sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 (PMID:15576556) and applied mutation signature N97A to reconstruct the assayed variant sequence.


enzyme_display_name: isocitrate dehydrogenase (NADP+)

organism: Sus scrofa

substrate_name: NADP+

source_db: brenda

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 (PMID:15576556) and applied mutation signature N97D to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

data_origin: experimental

enzyme: isocitrate dehydrogenase (NADP+)

substrate: NADP+

status: unverified

source: brenda


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 (PMID:15576556) and applied mutation signature T78A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 (PMID:15576556) and applied mutation signature S95A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 (PMID:15576556) and applied mutation signature T78D to reconstruct the assayed variant sequence.


substrate_name: isocitrate

substrate: isocitrate


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 (PMID:15576556) and applied mutation signature S95D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198 (PMID:15975917) and applied mutation signature T311N with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


substrate_name: DL-isocitrate

sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198 (PMID:15975917) and applied mutation signature T311S with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

substrate: DL-isocitrate


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198 (PMID:15975917) and applied mutation signature R83K with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198 (PMID:15975917) and applied mutation signature N328D with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198 (PMID:15975917) and applied mutation signature R83Q with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198 (PMID:15975917) and applied mutation signature N328S with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198 (PMID:15975917) and applied mutation signature T311A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


enzyme_display_name: isocitrate dehydrogenase (NAD+)

organism: Saccharomyces cerevisiae

substrate_name: D-isocitrate

mutation_signature: Unknown

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

proof_lines: octameric wild-type enzyme with AMP, without DTT, pH 7.4, 24°C

proof_lines: octameric wild-type enzyme with AMP and DTT, pH 7.4, 24°C

proof_lines: octameric wild-type enzyme without AMP, with DTT, pH 7.4, 24°C

enzyme: isocitrate dehydrogenase (NAD+)

substrate: D-isocitrate


sequence_variant_note: Mutation signature H2C could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: octameric enzyme mutant IDH1/IDH2C150S with AMP, with or without DTT, pH 7.4, 24°C


sequence_variant_note: Mutation signature H2C/C150S/C242S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: octameric enzyme mutant IDH1/IDH2C56S/C150S/C242S with AMP, without DTT, pH 7.4, 24°C


proof_lines: octameric enzyme mutant IDH1/IDH2C56S/C150S/C242S with AMP and DTT, pH 7.4, 24°C


sequence_variant_note: Mutation signature H2C/C242S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: octameric enzyme mutant IDH1/IDH2C56S/C242S with AMP and DTT, pH 7.4, 24°C


proof_lines: octameric enzyme mutant IDH1/IDH2C56S/C242S with AMP, without DTT, pH 7.4, 24°C


sequence_variant_note: Mutation signature H1G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: octameric enzyme IDH1G15D/IDH2 with AMP and DTT, pH 7.4, 24°C

proof_lines: octameric enzyme IDH1G15D/IDH2 with AMP, without DTT, pH 7.4, 24°C

proof_lines: octameric enzyme IDH1G15D/IDH2 without AMP, with DTT, pH 7.4, 24°C


proof_lines: octameric enzyme mutant IDH1/IDH2C150S without AMP and DTT, pH 7.4, 24°C


proof_lines: octameric enzyme mutant IDH1/IDH2C150S without AMP, with DTT, pH 7.4, 24°C


proof_lines: octameric enzyme mutant IDH1G15D/IDH2 without AMP and DTT, pH 7.4, 24°C


proof_lines: octameric enzyme mutant IDH1/IDH2C56S/C150S/C242S without AMP, with or without DTT, pH 7.4, 24°C


proof_lines: octameric enzyme mutant IDH1/IDH2C56S/C242S without AMP, with DTT, pH 7.4, 24°C


proof_lines: octameric enzyme mutant IDH1/IDH2C56S/C242S without AMP and DTT, pH 7.4, 24°C


organism: Haloferax volcanii

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R291S/K343D/Y344I/Y390P to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R291S/Y390P to reconstruct the assayed variant sequence.


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R291S/K343D/Y344I/V350A/Y390P to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R291S/K343D/Y390P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R291S to reconstruct the assayed variant sequence.


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


assay_conditions_summary: pH 8; cofactor NADP+


organism: Xylella fastidiosa

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


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

proof_lines: mutant enzymeD268K/I269Y/A275V, at pH 8.0 and 25°C


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


proof_lines: mutant enzyme D268K/I269Y, at pH 8.0 and 25°C


proof_lines: mutant enzyme K589T/H590L/R601L, at pH 8.0 and 25°C


proof_lines: mutant enzyme H590L/R601L, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198 and applied mutation signature D375N with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198 and applied mutation signature K260Q with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198 and applied mutation signature K260R with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.4; cofactor NAD+

proof_lines: pH 7.4, versus NADPH, recombinant wild-type enzyme and mutant Y316L


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


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198 and applied mutation signature T373S with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

column_label: Table 1 columns Enzyme and Km (NADP) (uM); uM converted to mM by dividing by 1000.

normalized_value_unit_evidence: Km 0.0055 mM for NADP.

raw_value_unit_evidence: Table 1 row T373S reports Km (NADP) 5.5 +/- 0.2 uM.

table_label: Table 1: Km values for NADP and Vmax values of wild-type and mutant isocitrate dehydrogenases

status: verified


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198 and applied mutation signature T373A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: Km 0.0062 mM for NADP.

raw_value_unit_evidence: Table 1 row T373A reports Km (NADP) 6.2 +/- 1.0 uM.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198 and applied mutation signature T373V with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: Km 0.0121 mM for NADP.

raw_value_unit_evidence: Table 1 row T373V reports Km (NADP) 12.1 +/- 1.1 uM.

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198 and applied mutation signature K374Q with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: Km 0.0154 mM for NADP.

raw_value_unit_evidence: Table 1 row K374Q reports Km (NADP) 15.4 +/- 1.0 uM.


organism: Homo sapiens

km_display: Not reported

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.

assay_conditions_summary: cofactor ADP

column_label: TABLE 4. Kinetic constants for isocitrate and ADP activation of wild type and mutant NAD-IDHs; row D234C / isocitrate; kcat column raw 0.27 s^-1 normalized 0.27 s^-1

row_label: D234C / isocitrate


assay_conditions_summary: pH 7.2; cofactor ADP

column_label: TABLE 4. Kinetic constants for isocitrate and ADP activation of wild type and mutant NAD-IDHs; row D234C / isocitrate; kcat column raw 0.27 s^-1 normalized 0.27 s^-1; Km column raw 3.4 mM normalized 3.4 mM; kcat/Km column raw 0.07 s^-1 mM^-1 normalized 0.07 s^-1 mM^-1


assay_conditions_summary: pH 7.2; cofactor NAD+

column_label: TABLE 3. Michaelis-Menten constants for Mn2+, Cd2+, and NAD of recombinant wild-type and mutant NAD-IDH; row D234C / NAD; kcat column raw 0.27 s^-1 normalized 0.27 s^-1; Km column raw 40 uM normalized 0.04 mM; kcat/Km column raw 0.007 s^-1 uM^-1 normalized 7.0 s^-1 mM^-1

row_label: D234C / NAD


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 4. Kinetic constants for isocitrate and ADP activation of wild type and mutant NAD-IDHs; row D230C / isocitrate; kcat column raw 2.49 s^-1 normalized 2.49 s^-1

row_label: D230C / isocitrate


column_label: TABLE 4. Kinetic constants for isocitrate and ADP activation of wild type and mutant NAD-IDHs; row D230C / isocitrate; kcat column raw 2.49 s^-1 normalized 2.49 s^-1; Km column raw 20.0 mM normalized 20.0 mM; kcat/Km column raw 0.09 s^-1 mM^-1 normalized 0.09 s^-1 mM^-1


column_label: TABLE 3. Michaelis-Menten constants for Mn2+, Cd2+, and NAD of recombinant wild-type and mutant NAD-IDH; row D230C / NAD; kcat column raw 2.49 s^-1 normalized 2.49 s^-1; Km column raw 1100 uM normalized 1.1 mM; kcat/Km column raw 0.002 s^-1 uM^-1 normalized 2.0 s^-1 mM^-1

row_label: D230C / NAD


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 4. Kinetic constants for isocitrate and ADP activation of wild type and mutant NAD-IDHs; row D215N / isocitrate; kcat column raw 11.8 s^-1 normalized 11.8 s^-1

row_label: D215N / isocitrate


column_label: TABLE 4. Kinetic constants for isocitrate and ADP activation of wild type and mutant NAD-IDHs; row D215N / isocitrate; kcat column raw 11.8 s^-1 normalized 11.8 s^-1; Km column raw 41.0 mM normalized 41.0 mM; kcat/Km column raw 0.29 s^-1 mM^-1 normalized 0.29 s^-1 mM^-1


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; kcat/Km column raw 0.062 s^-1 uM^-1 normalized 62.0 s^-1 mM^-1

row_label: D215N / NAD


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 4. Kinetic constants for isocitrate and ADP activation of wild type and mutant NAD-IDHs; row D217N / isocitrate; kcat column raw 19.6 s^-1 normalized 19.6 s^-1

row_label: D217N / isocitrate


column_label: TABLE 4. Kinetic constants for isocitrate and ADP activation of wild type and mutant NAD-IDHs; row D217N / isocitrate; kcat column raw 19.6 s^-1 normalized 19.6 s^-1; Km column raw 5.1 mM normalized 5.1 mM; kcat/Km column raw 3.58 s^-1 mM^-1 normalized 3.58 s^-1 mM^-1


column_label: TABLE 3. Michaelis-Menten constants for Mn2+, Cd2+, and NAD of recombinant wild-type and mutant NAD-IDH; row D217N / NAD; kcat column raw 19.6 s^-1 normalized 19.6 s^-1; Km column raw 680 uM normalized 0.68 mM; kcat/Km column raw 0.029 s^-1 uM^-1 normalized 29.0 s^-1 mM^-1

row_label: D217N / NAD


proof_lines: wild type enzyme in 20 mM isocitrate and 1 mM MnSO4

proof_lines: purified recombinant wild-type enzyme, pH 7.2, 25°C, in presence of 1 mM ADP


proof_lines: pH 7.2, 25°C, recombinant wild-type enzyme

proof_lines: purified recombinant wild-type enzyme, pH 7.2, 25°C


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 4. Kinetic constants for isocitrate and ADP activation of wild type and mutant NAD-IDHs; row D206N / isocitrate; kcat column raw 36.8 s^-1 normalized 36.8 s^-1

row_label: D206N / isocitrate


column_label: TABLE 4. Kinetic constants for isocitrate and ADP activation of wild type and mutant NAD-IDHs; row D206N / isocitrate; kcat column raw 36.8 s^-1 normalized 36.8 s^-1; Km column raw 3.5 mM normalized 3.5 mM; kcat/Km column raw 10.3 s^-1 mM^-1 normalized 10.3 s^-1 mM^-1


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; kcat/Km column raw 0.263 s^-1 uM^-1 normalized 263.0 s^-1 mM^-1

row_label: D206N / NAD


column_label: TABLE 4. Kinetic constants for isocitrate and ADP activation of wild type and mutant NAD-IDHs; row D234C / isocitrate; Km column raw 3.4 mM normalized 3.4 mM

normalized_value_unit_evidence: Km 3.4 mM

raw_value_unit_evidence: Km 3.4 mM


column_label: TABLE 4. Kinetic constants for isocitrate and ADP activation of wild type and mutant NAD-IDHs; row D206N / isocitrate; Km column raw 3.5 mM normalized 3.5 mM

normalized_value_unit_evidence: Km 3.5 mM

raw_value_unit_evidence: Km 3.5 mM


column_label: TABLE 4. Kinetic constants for isocitrate and ADP activation of wild type and mutant NAD-IDHs; row D217N / isocitrate; Km column raw 5.1 mM normalized 5.1 mM

normalized_value_unit_evidence: Km 5.1 mM

raw_value_unit_evidence: Km 5.1 mM


organism: Escherichia coli


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


substrate_name: NADPH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

substrate: NADPH


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+


sequence_variant_note: Mutation signature Y316F/K323Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.4, recombinant mutant Y316F and K323Q


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 (PMID:12054490) and applied mutation signature K321Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 (PMID:12054490) and applied mutation signature Y316F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 (PMID:12054490) and applied mutation signature K323Q with inferred residue-numbering offset -2 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


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 (PMID:12054490) and applied mutation signature Y316F/K321Q to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, recombinant mutant Y316F and K321Q


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 (PMID:12054490) and applied mutation signature Y316L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 (PMID:12054490) and applied mutation signature R314Q to reconstruct the assayed variant sequence.


ki_unit: mM

assay_conditions_summary: pH 7.4; cofactor NADPH

proof_lines: pH 7.4, versus NADPH, recombinant mutant R314Q


proof_lines: pH 7.4, versus NADPH, recombinant mutant Y316F


sequence_variant_note: Mutation signature R97Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 7.2; 298.15 K; cofactor NAD+

proof_lines: purified recombinant mutant gamma-R97Q, pH 7.2, 25°C


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

proof_lines: purified recombinant mutant beta-R99Q, pH 7.2, 25°C


proof_lines: purified recombinant wild-type enzyme and mutant beta-R99Q, pH 7.2, 25°C


assay_conditions_summary: pH 7.2; 298.15 K; cofactor ADP

proof_lines: purified recombinant mutant beta-R99Q, pH 7.2, 25°C, in presence of 1 mM ADP


proof_lines: purified recombinant mutant gamma-R97Q, pH 7.2, 25°C, in presence of 1 mM ADP


sequence_variant_note: Resolved canonical sequence from official_uniprot_accession_sequence_asset:O43837 and applied mutation signature Y137E with inferred residue-numbering offset +34 to reconstruct the assayed variant sequence.

column_label: Table 3 row betaY137E; column Km,isocitrate in presence of 1 mM ADP = 0.09 mM

raw_value_unit_evidence: Km raw_value=0.09 raw_unit=mM; table uncertainty=0.03 mM

table_label: Table 3. Kinetic parameters for wild-type and betaY137 mutants at pH 7.2


column_label: Table 3 row betaY137E; column Km,NAD = 0.09 mM

raw_value_unit_evidence: Km raw_value=0.09 raw_unit=mM; table uncertainty=0.02 mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_accession_sequence_asset:O43837 and applied mutation signature Y137F with inferred residue-numbering offset +34 to reconstruct the assayed variant sequence.

column_label: Table 3 row betaY137F; column Km,NAD = 0.12 mM

raw_value_unit_evidence: Km raw_value=0.12 raw_unit=mM; table uncertainty=0.02 mM


column_label: Table 3 row betaY137F; column Km,isocitrate in presence of 1 mM ADP = 0.28 mM

raw_value_unit_evidence: Km raw_value=0.28 raw_unit=mM; table uncertainty=0.03 mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_accession_sequence_asset:O43837 and applied mutation signature Y137S with inferred residue-numbering offset +34 to reconstruct the assayed variant sequence.

column_label: Table 3 row betaY137S; column Km,NAD = 0.63 mM

raw_value_unit_evidence: Km raw_value=0.63 raw_unit=mM; table uncertainty=0.13 mM


column_label: Table 3 row betaY137S; column Km,isocitrate in presence of 1 mM ADP = 0.92 mM

raw_value_unit_evidence: Km raw_value=0.92 raw_unit=mM; table uncertainty=0.38 mM


column_label: Table 3 row betaY137S; column Km,isocitrate = 1.2 mM

raw_value_unit_evidence: Km raw_value=1.2 raw_unit=mM; table uncertainty=0.2 mM


column_label: Table 3 row betaY137F; column Km,isocitrate = 1.8 mM

raw_value_unit_evidence: Km raw_value=1.8 raw_unit=mM; table uncertainty=0.3 mM


column_label: Table 3 row betaY137E; column Km,isocitrate = 3.4 mM

raw_value_unit_evidence: Km raw_value=3.4 raw_unit=mM; table uncertainty=0.6 mM


kcat_over_km_origin: calculated

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

assay_conditions_summary: pH 7.5; 310.15 K; buffer potassium phosphate

proof_lines: mutant enzyme R132H, in potassium phosphate buffer, at pH 7.5 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot:O75874 and applied mutation signature D273L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D273L, in potassium phosphate buffer, at pH 7.5 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot:O75874 and applied mutation signature D273S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D273S, in potassium phosphate buffer, at pH 7.5 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot:O75874 and applied mutation signature D273N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D273N, in potassium phosphate buffer, at pH 7.5 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot:O75874 and applied mutation signature K217Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K217Q, in potassium phosphate buffer, at pH 7.5 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot:O75874 and applied mutation signature K217M to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K217M, in potassium phosphate buffer, at pH 7.5 and 37°C


enzyme_display_name: phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating)

organism: Dicentrarchus labrax


assay_conditions_summary: pH 7.5; buffer Tris-HCl

column_label: Abstract reports Michaelis constants for NADP, 6-phosphogluconate, and Mg2+ as 0.88 microM, 26.66 microM, and 3.33 mM, respectively.

raw_value_unit_evidence: Km raw_value=3.33 mM raw_unit=mM

row_label: Bass liver 6-phosphogluconate dehydrogenase / Mg2+

table_label: PubMed XML abstract PMID 3355163

enzyme: phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating)


enzyme_display_name: phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating)

source_db: oed

source: oed


organism: Moorella thermoacetica

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A30E/R31I/T32D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 323.15 K; cofactor NADP+

column_label: Table 2, row 'A30E/R31I/T32D', NAD+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

table_label: Table 2

enzyme: phosphogluconate dehydrogenase (NADP(+)-dependent, decarboxylating)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31I/T32G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 323.15 K; cofactor NAD+

column_label: Table 2, row 'R31I/T32G', NAD+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

row_label: R31I/T32G / NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31T with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

column_label: Table 2, row 'R31T', NAD+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

row_label: R31T / NAD+


organism: Thermotoga maritima

sequence_source: multiple

sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature N32E/R33I/T34I to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 343.15 K; cofactor NAD+


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; 343.15 K; buffer 100 mM HEPES; cofactor NAD+

column_label: Table 1; row label: Wide-type; coenzyme column block: NAD+; Km (mM) NAD+ = 4.3 +/- 0.4; kcat (s^-1) NAD+ = 23.3 +/- 2.0; kcat/Km (mM^-1*s^-1) NAD+ = 5.4; normalized Km=4.3 mM, kcat=23.3 s^-1, kcat/Km=5.4 s^-1 mM^-1.

normalized_value_unit_evidence: normalized: Km=4.3 mM; kcat=23.3 s^-1; kcat/Km=5.4 s^-1 mM^-1

row_label: Mutation row: Wide-type; coenzyme column block: NAD+; metric columns: Km (mM), kcat (s^-1), kcat/Km (mM^-1*s^-1).

table_label: Table 1: Kinetics parameters of Tm6PGDH and its mutants


sequence_variant_note: Resolved canonical sequence from uniprotkb:O43837 and applied mutation signature D192N with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, beta-subunit mutant enzyme D192N


sequence_variant_note: Resolved canonical sequence from uniprotkb:P50213 and applied mutation signature D181N with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, alpha-subunit mutant enzyme D181N


sequence_variant_note: Mutation signature D190N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.2, gamma-subunit mutant enzyme D190N


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

assay_conditions_summary: cofactor NADP+

proof_lines: recombinant mutant R132C IDH1, pH not specified in the publication, temperature not specified in the publication


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

proof_lines: recombinant mutant R132H IDH1, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprotkb:O75874 and applied mutation signature R132S to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant R132S IDH1, pH not specified in the publication, temperature not specified in the publication


organism: Yarrowia lipolytica

sequence_variant_note: Resolved canonical sequence from uniprotkb:Q6C2Y4 and applied mutation signature R322D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; cofactor NADP+


assay_conditions_summary: pH 7.5; cofactor NADP+

proof_lines: pH 7.5, 25°C, recombinant mutant R322D, with Mg2+


proof_lines: pH 7.5, 25°C, recombinant wild-type enzyme, with Mg2+


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

proof_lines: pH 7.5, 25°C, recombinant enzyme, with Mg2+


proof_lines: pH 7.5, 25°C, recombinant enzyme, with Mn2+


proof_lines: pH 7.5, 25°C, recombinant enzyme mutant R322D


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 and applied mutation signature H319Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P33198#chain:9-421 and applied mutation signature H315Q to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+


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


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


substrate_name: D,L-isocitrate

substrate: D,L-isocitrate


assay_conditions_summary: cofactor NADPH


substrate_name: oxalosuccinate

proof_lines: reductase decarboxylase

substrate: oxalosuccinate


enzyme_display_name: phosphogluconate 2-dehydrogenase

organism: Burkholderia cepacia

proof_lines: isoform specific for NADP+ and isoform active with NAD+, with NADP+ as cofactor

proof_lines: isoform specific for NADP+, with NADP+ as cofactor, glucose grown bacteria

proof_lines: isoform specific for NADP+, with NADP+ as cofactor, 5 mM ATP, glucose grown bacteria

enzyme: phosphogluconate 2-dehydrogenase


proof_lines: enzyme active with NAD+ and NADP+-specific enzyme


assay_conditions_summary: cofactor NAD+


organism: Avena fatua

proof_lines:
source endosperm
source embryo


proof_lines:
source embryo
source endosperm


organism: Zea mays

proof_lines:
7.5 mM MgCl2
0.01 mM NADPH


proof_lines:
7.5 mM MgCl2
1 mM MnCl2
0.01 mM NADPH


organism: Candida tropicalis


organism: Ricinus communis

proof_lines:
cytosolic isoenzyme
proplastid isoenzyme


proof_lines:
proplastid isoenzyme
cytosolic isoenzyme


organism: Catharanthus roseus

proof_lines:
cytosolic isoenzyme
plastid isoenzyme


organism: Corynebacterium glutamicum

substrate_name: NADP+; 6-Phospho-D-gluconate

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

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

substrate: NADP+; 6-Phospho-D-gluconate


organism: Arthrospira platensis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T35S to reconstruct the assayed variant sequence.


organism: Burkholderia multivorans

substrate_name: NAD+; 6-Phospho-D-gluconate

substrate: NAD+; 6-Phospho-D-gluconate


organism: Beta vulgaris


organism: Corylus avellana


organism: Strongylocentrotus purpuratus

proof_lines:
homogenates
permeabilized cells


organism: Pseudomonas fluorescens

proof_lines:
with NADPH as coenzyme
with NADH as coenzyme


organism: Homo sapiens

substrate_name: Unknown

proof_lines: 25°C, pH 8.0, non-competitive inhibition

substrate: Unknown


organism: Petroselinum crispum


organism: [Candida] boidinii


organism: Gryllus firmus


organism: Glycine max


substrate_name: 6-Phospho-D-gluconate; NADP+

substrate: 6-Phospho-D-gluconate; NADP+


organism: Lathyrus oleraceus


organism: Spinacia oleracea

proof_lines:
isoenzyme 2
isoenzyme 1


organism: Neomoorella thermoacetica

sequence_variant_note: Resolved canonical sequence from package_asset_fasta:uniprot_A0A1J5NX54_canonical.fasta and applied mutation signature A30D/R31I/T32I to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetics parameters of 6PGDH and mutants.), body row 'A30D/R31I/T32I'; column 'Km' under coenzyme NADP+ = 228 micromolar; column 'kcat' under coenzyme NADP+ = 1.81 s^-1; column 'kcat/Km' under coenzyme NADP+ = 7.9 mM^-1*s^-1; the final column 'Ratio kcat/Km NAD+/NADP+' is a cross-coenzyme selectivity figure for the whole table row.

normalized_value_unit_evidence: Km: printed Table 2 cell 228 in the column head unit micromolar; 228 / 1000 = 0.228 mM, and the exported value is 0.228 mM. kcat: printed Table 2 cell 1.81 s^-1; the column head prints reciprocal seconds, so no conversion is applied and the exported value is 1.81 s^(-1). kcat/Km: printed Table 2 cell 7.9 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 7.9 s^(-1)*mM^(-1), while the exported ratio is 7.93859649122807.

raw_value_unit_evidence: Table 2, body row 'A30D/R31I/T32I', coenzyme NADP+ columns: Km = 228 micromolar; kcat = 1.81 s^-1; printed kcat/Km = 7.9 mM^-1*s^-1.

row_label: Table 2, body row 'A30D/R31I/T32I', coenzyme NADP+ cell group

table_label: Table 2: Kinetics parameters of 6PGDH and mutants. (Scientific Reports 2016, volume 6, article 32644)


sequence_variant_note: Resolved canonical sequence from package_asset_fasta:uniprot_A0A1J5NX54_canonical.fasta and applied mutation signature A30E/R31I/T32D to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetics parameters of 6PGDH and mutants.), body row 'A30E/R31I/T32D'; column 'Km' under coenzyme NADP+ = 660 micromolar; column 'kcat' under coenzyme NADP+ = 3.1 s^-1; column 'kcat/Km' under coenzyme NADP+ = 4.7 mM^-1*s^-1; the final column 'Ratio kcat/Km NAD+/NADP+' is a cross-coenzyme selectivity figure for the whole table row.

normalized_value_unit_evidence: Km: printed Table 2 cell 660 in the column head unit micromolar; 660 / 1000 = 0.66 mM, and the exported value is 0.66 mM. kcat: printed Table 2 cell 3.1 s^-1; the column head prints reciprocal seconds, so no conversion is applied and the exported value is 3.1 s^(-1). kcat/Km: printed Table 2 cell 4.7 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 4.7 s^(-1)*mM^(-1), while the exported ratio is 4.696969696969697.

raw_value_unit_evidence: Table 2, body row 'A30E/R31I/T32D', coenzyme NADP+ columns: Km = 660 micromolar; kcat = 3.1 s^-1; printed kcat/Km = 4.7 mM^-1*s^-1.

row_label: Table 2, body row 'A30E/R31I/T32D', coenzyme NADP+ cell group


column_label: Table 2 (Kinetics parameters of 6PGDH and mutants.), body row 'A30D/R31I/T32I'; column 'Km' under coenzyme NAD+ = 11.87 micromolar; column 'kcat' under coenzyme NAD+ = 5.75 s^-1; column 'kcat/Km' under coenzyme NAD+ = 484.2 mM^-1*s^-1; the final column 'Ratio kcat/Km NAD+/NADP+' is a cross-coenzyme selectivity figure for the whole table row.

normalized_value_unit_evidence: Km: printed Table 2 cell 11.87 in the column head unit micromolar; 11.87 / 1000 = 0.01187 mM, and the exported value is 0.01187 mM. kcat: printed Table 2 cell 5.75 s^-1; the column head prints reciprocal seconds, so no conversion is applied and the exported value is 5.75 s^(-1). kcat/Km: printed Table 2 cell 484.2 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 484.2 s^(-1)*mM^(-1), while the exported ratio is 484.41449031171015.

raw_value_unit_evidence: Table 2, body row 'A30D/R31I/T32I', coenzyme NAD+ columns: Km = 11.87 micromolar; kcat = 5.75 s^-1; printed kcat/Km = 484.2 mM^-1*s^-1.

row_label: Table 2, body row 'A30D/R31I/T32I', coenzyme NAD+ cell group


sequence_variant_note: Resolved canonical sequence from package_asset_fasta:uniprot_A0A1J5NX54_canonical.fasta and applied mutation signature A30C/R31I/T32K to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetics parameters of 6PGDH and mutants.), body row 'A30C/R31I/T32K'; column 'Km' under coenzyme NAD+ = 404 micromolar; column 'kcat' under coenzyme NAD+ = 6.0 s^-1; column 'kcat/Km' under coenzyme NAD+ = 14.8 mM^-1*s^-1; the final column 'Ratio kcat/Km NAD+/NADP+' is a cross-coenzyme selectivity figure for the whole table row.

normalized_value_unit_evidence: Km: printed Table 2 cell 404 in the column head unit micromolar; 404 / 1000 = 0.404 mM, and the exported value is 0.404 mM. kcat: printed Table 2 cell 6.0 s^-1; the column head prints reciprocal seconds, so no conversion is applied and the exported value is 6.0 s^(-1). kcat/Km: printed Table 2 cell 14.8 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 14.8 s^(-1)*mM^(-1), while the exported ratio is 14.85148514851485.

raw_value_unit_evidence: Table 2, body row 'A30C/R31I/T32K', coenzyme NAD+ columns: Km = 404 micromolar; kcat = 6.0 s^-1; printed kcat/Km = 14.8 mM^-1*s^-1.

row_label: Table 2, body row 'A30C/R31I/T32K', coenzyme NAD+ cell group


column_label: Table 2 (Kinetics parameters of 6PGDH and mutants.), body row 'A30C/R31I/T32K'; column 'Km' under coenzyme NADP+ = 698 micromolar; column 'kcat' under coenzyme NADP+ = 6.23 s^-1; column 'kcat/Km' under coenzyme NADP+ = 8.9 mM^-1*s^-1; the final column 'Ratio kcat/Km NAD+/NADP+' is a cross-coenzyme selectivity figure for the whole table row.

normalized_value_unit_evidence: Km: printed Table 2 cell 698 in the column head unit micromolar; 698 / 1000 = 0.698 mM, and the exported value is 0.698 mM. kcat: printed Table 2 cell 6.23 s^-1; the column head prints reciprocal seconds, so no conversion is applied and the exported value is 6.23 s^(-1). kcat/Km: printed Table 2 cell 8.9 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 8.9 s^(-1)*mM^(-1), while the exported ratio is 8.925501432664758.

raw_value_unit_evidence: Table 2, body row 'A30C/R31I/T32K', coenzyme NADP+ columns: Km = 698 micromolar; kcat = 6.23 s^-1; printed kcat/Km = 8.9 mM^-1*s^-1.

row_label: Table 2, body row 'A30C/R31I/T32K', coenzyme NADP+ cell group


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

column_label: Table 2 (Kinetics parameters of 6PGDH and mutants.), body row 'WT'; column 'Km' under coenzyme NADP+ = 13.9 micromolar; column 'kcat' under coenzyme NADP+ = 8.73 s^-1; column 'kcat/Km' under coenzyme NADP+ = 628.8 mM^-1*s^-1; the final column 'Ratio kcat/Km NAD+/NADP+' is a cross-coenzyme selectivity figure for the whole table row.

normalized_value_unit_evidence: Km: printed Table 2 cell 13.9 in the column head unit micromolar; 13.9 / 1000 = 0.0139 mM, and the exported value is 0.0139 mM. kcat: printed Table 2 cell 8.73 s^-1; the column head prints reciprocal seconds, so no conversion is applied and the exported value is 8.73 s^(-1). kcat/Km: printed Table 2 cell 628.8 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 628.8 s^(-1)*mM^(-1), while the exported ratio is 628.0575539568346.

raw_value_unit_evidence: Table 2, body row 'WT', coenzyme NADP+ columns: Km = 13.9 micromolar; kcat = 8.73 s^-1; printed kcat/Km = 628.8 mM^-1*s^-1.

row_label: Table 2, body row 'WT', coenzyme NADP+ cell group


sequence_variant_note: Resolved canonical sequence from package_asset_fasta:uniprot_A0A1J5NX54_canonical.fasta and applied mutation signature R31T to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetics parameters of 6PGDH and mutants.), body row 'R31T'; column 'Km' under coenzyme NAD+ = 605 micromolar; column 'kcat' under coenzyme NAD+ = 9.12 s^-1; column 'kcat/Km' under coenzyme NAD+ = 15 mM^-1*s^-1; the final column 'Ratio kcat/Km NAD+/NADP+' is a cross-coenzyme selectivity figure for the whole table row.

normalized_value_unit_evidence: Km: printed Table 2 cell 605 in the column head unit micromolar; 605 / 1000 = 0.605 mM, and the exported value is 0.605 mM. kcat: printed Table 2 cell 9.12 s^-1; the column head prints reciprocal seconds, so no conversion is applied and the exported value is 9.12 s^(-1). kcat/Km: printed Table 2 cell 15 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 15.0 s^(-1)*mM^(-1), while the exported ratio is 15.074380165289256.

raw_value_unit_evidence: Table 2, body row 'R31T', coenzyme NAD+ columns: Km = 605 micromolar; kcat = 9.12 s^-1; printed kcat/Km = 15 mM^-1*s^-1.

row_label: Table 2, body row 'R31T', coenzyme NAD+ cell group


column_label: Table 2 (Kinetics parameters of 6PGDH and mutants.), body row 'A30E/R31I/T32D'; column 'Km' under coenzyme NAD+ = 127 micromolar; column 'kcat' under coenzyme NAD+ = 10.8 s^-1; column 'kcat/Km' under coenzyme NAD+ = 85.1 mM^-1*s^-1; the final column 'Ratio kcat/Km NAD+/NADP+' is a cross-coenzyme selectivity figure for the whole table row.

normalized_value_unit_evidence: Km: printed Table 2 cell 127 in the column head unit micromolar; 127 / 1000 = 0.127 mM, and the exported value is 0.127 mM. kcat: printed Table 2 cell 10.8 s^-1; the column head prints reciprocal seconds, so no conversion is applied and the exported value is 10.8 s^(-1). kcat/Km: printed Table 2 cell 85.1 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 85.1 s^(-1)*mM^(-1), while the exported ratio is 85.03937007874016.

raw_value_unit_evidence: Table 2, body row 'A30E/R31I/T32D', coenzyme NAD+ columns: Km = 127 micromolar; kcat = 10.8 s^-1; printed kcat/Km = 85.1 mM^-1*s^-1.

row_label: Table 2, body row 'A30E/R31I/T32D', coenzyme NAD+ cell group


column_label: Table 2 (Kinetics parameters of 6PGDH and mutants.), body row 'R31T'; column 'Km' under coenzyme NADP+ = 35.5 micromolar; column 'kcat' under coenzyme NADP+ = 10.83 s^-1; column 'kcat/Km' under coenzyme NADP+ = 305.6 mM^-1*s^-1; the final column 'Ratio kcat/Km NAD+/NADP+' is a cross-coenzyme selectivity figure for the whole table row.

normalized_value_unit_evidence: Km: printed Table 2 cell 35.5 in the column head unit micromolar; 35.5 / 1000 = 0.0355 mM, and the exported value is 0.0355 mM. kcat: printed Table 2 cell 10.83 s^-1; the column head prints reciprocal seconds, so no conversion is applied and the exported value is 10.83 s^(-1). kcat/Km: printed Table 2 cell 305.6 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 305.6 s^(-1)*mM^(-1), while the exported ratio is 305.0704225352113.

raw_value_unit_evidence: Table 2, body row 'R31T', coenzyme NADP+ columns: Km = 35.5 micromolar; kcat = 10.83 s^-1; printed kcat/Km = 305.6 mM^-1*s^-1.

row_label: Table 2, body row 'R31T', coenzyme NADP+ cell group


sequence_variant_note: Resolved canonical sequence from package_asset_fasta:uniprot_A0A1J5NX54_canonical.fasta and applied mutation signature R31I to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetics parameters of 6PGDH and mutants.), body row 'R31I'; column 'Km' under coenzyme NADP+ = 26.5 micromolar; column 'kcat' under coenzyme NADP+ = 11.53 s^-1; column 'kcat/Km' under coenzyme NADP+ = 435.0 mM^-1*s^-1; the final column 'Ratio kcat/Km NAD+/NADP+' is a cross-coenzyme selectivity figure for the whole table row.

normalized_value_unit_evidence: Km: printed Table 2 cell 26.5 in the column head unit micromolar; 26.5 / 1000 = 0.0265 mM, and the exported value is 0.0265 mM. kcat: printed Table 2 cell 11.53 s^-1; the column head prints reciprocal seconds, so no conversion is applied and the exported value is 11.53 s^(-1). kcat/Km: printed Table 2 cell 435.0 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 435.0 s^(-1)*mM^(-1), while the exported ratio is 435.0943396226415.

raw_value_unit_evidence: Table 2, body row 'R31I', coenzyme NADP+ columns: Km = 26.5 micromolar; kcat = 11.53 s^-1; printed kcat/Km = 435.0 mM^-1*s^-1.

row_label: Table 2, body row 'R31I', coenzyme NADP+ cell group


sequence_variant_note: Resolved canonical sequence from package_asset_fasta:uniprot_A0A1J5NX54_canonical.fasta and applied mutation signature R31I/T32G to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetics parameters of 6PGDH and mutants.), body row 'R31I/T32G'; column 'Km' under coenzyme NADP+ = 104.4 micromolar; column 'kcat' under coenzyme NADP+ = 11.9 s^-1; column 'kcat/Km' under coenzyme NADP+ = 114.0 mM^-1*s^-1; the final column 'Ratio kcat/Km NAD+/NADP+' is a cross-coenzyme selectivity figure for the whole table row.

normalized_value_unit_evidence: Km: printed Table 2 cell 104.4 in the column head unit micromolar; 104.4 / 1000 = 0.1044 mM, and the exported value is 0.1044 mM. kcat: printed Table 2 cell 11.9 s^-1; the column head prints reciprocal seconds, so no conversion is applied and the exported value is 11.9 s^(-1). kcat/Km: printed Table 2 cell 114.0 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 114.0 s^(-1)*mM^(-1), while the exported ratio is 113.98467432950191.

raw_value_unit_evidence: Table 2, body row 'R31I/T32G', coenzyme NADP+ columns: Km = 104.4 micromolar; kcat = 11.9 s^-1; printed kcat/Km = 114.0 mM^-1*s^-1.

row_label: Table 2, body row 'R31I/T32G', coenzyme NADP+ cell group


column_label: Table 2 (Kinetics parameters of 6PGDH and mutants.), body row 'WT'; column 'Km' under coenzyme NAD+ = 1397 micromolar; column 'kcat' under coenzyme NAD+ = 12.6 s^-1; column 'kcat/Km' under coenzyme NAD+ = 9.0 mM^-1*s^-1; the final column 'Ratio kcat/Km NAD+/NADP+' is a cross-coenzyme selectivity figure for the whole table row.

normalized_value_unit_evidence: Km: printed Table 2 cell 1397 in the column head unit micromolar; 1397 / 1000 = 1.397 mM, and the exported value is 1.397 mM. kcat: printed Table 2 cell 12.6 s^-1; the column head prints reciprocal seconds, so no conversion is applied and the exported value is 12.6 s^(-1). kcat/Km: printed Table 2 cell 9.0 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 9.0 s^(-1)*mM^(-1), while the exported ratio is 9.019327129563349.

raw_value_unit_evidence: Table 2, body row 'WT', coenzyme NAD+ columns: Km = 1397 micromolar; kcat = 12.6 s^-1; printed kcat/Km = 9.0 mM^-1*s^-1.

row_label: Table 2, body row 'WT', coenzyme NAD+ cell group


column_label: Table 2 (Kinetics parameters of 6PGDH and mutants.), body row 'R31I/T32G'; column 'Km' under coenzyme NAD+ = 362 micromolar; column 'kcat' under coenzyme NAD+ = 12.94 s^-1; column 'kcat/Km' under coenzyme NAD+ = 35.8 mM^-1*s^-1; the final column 'Ratio kcat/Km NAD+/NADP+' is a cross-coenzyme selectivity figure for the whole table row.

normalized_value_unit_evidence: Km: printed Table 2 cell 362 in the column head unit micromolar; 362 / 1000 = 0.362 mM, and the exported value is 0.362 mM. kcat: printed Table 2 cell 12.94 s^-1; the column head prints reciprocal seconds, so no conversion is applied and the exported value is 12.94 s^(-1). kcat/Km: printed Table 2 cell 35.8 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 35.8 s^(-1)*mM^(-1), while the exported ratio is 35.74585635359116.

raw_value_unit_evidence: Table 2, body row 'R31I/T32G', coenzyme NAD+ columns: Km = 362 micromolar; kcat = 12.94 s^-1; printed kcat/Km = 35.8 mM^-1*s^-1.

row_label: Table 2, body row 'R31I/T32G', coenzyme NAD+ cell group


column_label: Table 2 (Kinetics parameters of 6PGDH and mutants.), body row 'R31I'; column 'Km' under coenzyme NAD+ = 354 micromolar; column 'kcat' under coenzyme NAD+ = 15.01 s^-1; column 'kcat/Km' under coenzyme NAD+ = 42.4 mM^-1*s^-1; the final column 'Ratio kcat/Km NAD+/NADP+' is a cross-coenzyme selectivity figure for the whole table row.

normalized_value_unit_evidence: Km: printed Table 2 cell 354 in the column head unit micromolar; 354 / 1000 = 0.354 mM, and the exported value is 0.354 mM. kcat: printed Table 2 cell 15.01 s^-1; the column head prints reciprocal seconds, so no conversion is applied and the exported value is 15.01 s^(-1). kcat/Km: printed Table 2 cell 42.4 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 42.4 s^(-1)*mM^(-1), while the exported ratio is 42.40112994350282.

raw_value_unit_evidence: Table 2, body row 'R31I', coenzyme NAD+ columns: Km = 354 micromolar; kcat = 15.01 s^-1; printed kcat/Km = 42.4 mM^-1*s^-1.

row_label: Table 2, body row 'R31I', coenzyme NAD+ cell group


organism: Synechocystis sp.

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S42T with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 305.15 K; cofactor NAD+


assay_conditions_summary: pH 7.3; cofactor NAD+

column_label: The literal NAD+ / Sy6PGDH row binds the wild-type enzyme, coenzyme, no-inhibitor state, Km, kcat, and printed efficiency. The current quotient differs only by stored precision and is derived from the exact same-row kcat and Km cells.

normalized_value_unit_evidence: kcat=4.89 s^-1; Km=4.46 mM; current same-row quotient=1.0964125560538116 s^-1 mM^-1; printed efficiency=1.10 s^-1 mM^-1.

raw_value_unit_evidence: NAD+ Sy6PGDH row: Km 4.46 ± 0.55 mM; kcat 4.89 ± 0.54 s^-1; printed kcat/Km 1.10 ± 0.08 s^-1 mM^-1.

row_label: NAD+ / Sy6PGDH / no inhibitor

table_label: Table 1: Kinetic parameters of cyanobacterial 6PGDHs for 6PG and coenzymes


assay_conditions_summary: pH 7.3; 305.15 K; cofactor NADP+


assay_conditions_summary: pH 7.3; cofactor NADP+

column_label: The literal 6PG / Sy6PGDH row binds the wild-type enzyme, substrate, no-inhibitor state, Km, kcat, and printed efficiency. The current quotient differs only by stored precision and is derived from the exact same-row kcat and Km cells.

row_label: 6PG / Sy6PGDH / no inhibitor


column_label: The literal NADP+ / Sy6PGDH row binds the wild-type enzyme, coenzyme, no-inhibitor state, Km, kcat, and printed efficiency. The current quotient differs only by stored precision and is derived from the exact same-row kcat and Km cells.

raw_value_unit_evidence: NADP+ Sy6PGDH row: Km 0.058 ± 0.003 mM; kcat 69.9 ± 5.5 s^-1; printed kcat/Km 1,207 ± 87 s^-1 mM^-1.

row_label: NADP+ / Sy6PGDH / no inhibitor


organism: Thermotoga maritima

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N32D/R33I/T34I to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 343.15 K; cofactor NADP+

proof_lines: mutant enzyme N32D/R33I/T34I, at pH 7.5 and 70°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N32E/R33I/T34I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N32E/R33I/T34I, at pH 7.5 and 70°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9WYR9 and applied mutation signature N32D to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetics parameters of Tm6PGDH and its mutants.), body row 'N32D'; column 'Km (mM)' under coenzyme NADP+ = 2.3; column 'kcat (s^-1)' under coenzyme NADP+ = 16.7; column 'kcat/Km (mM^-1*s^-1)' under coenzyme NADP+ = 7.3.

normalized_value_unit_evidence: Km: printed Table 1 cell 2.3 mM; the column head prints mM, so no conversion is applied and the exported value is 2.3 mM. kcat: printed Table 1 cell 16.7 s^-1; the column head prints s^-1 and no conversion is applied, and the exported value is 16.7 s^(-1). kcat/Km: printed Table 1 cell 7.3 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 7.3 s^(-1)*mM^(-1), while the exported ratio is 7.260869565217392.

raw_value_unit_evidence: Table 1, body row 'N32D', coenzyme NADP+ columns: Km = 2.3 mM; kcat = 16.7 s^-1; printed kcat/Km = 7.3 mM^-1*s^-1.

row_label: Table 1, body row 'N32D', coenzyme NADP+ cell group

table_label: Table 1: Kinetics parameters of Tm6PGDH and its mutants. (Scientific Reports 2016, volume 6, article 36311)


column_label: Table 1 (Kinetics parameters of Tm6PGDH and its mutants.), body row 'Wide-type'; column 'Km (mM)' under coenzyme NADP+ = 0.005; column 'kcat (s^-1)' under coenzyme NADP+ = 17.6; column 'kcat/Km (mM^-1*s^-1)' under coenzyme NADP+ = 3520.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.005 mM; the column head prints mM, so no conversion is applied and the exported value is 0.005 mM. kcat: printed Table 1 cell 17.6 s^-1; the column head prints s^-1 and no conversion is applied, and the exported value is 17.6 s^(-1). kcat/Km: printed Table 1 cell 3520 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 3520.0 s^(-1)*mM^(-1), while the exported ratio is 3520.0.

raw_value_unit_evidence: Table 1, body row 'Wide-type', coenzyme NADP+ columns: Km = 0.005 mM; kcat = 17.6 s^-1; printed kcat/Km = 3520 mM^-1*s^-1.

row_label: Table 1, body row 'Wide-type', coenzyme NADP+ cell group


column_label: Table 1 (Kinetics parameters of Tm6PGDH and its mutants.), body row 'Wide-type'; column 'Km (mM)' under coenzyme NAD+ = 4.3; column 'kcat (s^-1)' under coenzyme NAD+ = 23.3; column 'kcat/Km (mM^-1*s^-1)' under coenzyme NAD+ = 5.4.

normalized_value_unit_evidence: Km: printed Table 1 cell 4.3 mM; the column head prints mM, so no conversion is applied and the exported value is 4.3 mM. kcat: printed Table 1 cell 23.3 s^-1; the column head prints s^-1 and no conversion is applied, and the exported value is 23.3 s^(-1). kcat/Km: printed Table 1 cell 5.4 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 5.4 s^(-1)*mM^(-1), while the exported ratio is 5.418604651162791.

raw_value_unit_evidence: Table 1, body row 'Wide-type', coenzyme NAD+ columns: Km = 4.3 mM; kcat = 23.3 s^-1; printed kcat/Km = 5.4 mM^-1*s^-1.

row_label: Table 1, body row 'Wide-type', coenzyme NAD+ cell group


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N32D/R33L/T34S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N32D/R33L/T34S, at pH 7.5 and 70°C


column_label: Table 1 (Kinetics parameters of Tm6PGDH and its mutants.), body row 'N32D'; column 'Km (mM)' under coenzyme NAD+ = 4.0; column 'kcat (s^-1)' under coenzyme NAD+ = 29.3; column 'kcat/Km (mM^-1*s^-1)' under coenzyme NAD+ = 7.3.

normalized_value_unit_evidence: Km: printed Table 1 cell 4.0 mM; the column head prints mM, so no conversion is applied and the exported value is 4.0 mM. kcat: printed Table 1 cell 29.3 s^-1; the column head prints s^-1 and no conversion is applied, and the exported value is 29.3 s^(-1). kcat/Km: printed Table 1 cell 7.3 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 7.3 s^(-1)*mM^(-1), while the exported ratio is 7.325.

raw_value_unit_evidence: Table 1, body row 'N32D', coenzyme NAD+ columns: Km = 4.0 mM; kcat = 29.3 s^-1; printed kcat/Km = 7.3 mM^-1*s^-1.

row_label: Table 1, body row 'N32D', coenzyme NAD+ cell group


proof_lines: Km above 100 mM, mutant enzyme N32D/R33L/T34S, at pH 7.5 and 70°C


assay_conditions_summary: pH 7.5; 353.15 K; cofactor NADPH


assay_conditions_summary: pH 7.5; 353.15 K; cofactor NADP+


organism: Ctenopharyngodon idella

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


organism: Limnospira platensis


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T35S with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt Q8IKT2

organism: Plasmodium falciparum

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q8IKT2

source: skid


organism: Cyberlindnera jadinii

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

assay_conditions_summary: pH 7

proof_lines: dimeric enzyme with two 6-phospho-D-gluconate bound, pH not specified in the publication, temperature not specified in the publication


assay_conditions_summary: pH 7; 303.15 K; cofactor NAD+


enzyme_display_name: L-iditol 2-dehydrogenase

substrate_name: xylitol

source_db: uniprot

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

assay_conditions_summary: pH 10

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: xylitol

source: uniprot


substrate_name: L-threitol

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

substrate: L-threitol


smiles: CC(C(C)O)O


enzyme_display_name: UniProt P52209

proof_lines:
Raw SKiD Env: Temp=22°C, pH=7.5
Raw SKiD Env: Temp=25°C, pH=8

enzyme: UniProt P52209


assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADP+


enzyme_display_name: UniProt P00349

organism: Ovis aries

enzyme: UniProt P00349


assay_conditions_summary: cofactor NADP+


enzyme_display_name: UniProt P00350

organism: Escherichia coli

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

source_databases_merged: skid uniprot

enzyme: UniProt P00350


enzyme_display_name: UniProt P38720

organism: Saccharomyces cerevisiae

enzyme: UniProt P38720


organism: Moorella thermoacetica

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A30C/R31I/T32K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 323.15 K; buffer 100 mM HEPES; cofactor NAD+

column_label: Table 2, row 'A30C/R31I/T32K', NAD+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A30D/R31I/T32I to reconstruct the assayed variant sequence.

column_label: Table 2, row 'A30D/R31I/T32I', NAD+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 2, row 'R31I', NAD+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

row_label: R31I / NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31T with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 2, row 'R31T', NAD+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

row_label: R31T / NAD+


column_label: Table 2; row label: WT; coenzyme column block: NAD+; Km [uM] = 1397 +/- 111; kcat [s^-1] = 12.6 +/- 0.4; kcat/Km [mM^-1 s^-1] = 9.0; normalized Km=1.397 mM, kcat=12.6 s^-1, kcat/Km=9 s^-1 mM^-1.

normalized_value_unit_evidence: normalized: Km=1.397 mM; kcat=12.6 s^-1; kcat/Km=9 s^-1 mM^-1

row_label: Mutation row: WT; coenzyme column block: NAD+; metric columns: Km [uM], kcat [s^-1], kcat/Km [mM^-1 s^-1].

table_label: Table 2: Kinetics parameters of 6PGDH and mutants


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A30E/R31I/T32D to reconstruct the assayed variant sequence.

column_label: Table 2, row 'A30E/R31I/T32D', NAD+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31I with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31I/T32G to reconstruct the assayed variant sequence.

column_label: Table 2, row 'R31I/T32G', NAD+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

row_label: R31I/T32G / NAD+


assay_conditions_summary: pH 7.5; 323.15 K; cofactor NADP+

column_label: Table 2, row 'A30C/R31I/T32K', NADP+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

row_label: A30C/R31I/T32K / NADP+


column_label: Table 2, row 'A30D/R31I/T32I', NADP+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

row_label: A30D/R31I/T32I / NADP+


column_label: Table 2, row 'A30E/R31I/T32D', NADP+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

row_label: A30E/R31I/T32D / NADP+


column_label: Table 2, row 'R31I', NADP+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

row_label: R31I / NADP+


column_label: Table 2, row 'R31I/T32G', NADP+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

row_label: R31I/T32G / NADP+


column_label: Table 2, row 'R31T', NADP+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

row_label: R31T / NADP+


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

column_label: Table 2, row 'WT', NADP+ columns Km, kcat, and kcat/Km. PMC article HTML preserves the Scientific Reports primary kinetic table. Table units are Km uM, kcat s^-1, and kcat/Km mM^-1 s^-1; Km is normalized to mM by dividing by 1000, while kcat/Km is already s^-1 mM^-1.

row_label: WT / NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature N32D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 343.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature N32D/R33I/T34I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature N32D/R33L/T34S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature N32E/R33I/T34I to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.5; 343.15 K; buffer 100 mM HEPES; cofactor NADP+

column_label: Table 1; row label: Wide-type; coenzyme column block: NADP+; Km (mM) NADP+ = 0.005 +/- 0.0004; kcat (s^-1) NADP+ = 17.6 +/- 0.7; kcat/Km (mM^-1*s^-1) NADP+ = 3520; normalized Km=0.005 mM, kcat=17.6 s^-1, kcat/Km=3520 s^-1 mM^-1.

row_label: Mutation row: Wide-type; coenzyme column block: NADP+; metric columns: Km (mM), kcat (s^-1), kcat/Km (mM^-1*s^-1).


assay_conditions_summary: cofactor NADPH


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


organism: Dictyostelium discoideum

assay_conditions_summary: pH 8.6; buffer 50 mM tricine; cofactor NADP+

column_label: Scanned page 595, characterization paragraph: metric Km; row/segment NADP+; condition 1 mM 6-phosphogluconate; raw value 1.8 x 10^-5 M; normalized value 0.018 mM.

raw_value_unit_evidence: Km NADP+ = 1.8 x 10^-5 M (1 mM-6-phosphogluconate).

table_label: Scanned page 595, Results / 6-Phosphogluconate dehydrogenase / Characterization of the reaction


column_label: Scanned page 595, characterization paragraph: metric Km; row/segment 6-phosphogluconate; condition 5 mM NADP+; raw value 4.0 x 10^-5 M; normalized value 0.04 mM.

raw_value_unit_evidence: Km 6-phosphogluconate = 4.0 x 10^-5 M (5 mM-NADP+).


organism: [Candida] boidinii

proof_lines:
6-phosphogluconate
0.011 mM
Candida boidinii


proof_lines:
NADP+
0.013 mM
Candida boidinii


organism: Oryctolagus cuniculus

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

column_label: The abstract reports Km values for 6-phosphogluconate and NADP+ are approximately 54 microM and 23 microM, respectively.

raw_value_unit_evidence: Km raw_value=23 microM raw_unit=microM

row_label: Prose segment: NADP+ Km

table_label: PubMed PMID 3163 abstract


raw_value_unit_evidence: Km raw_value=54 microM raw_unit=microM

row_label: Prose segment: 6-phosphogluconate Km


organism: [Brevibacterium] flavum

assay_conditions_summary: pH 7.5; cofactor NADP+

column_label: PDF page 3 states Kms for 6PG and NADP+ were calculated from secondary plots to be 0.045 and 0.036 mM respectively; this row uses the second value for NADP+.

raw_value_unit_evidence: Km raw_value=0.036 raw_unit=mM

row_label: Kms for 6PG and NADP+ calculated from secondary plots

table_label: Results prose following Fig. 1 double-reciprocal plots


column_label: PDF page 3 states Kms for 6PG and NADP+ were calculated from secondary plots to be 0.045 and 0.036 mM respectively; this row uses the first value for 6PG.

raw_value_unit_evidence: Km raw_value=0.045 raw_unit=mM


organism: Trypanosoma brucei

proof_lines:
Trypanosoma brucei
2-deoxy 6-phosphogluconate
6-phosphogluconate


proof_lines: sheep liver 6-phosphogluconate dehydrogenase


organism: Dicentrarchus labrax

assay_conditions_summary: pH 7.5; buffer Tris-HCl

column_label: Abstract reports Michaelis constants for NADP, 6-phosphogluconate, and Mg2+ as 0.88 microM, 26.66 microM, and 3.33 mM, respectively.

raw_value_unit_evidence: Km raw_value=26.66 microM raw_unit=microM

row_label: Bass liver 6-phosphogluconate dehydrogenase / 6-phosphogluconate


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

proof_lines:
Veronese et al. 1974
Bacillus stearothermophilus
6-phosphogluconate dehydrogenase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S42T with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.3; 305.15 K; cofactor NADP+

normalized_value_unit_evidence: Km normalized_value=0.052 normalized_unit=mM; kcat normalized_value=64.5 normalized_unit=s^-1; kcat/Km normalized_value=1239.0 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Km raw_value=0.052 +/- 0.005 raw_unit=mM; kcat raw_value=64.5 +/- 8.8 raw_unit=s^-1; kcat/Km raw_value=1,239 +/- 41 raw_unit=s^-1 mM^-1.

row_label: Sy 6PGDH / 6PG

table_label: PMID 30107441 Table 1


assay_conditions_summary: pH 7.3; 305.15 K; cofactor NAD+


normalized_value_unit_evidence: Km normalized_value=4.46 normalized_unit=mM; kcat normalized_value=4.89 normalized_unit=s^-1; kcat/Km normalized_value=1.1 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Km raw_value=4.46 +/- 0.55 raw_unit=mM; kcat raw_value=4.89 +/- 0.54 raw_unit=s^-1; kcat/Km raw_value=1.10 +/- 0.08 raw_unit=s^-1 mM^-1.

row_label: Sy 6PGDH / NAD+


normalized_value_unit_evidence: Km normalized_value=0.058 normalized_unit=mM; kcat normalized_value=69.9 normalized_unit=s^-1; kcat/Km normalized_value=1207.0 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Km raw_value=0.058 +/- 0.003 raw_unit=mM; kcat raw_value=69.9 +/- 5.5 raw_unit=s^-1; kcat/Km raw_value=1,207 +/- 87 raw_unit=s^-1 mM^-1.

row_label: Sy 6PGDH / NADP+


organism: Homo sapiens


organism: Trypanosoma cruzi

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

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADP+

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


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

proof_lines: pH 7.5, 30°C, purified recombinant mutant enzyme


organism: Rhodopseudomonas palustris

assay_conditions_summary: pH 8


assay_conditions_summary: pH 8; cofactor NADP+


assay_conditions_summary: pH 6.5; cofactor NADPH


enzyme_display_name: 6-phosphogluconate dehydrogenase, decarboxylating 2, chloroplastic

organism: Spinacia oleracea

substrate_name: NADP

column_label: Results prose reports Km(6-PG) = 40 uM and Km(NADP) = 6 uM.

raw_value_unit_evidence: Km raw_value=6 raw_unit=uM

row_label: Purified chloroplast 6PGDH from spinach / NADP

table_label: Wiley full-text results prose, biochemical properties of purified cp6PGDH

substrate: NADP


sequence_variant_note: Mutation signature M13C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +14, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature M13Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


sequence_variant_note: Mutation signature M13I could not be applied safely because the resolved sequence does not match the expected reference residue(s).


proof_lines: mutant enzyme M13C, at a saturating concentration


proof_lines: mutant enzyme M13I, at a saturating concentration


assay_conditions_summary: pH 7.5; cofactor NADPH

proof_lines: wild type enzyme, at a saturating concentration of NADPH at pH 7.5


proof_lines: mutant enzyme M13F, at a saturating concentration


proof_lines: mutant enzyme M13Q, at a saturating concentration


proof_lines: mutant enzyme M13V, at a saturating concentration


sequence_variant_note: Resolved canonical sequence from uniprotkb:P00349 and applied mutation signature T263A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P00349 and applied mutation signature Y192A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P00349 and applied mutation signature K261A 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.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P00349 and applied mutation signature R447A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P00349 and applied mutation signature R288A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P00349 and applied mutation signature H187A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P00349 and applied mutation signature S129A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P00349 and applied mutation signature N188A to reconstruct the assayed variant sequence.


proof_lines: mutant enzyme N187A, at a saturating concentration of NADPH at pH 7.5


proof_lines: mutant enzyme S128A, at a saturating concentration of NADPH at pH 7.5


proof_lines: mutant enzyme H186A, at a saturating concentration of NADPH at pH 7.5


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W104L to reconstruct the assayed variant sequence.


organism: Arabidopsis thaliana


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

assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+

proof_lines: recombinant wild-type IDH1, pH not specified in the publication, temperature not specified in the publication


organism: Nicotiana tabacum

assay_conditions_summary: cofactor NADP+

proof_lines:
Mg2+-dependent reaction, ICDH2
Mg2+-dependent reaction, ICDH1


proof_lines: chloroplastic enzyme, at pH 7.5 and 30°C


organism: Pseudomonas sp.


assay_conditions_summary: cofactor NAD+


organism: Saccharolobus solfataricus

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


assay_conditions_summary: pH 8; cofactor NAD+


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


proof_lines:
pH 8.0, 25°C
at pH 7.5 and 22°C


organism: Mycobacterium tuberculosis

proof_lines: isoform ICD-1, presence of Zn2+, pH 7.5, 25°C

proof_lines: isoform ICD-1, presence of Mg2+, pH 7.5, 25°C

proof_lines: isoform ICD-2, presence of Mg2+, pH 7.5, 25°C


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

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


organism: Rattus norvegicus

proof_lines: enzyme from ischemic heart, pH 7.8, 25°C

proof_lines: enzyme from normoxic heart, pH 7.8, 25°C

proof_lines: pH 7.8, 25°C, enzyme from normoxic heart


proof_lines: pH 7.8, 25°C, enzyme from ischemic heart


assay_conditions_summary: pH 7.8; cofactor NADP+


organism: Cupriavidus necator

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


organism: Microcystis aeruginosa

assay_conditions_summary: pH 7.5; 323.15 K; cofactor NADP+

proof_lines:
with Mg2+, pH 7.5, 50°C
with Mg2+, pH 7.5, 37°C
with Mn2+, pH 7.5, 50°C


organism: Leishmania mexicana

sequence_source: uniprotkb:E9AN39 (GN=LMXM_10_0290); anchored by PMID:32980452 abstract

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADP+


assay_conditions_summary: pH 7.4; cofactor NADP+


organism: Pseudomonas psychrophila

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature L594E to reconstruct the assayed variant sequence.


enzyme_display_name: glucose 1-dehydrogenase [NAD(P)(+)]

organism: Priestia megaterium

substrate_name: D-glucose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P40288 and applied mutation signature Q252L/E170K/S100P/K166R/V72I/K137R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; buffer 100 mM PBS; cofactor NADP+

column_label: Table 1 (Kinetic parameters for purified BmGDHM0 and its variants), entry 7, enzyme row 'BmGDHM6' with mutation column 'Q252L/E170K/S100P/K166R/V72I/K137R'; column 'Specific activity [U mg^-1]' = 239; column 'Km [mM]' = 17.3; column 'kcat [s^-1]' = 119; column 'kcat/Km [s^-1 mM^-1]' = 6.9.

normalized_value_unit_evidence: Km: printed Table 1 cell 17.3 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 17.3 mM. kcat: printed Table 1 cell 119 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 119.0 s^(-1). kcat/Km: printed Table 1 cell 6.9 s^-1 mM^-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 6.9 s^(-1)*mM^(-1), which is the exact quotient of that entry's own printed component cells, 119 / 17.3 = 6.878612716763006 s^-1 mM^-1, written to the one decimal place that column uses.

raw_value_unit_evidence: Table 1, entry 7, enzyme row 'BmGDHM6', mutation column 'Q252L/E170K/S100P/K166R/V72I/K137R': specific activity = 239 U mg^-1; Km = 17.3 mM; kcat = 119 s^-1; printed kcat/Km = 6.9 s^-1 mM^-1.

table_label: Table 1: Kinetic parameters for purified BmGDHM0 and its variants (ChemBioChem 2020, 21, 2680-2688)

enzyme: glucose 1-dehydrogenase [NAD(P)(+)]

substrate: D-glucose


enzyme_display_name: Glucose 1-dehydrogenase

organism: Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)

substrate_name: NAD(+) (at 40 degrees Celsius and pH 8.8)

assay_conditions_summary: pH 8.8; cofactor NAD+

column_label: The paper states the assay was at A340 and 40 C in 20 mM Tris-HCl pH 8.8, 25 mM MgCl2, 2 M NaCl, and Section 3.3 reports Km [NAD+] = 1.2 + 0.3 mM.

raw_value_unit_evidence: Km raw_value=1.2 raw_unit=mM for NAD(+)

row_label: H. mediterranei glucose dehydrogenase forward reaction with NAD(+)

table_label: Section 3.3 Catalytic properties

enzyme: Glucose 1-dehydrogenase


substrate_name: NADP(+) (at 40 degrees Celsius and pH 8.8)

assay_conditions_summary: pH 8.8; cofactor NADP+

column_label: The paper states the assay was at A340 and 40 C in 20 mM Tris-HCl pH 8.8, 25 mM MgCl2, 2 M NaCl, and Section 3.3 reports Km [NADP+] = 0.024 + 0.002 mM.

raw_value_unit_evidence: Km raw_value=0.024 raw_unit=mM for NADP(+)

row_label: H. mediterranei glucose dehydrogenase forward reaction with NADP(+)


enzyme_display_name: Galactose 1-dehydrogenase

organism: Pseudomonas fluorescens

substrate_name: NADP(+)

assay_conditions_summary: pH 9.1; 303.15 K; buffer bis(hydroxyethyl)amine-HCl; cofactor NADP+

column_label: Primary paper article summary and kinetic constants prose state NADP+ limiting Michaelis constant Ka = 2.3 mM.

normalized_value_unit_evidence: NADP+ Km normalized 2.3 mM; CatLog Km = 2.3 mM.

raw_value_unit_evidence: The paper reports the limiting Michaelis constant for NADP+ as Ka = 2.3 mM.

row_label: NADP+ limiting Michaelis constant

table_label: Article summary and kinetic constants prose

enzyme: Galactose 1-dehydrogenase

substrate: NADP(+)


substrate_name: D-galactose

assay_conditions_summary: pH 9.1; 303.15 K; buffer 66 mM bis(hydroxyethyl)amine-HCl; cofactor NADH

column_label: PDF text lines 26-29 and 750-754 state the limiting Michaelis constant for D-galactose is Kb = 0.7 mM with NAD+ or NADP+ as cosubstrate.

normalized_value_unit_evidence: Km/Kb normalized_value=0.7 normalized_unit=mM; raw value is already reported in mM.

raw_value_unit_evidence: The paper reports: for D-galactose with NAD+ and with NADP+ as cosubstrate, Kb = 0.7 mM; pH 9.1 and 30 C.

row_label: D-galactose dehydrogenase from Pseudomonas fluorescens / D-galactose

table_label: Kinetic constants prose summary and initial-rate results section

substrate: D-galactose


organism: Leuconostoc mesenteroides

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature Q47E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NAD+

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row Q47E; Table 4, columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 310 uM; kcat cell = 48 500 min^-1; kcat/Km NAD+ cell = 156. captured primary segment: NAD+ | Q47E G6PD, the site-directed Q47E single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 310 uM | Table 4 kcat 48 500 min^-1 | Table 4 kcat/Km NAD+ printed cell 156 under the column head kcat/Km NAD+ (min^-1 uM^-1)

normalized_value_unit_evidence: Km: printed Km NAD+ cell 310 uM; 1 uM = 1/1000 mM, so 310 / 1000 = 0.31 mM; the export stores 0.31 mM, the same value. kcat: printed cell 48 500 min^-1; the printed turnover column is per MINUTE, so 48 500 / 60 = 808.3333333333334 s^(-1); the export stores 0.8 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km NAD+ cell 156 under the column head kcat/Km NAD+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 156 x 16.666666666666668 = 2600.0 s^(-1)*mM^(-1). The export stores 2600.0 s^(-1)*mM^(-1), the same value.

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row Q47E: Km NAD+ = 310 uM; kcat = 48 500 min^-1; kcat/Km NAD+ = 156 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row Q47E


substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T14A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature Y179F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NADP+

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row Y179F; Table 3, columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 14 uM; kcat cell = 15 800 min^-1; kcat/Km NADP+ cell = 1130. captured primary segment: NADP+ | Y179F G6PD, the site-directed Y179F single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 14 uM | Table 3 kcat 15 800 min^-1 | Table 3 kcat/Km NADP+ printed cell 1130 under the column head kcat/Km NADP+ (min^-1 uM^-1)

normalized_value_unit_evidence: Km: printed Km NADP+ cell 14 uM; 1 uM = 1/1000 mM, so 14 / 1000 = 0.014 mM; the export stores 0.014 mM, the same value. kcat: printed cell 15 800 min^-1; the printed turnover column is per MINUTE, so 15 800 / 60 = 263.3333333333333 s^(-1); the export stores 0.25 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km NADP+ cell 1130 under the column head kcat/Km NADP+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 1130 x 16.666666666666668 = 18833.333333333336 s^(-1)*mM^(-1). The export stores 18833.333333333332 s^(-1)*mM^(-1), the same value.

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row Y179F: Km NADP+ = 14 uM; kcat = 15 800 min^-1; kcat/Km NADP+ = 1130 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row Y179F


substrate_name: D-glucose (at 40 degrees Celsius and pH 8.8)


substrate_name: D-xylose (at 40 degrees Celsius and pH 8.8)


organism: Dictyostelium discoideum


substrate_name: D-glucose 6-phosphate

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

substrate: D-glucose 6-phosphate


organism: Trypanosoma cruzi

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1WBU6 and applied mutation signature K83A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer B (50 mM Tris pH 7; cofactor NADPH

column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'K83A'; column 'KM G6P (uM)' = 537; column 'kcat (s^-1)' = 2.8; column 'kcat/KM G6P (s^-1 uM^-1)' = 0.005.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.8 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 2.8 s^(-1). Km: printed Table 1 cell 537 uM; 537 / 1000 = 0.537 mM. kcat/Km: printed Table 1 cell 0.005 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.005 x 1000 = 5.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row K83A, G6P columns: KM G6P = 537 uM; kcat = 2.8 s^-1; printed kcat/KM G6P = 0.005 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row K83A, G6P columns


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1WBU6 and applied mutation signature L80G to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'L80G'; column 'KM G6P (uM)' = 74; column 'kcat (s^-1)' = 2.0; column 'kcat/KM G6P (s^-1 uM^-1)' = 0.027.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.0 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 2.0 s^(-1). Km: printed Table 1 cell 74 uM; 74 / 1000 = 0.074 mM. kcat/Km: printed Table 1 cell 0.027 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.027 x 1000 = 27.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row L80G, G6P columns: KM G6P = 74 uM; kcat = 2.0 s^-1; printed kcat/KM G6P = 0.027 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row L80G, G6P columns


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

column_label: Table 1 row WT; columns KM G6P (uM), kcat (s^-1), and kcat/KM G6P (s^-1 uM^-1); exact printed cells 77 +/- 20, 62 +/- 3, and 0.8, respectively; footnote a identifies triplicate nonlinear-regression kinetic determinations.

normalized_value_unit_evidence: Km 0.077 mM; kcat 62.0 s^-1; explicit paper kcat/Km 800.0 s^-1 mM^-1. The printed efficiency is converted by multiplying 0.8 by 1000 and is not recomputed as 62/0.077.

raw_value_unit_evidence: Table 1 row WT / G6P columns reports KM G6P 77 +/- 20 uM; kcat 62 +/- 3 s^-1; and an explicit kcat/KM G6P cell of 0.8 s^-1 uM^-1.

row_label: WT / G6P columns

table_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and epiandrosterone


organism: Saccharomyces cerevisiae

substrate_name: D-Glucose 6-phosphate

substrate: D-Glucose 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature K343R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row K343R; Table 3, columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 8.0 uM; kcat cell = 24 200 min^-1; kcat/Km NADP+ cell = 2030. captured primary segment: NADP+ | K343R G6PD, the site-directed K343R single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 8.0 uM | Table 3 kcat 24 200 min^-1 | Table 3 kcat/Km NADP+ printed cell 2030 under the column head kcat/Km NADP+ (min^-1 uM^-1)

normalized_value_unit_evidence: Km: printed Km NADP+ cell 8.0 uM; 1 uM = 1/1000 mM, so 8.0 / 1000 = 0.008 mM; the export stores 0.008 mM, the same value. kcat: printed cell 24 200 min^-1; the printed turnover column is per MINUTE, so 24 200 / 60 = 403.3333333333333 s^(-1); the export stores 0.4 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km NADP+ cell 2030 under the column head kcat/Km NADP+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 2030 x 16.666666666666668 = 33833.333333333336 s^(-1)*mM^(-1). The export stores 33833.333333333336 s^(-1)*mM^(-1), the same value.

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row K343R: Km NADP+ = 8.0 uM; kcat = 24 200 min^-1; kcat/Km NADP+ = 2030 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row K343R


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature T14S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row T14S; columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 14 uM; kcat cell = 22 700 min^-1; kcat/Km NADP+ cell = 1620. captured primary segment: NADP+ | T14S G6PD, the site-directed T14S single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 14 uM | Table 3 kcat 22 700 min^-1 | Table 3 kcat/Km NADP+ printed cell 1620 under the column head kcat/Km NADP+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row T14S: Km NADP+ = 14 uM; kcat = 22 700 min^-1; kcat/Km NADP+ = 1620 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row T14S


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L80G to reconstruct the assayed variant sequence.


substrate_name: glucose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P149G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: glucose 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q47E 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 Y179F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Comamonas testosteroni

substrate_name: Fusidic acid

column_label: PDF page 4, Table 1, row Fusidic acid, column Km (umol/l): 6.1; 6.1 uM = 0.0061 mM.

raw_value_unit_evidence: Km raw_value=6.1 raw_unit=umol/l

row_label: Fusidic acid

table_label: Table 1: Kinetic Constants for 3alpha-HSD/CR from C. testosteroni with Steroids

source_databases_merged: brenda uniprot

substrate: Fusidic acid


substrate_name: Isatin

column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Reduction, printed row 2, substrate `Isatin`, TBER1 column group: Km = 2.2 uM (normalized 0.0022 mM); kcat = 105 min-1 (normalized 1.75 s^-1); kcat/Km = 48 min-1 uM-1 (normalized 800.0 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 105 min-1 / 60 = 1.75 s^-1; the catalog holds 1.75 s^(-1). Km: printed cell 2.2 uM / 1000 = 0.0022 mM; the catalog holds 0.002 mM. kcat/Km: the paper prints the cell 48 min-1 uM-1, which is 48 x 1000 / 60 = 800.0 s^-1 mM^-1; the catalog holds 875.0 s^(-1)*mM^(-1).

table_label: Table 1 (journal page 1058) 'Substrate specificity for non-steroidal substrates in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5', decoded plain-numeral transcription

substrate: Isatin


organism: Escherichia coli

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

assay_conditions_summary: pH 8; 313.15 K; cofactor NADP+


substrate_name: isocitrate

substrate: isocitrate


substrate_name: DL-isocitrate

substrate: DL-isocitrate


organism: Arabidopsis thaliana

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

proof_lines: mutant enzyme C3636S, at pH 7.5 and 25°C


assay_conditions_summary: pH 7.5; cofactor NADP+


organism: Bifidobacterium longum subsp. infantis

sequence_variant_note: Resolved canonical sequence from UniProt B7GQR3 (strain ATCC 15697) anchored by PMID 26927087 / PMCID PMC4813160 Methods (RefSeq NC_011593.1 icd). and applied mutation signature D253A/S257K/K260Q/R314D/H315I/T327A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant D253A/S257K/K260Q/R314D/H315I/T327A


substrate_name: NAD+

sequence_source: UniProt B7GQR3 (strain ATCC 15697) anchored by PMID 26927087 / PMCID PMC4813160 Methods (RefSeq NC_011593.1 icd).

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

substrate: NAD+


assay_conditions_summary: pH 8; 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+


assay_conditions_summary: pH 8; cofactor NADP+

column_label: Table 3. Kinetic parameters and coenzyme specificity of different IDHs; row B. longum NADP-IDH (Mg2+) / NADP+; column NADP+ kcat (s^-1) raw value 36.4 s^-1; column NADP+ Km (uM) raw value 19.45 uM; column NADP+ kcat/Km (s^-1 uM^-1) raw value 1.87 s^-1*uM^-1

normalized_value_unit_evidence: kcat normalized_value=36.4 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=36.4 raw_unit=s^-1; Km raw_value=19.45 raw_unit=uM; kcat/Km raw_value=1.87 raw_unit=s^-1*uM^-1

row_label: B. longum NADP-IDH (Mg2+) / NADP+


organism: Archaeoglobus fulgidus

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


assay_conditions_summary: pH 8


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprotkb:P48735 and applied mutation signature K413Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+


organism: Plasmodium falciparum

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W104L to reconstruct the assayed variant sequence.


proof_lines:
pH 8.0, 25°C, wild-type enzyme
wild-type enzyme, pH 8.0, 25°C


organism: Colwellia maris


sequence_variant_note: Resolved canonical sequence from uniprot:P41561 and applied mutation signature A741S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P41561 and applied mutation signature E596L to reconstruct the assayed variant sequence.


organism: Mesocricetus auratus


substrate_name: androsterone

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

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

proof_lines: pH 7.4, 25°C, recombinant isozyme AKR1C4

proof_lines: pH 7.4, 25°C, recombinant isozyme AKR1C2 and isozyme AKR1C4

substrate: androsterone


substrate_name: benzenedihydrodiol

proof_lines: pH 7.4, 25°C, recombinant isozyme AKR1C3

proof_lines: pH 7.4, 25°C, recombinant isozyme AKR1C2

substrate: benzenedihydrodiol


proof_lines: pH 7.4, 25°C, recombinant isozyme AKR1C1


organism: Sus scrofa

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines: isoenzyme II, with 6-phosphonogluconate 0.1 mM

substrate: NADPH


substrate_name: D-galactose 6-phosphate

proof_lines:
isoenzyme I
isoenzyme II

substrate: D-galactose 6-phosphate


proof_lines:
isoenzyme II
isoenzyme I


organism: Mus musculus

substrate_name: 3-oxo-5beta-cholan-24-oic acid

assay_conditions_summary: cofactor NADP+

substrate: 3-oxo-5beta-cholan-24-oic acid


proof_lines: also in this range: 17alpha,21-dihydroxy-5beta-pregnan-3,11,20-trione, acenaphthequinone

proof_lines: also in this range: 3alpha-hydroxy-5beta-pregnan-17-one


substrate_name: glycolithocholic acid

substrate: glycolithocholic acid


substrate_name: cholic acid

proof_lines: 3alpha-hydroxy-5beta-androstan-17-one, 3alpha,21-dihydroxy-5beta-pregnan-20-one, 5beta-androstan-3alpha,17beta-diol, 5alpha-androstan-3alpha,17beta-diol, NADP+

substrate: cholic acid


substrate_name: Camphorquinone

substrate: Camphorquinone


proof_lines: also in this range: 2,3-hexanedione, 1-phenyl-1,2-propanedione, 2,3-pentanedione, pyridine-4-aldehyde, 2,3-butanedione


proof_lines:
pH 7.0, 25°C
isozyme AKR1C3
pH 7.0, 25°C, isozyme AKR1C2


substrate_name: geraniol

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

substrate: geraniol


substrate_name: cis-benzene dihydrodiol

substrate: cis-benzene dihydrodiol


substrate_name: NADH

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH

proof_lines: pH 7.4, 25°C, with substrate S-camphorquinone

substrate: NADH


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+


substrate_name: NADP+

substrate: NADP+


enzyme_display_name: glucose 1-dehydrogenase [NAD(P)+]

organism: Oncorhynchus mykiss

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

proof_lines:
pH 7.5, 25°C, coenzyme NAD+
at pH 7.5 and 25°C
pH 10, 25°C, coenzyme NAD+

enzyme: glucose 1-dehydrogenase [NAD(P)+]


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 10; 298.15 K; cofactor NADP+


substrate_name: 2-deoxy-D-glucose 6-phosphate

proof_lines:
pH 7.5, 25°C, coenzyme NAD+
pH 7.5, 25°C, coenzyme NADP+
pH 10, 25°C, coenzyme NADP+

substrate: 2-deoxy-D-glucose 6-phosphate


substrate_name: D-xylose

proof_lines:
pH 10, 25°C, coenzyme NAD+
pH 7.5, 25°C, coenzyme NAD+
pH 7.5, 25°C, coenzyme NADP+

substrate: D-xylose


organism: Pseudomonas putida