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


enzyme_display_name: (S)-malate dehydrogenase (NAD+, oxaloacetate-forming)

organism: Sus scrofa

substrate_name: L-malate

source_db: brenda

verification_status: unverified

km_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

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

substrate: L-malate

status: unverified

source: brenda


substrate_name: NAD+

kcat_display: Not reported

km_unit: mM

assay_conditions_summary: cofactor NAD+

enzyme: (S)-malate dehydrogenase (NAD+, oxaloacetate-forming)

substrate: NAD+


organism: Spinacia oleracea

substrate_name: NADH

assay_conditions_summary: cofactor NADH

proof_lines:
intact chloroplast enzyme fraction
chloroplast envelope enzyme fraction
broken chloroplast enzyme fraction

substrate: NADH


organism: Zea mays

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

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

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


substrate_name: oxaloacetate

substrate: oxaloacetate


substrate_name: (S)-malate

substrate: (S)-malate


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


organism: Escherichia coli K-12


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NAD+


organism: Saccharomyces cerevisiae

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


organism: Escherichia coli W

proof_lines:
in the presence of 5 mM L-aspartate
in the presence of 0.5 mM L-aspartate
nearly hyperbolic NAD+ saturation curve


proof_lines: in the presence of 1 mM L-aspartate, pH 7.9

proof_lines: in the presence of 2 mM L-aspartate, pH 5.5


enzyme_display_name: malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)

substrate_name: NADP+

mutation_type: substitution

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

substrate: NADP+


enzyme: malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)


organism: Escherichia coli

assay_conditions_summary: pH 7.5; cofactor NADP+


organism: Oryza sativa

assay_conditions_summary: pH 8; cofactor NADP+


assay_conditions_summary: pH 8


organism: Anas platyrhynchos


assay_conditions_summary: cofactor NADP+


organism: Flaveria floridana


organism: Sorghum bicolor


organism: Triticum aestivum


organism: Solanum lycopersicum


organism: Pigeon

protein_accession_database: UniProt

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

data_origin: experimental


organism: Pseudomonas aeruginosa


organism: Vigna mungo


substrate_name: Unknown

ki_unit: mM

assay_conditions_summary: pH 7.4; cofactor ATP

substrate: Unknown


organism: Citrobacter freundii


organism: Escherichia coli B


enzyme_display_name: malate dehydrogenase (decarboxylating)

organism: Brassica oleracea

enzyme: malate dehydrogenase (decarboxylating)


proof_lines:
with 30 mM Mg2+
with 8 mM Mg2+
with 80 mM Mg2+


organism: Sinorhizobium meliloti

proof_lines: assuming an octameric oligomerization state


organism: Zea mays

substrate_name: NADP+; L-Malate

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

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

proof_lines:
pH 8.0, 30°C, dark
pH 8.0, 30°C, light

substrate: NADP+; L-Malate


organism: Homo sapiens

sequence_source: uniprotkb

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

proof_lines: recombinant ME1, pH 7.4, temperature not specified in the publication


organism: Streptomyces avermitilis


enzyme_display_name: malate dehydrogenase

organism: Methanocaldococcus jannaschii

substrate_name: Oxaloacetate; NADH

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

enzyme: malate dehydrogenase

substrate: Oxaloacetate; NADH


organism: Methanothermus fervidus

substrate_name: NADH; Oxaloacetate

substrate: NADH; Oxaloacetate


organism: Talaromyces emersonii

substrate_name: H+; Oxaloacetate; NADH

substrate: H+; Oxaloacetate; NADH


organism: Plasmodium falciparum

substrate_name: L-Malate; NAD+

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

assay_conditions_summary: pH 10.2; cofactor NAD+

proof_lines:
Raw SKiD Env: Temp=-----, pH=10.2
Raw SKiD Env: Temp=-----, pH=7.5

substrate: L-Malate; NAD+


organism: Sus scrofa

substrate_name: NADH; H+; Oxaloacetate

substrate: NADH; H+; Oxaloacetate


organism: Thermus thermophilus


organism: Bos taurus

substrate_name: NAD+; L-Malate

substrate: NAD+; L-Malate


substrate_name: H+; NADH; Oxaloacetate

substrate: H+; NADH; Oxaloacetate


organism: Methanospirillum hungatei

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


organism: Schistosoma mansoni


organism: Triticum aestivum


organism: Corynebacterium glutamicum

substrate_name: Oxaloacetate; NADH; H+

substrate: Oxaloacetate; NADH; H+


organism: Trypanosoma cruzi

substrate_name: NADH; Phenylpyruvate; H+

substrate: NADH; Phenylpyruvate; H+


organism: Saccharomyces cerevisiae


organism: Sphyraena idiastes


organism: Rhodovulum steppense

proof_lines:
isoform MDH2, at pH 8.5 and 25°C
isoform MDH1, at pH 8.5 and 25°C
isoform MDH3, at pH 8.5 and 25°C


organism: Beggiatoa leptomitoformis


organism: Taenia solium

sequence_source: multiple

proof_lines: kcat is 47.4 sec(-1) for L-malate. kcat is 385.6 sec(-1) for NAD. kcat is 665.34 sec(-1) for oxaloacetate. kcat is 962.66 sec(-1) for NADH.

source_databases_merged: brenda uniprot


enzyme_display_name: (S)-malate dehydrogenase (NAD(+), oxaloacetate-forming)

source_db: oed

kcat_over_km_origin: calculated

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADH

source: oed


verification_status: verified

assay_conditions_summary: pH 7.4; 303.15 K; buffer A 50 mM potassium phosphate pH 7; cofactor NADH

column_label: The literal Native m-MDH NADH row binds substrate, native enzyme block, fixed oxaloacetate condition, Km, kcat, and printed efficiency; all current values match exactly.

normalized_value_unit_evidence: kcat=110000 s^-1; Km=0.025 mM; current same-row quotient=4400000 s^-1 mM^-1; printed efficiency=4400000 s^-1 mM^-1.

raw_value_unit_evidence: Native NADH row: Km 0.025 mM; kcat 11 x 10^4 s^-1; printed kcat/Km 4.4 x 10^6 s^-1 mM^-1.

row_label: Native m-MDH / NADH ([oxaloacetate] = 50 uM)

table_label: Table 2: native and recombinant T. emersonii m-MDH kinetic constants

enzyme: (S)-malate dehydrogenase (NAD(+), oxaloacetate-forming)

status: verified


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


column_label: The literal Native m-MDH oxaloacetate row binds substrate, native enzyme block, fixed NADH condition, Km, kcat, and printed efficiency. The current quotient differs from the two-significant-digit printed efficiency by 1.11% and is supported by the same row's exact kcat and Km cells.

normalized_value_unit_evidence: kcat=91000 s^-1; Km=0.02 mM; current same-row quotient=4550000 s^-1 mM^-1; printed efficiency=4500000 s^-1 mM^-1.

raw_value_unit_evidence: Native oxaloacetate row: Km 0.02 mM; kcat 9.1 x 10^4 s^-1; printed kcat/Km 4.5 x 10^6 s^-1 mM^-1.

row_label: Native m-MDH / Oxaloacetate ([NADH] = 200 uM)


enzyme_display_name: D-3-phosphoglycerate dehydrogenase

organism: Homo sapiens

source_db: uniprot

proof_lines: kcat is 4.5 min(-1) for 3-phosphoglycerate oxidation. kcat is 10.6 min(-1) for oxaloacetate reduction. kcat is 4.7 min(-1) for 2-oxoglutarate reduction.

enzyme: D-3-phosphoglycerate dehydrogenase

source: uniprot


enzyme_display_name: Malate dehydrogenase 2, mitochondrial

organism: Arabidopsis thaliana

enzyme: Malate dehydrogenase 2, mitochondrial


enzyme_display_name: Malate dehydrogenase 1, mitochondrial

enzyme: Malate dehydrogenase 1, mitochondrial


enzyme_display_name: Malate dehydrogenase

organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)

proof_lines: kcat is 1870 sec(-1) with oxaloacetate as substrate. kcat is 542 sec(-1) with NADH as substrate. kcat is 4.71 sec(-1) with L-malate as substrate. kcat is 3.66 sec(-1) with NAD(+) as substrate.

enzyme: Malate dehydrogenase


organism: Flavobacterium frigidimaris


organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

substrate_name: S-malate

proof_lines: kcat is 5.7 sec(-1) for NAD-dependent malate oxidation.

substrate: S-malate


organism: Thermosulfidibacter takaii (strain DSM 17441 / JCM 13301 / NBRC 103674 / ABI70S6)

proof_lines: kcat is 871 sec(-1) with oxaloacetate as substrate.


organism: Escherichia coli

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

assay_conditions_summary: pH 7.2; cofactor NADP+

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
At pH 7.2.

source_databases_merged: sabio_rk skid uniprot


organism: Ascaris suum


enzyme_display_name: NAD-dependent malic enzyme 2

organism: Bacillus subtilis (strain 168)

substrate_name: NAP

enzyme: NAD-dependent malic enzyme 2

substrate: NAP


organism: Lipomyces starkeyi


substrate_name: L-malate (NAD-MEH heterodimer in the presence of coenzyme A (CoA))

assay_conditions_summary: pH 6.5; cofactor CoA

proof_lines: versus (S)-malate, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2

proof_lines: versus NAD+, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2

proof_lines: kcat is 31.1 sec(-1) for the homodimer and 39 sec(-1) for the NAD-MEH heterodimer with NAD as substrate. In the presence of coenzyme A (CoA), kcat is 40.6 sec(-1) for the NAD-MEH heterodimer with NAD as substrate.


organism: Rhodopseudomonas palustris


enzyme_display_name: NAD-dependent malic enzyme 2, mitochondrial

substrate_name: L-malate (homodimer in the presence of coenzyme A (CoA))

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 44.1 sec(-1) for the homodimer and 39 sec(-1) for the NAD-MEH heterodimer with NAD as substrate. In the presence of coenzyme A (CoA), kcat is 69.1 sec(-1) for the homodimer and 40.6 sec(-1) for the NAD-MEH heterodimer with NAD as su


organism: Rattus norvegicus

substrate_name: Pyruvate; CO2; NADPH

substrate: Pyruvate; CO2; NADPH


substrate_name: L-Malate; NADP+

substrate: L-Malate; NADP+


substrate_name: Oxaloacetate

substrate: Oxaloacetate


organism: Zea mays


organism: Ricinus communis


substrate_name: NADP+; L-Malate


organism: Columba livia


organism: Saccharum officinarum


organism: Oryza sativa


organism: Amaranthus tricolor


organism: Homo sapiens

assay_conditions_summary: cofactor NAD+


organism: Pisum sativum

substrate_name: NADH; Oxaloacetate; H+

assay_conditions_summary: cofactor NADH

substrate: NADH; Oxaloacetate; H+


organism: Spinacia oleracea


organism: Echinococcus granulosus


organism: Cryptococcus neoformans


organism: Sorghum bicolor


organism: Setaria viridis


organism: Nicotiana tabacum


enzyme_display_name: isocitrate dehydrogenase (NAD(+))

organism: Congregibacter litoralis

substrate_name: NAD+

verification_status: corrected

assay_conditions_summary: pH 7.5; 308.15 K; cofactor NAD+

column_label: Table 1, wild-type ClIDH (Mn2+) row, NAD+ group: exact Km, kcat, and independently printed kcat/Km cells.

raw_value_unit_evidence: Table 1 wild-type ClIDH (Mn2+), NAD+ columns: Km 309.1 +/- 11.2 uM; kcat 84.7 s^-1; kcat/Km 0.27 uM^-1 s^-1. The NADP+ cells are dashes.

row_label: wild-type ClIDH (Mn2+)

table_label: Table 1. Kinetic parameters of wild-type and mutant ClIDH

enzyme: isocitrate dehydrogenase (NAD(+))

substrate: NAD+

status: corrected


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P08200 sequence version 1 via official REST API and applied mutation signature K344D/Y345I/V351A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 294.15 K; buffer KAC

column_label: PMID 8524825, source page 11668 / derived PDF page 3, Table 2, E. coli IDH at 21 C, row DIA----- (K344D/Y345I/V351A), NAD columns Km (uM), kcat (s^-1), and performance kcat/Km (uM^-1 s^-1).

normalized_value_unit_evidence: Same-row central values normalize to Km 0.85 mM, kcat 9.39 s^-1, and independently printed kcat/Km 11 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 DIA----- (K344D/Y345I/V351A), NAD block: Km 850.0 uM; kcat 9.39 s^-1; performance kcat/Km 0.011 uM^-1 s^-1.

table_label: Table 2


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P08200 sequence version 1 via official REST API and applied mutation signature K344D/Y345I/V351A/Y391K/R395S to reconstruct the assayed variant sequence.

column_label: PMID 8524825, source page 11668 / derived PDF page 3, Table 2, E. coli IDH at 21 C, row DIAKS--- (K344D/Y345I/V351A/Y391K/R395S), NAD columns Km (uM), kcat (s^-1), and performance kcat/Km (uM^-1 s^-1).

normalized_value_unit_evidence: Same-row central values normalize to Km 0.29 mM, kcat 6.00 s^-1, and independently printed kcat/Km 21 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 DIAKS--- (K344D/Y345I/V351A/Y391K/R395S), NAD block: Km 290.0 uM; kcat 6.00 s^-1; performance kcat/Km 0.021 uM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P08200 sequence version 1 via official REST API and applied mutation signature K344D/Y345I/V351A/Y391K/R395S/C332Y/C201I to reconstruct the assayed variant sequence.

column_label: PMID 8524825, source page 11668 / derived PDF page 3, Table 2, E. coli IDH at 21 C, row DIAKS-YI (K344D/Y345I/V351A/Y391K/R395S/C332Y/C201I), NAD columns Km (uM), kcat (s^-1), and performance kcat/Km (uM^-1 s^-1).

normalized_value_unit_evidence: Same-row central values normalize to Km 0.099 mM, kcat 16.20 s^-1, and independently printed kcat/Km 164 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 DIAKS-YI (K344D/Y345I/V351A/Y391K/R395S/C332Y/C201I), NAD block: Km 99.0 uM; kcat 16.20 s^-1; performance kcat/Km 0.164 uM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P08200 sequence version 1 via official REST API and applied mutation signature K344D/Y345I/V351A/Y391K/R395S/R292D to reconstruct the assayed variant sequence.

column_label: PMID 8524825, source page 11668 / derived PDF page 3, Table 2, E. coli IDH at 21 C, row DIAKSD-- (K344D/Y345I/V351A/Y391K/R395S/R292D), NAD columns Km (uM), kcat (s^-1), and performance kcat/Km (uM^-1 s^-1).

normalized_value_unit_evidence: Same-row central values normalize to Km 0.924 mM, kcat 9.74 s^-1, and independently printed kcat/Km 11 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 DIAKSD-- (K344D/Y345I/V351A/Y391K/R395S/R292D), NAD block: Km 924.0 uM; kcat 9.74 s^-1; performance kcat/Km 0.011 uM^-1 s^-1.


organism: Pyrococcus furiosus

substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D328K/I329Y to reconstruct the assayed variant sequence.

substrate: NADP+


enzyme_display_name: isocitrate dehydrogenase (NADP+)

organism: Rhodomicrobium vannielii

enzyme: isocitrate dehydrogenase (NADP+)


enzyme_display_name: isocitrate dehydrogenase (NADP(+))

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R153C to reconstruct the assayed variant sequence.

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

enzyme: isocitrate dehydrogenase (NADP(+))


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R153H to reconstruct the assayed variant sequence.


organism: Arabidopsis thaliana

substrate_name: isocitrate

sequence_variant_note: Mutation signature C3636S references residue 3636, which is outside the resolved sequence length.

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

substrate: isocitrate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P08200 sequence version 1 via official REST API and applied mutation signature K344D/Y345I/V351A/Y391K/R395S/C332Y to reconstruct the assayed variant sequence.

column_label: PMID 8524825, source page 11668 / derived PDF page 3, Table 2, E. coli IDH at 21 C, row DIAKS-Y- (K344D/Y345I/V351A/Y391K/R395S/C332Y), NADP columns Km (uM), kcat (s^-1), and performance kcat/Km (uM^-1 s^-1).

normalized_value_unit_evidence: Same-row central values normalize to Km 2.8 mM, kcat 3.34 s^-1, and independently printed kcat/Km 1.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 DIAKS-Y- (K344D/Y345I/V351A/Y391K/R395S/C332Y), NADP block: Km 2800 uM; kcat 3.34 s^-1; performance kcat/Km 0.0012 uM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S113N to reconstruct the assayed variant sequence.


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R148A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

column_label: PLOS ONE DOI 10.1371/journal.pone.0115025 Table 2; row ScIDH1 R148A; columns Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1).

row_label: ScIDH1 R148A

table_label: Table 2. Comparison of the kinetic parameters of the isocitrate oxidation activity of the wild-type and mutant IDH enzymes


enzyme_display_name: isocitrate dehydrogenase (NAD+)

organism: Streptococcus mutans

substrate_name: DL-isocitrate

proof_lines: pH 7.5, 37°C, recombinant enzyme mutant S102Y

enzyme: isocitrate dehydrogenase (NAD+)

substrate: DL-isocitrate


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+

proof_lines: pH 7.5, 37°C, recombinant enzyme mutant S102A


proof_lines: pH 7.5, 37°C, recombinant enzyme mutant S102G


proof_lines: pH 7.5, 37°C, recombinant enzyme mutant S102T


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


organism: Campylobacter concisus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+


proof_lines: mutant enzyme L580H/L591R/A640R, at pH 7.5 and 25°C


substrate_name: NAD+; Isocitrate

substrate: NAD+; Isocitrate


substrate_name: Isocitrate; NAD+

substrate: Isocitrate; NAD+


organism: Rattus norvegicus


substrate_name: NAD+; D-threo-Isocitrate

substrate: NAD+; D-threo-Isocitrate


organism: Homo sapiens


organism: Bos taurus


sequence_variant_note: Resolved canonical sequence from uniprotkb:P50213 and applied mutation signature D206N with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

column_label: TABLE 3. Michaelis-Menten constants for Mn2+, Cd2+, and NAD of recombinant wild-type and mutant NAD-IDH; row D206N / Mn2+; kcat column raw 36.8 s^-1 normalized 36.8 s^-1; Km column raw 0.32 mM normalized 0.32 mM


sequence_variant_note: Resolved canonical sequence from uniprotkb:P51553 and applied mutation signature D215N with inferred residue-numbering offset +39 to reconstruct the assayed variant sequence.

column_label: TABLE 3. Michaelis-Menten constants for Mn2+, Cd2+, and NAD of recombinant wild-type and mutant NAD-IDH; row D215N / Mn2+; kcat column raw 11.8 s^-1 normalized 11.8 s^-1; Km column raw 21.1 mM normalized 21.1 mM


sequence_variant_note: Resolved canonical sequence from uniprotkb:O43837 and applied mutation signature D217N with inferred residue-numbering offset +34 to reconstruct the assayed variant sequence.

column_label: TABLE 3. Michaelis-Menten constants for Mn2+, Cd2+, and NAD of recombinant wild-type and mutant NAD-IDH; row D217N / Mn2+; kcat column raw 19.6 s^-1 normalized 19.6 s^-1; Km column raw 0.10 mM normalized 0.10 mM


sequence_variant_note: Resolved canonical sequence from uniprotkb:P50213 and applied mutation signature D230C with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

column_label: TABLE 3. Michaelis-Menten constants for Mn2+, Cd2+, and NAD of recombinant wild-type and mutant NAD-IDH; row D230C / Mn2+; kcat column raw 2.49 s^-1 normalized 2.49 s^-1; Km column raw 7.13 mM normalized 7.13 mM


sequence_variant_note: Resolved canonical sequence from uniprotkb:P50213 and applied mutation signature D234C with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

column_label: TABLE 3. Michaelis-Menten constants for Mn2+, Cd2+, and NAD of recombinant wild-type and mutant NAD-IDH; row D234C / Mn2+; kcat column raw 0.27 s^-1 normalized 0.27 s^-1; Km column raw 0.46 mM normalized 0.46 mM


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


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NAD+

column_label: TABLE 3. Michaelis-Menten constants for Mn2+, Cd2+, and NAD of recombinant wild-type and mutant NAD-IDH; row D206N / NAD; kcat column raw 36.8 s^-1 normalized 36.8 s^-1; Km column raw 140 uM normalized 0.14 mM

row_label: D206N / NAD


column_label: TABLE 3. Michaelis-Menten constants for Mn2+, Cd2+, and NAD of recombinant wild-type and mutant NAD-IDH; row D215N / NAD; kcat column raw 11.8 s^-1 normalized 11.8 s^-1; Km column raw 190 uM normalized 0.19 mM

row_label: D215N / NAD


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


organism: Streptococcus suis

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


organism: Acinetobacter baumannii

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S113A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S113G with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S113T with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S22A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S22E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S22H with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+


organism: Fomitopsis palustris

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+


substrate_name: Unknown

substrate: Unknown


organism: Lathyrus oleraceus

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: mitochondrial isozyme, forward reaction, pH 8.0

proof_lines: cytosolic isozyme, forward reaction, pH 8.0

proof_lines: mitochondrial isozyme, reverse reaction, pH 7.0


proof_lines: pH 7.6, 25°C, peroxisomes from senecent leaves


substrate_name: NADPH

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: cytosolic isozyme, reverse reaction, pH 7.0

substrate: NADPH


assay_conditions_summary: pH 7


assay_conditions_summary: pH 8

proof_lines: above, mitochondrial isozyme, forward reaction, pH 8.0


assay_conditions_summary: pH 8; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D328K with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 343.15 K; cofactor NAD+


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; 343.15 K; cofactor NADP+


organism: Spirodela polyrhiza

proof_lines: chloroplastic isozyme ICDH2, pH 7.8, 25°C


assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADP+


protein_accession_database: NCBI Protein

sequence_variant_note: Resolved canonical sequence from GenBank:EAQ96042.1 and applied mutation signature D487R/L488H to reconstruct the assayed variant sequence.

proof_lines: mutant D487R/L488H, with Mn2+, pH 7.5, 35°C


assay_conditions_summary: pH 7.5; cofactor NAD+

proof_lines: wild-type enzyme, with Mg2+, pH 7.5, 35°C

proof_lines: wild-type enzyme, with Mn2+, pH 7.5, 35°C


assay_conditions_summary: pH 7.5; 308.15 K; cofactor NADP+


organism: Leptolyngbya laminosa

substrate_name: D,L-isocitrate

assay_conditions_summary: cofactor NADP+

proof_lines:
Mn2+-dependent reaction
Mg2+-dependent reaction

substrate: D,L-isocitrate


proof_lines:
Mg2+-dependent reaction
Mn2+-dependent reaction


organism: Micromonas commoda

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

proof_lines: pH 75, 25°C, recombinant His6-tagged enzyme


assay_conditions_summary: cofactor NAD+


organism: Pyrococcus horikoshii

substrate_name: homoisocitrate

assay_conditions_summary: pH 7.8; cofactor NAD+

column_label: Official ScienceDirect full text reports the catalytic constants for homoisocitrate in the Results > Catalytic properties paragraph.

raw_value_unit_evidence: homoisocitrate Km=18.3 uM; kcat=13.7 s^-1; kcat/Km=7.49 x 10^5 M^-1 s^-1

row_label: homoisocitrate

table_label: ScienceDirect HTML, Results > Catalytic properties prose

substrate: homoisocitrate


column_label: Official ScienceDirect full text reports the catalytic constants for isocitrate in the Results > Catalytic properties paragraph.

row_label: isocitrate


column_label: Official ScienceDirect full text reports the catalytic constants for coenzyme NAD+ in the Results > Catalytic properties paragraph; Methods states 0.5 mM isocitrate was used for NAD+ constants.

row_label: NAD+


organism: Campylobacter curvus

sequence_source: NCBI protein WP_018136314.1 (Campylobacter curvus); PMID 25775177; PMCID PMC4360740; DOI 10.1038/srep09150

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

column_label: PDF Table 1 row CcIDH NADP+; kcat normalized_value=2 normalized_unit=s^-1; Km normalized_value=0.4759 normalized_unit=mM; kcat/Km normalized_value=4 normalized_unit=s^-1*mM^-1. Export tuple: kcat=2, km=0.476, kcat_over_km=4.201680672268908.

raw_value_unit_evidence: kcat raw_value=2 raw_unit=s^-1; Km raw_value=475.9 raw_unit=uM; kcat/Km raw_value=0.004 raw_unit=uM^-1*s^-1.

row_label: CcIDH NADP+

table_label: Table 1. The kinetic parameters of the wild-type and mutant enzymes


column_label: PDF Table 1 row CcIDH NAD+; kcat normalized_value=10.8 normalized_unit=s^-1; Km normalized_value=0.0742 normalized_unit=mM; kcat/Km normalized_value=146 normalized_unit=s^-1*mM^-1. Export tuple: kcat=10.8, km=0.0742, kcat_over_km=145.55256064690028.

raw_value_unit_evidence: kcat raw_value=10.8 raw_unit=s^-1; Km raw_value=74.2 raw_unit=uM; kcat/Km raw_value=0.146 raw_unit=uM^-1*s^-1.

row_label: CcIDH NAD+


proof_lines:
pH 7.5
membrane-associated ICDH


organism: Zymomonas mobilis

proof_lines: pH 7.5, 37°C, with Mg2+, recombinant enzyme

proof_lines: pH 7.5, 37°C, with Mn2+, recombinant enzyme


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+


organism: Acidithiobacillus thiooxidans

assay_conditions_summary: pH 9; cofactor NADP+


assay_conditions_summary: pH 9; cofactor NAD+


organism: Colwellia maris

substrate_name: D-isocitrate

substrate: D-isocitrate


organism: Leishmania mexicana

assay_conditions_summary: pH 7.4; 310.15 K; buffer pH 7; cofactor NADP+

column_label: Table 1 row Lmex_IDH-50 / DL-Isocitrate reports Km 0.0020 +/- 0.0003 mM and kcat 78.98 +/- 3.10 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.002 normalized_unit=mM; kcat normalized_value=78.98 normalized_unit=s^-1

raw_value_unit_evidence: Km raw_value=0.0020 +/- 0.0003 raw_unit=mM; kcat raw_value=78.98 +/- 3.10 raw_unit=s^-1

row_label: Lmex_IDH-50 / DL-Isocitrate

table_label: ScienceDirect full-text Table 1: Apparent kinetic parameters of the IDH isoenzymes from L. Mexicana


assay_conditions_summary: pH 7.4; buffer pH 7; cofactor NADP+

normalized_value_unit_evidence: Km normalized_value=0.050 normalized_unit=mM; kcat normalized_value=84.39 normalized_unit=s^-1; kcat_over_km normalized_value=1690 normalized_unit=s^-1*mM^-1; current_export_kcat_over_km=1687.8 s^-1*mM^-1

row_label: Lmex_IDH-50 / NAD+


organism: Azotobacter vinelandii


organism: Pinus spp.


organism: Zea mays

substrate_name: Isocitrate; NADP+

proof_lines:
isozyme 2
isozyme 1

substrate: Isocitrate; NADP+


organism: Methylobacillus flagellatus

assay_conditions_summary: pH 8.5; cofactor NAD+

column_label: Table 1 row values under NAD+ are 113, 166, and 1.5.

normalized_value_unit_evidence: Km normalized_value=0.113 normalized_unit=mM; kcat normalized_value=166 normalized_unit=s^-1; kcat/Km normalized_value=1500 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: NAD+ columns report Km raw_value=113 raw_unit=uM; kcat raw_value=166 raw_unit=s^-1; kcat/Km raw_value=1.5 raw_unit=uM^-1 s^-1.

row_label: Mf IDH NAD+ cofactor kinetic parameter row

table_label: PMC5397045 Table 1


assay_conditions_summary: pH 8.5; cofactor NADP+

column_label: Results text states the apparent Km value for DL-isocitrate was 9.0 uM when NAD+ was used as cosubstrate.

raw_value_unit_evidence: DL-isocitrate with NAD+ reports Km raw_value=9.0 raw_unit=uM.

row_label: DL-isocitrate Km with NAD+ as cosubstrate

table_label: PMC5397045 Results text


organism: marine plankton environmental sample

assay_conditions_summary: pH 8.2; 291.15 K; cofactor NADP+


organism: Thermoleophilum minutum


organism: Desulfobacter vibrioformis

sequence_source: NCBI RefSeq protein WP_035237112.1


organism: Pisum sativum


organism: Streptococcus suis


organism: Solanum tuberosum


organism: Acetobacter peroxydans


organism: Ostreococcus tauri

sequence_variant_note: Mutation signature D344R/M345H could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 7.6; cofactor NADP+

proof_lines: pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R/M345H, with Mn2+


proof_lines: pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mg2+

proof_lines: pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme, with Mn2+


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

assay_conditions_summary: pH 7.6; cofactor NAD+

proof_lines: pH 7.6, temperature not specified in the publication, His6-tagged recombinant mutant D344R, with Mn2+


organism: Pyrococcus furiosus

sequence_source: GenBank:AAL80326.1 (Pyrococcus furiosus DSM 3638; locus_tag PF0202; coded_by AE009950.1:216620..217822; identical protein sequence to QEK77928.1 from CP023154.1).

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: pH 8.0, 70°C, the Km-value for NADP+ is about 65fold higher than the KM-value for NAD+


organism: Mus musculus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature K256Q to reconstruct the assayed variant sequence.

proof_lines: mutant K256Q of isoform IDH2, at pH 7.4 and 25°C


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature K413Q to reconstruct the assayed variant sequence.

proof_lines: mutant K413Q of isoform IDH2, at pH 7.4 and 25°C


proof_lines: wild type isoform IDH2, at pH 7.4 and 25°C


organism: Escherichia coli


organism: Ostreococcus sp. 'lucimarinus'

sequence_variant_note: Mutation signature D326R/M327H could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

proof_lines: pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H


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

column_label: Table 1 (The kinetic parameters of the wild-type and mutant enzymes); enzyme row 'OlIDH'; NADP+ block column 'Km (uM)' = 2211; column 'kcat (s^-1)' = 10.0; column 'kcat/Km (B)(uM^-1 s^-1)' = 0.0045. The three NAD+ cells of the same printed row belong to the NAD+ coenzyme measurement, and the two trailing columns (A/B) and (B/A) are that row's dimensionless coenzyme preference index.

normalized_value_unit_evidence: Km: printed Table 1 cell 2211 uM; 2211 / 1000 = 2.211 mM. kcat: printed Table 1 cell 10.0 s^-1; already in s^-1, no unit conversion applies, so the canonical value is 10.0 s^(-1). kcat/Km: printed Table 1 cell 0.0045 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.0045 x 1000 = 4.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row 'OlIDH', NADP+ block: Km = 2211 uM; kcat = 10.0 s^-1; kcat/Km = 0.0045 uM^-1 s^-1.

row_label: Table 1, enzyme row 'OlIDH', the three NADP+ cells (Km, kcat, kcat/Km (B))

table_label: Table 1: The kinetic parameters of the wild-type and mutant enzymes (Scientific Reports 2015, 5:9150)


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+


organism: Campylobacter sp.


sequence_variant_note: Mutation signature L584H/D595R references residue 584, which is outside the resolved sequence length.

proof_lines: pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R


column_label: Table 1 (The kinetic parameters of the wild-type and mutant enzymes); enzyme row 'CaIDH'; NAD+ block column 'Km (uM)' = 28.9; column 'kcat (s^-1)' = 7.0; column 'kcat/Km (A)(uM^-1 s^-1)' = 0.242. The three NADP+ cells of the same printed row belong to the NADP+ coenzyme measurement, and the two trailing columns (A/B) and (B/A) are that row's dimensionless coenzyme preference index.

normalized_value_unit_evidence: Km: printed Table 1 cell 28.9 uM; 28.9 / 1000 = 0.0289 mM. kcat: printed Table 1 cell 7.0 s^-1; already in s^-1, no unit conversion applies, so the canonical value is 7.0 s^(-1). kcat/Km: printed Table 1 cell 0.242 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.242 x 1000 = 242.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row 'CaIDH', NAD+ block: Km = 28.9 uM; kcat = 7.0 s^-1; kcat/Km = 0.242 uM^-1 s^-1.

row_label: Table 1, enzyme row 'CaIDH', the three NAD+ cells (Km, kcat, kcat/Km (A))


organism: Plasmodium falciparum

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+


organism: Synechocystis sp.


assay_conditions_summary: cofactor NADP+

proof_lines:
Mn2+-dependent raction
Mg2+-dependent reaction


enzyme_display_name: UniProt O75874

organism: Homo sapiens

source_db: skid

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=37°C, pH=6.8
Raw SKiD Env: Temp=21°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.2

enzyme: UniProt O75874

source: skid


assay_conditions_summary: pH 7.5; 294.15 K; cofactor NADPH

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=21°C, pH=7.5


assay_conditions_summary: pH 7.5; 294.15 K; cofactor NADP+

proof_lines:
Raw SKiD Env: Temp=21°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.5


enzyme_display_name: UniProt Q8GAX0

organism: Acidithiobacillus thiooxidans

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

enzyme: UniProt Q8GAX0


assay_conditions_summary: pH 9; 303.15 K; cofactor NAD+


organism: Methylobacillus flagellatus

assay_conditions_summary: pH 8.5; 315.15 K; cofactor NADP+


organism: Desulfotalea psychrophila

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

source_databases_merged: brenda skid


assay_conditions_summary: 278.15 K; cofactor NADP+


organism: Streptomyces lividans

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines: in 20 mM Tris-HCl (pH 8.0), at 25°C, in the presence of 2 mM Mn2+

proof_lines: in 20 mM Tris-HCl (pH 8.0), at 25°C, in the presence of 2 mM Mg2+


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


organism: Gryllus firmus

assay_conditions_summary: pH 8; 301.15 K; cofactor NADP+


proof_lines:
pH 7.5, isoenzyme IDP2
pH 7.5, isoenzyme IDP1
Raw SKiD Env: Temp=25°C, pH=7.4


organism: Saccharomyces cerevisiae

proof_lines:
isozyme IDP1
isozyme IDP2
Raw SKiD Env: Temp=-----, pH=-----


proof_lines:
isozyme IDP2
isozyme IDP1


enzyme_display_name: UniProt P33198

organism: Sus scrofa

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

source_databases_merged: skid uniprot

enzyme: UniProt P33198


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 7.5; cofactor NADP+

proof_lines:
pH 7.5, isoenzyme IDP3
isozyme IDP2 and IDP3
pH 7.5, isoenzyme IDP2


proof_lines:
pH 7.5, isoenzyme IDP3
isozyme IDP1
pH 7.5, isoenzyme IDP1


organism: Phaeodactylum tricornutum

proof_lines: in the presence of Mg2+, at pH 8.0 and 25°C

proof_lines: in the presence of Mn2+, at pH 8.0 and 25°C

proof_lines: kcat is 180.5 sec(-1) for NAD(+) with Mn(2+) as cofactor. kcat is 79.0 sec(-1) for NAD(+) with Mg(2+) as cofactor.


enzyme_display_name: UniProt P9WKL1

organism: Mycobacterium tuberculosis

enzyme: UniProt P9WKL1


enzyme_display_name: UniProt P48735

enzyme: UniProt P48735


assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+

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


organism: Saccharopolyspora erythraea

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADP+


organism: Thermotoga maritima

assay_conditions_summary: pH 8; 343.15 K; cofactor NADP+

proof_lines: pH 8.0, 70°C, Km-value for NAD+ is about 140fold higher than the KM-value for NADP+


proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.2
Raw SKiD Env: Temp=37°C, pH=6.2
Raw SKiD Env: Temp=37°C, pH=7.8


enzyme_display_name: UniProt P08200

organism: Escherichia coli

enzyme: UniProt P08200


enzyme_display_name: UniProt O29610

organism: Archaeoglobus fulgidus

proof_lines: kcat is 254.6 sec(-1) with isocitrate as substrate (at 60 degrees Celsius) (PubMed:17401542). kcat is 219.3 sec(-1) with NADP(+) as substrate (at 60 degrees Celsius) (PubMed:17401542).

enzyme: UniProt O29610


assay_conditions_summary: 333.15 K; cofactor NAD+


enzyme_display_name: UniProt O88844

organism: Mus musculus

enzyme: UniProt O88844


enzyme_display_name: UniProt Q9YE81

organism: Aeropyrum pernix

enzyme: UniProt Q9YE81


assay_conditions_summary: pH 8; 333.15 K; cofactor NADP+


organism: Bos taurus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+


enzyme_display_name: UniProt Q4E4L7

organism: Trypanosoma cruzi

assay_conditions_summary: cofactor NADP+

enzyme: UniProt Q4E4L7


enzyme_display_name: Isocitrate dehydrogenase [NADP]

organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

substrate_name: NADP(+)

assay_conditions_summary: 333.15 K; cofactor NADP+

enzyme: Isocitrate dehydrogenase [NADP]

substrate: NADP(+)


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132W to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; buffer includes 50 mM Tris; cofactor NADP+

column_label: Table 3; row R132W; column kcat (37 C); substrate isocitrate | Table 3; row R132W; column Km,ICT (37 C); substrate isocitrate | Table 3; row R132W; column Efficiency kcat/Km,ICT (37 C); substrate isocitrate

table_label: Table 3


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A134D with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; buffer IDH1 assay; cofactor NADP+

column_label: Table 1; row A134D; column kcat (21 C); substrate isocitrate | Table 1; row A134D; column Km,ICT (21 C); substrate isocitrate | Table 1; row A134D; column Efficiency kcat/Km,ICT (21 C); substrate isocitrate

table_label: Table 1


column_label: Table 1; row A134D; column kcat (37 C); substrate isocitrate | Table 1; row A134D; column Km,ICT (37 C); substrate isocitrate | Table 1; row A134D; column Efficiency kcat/Km,ICT (37 C); substrate isocitrate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H133Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

column_label: Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row H133Q IDH1, column kcat; kcat, cell 9.4 s^-1, normalized 9.4 s^-1; Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row H133Q IDH1, column Km,ICT; Km, cell 0.28 mM, normalized 0.28 mM; Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row H133Q IDH1, column Efficiency kcat/Km,ICT; kcat/Km, cell 35 s^-1 mM^-1, normalized 35 s^-1 mM^-1

raw_value_unit_evidence: kcat raw 9.4 s^-1 from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1; Km raw 0.28 mM from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1; kcat/Km raw 35 s^-1 mM^-1 from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1

row_label: H133Q IDH1


column_label: Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row H133Q IDH1, column kcat; kcat, cell 45 s^-1, normalized 45 s^-1; Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row H133Q IDH1, column Km,ICT; Km, cell 0.4 mM, normalized 0.4 mM; Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row H133Q IDH1, column Efficiency kcat/Km,ICT; kcat/Km, cell 110 s^-1 mM^-1, normalized 110 s^-1 mM^-1

raw_value_unit_evidence: kcat raw 45 s^-1 from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1; Km raw 0.4 mM from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1; kcat/Km raw 110 s^-1 mM^-1 from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R100Q with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

column_label: Table 1; row R100Q; column kcat (37 C); substrate isocitrate | Table 1; row R100Q; column Km,ICT (37 C); substrate isocitrate | Table 1; row R100Q; column Efficiency kcat/Km,ICT (37 C); substrate isocitrate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132C to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row R132C IDH1, column kcat; kcat, cell 1.61 s^-1, normalized 1.61 s^-1; Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row R132C IDH1, column Km,ICT; Km, cell 5.3 mM, normalized 5.3 mM; Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row R132C IDH1, column Efficiency kcat/Km,ICT; kcat/Km, cell 0.3 s^-1 mM^-1, normalized 0.3 s^-1 mM^-1

raw_value_unit_evidence: kcat raw 1.61 s^-1 from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1; Km raw 5.3 mM from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1; kcat/Km raw 0.3 s^-1 mM^-1 from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1

row_label: R132C IDH1


column_label: Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row R132C IDH1, column kcat; kcat, cell 4.4 s^-1, normalized 4.4 s^-1; Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row R132C IDH1, column Km,ICT; Km, cell 8.2 mM, normalized 8.2 mM; Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row R132C IDH1, column Efficiency kcat/Km,ICT; kcat/Km, cell 0.54 s^-1 mM^-1, normalized 0.54 s^-1 mM^-1

raw_value_unit_evidence: kcat raw 4.4 s^-1 from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1; Km raw 8.2 mM from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1; kcat/Km raw 0.54 s^-1 mM^-1 from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132K to reconstruct the assayed variant sequence.

column_label: Table 3; row R132K; column kcat (37 C); substrate isocitrate | Table 3; row R132K; column Km,ICT (37 C); substrate isocitrate | Table 3; row R132K; column Efficiency kcat/Km,ICT (37 C); substrate isocitrate


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132N to reconstruct the assayed variant sequence.

column_label: Table 3; row R132N; column kcat (37 C); substrate isocitrate | Table 3; row R132N; column Km,ICT (37 C); substrate isocitrate | Table 3; row R132N; column Efficiency kcat/Km,ICT (37 C); substrate isocitrate


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132Q to reconstruct the assayed variant sequence.

column_label: Table 3; row R132Q; column kcat (37 C); substrate isocitrate | Table 3; row R132Q; column Km,ICT (37 C); substrate isocitrate | Table 3; row R132Q; column Efficiency kcat/Km,ICT (37 C); substrate isocitrate


assay_conditions_summary: pH 7.5; 310.15 K; buffer IDH1 assay; cofactor NADPH

column_label: Table 2; row R100Q; column kcat (21 C); substrate 2-Oxoglutarate | Table 2; row R100Q; column Km,alphaKG (21 C); substrate 2-Oxoglutarate | Table 2; row R100Q; column Efficiency kcat/Km,alphaKG (21 C); substrate 2-Oxoglutarate


column_label: Table 2; row R100Q; column kcat (37 C); substrate 2-Oxoglutarate | Table 2; row R100Q; column Km,alphaKG (37 C); substrate 2-Oxoglutarate | Table 2; row R100Q; column Efficiency kcat/Km,alphaKG (37 C); substrate 2-Oxoglutarate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132A to reconstruct the assayed variant sequence.

column_label: Table 4; row R132A; column kcat (37 C); substrate 2-Oxoglutarate | Table 4; row R132A; column Km,alphaKG (37 C); substrate 2-Oxoglutarate | Table 4; row R132A; column Efficiency kcat/Km,alphaKG (37 C); substrate 2-Oxoglutarate

table_label: Table 4


column_label: Table 2; row R132C; column kcat (37 C); substrate 2-Oxoglutarate | Table 2; row R132C; column Km,alphaKG (37 C); substrate 2-Oxoglutarate | Table 2; row R132C; column Efficiency kcat/Km,alphaKG (37 C); substrate 2-Oxoglutarate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132G to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters for the neomorphic reaction, conversion of alphaKG to D2HG, catalyzed by IDH1, row R132G IDH1, column kcat; kcat, cell 0.45 s^-1, normalized 0.45 s^-1; Table 2. Kinetic parameters for the neomorphic reaction, conversion of alphaKG to D2HG, catalyzed by IDH1, row R132G IDH1, column Km,alphaKG; Km, cell 0.3 mM, normalized 0.3 mM; Table 2. Kinetic parameters for the neomorphic reaction, conversion of alphaKG to D2HG, catalyzed by IDH1, row R132G IDH1, column Efficiency kcat/Km,alphaKG; kcat/Km, cell 1.5 s^-1 mM^-1, normalized 1.5 s^-1 mM^-1

raw_value_unit_evidence: kcat raw 0.45 s^-1 from Table 2. Kinetic parameters for the neomorphic reaction, conversion of alphaKG to D2HG, catalyzed by IDH1; Km raw 0.3 mM from Table 2. Kinetic parameters for the neomorphic reaction, conversion of alphaKG to D2HG, catalyzed by IDH1; kcat/Km raw 1.5 s^-1 mM^-1 from Table 2. Kinetic parameters for the neomorphic reaction, conversion of alphaKG to D2HG, catalyzed by IDH1

row_label: R132G IDH1


column_label: Table 2. Kinetic parameters for the neomorphic reaction, conversion of alphaKG to D2HG, catalyzed by IDH1, row R132G IDH1, column kcat; kcat, cell 1.59 s^-1, normalized 1.59 s^-1; Table 2. Kinetic parameters for the neomorphic reaction, conversion of alphaKG to D2HG, catalyzed by IDH1, row R132G IDH1, column Km,alphaKG; Km, cell 0.34 mM, normalized 0.34 mM; Table 2. Kinetic parameters for the neomorphic reaction, conversion of alphaKG to D2HG, catalyzed by IDH1, row R132G IDH1, column Efficiency kcat/Km,alphaKG; kcat/Km, cell 5 s^-1 mM^-1, normalized 5 s^-1 mM^-1

raw_value_unit_evidence: kcat raw 1.59 s^-1 from Table 2. Kinetic parameters for the neomorphic reaction, conversion of alphaKG to D2HG, catalyzed by IDH1; Km raw 0.34 mM from Table 2. Kinetic parameters for the neomorphic reaction, conversion of alphaKG to D2HG, catalyzed by IDH1; kcat/Km raw 5 s^-1 mM^-1 from Table 2. Kinetic parameters for the neomorphic reaction, conversion of alphaKG to D2HG, catalyzed by IDH1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132K to reconstruct the assayed variant sequence.

column_label: Table 4; row R132K; column kcat (37 C); substrate 2-Oxoglutarate | Table 4; row R132K; column Km,alphaKG (37 C); substrate 2-Oxoglutarate | Table 4; row R132K; column Efficiency kcat/Km,alphaKG (37 C); substrate 2-Oxoglutarate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132N to reconstruct the assayed variant sequence.

column_label: Table 4; row R132N; column kcat (37 C); substrate 2-Oxoglutarate | Table 4; row R132N; column Km,alphaKG (37 C); substrate 2-Oxoglutarate | Table 4; row R132N; column Efficiency kcat/Km,alphaKG (37 C); substrate 2-Oxoglutarate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132Q to reconstruct the assayed variant sequence.

column_label: Table 4; row R132Q; column kcat (37 C); substrate 2-Oxoglutarate | Table 4; row R132Q; column Km,alphaKG (37 C); substrate 2-Oxoglutarate | Table 4; row R132Q; column Efficiency kcat/Km,alphaKG (37 C); substrate 2-Oxoglutarate


column_label: Table 4; row R132W; column kcat (37 C); substrate 2-Oxoglutarate | Table 4; row R132W; column Km,alphaKG (37 C); substrate 2-Oxoglutarate | Table 4; row R132W; column Efficiency kcat/Km,alphaKG (37 C); substrate 2-Oxoglutarate


assay_conditions_summary: pH 7.2; 310.15 K; buffer attribution

proof_lines:
WT alphaKG
isocitrate
pH 7.2


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S113N to reconstruct the assayed variant sequence.


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

column_label: Table II (Kinetic Constants from Initial Rate Studies), Forward Reactions section, first substrate-pair block in which isocitrate was varied with NADP, printed row 'isocitrate', enzyme column group 'S113' (the wild-type enzyme): column 'Km (mM)' = 0.011; the column 'kcat (s-1)' cell printed for that substrate-pair block in the same enzyme column group = 80.5; column 'Ki (mM)' = 0.004. Table II carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table II cell 80.5 s-1; already in s^-1, so no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 80.5 s^(-1). Km: printed Table II cell 0.011 mM; already in mM, so no unit conversion applies; the paper value is 0.011 mM. kcat/Km: Table II has no kcat/Km column, so the paper value 7318.181818181819 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 80.5 / 0.011 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table II, Forward Reactions, isocitrate and NADP experiment, isocitrate row, S113 wild-type enzyme group: kcat = 80.5 s-1; Km = 0.011 mM; Table II prints no kcat/Km cell for this measurement.

table_label: Table II: Kinetic Constants from Initial Rate Studies (Biochemistry 1993, 32(36):9302-9309)


column_label: Table II (Kinetic Constants from Initial Rate Studies), Reverse Reaction Catalyzed by Wild-Type S113 Enzyme block, which prints one enzyme form only: entry 'KaKg' = 0.57 mM, the Michaelis constant of a-ketoglutarate named by footnote c as a-ketoglutarate; entry 'kcat' = 14.9 s-1 for the same reverse reaction. Table II carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table II cell 14.9 s-1; already in s^-1, so no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 14.9 s^(-1). Km: printed Table II cell 0.57 mM; already in mM, so no unit conversion applies; the paper value is 0.57 mM. kcat/Km: Table II has no kcat/Km column, so the paper value 26.140350877192986 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 14.9 / 0.57 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table II, Reverse Reaction Catalyzed by Wild-Type S113 Enzyme block, KaKg entry: kcat = 14.9 s-1; Km = 0.57 mM; Table II prints no kcat/Km cell for this measurement.


substrate_name: L-Malate

proof_lines: Escherichia coli isocitrate dehydrogenase

substrate: L-Malate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S113L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 294.15 K; cofactor NAD+


column_label: Table II (Kinetic Constants from Initial Rate Studies), Forward Reactions section, third substrate-pair block in which isocitrate was varied with NAD, printed row 'NAD', enzyme column group 'S113' (the wild-type enzyme): column 'Km (mM)' = 4.7; the column 'kcat (s-1)' cell printed for that substrate-pair block in the same enzyme column group = 3.22; column 'Ki (mM)' = 2.7. Table II carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table II cell 3.22 s-1; already in s^-1, so no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 3.22 s^(-1). Km: printed Table II cell 4.7 mM; already in mM, so no unit conversion applies; the paper value is 4.7 mM. kcat/Km: Table II has no kcat/Km column, so the paper value 0.6851063829787234 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 3.22 / 4.7 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table II, Forward Reactions, isocitrate and NAD experiment, NAD row, S113 wild-type enzyme group: kcat = 3.22 s-1; Km = 4.7 mM; Table II prints no kcat/Km cell for this measurement.


assay_conditions_summary: pH 7.3; 294.15 K; cofactor NADP+


assay_conditions_summary: pH 7.3; 371.65 K; cofactor NADP+


assay_conditions_summary: pH 7.3; 294.15 K; cofactor NADPH

column_label: Table II (Kinetic Constants from Initial Rate Studies), Reverse Reaction Catalyzed by Wild-Type S113 Enzyme block, which prints one enzyme form only: entry 'KnaDPH' = 0.007 mM, the Michaelis constant of NADPH; entry 'kcat' = 14.9 s-1 for the same reverse reaction. Table II carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table II cell 14.9 s-1; already in s^-1, so no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 14.9 s^(-1). Km: printed Table II cell 0.007 mM; already in mM, so no unit conversion applies; the paper value is 0.007 mM. kcat/Km: Table II has no kcat/Km column, so the paper value 2128.5714285714284 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 14.9 / 0.007 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table II, Reverse Reaction Catalyzed by Wild-Type S113 Enzyme block, KnaDPH entry: kcat = 14.9 s-1; Km = 0.007 mM; Table II prints no kcat/Km cell for this measurement.


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature D273L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

column_label: Table 3 columns IDH1 reaction, kcat s^-1, Km mM, kcat/Km mM^-1 s^-1; D273L row has the listed metric cells

row_label: D273L, isocitrate -> alphaKG


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature D273N to reconstruct the assayed variant sequence.

column_label: Table 3 columns IDH1 reaction, kcat s^-1, Km mM, kcat/Km mM^-1 s^-1; D273N row has the listed metric cells

raw_value_unit_evidence: Table 3 D273N row reports kcat 22 +/- 1 s^-1, Km 19 +/- 2 mM, and kcat/Km 1.2 +/- 0.1 mM^-1 s^-1

row_label: D273N, isocitrate -> alphaKG


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D273S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature K217M to reconstruct the assayed variant sequence.

column_label: Table 3 columns IDH1 reaction, kcat s^-1, Km mM, kcat/Km mM^-1 s^-1; K217M row has the listed metric cells

row_label: K217M, isocitrate -> alphaKG


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature K217Q to reconstruct the assayed variant sequence.

column_label: Table 3 columns IDH1 reaction, kcat s^-1, Km mM, kcat/Km mM^-1 s^-1; K217Q row has the listed metric cells

row_label: K217Q, isocitrate -> alphaKG


assay_conditions_summary: pH 6.2; 310.15 K; buffer contexts

proof_lines:
WT IDH1
isocitrate to alphaKG
KPhos buffer


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K256Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature K413Q to reconstruct the assayed variant sequence.

column_label: Table 1, isocitrate kinetics section, K413Q row reports K_m 55.5 +/- 7.1, kcat 4.61 +/- 0.15, and kcat/K_m 0.083 +/- 0.008.

row_label: Isocitrate kinetics / K413Q


column_label: Table 1, isocitrate kinetics section, WT row reports K_m 54.4 +/- 5.6, kcat 5.60 +/- 0.14, and kcat/K_m 0.111 +/- 0.011.

row_label: Isocitrate kinetics / WT


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature K256Q to reconstruct the assayed variant sequence.

column_label: Table 1, NADP+ kinetics section, K256Q row reports K_m 14.8 +/- 1.3, kcat 3.13 +/- 0.13, and kcat/K_m 0.205 +/- 0.022.

row_label: NADP+ kinetics / K256Q


column_label: Table 1, NADP+ kinetics section, K413Q row reports K_m 112.2 +/- 13.2, kcat 7.69 +/- 0.49, and kcat/K_m 0.059 +/- 0.001.

row_label: NADP+ kinetics / K413Q


organism: Pyrococcus furiosus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D328K with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 343.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D328K/I329Y to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8; 343.15 K; cofactor NADP+


organism: Methanococcoides methylutens

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H590L/R601D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.2; 318.15 K; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H590L/R601D/R650S to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8.2; 323.15 K; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K344D/Y345I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K344D/Y345I/V351A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K344D/Y345I/V351A/Y391K/R395S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K344D/Y345I/V351A/Y391K/R395S/C332Y/C201I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K344D/Y345I/V351A/Y391K/R395S/R292D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R101Q with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R110Q with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R120Q with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R133Q with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


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


organism: Bifidobacterium longum

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D253A/S257K/K260Q/R314D/H315I/T327A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R314D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R314D/H315I/T327A to reconstruct the assayed variant sequence.


column_label: Table 2 wild-type row NAD+ Km and kcat and kcat/Km columns.

row_label: Wild-type D/S/K/R/H/T row under NAD+ columns

table_label: Table 2: kinetic parameters of wild-type BlIDH and mutants


organism: Campylobacter sp.

sequence_variant_note: Mutation signature L584H/D595R references residue 584, which is outside the resolved sequence length.

assay_conditions_summary: 298.15 K; cofactor NADP+


column_label: PDF Table 1 row CaIDH NAD+; kcat normalized_value=7 normalized_unit=s^-1; Km normalized_value=0.0289 normalized_unit=mM; kcat/Km normalized_value=242 normalized_unit=s^-1*mM^-1. Export tuple: kcat=7, km=0.0289, kcat_over_km=242.21453287197232.

raw_value_unit_evidence: kcat raw_value=7 raw_unit=s^-1; Km raw_value=28.9 raw_unit=uM; kcat/Km raw_value=0.242 raw_unit=uM^-1*s^-1.

row_label: CaIDH NAD+


column_label: PDF Table 1 row CaIDH NADP+; kcat normalized_value=1.9 normalized_unit=s^-1; Km normalized_value=0.5132 normalized_unit=mM; kcat/Km normalized_value=4 normalized_unit=s^-1*mM^-1. Export tuple: kcat=1.9, km=0.513, kcat_over_km=3.7037037037037033.

raw_value_unit_evidence: kcat raw_value=1.9 raw_unit=s^-1; Km raw_value=513.2 raw_unit=uM; kcat/Km raw_value=0.004 raw_unit=uM^-1*s^-1.

row_label: CaIDH NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K344D/Y345I/V351A/Y391G/R395G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K344D/Y345I/V351A/Y391K/R395S/C332Y to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.5; 294.15 K; buffer KAC; cofactor NAD+

column_label: Table 2; row label: KYYRRC (wild type); coenzyme column block: NAD; Km [uM] = 4700.0; kcat [sec^-1] = 3.22; kcat/Km [uM^-1 sec^-1] = 0.00069; normalized Km=4.7 mM, kcat=3.22 s^-1, kcat/Km=0.69 s^-1 mM^-1.

normalized_value_unit_evidence: normalized: Km=4.7 mM; kcat=3.22 s^-1; kcat/Km=0.69 s^-1 mM^-1

raw_value_unit_evidence: Table 2; KYYRRC (wild type); NAD column block; Km = 4700.0 uM; kcat = 3.22 sec^-1; kcat/Km = 0.00069 uM^-1 sec^-1.

row_label: Table row: KYYRRC (wild type); coenzyme column block: NAD; metric columns: Km [uM], kcat [sec^-1], kcat/Km [uM^-1 sec^-1].

table_label: Table 2: Kinetic parameters of wild-type and mutant enzymes toward NADP and NAD


enzyme_display_name: L-xylulose reductase

organism: Trichoderma reesei

substrate_name: xylitol

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

enzyme: L-xylulose reductase

substrate: xylitol


substrate_name: D-sorbitol

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

substrate: D-sorbitol


substrate_name: D-ribulose

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

assay_conditions_summary: pH 7

substrate: D-ribulose


enzyme_display_name: L-iditol 2-dehydrogenase

substrate_name: D-fructose (at pH 7.1)

proof_lines: kcat is 1.7 sec(-1) for the oxidation of D-sorbitol at pH 7.1, and 5.2 sec(-1) at pH 10.0. kcat is 5.9 sec(-1) the oxidation of xylitol as substrate at pH 10.0. kcat is 5.3 sec(-1) the oxidation of L-threitol as substrate at pH 10.0. kcat i

enzyme: L-iditol 2-dehydrogenase

substrate: D-fructose (at pH 7.1)


substrate_name: NAD(+)

substrate: NAD(+)


enzyme_display_name: isocitrate dehydrogenase (NAD(+))

organism: Ostreococcus sp. 'lucimarinus'

substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A4SBK5 and applied mutation signature D326R/M327H to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

column_label: Table 1 (The kinetic parameters of the wild-type and mutant enzymes); enzyme row 'OlIDH R326H327'; NAD+ block column 'Km (uM)' = 2941.3; column 'kcat (s^-1)' = 29.1; column 'kcat/Km (A)(uM^-1 s^-1)' = 0.01. The three NADP+ cells of the same printed row belong to the NADP+ coenzyme measurement, and the two trailing columns (A/B) and (B/A) are that row's dimensionless coenzyme preference index.

normalized_value_unit_evidence: Km: printed Table 1 cell 2941.3 uM; 2941.3 / 1000 = 2.9413 mM. kcat: printed Table 1 cell 29.1 s^-1; already in s^-1, no unit conversion applies, so the canonical value is 29.1 s^(-1). kcat/Km: printed Table 1 cell 0.01 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.01 x 1000 = 10.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row 'OlIDH R326H327', NAD+ block: Km = 2941.3 uM; kcat = 29.1 s^-1; kcat/Km = 0.01 uM^-1 s^-1.

row_label: Table 1, enzyme row 'OlIDH R326H327', the three NAD+ cells (Km, kcat, kcat/Km (A))

enzyme: isocitrate dehydrogenase (NAD(+))

substrate: NAD+


assay_conditions_summary: 298.15 K; cofactor NAD+

column_label: PDF Table 1 row OlIDH NAD+; kcat normalized_value=60.6 normalized_unit=s^-1; Km normalized_value=0.1366 normalized_unit=mM; kcat/Km normalized_value=444 normalized_unit=s^-1*mM^-1. Export tuple: kcat=60.6, km=0.136, kcat_over_km=445.5882352941176.

raw_value_unit_evidence: kcat raw_value=60.6 raw_unit=s^-1; Km raw_value=136.6 raw_unit=uM; kcat/Km raw_value=0.444 raw_unit=uM^-1*s^-1.

row_label: OlIDH NAD+


substrate_name: NADP+

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

column_label: Table 1 (The kinetic parameters of the wild-type and mutant enzymes); enzyme row 'OlIDH R326H327'; NADP+ block column 'Km (uM)' = 8.2; column 'kcat (s^-1)' = 1.8; column 'kcat/Km (B)(uM^-1 s^-1)' = 0.22. The three NAD+ cells of the same printed row belong to the NAD+ coenzyme measurement, and the two trailing columns (A/B) and (B/A) are that row's dimensionless coenzyme preference index.

normalized_value_unit_evidence: Km: printed Table 1 cell 8.2 uM; 8.2 / 1000 = 0.0082 mM. kcat: printed Table 1 cell 1.8 s^-1; already in s^-1, no unit conversion applies, so the canonical value is 1.8 s^(-1). kcat/Km: printed Table 1 cell 0.22 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.22 x 1000 = 220.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row 'OlIDH R326H327', NADP+ block: Km = 8.2 uM; kcat = 1.8 s^-1; kcat/Km = 0.22 uM^-1 s^-1.

row_label: Table 1, enzyme row 'OlIDH R326H327', the three NADP+ cells (Km, kcat, kcat/Km (B))

substrate: NADP+


column_label: PDF Table 1 row OlIDH NADP+; kcat normalized_value=10 normalized_unit=s^-1; Km normalized_value=2.211 normalized_unit=mM; kcat/Km normalized_value=4.5 normalized_unit=s^-1*mM^-1. Export tuple: kcat=10, km=2.211, kcat_over_km=4.522840343735867.

raw_value_unit_evidence: kcat raw_value=10 raw_unit=s^-1; Km raw_value=2211 raw_unit=uM; kcat/Km raw_value=0.0045 raw_unit=uM^-1*s^-1.

row_label: OlIDH NADP+


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R148H to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

column_label: PLOS ONE DOI 10.1371/journal.pone.0115025 Table 3; row ScIDH1 R148H; columns Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1).

raw_value_unit_evidence: Table 3 row ScIDH1 R148H: Km 30.0 uM; kcat 0.34 s^-1; kcat/Km 0.011 uM^-1 s^-1.

row_label: ScIDH1 R148H

table_label: Table 3. Comparison of the kinetic parameters for the alpha-KG reduction activity of the mutant IDHs


substrate_name: isocitrate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R148E to reconstruct the assayed variant sequence.

column_label: PLOS ONE DOI 10.1371/journal.pone.0115025 Table 2; row ScIDH1 R148E; columns Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1).

row_label: ScIDH1 R148E

substrate: isocitrate


column_label: PLOS ONE DOI 10.1371/journal.pone.0115025 Table 2; row ScIDH1 R148H; columns Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1).

raw_value_unit_evidence: Table 2 row ScIDH1 R148H: Km 24.8 uM; kcat 0.27 s^-1; kcat/Km 0.011 uM^-1 s^-1.


column_label: PLOS ONE DOI 10.1371/journal.pone.0115025 Table 2; row ScIDH1; columns Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1).

raw_value_unit_evidence: Table 2 row ScIDH1: Km 10.5 uM; kcat 26.3 s^-1; kcat/Km 2.5 uM^-1 s^-1.


enzyme_display_name: galactitol 2-dehydrogenase

organism: Agrobacterium fabrum (strain C58 / ATCC 33970)

substrate_name: galactitol

proof_lines: kcat is 3.5 sec(-1) with galactitol as substrate. kcat is 4.4 sec(-1) with D-sorbitol as substrate.

enzyme: galactitol 2-dehydrogenase

substrate: galactitol


enzyme_display_name: isocitrate dehydrogenase (NADP(+))

organism: Yarrowia lipolytica

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R141H with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

column_label: PLOS ONE DOI 10.1371/journal.pone.0115025 Table 3; row YlIDH R141H; columns Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1).

raw_value_unit_evidence: Table 3 row YlIDH R141H: Km 47.3 uM; kcat 0.43 s^-1; kcat/Km 0.009 uM^-1 s^-1.

row_label: YlIDH R141H

enzyme: isocitrate dehydrogenase (NADP(+))


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R141A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

column_label: PLOS ONE DOI 10.1371/journal.pone.0115025 Table 2; row YlIDH R141A; columns Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1).

raw_value_unit_evidence: Table 2 row YlIDH R141A: Km 367.2 uM; kcat 1.2 s^-1; kcat/Km 0.003 uM^-1 s^-1.

row_label: YlIDH R141A


column_label: PLOS ONE DOI 10.1371/journal.pone.0115025 Table 2; row YlIDH R141H; columns Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1).

raw_value_unit_evidence: Table 2 row YlIDH R141H: Km 25.6 uM; kcat 0.14 s^-1; kcat/Km 0.005 uM^-1 s^-1.


column_label: PLOS ONE DOI 10.1371/journal.pone.0115025 Table 2; row YlIDH; columns Km (uM), kcat (s^-1), and kcat/Km (uM^-1 s^-1).

raw_value_unit_evidence: Table 2 row YlIDH: Km 11.7 uM; kcat 26.6 s^-1; kcat/Km 2.3 uM^-1 s^-1.

row_label: YlIDH


organism: Plasmodium falciparum


assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+


organism: Campylobacter curvus

column_label: Table 1, CcIDH row under NAD+ reports K_m 74.2 +/- 8.2, kcat 10.8 +/- 1.4, and kcat/Km 0.146.

raw_value_unit_evidence: Table 1 CcIDH NAD+ columns: K_m 74.2 +/- 8.2 microM; kcat 10.8 +/- 1.4 s^-1; kcat/Km 0.146 microM^-1 s^-1

row_label: CcIDH / NAD+


column_label: Table 1, CcIDH row under NADP+ reports K_m 475.9 +/- 6.5, kcat 2 +/- 0.2, and kcat/Km 0.004.

raw_value_unit_evidence: Table 1 CcIDH NADP+ columns: K_m 475.9 +/- 6.5 microM; kcat 2 +/- 0.2 s^-1; kcat/Km 0.004 microM^-1 s^-1

row_label: CcIDH / NADP+


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.5; 296.15 K; cofactor NADPH

proof_lines:
varying alphaKG
ICDH-1
pH 7.5


assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADP+

proof_lines:
fixed isocitrate
varying NADP+
ICDH-1


assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADPH

proof_lines:
NADPH Michaelis-Menten assay
varying NADPH
ICDH-1


organism: Congregibacter litoralis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D487R/L488H to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 308.15 K; buffer Mn2+ as divalent cation. The methods describe 35 mM Tris-HCl; cofactor NAD+

column_label: Table 1: Kinetic parameters of wild-type and mutant ClIDH, row D487R/L488H (Mn2+), NAD+ columns: Km raw_value=663.8 +/- 48.6 raw_unit=uM, kcat raw_value=9.7 raw_unit=s^-1, kcat/Km raw_value=0.015 raw_unit=uM^-1 s^-1. Km normalized to 0.6638 mM, kcat normalized to 9.7 s^-1, paper rounded kcat/Km normalized to 15 s^-1*mM^-1; CatLog stores computed ratio 14.608433734939757 from exact kcat and rounded Km.

normalized_value_unit_evidence: Km 663.8 uM -> 0.6638 mM, matching CatLog 0.664 mM after rounding; kcat 9.7 s^-1 exact; kcat/Km paper 0.015 uM^-1 s^-1 -> 15 s^-1*mM^-1, consistent with CatLog computed ratio 14.608433734939757 from table kcat/Km inputs.


assay_conditions_summary: pH 7.5; 308.15 K; buffer Mn2+ as divalent cation. The methods describe 35 mM Tris-HCl; cofactor NADP+

column_label: Table 1: Kinetic parameters of wild-type and mutant ClIDH, row D487R/L488H (Mn2+), NADP+ columns: Km raw_value=156.7 +/- 4.8 raw_unit=uM, kcat raw_value=55.1 raw_unit=s^-1, kcat/Km raw_value=0.35 raw_unit=uM^-1 s^-1. Km normalized to 0.1567 mM, kcat normalized to 55.1 s^-1, paper rounded kcat/Km normalized to 350 s^-1*mM^-1; CatLog stores computed ratio 350.95541401273886 from exact kcat and rounded Km.

normalized_value_unit_evidence: Km 156.7 uM -> 0.1567 mM, matching CatLog 0.157 mM after rounding; kcat 55.1 s^-1 exact; kcat/Km paper 0.35 uM^-1 s^-1 -> 350 s^-1*mM^-1, consistent with CatLog computed ratio 350.95541401273886 from table kcat/Km inputs.


organism: Micromonas commoda

assay_conditions_summary: pH 7.5; 298.15 K; buffer pH 7; cofactor NAD+

column_label: Table 1, MiIDH row under NAD+ reports K_m 126 +/- 5.3, kcat 22.5 +/- 2, and kcat/Km 0.179.

raw_value_unit_evidence: Table 1 MiIDH NAD+ columns: K_m 126 +/- 5.3 microM; kcat 22.5 +/- 2 s^-1; kcat/Km 0.179 microM^-1 s^-1

row_label: MiIDH / NAD+


assay_conditions_summary: pH 7.5; 298.15 K; buffer pH 7; cofactor NADP+

column_label: Table 1, MiIDH row under NADP+ reports K_m 1827 +/- 42.4, kcat 1.4 +/- 0.2, and kcat/Km 0.0008.

raw_value_unit_evidence: Table 1 MiIDH NADP+ columns: K_m 1827 +/- 42.4 microM; kcat 1.4 +/- 0.2 s^-1; kcat/Km 0.0008 microM^-1 s^-1

row_label: MiIDH / NADP+


enzyme_display_name: isocitrate dehydrogenase (NADP+)

organism: Rhodomicrobium vannielii

assay_conditions_summary: cofactor NADP+

column_label: Abstract reports Km values of 2.5 microM for NADP and 0.77 mM for NAD.

raw_value_unit_evidence: Km raw_value=2.5 microM raw_unit=microM

row_label: Rhodomicrobium vannielii isocitrate dehydrogenase / NADP+

table_label: PubMed XML abstract PMID 1935983

enzyme: isocitrate dehydrogenase (NADP+)


column_label: Table 2. The kinetic parameters of wild-type Bl IDH and mutants; row Wild-type Bl IDH / NADP+; column NADP+ kcat (s^-1) raw value 36.38 s^-1; column NADP+ Km (uM) raw value 19.45 uM; column NADP+ kcat/Km (s^-1 mM^-1) raw value 1870 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=36.38 normalized_unit=s^-1; Km normalized_value=0.01945 normalized_unit=mM; kcat/Km normalized_value=1870 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=36.38 raw_unit=s^-1; Km raw_value=19.45 raw_unit=uM; kcat/Km raw_value=1870 raw_unit=s^-1*mM^-1

row_label: Wild-type Bl IDH / NADP+


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R153C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R153H to reconstruct the assayed variant sequence.


organism: Acidithiobacillus thiooxidans

assay_conditions_summary: pH 9; 303.15 K; cofactor NAD+

proof_lines:
NAD(+)
NADP(+)
isocitrate dehydrogenase


assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+


organism: Bifidobacterium longum subsp. infantis

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


column_label: Table 2. The kinetic parameters of wild-type Bl IDH and mutants; row Wild-type Bl IDH / NAD+; column NAD+ kcat (s^-1) raw value 11.7 s^-1; column NAD+ Km (uM) raw value 3584 uM; column NAD+ kcat/Km (s^-1 mM^-1) raw value 3.3 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=11.7 normalized_unit=s^-1; Km normalized_value=3.584 normalized_unit=mM; kcat/Km normalized_value=3.3 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=11.7 raw_unit=s^-1; Km raw_value=3584 raw_unit=uM; kcat/Km raw_value=3.3 raw_unit=s^-1*mM^-1

row_label: Wild-type Bl IDH / NAD+


organism: Streptomyces lividans


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

substrate_name: NADP(+) (for native enzyme)

proof_lines:
Haloferax volcanii
isocitrate dehydrogenases
NADP-linked

substrate: NADP(+) (for native enzyme)


substrate_name: isocitrate (for native enzyme)

proof_lines:
Haloferax volcanii
isocitrate dehydrogenases
native enzyme

substrate: isocitrate (for native enzyme)


organism: Thermus thermophilus

assay_conditions_summary: pH 8; 333.15 K; buffer 50 mM HEPES; cofactor NAD+

column_label: Table II row ICDH has Homocitrate Km = 114 +/- 2 uM and kcat = 5 +/- 0 s^-1; derived kcat/Km = 5 / 0.114 = 43.859649122807014 s^-1*mM^-1. The table also prints rounded kcat/Km 4.4 x 10^4 s^-1 M^-1.

normalized_value_unit_evidence: Km normalized_value=0.114 normalized_unit=mM from 114 uM / 1000; kcat normalized_value=5 normalized_unit=s^-1; kcat/Km derived normalized_value=43.859649122807014 normalized_unit=s^-1*mM^-1 from 5 / 0.114.

raw_value_unit_evidence: Table II ICDH row under Homocitrate reports Km 114 +/- 2 uM, kcat 5 +/- 0 s^-1, and rounded printed kcat/Km 4.4 x 10^4 s^-1 M^-1.

row_label: ICDH row / Homocitrate columns

table_label: PMID 12427751 Table II: Kinetic properties of HICDH and ICDH from T. thermophilus HB27


column_label: Table II row ICDH has Isocitrate Km = 67 +/- 6 uM and kcat = 68 +/- 3 s^-1; derived kcat/Km = 68 / 0.067 = 1014.9253731343283 s^-1*mM^-1. The table also prints rounded kcat/Km 1.0 x 10^6 s^-1 M^-1.

normalized_value_unit_evidence: Km normalized_value=0.067 normalized_unit=mM from 67 uM / 1000; kcat normalized_value=68 normalized_unit=s^-1; kcat/Km derived normalized_value=1014.9253731343283 normalized_unit=s^-1*mM^-1 from 68 / 0.067.

raw_value_unit_evidence: Table II ICDH row under Isocitrate reports Km 67 +/- 6 uM, kcat 68 +/- 3 s^-1, and rounded printed kcat/Km 1.0 x 10^6 s^-1 M^-1.

row_label: ICDH row / Isocitrate columns


organism: Hydrogenobacter thermophilus


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: D-threo-isocitrate

assay_conditions_summary: pH 7.6; buffer 100 mM TEA; cofactor NADP+

column_label: The paper states that Km values for D,L-isocitrate, DS-threo-isocitrate, and NADP(+) are 23, 12, and 24 uM, respectively.

raw_value_unit_evidence: Km raw_value=12 uM raw_unit=uM

row_label: C. glutamicum purified ICD / DS-threo-isocitrate

table_label: J. Bacteriol PDF PMID 7836312 page 780 / Purification and characterization of ICD

substrate: D-threo-isocitrate


raw_value_unit_evidence: Km raw_value=24 uM raw_unit=uM

row_label: C. glutamicum purified ICD / NADP(+)


enzyme_display_name: isocitrate dehydrogenase (NAD+)

organism: Methylococcus capsulatus

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

assay_conditions_summary: cofactor NAD+

proof_lines:
Methylococcus capsulatus
isocitrate dehydrogenase
NAD+-dependent

enzyme: isocitrate dehydrogenase (NAD+)


organism: Microcystis aeruginosa

substrate_name: DL-isocitrate

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

substrate: DL-isocitrate


organism: Bos taurus

substrate_name: D-fructose/L-sorbose

proof_lines: kcat is 29 sec(-1) for D-sorbitol oxidation (at pH 8.0). kcat is 26 sec(-1) for xylitol oxidation (at pH 8.0). kcat is 21 sec(-1) for L-iditol oxidation (at pH 8.0). kcat is 22 sec(-1) for ribitol oxidation (at pH 8.0). kcat is 24 sec(-1) f

substrate: D-fructose/L-sorbose


substrate_name: NADH

assay_conditions_summary: pH 7.4; cofactor NADH

substrate: NADH


organism: Caldococcus noboribetus

column_label: Abstract states apparent Km values were 72 and 43 microM for D,L-isocitrate and NADP, respectively.

raw_value_unit_evidence: Km raw_value=43 raw_unit=microM

row_label: Caldococcus noboribetus isocitrate dehydrogenase with NADP

table_label: PubMed abstract PMID 9252109


organism: Chlamydomonas reinhardtii

proof_lines: Purification and properties of isocitrate dehydrogenase (NADP)


organism: Archaeoglobus fulgidus

assay_conditions_summary: pH 8; 371.65 K; cofactor NADP+

column_label: Valid Springer PDF text, Table 5, AfIDH row, NADP+ columns: Km 16.5 uM, kcat 219.3 s^-1, kcat/Km 13.3 uM^-1 s^-1. Local text refs: supantha_download_20260707_2312_springer_text.txt lines 570-583 and per-page extraction page 10 lines 54-61.

normalized_value_unit_evidence: Paper Table 5 normalizes to Km 0.0165 mM, kcat 219.3 s^-1, and explicit kcat/Km 13300 s^-1*mM^-1. The export carries Km 0.017 mM, kcat 219.3 s^-1, and kcat/Km 12900 s^-1*mM^-1.

raw_value_unit_evidence: Table 5 AfIDH row reports NADP+ Km 16.5 uM, kcat 219.3 s^-1, and kcat/Km 13.3 uM^-1 s^-1.

row_label: AfIDH row; NADP+ columns

table_label: Table 5. Kinetics of chimers and wild-type enzymes


organism: Mycolicibacterium phlei

column_label: Abstract reports the Km values for isocitrate and NADP were 74 and 53 microM, respectively.

raw_value_unit_evidence: Km raw_value=53 microM raw_unit=microM

row_label: NADP-dependent isocitrate dehydrogenase / NADP

table_label: PubMed XML abstract PMID 3448153


organism: Methylobacillus flagellatus

assay_conditions_summary: pH 8.5; 315.15 K; cofactor NADP+


substrate_name: Oxalosuccinate

substrate: Oxalosuccinate


organism: Yarrowia lipolytica

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+


enzyme_display_name: Isocitrate dehydrogenase [NADP], mitochondrial

organism: Sus scrofa

substrate_name: manganese

smiles: [Mn]

substrate: manganese


enzyme_display_name: L-lactate dehydrogenase

organism: Lactiplantibacillus pentosus

substrate_name: pyruvate (at pH 5)

assay_conditions_summary: pH 5

enzyme: L-lactate dehydrogenase

substrate: pyruvate (at pH 5)


enzyme_display_name: malate dehydrogenase (decarboxylating)

organism: Arabidopsis thaliana

assay_conditions_summary: pH 6.4; cofactor CoA

proof_lines: pH 6.4, temperature not specified in the publication, NAD-ME1

proof_lines: pH 6.5, temperature not specified in the publication, NAD-MEH

proof_lines: pH 6.6, temperature not specified in the publication, NAD-ME2

enzyme: malate dehydrogenase (decarboxylating)


enzyme_display_name: Isocitrate dehydrogenase [NADP] cytoplasmic

organism: Homo sapiens

substrate_name: magnesium chloride

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

substrate: magnesium chloride


substrate_name: NADP(+)

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

column_label: Figure 2 kinetic parameter panel row KM,NADP+ (microM), WT column, reports 49.

raw_value_unit_evidence: Figure 2 lists WT KM,NADP+ = 49 microM for the oxidative reaction.

row_label: WT human IDH1 oxidative reaction / NADP+

table_label: PMC Figure 2 kinetic parameter panel, PMID 19935646

enzyme: Isocitrate dehydrogenase [NADP] cytoplasmic

substrate: NADP(+)


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature H133Q to reconstruct the assayed variant sequence.

proof_lines: kcat less than 0.016 s-1 or equal, mutant enzyme H133Q, at pH 7.5 and 37°C


assay_conditions_summary: pH 7.5; buffer Bis-Tris

proof_lines: wild type enzyme, in Bis-Tris buffer, at pH 6.2 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature A134D to reconstruct the assayed variant sequence.

proof_lines: kcat less than 0.019 s-1 or equal, mutant enzyme A134D, at pH 7.5 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R100Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132C to reconstruct the assayed variant sequence.


substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132C to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: Table 2. Kinetic parameters for the neomorphic reaction, conversion of alphaKG to D2HG, catalyzed by IDH1, row R132C IDH1, column Km,NADPH; Km, cell 0.01 mM, normalized 0.01 mM

normalized_value_unit_evidence: Km 0.01 mM

raw_value_unit_evidence: Km raw 0.01 mM from Table 2. Kinetic parameters for the neomorphic reaction, conversion of alphaKG to D2HG, catalyzed by IDH1

row_label: R132C IDH1

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132H to reconstruct the assayed variant sequence.

proof_lines: Km less than 0.025 mM or equal, mutant enzyme R132H, at pH 7.5 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132G to reconstruct the assayed variant sequence.

proof_lines: Km less than 0.025 mM, mutant enzyme R132G, at pH 7.5 and 37°C


proof_lines: Km less than 0.025 mM or equal, mutant enzyme R132C, at pH 7.5 and 21°C


proof_lines: Km less than 0.025 mM or equal, mutant enzyme R132G, at pH 7.5 and 21°C


assay_conditions_summary: pH 7.5; cofactor NADP+

column_label: Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row R132G IDH1, column Km,NADP+; Km, cell 0.067 mM, normalized 0.067 mM

raw_value_unit_evidence: Km raw 0.067 mM from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1

row_label: R132G IDH1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R100Q to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row R100Q IDH1, column Km,NADP+; Km, cell 0.07 mM, normalized 0.07 mM

normalized_value_unit_evidence: Km 0.07 mM

raw_value_unit_evidence: Km raw 0.07 mM from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1

row_label: R100Q IDH1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H133Q to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row H133Q IDH1, column Km,NADP+; Km, cell 0.101 mM, normalized 0.101 mM

raw_value_unit_evidence: Km raw 0.101 mM from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1

row_label: H133Q IDH1


column_label: Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row R132G IDH1, column Km,NADP+; Km, cell 0.14 mM, normalized 0.14 mM

normalized_value_unit_evidence: Km 0.14 mM

raw_value_unit_evidence: Km raw 0.14 mM from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1


column_label: Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row H133Q IDH1, column Km,NADP+; Km, cell 0.16 mM, normalized 0.16 mM

normalized_value_unit_evidence: Km 0.16 mM

raw_value_unit_evidence: Km raw 0.16 mM from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1


column_label: Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row R100Q IDH1, column Km,NADP+; Km, cell 0.18 mM, normalized 0.18 mM

normalized_value_unit_evidence: Km 0.18 mM

raw_value_unit_evidence: Km raw 0.18 mM from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1


column_label: Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row R132C IDH1, column Km,NADP+; Km, cell 0.58 mM, normalized 0.58 mM

normalized_value_unit_evidence: Km 0.58 mM

raw_value_unit_evidence: Km raw 0.58 mM from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A134D to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row A134D IDH1, column Km,NADP+; Km, cell 0.7 mM, normalized 0.7 mM

normalized_value_unit_evidence: Km 0.7 mM

raw_value_unit_evidence: Km raw 0.7 mM from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1

row_label: A134D IDH1


column_label: Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row R132C IDH1, column Km,NADP+; Km, cell 0.75 mM, normalized 0.75 mM

normalized_value_unit_evidence: Km 0.75 mM

raw_value_unit_evidence: Km raw 0.75 mM from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1


assay_conditions_summary: pH 7.5; buffer IDH1 assay; cofactor NADP+

column_label: Table 1; row R132H; column Km,NADP+ (21 C); substrate NADP+

normalized_value_unit_evidence: normalized: Km=1.0 mM

raw_value_unit_evidence: Table 1 row R132H cells: Km=1.0 +/- 0.9 mM


column_label: Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1, row A134D IDH1, column Km,NADP+; Km, cell 1.2 mM, normalized 1.2 mM

normalized_value_unit_evidence: Km 1.2 mM

raw_value_unit_evidence: Km raw 1.2 mM from Table 1. Kinetic parameters for the normal reaction, conversion of ICT to alphaKG, catalyzed by IDH1


column_label: Table 1; row R132H; column Km,NADP+ (37 C); substrate NADP+

normalized_value_unit_evidence: normalized: Km=1.6 mM

raw_value_unit_evidence: Table 1 row R132H cells: Km=1.6 +/- 0.5 mM


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198 (PMID:14512428) and applied mutation signature K212R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 and applied mutation signature Y140F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 and applied mutation signature Y140E to reconstruct the assayed variant sequence.


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

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


assay_conditions_summary: pH 7.4; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 and applied mutation signature Y140T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 and applied mutation signature Y140K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 and applied mutation signature K212Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 and applied mutation signature K212Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 and applied mutation signature K212R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D230C with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

proof_lines: D230C, alpha-subunit mutant, in 20 mM isocitrate and 1mM MnSO4


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D215N with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: D215N, gamma-subunit mutant, in 20 mM isocitrate and 1mM MnSO4


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature A134D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R100Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature H133Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132A to reconstruct the assayed variant sequence.


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


assay_conditions_summary: pH 7.5; 294.15 K; cofactor NADPH

proof_lines: Km less than 0.0025 mM or equal, mutant enzyme R100Q, at pH 7.5 and 21°C


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH


proof_lines: Km less than 0.005 mM or equal, mutant enzyme R132H, at pH 7.5 and 21°C


proof_lines: Km less than 0.01 mM or equal, wild type enzyme, at pH 7.5 and 37°C


organism: Acinetobacter baumannii

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

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

proof_lines: pH 8.0, 25°C, in presence of Mg2+, mutant enzyme S113A


proof_lines: pH 8.0, 25°C, in presence of Mg2+, mutant enzyme S113T


proof_lines: pH 8.0, 25°C, in presence of Mg2+, mutant enzyme S22E


proof_lines: pH 8.0, 25°C, in presence of Mg2+, mutant enzyme S113G


proof_lines: pH 8.0, 25°C, in presence of Mg2+, mutant enzyme S22A


proof_lines: pH 8.0, 25°C, in presence of Mg2+, mutant enzyme S22H


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

proof_lines: pH 8.0, 25°C, in presence of Mg2+, wild-type enzyme

proof_lines: pH 8.0, 25°C, in presence of Mn2+, wild-type enzyme


assay_conditions_summary: cofactor NADP+

proof_lines: in the presence of Mg2+, pH and temperature not specified in the publication

proof_lines: in the presence of Mn2+, pH and temperature not specified in the publication