organism: Solanum lycopersicum

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: NAD(+) with 3-aminopropanal as substrate


enzyme_display_name: butanal dehydrogenase

organism: Clostridium acetobutylicum

substrate_name: Acetyl-CoA; NADH; H+

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

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

km_unit: mM

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

assay_conditions_summary: cofactor NADH

enzyme: butanal dehydrogenase

substrate: Acetyl-CoA; NADH; H+

status: unverified


substrate_name: NADH

source_db: brenda

source_license: CC BY 4.0

substrate: NADH

source: brenda


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: butanoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: butanoyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: Butanal

smiles: CCCC=O

substrate: Butanal


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


enzyme_display_name: Aminoaldehyde dehydrogenase 1

source_db: uniprot

verification_status: verified

protein_accession_database: UniProt

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

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

data_origin: experimental

enzyme: Aminoaldehyde dehydrogenase 1

status: verified

source: uniprot


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


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

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

verification_status: corrected

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

column_label: Table 3. Kinetic parameters of ALDH10 family from tomato for selected substrates and the coenzyme NAD+, row BAL, column SlAMADH1 Km; Km, cell 2051 +/- 83 uM, normalized 2.051 mM

raw_value_unit_evidence: Km raw 2051 +/- 83 uM from Table 3. Kinetic parameters of ALDH10 family from tomato for selected substrates and the coenzyme NAD+, row BAL, column SlAMADH1 Km

row_label: SlAMADH1 / BAL

substrate: betaine aldehyde

status: corrected


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


organism: Levilactobacillus brevis

assay_conditions_summary: pH 7.15; 303.15 K; cofactor CoA


organism: Pseudomonas putida


enzyme_display_name: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)

organism: Corynebacterium glutamicum

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

mutation_type: substitution

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

enzyme: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)


proof_lines: pH 8.0, 25°C, recombinant mutant D35G/L36T/T37K/P192S


proof_lines: pH 8.0, 25°C, recombinant mutant D35G/L36T/P192S


proof_lines: pH 8.0, 25°C, recombinant mutant D35G/L36T/T37K


organism: Daucus carota


assay_conditions_summary: pH 7.5; 308.15 K; cofactor NAD+


organism: Pyrococcus woesei

sequence_source: multiple

proof_lines: 50°C, pH not specified in the publication


source_databases_merged: brenda uniprot


organism: Pyrobaculum calidifontis

substrate_name: D-glyceraldehyde 3-phosphate

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

assay_conditions_summary: pH 7; cofactor NADP+

proof_lines: recombinant enzyme, pH 7.0, 80°C, with NAD+

proof_lines: recombinant enzyme, pH 7.0, 80°C, with NADP+

substrate: D-glyceraldehyde 3-phosphate


assay_conditions_summary: pH 7; cofactor NAD+


enzyme_display_name: Vanillin dehydrogenase

organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)

substrate_name: vanillin in the presence of 0.5 mM NAD(+) (at pH 7.0)

assay_conditions_summary: pH 7

proof_lines: kcat is 21.03 sec(-1) with vanillin as substrate in the presence of 0.5 mM NAD(+). kcat is 23.42 sec(-1) with 3,4-dihydroxybenzaldehyde as substrate in the presence of 0.5 mM NAD(+). kcat is 22.92 sec(-1) with 4-hydroxybenzaldehyde as subst

enzyme: Vanillin dehydrogenase


substrate_name: 3,4-dihydroxybenzaldehyde in the presence of 0.5 mM NAD(+) (at pH 7.0)


substrate_name: 4-hydroxybenzaldehyde in the presence of 0.5 mM NAD(+) (at pH 7.0)


substrate_name: NAD(+) in the presence of 1 mM vanillin

substrate: NAD(+) in the presence of 1 mM vanillin


substrate_name: NADP(+) in the presence of 1 mM vanillin


organism: Pyrococcus furiosus

substrate_name: NADPH

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

assay_conditions_summary: 323.15 K; cofactor NADPH


substrate_name: NADH

assay_conditions_summary: 323.15 K; cofactor NADH


organism: Synechocystis sp.


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


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 +


organism: Bacillus subtilis (strain 168)

substrate_name: NADP (at pH 9.2 and 25 degrees Celsius)

proof_lines: kcat is 1 sec(-1) for dehydrogenase activity with NAD (at pH 9.2 and 25 degrees Celsius). kcat is 8 sec(-1) for dehydrogenase activity with NADP (at pH 9.2 and 25 degrees Celsius).

substrate: NADP (at pH 9.2 and 25 degrees Celsius)


substrate_name: NAD (at pH 9.2 and 25 degrees Celsius)

substrate: NAD (at pH 9.2 and 25 degrees Celsius)


organism: Sulfurisphaera tokodaii

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

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines:
pH 8.0, 60°C, cosubstrate: NADP+
pH 8.0, 60°C, cosubstrate: NAD+


enzyme_display_name: NADH-dependent phenylglyoxylate dehydrogenase subunit beta

organism: Aromatoleum evansii

substrate_name: phenylglyoxylate (under anaerobic conditions at 37 degrees Celsius and pH 7.8)


substrate_name: coenzyme-A (under anaerobic conditions at 37 degrees Celsius and pH 7.8)

enzyme: NADH-dependent phenylglyoxylate dehydrogenase subunit beta


substrate_name: NAD (under anaerobic conditions at 37 degrees Celsius and pH 7.8)

assay_conditions_summary: pH 7.8; cofactor NAD+


enzyme_display_name: NADH-dependent phenylglyoxylate dehydrogenase subunit delta

substrate: phenylglyoxylate (under anaerobic conditions at 37 degrees Celsius and pH 7.8)


enzyme: NADH-dependent phenylglyoxylate dehydrogenase subunit delta

substrate: coenzyme-A (under anaerobic conditions at 37 degrees Celsius and pH 7.8)


substrate: NAD (under anaerobic conditions at 37 degrees Celsius and pH 7.8)


enzyme_display_name: NADH-dependent phenylglyoxylate dehydrogenase subunit epsilon


enzyme: NADH-dependent phenylglyoxylate dehydrogenase subunit epsilon


enzyme_display_name: NADH-dependent phenylglyoxylate dehydrogenase subunit gamma


assay_conditions_summary: pH 7.8; cofactor CoA

column_label: Results prose and Table 6 property row Apparent Km values; substrate CoA; metric Km; raw value 55 uM; normalized value 0.055 mM.

raw_value_unit_evidence: Apparent Km value 55 uM CoA.

row_label: Apparent Km values / CoA

table_label: Results prose and Table 6. Properties of the new enzyme phenylglyoxylate:acceptor oxidoreductase from A. evansii

enzyme: NADH-dependent phenylglyoxylate dehydrogenase subunit gamma


column_label: Results prose and Table 6 property row Apparent Km values; substrate NAD+; metric Km; raw value 74 uM; normalized value 0.074 mM.

raw_value_unit_evidence: Apparent Km value 74 uM NAD+.

row_label: Apparent Km values / NAD+


enzyme_display_name: NADH-dependent phenylglyoxylate dehydrogenase subunit alpha

column_label: Results prose and Table 6 property row Apparent Km values; substrate phenylglyoxylate; metric Km; raw value 45 uM; normalized value 0.045 mM.

normalized_value_unit_evidence: 45 uM = 0.045 mM phenylglyoxylate.

raw_value_unit_evidence: Apparent Km value 45 uM phenylglyoxylate.

row_label: Apparent Km values / phenylglyoxylate


enzyme: NADH-dependent phenylglyoxylate dehydrogenase subunit alpha


organism: Methanothermus fervidus

substrate: NADPH


substrate_name: NADP+


substrate_name: NAD+


enzyme_display_name: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)(+)) (phosphorylating)

source_db: oed

sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_fasta:Q01651 and applied mutation signature D35G to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row D35G / NAD; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 0.54+/-0.07, Kcat 382+/-32, Kcat/Km 707+/-82.

normalized_value_unit_evidence: Km normalized_value=0.54 normalized_unit=mM; kcat normalized_value=6.366666666667 normalized_unit=s^-1; kcat/Km normalized_value=11.783333333333 normalized_unit=s^-1 mM^-1.

row_label: D35G / NAD

source: oed


sequence_variant_note: Mutation signature D35G/L36T/P192S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

enzyme: glyceraldehyde-3-phosphate dehydrogenase (NAD(P)(+)) (phosphorylating)


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_fasta:Q01651 and applied mutation signature D35G/L36T/T37K to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row M1(D35G/L36T/T37K) / NAD; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 0.47+/-0.03, Kcat 252+/-33, Kcat/Km 536+/-48.

normalized_value_unit_evidence: Km normalized_value=0.47 normalized_unit=mM; kcat normalized_value=4.2 normalized_unit=s^-1; kcat/Km normalized_value=8.933333333333 normalized_unit=s^-1 mM^-1.


kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_fasta:Q01651 and applied mutation signature D35G/L36T/T37K/P192S to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row M3(D35G/L36T/T37K/P192S) / NAD; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 0.10+/-0.014, Kcat 164+/-12, Kcat/Km 1640+/-108.

normalized_value_unit_evidence: Km normalized_value=0.1 normalized_unit=mM; kcat normalized_value=2.733333333333 normalized_unit=s^-1; kcat/Km normalized_value=27.333333333333 normalized_unit=s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_fasta:Q01651 and applied mutation signature L36T to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row L36T / NAD; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 0.14+/-0.02, Kcat 87+/-6, Kcat/Km 620+/-132.

normalized_value_unit_evidence: Km normalized_value=0.14 normalized_unit=mM; kcat normalized_value=1.45 normalized_unit=s^-1; kcat/Km normalized_value=10.333333333333 normalized_unit=s^-1 mM^-1.

row_label: L36T / NAD


column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row D35G / NADP; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 0.83+/-0.12, Kcat 178+/-11, Kcat/Km 215+/-22.

normalized_value_unit_evidence: Km normalized_value=0.83 normalized_unit=mM; kcat normalized_value=2.966666666667 normalized_unit=s^-1; kcat/Km normalized_value=3.583333333333 normalized_unit=s^-1 mM^-1.

row_label: D35G / NADP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q01651 and applied mutation signature D35G/L36T/T37K to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row M1(D35G/L36T/T37K) / NADP; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 0.10+/-0.01, Kcat 480+/-36, Kcat/Km 4800+/-232.

normalized_value_unit_evidence: Km normalized_value=0.1 normalized_unit=mM; kcat normalized_value=8 normalized_unit=s^-1; kcat/Km normalized_value=80 normalized_unit=s^-1 mM^-1.


column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row M3(D35G/L36T/T37K/P192S) / NADP; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 0.070+/-0.003, Kcat 428+/-45, Kcat/Km 5868+/-352.

normalized_value_unit_evidence: Km normalized_value=0.07 normalized_unit=mM; kcat normalized_value=7.133333333333 normalized_unit=s^-1; kcat/Km normalized_value=97.8 normalized_unit=s^-1 mM^-1.


column_label: Table 2. Kinetic parameters of wildtype and mutant glyceraldehyde 3-phosphate dehydrogenase; row L36T / NADP; columns Km (mM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); cells Km 1.46+/-0.35, Kcat 95+/-9, Kcat/Km 65+/-9.

normalized_value_unit_evidence: Km normalized_value=1.46 normalized_unit=mM; kcat normalized_value=1.583333333333 normalized_unit=s^-1; kcat/Km normalized_value=1.083333333333 normalized_unit=s^-1 mM^-1.

row_label: L36T / NADP


assay_conditions_summary: pH 8; cofactor NADPH

column_label: PMID 22841742 / DOI 10.1016/j.febslet.2012.07.059, Table 4, row Reduction / NADPH, K_m (mM) column = 0.18 +/- 0.07 mM (paper variable substrate NADPH).

raw_value_unit_evidence: Table 4 row Reduction / NADPH, K_m column: 0.18 +/- 0.07 mM; fixed substrate: 10 mM 3-PG; Vmax column: 86.9 +/- 22.1 U/mg; Ki column: 0.035 +/- 0.015 mM (Ki1 Ki2 Ki3). For DL-GAP, NAD+, NADP+ and 3-PG the kinetic parameters were fit with a single-inhibitory-site model; for NADH and NADPH they were fit with a three-inhibitory-site model; phosphate was fit with Michaelis-Menten. Footnotes: oxidation rows measured at 60 deg C; reduction rows measured at 50 deg C.

row_label: Reduction / NADPH

table_label: Table 4. Kinetic parameters of phosphorylating glyceraldehyde 3-phosphate dehydrogenase (St-GAPDH) for the oxidative and reductive reactions


column_label: PMID 22841742 / DOI 10.1016/j.febslet.2012.07.059, Table 4, row Oxidation / NADP+, K_m (mM) column = 0.28 +/- 0.08 mM (paper variable substrate NADP+).

raw_value_unit_evidence: Table 4 row Oxidation / NADP+, K_m column: 0.28 +/- 0.08 mM; fixed substrate: 10 mM DL-GAP, 10 mM phosphate; Vmax column: 8.2 +/- 1.5 U/mg; Ki column: 0.75 +/- 0.21 mM. For DL-GAP, NAD+, NADP+ and 3-PG the kinetic parameters were fit with a single-inhibitory-site model; for NADH and NADPH they were fit with a three-inhibitory-site model; phosphate was fit with Michaelis-Menten. Footnotes: oxidation rows measured at 60 deg C; reduction rows measured at 50 deg C.

row_label: Oxidation / NADP+


substrate_name: 3-phospho-D-glyceroyl phosphate

assay_conditions_summary: pH 8

substrate: 3-phospho-D-glyceroyl phosphate


column_label: PMID 22841742 / DOI 10.1016/j.febslet.2012.07.059, Table 4, row Oxidation / NAD+, K_m (mM) column = 16.8 +/- 8.9 mM (paper variable substrate NAD+).

raw_value_unit_evidence: Table 4 row Oxidation / NAD+, K_m column: 16.8 +/- 8.9 mM; fixed substrate: 10 mM DL-GAP, 10 mM phosphate; Vmax column: 14.5 +/- 5.5 U/mg; Ki column: 10.7 +/- 5.3 mM. For DL-GAP, NAD+, NADP+ and 3-PG the kinetic parameters were fit with a single-inhibitory-site model; for NADH and NADPH they were fit with a three-inhibitory-site model; phosphate was fit with Michaelis-Menten. Footnotes: oxidation rows measured at 60 deg C; reduction rows measured at 50 deg C.

row_label: Oxidation / NAD+


substrate_name: phosphate

assay_conditions_summary: pH 8; cofactor NAD+

column_label: PMID 22841742 / DOI 10.1016/j.febslet.2012.07.059, Table 4, row Oxidation / Phosphate, K_m (mM) column = 107 +/- 22 mM (paper variable substrate Phosphate).

normalized_value_unit_evidence: km=107 mM

raw_value_unit_evidence: Table 4 row Oxidation / Phosphate, K_m column: 107 +/- 22 mM; fixed substrate: 10 mM DL-GAP, 1 mM NADP+; Vmax column: 48.4 +/- 7.4 U/mg; Ki column: -. For DL-GAP, NAD+, NADP+ and 3-PG the kinetic parameters were fit with a single-inhibitory-site model; for NADH and NADPH they were fit with a three-inhibitory-site model; phosphate was fit with Michaelis-Menten. Footnotes: oxidation rows measured at 60 deg C; reduction rows measured at 50 deg C.

row_label: Oxidation / Phosphate

substrate: phosphate


enzyme_display_name: Aminoaldehyde dehydrogenase 2, peroxisomal

organism: Pisum sativum

column_label: Table 3; row APAL / 3-aminopropanal; column PsAMADH2 Km (uM); raw 10 uM; normalized 0.01 mM.

raw_value_unit_evidence: Table 3 row APAL / 3-aminopropanal gives PsAMADH2 Km 10 uM.

row_label: APAL / 3-aminopropanal (PsAMADH2; UniProt Q93YB2)

table_label: PMID 20026072, Table 3: kinetic parameters of PsAMADHs for the natural substrates and coenzyme NAD+


column_label: Table 3; row ABAL / 4-aminobutanal; column PsAMADH2 Km (uM); raw 29 uM; normalized 0.029 mM.

raw_value_unit_evidence: Table 3 row ABAL / 4-aminobutanal gives PsAMADH2 Km 29 uM.

row_label: ABAL / 4-aminobutanal (PsAMADH2; UniProt Q93YB2)

enzyme: Aminoaldehyde dehydrogenase 2, peroxisomal


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

column_label: Table 3; row GBAL / 4-guanidinobutanal; column PsAMADH2 Km (uM); raw 7 uM; normalized 0.007 mM.

raw_value_unit_evidence: Table 3 row GBAL / 4-guanidinobutanal gives PsAMADH2 Km 7 uM.

row_label: GBAL / 4-guanidinobutanal (PsAMADH2; UniProt Q93YB2)


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

column_label: Table 3; row NAD+ with APAL substrate; column PsAMADH2 Km (uM); raw 55 uM; normalized 0.055 mM.

raw_value_unit_evidence: Table 3 row NAD+ with APAL substrate gives PsAMADH2 Km 55 uM.

row_label: NAD+ with APAL substrate (PsAMADH2; UniProt Q93YB2)


enzyme_display_name: Aminoaldehyde dehydrogenase 1, peroxisomal

column_label: Table 3; row APAL / 3-aminopropanal; column PsAMADH1 Km (uM); raw 75 uM; normalized 0.075 mM.

raw_value_unit_evidence: Table 3 row APAL / 3-aminopropanal gives PsAMADH1 Km 75 uM.

row_label: APAL / 3-aminopropanal (PsAMADH1; UniProt Q8VWZ1)


enzyme: Aminoaldehyde dehydrogenase 1, peroxisomal


column_label: Table 3; row GBAL / 4-guanidinobutanal; column PsAMADH1 Km (uM); raw 11 uM; normalized 0.011 mM.

raw_value_unit_evidence: Table 3 row GBAL / 4-guanidinobutanal gives PsAMADH1 Km 11 uM.

row_label: GBAL / 4-guanidinobutanal (PsAMADH1; UniProt Q8VWZ1)


column_label: Table 3; row NAD+ with APAL substrate; column PsAMADH1 Km (uM); raw 40 uM; normalized 0.04 mM.

raw_value_unit_evidence: Table 3 row NAD+ with APAL substrate gives PsAMADH1 Km 40 uM.

row_label: NAD+ with APAL substrate (PsAMADH1; UniProt Q8VWZ1)

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


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal

organism: Arabidopsis thaliana

assay_conditions_summary: pH 9; cofactor NAD+

column_label: Table 2 / Kinetic parameters of both AtALDH10 isoforms for aminoaldehydes and NAD+ AtALDH10A9 / Km column / ABAL row = 31+/-4 uM.

normalized_value_unit_evidence: Km=0.031 mM converted from 31+/-4 uM.

raw_value_unit_evidence: AtALDH10A9 Km column for ABAL reports 31+/-4 uM.

row_label: AtALDH10A9 / Km column / ABAL row


assay_conditions_summary: pH 9.5; cofactor NAD+

column_label: Table 1 / Kinetic parameters for AtALDH10A8 and AtALDH10A9 AtALDH10A9 / Km column / APAL row = 17.3+/-4.1 uM.

normalized_value_unit_evidence: Km=0.0173 mM converted from 17.3+/-4.1 uM.

raw_value_unit_evidence: AtALDH10A9 Km column for APAL reports 17.3+/-4.1 uM.

row_label: AtALDH10A9 / Km column / APAL row

enzyme: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal


column_label: Table 2 / Kinetic parameters of both AtALDH10 isoforms for aminoaldehydes and NAD+ AtALDH10A9 / Km column / NAD+ row = 33+/-4 uM.

normalized_value_unit_evidence: Km=0.033 mM converted from 33+/-4 uM.

raw_value_unit_evidence: AtALDH10A9 Km column for NAD+ reports 33+/-4 uM.

row_label: AtALDH10A9 / Km column / NAD+ row


enzyme_display_name: Aminoaldehyde dehydrogenase ALDH10A8, chloroplastic

column_label: Table 2 / Kinetic parameters of both AtALDH10 isoforms for aminoaldehydes and NAD+ AtALDH10A8 / Km column / ABAL row = 19+/-5 uM.

normalized_value_unit_evidence: Km=0.019 mM converted from 19+/-5 uM.

raw_value_unit_evidence: AtALDH10A8 Km column for ABAL reports 19+/-5 uM.

row_label: AtALDH10A8 / Km column / ABAL row


column_label: Table 2 / Kinetic parameters of both AtALDH10 isoforms for aminoaldehydes and NAD+ AtALDH10A8 / Km column / APAL row = 2+/-0.3 uM.

normalized_value_unit_evidence: Km=0.002 mM converted from 2+/-0.3 uM.

raw_value_unit_evidence: AtALDH10A8 Km column for APAL reports 2+/-0.3 uM.

row_label: AtALDH10A8 / Km column / APAL row

enzyme: Aminoaldehyde dehydrogenase ALDH10A8, chloroplastic


assay_conditions_summary: pH 8.5; cofactor NAD+

column_label: Table 1 / Kinetic parameters for AtALDH10A8 and AtALDH10A9 AtALDH10A8 / Km column / NAD+ row with APAL = 13.2+/-1.5 uM.

normalized_value_unit_evidence: Km=0.0132 mM converted from 13.2+/-1.5 uM.

raw_value_unit_evidence: AtALDH10A8 Km column for NAD+ in the APAL-dependent row reports 13.2+/-1.5 uM.


assay_conditions_summary: cofactor NADPH

column_label: Main text on printed page 4519 reports apparent Km values for NADPH and NADH in the reductive reaction were virtually identical, 10 +/- 1 uM.

raw_value_unit_evidence: Km raw_value=10 +/- 1 raw_unit=uM

row_label: Synechocystis sp. strain PCC 6803 GAPDH2

table_label: Main text, printed page 4519, kinetic paragraph for pyridine nucleotides


assay_conditions_summary: cofactor NADH

substrate: NADH


substrate_name: NAD(P)+

column_label: Main text across printed pages 4518-4519 reports apparent Km and Vmax measured for both NAD and NADP in the oxidative reaction, with identical values within experimental errors: Km 30 +/- 5 uM.

raw_value_unit_evidence: Km raw_value=30 +/- 5 raw_unit=uM

table_label: Main text, printed pages 4518-4519, kinetic paragraph for pyridine nucleotides

substrate: NAD(P)+


enzyme_display_name: vanillin dehydrogenase

organism: Sphingobium sp. SYK-6

substrate_name: syringaldehyde

enzyme: vanillin dehydrogenase

substrate: syringaldehyde


substrate_name: Vanillin

substrate: Vanillin


enzyme_display_name: pyruvate dehydrogenase (NADP+)

organism: Euglena gracilis

assay_conditions_summary: cofactor NADP+

column_label: Abstract reports Km values for pyruvate, CoA, and NADP+ were estimated to be 27, 6.6, and 28 microM, respectively.

raw_value_unit_evidence: Km raw_value=28 microM raw_unit=microM

row_label: Euglena gracilis pyruvate:NADP+ oxidoreductase / NADP+

table_label: PubMed XML abstract PMID 2508561

enzyme: pyruvate dehydrogenase (NADP+)

substrate: NADP+


substrate_name: methyl viologen

proof_lines:
methyl viologen
pyruvate:NADP+ oxidoreductase
Euglena gracilis

substrate: methyl viologen


enzyme_display_name: coniferyl-aldehyde dehydrogenase

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines:
at pH 8.8 and 26°C
at pH 8.0 and 40°C

enzyme: coniferyl-aldehyde dehydrogenase

substrate: Unknown


organism: Micrococcus sp.

proof_lines: pH 7, temperature not specified in the publication


enzyme_display_name: erythrose-4-phosphate dehydrogenase

organism: Escherichia coli

substrate_name: D-erythrose 4-phosphate

sequence_variant_note: Mutation signature H176N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

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

enzyme: erythrose-4-phosphate dehydrogenase

substrate: D-erythrose 4-phosphate


assay_conditions_summary: cofactor NAD+

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C311Y with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C311A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature M179T with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +8, so it is treated as a source-provided variant sequence.


enzyme_display_name: salicylaldehyde dehydrogenase

organism: Alteromonas naphthalenivorans

substrate_name: Salicylaldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E175A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 35°C, recombinant His-tagged mutant E175A

enzyme: salicylaldehyde dehydrogenase

substrate: Salicylaldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N149A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 35°C, recombinant His-tagged mutant N149A


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

proof_lines: pH 7.5, 35°C, recombinant His-tagged enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V153A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 35°C, recombinant His-tagged mutant V153A


assay_conditions_summary: pH 7.5; cofactor NAD+


enzyme_display_name: Vanillin dehydrogenase

substrate_name: vanillin in the presence of 0.5 mM NAD(+) (at pH 7.0)

assay_conditions_summary: pH 7; cofactor NADP+

enzyme: Vanillin dehydrogenase


substrate_name: 3,4-dihydroxybenzaldehyde in the presence of 0.5 mM NAD(+) (at pH 7.0)


substrate_name: 4-hydroxybenzaldehyde in the presence of 0.5 mM NAD(+) (at pH 7.0)


substrate_name: NAD(+) in the presence of 1 mM vanillin

substrate: NAD(+) in the presence of 1 mM vanillin


substrate_name: NADP(+) in the presence of 1 mM vanillin


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


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M179T with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8.9; 298.15 K; cofactor NAD+

column_label: Table II row Wild-type GapB-encoded protein / NAD+ (E4PDH activity): kcat cell 20 s^-1; KM cell 0.8 mM; no kcat/KM column/cell is printed, so kcat_over_km 25.0 s^-1 mM^-1 is the quotient 20 / 0.8 of the two printed cells.

normalized_value_unit_evidence: kcat 20 s^-1; Km 0.8 mM; kcat/Km derived as 20 / 0.8 = 25.0 s^-1 mM^-1 from the two printed component cells; the paper prints no kcat/KM value.

raw_value_unit_evidence: Table II row Wild-type GapB-encoded protein / NAD+ (E4PDH activity): kcat=20 s^-1; km=0.8 mM; kcat_over_km=not explicitly reported.

row_label: Wild-type GapB-encoded protein | NAD+ (E4PDH activity)

table_label: Table II. Kinetic parameters of wild-type and mutants of GapB-encoded protein, and wild-type and mutant of B. stearothermophilus GAPDH


organism: Escherichia coli (strain K12)

substrate_name: decanal

smiles: CCCCCCCCCC=O

substrate: decanal


substrate_name: NAD (at pH 8.5)

substrate: NAD (at pH 8.5)


substrate_name: succinic semialdehyde (at pH 8.5)

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

substrate: succinic semialdehyde (at pH 8.5)


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E175A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 308.15 K; cofactor NAD+

normalized_value_unit_evidence: Km normalized 0.1056 mM; kcat normalized 157.6 s^-1; kcat/Km normalized from exact kcat/Km columns as 1492.4242424242423 s^-1 mM^-1; printed kcat/Km column rounds to 1500 s^-1 mM^-1.

row_label: E175A; NAD+

table_label: Table 2. Apparent kinetic parameters of the wild-type and mutant SALDan enzymes.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N149A to reconstruct the assayed variant sequence.


column_label: Public PMC HTML Table 2, row WT / NAD+, gives App Km 39.5 +/- 3.2 uM, App kcat 234.3 +/- 24.2 s^-1, and App kcat/Km 5.9 +/- 0.5 s^-1 uM^-1. The catalog value is the exact quotient of the same row's exact central kcat and Km cells; the paper's independently printed efficiency column is rounded and concordant.

normalized_value_unit_evidence: Km=0.0395 mM; kcat=234.3 s^-1; exact same-row kcat/Km=234.3/0.0395=5931.645569620254 s^-1*mM^-1; the independently printed rounded efficiency is 5900 s^-1*mM^-1.

row_label: WT; NAD+


column_label: PMC HTML Table 2 row E175A / SALD has columns App Km (uM)=15.1 +/- 2.6, App kcat (s^-1)=82.2 +/- 10.1, App kcat/Km (s^-1 uM^-1)=5.4 +/- 0.9.

normalized_value_unit_evidence: Km normalized 0.0151 mM; kcat normalized 82.2 s^-1; kcat/Km normalized from exact kcat/Km columns as 5443.7086092715235 s^-1 mM^-1; printed kcat/Km column rounds to 5400 s^-1 mM^-1.

row_label: E175A; SALD


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V153A to reconstruct the assayed variant sequence.


column_label: Public PMC HTML Table 2, row WT / SALD, gives App Km 3.8 +/- 0.5 uM, App kcat 123.6 +/- 13.6 s^-1, and App kcat/Km 32.5 +/- 4.2 s^-1 uM^-1. The catalog value is the exact quotient of the same row's exact central kcat and Km cells; the paper's independently printed efficiency column is rounded and concordant.

normalized_value_unit_evidence: Km=0.0038 mM; kcat=123.6 s^-1; exact same-row kcat/Km=123.6/0.0038=32526.315789473683 s^-1*mM^-1; the independently printed rounded efficiency is 32500 s^-1*mM^-1.

row_label: WT; SALD


enzyme_display_name: fluoroacetaldehyde dehydrogenase

organism: Streptantibioticus cattleyicolor

substrate_name: fluoroacetaldehyde

smiles: C(C=O)F

column_label: PMID 11571203 / PMCID PMC93250 / DOI 10.1128/AEM.67.10.4919-4921, Table 2, row Fluoroacetaldehyde, Km (uM) footnote b column = 80; normalized Km = 0.08 mM.

normalized_value_unit_evidence: Km=0.08 mM (converted from 80 uM).

raw_value_unit_evidence: Table 2 row Fluoroacetaldehyde, Km (uM) footnote b column = 80.

row_label: Fluoroacetaldehyde

table_label: Table 2: Substrate specificity of fluoroacetaldehyde dehydrogenase from S. cattleya

enzyme: fluoroacetaldehyde dehydrogenase

substrate: fluoroacetaldehyde


substrate_name: glycoaldehyde

smiles: C(C=O)O

column_label: PMID 11571203 / PMCID PMC93250 / DOI 10.1128/AEM.67.10.4919-4921, Table 2, row Glycoaldehyde, Km (uM) footnote b column = 150; normalized Km = 0.15 mM.

normalized_value_unit_evidence: Km=0.15 mM (converted from 150 uM).

raw_value_unit_evidence: Table 2 row Glycoaldehyde, Km (uM) footnote b column = 150.

row_label: Glycoaldehyde

substrate: glycoaldehyde


substrate_name: benzaldehyde

column_label: PMID 11571203 / PMCID PMC93250 / DOI 10.1128/AEM.67.10.4919-4921, Table 2, row Benzaldehyde, Km (uM) footnote b column = 320; normalized Km = 0.32 mM.

normalized_value_unit_evidence: Km=0.32 mM (converted from 320 uM).

raw_value_unit_evidence: Table 2 row Benzaldehyde, Km (uM) footnote b column = 320.

row_label: Benzaldehyde

substrate: benzaldehyde


substrate_name: acetaldehyde

column_label: PMID 11571203 / PMCID PMC93250 / DOI 10.1128/AEM.67.10.4919-4921, Table 2, row Acetaldehyde, Km (uM) footnote b column = 810; normalized Km = 0.81 mM.

normalized_value_unit_evidence: Km=0.81 mM (converted from 810 uM).

raw_value_unit_evidence: Table 2 row Acetaldehyde, Km (uM) footnote b column = 810.

row_label: Acetaldehyde

substrate: acetaldehyde


organism: Bacillus subtilis

assay_conditions_summary: pH 9.2; 298.15 K; cofactor NAD+


substrate_name: NADP+

assay_conditions_summary: pH 9.2; 298.15 K; cofactor NADP+


substrate_name: D-Erythrose

assay_conditions_summary: pH 8.9; 298.15 K; cofactor NADH

column_label: Results main text, JBC page 15110, sentence on the catalytic efficiency of the GapB-encoded protein tested with erythrose; Wild-type GapB-encoded protein / erythrose: kcat 0.36 s^-1; KM 90 mM; no kcat/KM value is printed, so kcat_over_km 0.004 s^-1 mM^-1 is the quotient 0.36 / 90 of the two printed prose values.

normalized_value_unit_evidence: kcat 0.36 s^-1; Km 90 mM; kcat/Km derived as 0.36 / 90 = 0.004 s^-1 mM^-1 from the two printed prose values; the paper prints no kcat/KM value.

raw_value_unit_evidence: Results main text, JBC page 15110, sentence on the catalytic efficiency of the GapB-encoded protein tested with erythrose; Wild-type GapB-encoded protein / erythrose: kcat=0.36 s^-1; km=90 mM; kcat_over_km=0.004 s^-1 mM^-1 derived as the quotient 0.36 / 90 s^-1 / mM; no kcat/KM value is printed in the paper.

substrate: D-Erythrose


substrate_name: D-Erythrose 4-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C311A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

substrate: D-Erythrose 4-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C311Y with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


column_label: Table II row Wild-type GapB-encoded protein / D-Erythrose 4-phosphate (E4PDH activity): kcat cell 20 s^-1; KM cell 0.51 mM; no kcat/KM column/cell is printed, so kcat_over_km 39.21568627450981 s^-1 mM^-1 is the quotient 20 / 0.51 of the two printed cells.

normalized_value_unit_evidence: kcat 20 s^-1; Km 0.51 mM; kcat/Km derived as 20 / 0.51 = 39.21568627450981 s^-1 mM^-1 from the two printed component cells; the paper prints no kcat/KM value.

raw_value_unit_evidence: Table II row Wild-type GapB-encoded protein / D-Erythrose 4-phosphate (E4PDH activity): kcat=20 s^-1; km=0.51 mM; kcat_over_km=not explicitly reported.

row_label: Wild-type GapB-encoded protein | D-Erythrose 4-phosphate (E4PDH activity)


substrate_name: NAD(+)

column_label: Abstract states apparent Km values for NAD and CHMS were 19.5 +/- 2.7 microM and 9.2 +/- 1.4 microM, respectively, for the E. coli enzyme.

raw_value_unit_evidence: Km raw_value=19.5 microM raw_unit=microM

row_label: E. coli CHMS dehydrogenase / NAD

table_label: PubMed XML abstract

substrate: NAD(+)


raw_value_unit_evidence: Km raw_value=9.2 microM raw_unit=microM

row_label: E. coli CHMS dehydrogenase / CHMS


organism: Pyrococcus woesei

substrate_name: phosphate

column_label: Scanned Table 2 row Phosphate reports Km (mM) of enzyme from P. woesei = 40.

raw_value_unit_evidence: Km raw_value=40 raw_unit=mM

row_label: Phosphate

table_label: PMC213258 scanned Table 2, Kinetic properties of P. woesei glyceraldehyde-3-phosphate dehydrogenase from original organism and transformed E. coli cells

substrate: phosphate


substrate_name: NADP(+)

column_label: Scanned Table 2 row NADP+ reports Km (mM) of enzyme from P. woesei = 0.01.

raw_value_unit_evidence: Km raw_value=0.01 raw_unit=mM

row_label: NADP+

substrate: NADP(+)


substrate_name: D-erythrose 4-phosphate

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

assay_conditions_summary: pH 8.6; cofactor NAD+

column_label: PDF text lines 29-31 and 402-409; page 1 abstract and page 6 Results prose name Kmapp(E4P) and kcatapp for E4P.

raw_value_unit_evidence: Abstract reports Kmapp(E4P) = 0.96 mM and kcatapp(E4P) = 200 s^-1; Results reports Kmapp(E4P) = 0.96 +/- 0.13 mM and kcatapp = 200 s^-1.

row_label: D-erythrose 4-phosphate; purified gapB/epd E4PDH

table_label: Abstract and Results prose: kinetic parameters of purified E4PDH


substrate_name: D-erythrose 4-phosphate (at 25 degrees Celsius and pH 8.9)


enzyme_display_name: Glutamyl-tRNA reductase

substrate_name: NADPH

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

enzyme: Glutamyl-tRNA reductase

substrate: NADPH


enzyme_display_name: Pyruvate dehydrogenase [NADP(+)], mitochondrial

column_label: Results text, NADP+ as third listed substrate/cofactor: 30 uM.

raw_value_unit_evidence: Apparent Km values for pyruvate, CoA, and NADP+ were 210, 8, and 30 uM, respectively.

row_label: Pyruvate:NADP+ oxidoreductase substrate/cofactor profile

table_label: Results text: kinetic profiles

data_origin: curated


enzyme_display_name: glutamyl-tRNA reductase

assay_conditions_summary: pH 8.1; 310.15 K; cofactor NADPH

enzyme: glutamyl-tRNA reductase


organism: Geobacillus stearothermophilus

column_label: Table II row Wild-type B. stearothermophilus GAPDH / D-Erythrose 4-phosphate (E4PDH activity): kcat cell 0.1 s^-1; KM cell 3.3 mM; no kcat/KM column/cell is printed, so kcat_over_km 0.030303030303030307 s^-1 mM^-1 is the quotient 0.1 / 3.3 of the two printed cells.

normalized_value_unit_evidence: kcat 0.1 s^-1; Km 3.3 mM; kcat/Km derived as 0.1 / 3.3 = 0.030303030303030307 s^-1 mM^-1 from the two printed component cells; the paper prints no kcat/KM value.

raw_value_unit_evidence: Table II row Wild-type B. stearothermophilus GAPDH / D-Erythrose 4-phosphate (E4PDH activity): kcat=0.1 s^-1; km=3.3 mM; kcat_over_km=not explicitly reported.

row_label: Wild-type B. stearothermophilus GAPDH | D-Erythrose 4-phosphate (E4PDH activity)


column_label: Table II row Wild-type B. stearothermophilus GAPDH / NAD+ (E4PDH activity): kcat cell 0.1 s^-1; KM cell 0.08 mM; no kcat/KM column/cell is printed, so kcat_over_km 1.25 s^-1 mM^-1 is the quotient 0.1 / 0.08 of the two printed cells.

normalized_value_unit_evidence: kcat 0.1 s^-1; Km 0.08 mM; kcat/Km derived as 0.1 / 0.08 = 1.25 s^-1 mM^-1 from the two printed component cells; the paper prints no kcat/KM value.

raw_value_unit_evidence: Table II row Wild-type B. stearothermophilus GAPDH / NAD+ (E4PDH activity): kcat=0.1 s^-1; km=0.08 mM; kcat_over_km=not explicitly reported.

row_label: Wild-type B. stearothermophilus GAPDH | NAD+ (E4PDH activity)


enzyme_display_name: D-erythrose-4-phosphate dehydrogenase

substrate_name: glyceraldehyde 3-phosphate (at 25 degrees Celsius and pH 8.9)

enzyme: D-erythrose-4-phosphate dehydrogenase


organism: Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NBRC 12016 / NCIMB 10680 / K1)

substrate_name: succinate semialdehyde

substrate: succinate semialdehyde


enzyme_display_name: UniProt Q13WK4

organism: Paraburkholderia xenovorans

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q13WK4

substrate: NADP+

source: skid


substrate_name: propionaldehyde

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

substrate: propionaldehyde


substrate_name: Isovaleraldehyde

smiles: CC(C)CC=O

substrate: Isovaleraldehyde


substrate_name: heptaldehyde

smiles: CCCCCCC=O

substrate: heptaldehyde


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: benzaldehyde


substrate_name: Valeraldehyde

smiles: CCCCC=O

substrate: Valeraldehyde


substrate_name: NAD+

substrate: NAD+


enzyme_display_name: UniProt A9SS48

organism: Physcomitrium patens

enzyme: UniProt A9SS48


substrate_name: NADP+


substrate_name: Glutaric semialdehyde

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

substrate: Glutaric semialdehyde


enzyme_display_name: Aminoaldehyde dehydrogenase 1a

organism: Zea mays

substrate_name: betaine aldehyde

enzyme: Aminoaldehyde dehydrogenase 1a

substrate: betaine aldehyde


enzyme_display_name: retinal dehydrogenase

organism: Rattus norvegicus

substrate_name: all-trans-retinal

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

proof_lines: cellular retinol-binding protein-bound retinal has lower Km of 0.0002 mM

proof_lines: retinal bovine serum albumin, Km is 25 times lower than the Km for acetaldehyde

enzyme: retinal dehydrogenase

substrate: all-trans-retinal


substrate_name: citral

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

substrate: citral


smiles: CCCCCC=CC=CC=O


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: decanal

smiles: CCCCCCCCC=O

substrate: decanal


organism: Homo sapiens

substrate_name: 3-phospho-D-glyceroyl phosphate

assay_conditions_summary: pH 7

proof_lines:
enzyme form E6.8, pH 7
enzyme form E9.0, pH 9
enzyme form E8.5, pH 9

substrate: 3-phospho-D-glyceroyl phosphate


assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+

proof_lines:
enzyme form E8.5, pH 9
pH 8.5, 25°C
enzyme form E9.0, pH 9


substrate_name: 1,3-diphosphoglyceric acid

assay_conditions_summary: pH 7; cofactor NAD+

proof_lines:
enzyme form E6.6, pH 7
enzyme form E8.5, pH 7
enzyme form E9.0, pH 7

substrate: 1,3-diphosphoglyceric acid


substrate_name: DL-glyceraldehyde

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

substrate: DL-glyceraldehyde


substrate_name: erythrose 4-phosphate

proof_lines:
enzyme form E8.5, pH 7
enzyme form E9.0, pH 7

substrate: erythrose 4-phosphate


enzyme_display_name: sulfoacetaldehyde dehydrogenase

organism: Rhodopseudomonas palustris

enzyme: sulfoacetaldehyde dehydrogenase


assay_conditions_summary: pH 9; 295.15 K; cofactor NAD+


assay_conditions_summary: pH 9; 295.15 K; cofactor NADP+

substrate: NADP+


enzyme_display_name: 2-formylbenzoate dehydrogenase

organism: Alcaligenes faecalis

enzyme: 2-formylbenzoate dehydrogenase


assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+


organism: Euglena gracilis

assay_conditions_summary: pH 8.7; 308.15 K; cofactor NADP+


substrate_name: succinate semialdehyde

substrate: succinate semialdehyde


enzyme_display_name: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+)

substrate_name: propionaldehyde

sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_batch:Q13WK4 and applied mutation signature H485A to reconstruct the assayed variant sequence.

smiles: CCC=O

assay_conditions_summary: pH 7.5; cofactor NADP+

column_label: Figure 1B; H485A_ALDHC row; kcat (min^-1) column; raw value 5.75 +/- 0.31 min^-1.

raw_value_unit_evidence: Figure 1B reports kcat = 5.75 +/- 0.31 min^-1.

row_label: H485A_ALDHC row

table_label: PMID 21495107, Figure 1B: kcat values for native and mutant ALDHC

substrate: propionaldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K168A to reconstruct the assayed variant sequence.

proof_lines: K168A mutant enzyme, pH 7.5, temperature not specified in the publication

enzyme: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E400A to reconstruct the assayed variant sequence.

proof_lines: E400A mutant enzyme, pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_batch:Q13WK4 and applied mutation signature E496A to reconstruct the assayed variant sequence.

column_label: Figure 1B; E496A_ALDHC row; kcat (min^-1) column; raw value 16.2 +/- 0.77 min^-1.

normalized_value_unit_evidence: 16.2 +/- 0.77 min^-1 normalized to 0.27 s^-1; exported row is 16.2 s^-1.

raw_value_unit_evidence: Figure 1B reports kcat = 16.2 +/- 0.77 min^-1.

row_label: E496A_ALDHC row


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_batch:Q13WK4 and applied mutation signature E167A to reconstruct the assayed variant sequence.

column_label: Figure 1B; E167A_ALDHC row; kcat (min^-1) column; raw value 36.8 +/- 1.6 min^-1.

raw_value_unit_evidence: Figure 1B reports kcat = 36.8 +/- 1.6 min^-1.

row_label: E167A_ALDHC row


column_label: Figure 1B; Native_ALDHC row; kcat (min^-1) column; raw value 162 +/- 6.2 min^-1.

normalized_value_unit_evidence: 162 +/- 6.2 min^-1 normalized to 2.7 s^-1; exported row is 162.0 s^-1.

raw_value_unit_evidence: Figure 1B reports kcat = 162 +/- 6.2 min^-1.

row_label: Native_ALDHC row


organism: Mycobacterium tuberculosis

substrate_name: Succinate semialdehyde; H2O; NADP+

assay_conditions_summary: cofactor NADP+

substrate: Succinate semialdehyde; H2O; NADP+


substrate_name: NAD+; H2O; Succinate semialdehyde

assay_conditions_summary: cofactor NAD+

substrate: NAD+; H2O; Succinate semialdehyde


enzyme_display_name: UniProt B1XMM6

organism: Synechococcus sp.

assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADP+

enzyme: UniProt B1XMM6


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

assay_conditions_summary: pH 8.2; 298.15 K; cofactor NADP+

proof_lines: recombinant mutant R121A, pH 8.2, 25°C, with NADP+


proof_lines: recombinant mutant R457A, pH 8.2, 25°C, with NADP+


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

proof_lines: recombinant wild-type enzyme, pH 8.2, 25°C, with NADP+


sequence_variant_note: Resolved canonical sequence from pdb_accession and applied mutation signature R228A with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.2; 298.15 K; cofactor NAD+

proof_lines: recombinant mutant R228A, pH 8.2, 25°C, with succinate semialdehyde


proof_lines: recombinant wild-type enzyme, pH 8.2, 25°C, with succinate semialdehyde


proof_lines: recombinant mutant R228A, pH 8.2, 25°C, with NADP+


proof_lines: recombinant mutant Y296A, pH 8.2, 25°C, with NADP+


sequence_variant_note: Resolved canonical sequence from pdb_accession and applied mutation signature N175A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant N175A, pH 8.2, 25°C, with NADP+


organism: Nostoc sp. PCC 7120 = FACHB-418

assay_conditions_summary: pH 9.5; cofactor NADP+

proof_lines: pH 9.5, 25°C, recombinant wild-type enzyme


assay_conditions_summary: pH 9.5; cofactor NAD+


substrate_name: benzaldehyde

substrate: benzaldehyde


proof_lines: in 50 mM Tris-HCl (pH 7.5), at 25°C, cosubstrate: propionaldehyde


substrate_name: formaldehyde

substrate: formaldehyde


substrate_name: Isovaleraldehyde

substrate: Isovaleraldehyde


substrate_name: NAD+

assay_conditions_summary: pH 7.5; cofactor NAD+

substrate: NAD+


substrate_name: Valeraldehyde

substrate: Valeraldehyde


substrate_name: heptaldehyde

substrate: heptaldehyde


enzyme_display_name: malonyl-CoA reductase (malonate semialdehyde-forming)

organism: Chloroflexus aurantiacus

substrate_name: NADPH

assay_conditions_summary: pH 7.8; cofactor NADPH

proof_lines: isolated C-terminal fragment, pH 7.8, 57°C

substrate: NADPH


organism: Saccharolobus solfataricus

substrate_name: NADP+

assay_conditions_summary: pH 6.5; cofactor NADP+

column_label: Table 2: SSADH-II with NADP+ as cosubstrate, row NADP+: Km=0.01 mM; kcat=16.5 s^-1; kcat/Km=3066.4 mM^-1 s^-1


column_label: Table 2: SSADH-II with NADP+ as cosubstrate, row Succinic semialdehyde (C4): Km=0.004 mM; kcat=18.4 s^-1; kcat/Km=3454.2 mM^-1 s^-1

row_label: Succinic semialdehyde (C4)


column_label: Table 3: SSADH-II with NAD+ as cosubstrate, row a-Ketoglutaric semialdehyde (C5): Km=0.1 mM; kcat=27.3 s^-1; kcat/Km=215.3 mM^-1 s^-1

row_label: a-Ketoglutaric semialdehyde (C5)


assay_conditions_summary: pH 6.5; cofactor NAD+

column_label: Table 3: SSADH-II with NAD+ as cosubstrate, row NAD+: Km=11.1 mM; kcat=136.3 s^-1; kcat/Km=12.3 mM^-1 s^-1

row_label: NAD+


substrate_name: malonyl-CoA

protein_accession_database: NCBI Protein

assay_conditions_summary: pH 7.8; cofactor CoA

enzyme: malonyl-CoA reductase (malonate semialdehyde-forming)

substrate: malonyl-CoA


organism: Cryptosporidium parvum

substrate_name: hexacosanoyl-CoA

assay_conditions_summary: pH 7.2; cofactor CoA

proof_lines: pH 7.2, temperature not specified in the publication

substrate: hexacosanoyl-CoA


organism: Arabidopsis thaliana

substrate_name: hexadecanoyl-[acyl-carrier protein]

substrate: hexadecanoyl-[acyl-carrier protein]


organism: Nocardioides sp.

assay_conditions_summary: pH 9.4; cofactor NAD+

proof_lines: kcat is 39 sec(-1) with 2-carboxybenzaldehyde as substrate. kcat is 32 sec(-1) with NAD as substrate.


organism: Synechocystis sp. PCC 6803

proof_lines: pH 9.7, 45°C, recombinant detagged enzyme


assay_conditions_summary: pH 9.7; 318.15 K; cofactor NADP+


enzyme_display_name: Succinate-semialdehyde dehydrogenase [NADP(+)] GabD

organism: Escherichia coli (strain K12)

proof_lines: The succinate-semialdehyde dehydrogenase activity measured in the presence of NADP(+) is approximately 20-fold higher than that measured in the presence of NAD(+).


organism: Physcomitrium patens

substrate_name: Glutaric semialdehyde

smiles: O=CCCCCC(=O)O

assay_conditions_summary: pH 8.2; 298.15 K; buffer pH 8; cofactor NADP+

column_label: Table 1; row WT-PpALDH21 under GRSAL (NADP+); Km, kcat, and kcat/Km columns.

normalized_value_unit_evidence: Km paper=0.551 mM; kcat paper=0.27 s^-1; kcat/Km paper=0.5 s^-1 mM^-1.

row_label: WT-PpALDH21; GRSAL (NADP+)

table_label: Table 1. Kinetic parameters for WT-PpALDH21 and mutant variants with two coenzymes and two best substrates

substrate: Glutaric semialdehyde


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R228A with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.


column_label: Table 1, NAD+ (SSAL) group, WT-PpALDH21 row reports K_m 5370 +/- 140, kcat 3.3 +/- 0.1, and kcat/K_m 6.2 +/- 0.2 x 10^2.

row_label: NAD+ (SSAL) / WT-PpALDH21

table_label: Table 1


column_label: Table 1; row WT-PpALDH21 under NADP+ (SSAL); Km, kcat, and kcat/Km columns.

normalized_value_unit_evidence: Km paper=0.024 mM; kcat paper=15.2 s^-1; kcat/Km paper=630.0 s^-1 mM^-1.

row_label: WT-PpALDH21; NADP+ (SSAL)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N175A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

smiles: O=CCCC(=O)O


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A9SS48 and applied mutation signature R121A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for WT-PpALDH21 and mutant variants with two coenzymes and two best substrates), SSAL (NADP+) block, enzyme row R121A; column Km (uM) = 268 ± 10; column kcat (sec^-1) = 0.02 ± 0.01; column kcat/Km (sec^-1 M^-1) = 8.8 ± 0.7 x 10^1.

normalized_value_unit_evidence: Km: printed Table 1 cell 268 uM; 268 / 1000 = 0.268 mM. kcat: printed Table 1 cell 0.02 s^-1; already in s^-1, no unit conversion applies. kcat/Km: printed Table 1 cell 8.8 x 10^1 s^-1 M^-1 = 88.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 88.0 / 1000 = 0.088 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, SSAL (NADP+) block, enzyme row R121A: Km = 268 ± 10 uM; kcat = 0.02 ± 0.01 s^-1; printed kcat/Km = 8.8 ± 0.7 x 10^1 s^-1 M^-1 (the printed column heads read Km (µM), kcat (sec^-1) and kcat/Km (sec^-1 M^-1)).

table_label: Table 1: Kinetic parameters for WT-PpALDH21 and mutant variants with two coenzymes and two best substrates (The Plant Journal 2017, 92:229-243)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A9SS48 and applied mutation signature R457A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for WT-PpALDH21 and mutant variants with two coenzymes and two best substrates), SSAL (NADP+) block, enzyme row R457A; column Km (uM) = 135 ± 7; column kcat (sec^-1) = 0.02 ± 0.01; column kcat/Km (sec^-1 M^-1) = 1.8 ± 0.2 x 10^2.

normalized_value_unit_evidence: Km: printed Table 1 cell 135 uM; 135 / 1000 = 0.135 mM. kcat: printed Table 1 cell 0.02 s^-1; already in s^-1, no unit conversion applies. kcat/Km: printed Table 1 cell 1.8 x 10^2 s^-1 M^-1 = 180.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 180.0 / 1000 = 0.18 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, SSAL (NADP+) block, enzyme row R457A: Km = 135 ± 7 uM; kcat = 0.02 ± 0.01 s^-1; printed kcat/Km = 1.8 ± 0.2 x 10^2 s^-1 M^-1 (the printed column heads read Km (µM), kcat (sec^-1) and kcat/Km (sec^-1 M^-1)).


column_label: Table 1; row WT-PpALDH21 under SSAL (NADP+); Km, kcat, and kcat/Km columns.

normalized_value_unit_evidence: Km paper=0.181 mM; kcat paper=15.8 s^-1; kcat/Km paper=87.0 s^-1 mM^-1.

row_label: WT-PpALDH21; SSAL (NADP+)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y296A to reconstruct the assayed variant sequence.


organism: Clostridium kluyveri

substrate_name: coenzyme A

assay_conditions_summary: pH 8.5; cofactor CoA

substrate: coenzyme A


substrate_name: succinyl-CoA

assay_conditions_summary: pH 7; cofactor CoA

column_label: Table 3 Km mM column; direction Forward; substrate succinyl-CoA; value 3.2 (+/- 0.6) x 10^-3

raw_value_unit_evidence: Table 3 forward row succinyl-CoA Km = 3.2 (+/- 0.6) x 10^-3 mM

row_label: Forward row succinyl-CoA

table_label: Wiley PDF page 126 Table 3. Kinetic values for succinate-semialdehyde dehydrogenase

substrate: succinyl-CoA


assay_conditions_summary: pH 8.5; cofactor NADP+

column_label: Table 3 Km mM column; direction Reverse; substrate NADP+; value 4.0 (+/- 1.7) x 10^-3

raw_value_unit_evidence: Table 3 reverse row NADP+ Km = 4.0 (+/- 1.7) x 10^-3 mM

row_label: Reverse row NADP+

substrate: NADP+


assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 3 Km mM column; direction Forward; substrate NADPH; value 4.3 (+/- 1.3) x 10^-3

raw_value_unit_evidence: Table 3 forward row NADPH Km = 4.3 (+/- 1.3) x 10^-3 mM

row_label: Forward row NADPH


enzyme_display_name: Malonyl-CoA reductase

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

substrate_name: NADP (with 0.2 mM malonyl-CoA)

assay_conditions_summary: cofactor NADPH

column_label: Full-text properties paragraph maps NADPH to 25 uM Km for recombinant S. tokodaii enzyme

raw_value_unit_evidence: Km raw_value=25 raw_unit=uM

row_label: Sulfolobus tokodaii recombinant malonyl-CoA reductase NADPH item

table_label: PMID 17041055 PMC full text

enzyme: Malonyl-CoA reductase

substrate: NADP (with 0.2 mM malonyl-CoA)


substrate_name: malonyl-CoA (with 0.5 mM NADP)

assay_conditions_summary: cofactor CoA

column_label: Full-text properties paragraph maps malonyl-CoA to 40 uM Km for recombinant S. tokodaii enzyme

raw_value_unit_evidence: Km raw_value=40 raw_unit=uM

row_label: Sulfolobus tokodaii recombinant malonyl-CoA reductase malonyl-CoA item

substrate: malonyl-CoA (with 0.5 mM NADP)


organism: Listeria monocytogenes

substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


organism: Streptomyces coelicolor


enzyme_display_name: UniProt A0A2H4PMI3

organism: Zea mays

enzyme: UniProt A0A2H4PMI3


substrate_name: D-glyceraldehyde 3-phosphate

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

substrate: D-glyceraldehyde 3-phosphate


substrate_name: 2-aminoadipic semialdehyde

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

substrate: 2-aminoadipic semialdehyde


substrate_name: L-glutamate 5-semialdehyde

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

substrate: L-glutamate 5-semialdehyde


enzyme_display_name: UniProt P09546

organism: Escherichia coli

enzyme: UniProt P09546


substrate_name: NAD+

substrate: NAD+


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

column_label: Table 1, row NADP+ with fixed substrate concentration 50 uM and [Mg2+] 10 mM, columns kcat (s^-1), Km (uM), and kcat/K (M^-1 s^-1), cells 2.7 +/- 0.1, 9.2 +/- 1.0, and (2.9 +/- 0.1) x 10^5.

normalized_value_unit_evidence: kcat 2.7 s^-1; Km 9.2 uM = 0.0092 mM; kcat/K 2.9 x 10^5 M^-1 s^-1 = 290 s^-1 mM^-1. Current export mixes this kcat with Km 0.0613 mM and kcat/K 44.045676998368684 s^-1 mM^-1 from a different condition.

row_label: NADP+, fixed substrate concentration 50 uM, [Mg2+] 10 mM

table_label: Table 1: Steady-State Kinetic Parameters for GabD1


substrate_name: Succinic semialdehyde

column_label: Table 1, row SSA with fixed substrate concentration 200 uM and [Mg2+] 10 mM, columns kcat (s^-1), Km (uM), and kcat/K (M^-1 s^-1), cells 4.7 +/- 0.1, 3.0 +/- 0.2, and (1.6 +/- 0.1) x 10^6.

normalized_value_unit_evidence: kcat 4.7 s^-1; Km 3.0 uM = 0.003 mM; kcat/K 1.6 x 10^6 M^-1 s^-1 = 1600 s^-1 mM^-1. Current export mixes this kcat with Km 0.0133 mM and kcat/K 353.3834586466166 s^-1 mM^-1 from a different condition.

row_label: SSA, fixed substrate concentration 200 uM, [Mg2+] 10 mM

substrate: Succinic semialdehyde


organism: Streptococcus pyogenes

assay_conditions_summary: pH 7; 303.15 K; cofactor NAD+

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.


assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+

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: Acinetobacter baumannii

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


substrate_name: succinate semialdehyde

substrate: succinate semialdehyde


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

assay_conditions_summary: pH 6.5; 343.15 K; cofactor NADP+

column_label: Tables 2 and 3: SSADH-II NADP+/NAD+ rows, row a-Ketoglutaric semialdehyde (C5): Km=0.1 or 0.2 mM; kcat=27.3 or 21.2 s^-1; kcat/Km=215.3 or 134.1 mM^-1 s^-1


assay_conditions_summary: pH 6.5; 343.15 K; cofactor NAD+

column_label: Table 3: SSADH-II with NAD+ as cosubstrate, row NAD+: Km=11.1 mM; kcat=136.3 s^-1; kcat/Km=12.3 mM^-1 s^-1


substrate_name: NADP+


column_label: Table 2: SSADH-II with NADP+ as cosubstrate, row Succinic semialdehyde (C4): Km=0.004 mM; kcat=18.4 s^-1; kcat/Km=3454.2 mM^-1 s^-1


organism: Neptuniibacter caesariensis

assay_conditions_summary: pH 9; cofactor NAD+


substrate_name: Sulfoacetaldehyde

assay_conditions_summary: pH 9

substrate: Sulfoacetaldehyde


assay_conditions_summary: pH 9; cofactor NADP+


organism: Aromatoleum evansii

substrate_name: 3,4-dehydroadipyl-CoA semialdehyde

assay_conditions_summary: pH 7.2; cofactor CoA

substrate: 3,4-dehydroadipyl-CoA semialdehyde


assay_conditions_summary: pH 7.2; cofactor NADP+


enzyme_display_name: geranial dehydrogenase

organism: Persicaria minor

assay_conditions_summary: pH 9.5; 308.15 K; cofactor NAD+

proof_lines: isoform citral dehydrogenase II, at pH 9.5 and 35°C

proof_lines: isoform citral dehydrogenase I, at pH 9.5 and 35°C

enzyme: geranial dehydrogenase


substrate_name: citral

substrate: citral


substrate_name: trans-cinnamaldehyde

substrate: trans-cinnamaldehyde


substrate_name: alpha-methyl cinnamaldehyde

substrate: alpha-methyl cinnamaldehyde


substrate_name: S-perillyl aldehyde

substrate: S-perillyl aldehyde


enzyme_display_name: malonyl CoA reductase (malonate semialdehyde-forming)

organism: Chloroflexus aurantiacus

substrate_name: NADPH

substrate: NADPH


organism: Hyalomma dromedarii

substrate_name: D-glucose

substrate: D-glucose


assay_conditions_summary: cofactor NADP+

proof_lines:
isoform B, with NADP+
isoform B, with NAD+
isoform A, with NADP+


proof_lines:
isoform A
isoform B


substrate_name: p-nitrobenzaldehyde

substrate: p-nitrobenzaldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


assay_conditions_summary: cofactor NAD+


substrate_name: formaldehyde

substrate: formaldehyde


substrate: NADP+


substrate_name: glyoxylic acid

substrate: glyoxylic acid


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


organism: Solanum tuberosum


substrate_name: NAD+

substrate: NAD+


substrate_name: 2-aminoadipic semialdehyde

proof_lines: pH 7.5, 30°C, recombinant wild-type enzyme

substrate: 2-aminoadipic semialdehyde


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADP+


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+


substrate_name: Glutaric semialdehyde

substrate: Glutaric semialdehyde


substrate_name: L-glutamate 5-semialdehyde

substrate: L-glutamate 5-semialdehyde


substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.15; 303.15 K; cofactor CoA

substrate: acetyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


organism: Oryza sativa

substrate_name: NADP+

assay_conditions_summary: pH 7.5; 308.15 K; cofactor NADP+


assay_conditions_summary: pH 7.5; 308.15 K; cofactor NAD+


proof_lines:
cosubstrate NADP+, pH 7.5, 35°C
cosubstrate NAD+, pH 7.5, 35°C


organism: Klebsiella pneumoniae


organism: Nicotiana plumbaginifolia

proof_lines:
isoform I
isoform II


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A2H4PMI3 and applied mutation signature F505A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer 100 mM sodium pyrophosphate; cofactor NAD+

column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GSAL block, enzyme row F505A: Km (uM) = 170; kcat (s^-1) = 0.03; kcat/Km (s^-1 M^-1) = 1.9 x 10^2.

normalized_value_unit_evidence: Km: printed cell 170 uM; 1 uM is 1/1000 mM, so 170 / 1000 = 0.17 mM. kcat: printed cell 0.03 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.03 s^(-1). kcat/Km: printed cell 1.9 x 10^2 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 190 / 1000 = 0.19 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.03 / 0.17 = 0.1764705882352941 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.19 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GSAL block, enzyme row F505A: Km = 170 uM; kcat = 0.03 s^-1; printed kcat/Km = 1.9 x 10^2 s^-1 M^-1.

row_label: Table 2, GSAL block, enzyme row F505A

table_label: Table 2. Kinetic parameters for ZmALDH12 active-site mutant variants. (J Mol Biol 2019, 431(3):576-592); printed column heads Enzyme | Km (uM) | kcat (s^-1) | kcat/Km (s^-1 M^-1), GSAL block


assay_conditions_summary: pH 7.5; buffer 3.0 mM NAD+ in 100 mM pyrophosphate; cofactor NAD+

column_label: The literal ZmALDH12 AASAL row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the independently printed efficiency is retained separately and is not substituted.

normalized_value_unit_evidence: Km=0.173 mM; kcat=0.04 s^-1; current same-row quotient=0.23121387283236997 s^-1 mM^-1; printed efficiency=0.2 s^-1 mM^-1; printed cell is preserved separately.

raw_value_unit_evidence: AASAL cells: Km 173 ± 12 μM; kcat 0.04 ± 0.02 s^-1; printed kcat/Km 2.0 ± 0.2 × 10^2 s^-1 M^-1.

row_label: ZmALDH12 / AASAL

table_label: Table 1. Kinetic parameters for ZmALDH12 and PpALDH12


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A2H4PMI3 and applied mutation signature F202A to reconstruct the assayed variant sequence.

column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GSAL block, enzyme row F202A: Km (uM) = 969; kcat (s^-1) = 0.15; kcat/Km (s^-1 M^-1) = 1.5 x 10^2.

normalized_value_unit_evidence: Km: printed cell 969 uM; 1 uM is 1/1000 mM, so 969 / 1000 = 0.969 mM. kcat: printed cell 0.15 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.15 s^(-1). kcat/Km: printed cell 1.5 x 10^2 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 150 / 1000 = 0.15 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.15 / 0.969 = 0.15479876160990713 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.15 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GSAL block, enzyme row F202A: Km = 969 uM; kcat = 0.15 s^-1; printed kcat/Km = 1.5 x 10^2 s^-1 M^-1.

row_label: Table 2, GSAL block, enzyme row F202A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E205A to reconstruct the assayed variant sequence.


column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GRSAL block, enzyme row F202A: Km (uM) = 480; kcat (s^-1) = 0.21; kcat/Km (s^-1 M^-1) = 4.4 x 10^2.

normalized_value_unit_evidence: Km: printed cell 480 uM; 1 uM is 1/1000 mM, so 480 / 1000 = 0.48 mM. kcat: printed cell 0.21 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.21 s^(-1). kcat/Km: printed cell 4.4 x 10^2 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 440 / 1000 = 0.44 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.21 / 0.48 = 0.4375 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.44 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GRSAL block, enzyme row F202A: Km = 480 uM; kcat = 0.21 s^-1; printed kcat/Km = 4.4 x 10^2 s^-1 M^-1.

row_label: Table 2, GRSAL block, enzyme row F202A

table_label: Table 2. Kinetic parameters for ZmALDH12 active-site mutant variants. (J Mol Biol 2019, 431(3):576-592); printed column heads Enzyme | Km (uM) | kcat (s^-1) | kcat/Km (s^-1 M^-1), GRSAL block


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A2H4PMI3 and applied mutation signature K329A to reconstruct the assayed variant sequence.

column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GSAL block, enzyme row K329A: Km (uM) = 958; kcat (s^-1) = 0.26; kcat/Km (s^-1 M^-1) = 2.7 x 10^2.

normalized_value_unit_evidence: Km: printed cell 958 uM; 1 uM is 1/1000 mM, so 958 / 1000 = 0.958 mM. kcat: printed cell 0.26 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.26 s^(-1). kcat/Km: printed cell 2.7 x 10^2 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 270 / 1000 = 0.27 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.26 / 0.958 = 0.27139874739039666 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.27 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GSAL block, enzyme row K329A: Km = 958 uM; kcat = 0.26 s^-1; printed kcat/Km = 2.7 x 10^2 s^-1 M^-1.

row_label: Table 2, GSAL block, enzyme row K329A


column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GRSAL block, enzyme row K329A: Km (uM) = 442; kcat (s^-1) = 0.31; kcat/Km (s^-1 M^-1) = 7.0 x 10^2.

normalized_value_unit_evidence: Km: printed cell 442 uM; 1 uM is 1/1000 mM, so 442 / 1000 = 0.442 mM. kcat: printed cell 0.31 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.31 s^(-1). kcat/Km: printed cell 7.0 x 10^2 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 700 / 1000 = 0.7 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.31 / 0.442 = 0.7013574660633484 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.7 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GRSAL block, enzyme row K329A: Km = 442 uM; kcat = 0.31 s^-1; printed kcat/Km = 7.0 x 10^2 s^-1 M^-1.

row_label: Table 2, GRSAL block, enzyme row K329A


substrate_name: D-glyceraldehyde 3-phosphate

column_label: The literal ZmALDH12 D-GAP row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the independently printed efficiency is retained separately and is not substituted.

normalized_value_unit_evidence: Km=1.86 mM; kcat=0.4 s^-1; current same-row quotient=0.21505376344086022 s^-1 mM^-1; printed efficiency=0.21 s^-1 mM^-1; printed cell is preserved separately.

raw_value_unit_evidence: D-GAP cells: Km 1860 ± 99 μM; kcat 0.4 ± 0.1 s^-1; printed kcat/Km 2.1 ± 0.2 × 10^2 s^-1 M^-1.

row_label: ZmALDH12 / D-GAP

substrate: D-glyceraldehyde 3-phosphate


column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GRSAL block, enzyme row F505A: Km (uM) = 379; kcat (s^-1) = 0.52; kcat/Km (s^-1 M^-1) = 1.4 x 10^3.

normalized_value_unit_evidence: Km: printed cell 379 uM; 1 uM is 1/1000 mM, so 379 / 1000 = 0.379 mM. kcat: printed cell 0.52 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.52 s^(-1). kcat/Km: printed cell 1.4 x 10^3 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1400 / 1000 = 1.4 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.52 / 0.379 = 1.3720316622691293 s^-1 mM^-1, against the printed catalytic-efficiency cell 1.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GRSAL block, enzyme row F505A: Km = 379 uM; kcat = 0.52 s^-1; printed kcat/Km = 1.4 x 10^3 s^-1 M^-1.

row_label: Table 2, GRSAL block, enzyme row F505A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A2H4PMI3 and applied mutation signature E205A to reconstruct the assayed variant sequence.

column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GRSAL block, enzyme row E205A: Km (uM) = 32; kcat (s^-1) = 0.53; kcat/Km (s^-1 M^-1) = 1.6 x 10^4.

normalized_value_unit_evidence: Km: printed cell 32 uM; 1 uM is 1/1000 mM, so 32 / 1000 = 0.032 mM. kcat: printed cell 0.53 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.53 s^(-1). kcat/Km: printed cell 1.6 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 16000 / 1000 = 16.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.53 / 0.032 = 16.5625 s^-1 mM^-1, against the printed catalytic-efficiency cell 16.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GRSAL block, enzyme row E205A: Km = 32 uM; kcat = 0.53 s^-1; printed kcat/Km = 1.6 x 10^4 s^-1 M^-1.

row_label: Table 2, GRSAL block, enzyme row E205A


assay_conditions_summary: pH 7.5; buffer 0.3 mM sub-saturating GSAL in 100 mM pyrophosphate; cofactor NADP+

column_label: The literal ZmALDH12 NADP+ row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the independently printed efficiency is retained separately and is not substituted.

normalized_value_unit_evidence: Km=2.872 mM; kcat=0.8 s^-1; current same-row quotient=0.2785515320334262 s^-1 mM^-1; printed efficiency=0.27 s^-1 mM^-1; printed cell is preserved separately.

row_label: ZmALDH12 / NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A2H4PMI3 and applied mutation signature S331A to reconstruct the assayed variant sequence.

column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GRSAL block, enzyme row S331A: Km (uM) = 227; kcat (s^-1) = 0.89; kcat/Km (s^-1 M^-1) = 3.9 x 10^3.

normalized_value_unit_evidence: Km: printed cell 227 uM; 1 uM is 1/1000 mM, so 227 / 1000 = 0.227 mM. kcat: printed cell 0.89 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 0.89 s^(-1). kcat/Km: printed cell 3.9 x 10^3 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3900 / 1000 = 3.9 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.89 / 0.227 = 3.920704845814978 s^-1 mM^-1, against the printed catalytic-efficiency cell 3.9 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GRSAL block, enzyme row S331A: Km = 227 uM; kcat = 0.89 s^-1; printed kcat/Km = 3.9 x 10^3 s^-1 M^-1.

row_label: Table 2, GRSAL block, enzyme row S331A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A2H4PMI3 and applied mutation signature D226A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer 100 mM sodium pyrophosphate; cofactor NADP+

column_label: Table 1 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 1, ZmALDH12 D226A block, substrate row NADP+: Km (uM) = 71; kcat (s^-1) = 1.5; kcat/Km (s^-1 M^-1) = 2.1 x 10^4.

normalized_value_unit_evidence: Km: printed cell 71 uM; 1 uM is 1/1000 mM, so 71 / 1000 = 0.071 mM. kcat: printed cell 1.5 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 1.5 s^(-1). kcat/Km: printed cell 2.1 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 21000 / 1000 = 21.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.5 / 0.071 = 21.126760563380284 s^-1 mM^-1, against the printed catalytic-efficiency cell 21.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, ZmALDH12 D226A block, substrate row NADP+: Km = 71 uM; kcat = 1.5 s^-1; printed kcat/Km = 2.1 x 10^4 s^-1 M^-1.

table_label: Table 1. Kinetic parameters for ZmALDH12 and PpALDH12. (J Mol Biol 2019, 431(3):576-592); printed column heads Substrate | Km (uM) | kcat (s^-1) | kcat/Km (s^-1 M^-1), ZmALDH12 D226A block


column_label: Table 1 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 1, ZmALDH12 D226A block, substrate row NAD+: Km (uM) = 119; kcat (s^-1) = 1.7; kcat/Km (s^-1 M^-1) = 1.4 x 10^4.

normalized_value_unit_evidence: Km: printed cell 119 uM; 1 uM is 1/1000 mM, so 119 / 1000 = 0.119 mM. kcat: printed cell 1.7 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 1.7 s^(-1). kcat/Km: printed cell 1.4 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 14000 / 1000 = 14.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.7 / 0.119 = 14.285714285714286 s^-1 mM^-1, against the printed catalytic-efficiency cell 14.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, ZmALDH12 D226A block, substrate row NAD+: Km = 119 uM; kcat = 1.7 s^-1; printed kcat/Km = 1.4 x 10^4 s^-1 M^-1.


column_label: Table 2 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 2, GSAL block, enzyme row S331A: Km (uM) = 624; kcat (s^-1) = 1.83; kcat/Km (s^-1 M^-1) = 2.8 x 10^3.

normalized_value_unit_evidence: Km: printed cell 624 uM; 1 uM is 1/1000 mM, so 624 / 1000 = 0.624 mM. kcat: printed cell 1.83 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 1.83 s^(-1). kcat/Km: printed cell 2.8 x 10^3 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2800 / 1000 = 2.8 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.83 / 0.624 = 2.932692307692308 s^-1 mM^-1, against the printed catalytic-efficiency cell 2.8 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, GSAL block, enzyme row S331A: Km = 624 uM; kcat = 1.83 s^-1; printed kcat/Km = 2.8 x 10^3 s^-1 M^-1.

row_label: Table 2, GSAL block, enzyme row S331A


column_label: The literal ZmALDH12 GRSAL row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the independently printed efficiency is retained separately and is not substituted.

normalized_value_unit_evidence: Km=0.084 mM; kcat=1.9 s^-1; current same-row quotient=22.619047619047617 s^-1 mM^-1; printed efficiency=23 s^-1 mM^-1; printed cell is preserved separately.

raw_value_unit_evidence: GRSAL cells: Km 84 ± 5 μM; kcat 1.9 ± 0.2 s^-1; printed kcat/Km 2.3 ± 0.4 × 10^4 s^-1 M^-1.

row_label: ZmALDH12 / GRSAL


assay_conditions_summary: pH 7.5; buffer 0.3 mM sub-saturating GSAL in 100 mM pyrophosphate; cofactor NAD+

column_label: The literal ZmALDH12 NAD+ row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the independently printed efficiency is retained separately and is not substituted.

normalized_value_unit_evidence: Km=0.185 mM; kcat=3.1 s^-1; current same-row quotient=16.756756756756758 s^-1 mM^-1; printed efficiency=17 s^-1 mM^-1; printed cell is preserved separately.

raw_value_unit_evidence: NAD+ cells: Km 185 ± 14 μM; kcat 3.1 ± 0.1 s^-1; printed kcat/Km 1.7 ± 0.2 × 10^4 s^-1 M^-1.

row_label: ZmALDH12 / NAD+


column_label: Table 1 prints the three column heads Km (uM), kcat (s^-1) and kcat/Km (s^-1 M^-1) for each block. The cited cell set is Table 1, ZmALDH12 D226A block, substrate row GSAL: Km (uM) = 266; kcat (s^-1) = 3.6; kcat/Km (s^-1 M^-1) = 1.3 x 10^4.

normalized_value_unit_evidence: Km: printed cell 266 uM; 1 uM is 1/1000 mM, so 266 / 1000 = 0.266 mM. kcat: printed cell 3.6 s^-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 3.6 s^(-1). kcat/Km: printed cell 1.3 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 13000 / 1000 = 13.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.6 / 0.266 = 13.533834586466165 s^-1 mM^-1, against the printed catalytic-efficiency cell 13.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, ZmALDH12 D226A block, substrate row GSAL: Km = 266 uM; kcat = 3.6 s^-1; printed kcat/Km = 1.3 x 10^4 s^-1 M^-1.


column_label: The literal ZmALDH12 GSAL row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the independently printed efficiency is retained separately and is not substituted.

normalized_value_unit_evidence: Km=0.198 mM; kcat=6.8 s^-1; current same-row quotient=34.34343434343434 s^-1 mM^-1; printed efficiency=34 s^-1 mM^-1; printed cell is preserved separately.

raw_value_unit_evidence: GSAL cells: Km 198 ± 21 μM; kcat 6.8 ± 0.5 s^-1; printed kcat/Km 3.4 ± 0.6 × 10^4 s^-1 M^-1.

row_label: ZmALDH12 / GSAL


organism: Salmonella enterica

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


organism: Paraburkholderia xenovorans

substrate_name: propionaldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I195F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

proof_lines: I195F mutant, steady state, pH 8.0, 25°C

substrate: propionaldehyde


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

proof_lines: wild-type protein, steady state, pH 8.0, 25°C

source_databases_merged: brenda oed


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I195L to reconstruct the assayed variant sequence.

proof_lines: I195L mutant, steady state, pH 8.0, 25°C


substrate_name: Butyraldehyde

smiles: CCCC=O

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: kcat is 17.2 and 16.3 sec(-1) with acetaldehyde and propanaldehyde as substrate, respectively (at pH 8 and 25 degrees Celsius).

substrate: Butyraldehyde


substrate_name: Isobutyraldehyde

substrate: Isobutyraldehyde


assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C


proof_lines: with acetaldehyde as substrate, pH 8.0 and 25°C


organism: Bilophila wadsworthia (strain 3_1_6)

substrate_name: sulfoacetaldehyde

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 54.76 sec(-1) with sulfoacetaldehyde as substrate. kcat is 33.8 sec(-1) with CoA as substrate. kcat is 38.9 sec(-1) with NADP(+) as substrate.

substrate: sulfoacetaldehyde


substrate_name: CoA

substrate: CoA


substrate_name: NADP(+)

substrate: NADP(+)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: acetaldehyde (in the presence of HsaF)

proof_lines: kcat is 9.4 sec(-1) with acetaldehyde as substrate (in the presence of HsaF). kcat is 19.0 sec(-1) with acetaldehyde as substrate (in the absence of HsaF). kcat is 11.1 sec(-1) with propanal as substrate (in the presence of HsaF). kcat is 2

substrate: acetaldehyde (in the presence of HsaF)


substrate_name: propanal (in the presence of HsaF)

substrate: propanal (in the presence of HsaF)


substrate_name: coenzyme A (in the presence of HsaF)

substrate: coenzyme A (in the presence of HsaF)


substrate_name: NAD(+) (in the presence or absence of HsaF)


substrate_name: NADP(+) (in the presence of HsaF)

substrate: NADP(+) (in the presence of HsaF)


organism: Thermus thermophilus

substrate_name: acetaldehyde

proof_lines:
BphJ-TTHB246 complex, pH 8.0, 25°C
TTHB247-BphI complex, pH 8.0, 25°C
TTHB246-TTHB247 complex, pH 8.0, 25°C

substrate: acetaldehyde


enzyme_display_name: Acetaldehyde dehydrogenase 4

organism: Paraburkholderia xenovorans (strain LB400)

substrate_name: NADP(+) (at pH 8 and 25 degrees Celsius)

column_label: Table 4 row NADP+, column Km,app (uM), gives 561 +/- 21 uM, normalized to 0.561 mM.

row_label: BphJ / NADP+

table_label: Table 4

enzyme: Acetaldehyde dehydrogenase 4


organism: Burkholderia xenovorans

substrate_name: Propanal; NAD+; Coenzyme A

column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase BphJ / aldolase TTHB246 / substrate propionaldehyde; columns Km, kcat; cells Km 16.1+/-1.2, kcat 2.3+/-0.05.

normalized_value_unit_evidence: kcat normalized_value=2.3 normalized_unit=s^-1; Km normalized_value=16.1 normalized_unit=mM.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase BphJ / aldolase TTHB246 / substrate propionaldehyde: Km 16.1+/-1.2; kcat 2.3+/-0.05 s^-1.

substrate: Propanal; NAD+; Coenzyme A


substrate_name: NAD+; Coenzyme A; Propanal

column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase BphJ / aldolase BphI / substrate propionaldehyde; columns Km, kcat; cells Km 23.1+/-1.7, kcat 16.3+/-0.5.

normalized_value_unit_evidence: kcat normalized_value=16.3 normalized_unit=s^-1; Km normalized_value=23.1 normalized_unit=mM.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase BphJ / aldolase BphI / substrate propionaldehyde: Km 23.1+/-1.7; kcat 16.3+/-0.5 s^-1.

substrate: NAD+; Coenzyme A; Propanal


substrate_name: propanal

column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase BphJ / aldolase BphI / substrate propionaldehyde; columns Km, kcat, kcat/Km; cells Km 23.1+/-1.7, kcat 16.3+/-0.5, kcat/Km 7.0+/-0.05 x10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=16.3 normalized_unit=s^-1; Km normalized_value=23.1 normalized_unit=mM; kcat/Km normalized_value=0.70 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase BphJ / aldolase BphI / substrate propionaldehyde: Km 23.1+/-1.7; kcat 16.3+/-0.5 s^-1; kcat/Km 7.0+/-0.05 x10^2 M^-1 s^-1.

substrate: propanal


column_label: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde; row dehydrogenase BphJ / aldolase TTHB246 / substrate propionaldehyde; columns Km, kcat, kcat/Km; cells Km 16.1+/-1.2, kcat 2.3+/-0.05, kcat/Km 1.4+/-0.1 x10^2 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=2.3 normalized_unit=s^-1; Km normalized_value=16.1 normalized_unit=mM; kcat/Km normalized_value=0.14 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 5. Steady State Kinetic Parameters of Dehydrogenases TTHB247 and BphJ toward Acetaldehyde and Propionaldehyde row dehydrogenase BphJ / aldolase TTHB246 / substrate propionaldehyde: Km 16.1+/-1.2; kcat 2.3+/-0.05 s^-1; kcat/Km 1.4+/-0.1 x10^2 M^-1 s^-1.


organism: Zea mays

substrate_name: NAD+

assay_conditions_summary: pH 7.5; 303.15 K; buffer pH 7; cofactor NAD+

column_label: Table 1 / row NAD+ / enzyme block ZmALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 ZmALDH12 row NAD+ normalized: Km 0.185 mM; kcat 3.1 s^-1; kcat/Km 17.0 s^-1 mM^-1.

substrate: NAD+


substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from genbank:MF663524.1;protein:ATW64820.1;rcsb:6D97 and applied mutation signature D226A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer pH 7; cofactor NADP+

column_label: Table 1 / row NADP+ / enzyme block ZmALDH12 D226A / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 ZmALDH12 D226A row NADP+ normalized: Km 0.071 mM; kcat 1.5 s^-1; kcat/Km 21.0 s^-1 mM^-1.

row_label: ZmALDH12 D226A / NADP+

substrate: NADP+


column_label: Table 1 / row NADP+ / enzyme block ZmALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 ZmALDH12 row NADP+ normalized: Km 2.872 mM; kcat 0.8 s^-1; kcat/Km 0.27 s^-1 mM^-1.


substrate_name: 2-aminoadipic semialdehyde

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

column_label: Table 1 / row AASAL / enzyme block ZmALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 ZmALDH12 row AASAL normalized: Km 0.173 mM; kcat 0.04 s^-1; kcat/Km 0.2 s^-1 mM^-1.

substrate: 2-aminoadipic semialdehyde


substrate_name: D-glyceraldehyde 3-phosphate

column_label: Table 1 / row D-GAP / enzyme block ZmALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 ZmALDH12 row D-GAP normalized: Km 1.86 mM; kcat 0.4 s^-1; kcat/Km 0.21 s^-1 mM^-1.

substrate: D-glyceraldehyde 3-phosphate


substrate_name: L-glutamate 5-semialdehyde

column_label: Table 1 / row GSAL / enzyme block ZmALDH12 D226A / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 ZmALDH12 D226A row GSAL normalized: Km 0.266 mM; kcat 3.6 s^-1; kcat/Km 13.0 s^-1 mM^-1.

row_label: ZmALDH12 D226A / GSAL

substrate: L-glutamate 5-semialdehyde


sequence_variant_note: Resolved canonical sequence from genbank:MF663524.1;protein:ATW64820.1;rcsb:6D97 and applied mutation signature E205A to reconstruct the assayed variant sequence.

column_label: Table 2 / row E205A / GSAL / enzyme block E205A / GSAL half columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 2 E205A row E205A / GSAL normalized: Km 0.12 mM; kcat 0.21 s^-1; kcat/Km 1.8 s^-1 mM^-1.

row_label: E205A / E205A / GSAL

table_label: Table 2


sequence_variant_note: Resolved canonical sequence from genbank:MF663524.1;protein:ATW64820.1;rcsb:6D97 and applied mutation signature F202A to reconstruct the assayed variant sequence.

column_label: Table 2 / row F202A / GSAL / enzyme block F202A / GSAL half columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 2 F202A row F202A / GSAL normalized: Km 0.969 mM; kcat 0.15 s^-1; kcat/Km 0.15 s^-1 mM^-1.

row_label: F202A / F202A / GSAL


sequence_variant_note: Resolved canonical sequence from genbank:MF663524.1;protein:ATW64820.1;rcsb:6D97 and applied mutation signature F505A to reconstruct the assayed variant sequence.

column_label: Table 2 / row F505A / GSAL / enzyme block F505A / GSAL half columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 2 F505A row F505A / GSAL normalized: Km 0.17 mM; kcat 0.03 s^-1; kcat/Km 0.19 s^-1 mM^-1.

row_label: F505A / F505A / GSAL


sequence_variant_note: Resolved canonical sequence from genbank:MF663524.1;protein:ATW64820.1;rcsb:6D97 and applied mutation signature K329A to reconstruct the assayed variant sequence.

column_label: Table 2 / row K329A / GSAL / enzyme block K329A / GSAL half columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 2 K329A row K329A / GSAL normalized: Km 0.958 mM; kcat 0.26 s^-1; kcat/Km 0.27 s^-1 mM^-1.

row_label: K329A / K329A / GSAL


sequence_variant_note: Resolved canonical sequence from genbank:MF663524.1;protein:ATW64820.1;rcsb:6D97 and applied mutation signature S331A to reconstruct the assayed variant sequence.

column_label: Table 2 / row S331A / GSAL / enzyme block S331A / GSAL half columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 2 S331A row S331A / GSAL normalized: Km 0.624 mM; kcat 1.83 s^-1; kcat/Km 2.8 s^-1 mM^-1.

row_label: S331A / S331A / GSAL


column_label: Table 1 / row GSAL / enzyme block ZmALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 ZmALDH12 row GSAL normalized: Km 0.198 mM; kcat 6.8 s^-1; kcat/Km 34.0 s^-1 mM^-1.


column_label: Table 1 / row NAD+ / enzyme block ZmALDH12 D226A / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 ZmALDH12 D226A row NAD+ normalized: Km 0.119 mM; kcat 1.7 s^-1; kcat/Km 14.0 s^-1 mM^-1.

row_label: ZmALDH12 D226A / NAD+


organism: Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)

assay_conditions_summary: pH 9; cofactor CoA

column_label: PMC full text states Km(app) values for NADP+, CoA, and sulfoacetaldehyde were 64, 102, and 330 uM, respectively; NADP+ maps to 64 uM.

raw_value_unit_evidence: Km raw_value=64 raw_unit=uM

row_label: SauS Km(app) values prose

table_label: PMID 20693281 PMC Purification and Characterization of SauS prose


substrate_name: CoA

column_label: PMC full text states Km(app) values for NADP+, CoA, and sulfoacetaldehyde were 64, 102, and 330 uM, respectively; CoA maps to 102 uM.

raw_value_unit_evidence: Km raw_value=102 raw_unit=uM


substrate_name: sulfoacetaldehyde

column_label: PMC full text states Km(app) values for NADP+, CoA, and sulfoacetaldehyde were 64, 102, and 330 uM, respectively; sulfoacetaldehyde maps to 330 uM.

raw_value_unit_evidence: Km raw_value=330 raw_unit=uM


substrate_name: Butyraldehyde

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

column_label: Table 3 row butyraldehyde confirms Km and kcat but reports kcat/Km as 3.0 x10^2 M^-1 s^-1, normalized to 0.3 s^-1*mM^-1.

normalized_value_unit_evidence: Km 31.7 mM; kcat 9.5 s^-1; paper kcat/Km 0.3 s^-1*mM^-1

row_label: BphJ / butyraldehyde

table_label: Table 3

substrate: Butyraldehyde


substrate_name: Isobutyraldehyde

smiles: CC(C)C=O

column_label: Table 3 row isobutyraldehyde reports kcat/Km,app as 14.0 x10^2 M^-1 s^-1, normalized to 1.4 s^-1*mM^-1.

normalized_value_unit_evidence: Km 7.7 mM; kcat 11.2 s^-1; paper kcat/Km 1.4 s^-1*mM^-1

row_label: BphJ / isobutyraldehyde

substrate: Isobutyraldehyde


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

column_label: Table 4 row NAD+ confirms Km and kcat but reports kcat/Km as 4.0 x10^5 M^-1 s^-1, normalized to 400 s^-1*mM^-1.

row_label: BphJ / NAD+


column_label: Table 4 row NADP+ confirms Km and kcat but reports kcat/Km as 0.22 x10^5 M^-1 s^-1, normalized to 22 s^-1*mM^-1.


organism: Physcomitrium patens

column_label: Table 1 / row AASAL / enzyme block PpALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 PpALDH12 row AASAL normalized: Km 0.211 mM; kcat 0.005 s^-1; kcat/Km 0.026 s^-1 mM^-1.

row_label: PpALDH12 / AASAL


column_label: Table 1 / row GSAL / enzyme block PpALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 PpALDH12 row GSAL normalized: Km 0.228 mM; kcat 0.44 s^-1; kcat/Km 1.9 s^-1 mM^-1.

row_label: PpALDH12 / GSAL


column_label: Table 1 / row NAD+ / enzyme block PpALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 PpALDH12 row NAD+ normalized: Km 0.227 mM; kcat 0.17 s^-1; kcat/Km 0.74 s^-1 mM^-1.

row_label: PpALDH12 / NAD+


column_label: Table 1 / row NADP+ / enzyme block PpALDH12 / columns Km (uM), kcat (s^-1), and kcat/Km (s^-1 M^-1); table note preserves pH 7.5 pyrophosphate assay conditions and coenzyme/substrate setup.

normalized_value_unit_evidence: Table 1 PpALDH12 row NADP+ normalized: Km 3.066 mM; kcat 0.05 s^-1; kcat/Km 0.014 s^-1 mM^-1.

row_label: PpALDH12 / NADP+