substrate_name: phenylacetaldehyde

column_label: Table 2. Kinetic parameters of the recombinant Aad1p from Phanerochaete chrysosporium; row Reduction / Phenylacetaldehyde; columns KM (uM); Kcat (min^-1); kcat/KM (uM^-1 min^-1); raw row cells: Phenylacetaldehyde | KM 530 +/- 90 uM | Kcat 670 +/- 25 min^-1 | kcat/KM 1.3 +/- 0.3 uM^-1 min^-1 | Ki ni uM

normalized_value_unit_evidence: kcat normalized_value=11.16 normalized_unit=s^-1; Km normalized_value=0.53 normalized_unit=mM; kcat/Km normalized_value=21.056603773584904 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=670 +/- 25 raw_unit=min^-1; Km raw_value=530 +/- 90 raw_unit=uM; kcat/Km raw_value=1.3 +/- 0.3 raw_unit=uM^-1*min^-1; Ki raw_value=ni raw_unit=uM

row_label: Reduction / Phenylacetaldehyde

substrate: phenylacetaldehyde


enzyme_display_name: aryl-alcohol dehydrogenase (NADP+)

organism: Phanerodontia chrysosporium

substrate_name: trans-cinnamaldehyde

source_db: brenda

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

proof_lines: pH 6.1, temperature not specified in the publication

data_origin: experimental

enzyme: aryl-alcohol dehydrogenase (NADP+)

substrate: trans-cinnamaldehyde

status: unverified

source: brenda


substrate_name: NADPH

assay_conditions_summary: pH 6.1; cofactor NADPH

column_label: Table 2. Kinetic parameters of the recombinant Aad1p from Phanerochaete chrysosporium; row Coenzymes / NADPH; columns KM (uM); Kcat (min^-1); kcat/KM (uM^-1 min^-1); raw row cells: NADPH | KM 39 +/- 5 uM | Kcat 680 +/- 30 min^-1 | kcat/KM 17 +/- 3 uM^-1 min^-1 | Ki ni uM

normalized_value_unit_evidence: kcat normalized_value=11.33 normalized_unit=s^-1; Km normalized_value=0.039 normalized_unit=mM; kcat/Km normalized_value=290.5128205128205 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=680 +/- 30 raw_unit=min^-1; Km raw_value=39 +/- 5 raw_unit=uM; kcat/Km raw_value=17 +/- 3 raw_unit=uM^-1*min^-1; Ki raw_value=ni raw_unit=uM

row_label: Coenzymes / NADPH

substrate: NADPH


enzyme_display_name: homoisocitrate dehydrogenase

organism: Thermus thermophilus

substrate_name: Unknown

kcat_display: Not reported

km_display: Not reported

kcat_over_km_display: Not reported

ki_unit: mM

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

enzyme: homoisocitrate dehydrogenase

substrate: Unknown


enzyme_display_name: aryl-alcohol dehydrogenase

organism: Thauera sp.

substrate_name: benzyl alcohol

enzyme: aryl-alcohol dehydrogenase

substrate: benzyl alcohol


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


substrate_name: 4-Hydroxybenzyl alcohol

substrate: 4-Hydroxybenzyl alcohol


organism: Taiwanofungus camphoratus

substrate_name: veratraldehyde

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

assay_conditions_summary: pH 6

proof_lines: at pH 6.0 temperature not specified in the publication

substrate: veratraldehyde


enzyme_display_name: Ketol-acid reductoisomerase (NADP(+))

organism: Escherichia coli (strain K12)

substrate_name: magnesium (with S2AL and NADPH as substrates)

source_db: uniprot

smiles: [Mg]

assay_conditions_summary: pH 8; cofactor NADPH

proof_lines: kcat is 7.2 min(-1) for reductoisomerase activity with NADPH as substrate (PubMed:9015391). kcat is 3.1 min(-1) for reductoisomerase activity with NADPH as substrate (PubMed:9015391). kcat is 0.11 min(-1) for reductoisomerase activity with

enzyme: Ketol-acid reductoisomerase (NADP(+))

source: uniprot


substrate_name: pyruvate (at pH 8 and 37 degrees Celsius)


substrate_name: 3-hydroxypyruvate (at pH 8 and 37 degrees Celsius)


substrate_name: 2-ketovalerate (at pH 8 and 37 degrees Celsius)


substrate_name: 2-ketobutyrate (at pH 8 and 37 degrees Celsius)


substrate_name: 2-ketoisovalerate (at pH 8 and 37 degrees Celsius)

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


enzyme_display_name: 3-isopropylmalate dehydrogenase

organism: Shewanella oneidensis

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from reviewed_uniprot_snapshot:Q8E9N3 and applied mutation signature S266A to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NAD+

column_label: Table 1; row SoIPMDH-S266A; column group NAD+; columns KM (µM), kcat (s^-1), and kcat/KM (µM^-1 s^-1).

raw_value_unit_evidence: Table 1; row SoIPMDH-S266A; NAD+ columns: KM 75.6 ± 1.8 µM; kcat 15.6 ± 0.1 s^-1; kcat/KM 0.21 µM^-1 s^-1.

table_label: Table 1

enzyme: 3-isopropylmalate dehydrogenase

status: corrected


sequence_variant_note: Resolved canonical sequence from reviewed_uniprot_snapshot:Q8E9N3 and applied mutation signature A268I to reconstruct the assayed variant sequence.

column_label: Table 1; row SoIPMDH-A268I; column group IPM; columns KM (µM), kcat (s^-1), and kcat/KM (µM^-1 s^-1).

raw_value_unit_evidence: Table 1; row SoIPMDH-A268I; IPM columns: KM 34.5 ± 6.2 µM; kcat 16.1 ± 0.8 s^-1; kcat/KM 0.47 µM^-1 s^-1.


column_label: Table 1; row SoIPMDH-S266A; column group IPM; columns KM (µM), kcat (s^-1), and kcat/KM (µM^-1 s^-1).

raw_value_unit_evidence: Table 1; row SoIPMDH-S266A; IPM columns: KM 22.6 ± 6.7 µM; kcat 16.7 ± 1.2 s^-1; kcat/KM 0.74 µM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S266A to reconstruct the assayed variant sequence.

column_label: Table 1; row SoIPMDH; column group NAD+; columns KM (µM), kcat (s^-1), and kcat/KM (µM^-1 s^-1).

raw_value_unit_evidence: Table 1; row SoIPMDH; NAD+ columns: KM 81.4 ± 9.9 µM; kcat 17.1 ± 0.6 s^-1; kcat/KM 0.21 µM^-1 s^-1.

row_label: SoIPMDH


column_label: Table 1; row SoIPMDH; column group IPM; columns KM (µM), kcat (s^-1), and kcat/KM (µM^-1 s^-1).

raw_value_unit_evidence: Table 1; row SoIPMDH; IPM columns: KM 14.1 ± 2.4 µM; kcat 17.4 ± 0.5 s^-1; kcat/KM 1.23 µM^-1 s^-1.


column_label: Table 1; row SoIPMDH-A268I; column group NAD+; columns KM (µM), kcat (s^-1), and kcat/KM (µM^-1 s^-1).

raw_value_unit_evidence: Table 1; row SoIPMDH-A268I; NAD+ columns: KM 278.5 ± 36.5 µM; kcat 17.4 ± 0.8 s^-1; kcat/KM 0.06 µM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from reviewed_uniprot_snapshot:Q8E9N3 and applied mutation signature L106M to reconstruct the assayed variant sequence.

column_label: Table 1; row SoIPMDH-L106M; column group IPM; columns KM (µM), kcat (s^-1), and kcat/KM (µM^-1 s^-1).

raw_value_unit_evidence: Table 1; row SoIPMDH-L106M; IPM columns: KM 12.2 ± 1.2 µM; kcat 48.1 ± 0.8 s^-1; kcat/KM 3.92 µM^-1 s^-1.


column_label: Table 1; row SoIPMDH-L106M; column group NAD+; columns KM (µM), kcat (s^-1), and kcat/KM (µM^-1 s^-1).

raw_value_unit_evidence: Table 1; row SoIPMDH-L106M; NAD+ columns: KM 70.8 ± 4.3 µM; kcat 50.5 ± 0.8 s^-1; kcat/KM 0.71 µM^-1 s^-1.


enzyme_display_name: ketol-acid reductoisomerase (NADP+)

organism: Alicyclobacillus acidocaldarius subsp. acidocaldarius

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R48P/S51L/S52D/R84A to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NADPH

proof_lines: mutant R48P/S51L/S52D/R84A, pH not specified in the publication, temperature not specified in the publication

enzyme: ketol-acid reductoisomerase (NADP+)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R48P/S51L/S52D to reconstruct the assayed variant sequence.

proof_lines: mutant R48P/S51L/S52D, pH not specified in the publication, temperature not specified in the publication


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


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


organism: Sulfurisphaera tokodaii

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

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

proof_lines: pH 7.5, 70°C, recombinant mutant F3S/S232G


proof_lines: pH 7.5, 70°C, recombinant wild-type enzyme


proof_lines: pH 7.5, 70°C, recombinant mutant F3S/L288P


assay_conditions_summary: pH 7.5; cofactor NAD+


proof_lines: pH 7.5, 70°C, recombinant wild-type enzyme and mutant F3S


organism: Arabidopsis thaliana

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L134F to reconstruct the assayed variant sequence.

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

proof_lines: mutant L134F, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: UniProt P93832

source_db: skid

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

sequence_source: multiple

proof_lines: kcat is 373 min(-1) with 3-isopropylmalate as substrate (at pH 7.5) (PubMed:20840499, PubMed:21697089). kcat is 274 min(-1) with 3-isopropylmalate as substrate (at pH 7.5 and 25 degrees Celsius) (PubMed:27137927). kcat is 1 min(-1) with 3-(

source_databases_merged: skid uniprot

enzyme: UniProt P93832

source: skid


enzyme_display_name: 3-isopropylmalate dehydrogenase 1, chloroplastic

proof_lines: kcat is 37 min(-1) with 3-isopropylmalate as substrate (PubMed:20840499, PubMed:21697089). kcat is 51 min(-1) with 3-(2'-methylthio)ethylmalate as substrate (PubMed:21697089).


enzyme_display_name: 3-isopropylmalate dehydrogenase 3, chloroplastic

proof_lines: kcat is 543 min(-1) with 3-isopropylmalate as substrate (PubMed:20840499, PubMed:21697089). kcat is 1 min(-1) with 3-(2'-methylthio)ethylmalate as substrate (PubMed:21697089).


organism: Streptomyces avermitilis

verification_status: verified

assay_conditions_summary: pH 8

column_label: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates; row label 2H2M3KB; enzyme column Sav Required metric(s) kcat, kcat_over_km, km match the explicit paper table after unit conversion.

normalized_value_unit_evidence: kcat paper=0.24 s^-1; km paper=0.8 mM; kcat_over_km paper=0.3 s^-1 mM^-1

raw_value_unit_evidence: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates, row 2H2M3KB, enzyme Sav; kcat (s^-1): 0.24 ± 0.2; K_M (mM): 0.8 ± 0.09; kcat/K_M (M^-1 s^-1): 300 ± 39.

row_label: 2H2M3KB | Sav

status: verified


column_label: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates; row label 3H3M2KB; enzyme column Sav Explicit paper metric(s) kcat_over_km differ from the export value; kcat paper=1.2 s^-1; km paper=13 mM; kcat_over_km paper=0.52 s^-1 mM^-1; kcat export=1.2 s^(-1); kcat_over_km export=0.0923076923076923 s^(-1)*mM^(-1); km export=13 mM.

raw_value_unit_evidence: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates, row 3H3M2KB, enzyme Sav; kcat (s^-1): 1.2 ± 0.17; K_M (mM): 13 ± 0.9; kcat/K_M (M^-1 s^-1): 520 ± 58.

row_label: 3H3M2KB | Sav


column_label: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates; row label MAA; enzyme column Sav Required metric(s) kcat, kcat_over_km, km match the explicit paper table after unit conversion.

normalized_value_unit_evidence: kcat paper=1.8 s^-1; km paper=30 mM; kcat_over_km paper=0.06 s^-1 mM^-1

raw_value_unit_evidence: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates, row MAA, enzyme Sav; kcat (s^-1): 1.8 ± 0.1; K_M (mM): 30 ± 2; kcat/K_M (M^-1 s^-1): 60 ± 7.

row_label: MAA | Sav


substrate_name: Hydroxypyruvate

column_label: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates; row label HP; enzyme column Sav Explicit paper metric(s) kcat_over_km differ from the export value; kcat paper=2 s^-1; km paper=60 mM; kcat_over_km paper=0.05 s^-1 mM^-1; kcat export=2 s^(-1); kcat_over_km export=0.03333333333333333 s^(-1)*mM^(-1); km export=60 mM.

raw_value_unit_evidence: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates, row HP, enzyme Sav; kcat (s^-1): 2 ± 0.2; K_M (mM): 60 ± 5; kcat/K_M (M^-1 s^-1): 50 ± 5.

row_label: HP | Sav

substrate: Hydroxypyruvate


substrate_name: pyruvate

column_label: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates; row label Pyr; enzyme column Sav Required metric(s) kcat, kcat_over_km, km match the explicit paper table after unit conversion.

normalized_value_unit_evidence: kcat paper=3.6 s^-1; km paper=1200 mM; kcat_over_km paper=0.003 s^-1 mM^-1

raw_value_unit_evidence: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates, row Pyr, enzyme Sav; kcat (s^-1): 3.6 ± 0.4; K_M (mM): 1200 ± 110; kcat/K_M (M^-1 s^-1): 3 ± 0.3.

row_label: Pyr | Sav

substrate: pyruvate


organism: Streptomyces ambofaciens

column_label: Table 1, row 2H2M3KB / Sam, columns kcat (s^-1), KM (mM), and kcat/KM (M^-1 s^-1).

row_label: 2H2M3KB / Sam

table_label: Table 1: Kinetic parameters of selected KARI homologues against native substrates


column_label: Table 1, row 3H3M2KB / Sam, columns kcat (s^-1), KM (mM), and kcat/KM (M^-1 s^-1).

row_label: 3H3M2KB / Sam


column_label: Table 2, row HP / Sam, columns kcat (s^-1), KM (mM), and kcat/KM (M^-1 s^-1).

row_label: HP / Sam

table_label: Table 2: Kinetic parameters of selected KARI homologues against non-native substrates


column_label: Table 2, row MAA / Sam, columns kcat (s^-1), KM (mM), and kcat/KM (M^-1 s^-1).

row_label: MAA / Sam


column_label: Table 2, row Pyr / Sam, columns kcat (s^-1), KM (mM), and kcat/KM (M^-1 s^-1).

row_label: Pyr / Sam


organism: Shewanella benthica

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I268A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.6; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M106L to reconstruct the assayed variant sequence.


organism: Corynebacterium glutamicum

column_label: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates; row label MAA; enzyme column Cgl Required metric(s) kcat, kcat_over_km, km match the explicit paper table after unit conversion.

normalized_value_unit_evidence: kcat paper=0.4 s^-1; km paper=40 mM; kcat_over_km paper=0.01 s^-1 mM^-1

raw_value_unit_evidence: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates, row MAA, enzyme Cgl; kcat (s^-1): 0.4 ± 0.03; K_M (mM): 40 ± 1.5; kcat/K_M (M^-1 s^-1): 10 ± 1.3.

row_label: MAA | Cgl


column_label: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates; row label HP; enzyme column Cgl Explicit paper metric(s) kcat_over_km differ from the export value; kcat paper=0.5 s^-1; km paper=40 mM; kcat_over_km paper=0.06 s^-1 mM^-1; kcat export=0.5 s^(-1); kcat_over_km export=0.0125 s^(-1)*mM^(-1); km export=40 mM.

raw_value_unit_evidence: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates, row HP, enzyme Cgl; kcat (s^-1): 0.5 ± 0.04; K_M (mM): 40 ± 4; kcat/K_M (M^-1 s^-1): 60 ± 3.9.

row_label: HP | Cgl


column_label: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates; row label 3H3M2KB; enzyme column Cgl Explicit paper metric(s) kcat_over_km differ from the export value; kcat paper=0.9 s^-1; km paper=2.3 mM; kcat_over_km paper=0.391 s^-1 mM^-1; kcat export=0.9 s^(-1); kcat_over_km export=0.391304347826087 s^(-1)*mM^(-1); km export=2.3 mM.

raw_value_unit_evidence: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates, row 3H3M2KB, enzyme Cgl; kcat (s^-1): 0.9 ± 0.08; K_M (mM): 2.3 ± 0.25; kcat/K_M (M^-1 s^-1): 391 ± 38.

row_label: 3H3M2KB | Cgl


column_label: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates; row label Pyr; enzyme column Cgl Explicit paper metric(s) kcat_over_km differ from the export value; kcat paper=8.6 s^-1; km paper=1070 mM; kcat_over_km paper=0.008 s^-1 mM^-1; kcat export=8.6 s^(-1); kcat_over_km export=0.008037383177570093 s^(-1)*mM^(-1); km export=1070 mM.

raw_value_unit_evidence: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates, row Pyr, enzyme Cgl; kcat (s^-1): 8.6 ± 0.9; K_M (mM): 1070 ± 118; kcat/K_M (M^-1 s^-1): 8 ± 0.7.

row_label: Pyr | Cgl


organism: Methanococcus aeolicus

proof_lines: mutant G50D/S52D, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: UniProt P9WKJ7

organism: Mycobacterium tuberculosis

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P9WKJ7


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P93832 and applied mutation signature R146K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

column_label: Table 2 (Steady-state kinetic parameters), mutant row 'R146K'; column 'kcat' (unit head min-1) = 1.4; column 'KmIPM' (unit head uM) = 119; column 'kcat/KmIPM' (unit head M-1 s-1) = 192. The unit head of the third column is printed by the layout renderer across three lines as M, then -1 -1, then s.

raw_value_unit_evidence: Table 2 (Steady-state kinetic parameters), mutant row 'R146K': column 'kcat' printed 1.4 min-1; column 'KmIPM' printed 119 uM; column 'kcat/KmIPM' printed 192 M-1 s-1.

row_label: Table 2, mutant row 'R146K'

table_label: Table 2: Steady-state kinetic parameters (J. Biol. Chem. 2016, 291(26):13421-13430)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P93832 and applied mutation signature R146A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters), mutant row 'R146A'; column 'kcat' (unit head min-1) = 1.8; column 'KmIPM' (unit head uM) = 70.7; column 'kcat/KmIPM' (unit head M-1 s-1) = 429. The unit head of the third column is printed by the layout renderer across three lines as M, then -1 -1, then s.

raw_value_unit_evidence: Table 2 (Steady-state kinetic parameters), mutant row 'R146A': column 'kcat' printed 1.8 min-1; column 'KmIPM' printed 70.7 uM; column 'kcat/KmIPM' printed 429 M-1 s-1.

row_label: Table 2, mutant row 'R146A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P93832 and applied mutation signature L132A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters), mutant row 'L132A'; column 'kcat' (unit head min-1) = 28.0; column 'KmIPM' (unit head uM) = 24.2; column 'kcat/KmIPM' (unit head M-1 s-1) = 19,290. The unit head of the third column is printed by the layout renderer across three lines as M, then -1 -1, then s.

raw_value_unit_evidence: Table 2 (Steady-state kinetic parameters), mutant row 'L132A': column 'kcat' printed 28.0 min-1; column 'KmIPM' printed 24.2 uM; column 'kcat/KmIPM' printed 19,290 M-1 s-1.

row_label: Table 2, mutant row 'L132A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P93832 and applied mutation signature V235A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters), mutant row 'V235A'; column 'kcat' (unit head min-1) = 120; column 'KmIPM' (unit head uM) = 11.4; column 'kcat/KmIPM' (unit head M-1 s-1) = 180,300. The unit head of the third column is printed by the layout renderer across three lines as M, then -1 -1, then s.

raw_value_unit_evidence: Table 2 (Steady-state kinetic parameters), mutant row 'V235A': column 'kcat' printed 120 min-1; column 'KmIPM' printed 11.4 uM; column 'kcat/KmIPM' printed 180,300 M-1 s-1.

row_label: Table 2, mutant row 'V235A'


enzyme_display_name: 3-isopropylmalate dehydrogenase 2, chloroplastic

substrate_name: 3-isopropylmalate (at pH 7.5 and 25 degrees Celsius)

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


assay_conditions_summary: pH 8; 295.15 K; cofactor NADH

proof_lines:
pH 8.0, 22°C
Raw SKiD Env: Temp=22°C, pH=8

source_databases_merged: brenda skid


assay_conditions_summary: pH 8; 295.15 K; cofactor NADPH

column_label: Table 1 | Kinetic Analysis of CgKARI; row NADPH; columns kcat [min^-1], Km [mM], and kcat/Km [mM^-1 min^-1]: 13.05725, 0.02258, and 578.2663.

row_label: NADPH

table_label: Table 1 | Kinetic Analysis of CgKARI


proof_lines:
pH 8.0, 22°C
pH 8.0 25°C
Raw SKiD Env: Temp=22°C, pH=8


substrate_name: 3-isopropylmalate (at pH 7.5 and in reduced form)

enzyme: 3-isopropylmalate dehydrogenase 1, chloroplastic


substrate_name: NAD(+) (at pH 7.5 and in reduced form)

substrate: NAD(+) (at pH 7.5 and in reduced form)


substrate_name: D-malate (at pH 7.5 and in reduced form)


organism: Sulfolobus acidocaldarius

substrate_name: homoisocitrate

assay_conditions_summary: pH 8; 333.15 K; cofactor NAD+

column_label: Primary PDF page 5, Table 2, row Saci_0600 and HIC columns kcat [s^-1], Km [uM], and kcat/Km [s^-1 uM^-1].

row_label: Saci_0600; HIC

table_label: Table 2 - Kinetic constants of Saci_0600 and Saci_2375

substrate: homoisocitrate


column_label: Primary PDF page 5, Table 2, row Saci_0600 and 3-IPM columns kcat [s^-1], Km [uM], and kcat/Km [s^-1 uM^-1].


substrate_name: NAD+

column_label: Primary PDF page 5, results paragraph immediately above Table 2: 'The Km value for NAD+ was 120 uM.'

raw_value_unit_evidence: Results prose: The Km value for NAD+ was 120 uM.

row_label: Saci_0600 NAD+ kinetic constant

table_label: Results prose immediately above Table 2


assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines: pH 8.0, 25°C, 2 mM Mg2+, cofactor: NADPH

proof_lines: pH 8.0, 25°C, 10 mM Mg2+, cofactor: NADH


assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

column_label: Table 3 row Sac-KARI, NADH columns give KM 6.0 uM, kcat 0.056 s^-1, and kcat/KM 9.5 mM^-1 s^-1.

normalized_value_unit_evidence: Paper-normalized metrics: KM 0.006 mM; kcat 0.056 s^-1; paper-reported kcat/KM 9.5 s^-1 mM^-1. The package expected 9.333333333333334 is the same-row rounded calculation 0.056 / 0.006.

row_label: Sac-KARI / NADH columns

table_label: Table 3. Kinetic parameters of KARI variants determined using NADPH or NADH with saturating concentrations of 2(S)-AL as substrate


substrate_name: NADPH

column_label: Table 3 row Sac-KARI, NADPH columns give KM 0.4 uM, kcat 0.064 s^-1, and kcat/KM 185.8 mM^-1 s^-1.

normalized_value_unit_evidence: Paper-normalized metrics: KM 0.0004 mM; kcat 0.064 s^-1; paper-reported kcat/KM 185.8 s^-1 mM^-1. The package expected 160.0 is the same-row rounded calculation 0.064 / 0.0004.

row_label: Sac-KARI / NADPH columns


substrate_name: Heptanal

smiles: CCCCCCC=O

proof_lines: pH 6.1, temperature not specified in the publication

substrate: Heptanal


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


enzyme_display_name: UniProt C0IR58

organism: Ralstonia sp.

assay_conditions_summary: pH 8.3; 303.15 K; cofactor NAD+

enzyme: UniProt C0IR58


substrate_name: NADP+

assay_conditions_summary: pH 8.3; 303.15 K; cofactor NADP+

substrate: NADP+


organism: Methanocaldococcus jannaschii


substrate_name: D-malate

source_databases_merged: brenda uniprot

substrate: D-malate


organism: Neurospora crassa

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


enzyme_display_name: UniProt Q2FWK4

organism: Staphylococcus aureus

enzyme: UniProt Q2FWK4


enzyme_display_name: UniProt Q5SIY4

organism: Thermus thermophilus

assay_conditions_summary: pH 8; 343.15 K; cofactor NAD+

proof_lines:
Raw SKiD Env: Temp=70°C, pH=8
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=70°C, pH=7.6

enzyme: UniProt Q5SIY4


proof_lines:
Raw SKiD Env: Temp=20°C, pH=7.6
Raw SKiD Env: Temp=20°C, pH=-----


organism: Escherichia coli (strain K12)

substrate_name: 2-ketopantoate (at pH 8 and 37 degrees Celsius)

proof_lines: kcat is 7.2 min(-1) for reductoisomerase activity with NADPH as substrate (PubMed:9015391). kcat is 3.1 min(-1) for reductoisomerase activity with NADPH as substrate (PubMed:9015391). kcat is 0.11 min(-1) for reductoisomerase activity with


substrate_name: 2-acetolactate (at pH 8 and 37 degrees Celsius)


substrate_name: NADP

substrate: NADP


substrate_name: NADH

assay_conditions_summary: pH 8; cofactor NADH


organism: Slackia exigua (strain ATCC 700122 / DSM 15923 / CIP 105133 / JCM 11022 / KCTC 5966 / S-7)

substrate_name: NADPH (at pH 7)

assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 1 row Se_KARI with mutations column dash reports K_M for cofactors [uM] / NADPH = 1.0.

raw_value_unit_evidence: Km raw_value=1.0 raw_unit=uM

row_label: Se_KARI / mutations column dash

table_label: PMC3704004 Table 1, Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and variants

substrate: NADPH (at pH 7)


substrate_name: NADH (at pH 7)

assay_conditions_summary: pH 7; cofactor NADH

column_label: Table 1 row Se_KARI with mutations column dash reports K_M for cofactors [uM] / NADH = 45.

raw_value_unit_evidence: Km raw_value=45 raw_unit=uM

substrate: NADH (at pH 7)


organism: Spinacia oleracea

assay_conditions_summary: pH 8.2; cofactor NADPH

proof_lines: pH 8.2, 30°C, chimeric enzyme Arabidopsis thaliana acetohydroxy acid synthase is genetically fused in frame with the nucleotide sequence coding for the Spinacia oleracea acetohydroxy acid isomeroreductase and expressed in E. coli

substrate: NADPH


proof_lines:
pH 8.2, 30°C
pH 8, 30°C, isoenzyme 1


assay_conditions_summary: pH 8.2; 303.15 K; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature F431S with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

proof_lines: pH 8.2, 30°C, deletion mutant DELTA423-430/F431S


organism: Saccharomyces cerevisiae

substrate_name: (2R,3S)-3-propylmalic acid

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

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

assay_conditions_summary: pH 7.8; cofactor NAD+

column_label: PMID 17116397 Table 1, compound 12 / ScHICDH row, Km = 290 uM, kcat = 0.70 s^-1, kcat/Km = 0.0024 s^-1/uM.

raw_value_unit_evidence: Table 1 row for compound 12 reports Km = 290 uM, kcat = 0.70 s^-1, and kcat/Km = 0.0024 s^-1/uM.

row_label: compound 12 / (2R,3S)-3-propylmalic acid / ScHICDH

table_label: Table 1. Kinetic parameters of substrate analogs

substrate: (2R,3S)-3-propylmalic acid


organism: Pyrococcus horikoshii


substrate_name: isocitrate

substrate: isocitrate


organism: Lactococcus lactis subsp. lactis (strain IL1403)

column_label: Table 1 row Ll_KARI / mutations column dash; K_M for cofactors [uM] / NADPH = 13.

raw_value_unit_evidence: Km raw_value=13 raw_unit=uM for NADPH.

row_label: Ll_KARI / mutations column dash

table_label: PMC3704004 Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and variants


column_label: Table 1 row Ll_KARI / mutations column dash; K_M for cofactors [uM] / NADH = 285.

raw_value_unit_evidence: Km raw_value=285 raw_unit=uM for NADH.


enzyme_display_name: UniProt C8WR67

organism: Alicyclobacillus acidocaldarius subsp. acidocaldarius

assay_conditions_summary: cofactor NADH

enzyme: UniProt C8WR67


assay_conditions_summary: cofactor NADPH


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: NADPH (with HP as substrate)

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature S2A with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

proof_lines: kcat is 12.5 sec(-1) for reductoisomerase activity with HP as substrate. kcat is 1.4 sec(-1) for reductoisomerase activity with S2AL as substrate.

substrate: NADPH (with HP as substrate)


substrate_name: HP

substrate: HP


proof_lines: reductive carboxylation of alpha-ketoadipate

proof_lines: The KM for homoisocitrate is lower than 10 uM.

substrate: NADH


substrate_name: alpha-ketoadipate

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

substrate: alpha-ketoadipate


enzyme_display_name: UniProt D2YZL2

organism: Shewanella benthica

proof_lines:
Raw SKiD Env: Temp=20°C, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.6

enzyme: UniProt D2YZL2


enzyme_display_name: UniProt P50455

organism: Sulfurisphaera tokodaii

enzyme: UniProt P50455


substrate_name: malate

substrate: malate


organism: Arabidopsis thaliana

proof_lines: kcat is 543 min(-1) with 3-isopropylmalate as substrate (PubMed:20840499, PubMed:21697089). kcat is 1 min(-1) with 3-(2'-methylthio)ethylmalate as substrate (PubMed:21697089).

enzyme: 3-isopropylmalate dehydrogenase 3, chloroplastic


assay_conditions_summary: pH 8.2; 303.15 K; cofactor NADH


organism: Corynebacterium glutamicum


substrate_name: NAD+

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: oxidate decarboxylation of homoisocitrate

substrate: NAD+


enzyme_display_name: UniProt Q5SIJ1

enzyme: UniProt Q5SIJ1


enzyme_display_name: homoisocitrate dehydrogenase

substrate_name: homoisocitrate

substrate: homoisocitrate


enzyme_display_name: Aldo-keto reductase family 1 member A1

organism: Rattus norvegicus

substrate_name: acrolein

smiles: C=CC=O

proof_lines: kcat is 3.0 sec(-1) for D,L glyceraldehyde as substrate (PubMed:22820017). kcat is 3.0 sec(-1) for methylglyoxal as substrate (PubMed:22820017). kcat is 3.4 sec(-1) for 3-deoxyglucosone as substrate (PubMed:22820017). kcat is 3.1 sec(-1) fo

enzyme: Aldo-keto reductase family 1 member A1

substrate: acrolein


enzyme_display_name: UniProt Q8E9N3

organism: Shewanella oneidensis

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NAD+

enzyme: UniProt Q8E9N3


enzyme_display_name: 3-isopropylmalate dehydrogenase

proof_lines: pressure 250 MPa, 20°C, pH not specified in the publication

proof_lines: pressure 200 MPa, 20°C, pH not specified in the publication

proof_lines: pressure 100 MPa, 20°C, pH not specified in the publication


substrate_name: NAD (at 40 degrees Celsius)

substrate: NAD (at 40 degrees Celsius)


enzyme_display_name: Ketol-acid reductoisomerase (NADP(+))

substrate_name: NADPH

assay_conditions_summary: pH 8; cofactor NADPH


enzyme_display_name: aryl-alcohol dehydrogenase

organism: Lactiplantibacillus plantarum WCFS1

substrate_name: benzyl alcohol

enzyme: aryl-alcohol dehydrogenase

substrate: benzyl alcohol


enzyme_display_name: ketol-acid reductoisomerase (NADP+)

proof_lines: pH 8.2, 30°C, chimeric enzyme Aabidopsis thaliana acetohydroxy acid synthase genetically fused in frame with the nucleotide sequence coding for the Spinacia oleracea acetohydroxy acid isomeroreductase and expressed in E. coli


enzyme_display_name: aryl-alcohol dehydrogenase (NADP(+))

organism: Ralstonia sp.

source_db: oed

column_label: Table II. Kinetic parameters for engineered RasADH variants; row label: (S)-1-phenylethanol block / Wild type RasADH / NAD+ (footnote a); columns: KM (mM), kcat (min^-1), kcat/KM (mM^-1 min^-1).

raw_value_unit_evidence: Table II row (S)-1-phenylethanol block / Wild type RasADH / NAD+ (footnote a) reports Km=9.9 +/- 1.1 mM, kcat=0.69 +/- 0.03 min^-1, and kcat/Km=0.069 mM^-1 min^-1.

enzyme: aryl-alcohol dehydrogenase (NADP(+))

source: oed


enzyme_display_name: ketol-acid reductoisomerase (NADP(+))

organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R68D/K69L/K75V/R76D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 295.15 K; cofactor NADH

column_label: Table 2 row R68D:K69L:K75V:R76D; NADH Km, kcat, and kcat/Km columns; cells 19 uM, 5.3 min^-1, 2.7e5 min^-1 M^-1.

raw_value_unit_evidence: Km = 19 uM; kcat = 5.3 min^-1; printed kcat/Km = 2.7e5 min^-1 M^-1

row_label: R68D:K69L:K75V:R76D; NADH

table_label: Table 2: Kinetic Parameters of Wild-Type and Mutant KARIs

enzyme: ketol-acid reductoisomerase (NADP(+))


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R76D to reconstruct the assayed variant sequence.

column_label: Table 2 row R76D; NADH Km, kcat, and kcat/Km columns; cells 82 uM, 5.3 min^-1, 6.5e4 min^-1 M^-1.

raw_value_unit_evidence: Km = 82 uM; kcat = 5.3 min^-1; printed kcat/Km = 6.5e4 min^-1 M^-1

row_label: R76D; NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R76Q/R68A to reconstruct the assayed variant sequence.


substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K69L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 295.15 K; cofactor NADP+

column_label: Table 1 row K69L; NADP+ Km, kcat, and kcat/Km columns; cells 8.9 uM, 0.019 min^-1, 2.1e3 min^-1 M^-1.

raw_value_unit_evidence: Km = 8.9 uM; kcat = 0.019 min^-1; printed kcat/Km = 2.1e3 min^-1 M^-1

row_label: K69L; NADP+

table_label: Table 1: Kinetic Parameters of Wild-Type and Mutant KARIs

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K75Q to reconstruct the assayed variant sequence.

column_label: Table 1 row K75Q; NADP+ Km, kcat, and kcat/Km columns; cells 11.2 uM, 0.04 min^-1, 3.6e3 min^-1 M^-1.

raw_value_unit_evidence: Km = 11.2 uM; kcat = 0.04 min^-1; printed kcat/Km = 3.6e3 min^-1 M^-1

row_label: K75Q; NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R68Q to reconstruct the assayed variant sequence.

column_label: Table 1 row R68Q; NADP+ Km, kcat, and kcat/Km columns; cells 29 uM, 0.009 min^-1, 3.1e2 min^-1 M^-1.

raw_value_unit_evidence: Km = 29 uM; kcat = 0.009 min^-1; printed kcat/Km = 3.1e2 min^-1 M^-1

row_label: R68Q; NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R76Q to reconstruct the assayed variant sequence.

column_label: Table 1 row R76Q; NADP+ Km, kcat, and kcat/Km columns; cells 72 uM, 0.012 min^-1, 1.7e2 min^-1 M^-1.

raw_value_unit_evidence: Km = 72 uM; kcat = 0.012 min^-1; printed kcat/Km = 1.7e2 min^-1 M^-1

row_label: R76Q; NADP+


assay_conditions_summary: pH 8; 295.15 K; cofactor NADPH

column_label: Table 1 row K69L; NADPH Km, kcat, and kcat/Km columns; cells 7.6 uM, 12.7 min^-1, 1.7e6 min^-1 M^-1.

raw_value_unit_evidence: Km = 7.6 uM; kcat = 12.7 min^-1; printed kcat/Km = 1.7e6 min^-1 M^-1

row_label: K69L; NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y181F to reconstruct the assayed variant sequence.

enzyme: 3-isopropylmalate dehydrogenase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y181H with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


column_label: Table 1; row K75Q; NADPH columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Table 1 row K75Q NADPH cells: Km=2.5 uM; kcat=0.56 min^-1; kcat/Km=2.3e5 min^-1 M^-1.


column_label: Table 2 row R68D:K69L:K75V:R76D; NADPH Km, kcat, and kcat/Km columns; cells 222 uM, 1.97 min^-1, 8.9e3 min^-1 M^-1.

raw_value_unit_evidence: Km = 222 uM; kcat = 1.97 min^-1; printed kcat/Km = 8.9e3 min^-1 M^-1

row_label: R68D:K69L:K75V:R76D; NADPH


column_label: Table 1; row R68Q; NADPH columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Table 1 row R68Q NADPH cells: Km=24.5 uM; kcat=0.40 min^-1; kcat/Km=1.6e4 min^-1 M^-1.


column_label: Table 2; row R76D; NADPH columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Table 2 row R76D NADPH cells: Km=401 uM; kcat=1.8 min^-1; kcat/Km=4.5e3 min^-1 M^-1.

table_label: Table 2


column_label: Table 1; row R76Q; NADPH columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Table 1 row R76Q NADPH cells: Km=36.5 uM; kcat=0.37 min^-1; kcat/Km=1e4 min^-1 M^-1.


column_label: Table 2; row R76Q:R68A; NADPH columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Table 2 row R76Q:R68A NADPH cells: Km=160 uM; kcat=0.26 min^-1; kcat/Km=1.6e3 min^-1 M^-1.


column_label: Table 1 row WT; NADPH Km, kcat, and kcat/Km columns; cells 7.3 uM, 7.2 min^-1, 9.9e5 min^-1 M^-1.

raw_value_unit_evidence: Km = 7.3 uM; kcat = 7.2 min^-1; printed kcat/Km = 9.9e5 min^-1 M^-1

row_label: WT; NADPH


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


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


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


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

proof_lines:
ketol-acid reductoisomerase
Escherichia coli
bifunctional enzyme


substrate_name: alpha-Ketovaline

substrate: alpha-Ketovaline


substrate_name: pyruvate

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

substrate: pyruvate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G37D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.3; 303.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N15G/G37D/R38V/R39S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N15G/G37D/R38V/R39S/A86N/S88A to reconstruct the assayed variant sequence.


column_label: Table II. Kinetic parameters for engineered RasADH variants; row label: NAD+ block / Wild type RasADH / (S)-1-PhEtOH; columns: KM (mM), kcat (min^-1), kcat/KM (mM^-1 min^-1).

raw_value_unit_evidence: Table II row NAD+ block / Wild type RasADH / (S)-1-PhEtOH reports Km=3.1 +/- 0.3 mM, kcat=1.3 +/- 0.1 min^-1, and kcat/Km=0.42 mM^-1 min^-1.


assay_conditions_summary: pH 8.3; 303.15 K; cofactor NADP+


column_label: Table II. Kinetic parameters for engineered RasADH variants; row label: NADP+ block / Wild type RasADH / (S)-1-PhEtOH; columns: KM (mM), kcat (min^-1), kcat/KM (mM^-1 min^-1).

raw_value_unit_evidence: Table II row NADP+ block / Wild type RasADH / (S)-1-PhEtOH reports Km=0.051 +/- 0.004 mM, kcat=99 +/- 2 min^-1, and kcat/Km=1,940 mM^-1 min^-1.


sequence_variant_note: Mutation signature D292N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature L132A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature L133A 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 +1, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -12, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature R146K 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: Resolved canonical sequence from uniprot_accession and applied mutation signature V235A with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.


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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

column_label: Valid OSTI/JBC PDF page 6, Table 2, Wild type row and the three metric-labeled columns; the caption fixes NAD+ at 1 mM.

row_label: Wild type; IPM

table_label: Table 2: Steady-state kinetic parameters


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P93832 and applied mutation signature Y181A to reconstruct the assayed variant sequence.

column_label: Valid OSTI/JBC PDF page 6, Table 2, Y181A row and the three metric-labeled columns; the caption fixes NAD+ at 1 mM.

row_label: Y181A; IPM


organism: Streptomyces avermitilis

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

column_label: Table 1: Kinetic parameters of selected KARI homologues against native substrates, substrate 2H2E3KB, enzyme column Sav. kcat row reports 0.4 +/- 0.04 s^-1; KM row reports 2.6 +/- 0.3 mM; explicit kcat/KM row reports 153 +/- 10 M^-1 s^-1, normalized to 0.153 s^-1*mM^-1 and consistent with CatLog's computed 0.15384615384615385 ratio from the same kcat and KM cells.

normalized_value_unit_evidence: kcat 0.4 s^-1 matches CatLog 0.4 s^-1; KM 2.6 mM matches CatLog 2.6 mM; explicit kcat/KM 153 M^-1 s^-1 -> 0.153 s^-1*mM^-1, consistent with CatLog computed ratio 0.15384615384615385 from 0.4/2.6.

raw_value_unit_evidence: Table 1 substrate 2H2E3KB, enzyme column Sav: kcat=0.4 +/- 0.04 s^-1; KM=2.6 +/- 0.3 mM; kcat/KM=153 +/- 10 M^-1 s^-1.

row_label: 2H2E3KB / Sav


column_label: Table 1, row 2H2M3KB / Sav, columns kcat (s^-1), KM (mM), and kcat/KM (M^-1 s^-1).

row_label: 2H2M3KB / Sav


column_label: Table 2, row MAA / Sav, columns kcat (s^-1), KM (mM), and kcat/KM (M^-1 s^-1).

row_label: MAA / Sav


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

column_label: Table 1, row 3H3E2KB / Sav, columns kcat (s^-1), KM (mM), and kcat/KM (M^-1 s^-1).

row_label: 3H3E2KB / Sav


substrate_name: Hydroxypyruvate

column_label: Table 2, row HP / Sav, columns kcat (s^-1), KM (mM), and kcat/KM (M^-1 s^-1).

row_label: HP / Sav

substrate: Hydroxypyruvate


column_label: Table 2, row Pyr / Sav, columns kcat (s^-1), KM (mM), and kcat/KM (M^-1 s^-1).

row_label: Pyr / Sav


organism: Acidithiobacillus ferrooxidans

assay_conditions_summary: cofactor NAD+

column_label: Results prose reports 3-isopropylmalate Km as 26 microM.

normalized_value_unit_evidence: 26 microM = 0.026 mM

raw_value_unit_evidence: Km value for 3-IPM was 26 microM

row_label: 3-isopropylmalate Km statement

table_label: Results prose on J-STAGE PDF journal page 374


substrate_name: NAD

column_label: Results prose reports NAD+ Km as 0.8 mM.

raw_value_unit_evidence: Km value for NAD+ was 0.8 mM

row_label: NAD+ Km statement

substrate: NAD


substrate_name: D-malate

column_label: Results prose reports D-malate Km as 4 mM.

raw_value_unit_evidence: Km values for D-malate and L-malate were 4 and 12 mM respectively

row_label: D-malate Km statement

substrate: D-malate


substrate_name: L-malate

column_label: Results prose reports L-malate Km as 12 mM.

row_label: L-malate Km statement

substrate: L-malate


organism: Sulfolobus acidocaldarius

substrate_name: NADH

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

column_label: Table 3 row Sac-KARI, NADH columns give KM 6.0 uM, kcat 0.056 s^-1, and kcat/KM 9.5 mM^-1 s^-1.

row_label: Sac-KARI / NADH columns


assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

column_label: Table 3 row Sac-KARI, NADPH columns give KM 0.4 uM, kcat 0.064 s^-1, and kcat/KM 185.8 mM^-1 s^-1.

row_label: Sac-KARI / NADPH columns

substrate: NADPH


organism: Thermus thermophilus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E57V/S72I/R85M/Y86A/M208T/F217Y/R310M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E57V/S72I/R85M/Y86A/M208T/F217Y/V238M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E57V/S72I/R85M/Y86A/M208T/V238M/R310M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H15Y/E57V/S72I/R85M/Y86A/M208T/F217Y/V238M/R310M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R85V/Y86A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S72I/R85M/Y86A/M208T/F217Y/V238M/R310M to reconstruct the assayed variant sequence.


column_label: Table 1 | Kinetic Analysis of CgKARI; row (S)-2-acetolactate; columns kcat [min^-1], Km [mM], and kcat/Km [mM^-1 min^-1]: 14.08963, 2.16103, and 6.51986.

raw_value_unit_evidence: Table 1 row (S)-2-acetolactate: kcat 14.08963 min^-1; Km 2.16103 mM; kcat/Km 6.51986 mM^-1 min^-1.


column_label: Table 1, NADH row; Km [mM], kcat [min^-1], and kcat/Km [mM^-1 min^-1] columns.

row_label: NADH

table_label: Table 1. Kinetic Analysis of CgKARI


column_label: Table 1 | Kinetic Analysis of CgKARI; row NADPH; columns kcat [min^-1], Km [mM], and kcat/Km [mM^-1 min^-1]: 13.05725, 0.02258, and 578.2663.

row_label: NADPH


organism: Meiothermus ruber

assay_conditions_summary: pH 7; 323.15 K; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T84S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 323.15 K; cofactor NADH


organism: Streptomyces ambofaciens

column_label: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates; row label 2H2E3KB; enzyme column Sam Explicit paper metric(s) kcat_over_km differ from the export value; kcat paper=1.3 s^-1; km paper=6.7 mM; kcat_over_km paper=0.194 s^-1 mM^-1; kcat_over_km export=0.19402985074626866 s^(-1)*mM^(-1).

raw_value_unit_evidence: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates, row 2H2E3KB, enzyme Sam; kcat (s^-1): 1.3 ± 0.09; K_M (mM): 6.7 ± 0.7; kcat/K_M (M^-1 s^-1): 194 ± 20.

row_label: 2H2E3KB | Sam


column_label: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates; row label 2H2M3KB; enzyme column Sam Required metric(s) kcat_over_km match the explicit paper table after unit conversion.

normalized_value_unit_evidence: kcat paper=0.63 s^-1; km paper=2 mM; kcat_over_km paper=0.315 s^-1 mM^-1

raw_value_unit_evidence: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates, row 2H2M3KB, enzyme Sam; kcat (s^-1): 0.63 ± 0.5; K_M (mM): 2 ± 0.15; kcat/K_M (M^-1 s^-1): 315 ± 33.

row_label: 2H2M3KB | Sam


column_label: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates; row label MAA; enzyme column Sam Required metric(s) kcat_over_km match the explicit paper table after unit conversion.

normalized_value_unit_evidence: kcat paper=1.2 s^-1; km paper=40 mM; kcat_over_km paper=0.03 s^-1 mM^-1

raw_value_unit_evidence: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates, row MAA, enzyme Sam; kcat (s^-1): 1.2 ± 0.09; K_M (mM): 40 ± 4; kcat/K_M (M^-1 s^-1): 30 ± 3.

row_label: MAA | Sam


column_label: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates; row label 3H3E2KB; enzyme column Sam Required metric(s) kcat_over_km match the explicit paper table after unit conversion.

normalized_value_unit_evidence: kcat paper=0.9 s^-1; km paper=20 mM; kcat_over_km paper=0.045 s^-1 mM^-1

raw_value_unit_evidence: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates, row 3H3E2KB, enzyme Sam; kcat (s^-1): 0.9 ± 0.1; K_M (mM): 20 ± 2; kcat/K_M (M^-1 s^-1): 45 ± 4.

row_label: 3H3E2KB | Sam


column_label: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates; row label 3H3M2KB; enzyme column Sam Required metric(s) kcat_over_km match the explicit paper table after unit conversion.

normalized_value_unit_evidence: kcat paper=0.8 s^-1; km paper=4 mM; kcat_over_km paper=0.2 s^-1 mM^-1

raw_value_unit_evidence: PMC4353338 Table 1. Kinetic parameters of selected KARI homologues against native substrates, row 3H3M2KB, enzyme Sam; kcat (s^-1): 0.8 ± 0.1; K_M (mM): 4 ± 0.3; kcat/K_M (M^-1 s^-1): 200 ± 54.

row_label: 3H3M2KB | Sam


column_label: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates; row label HP; enzyme column Sam Required metric(s) kcat_over_km match the explicit paper table after unit conversion.

normalized_value_unit_evidence: kcat paper=1 s^-1; km paper=50 mM; kcat_over_km paper=0.02 s^-1 mM^-1

raw_value_unit_evidence: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates, row HP, enzyme Sam; kcat (s^-1): 1 ± 0.09; K_M (mM): 50 ± 4; kcat/K_M (M^-1 s^-1): 20 ± 2.2.

row_label: HP | Sam


column_label: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates; row label Pyr; enzyme column Sam Required metric(s) kcat_over_km match the explicit paper table after unit conversion.

normalized_value_unit_evidence: kcat paper=6.3 s^-1; km paper=1050 mM; kcat_over_km paper=0.006 s^-1 mM^-1

raw_value_unit_evidence: PMC4353338 Table 2. Kinetic parameters of selected KARI homologues against non-native substrates, row Pyr, enzyme Sam; kcat (s^-1): 6.3 ± 0.5; K_M (mM): 1050 ± 99; kcat/K_M (M^-1 s^-1): 6 ± 0.5.

row_label: Pyr | Sam


organism: Yokenella sp. WZY002

substrate_name: benzaldehyde

assay_conditions_summary: pH 6.5; 338.15 K; cofactor NADPH

column_label: Table 5 row Benzaldehyde / NADPH (0.4 mM); columns Apparent Km (mM), Kcat (s^-1), Kcat/Km (s^-1 mM^-1)

row_label: Benzaldehyde / NADPH (0.4 mM)

table_label: PMCID PMC3993188 Table 5

substrate: benzaldehyde


assay_conditions_summary: pH 6.5; 338.15 K; cofactor NADP+

column_label: Table 5 row Benzyl alcohol / NADP+ (0.4 mM); columns Apparent Km (mM), Kcat (s^-1), Kcat/Km (s^-1 mM^-1)

row_label: Benzyl alcohol / NADP+ (0.4 mM)


substrate_name: crotonaldehyde

smiles: C/C=C/C=O

assay_conditions_summary: pH 8; 328.15 K; cofactor NADPH

column_label: Table 5 row Crotonaldehyde / NADPH (0.4 mM); columns Apparent Km (mM), Kcat (s^-1), Kcat/Km (s^-1 mM^-1)

row_label: Crotonaldehyde / NADPH (0.4 mM)

substrate: crotonaldehyde


substrate_name: crotonyl alcohol

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

assay_conditions_summary: pH 8; 328.15 K; cofactor NADP+

column_label: Table 5 row Crotyl alcohol / NADP+ (0.4 mM); columns Apparent Km (mM), Kcat (s^-1), Kcat/Km (s^-1 mM^-1)

row_label: Crotyl alcohol / NADP+ (0.4 mM)

substrate: crotonyl alcohol


column_label: Table 5 row NADP+ / Crotyl alcohol (40 mM); columns Apparent Km (mM), Kcat (s^-1), Kcat/Km (s^-1 mM^-1)

row_label: NADP+ / Crotyl alcohol (40 mM)


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

substrate_name: beta-isopropylmalate

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

substrate: beta-isopropylmalate


substrate_name: isocitrate

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

assay_conditions_summary: pH 8; 333.15 K; cofactor NAD+

column_label: Table II row HICDH has Isocitrate Km = 405 +/- 15 uM and kcat = 171 +/- 2 s^-1; derived kcat/Km = 171 / 0.405 = 422.2222222222222 s^-1*mM^-1. The table also prints rounded kcat/Km 4.2 x 10^5 s^-1 M^-1.

normalized_value_unit_evidence: Km normalized_value=0.405 normalized_unit=mM from 405 uM / 1000; kcat normalized_value=171 normalized_unit=s^-1; kcat/Km derived normalized_value=422.2222222222222 normalized_unit=s^-1*mM^-1 from 171 / 0.405.

raw_value_unit_evidence: Table II HICDH row under Isocitrate reports Km 405 +/- 15 uM, kcat 171 +/- 2 s^-1, and rounded printed kcat/Km 4.2 x 10^5 s^-1 M^-1.

row_label: HICDH row / Isocitrate columns

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

enzyme: homoisocitrate dehydrogenase

substrate: isocitrate


substrate_name: homoisocitrate

column_label: Table II row HICDH has Homocitrate Km = 7,486 +/- 500 uM and kcat = 171 +/- 8 s^-1; derived kcat/Km = 171 / 7.486 = 22.84263959390863 s^-1*mM^-1. The table also prints rounded kcat/Km 2.3 x 10^4 s^-1 M^-1.

normalized_value_unit_evidence: Km normalized_value=7.486 normalized_unit=mM from 7,486 uM / 1000; kcat normalized_value=171 normalized_unit=s^-1; kcat/Km derived normalized_value=22.84263959390863 normalized_unit=s^-1*mM^-1 from 171 / 7.486.

raw_value_unit_evidence: Table II HICDH row under Homocitrate reports Km 7,486 +/- 500 uM, kcat 171 +/- 8 s^-1, and rounded printed kcat/Km 2.3 x 10^4 s^-1 M^-1.

row_label: HICDH row / Homocitrate columns

substrate: homoisocitrate


organism: Mycobacterium tuberculosis


organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

assay_conditions_summary: pH 8.5; cofactor NAD+

column_label: Primary PMC HTML Table 3 row IPMDH_Mj, beta-Isopropylmalate group, K_m (uM) column = 24 +/- 3.

normalized_value_unit_evidence: Normalized paper Km: 24 uM = 0.024 mM, matching export Km 0.024 mM.

raw_value_unit_evidence: Table 3 row IPMDH_Mj reports beta-Isopropylmalate K_m 24 +/- 3 uM and kcat/Km 8.8 x 10^4 M^-1 s^-1.

row_label: IPMDH_Mj row; beta-Isopropylmalate K_m column

table_label: Table 3. Kinetic parameters for IPMDH homologs


organism: Saccharomyces cerevisiae

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


column_label: Primary PDF page 5, Table 2, row Saci_0600 and 3-IPM columns kcat [s^-1], Km [uM], and kcat/Km [s^-1 uM^-1].


column_label: Primary PDF page 5, Table 2, row Saci_0600 and HIC columns kcat [s^-1], Km [uM], and kcat/Km [s^-1 uM^-1].

row_label: Saci_0600; HIC


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

enzyme: ketol-acid reductoisomerase (NADP+)


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


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


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

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH


enzyme_display_name: Homoisocitrate dehydrogenase

assay_conditions_summary: buffer TES

column_label: Table 1 row threo-isohomocitrate under MJ1596 reports Km (mM)=0.037, Vmax=2.6, and Vmax/Km=69.

raw_value_unit_evidence: Km raw_value=0.037 raw_unit=mM

row_label: threo-isohomocitrate / MJ1596

table_label: Table 1. Kinetic data for the overproduced NAD-dependent dehydrogenases from M. jannaschii

enzyme: Homoisocitrate dehydrogenase


substrate_name: NAD+

assay_conditions_summary: pH 8; 313.15 K; cofactor NAD+

proof_lines:
pH 8.0, 40°C, mutant V126A
pH 8.0, 60°C, mutant V126A

substrate: NAD+


proof_lines:
pH 8.0, 40°C, mutant V126S
pH 8.0, 60°C, mutant V126S


proof_lines:
pH 8.0, 40°C, mutant V126G
pH 8.0, 60°C, V126G
pH 8.0, 60°C, mutant V126G


proof_lines:
pH 8.0, 40°C, mutant V126T
pH 8.0, 60°C, mutant V126T


proof_lines:
pH 8.0, 40°C, mutant V126E
pH 8.0, 60°C, mutant V126E


proof_lines:
pH 8.0, 40°C, mutant V126I
pH 8.0, 60°C, mutant V126I


proof_lines:
pH 8.0, 40°C, mutant V126L
pH 8.0, 60°C, mutant V126L


proof_lines:
pH 8.0, 40°C, mutant V126F
pH 8.0, 60°C, mutant V126F


proof_lines:
pH 8.0, 40°C, mutant V126M
pH 8.0, 60°C, mutant V126M


assay_conditions_summary: pH 7.6; 343.15 K; cofactor NAD+


proof_lines: pH 7.6, 70°C, recombinant mutant V181T/P324T/A335E


proof_lines: pH 7.6, 70°C, recombinant mutants F53L and V61I


proof_lines: pH 7.6, 70°C, recombinant mutants S261N and A335E


proof_lines: pH 7.6, 70°C, recombinant mutant L134N/V181T/P324T/A335E


substrate_name: threo-D,L-isopropylmalate

substrate: threo-D,L-isopropylmalate


substrate_name: NADPH

assay_conditions_summary: pH 8; 295.15 K; cofactor NADPH

proof_lines: pH 8.0, 22°C, reaction with acetolactate, mutant enzyme K75Q


substrate_name: NADP+

assay_conditions_summary: pH 8; 295.15 K; cofactor NADP+

proof_lines: pH 8.0, 22°C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme R68Q


proof_lines: pH 8.0, 22°C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme R76Q


proof_lines: pH 8.0, 22°C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme K69L


proof_lines: pH 8.0, 22°C, reaction with 2,3-dihydroxy-3-methylbutanoate, mutant enzyme K75Q


assay_conditions_summary: pH 8; 295.15 K; cofactor NADH

proof_lines:
wild type enzyme
pH 8.0, 22°C, wild type enzyme

substrate: NADH


proof_lines: pH 8.0, 22°C, reaction with acetolactate, mutant enzyme R76Q

proof_lines: pH 8.0, 22°C, reaction with 2-acetolactate, mutant enzyme R76Q


proof_lines: pH 8.0, 22°C, reaction with acetolactate, mutant enzyme R68Q

proof_lines: pH 8.0, 22°C, reaction with 2-acetolactate, mutant enzyme R68QL


proof_lines: pH 8.0, 22°C, mutant enzyme R68D/K69L/K75V/R76D

proof_lines: pH 8, 22°C, mutant enzyme R68D/K69L/K75V/R76D


proof_lines:
pH 8, 22°C, mutant enzyme R76Q/R68A
mutant enzyme R76Q/R68A


proof_lines: pH 8, 22°C, mutant enzyme R68D/K69L/K75V/R76D and mutant enzyme R76D


proof_lines:
pH 8, 22°C, wild type enzyme
pH 8.0, 37°C, wild-type enzyme
pH 8.0, 22°C, wild type enzyme


proof_lines: pH 8.0, 22°C, reaction with acetolactate, mutant enzyme K69L


proof_lines:
pH 8, 22°C, mutant enzyme R76D
mutant enzyme R76D


proof_lines: mutant enzyme E270A, in the presence of K+, at pH 7.6 and 20°C

proof_lines: mutant enzyme E270A, in the presence of 25 mM K+, at pH 7.6 and 20°C


assay_conditions_summary: pH 7.6; 293.15 K; cofactor NAD+


organism: Streptococcus pneumoniae

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH


proof_lines: wild type enzyme, in the presence of K+, at pH 7.6 and 20°C


assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+


enzyme_display_name: hydroxymethylglutaryl-CoA reductase

organism: Pseudomonas sp. 'mevalonii'

substrate_name: CoASH

proof_lines: H381A mutant, oxidative acylation of mevalonate

enzyme: hydroxymethylglutaryl-CoA reductase

substrate: CoASH


proof_lines: wild-type enzyme, oxidative acylation of mevalonate


proof_lines: H381Q mutant, oxidative acylation of mevalonate


assay_conditions_summary: cofactor NAD+


proof_lines: H381N mutant, oxidative acylation of mevalonate


substrate_name: (R,S)-mevalonate

smiles: CC(CCO)(CC(=O)[O-])O

substrate: (R,S)-mevalonate


proof_lines: H381K mutant, oxidative acylation of mevalonate


substrate_name: Tartrate

assay_conditions_summary: pH 7.3; 294.15 K; cofactor NADP+

proof_lines: pH 7.3, 21°C, reaction with NADP+, wild-type enzyme

proof_lines: pH 7.3, 21°C, reaction with NAD+, wild-type enzyme

proof_lines: pH 7.3, 21°C, cofactor: NAD+, wild-type enzyme

substrate: Tartrate


proof_lines: pH 7.3, 21°C, reaction with tartrate, wild-type enzyme

proof_lines: pH 7.3, 21°C, reaction with isopropylmalate, wild-type enzyme

proof_lines: pH 7.3, 21°C, reaction with malate, wild-type enzyme

substrate: NADP+


substrate_name: malate

assay_conditions_summary: pH 7.3; 294.15 K; cofactor NAD+

proof_lines: pH 7.3, 21°C, reaction with NAD+, mutant enzyme E87Q

proof_lines: pH 7.3, 21°C, cofactor: NAD+, isopropylmalate dehydrogenase mutant E87Q

substrate: malate


substrate_name: isopropylmalate

proof_lines: pH 7.3, 21°C, reaction with NAD+, mutant enzyme E87G

proof_lines: pH 7.3, 21°C, cofactor: NAD+, mutant enzyme E87G

substrate: isopropylmalate


proof_lines: pH 7.3, 21°C, reaction with isopropylmalate, mutant enzyme E87G

proof_lines: pH 7.3, 21°C, reaction with tartrate, mutant enzyme E87G

proof_lines: pH 7.3, 21°C, isopropylmalate dehydrogenase mutant E87G


proof_lines: pH 7.3, 21°C, cofactor: NAD+, mutant enzyme E87Q


proof_lines: pH 7.3, 21°C, reaction with isopropylmalate, mutant enzyme E87Q

proof_lines: pH 7.3, 21°C, isopropylmalate dehydrogenase mutant E87Q

proof_lines: pH 7.3, 21°C, reaction with malate, mutant enzyme E87Q


proof_lines: pH 7.3, 21°C, cofactor: NAD+, isopropylmalate dehydrogenase mutant E87G


proof_lines: pH 7.3, 21°C, reaction with malate, mutant enzyme E87G or reaction with tartrate, mutant enzyme E87Q


proof_lines: pH 7.3, 21°C, reaction with NADP+, wild-type enzyme

proof_lines: pH 7.3, 21°C, reaction with NAD+, wild-type enzyme

proof_lines: pH 7.3, 21°C, cofactor: NAD+, wild-type enzyme


proof_lines: mutant enzyme A172D, at 55°C, pH not specified in the publication


assay_conditions_summary: 328.15 K; cofactor NAD+


proof_lines: mutant enzyme A172Q, at 55°C, pH not specified in the publication


proof_lines: mutant enzyme A172N, at 55°C, pH not specified in the publication


proof_lines: mutant enzyme A172E, at 55°C, pH not specified in the publication


proof_lines:
pH 8.0, 40°C, mutant enzyme C275T
pH 8.0, 70°C, mutant enzyme C275T


proof_lines: pH 8.0, 40°C, reaction with 3-D-isopropylmalate, mutant enzyme C275T


proof_lines: pH 8.0, 40°C, mutant enzyme A31G/G43A/A709G

proof_lines: pH 8.0, 70°C, mutant enzyme A31G/G43A/A709G


proof_lines:
pH 8.0, 40°C, mutant enzyme G43A
pH 8.0, 70°C, mutant enzyme G43A


proof_lines:
pH 8.0, 40°C, mutant enzyme G43A
pH 8.0, 70°C, mutant enzyme G43A
at 70°C, mutant enzyme G43A


proof_lines:
pH 8.0, 40°C, mutant enzyme G376A
pH 8.0, 70°C, mutant enzyme G376A


proof_lines: pH 8.0, 40°C, isopropylmalate dehydrogenase cold-adapted mutant T1155

proof_lines: at 40°C, isopropylmalate dehydrogenase cold-adapted mutant P215

proof_lines: 70°C, isopropylmalate dehydrogenase cold-adapted mutant P215


organism: Bacillus subtilis


proof_lines: pH 7.3, 21°C, reaction with NADP+, mutant enzyme S226R/D278K/I279Y

proof_lines: pH 7.3, 21°C, reaction with NAD+, mutant enzyme S226R/D278K/I279Y


proof_lines: pH 7.3, 21°C, reaction with isopropylmalate, mutant enzyme S226R/D278K/I279Y

proof_lines: pH 7.3, 21°C, mutant enzyme S226R/D278K/I279Y


proof_lines: pH 7.3, 21°C, reaction with NAD+, wild-type enzyme

proof_lines: pH 7.3, 21°C, reaction with NADP+, wild-type enzyme

proof_lines: pH 7.3, 21°C, cofactor: NAD+, wild-type enzyme


proof_lines: pH 7.3, 21°C, reaction with isopropylmalate, wild-type enzyme

proof_lines: pH 7.3, 21°C, reaction with tartrate, wild-type enzyme or reaction with malate, mutant enzyme E87Q


proof_lines: pH 7.3, 21°C, reaction with NAD+, mutant enzyme S226R

proof_lines: pH 7.3, 21°C, reaction with NADP+, mutant enzyme S226R


proof_lines: pH 7.3, 21°C, reaction with isopropylmalate, mutant enzyme S226R


proof_lines: pH 7.3, 21°C, mutant enzyme D278K, I279T, P325Y and 395-Arg


organism: Arabidopsis thaliana


enzyme_display_name: glyoxylate reductase (NADP+)

organism: Oryza sativa Japonica Group

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADPH

proof_lines:
isoform GR1, at pH 7.4 and 30°C
isoform GR2, at pH 7.4 and 30°C

enzyme: glyoxylate reductase (NADP+)


substrate_name: glyoxylate

proof_lines: isoform GR1, with NADPH as cosubstrate, at pH 7.4 and 30°C

proof_lines: isoform GR2, with NADPH as cosubstrate, at pH 7.4 and 30°C

proof_lines: isoform GR2, with NADH as cosubstrate, at pH 7.4 and 30°C

substrate: glyoxylate


substrate_name: NADH

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADH

proof_lines:
isoform GR2, at pH 7.4 and 30°C
isoform GR1, at pH 7.4 and 30°C


substrate_name: Unknown

proof_lines: isoform GR1, with glyoxylate and NADH as substrates, at pH 7.4 and 30°C

proof_lines: isoform GR2, with glyoxylate and NADH as substrates, at pH 7.4 and 30°C

proof_lines: isoform GR1, with glyoxylate and NADPH as substrates, at pH 7.4 and 30°C

substrate: Unknown


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

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


proof_lines: mutant F137L, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant L133F, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: hydroxypyruvate reductase

organism: Methylorubrum extorquens AM1

assay_conditions_summary: cofactor NADH

enzyme: hydroxypyruvate reductase


assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: Hydroxypyruvate

proof_lines: enzyme in high-salt fraction of DEAE-cellulose chromatography

substrate: Hydroxypyruvate


substrate_name: glycerate

substrate: glycerate


organism: Oryza sativa

assay_conditions_summary: pH 7.1; 298.15 K; cofactor NADPH

proof_lines: isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.1 and 25°C

proof_lines: isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.1 and 25°C

proof_lines: isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 6.5 and 25°C


substrate_name: Succinic semialdehyde

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

proof_lines:
isoform GLYR2, at pH 7.1 and 25°C
isoform GLYR1, at pH 6.5 and 25°C

substrate: Succinic semialdehyde


proof_lines:
reductive deacylation to mevalonate
mevaldate reduction to mevalonate


substrate_name: CoA

assay_conditions_summary: cofactor CoA

proof_lines:
oxidative acylation of mevalonate
mevaldate oxidation

substrate: CoA


proof_lines:
reductive deacylation to mevalonate
oxidative acylation of mevalonate
mevaldate oxidation


proof_lines:
mevaldate oxidation
oxidative acylation of mevalonate


assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADPH

proof_lines: with succinic semialdehyde as substrate, pH 7.6, 30°C

proof_lines: recombinant enzyme, using succinic semialdehyde as fixed substrate, in 50 mM HEPES (pH 7.6), at 30°C

proof_lines: with glyoxylate as substrate, pH 7.6, 30°C


proof_lines: recombinant enzyme, in 50 mM HEPES (pH 7.6), at 30°C

proof_lines: recombinant protein from Escherichia coli


organism: Malus domestica

proof_lines:
isoform GLYR1, at pH 7.5 and 25°C
isoform GLYR2, at pH 7.3 and 25°C


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines: isoform GLYR1, with succinic semialdehyde as cosubstrate, at pH 7.5 and 25°C

proof_lines: isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.3 and 25°C

proof_lines: isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.3 and 25°C


proof_lines:
isoform GLYR2, at pH 7.3 and 25°C
isoform GLYR1, at pH 7.5 and 25°C


organism: Staphylococcus aureus


proof_lines: pH 8.0, 25°C, intact N-isopropyloxalyl hydroxamate is present in only 25% of binding sites, whereas its deoxygenated form is present in the remaining sites. This deoxy form of N-isopropyloxalyl hydroxamate binds rapidly to the enzyme, but w

proof_lines: pH 8.0, temperature not specified in the publication


organism: Thermus thermophilus


mutation_signature: stopped flow experiment

mutation_type: truncation


assay_conditions_summary: cofactor NADP+

proof_lines: competitive with NADPH when glyoxylate is the fixed substrate

proof_lines: uncompetitive with succinic semialdehyde


substrate_name: glycolate

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

proof_lines:
uncompetitive with NADPH
mixed type inhibition with glyoxylate

substrate: glycolate


proof_lines: mixed type inhibition with succinic semialdehyde


organism: Saccharolobus solfataricus

assay_conditions_summary: pH 7.5; 328.15 K; cofactor NADH


assay_conditions_summary: pH 7.5; 328.15 K; cofactor NADPH


proof_lines: pH 7.5, 55°C, 5 mM Mg2+, cofactor: NADPH


organism: Escherichia coli


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


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH


enzyme_display_name: phosphoglycerate dehydrogenase

organism: Bombyx mori

proof_lines: pH and temperature not specified in the publication

enzyme: phosphoglycerate dehydrogenase


enzyme_display_name: tartrate dehydrogenase

organism: Sus scrofa

substrate_name: NADH; H+; 2-Hydroxy-3-oxosuccinate

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

enzyme: tartrate dehydrogenase

substrate: NADH; H+; 2-Hydroxy-3-oxosuccinate


organism: Pseudomonas putida

proof_lines: 2 mM 2,3-dihydroxysuccinate as substrate


proof_lines:
cofactor NADH
cofactor NADPH


enzyme_display_name: diiodophenylpyruvate reductase

organism: Bos taurus

enzyme: diiodophenylpyruvate reductase


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D225A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor NAD+

proof_lines: mutant D225A, pH 7.5, temperature not specified in the publication

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R108Q to reconstruct the assayed variant sequence.

proof_lines: mutant R108Q, pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R108L to reconstruct the assayed variant sequence.

proof_lines: mutant R108L, pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D250A to reconstruct the assayed variant sequence.

proof_lines: mutant D250A, pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R98Q to reconstruct the assayed variant sequence.

proof_lines: mutant R98Q, pH 7.5, temperature not specified in the publication


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

proof_lines: wild-type, pH 7.5, temperature not specified in the publication


substrate_name: D-malate

substrate: D-malate


substrate_name: H+; NADH; 2-Oxoglutarate

substrate: H+; NADH; 2-Oxoglutarate


substrate_name: NADH; H+; 2-Oxoglutarate

substrate: NADH; H+; 2-Oxoglutarate


substrate_name: 2-Oxoglutarate; H+; NADH

substrate: 2-Oxoglutarate; H+; NADH


substrate_name: H+; 2-Oxoglutarate; NADH

substrate: H+; 2-Oxoglutarate; NADH


assay_conditions_summary: pH 7.2; 310.15 K; cofactor NAD+


substrate_name: oxaloacetate

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

substrate: oxaloacetate


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


enzyme_display_name: 3-hydroxybenzyl-alcohol dehydrogenase

organism: Penicillium urticae

substrate_name: 3-Hydroxybenzyl alcohol

enzyme: 3-hydroxybenzyl-alcohol dehydrogenase

substrate: 3-Hydroxybenzyl alcohol


proof_lines:
isoform PGDH1, at pH 8.1 and 37°C
isoform PGDH1, at pH 7.2 and 37°C


assay_conditions_summary: pH 8.1; cofactor NAD+


proof_lines:
isoform PGDH3, at pH 7.2 and 37°C
isoform PGDH3, at pH 8.1 and 37°C


assay_conditions_summary: pH 7.2; cofactor NAD+


proof_lines:
isoform PGDH2, at pH 7.2 and 37°C
isoform PGDH2, at pH 8.1 and 37°C


enzyme_display_name: UniProt Q76KF5

organism: Entamoeba histolytica

proof_lines:
Raw SKiD Env: Temp=25°C, pH=9
Raw SKiD Env: Temp=-----, pH=9

enzyme: UniProt Q76KF5


substrate_name: phosphohydroxypyruvate

substrate: phosphohydroxypyruvate


substrate_name: NADPH

assay_conditions_summary: pH 6.5; cofactor NADPH


substrate_name: NADH

assay_conditions_summary: pH 6.5; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 9; cofactor NAD+


organism: Sulfurisphaera tokodaii

assay_conditions_summary: cofactor NADH

proof_lines: value for 3-phosphohydroxypyruvate reduction using NADH as a cofactor


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

assay_conditions_summary: cofactor NADPH

proof_lines: value for 3-phosphohydroxypyruvate reduction using NADPH as a cofactor


substrate: NADPH


assay_conditions_summary: cofactor NAD+

proof_lines: value for 3-phospho-D-glycerate oxidation using NAD+ as a cofactor


proof_lines: value for 3-phospho-D-glycerate oxidation


enzyme_display_name: UniProt O43175

organism: Homo sapiens

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NAD+

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.5
Raw SKiD Env: Temp=22°C, pH=8
Raw SKiD Env: Temp=-----, pH=8.5

enzyme: UniProt O43175


proof_lines:
Raw SKiD Env: Temp=22°C, pH=8
Raw SKiD Env: Temp=-----, pH=7.5
Raw SKiD Env: Temp=-----, pH=8.5


enzyme_display_name: D-3-phosphoglycerate dehydrogenase

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

enzyme: D-3-phosphoglycerate dehydrogenase


organism: Rickettsia prowazekii

assay_conditions_summary: pH 7.4; cofactor NADPH

proof_lines: pH 7.4, temperature not specified in the publication


substrate_name: glycerone phosphate

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

proof_lines: cosubstrate NADPH, pH 7.4, temperature not specified in the publication

substrate: glycerone phosphate


proof_lines: Essentially identical kinetic constants are found when NADH and NAD(+) are substituted for NADPH and NADP(+), respectively.


proof_lines: pH 7.4, 23°C, feedback-resistant mutant enzyme


assay_conditions_summary: pH 7.4; cofactor NADH


substrate_name: reduced nicotinamide hypoxanthine dinucleotide

proof_lines: pH 7.4, 23°C, wild-type mutant enzyme and feedback-resistant mutant enzyme


organism: Mycobacterium tuberculosis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R72L with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7

proof_lines: mutant enzyme R72L, pH 7.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R72A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R72A, pH 7.0, temperature not specified in the publication


substrate_name: Dihydroxyfumarate

substrate: Dihydroxyfumarate


enzyme_display_name: D-3-phosphoglycerate dehydrogenase 1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 0.2 sec(-1) for 2-oxoglutarate reduction.

enzyme: D-3-phosphoglycerate dehydrogenase 1


enzyme_display_name: D-3-phosphoglycerate dehydrogenase 2

proof_lines: kcat is 0.25 sec(-1) for 2-oxoglutarate reduction.

enzyme: D-3-phosphoglycerate dehydrogenase 2


enzyme_display_name: UniProt P0A9T0

proof_lines: kcat is 0.55 sec(-1) for 3-phospho-D-glycerate oxidation. kcat is 27.8 sec(-1) for 3-phosphonooxypyruvate reduction. kcat is 33.3 sec(-1) for 2-oxoglutarate reduction. kcat is 0.71 sec(-1) for (R)-2-hydroxyglutarate oxidation. kcat is 0.25

enzyme: UniProt P0A9T0


organism: Escherichia coli (strain K12)

substrate_name: NADP(+)

substrate: NADP(+)


substrate_name: acetylpyridine

substrate: acetylpyridine


substrate_name: Thionicotinamide

substrate: Thionicotinamide


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D463A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor NADH


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


organism: Streptomyces coelicolor

assay_conditions_summary: pH 7; buffer 50 mM MOPS

proof_lines: in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication

proof_lines: in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication


substrate_name: L-Tartrate

substrate: L-Tartrate


substrate_name: D-malate


substrate_name: beta-isopropylmalate

column_label: Abstract states beta-isopropylmalate is a substrate for tartrate dehydrogenase with a Km of 14 +/- 2 microM.

raw_value_unit_evidence: Km raw_value=14 +/- 2 raw_unit=microM

row_label: Pseudomonas putida tartrate dehydrogenase with beta-isopropylmalate

table_label: PubMed abstract PMID 8053675

substrate: beta-isopropylmalate


organism: Aphanothece halophytica

proof_lines:
Aphanothece halophytica
3-phosphohydroxypyruvate
3-phosphoglycerate dehydrogenase


proof_lines:
Aphanothece halophytica
3-phospho-D-glycerate
3-phosphoglycerate dehydrogenase


proof_lines:
pig heart
malate dehydrogenase
meso-tartrate


substrate_name: NAD+

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

substrate: NAD+


substrate_name: Glycerate 3-phosphate

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

assay_conditions_summary: pH 7.6; 310.15 K; cofactor NAD+

column_label: Table 1, reaction column '3-phosphoglycerate → 3-phosphohydroxypyravate': row 'Kcat (1/min)' cell = 4.5 (printed as '4.5 ± ...'), row 'Km, 3-phosphoglycerate (mM)' cell = 0.26. Table 1 prints no kcat/Km column; the kcat/Km entry is the quotient of those two cells, 4.5 (1/min) / 0.26 (mM).

normalized_value_unit_evidence: kcat raw 4.5 1/min normalizes to 0.075 s^-1 (divide by 60); km raw 0.26 mM normalizes to 0.26 mM; kcat/Km = 0.075 s^-1 / 0.26 mM = 0.28846153846153844 s^-1 mM^-1 (quotient of the two printed Table 1 cells; the paper prints no kcat/Km column).

raw_value_unit_evidence: Table 1; reaction column 3-phosphoglycerate → 3-phosphohydroxypyravate; column 'Kcat (1/min)'; raw value 4.5 1/min | Table 1; reaction column 3-phosphoglycerate → 3-phosphohydroxypyravate; column 'Km, 3-phosphoglycerate (mM)'; raw value 0.26 mM

row_label: 3-phosphoglycerate → 3-phosphohydroxypyravate | Km, 3-phosphoglycerate (mM)

table_label: Table 1. Michaelis-Menten Parameters of the Different Reactions Catalyzed by PHGDH, Compared to Intracellular Concentrations of the Corresponding Substrates and Products in Different Cell Lines.

substrate: Glycerate 3-phosphate


column_label: Table 1, reaction column '3-phosphoglycerate → 3-phosphohydroxypyravate': row 'Kcat (1/min)' cell = 4.5 (printed as '4.5 ± ...'), row 'Km, NAD+ (mM)' cell = 0.022. Table 1 prints no kcat/Km column; the kcat/Km entry is the quotient of those two cells, 4.5 (1/min) / 0.022 (mM).

normalized_value_unit_evidence: kcat raw 4.5 1/min normalizes to 0.075 s^-1 (divide by 60); km raw 0.022 mM normalizes to 0.022 mM; kcat/Km = 0.075 s^-1 / 0.022 mM = 3.409090909090909 s^-1 mM^-1 (quotient of the two printed Table 1 cells; the paper prints no kcat/Km column).

raw_value_unit_evidence: Table 1; reaction column 3-phosphoglycerate → 3-phosphohydroxypyravate; column 'Kcat (1/min)'; raw value 4.5 1/min | Table 1; reaction column 3-phosphoglycerate → 3-phosphohydroxypyravate; column 'Km, NAD+ (mM)'; raw value 0.022 mM

row_label: 3-phosphoglycerate → 3-phosphohydroxypyravate | Km, NAD+ (mM)


enzyme_display_name: D-3-phosphoglycerate dehydrogenase 2, chloroplastic

organism: Arabidopsis thaliana

substrate_name: 3-phosphonooxypyruvate (at pH 7.1)

assay_conditions_summary: pH 7.1; cofactor NAD+

substrate: 3-phosphonooxypyruvate (at pH 7.1)


substrate_name: NADH (at pH 7.1)

enzyme: D-3-phosphoglycerate dehydrogenase 2, chloroplastic

substrate: NADH (at pH 7.1)


proof_lines:
NAD+
0.09 mM
Pseudomonas putida


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K263A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature K263A matches the mutant residue at offset +0 and the reference residue at offset -9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


proof_lines: pH 7.5, 25°C, recombinant mutant G317V/G318V


proof_lines: pH 7.5, 25°C, recombinant mutant G316V/G317V


proof_lines: pH 7.5, 25°C, recombinant mutant G316V/G318V


substrate_name: Unknown

substrate: Unknown


organism: Cereibacter sphaeroides


substrate: D-malate


proof_lines:
reaction with D-malate
reaction with (+ L-(+)-tartrate)


assay_conditions_summary: pH 7.6; 310.15 K; buffer 50 mM MOPS


substrate_name: oxaloacetate

substrate: oxaloacetate


assay_conditions_summary: pH 7.6; 310.15 K; cofactor NADH

proof_lines: with 2-oxoglutarate as cosubstrate, at pH 7.6 and 37°C

proof_lines: with oxaloacetate as cosubstrate, at pH 7.6 and 37°C


organism: Escherichia coli


proof_lines: pH 7.5, wild-type enzyme and mutant Q375A


proof_lines: pH and temperature not specified in the publication


proof_lines: pH and temperature not specified in the publication, 12-33/s


substrate_name: pyridinealdehyde adenine dinucleotide

assay_conditions_summary: pH 7.5; buffer 200 mM KPO4

proof_lines: pH 7.5, temperature not specified in the publication

substrate: pyridinealdehyde adenine dinucleotide


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+

proof_lines: with 3-phospho-D-glycerate as cosubstrate, at pH 7.6 and 37°C

proof_lines: pH 8.5, temperature not specified in the publication


proof_lines: mutant enzyme K141R, pH 7.0, temperature not specified in the publication


proof_lines: wild-type enzyme, pH 7.0, temperature not specified in the publication


assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+


organism: Glycine max

substrate_name: NADH

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 7.5; cofactor NADPH

substrate: NADPH


assay_conditions_summary: pH 9.4; cofactor NAD+


enzyme_display_name: ketol-acid reductoisomerase (NADP+)

substrate_name: Hydroxypyruvate

substrate: Hydroxypyruvate


proof_lines: pH 8.0, temperature not specified in the publication


organism: Campylobacter jejuni


organism: Triticum aestivum

assay_conditions_summary: cofactor NAD+


assay_conditions_summary: cofactor NADH


enzyme_display_name: aryl-alcohol dehydrogenase

organism: Streptomyces sp.

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

enzyme: aryl-alcohol dehydrogenase


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: coniferyl aldehyde

substrate: coniferyl aldehyde


substrate_name: alpha-ketoglutarate

substrate: alpha-ketoglutarate


proof_lines:
double mutant H344A/N364A
apparent, double mutant H344A/N364A


proof_lines:
mutant N346A
apparent, mutant N346A


enzyme_display_name: fructuronate reductase

substrate_name: D-fructuronate

enzyme: fructuronate reductase

substrate: D-fructuronate


substrate_name: D-mannonate

substrate: D-mannonate


assay_conditions_summary: pH 7

proof_lines: mutant enzyme R132K, pH 7.0, temperature not specified in the publication


proof_lines: mutant enzyme R72A/R132K, pH 7.0, temperature not specified in the publication


enzyme_display_name: lactaldehyde reductase

substrate_name: L-lactaldehyde

smiles: CC(C=O)O

enzyme: lactaldehyde reductase

substrate: L-lactaldehyde


smiles: CC(CO)O


enzyme_display_name: (R)-aminopropanol dehydrogenase

assay_conditions_summary: pH 7; cofactor NAD+

proof_lines: at pH 9.6 with aminopropanol as substrate

enzyme: (R)-aminopropanol dehydrogenase

substrate: NAD+


enzyme_display_name: 3-isopropylmalate dehydrogenase

substrate_name: D-malate

enzyme: 3-isopropylmalate dehydrogenase


organism: Pseudomonas fluorescens

substrate_name: NAD+


substrate_name: (R)-malate

substrate: (R)-malate


enzyme_display_name: malate dehydrogenase (NADP+)

organism: Sorghum bicolor

proof_lines: recombinant enzyme cloned from expression vector pJ2PCC2

proof_lines: recombinant enzyme cloned from expression vector pJ2PCC1

enzyme: malate dehydrogenase (NADP+)


assay_conditions_summary: cofactor NADPH

proof_lines: recombinant enzyme cloned from expression vector pJCPCC2


organism: Thermus thermophilus

substrate_name: isopropylmalate

substrate: isopropylmalate


assay_conditions_summary: pH 7.6; 343.15 K; cofactor NAD+

proof_lines: pH 7.6, 70°C, reaction with isopropylmalate

proof_lines: pH 7.6, 40°C, reaction with isopropylmalate


substrate_name: tert-butylmalate

substrate: tert-butylmalate


assay_conditions_summary: pH 7.6; 313.15 K; cofactor NAD+


organism: Pseudomonas aeruginosa

substrate_name: erythro-Lg-beta-isopropylmalate

substrate: erythro-Lg-beta-isopropylmalate


assay_conditions_summary: pH 9; 295.15 K; cofactor NAD+


assay_conditions_summary: pH 7.6; 333.15 K; cofactor NAD+

proof_lines: 60°C, pH 7.6, pH 7.6, mutant enzyme A172V


organism: Salmonella enterica subsp. enterica serovar Typhimurium

assay_conditions_summary: pH 9; cofactor NAD+


enzyme_display_name: L-threonine 3-dehydrogenase

organism: Thermoplasma volcanium

substrate_name: L-threonine

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

enzyme: L-threonine 3-dehydrogenase

substrate: L-threonine


assay_conditions_summary: pH 10; 343.15 K; cofactor NAD+


smiles: CC(CN)O


substrate_name: L-serine

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

substrate: L-serine


substrate_name: L-threoninol

smiles: CC(C(CO)N)O

substrate: L-threoninol


enzyme_display_name: acylglycerone-phosphate reductase

organism: Cavia porcellus

substrate_name: NADPH

proof_lines: Km-value below: hexadecyldihydroxyacetone phosphate + NADPH, microsomal enzyme

enzyme: acylglycerone-phosphate reductase


substrate_name: Hexadecyldihydroxyacetone phosphate

substrate: Hexadecyldihydroxyacetone phosphate


organism: uncultured archaeon

proof_lines: 30°C, pH not specified in the publication, mutant enzyme D179N


proof_lines: 30°C, pH not specified in the publication, mutant enzyme D179A


substrate_name: 1-O-Hexadecyl glycerone phosphate; NADPH; H+

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


substrate_name: NADH

proof_lines: cosubstrate hexadecyldihydroxyacetone phosphate, microsomal enzyme, NADPH, cosubstrate hexadecyldihydroxyacetone phosphate, peroxisomal enzyme

substrate: NADH


organism: Carthamus tinctorius

substrate_name: acetoacetyl-[acyl-carrier protein]

substrate: acetoacetyl-[acyl-carrier protein]


substrate: NADPH


proof_lines: 30°C, pH not specified in the publication, mutant enzyme T177A


proof_lines: 30°C, pH not specified in the publication, mutant enzyme S111A


proof_lines: 30°C, pH not specified in the publication, mutant enzyme Y136F


proof_lines: 30°C, pH not specified in the publication, wild-type enzyme


assay_conditions_summary: 303.15 K; cofactor NAD+

proof_lines: 30°C, pH not specified in the publication, mutant enzyme S74A


organism: Aquarana catesbeiana


enzyme_display_name: all-trans-retinol dehydrogenase (NAD+)

organism: Branchiostoma floridae

substrate_name: all-trans-retinal

proof_lines:
isoform 1, pH 6.0, 37°C
isoform 2, pH 6.0, 37°C

enzyme: all-trans-retinol dehydrogenase (NAD+)

substrate: all-trans-retinal


assay_conditions_summary: pH 6; 310.15 K; cofactor NADH

proof_lines:
isoform 2, pH 6.0, 37°C
isoform 1, pH 6.0, 37°C


enzyme_display_name: pantoate 4-dehydrogenase

organism: Pseudomonas sp. P2

substrate_name: D-pantoate

assay_conditions_summary: pH 10

enzyme: pantoate 4-dehydrogenase

substrate: D-pantoate


substrate_name: ketopantoate

substrate: ketopantoate


organism: Kangiella koreensis


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

organism: Rattus norvegicus

proof_lines: Vmax was measured using transfected cell lysates.


substrate_name: androsterone

enzyme: 17-beta-hydroxysteroid dehydrogenase type 6

substrate: androsterone


substrate_name: dihydrotestosterone

substrate: dihydrotestosterone


substrate_name: testosterone

substrate: testosterone


substrate_name: estradiol

substrate: estradiol


substrate_name: NAD

substrate: NAD


substrate_name: NADP

substrate: NADP


organism: Pyrococcus horikoshii

substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E199A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor NAD+

substrate: NAD+


substrate_name: L-threonine

substrate: L-threonine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature R204A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


proof_lines: pH 7.5, 65°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E152A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E152Q with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E152T with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E152S with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E152C with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E152D with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


organism: Homo sapiens

proof_lines: The kinetic parameters were determined using microsomes from transfected cells.


substrate_name: all-trans-retinol

substrate: all-trans-retinol


substrate_name: allopregnanolone

substrate: allopregnanolone


substrate_name: dehydroepiandrosterone

substrate: dehydroepiandrosterone


enzyme_display_name: UniProt Q97BK3

enzyme: UniProt Q97BK3


substrate_name: L-serine

substrate: L-serine


enzyme_display_name: pyridoxal 4-dehydrogenase

organism: Microbacterium luteolum

substrate_name: pyridoxal

assay_conditions_summary: pH 8

enzyme: pyridoxal 4-dehydrogenase

substrate: pyridoxal


substrate_name: L-fucose

substrate: L-fucose


substrate_name: L-Xylose

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

assay_conditions_summary: pH 8; buffer 50 mM sodium phosphate; cofactor NAD+

column_label: Table II; row L-Xylose; columns Km and Kcat confirm required row metrics; Kcat/Km column present but not used for this BRENDA row

normalized_value_unit_evidence: normalized required metrics: Km=3.5 mM; Kcat=214 s^-1; printed Kcat/Km=6.1 s^-1 mM^-1 not required by this row

raw_value_unit_evidence: Table II cells: compound=L-Xylose; Km=3.5 +/- 0.19 mM; Kcat=214 +/- 1.4 s^-1; printed Kcat/Km=6.1 s^-1 mM^-1

row_label: L-Xylose

table_label: Table II

substrate: L-Xylose


substrate_name: D-arabinose

column_label: Table II; row D-Arabinose; columns Km and Kcat confirm required row metrics; Kcat/Km column present but not required here

normalized_value_unit_evidence: normalized required metrics: Km=0.91 mM; Kcat=175 s^-1; table Kcat/Km=192.3 s^-1 mM^-1 not required by this row

raw_value_unit_evidence: Table II cells: compound=D-Arabinose; Km=0.91 +/- 0.08 mM; Kcat=175 +/- 1.9 s^-1; Kcat/Km=192.3 s^-1 mM^-1

row_label: D-Arabinose

substrate: D-arabinose


assay_conditions_summary: pH 8; cofactor NAD+

proof_lines:
cosubstrate L-fucose, pH 8.0, 30°C
cosubstrate pyridoxal, pH 8.0, 30°C
30°C, pH 8.0


substrate_name: NADP+

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines:
cosubstrate L-fucose, pH 8.0, 30°C
30°C, pH 8.0

substrate: NADP+


organism: Saccharomyces cerevisiae

substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S36A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor NADPH

substrate: NADPH


substrate_name: acetoacetyl-CoA

assay_conditions_summary: pH 8; cofactor CoA

substrate: acetoacetyl-CoA


organism: Mus musculus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M333E 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 uniprot_ec_organism_unique and applied mutation signature R180K to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt P14697

organism: Cupriavidus necator

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

enzyme: UniProt P14697


assay_conditions_summary: pH 8; 303.15 K; cofactor CoA


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: acetoacetyl-CoA (at 25 degrees Celsius and at pH 7.0)

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: kcat is 4.3 sec(-1) with beta-ketododecanoyl-CoA as substrate. kcat is 3.5 sec(-1) with beta-ketooctanoyl-CoA as substrate. kcat is 1.9 sec(-1) with acetoacetyl-CoA as substrate. kcat is 2.6 sec(-1) with NADPH as substrate (PubMed:11932442)


substrate_name: NADPH (at 25 degrees Celsius and at pH 7.0)

assay_conditions_summary: pH 7; cofactor NADPH


organism: Arthrobacter sp.

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


organism: Pyrococcus furiosus

assay_conditions_summary: pH 7; cofactor NAD+


assay_conditions_summary: pH 7


enzyme_display_name: UniProt D6PBM7

enzyme: UniProt D6PBM7


enzyme_display_name: Dehydrogenase/reductase SDR family member 6

assay_conditions_summary: cofactor NADH

proof_lines: kcat is 19 sec(-1) for the NADH-dependent reduction of 4-oxo-L-proline. kcat is 0.02 sec(-1) for the NAD(+)-dependent oxidation of (R)-3-hydroxybutanoate.


enzyme: Dehydrogenase/reductase SDR family member 6


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

assay_conditions_summary: pH 7.5; 338.15 K; cofactor NAD+


organism: Mesorhizobium loti

assay_conditions_summary: pH 9.2; 303.15 K; cofactor NAD+


proof_lines: kcat is 14 sec(-1) for the NADH-dependent reduction of 4-oxo-L-proline. kcat is 0.02 sec(-1) for the NAD(+)-dependent oxidation of (R)-3-hydroxybutanoate.


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 1.14 sec(-1) with acetoacetyl-CoA as substrate. kcat is 5.72 sec(-1) with beta-keto-octanoyl-CoA as substrate.


organism: Thermococcus kodakarensis KOD1

assay_conditions_summary: 323.15 K; cofactor NAD+


assay_conditions_summary: cofactor NADPH

proof_lines:
skin fibroblasts, normal cells
skin Zellwenger syndrome fibroblasts


organism: Cytophaga sp.

assay_conditions_summary: pH 9


proof_lines: cosubstrate hexadecyldihydroxyacetone phosphate, brain

proof_lines: cosubstrate palmitoyldihydroxyacetone phosphate, brain


enzyme_display_name: UniProt Q8KZM4

proof_lines:
Raw SKiD Env: Temp=10°C, pH=9
Raw SKiD Env: Temp=40°C, pH=9
Raw SKiD Env: Temp=50°C, pH=9

enzyme: UniProt Q8KZM4


substrate_name: NAD


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P49327 and applied mutation signature K1699A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

column_label: TABLE THREE beta-ketoacyl reductase block, enzyme row K1699A; columns kcat (min^-1), KNADPH (uM) and kcat/KNADPH (uM^-1 min^-1); kcat cell = 20 min^-1; KNADPH cell = 52 uM; kcat/KNADPH cell = 0.39; author manuscript page 15 (PDF page 15). captured primary segment: NADPH | K1699A HFAS, the site-directed K1699A mutant of recombinant human fatty-acid synthase (HFAS) expressed in Sf9 insect cells | TABLE THREE beta-ketoacyl reductase block, enzyme row K1699A: Km NADPH 52 uM | kcat 20 min^-1 | kcat/Km NADPH printed cell 0.39 under the column head kcat/KNADPH (uM^-1 min^-1)

raw_value_unit_evidence: TABLE THREE beta-ketoacyl reductase block, enzyme row K1699A: KNADPH = 52 uM; kcat = 20 min^-1; printed kcat/KNADPH = 0.39 uM^-1 min^-1.

table_label: TABLE THREE (kinetic evaluation of the wild-type and Lys-1699 mutant HFAS enzymes), beta-ketoacyl reductase block; printed column heads enzyme | kcat (min^-1) | KNADPH (uM) | KACAC (uM) | kcat/KNADPH (uM^-1 min^-1) | kcat/KACAC (uM^-1 min^-1)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P49327 and applied mutation signature K1699Q with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

column_label: TABLE THREE beta-ketoacyl reductase block, enzyme row K1699Q; columns kcat (min^-1), KNADPH (uM) and kcat/KNADPH (uM^-1 min^-1); kcat cell = 26 min^-1; KNADPH cell = 123 uM; kcat/KNADPH cell = 0.21; author manuscript page 15 (PDF page 15). captured primary segment: NADPH | K1699Q HFAS, the site-directed K1699Q mutant of recombinant human fatty-acid synthase (HFAS) expressed in Sf9 insect cells | TABLE THREE beta-ketoacyl reductase block, enzyme row K1699Q: Km NADPH 123 uM | kcat 26 min^-1 | kcat/Km NADPH printed cell 0.21 under the column head kcat/KNADPH (uM^-1 min^-1)

raw_value_unit_evidence: TABLE THREE beta-ketoacyl reductase block, enzyme row K1699Q: KNADPH = 123 uM; kcat = 26 min^-1; printed kcat/KNADPH = 0.21 uM^-1 min^-1.


column_label: PMC2442872 section T3; table subsection beta-ketoacyl reductase; row label WT | beta-ketoacyl reductase | NADPH; column label kcat plus substrate-specific K and kcat/K columns

normalized_value_unit_evidence: Unit conversion gives kcat 4.0 s^-1, Km 0.004 mM, and kcat/Km 1000.0 s^-1 mM^-1; these equal the exported central values.

raw_value_unit_evidence: PMC2442872 section T3, row WT | beta-ketoacyl reductase | NADPH; columns kcat, K_NADPH, and kcat/K_NADPH columns: 240 ± 12 min^-1; K_NADPH 4 ± 2 µM; kcat/K_NADPH 60 ± 33 µM^-1 min^-1.

row_label: WT | beta-ketoacyl reductase | NADPH

table_label: Table 3 beta-ketoacyl reductase WT subsection


assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

column_label: TABLE THREE beta-ketoacyl reductase block, enzyme row K1699A; columns kcat (min^-1), KACAC (uM) and kcat/KACAC (uM^-1 min^-1); kcat cell = 20 min^-1; KACAC cell = 2.0 uM; kcat/KACAC cell = 10; author manuscript page 15 (PDF page 15). captured primary segment: acetoacetyl-CoA | K1699A HFAS, the site-directed K1699A mutant of recombinant human fatty-acid synthase (HFAS) expressed in Sf9 insect cells | TABLE THREE beta-ketoacyl reductase block, enzyme row K1699A: Km ACAC 2.0 uM | kcat 20 min^-1 | kcat/Km ACAC printed cell 10 under the column head kcat/KACAC (uM^-1 min^-1)

raw_value_unit_evidence: TABLE THREE beta-ketoacyl reductase block, enzyme row K1699A: KACAC = 2.0 uM; kcat = 20 min^-1; printed kcat/KACAC = 10 uM^-1 min^-1.