 8.5; 310.15 K; buffer 100 mM HEPES

proof_lines: isoform RALDH4, using 13-cis retinal as substrate, in 100 mM HEPES buffer, pH 8.5, at 37°C

proof_lines: isoform RALDH4, using 9-cis retinal as substrate, in 100 mM HEPES buffer, pH 8.5, at 37°C

proof_lines: recombinant isozyme type-1, pH 7.5, 25°C, with substrate all-trans-retinal

substrate: Unknown


organism: Aromatoleum aromaticum

sequence_source: UniProt:Q5P171 (ebA4954)

assay_conditions_summary: pH 8.5; cofactor NAD+

column_label: PMC3911259 Table 4 columns K0.5 (uM), kcat (s^-1), and kcat/K0.5 (uM^-1 s^-1): NAD Michaelis-Menten row reports 18, 53, and 3.0.

row_label: NAD (1 mM), Michaelis-Menten

table_label: PMC3911259 Table 4


assay_conditions_summary: pH 8.5; cofactor NADP+

column_label: PMC3911259 Table 4 columns K0.5 (uM), kcat (s^-1), and kcat/K0.5 (uM^-1 s^-1): NADP Michaelis-Menten row reports 25, 63, and 2.5.

row_label: NADP (1 mM), Michaelis-Menten


substrate_name: acetaldehyde

substrate: acetaldehyde


organism: Oryctolagus cuniculus

smiles: CCCCCC(C=CC=O)O


substrate_name: malonaldehyde

substrate: malonaldehyde


substrate_name: propanal

substrate: propanal


organism: Homo sapiens

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


proof_lines: pH 8.5, 25°C, recombinant wild-type ALDH1A1 enzyme


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.


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: octanal

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L459F/N460G with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.

smiles: CCCCCCCC=O

proof_lines: recombinant mutant L459F/N460G, pH 8.5, 25°C

substrate: octanal


substrate: NAD+


organism: Antirrhinum majus

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).


organism: Bos taurus

substrate_name: all-trans retinal

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

substrate: all-trans retinal


enzyme_display_name: Retinaldehyde dehydrogenase 3

column_label: PMC5069622 biochemical characterization prose reports all-trans retinal (KM = 9.3 x 10^-6 M); this normalizes to 0.0093 mM.

raw_value_unit_evidence: Km raw_value=9.3 x 10^-6 M raw_unit=M

row_label: Prose segment: all-trans retinal

table_label: PMC5069622 Results and Discussion, Biochemical characterization prose

enzyme: Retinaldehyde dehydrogenase 3


substrate_name: NAD

column_label: Supplementary Table S1 row Variable substrate NAD+ / Fixed substrate All-trans Retinal, KM column: 4.8x10-6 M, normalized to 0.0048 mM, matching CatLog NAD Km.

normalized_value_unit_evidence: Km normalized_value=0.0048 normalized_unit=mM after M-to-mM conversion; CatLog value=0.0048 mM.

raw_value_unit_evidence: Supplementary Table S1 row Variable substrate NAD+ / Fixed substrate All-trans Retinal reports KM raw_value=4.8x10-6 raw_unit=M.

row_label: Variable substrate NAD+ / fixed substrate All-trans Retinal

table_label: Supplementary Table S1. Steady-state kinetic parameters of hALDH1A3

substrate: NAD


column_label: PMC5069622 biochemical characterization prose reports acetaldehyde (KM = 2.4 x 10^-3 M); this normalizes to 2.4 mM.

raw_value_unit_evidence: Km raw_value=2.4 x 10^-3 M raw_unit=M

row_label: Prose segment: acetaldehyde


organism: Sphingopyxis fribergensis


organism: Pseudomonas putida

substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


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

assay_conditions_summary: pH 8


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

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


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


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


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


enzyme_display_name: Retinal dehydrogenase 2

substrate_name: all-trans-retinal

column_label: Table II row All-trans-retinal column Km reports 0.4 +/- 0.1 uM.

raw_value_unit_evidence: Km raw_value=0.4 +/- 0.1 raw_unit=uM

row_label: All-trans-retinal

table_label: Table II. Relative efficiencies of RalDH(II)/rL for aldehyde substrates

enzyme: Retinal dehydrogenase 2


column_label: The RalDH(II)/rL and Retinal paragraph reports NAD Km 70 +/- 0.6 uM.

raw_value_unit_evidence: Km raw_value=70 +/- 0.6 raw_unit=uM

row_label: RalDH(II)/rL

table_label: Main text section RalDH(II)/rL and Retinal


substrate_name: NADP

column_label: The RalDH(II)/rL and Retinal paragraph reports NADP Km 400 +/- 7 uM.

raw_value_unit_evidence: Km raw_value=400 +/- 7 raw_unit=uM

substrate: NADP


organism: Brevibacterium sp.

substrate_name: phenylacetaldehyde

assay_conditions_summary: pH 9; buffer glycine-NaOH; cofactor NAD+

column_label: Table 3 reports Phenylacetaldehyde Km (uM) = 1.24 and Vmax = 4.63 umol min^-1 mg^-1.

raw_value_unit_evidence: Km raw_value=1.24 raw_unit=uM

row_label: Phenylacetaldehyde

table_label: Table 3 - Kinetic parameters for PADH


substrate_name: NAD+

column_label: Table 3 reports NAD+ Km (uM) = 116 and Vmax = 4.40 umol min^-1 mg^-1.

raw_value_unit_evidence: Km raw_value=116 raw_unit=uM

row_label: NAD+


organism: Taeniopygia guttata

substrate_name: retinal

substrate: retinal


substrate_name: NAD (at pH 8.0)

assay_conditions_summary: pH 7.1; 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)

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


substrate_name: acetaldehyde (at pH 8.0)

assay_conditions_summary: pH 8; cofactor NAD+

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)

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: hexadecanal dehydrogenase (acylating)

organism: Porphyromonas gingivalis

substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.15; 303.15 K; cofactor CoA

enzyme: hexadecanal dehydrogenase (acylating)

substrate: acetyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


organism: Pseudomonas sp.

smiles: C[N+](C)(C)CCCC=O


assay_conditions_summary: pH 9.5; 303.15 K; cofactor NAD+


assay_conditions_summary: pH 8.5; 301.15 K; cofactor NAD+


substrate_name: NADP+

assay_conditions_summary: pH 8.5; 301.15 K; cofactor NADP+

substrate: NADP+


enzyme_display_name: cinnamoyl-CoA reductase

organism: Petunia x hybrida

assay_conditions_summary: pH 6; cofactor NADPH

column_label: Table 1, column p-Coumaroyl-CoA, metric rows Km (uM), kcat (s^-1), and kcat/Km (mM^-1 s^-1)

row_label: p-Coumaroyl-CoA

table_label: Table 1. Kinetic Constants of Ph-CCR1 with Various Hydroxycinnamoyl-CoA Esters.

enzyme: cinnamoyl-CoA reductase


substrate_name: sinapoyl-CoA

column_label: Table 1, column Sinapoyl-CoA, metric rows Km (uM), kcat (s^-1), and kcat/Km (mM^-1 s^-1)

row_label: Sinapoyl-CoA

substrate: sinapoyl-CoA


substrate_name: feruloyl-CoA

column_label: Table 1, column Feruloyl-CoA, metric rows Km (uM), kcat (s^-1), and kcat/Km (mM^-1 s^-1)

row_label: Feruloyl-CoA

substrate: feruloyl-CoA


organism: Lathyrus oleraceus

substrate_name: NADH

assay_conditions_summary: cofactor NADH

proof_lines:
aldehyde generation
alcohol generation

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


organism: Marinobacter nauticus

substrate_name: hexadecanoyl-CoA

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

substrate: hexadecanoyl-CoA


smiles: CCCCC=CCCCCCCCCCC=O


organism: Populus tomentosa

assay_conditions_summary: pH 6; 313.15 K; buffer NADPH in 100 mM phosphate; cofactor CoA

column_label: Table 2; PtoCCR7 row; p-Coumaroyl-CoA; Km, kcat, and kcat/Km columns.

raw_value_unit_evidence: Table 2 PtoCCR7 row, p-Coumaroyl-CoA columns: Km 15.95 uM; kcat 1.10 min^-1; kcat/Km 0.07 uM^-1 min^-1.

row_label: PtoCCR7 / p-Coumaroyl-CoA

table_label: Table 2. Kinetic parameters of PtoCCR7


substrate_name: caffeoyl-CoA

column_label: Table 2; PtoCCR7 row; Caffeoyl-CoA; Km, kcat, and kcat/Km columns.

raw_value_unit_evidence: Table 2 PtoCCR7 row, Caffeoyl-CoA columns: Km 23.76 uM; kcat 2.17 min^-1; kcat/Km 0.09 uM^-1 min^-1.

row_label: PtoCCR7 / Caffeoyl-CoA

substrate: caffeoyl-CoA


column_label: Table 2; PtoCCR7 row; Feruloyl-CoA; Km, kcat, and kcat/Km columns.

raw_value_unit_evidence: Table 2 PtoCCR7 row, Feruloyl-CoA columns: Km 14.31 uM; kcat 61.95 min^-1; kcat/Km 4.33 uM^-1 min^-1.

row_label: PtoCCR7 / Feruloyl-CoA


column_label: Table 2; PtoCCR7 row; Sinapoyl-CoA; Km, kcat, and kcat/Km columns.

raw_value_unit_evidence: Table 2 PtoCCR7 row, Sinapoyl-CoA columns: Km 41.02 uM; kcat 3.84 min^-1; kcat/Km 0.09 uM^-1 min^-1.

row_label: PtoCCR7 / Sinapoyl-CoA


organism: Arabidopsis thaliana

substrate_name: [hexadecanoyl]-acyl carrier protein

assay_conditions_summary: pH 7; 303.15 K; buffer 100 mM phosphate

proof_lines: in 100 mM phosphate buffer, pH 7.0, at 30°C

substrate: [hexadecanoyl]-acyl carrier protein


assay_conditions_summary: pH 7; 303.15 K; buffer 100 mM phosphate; cofactor CoA


organism: Fragaria x ananassa

assay_conditions_summary: pH 6; cofactor CoA

proof_lines: pH 6.0, 25°C, recombinant GST-tagged enzyme


organism: Anas platyrhynchos


enzyme_display_name: long-chain-aldehyde dehydrogenase

organism: Simmondsia chinensis

substrate_name: decyl aldehyde

enzyme: long-chain-aldehyde dehydrogenase

substrate: decyl aldehyde


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


enzyme_display_name: formaldehyde dehydrogenase

organism: Ogataea angusta

substrate_name: formaldehyde

proof_lines: KM value of the used FdDH in solution from the wild strains

enzyme: formaldehyde dehydrogenase

substrate: formaldehyde


proof_lines: immobilized enzyme in a bioactive layer on the transducer surface, apparent Michaelis-Menten constant derived from the formaldehyde calibration curves is 120 mM with a linear detection range for formaldehyde up to 20 mM


organism: Forsythia suspensa

assay_conditions_summary: cofactor CoA


enzyme_display_name: Cinnamoyl-CoA reductase 1

organism: Medicago truncatula

substrate_name: feruloyl-CoA (at pH 6.25 and 30 degrees Celsius)

assay_conditions_summary: pH 6.25; cofactor CoA

proof_lines: kcat is 60.1 min(-1) with feruloyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 5.5 min(-1) with sinapoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 3.1 min(-1) with ca

enzyme: Cinnamoyl-CoA reductase 1


substrate_name: sinapoyl-CoA (at pH 6.25 and 30 degrees Celsius)


substrate_name: caffeoyl-CoA (at pH 6.25 and 30 degrees Celsius)


substrate_name: coumaroyl-CoA (at pH 6.25 and 30 degrees Celsius)


enzyme_display_name: Cinnamoyl-CoA reductase 2

proof_lines: kcat is 18.1 min(-1) with feruloyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 12.0 min(-1) with sinapoyl-CoA as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:20876124). kcat is 9.0 min(-1) with c

enzyme: Cinnamoyl-CoA reductase 2

substrate: feruloyl-CoA (at pH 6.25 and 30 degrees Celsius)


substrate: sinapoyl-CoA (at pH 6.25 and 30 degrees Celsius)


substrate: caffeoyl-CoA (at pH 6.25 and 30 degrees Celsius)


substrate: coumaroyl-CoA (at pH 6.25 and 30 degrees Celsius)


organism: Solanum lycopersicum


substrate_name: coumaroyl-CoA

substrate: coumaroyl-CoA


organism: Leucaena leucocephala

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S212G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S212G, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R51G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R51G, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D77G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D77G, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V200E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V200E, pH and temperature not specified in the publication


organism: Populus tremuloides

column_label: Table 1 row Caffeoyl-CoA has Km, Vmax, and Kcat columns only; no kcat/Km column.

normalized_value_unit_evidence: Km 0.0763 mM; kcat 0.0116667 s^-1; no explicit kcat/Km column; exported kcat and kcat_over_km are not supported in s^-1 units.

row_label: Caffeoyl-CoA

table_label: Table 1 Kinetic properties of CCR catalysis with various cinnamoyl-CoA esters


column_label: Table 1 row 5-Hydroxyferuloyl-CoA has Km, Vmax, and Kcat columns only; no kcat/Km column.

normalized_value_unit_evidence: Km 0.099 mM; kcat 0.0816667 s^-1; no explicit kcat/Km column; exported kcat and kcat_over_km are not supported in s^-1 units.

raw_value_unit_evidence: Table 1 row 5-Hydroxyferuloyl-CoA: Km 99.0 +/- 1.0 uM; Vmax 97.0 +/- 3.0 uM min^-1; Kcat 4.9 +/- 0.2 min^-1.


column_label: Table 1 row Sinapoyl-CoA has Km, Vmax, and Kcat columns only; no kcat/Km column.

normalized_value_unit_evidence: Km 0.1045 mM; kcat 0.0883333 s^-1; no explicit kcat/Km column; exported kcat and kcat_over_km are not supported in s^-1 units.


column_label: Table 1 row feruloyl-CoA has Km, Vmax, and Kcat columns only; no kcat/Km column.

normalized_value_unit_evidence: Km 0.0137 mM; kcat 0.13 s^-1; no explicit kcat/Km column; exported kcat_over_km is not supported as s^-1 mM^-1.

row_label: feruloyl-CoA


organism: Pinus massoniana

proof_lines: at pH 6.0, temperature not specified in the publication


organism: Pinus koraiensis


enzyme_display_name: Cinnamoyl-CoA reductase CAD2

substrate_name: coumaraldehyde (at pH 6.25 and 30 degrees Celsius)

proof_lines: kcat is 0.46 sec(-1) with coumaraldehyde as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:25217505). kcat is 0.10 sec(-1) with coniferaldehyde as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:25217505). kcat is 0.24 sec(-1)

enzyme: Cinnamoyl-CoA reductase CAD2


substrate_name: coniferaldehyde (at pH 6.25 and 30 degrees Celsius)


substrate_name: sinapaldehyde (at pH 6.25 and 30 degrees Celsius)


organism: Bacillus subtilis (strain 168)


substrate_name: hexadecanal

smiles: CCCCCCCCCCCCCCCC=O

assay_conditions_summary: pH 7; cofactor CoA

substrate: hexadecanal


substrate_name: feruloyl-CoA


substrate_name: sinapoyl-CoA


enzyme_display_name: UniProt A0A059TC02

organism: Petunia x hybrida

assay_conditions_summary: pH 6; 298.15 K; cofactor CoA

proof_lines: kcat is 1.2 sec(-1) with p-coumaroyl-CoA as substrate (PubMed:25217505). kcat is 5.8 sec(-1) with feruloyl-CoA as substrate (PubMed:25217505). kcat is 3.4 sec(-1) with sinapoyl-CoA as substrate (PubMed:25217505).

source_databases_merged: skid uniprot

enzyme: UniProt A0A059TC02


enzyme_display_name: Aminoaldehyde dehydrogenase 1

smiles: C(CC=O)CN

assay_conditions_summary: pH 9; cofactor NAD+

column_label: Table 3; row ABAL; SlAMADH1 Km column

normalized_value_unit_evidence: Km=0.278 mM converted from 278 uM

raw_value_unit_evidence: Table 3 SlAMADH1 / ABAL Km 278 +/- 19 uM

row_label: SlAMADH1 / ABAL

table_label: Table 3

enzyme: Aminoaldehyde dehydrogenase 1


smiles: C(CN)C=O

column_label: Table 3; row APAL; SlAMADH1 Km column

normalized_value_unit_evidence: Km=0.041 mM converted from 41 uM

raw_value_unit_evidence: Table 3 SlAMADH1 / APAL Km 41 +/- 5 uM

row_label: SlAMADH1 / APAL


column_label: Table 3; row TMABAL; SlAMADH1 Km column

normalized_value_unit_evidence: Km=0.017 mM converted from 17 uM

raw_value_unit_evidence: Table 3 SlAMADH1 / TMABAL Km 17 +/- 1.4 uM

row_label: SlAMADH1 / TMABAL


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

column_label: Table 3; row GBAL; SlAMADH1 Km column

normalized_value_unit_evidence: Km=0.085 mM converted from 85 uM

raw_value_unit_evidence: Table 3 SlAMADH1 / GBAL Km 85 +/- 13 uM

row_label: SlAMADH1 / GBAL


substrate_name: betaine aldehyde

assay_conditions_summary: pH 9; buffer 0.15 M Tris-HCl; cofactor NAD+

column_label: TABLE 3; row BAL; enzyme column group SlAMADH1; metric column Km; raw cell 2051 +/- 83 uM; SlAMADH2 BAL cells are not determined.

normalized_value_unit_evidence: 2051 uM = 2.051 mM; reported uncertainty 83 uM = 0.083 mM; exported row value is 2.1 mM from source rounding.

raw_value_unit_evidence: Table 3 BAL row under SlAMADH1 reports Km 2051 +/- 83 uM.

row_label: Ligand BAL (betaine aldehyde); enzyme SlAMADH1 / Aminoaldehyde dehydrogenase 1

table_label: PMCID PMC3611018 TABLE 3. Kinetic parameters of ALDH10 family from tomato for selected substrates and the coenzyme NAD+

substrate: betaine aldehyde


substrate_name: NAD(+) with 3-aminopropanal as substrate

column_label: Table 3; row NAD +; SlAMADH1 Km column

normalized_value_unit_evidence: Km=0.072 mM converted from 72 uM

raw_value_unit_evidence: Table 3 SlAMADH1 / NAD + Km 72 +/- 7 uM

row_label: SlAMADH1 / NAD +


enzyme_display_name: Aminoaldehyde dehydrogenase 2

column_label: Table 3; row ABAL; SlAMADH2 Km column

normalized_value_unit_evidence: Km=0.054 mM converted from 54 uM

raw_value_unit_evidence: Table 3 SlAMADH2 / ABAL Km 54 +/- 5 uM

row_label: SlAMADH2 / ABAL

enzyme: Aminoaldehyde dehydrogenase 2


column_label: Table 3; row APAL; SlAMADH2 Km column

normalized_value_unit_evidence: Km=0.009 mM converted from 9 uM

raw_value_unit_evidence: Table 3 SlAMADH2 / APAL Km 9 +/- 1.4 uM

row_label: SlAMADH2 / APAL


column_label: Table 3; row TMABAL; SlAMADH2 Km column

normalized_value_unit_evidence: Km=0.141 mM converted from 141 uM

raw_value_unit_evidence: Table 3 SlAMADH2 / TMABAL Km 141 +/- 17 uM

row_label: SlAMADH2 / TMABAL


column_label: Table 3; row GBAL; SlAMADH2 Km column

normalized_value_unit_evidence: Km=0.022 mM converted from 22 uM

raw_value_unit_evidence: Table 3 SlAMADH2 / GBAL Km 22 +/- 3 uM

row_label: SlAMADH2 / GBAL


enzyme_display_name: Aminoaldehyde dehydrogenase 1a

organism: Zea mays

column_label: Table 4; row NAD +; ZmAMADH1a Km column

normalized_value_unit_evidence: Km=0.091 mM converted from 91 uM

raw_value_unit_evidence: Table 4 ZmAMADH1a / NAD + Km 91 +/- 4 uM

row_label: ZmAMADH1a / NAD +

table_label: Table 4

enzyme: Aminoaldehyde dehydrogenase 1a

substrate: NAD(+) with 3-aminopropanal as substrate


column_label: Table 4; row ABAL; ZmAMADH2 Km column

normalized_value_unit_evidence: Km=0.059 mM converted from 59 uM

raw_value_unit_evidence: Table 4 ZmAMADH2 / ABAL Km 59 +/- 2 uM

row_label: ZmAMADH2 / ABAL


column_label: Table 4; row APAL; ZmAMADH2 Km column

normalized_value_unit_evidence: Km=0.098 mM converted from 98 uM

raw_value_unit_evidence: Table 4 ZmAMADH2 / APAL Km 98 +/- 8 uM

row_label: ZmAMADH2 / APAL


column_label: Table 4; row TMABAL; ZmAMADH2 Km column

normalized_value_unit_evidence: Km=0.016 mM converted from 16 uM

raw_value_unit_evidence: Table 4 ZmAMADH2 / TMABAL Km 16 +/- 1.1 uM

row_label: ZmAMADH2 / TMABAL


column_label: Table 4; row GBAL; ZmAMADH2 Km column

normalized_value_unit_evidence: Km=0.011 mM converted from 11 uM

raw_value_unit_evidence: Table 4 ZmAMADH2 / GBAL Km 11 +/- 1.2 uM

row_label: ZmAMADH2 / GBAL


column_label: Table 4; row NAD +; ZmAMADH2 Km column

normalized_value_unit_evidence: Km=0.086 mM converted from 86 uM

raw_value_unit_evidence: Table 4 ZmAMADH2 / NAD + Km 86 +/- 3 uM

row_label: ZmAMADH2 / NAD +


enzyme_display_name: Aminoaldehyde dehydrogenase 1b

column_label: Table 4; row ABAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.026 mM converted from 26 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / ABAL Km 26 +/- 4 uM

row_label: ZmAMADH1b / ABAL

enzyme: Aminoaldehyde dehydrogenase 1b


column_label: Table 4; row APAL; ZmAMADH1b Km column

raw_value_unit_evidence: Table 4 ZmAMADH1b / APAL Km 11 +/- 2 uM

row_label: ZmAMADH1b / APAL


column_label: Table 4; row TMABAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.01 mM converted from 10 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / TMABAL Km 10 +/- 2 uM

row_label: ZmAMADH1b / TMABAL


column_label: Table 4; row GBAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.005 mM converted from 5 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / GBAL Km 5 +/- 1 uM

row_label: ZmAMADH1b / GBAL


column_label: Table 4; row BAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.029 mM converted from 29 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / BAL Km 29 +/- 4 uM

row_label: ZmAMADH1b / BAL


column_label: Table 4; row NAD +; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.079 mM converted from 79 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / NAD + Km 79 +/- 6 uM

row_label: ZmAMADH1b / NAD +


column_label: Table 4; row ABAL; ZmAMADH1a Km column

normalized_value_unit_evidence: Km=0.028 mM converted from 28 uM

raw_value_unit_evidence: Table 4 ZmAMADH1a / ABAL Km 28 +/- 3 uM

row_label: ZmAMADH1a / ABAL


column_label: Table 4; row APAL; ZmAMADH1a Km column

raw_value_unit_evidence: Table 4 ZmAMADH1a / APAL Km 9 +/- 2 uM

row_label: ZmAMADH1a / APAL


column_label: Table 4; row TMABAL; ZmAMADH1a Km column

normalized_value_unit_evidence: Km=0.006 mM converted from 6 uM

raw_value_unit_evidence: Table 4 ZmAMADH1a / TMABAL Km 6 +/- 0.8 uM

row_label: ZmAMADH1a / TMABAL


column_label: Table 4; row GBAL; ZmAMADH1a Km column

normalized_value_unit_evidence: Km=0.003 mM converted from 3 uM

raw_value_unit_evidence: Table 4 ZmAMADH1a / GBAL Km 3 +/- 0.7 uM

row_label: ZmAMADH1a / GBAL


column_label: Table 3; row NAD +; SlAMADH2 Km column

normalized_value_unit_evidence: Km=0.089 mM converted from 89 uM

raw_value_unit_evidence: Table 3 SlAMADH2 / NAD + Km 89 +/- 3 uM

row_label: SlAMADH2 / NAD +


substrate_name: Feruloyl-CoA

assay_conditions_summary: pH 6.25; 303.15 K; cofactor CoA

substrate: Feruloyl-CoA


substrate_name: caffeoyl-CoA


substrate: sinapoyl-CoA


column_label: ScienceDirect PMID 11430991 Table 1 row Feruloyl-CoA under Km (uM) AtCCR1 reports 0.96.

raw_value_unit_evidence: Feruloyl-CoA Km AtCCR1 0.96 uM

row_label: Feruloyl-CoA

table_label: PMID 11430991 Table 1. Kinetic parameters of AtCCR1 and AtCCR2 fusion proteins

substrate: feruloyl-CoA


substrate_name: p-coumaroyl-CoA

column_label: ScienceDirect PMID 16122934 Table 1 row p-Coumaroyl-CoA under Km +/- S.D. (uM) reports 2.27 +/- 0.07.

raw_value_unit_evidence: p-Coumaroyl-CoA Km 2.27 +/- 0.07 uM

row_label: p-Coumaroyl-CoA

table_label: PMID 16122934 Table 1. Kinetic parameters for recombinant AtCCR1

substrate: p-coumaroyl-CoA


column_label: ScienceDirect PMID 11430991 Table 1 row Sinapoyl-CoA under Km (uM) AtCCR1 reports 6.32.

raw_value_unit_evidence: Sinapoyl-CoA Km AtCCR1 6.32 uM

row_label: Sinapoyl-CoA


substrate: caffeoyl-CoA


organism: Homo sapiens


substrate_name: acrolein

smiles: C=CC=O

substrate: acrolein


substrate_name: formaldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


substrate_name: butyraldehyde

smiles: CCCC=O

substrate: butyraldehyde


substrate_name: hexanaldehyde

smiles: CCCCCC=O

substrate: hexanaldehyde


assay_conditions_summary: pH 9


substrate: formaldehyde


assay_conditions_summary: pH 9; cofactor NADPH


organism: Sorghum bicolor

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T154A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 303.15 K; cofactor CoA


column_label: PMID 27956488 / PMCID PMC5291045 / DOI 10.1104/pp.16.01671, Table IV. Kinetic values for wild-type SbCCR1 in the presence of three hydroxycinnamoyl-CoA substrates, row Wild-type SbCCR1 / p-Coumaroyl-CoA (4-coumaroyl-CoA), kcat, Km, and kcat/Km columns for the expected substrate/mutation context.

raw_value_unit_evidence: Table IV. Kinetic values for wild-type SbCCR1 in the presence of three hydroxycinnamoyl-CoA substrates, row Wild-type SbCCR1 / p-Coumaroyl-CoA (4-coumaroyl-CoA): kcat 0.05 s^-1; Km 100 uM; kcat/Km 0.0005 uM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProt C5YLL4 plus paper-linked PDB 5TQM and applied mutation signature T154Y to reconstruct the assayed variant sequence.

column_label: PMID 27956488 / PMCID PMC5291045, Table V, row T154Y / p-Coumaroyl-CoA (4-coumaroyl-CoA), columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1), with the Enzyme Kinetic Assays conditions.

normalized_value_unit_evidence: Same-row central values: kcat 8.42 s^-1; Km 0.113 mM; independently printed kcat/Km 74.5 s^-1 mM^-1.

raw_value_unit_evidence: Table V row T154Y / p-Coumaroyl-CoA (4-coumaroyl-CoA): kcat 8.42 s^-1; Km 113 uM; independently printed kcat/Km 0.0745 uM^-1 s^-1.

table_label: Table V


column_label: PMID 27956488 / PMCID PMC5291045, Table IV, row Wild-type SbCCR1 / Caffeoyl-CoA, columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1), with the Enzyme Kinetic Assays conditions.

normalized_value_unit_evidence: Same-row central values: kcat 0.01 s^-1; Km 0.014 mM; independently printed kcat/Km 0.8 s^-1 mM^-1.

raw_value_unit_evidence: Table IV row Wild-type SbCCR1 / Caffeoyl-CoA: kcat 0.01 s^-1; Km 14 uM; independently printed kcat/Km 0.0008 uM^-1 s^-1.

row_label: Wild-type SbCCR1 / Caffeoyl-CoA

table_label: Table IV


column_label: PMID 27956488 / PMCID PMC5291045 / DOI 10.1104/pp.16.01671, Table IV. Kinetic values for wild-type SbCCR1 in the presence of three hydroxycinnamoyl-CoA substrates, row Wild-type SbCCR1 / Feruloyl-CoA, kcat, Km, and kcat/Km columns for the expected substrate/mutation context.

raw_value_unit_evidence: Table IV. Kinetic values for wild-type SbCCR1 in the presence of three hydroxycinnamoyl-CoA substrates, row Wild-type SbCCR1 / Feruloyl-CoA: kcat 3.96 s^-1; Km 70 uM; kcat/Km 0.0566 uM^-1 s^-1.

row_label: Wild-type SbCCR1 / Feruloyl-CoA


sequence_source: UniProt C5YLL4 plus paper-linked PDB 5TQM

column_label: PMID 27956488 / PMCID PMC5291045, Table V, row T154Y / Feruloyl-CoA, columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1), with the Enzyme Kinetic Assays conditions.

normalized_value_unit_evidence: Same-row central values: kcat 17.24 s^-1; Km 0.063 mM; independently printed kcat/Km 273.6 s^-1 mM^-1.

raw_value_unit_evidence: Table V row T154Y / Feruloyl-CoA: kcat 17.24 s^-1; Km 63 uM; independently printed kcat/Km 0.2736 uM^-1 s^-1.

row_label: T154Y / Feruloyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y310F to reconstruct the assayed variant sequence.


enzyme_display_name: Aminoaldehyde dehydrogenase BADH

organism: Spinacia oleracea

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

assay_conditions_summary: pH 8; cofactor NAD+

column_label: Primary PMC HTML Table I BAL section, Wild type row, Km column = 69 +/- 5 uM.

normalized_value_unit_evidence: Normalized paper Km: 69 uM = 0.069 mM, matching export Km 0.069 mM.

raw_value_unit_evidence: Table I BAL wild-type row reports Km 69 +/- 5 uM.

row_label: BAL section; Wild type row; Km column

table_label: Table I. Kinetic parameters of wild-type and mutant SoBADH enzymes using different omega-aminoaldehydes as substrates

enzyme: Aminoaldehyde dehydrogenase BADH


column_label: Primary PMC HTML Table I ABAL section, Wild type row, Km column = 5.5 +/- 0.6 uM.

normalized_value_unit_evidence: Normalized paper Km: 5.5 uM = 0.0055 mM, matching export Km 0.0055 mM.

raw_value_unit_evidence: Table I ABAL wild-type row reports Km 5.5 +/- 0.6 uM.

row_label: ABAL section; Wild type row; Km column


column_label: Primary PMC HTML Table I APAL section, Wild type row, Km column = 2.6 +/- 0.3 uM.

normalized_value_unit_evidence: Normalized paper Km: 2.6 uM = 0.0026 mM, matching export Km 0.0026000000000000003 mM.

raw_value_unit_evidence: Table I APAL wild-type row reports Km 2.6 +/- 0.3 uM.

row_label: APAL section; Wild type row; Km column


column_label: Primary PMC HTML Table I TMABAL section, Wild type row, Km column = 3.6 +/- 0.2 uM.

normalized_value_unit_evidence: Normalized paper Km: 3.6 uM = 0.0036 mM, matching export Km 0.0036000000000000003 mM.

raw_value_unit_evidence: Table I TMABAL wild-type row reports Km 3.6 +/- 0.2 uM.

row_label: TMABAL section; Wild type row; Km column


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal

organism: Arabidopsis thaliana

column_label: Table 2 AtALDH10A9 Km [uM] column TMABAL row = 17+/-2.

normalized_value_unit_evidence: Km=0.017 mM converted from 17+/-2 uM.

raw_value_unit_evidence: AtALDH10A9 Km column for TMABAL reports 17+/-2 uM.

row_label: AtALDH10A9 / Km column / TMABAL row

table_label: Table 2 / Kinetic parameters of both AtALDH10 isoforms for aminoaldehydes and NAD+


column_label: Table 2 AtALDH10A9 Km [uM] column GBAL row = 7+/-0.5.

normalized_value_unit_evidence: Km=0.007 mM converted from 7+/-0.5 uM.

raw_value_unit_evidence: AtALDH10A9 Km column for GBAL reports 7+/-0.5 uM.

row_label: AtALDH10A9 / Km column / GBAL row

enzyme: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A8, chloroplastic

column_label: Table 2 AtALDH10A8 Km [uM] column TMABAL row = 15+/-3.

normalized_value_unit_evidence: Km=0.015 mM converted from 15+/-3 uM.

raw_value_unit_evidence: AtALDH10A8 Km column for TMABAL reports 15+/-3 uM.

row_label: AtALDH10A8 / Km column / TMABAL row


column_label: Table 2 AtALDH10A8 Km [uM] column GBAL row = 4+/-2.

normalized_value_unit_evidence: Km=0.004 mM converted from 4+/-2 uM.

raw_value_unit_evidence: AtALDH10A8 Km column for GBAL reports 4+/-2 uM.

row_label: AtALDH10A8 / Km column / GBAL row

enzyme: Aminoaldehyde dehydrogenase ALDH10A8, chloroplastic


substrate_name: NAD

proof_lines:
ALDH9A1
substrate specificity
NAD

substrate: NAD


substrate_name: NADP

proof_lines:
ALDH9A1
coenzyme specificity
NADP

substrate: NADP


substrate_name: gamma-trimethylaminobutyraldehyde

substrate: gamma-trimethylaminobutyraldehyde


substrate_name: heptanal

smiles: CCCCCCC=O

proof_lines:
ALDH9A1
aldehyde specificity
heptanal

substrate: heptanal


substrate_name: octanal

proof_lines:
ALDH9A1
aldehyde specificity
octanal

substrate: octanal


substrate_name: NAD(+) with 4-aminobutanal as substrate

substrate: NAD(+) with 4-aminobutanal as substrate


column_label: Table 1, column p-Coumaroyl-CoA, metric rows Km (uM), kcat (s^-1), and kcat/Km (mM^-1 s^-1)


substrate_name: feruloyl-CoA

column_label: Table 1, column Feruloyl-CoA, metric rows Km (uM), kcat (s^-1), and kcat/Km (mM^-1 s^-1)


substrate_name: sinapoyl-CoA

column_label: Table 1, column Sinapoyl-CoA, metric rows Km (uM), kcat (s^-1), and kcat/Km (mM^-1 s^-1)


organism: Rattus norvegicus

assay_conditions_summary: pH 7.4; cofactor NAD+

column_label: Table II, enzyme column Rat liver TMABA-DH, row NAD+, column Km (uM).

normalized_value_unit_evidence: Km=0.028 mM converted from 28 uM.

raw_value_unit_evidence: Table II reports Rat liver TMABA-DH NAD+ Km=28 uM.

row_label: Rat liver TMABA-DH / NAD+

table_label: Table II: Substrate specificity of purified TMABA-DH and heterologously expressed enzymes


assay_conditions_summary: pH 9; buffer pH 9; cofactor NADP+

column_label: Table II, enzyme column Rat liver TMABA-DH, row NADP+, column Km (microM).

normalized_value_unit_evidence: Km normalized_value=1.63 normalized_unit=mM converted from 1630 microM.

raw_value_unit_evidence: Table II reports Rat liver TMABA-DH / NADP+ Km=1630 microM.

row_label: Rat liver TMABA-DH / NADP+


assay_conditions_summary: pH 9; buffer pH 9; cofactor NAD+

column_label: Table II, enzyme column Rat liver TMABA-DH, row gamma-trimethylaminobutyraldehyde, column Km (microM).

normalized_value_unit_evidence: Km normalized_value=0.0014 normalized_unit=mM converted from 1.4 microM.

raw_value_unit_evidence: Table II reports Rat liver TMABA-DH / gamma-trimethylaminobutyraldehyde Km=1.4 microM.


column_label: Table II, enzyme column Rat liver TMABA-DH, row gamma-aminobutyraldehyde, column Km (uM).

normalized_value_unit_evidence: Km=0.024 mM converted from 24 uM.

raw_value_unit_evidence: Table II reports Rat liver TMABA-DH gamma-aminobutyraldehyde Km=24 uM.

row_label: Rat liver TMABA-DH / gamma-aminobutyraldehyde


column_label: Table II, enzyme column Rat liver TMABA-DH, row Heptanal (C7), column Km (uM).

normalized_value_unit_evidence: Km=0.007 mM converted from 7 uM.

raw_value_unit_evidence: Table II reports Rat liver TMABA-DH Heptanal (C7) Km=7 uM.

row_label: Rat liver TMABA-DH / Heptanal (C7)


column_label: Table II, enzyme column Rat liver TMABA-DH, row Octanal (C8), column Km (microM).

normalized_value_unit_evidence: Km normalized_value=0.006 normalized_unit=mM converted from 6 microM.

raw_value_unit_evidence: Table II reports Rat liver TMABA-DH / Octanal (C8) Km=6 microM.

row_label: Rat liver TMABA-DH / Octanal (C8)


enzyme_display_name: glutamate-5-semialdehyde dehydrogenase

substrate_name: NADP+

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

enzyme: glutamate-5-semialdehyde dehydrogenase

substrate: NADP+


substrate_name: L-glutamate 5-semialdehyde

assay_conditions_summary: cofactor NADP+

column_label: Abstract prose reports apparent Km values: 1.8 mM for pyrroline 5-carboxylate; this is the radiochemical assay substrate for the gamma-glutamate semialdehyde dehydrogenase paper.

raw_value_unit_evidence: apparent Km = 1.8 mM for pyrroline 5-carboxylate

row_label: pyrroline 5-carboxylate assay substrate for gamma-glutamate semialdehyde dehydrogenase

table_label: PubMed/NCBI abstract prose

substrate: L-glutamate 5-semialdehyde


substrate_name: phosphate

column_label: Abstract prose reports apparent Km values including 11.3 mM for phosphate.

raw_value_unit_evidence: apparent Km = 11.3 mM for phosphate

row_label: phosphate

substrate: phosphate


enzyme_display_name: Aldehyde dehydrogenase family 3 member B1

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_name: hexadecanal

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: Pseudomonas aeruginosa (strain LESB58)

substrate_name: formaldehyde

proof_lines:
formaldehyde activity
P. aeruginosa FDH


substrate_name: NAD(+)

assay_conditions_summary: cofactor NAD+

proof_lines:
NAD+ binding
P. aeruginosa FDH

substrate: NAD(+)


organism: Fragaria x ananassa

column_label: Table 1 row feruloyl-CoA gives Km 16.11 microM, Kcat 2.34 x 10^-3 s^-1, and Kcat/Km 1.45 x 10^-4 s^-1 microM^-1.

normalized_value_unit_evidence: Km normalized_value=0.01611 mM; Kcat normalized_value=0.00234 s^-1; Kcat/Km normalized_value=0.145 s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=16.11 microM; Kcat raw_value=2.34 x 10^-3 s^-1; Kcat/Km raw_value=1.45 x 10^-4 s^-1 microM^-1

row_label: GST-FaCCR / feruloyl-CoA

table_label: Official PMC full-text Table 1: Kinetic parameters for recombinant GST-FaCCR

substrate: feruloyl-CoA


substrate_name: propanal

assay_conditions_summary: pH 9; buffer 0.1 M sodium pyrophosphate

column_label: Table 3; row Km propionaldehyde (0.5 mM NAD); column Cytoplasmic rat liver isozyme.

normalized_value_unit_evidence: Km 0.0075 mM from 7.5 microM.

raw_value_unit_evidence: Table 3 row Km propionaldehyde (0.5 mM NAD), column Cytoplasmic rat liver isozyme: 7.5 +/- 1.3 microM (n=3). Footnote: propionaldehyde Km determined in 0.1 M sodium pyrophosphate buffer, pH 9.0.

row_label: Km propionaldehyde (0.5 mM NAD) / cytoplasmic rat liver isozyme

table_label: Table 3. Kinetic properties of partially purified cytoplasmic rat liver aldehyde dehydrogenase metabolizing gamma-aminobutyraldehyde and comparison with homogeneous E3 isozyme from human liver

substrate: propanal


organism: Populus tomentosa

assay_conditions_summary: pH 6; 313.15 K; cofactor CoA

proof_lines: pH 6.0, 40°C, recombinant His-tagged mutant A132T


proof_lines: pH 6.0, 40°C, recombinant His-tagged mutant F155Y


proof_lines: pH 6.0, 40°C, recombinant His-tagged enzyme

proof_lines: pH 6.25, 37°C, recombinant His-tagged enzyme


proof_lines: pH 6.0, 40°C, recombinant His-tagged mutant A132S


substrate_name: caffeoyl-CoA

substrate: caffeoyl-CoA


substrate: sinapoyl-CoA


proof_lines: pH 6.0, 40°C, recombinant His-tagged mutant A43V


proof_lines: pH 6.0, 40°C, recombinant His-tagged mutant F155H


proof_lines: pH 6.0, 40°C, recombinant His-tagged mutant L192M


proof_lines: pH 6.0, 40°C, recombinant His-tagged wild-type enzyme


substrate_name: betaine aldehyde

substrate: betaine aldehyde


organism: Pseudomonas putida

substrate_name: n-Hexanol

smiles: CCCCCCO

substrate: n-Hexanol


substrate_name: Isopentanol

smiles: CC(C)CCO

substrate: Isopentanol


substrate_name: benzyl alcohol

substrate: benzyl alcohol


substrate_name: acetaldehyde

substrate: acetaldehyde


substrate_name: Isobutyraldehyde

smiles: CC(C)C=O

substrate: Isobutyraldehyde


substrate_name: n-Pentanol

smiles: CCCCCO

substrate: n-Pentanol


substrate_name: n-butanol

smiles: CCCCO

substrate: n-butanol


substrate_name: isobutanol

smiles: CC(C)CO

substrate: isobutanol


substrate_name: propionaldehyde

substrate: propionaldehyde


substrate_name: n-Propanol

smiles: CCCO

substrate: n-Propanol


enzyme_display_name: phenylacetaldehyde dehydrogenase

organism: Escherichia coli

substrate_name: benzaldehyde

enzyme: phenylacetaldehyde dehydrogenase

substrate: benzaldehyde


substrate_name: NAD+

assay_conditions_summary: pH 7.5; cofactor NAD+

proof_lines: with phenylacetaldehyde as cosubstrate, at pH 7.7, temperature not specified in the publication

substrate: NAD+


substrate_name: NADP+

assay_conditions_summary: pH 7.5; cofactor NADP+

substrate: NADP+


substrate_name: hexanal

substrate: hexanal


substrate_name: Heptanal

substrate: Heptanal


substrate_name: phenylacetaldehyde

proof_lines: with NAD+ as cosubstrate, at pH, temperature not specified in the publication

substrate: phenylacetaldehyde


enzyme_display_name: cinnamoyl-CoA reductase

substrate_name: caffeoyl-CoA

enzyme: cinnamoyl-CoA reductase

substrate: caffeoyl-CoA


substrate_name: feruloyl-CoA

substrate: feruloyl-CoA


organism: Glycine max

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines:
cosubstrate feruloyl-CoA
cosubstrate sinapoyl-CoA
cosubstrate p-coumaroyl-CoA

substrate: NADPH


assay_conditions_summary: cofactor CoA


substrate_name: p-Coumaroyl-CoA

substrate: p-Coumaroyl-CoA


substrate_name: sinapoyl-CoA

substrate: sinapoyl-CoA


substrate_name: cinnamoyl-CoA

substrate: cinnamoyl-CoA


enzyme_display_name: aspartate-semialdehyde dehydrogenase

enzyme: aspartate-semialdehyde dehydrogenase


substrate_name: L-aspartate 4-semialdehyde

substrate: L-aspartate 4-semialdehyde


substrate_name: N-acetyl-L-glumate 5-semialdehyde

substrate: N-acetyl-L-glumate 5-semialdehyde


substrate_name: phosphate

substrate: phosphate


enzyme_display_name: 2-oxoaldehyde dehydrogenase (NADP+)

organism: Capra hircus

substrate_name: NADP+; H2O; Methylglyoxal

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

enzyme: 2-oxoaldehyde dehydrogenase (NADP+)

substrate: NADP+; H2O; Methylglyoxal


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


organism: Vicia faba

substrate_name: gamma-guanidinobutyraldehyde

substrate: gamma-guanidinobutyraldehyde


substrate_name: gamma-aminobutyraldehyde

smiles: C(CC=O)CN

substrate: gamma-aminobutyraldehyde


substrate_name: NAD+

substrate: NAD+


organism: Ovis aries

substrate_name: H2O; Methylglyoxal; NADP+

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

substrate: H2O; Methylglyoxal; NADP+


proof_lines: amine as activator in aldehyde oxidation

proof_lines: in the presence of L-2-aminopropan-1-ol (Km 83 mM), at pH 9.3 and 25°C


enzyme_display_name: long-chain acyl-protein thioester reductase

organism: Anas platyrhynchos

substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


enzyme: long-chain acyl-protein thioester reductase


proof_lines: in the presence of L-serine methyl ester (Km 8.0 mM)


substrate_name: NADP+

substrate: NADP+


enzyme_display_name: pyruvate dehydrogenase (NADP+)

organism: Euglena gracilis

substrate_name: CoA

proof_lines:
with NADP+
with methyl viologen

enzyme: pyruvate dehydrogenase (NADP+)

substrate: CoA


substrate_name: pyruvate

substrate: pyruvate


substrate_name: H2O; NADP+; Methylglyoxal

substrate: H2O; NADP+; Methylglyoxal


organism: Zea mays

assay_conditions_summary: pH 9; cofactor NAD+

column_label: Table 4; row ABAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.026 mM converted from 26 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / ABAL Km 26 +/- 4 uM

row_label: ZmAMADH1b / ABAL


smiles: C(CN)C=O

column_label: Table 4; row APAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.011 mM converted from 11 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / APAL Km 11 +/- 2 uM

row_label: ZmAMADH1b / APAL


smiles: C[N+](C)(C)CCCC=O

column_label: Table 4; row TMABAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.01 mM converted from 10 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / TMABAL Km 10 +/- 2 uM

row_label: ZmAMADH1b / TMABAL


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

column_label: Table 4; row GBAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.005 mM converted from 5 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / GBAL Km 5 +/- 1 uM

row_label: ZmAMADH1b / GBAL


substrate_name: betaine aldehyde

column_label: Table 4; row BAL; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.029 mM converted from 29 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / BAL Km 29 +/- 4 uM

row_label: ZmAMADH1b / BAL

substrate: betaine aldehyde


substrate_name: NAD(+) with 3-aminopropanal as substrate

column_label: Table 4; row NAD +; ZmAMADH1b Km column

normalized_value_unit_evidence: Km=0.079 mM converted from 79 uM

raw_value_unit_evidence: Table 4 ZmAMADH1b / NAD + Km 79 +/- 6 uM

row_label: ZmAMADH1b / NAD +


column_label: Table 4; row ABAL; ZmAMADH1a Km column

normalized_value_unit_evidence: Km=0.028 mM converted from 28 uM

raw_value_unit_evidence: Table 4 ZmAMADH1a / ABAL Km 28 +/- 3 uM

row_label: ZmAMADH1a / ABAL


column_label: Table 4; row APAL; ZmAMADH1a Km column

normalized_value_unit_evidence: Km=0.009 mM converted from 9 uM

raw_value_unit_evidence: Table 4 ZmAMADH1a / APAL Km 9 +/- 2 uM

row_label: ZmAMADH1a / APAL


column_label: Table 4; row TMABAL; ZmAMADH1a Km column

normalized_value_unit_evidence: Km=0.006 mM converted from 6 uM

raw_value_unit_evidence: Table 4 ZmAMADH1a / TMABAL Km 6 +/- 0.8 uM

row_label: ZmAMADH1a / TMABAL


column_label: Table 4; row GBAL; ZmAMADH1a Km column

normalized_value_unit_evidence: Km=0.003 mM converted from 3 uM

raw_value_unit_evidence: Table 4 ZmAMADH1a / GBAL Km 3 +/- 0.7 uM

row_label: ZmAMADH1a / GBAL