sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q102E with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


enzyme_display_name: L-lactate dehydrogenase

organism: Geobacillus stearothermophilus

source_db: oed

verification_status: verified

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.

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

assay_conditions_summary: pH 6; 298.15 K; cofactor NADH

column_label: Table 1, compound row 1j (2-oxoadipate), WT column of each printed group: column kcat (s^-1) = 5.3; column KM (mM) = 1.6; column kcat/KM (M^-1 s^-1) = 3.3 x 10^3.

normalized_value_unit_evidence: KM: printed Table 1 cell 1.6 mM; the column head prints mM, so no unit conversion applies and the exported value is 1.6 mM. kcat: printed Table 1 cell 5.3 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 5.3 s^(-1). kcat/KM: printed Table 1 cell 3.3 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell converts to 3.3 s^-1 mM^-1. Quotient disclosure for this cell group: 5.3 / 1.6 = 3.3124999999999996 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 1 uses.

raw_value_unit_evidence: Table 1, compound row 1j (2-oxoadipate), WT column: kcat = 5.3 s^-1; KM = 1.6 mM; printed kcat/KM = 3.3 x 10^3 M^-1 s^-1.

row_label: Table 1, compound row 1j (2-oxoadipate), WT column group

table_label: Table 1: Steady State Kinetic Parameters (Biochemistry 1995, volume 34, number 13, pages 4225-4230); printed column groups kcat (s^-1), KM (mM) and kcat/KM (M^-1 s^-1)

data_origin: experimental

enzyme: L-lactate dehydrogenase

status: verified

source: oed


verification_status: unverified

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I240K with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

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

mutation_type: substitution

status: unverified


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I240K/R171Y with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I240R with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q102D with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T246A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T246L with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T246S with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T246V with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


column_label: Table I (Kinetic Parameters of BSLDH and Its Mutants), substrate row '2-ketobutyrate (1b)', enzyme column 'WT'; constant 'kcat (s^-1)' = 124; constant 'KM (mM)' = 0.4; constant 'kcat/KM (M^-1 s^-1)' = 3.1 x 10^5.

normalized_value_unit_evidence: kcat: printed Table I cell 124 s^-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the exported value is 124.0 s^(-1). Km: printed Table I cell 0.4 mM; already in mM, no unit conversion applies; the exported value is 0.4 mM. kcat/Km: printed Table I cell 3.1 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.1 x 10^5 / 1000 = 310.0 s^-1 mM^-1; the exported value is 310.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, substrate row '2-ketobutyrate (1b)', enzyme column 'WT': kcat = 124 s^-1; KM = 0.4 mM; printed kcat/KM = 3.1 x 10^5 M^-1 s^-1.

table_label: Table I: Kinetic Parameters of BSLDH and Its Mutants (Biochemistry 1993, 32(47):12730-12735)


organism: Homo sapiens


organism: Plasmodium falciparum


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


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


smiles: CCCCCCC(=O)C(=O)[O-]


substrate_name: 3-Acetylpyridine-adenine dinucleotide

substrate: 3-Acetylpyridine-adenine dinucleotide


organism: Plasmodium malariae


organism: Plasmodium ovale


organism: Plasmodium vivax


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


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00344 and applied mutation signature T246V with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters of BSLDH and Its Mutants), substrate row 'hydroxypyruvate (1f)', enzyme column 'T246V'; constant 'kcat (s^-1)' = 78; constant 'KM (mM)' = 9; constant 'kcat/KM (M^-1 s^-1)' = 8.6 x 10^3.

normalized_value_unit_evidence: kcat: printed Table I cell 78 s^-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 78.0 s^(-1). Km: printed Table I cell 9 mM; already in mM, no unit conversion applies; the paper value is 9.0 mM. kcat/Km: printed Table I cell 8.6 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.6 x 10^3 / 1000 = 8.6 s^-1 mM^-1; the paper value is 8.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, substrate row 'hydroxypyruvate (1f)', enzyme column 'T246V': kcat = 78 s^-1; KM = 9 mM; printed kcat/KM = 8.6 x 10^3 M^-1 s^-1.

status: corrected


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


column_label: Table 1, compound row 1k (omega-amino-alpha-ketobutyrate), WT column of each printed group: column kcat (s^-1) = 0.3; column KM (mM) = 38; column kcat/KM (M^-1 s^-1) = 7.9.

normalized_value_unit_evidence: KM: printed Table 1 cell 38 mM; the column head prints mM, so no unit conversion applies and the exported value is 38.0 mM. kcat: printed Table 1 cell 0.3 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 0.3 s^(-1). kcat/KM: printed Table 1 cell 7.9 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell converts to 0.0079 s^-1 mM^-1. Quotient disclosure for this cell group: 0.3 / 38 = 0.007894736842105263 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures Table 1 uses.

raw_value_unit_evidence: Table 1, compound row 1k (omega-amino-alpha-ketobutyrate), WT column: kcat = 0.3 s^-1; KM = 38 mM; printed kcat/KM = 7.9 M^-1 s^-1.

row_label: Table 1, compound row 1k (omega-amino-alpha-ketobutyrate), WT column group


substrate_name: alpha-Ketovaline

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

substrate: alpha-Ketovaline


organism: Cryptosporidium parvum

substrate_name: APAD+

substrate: APAD+


substrate_name: APADH

substrate: APADH


substrate_name: L-Lactate

substrate: L-Lactate


assay_conditions_summary: pH 9.2; 298.15 K; buffer 1 mL of 0.1 M Tris-HCl; cofactor NAD+

column_label: Table 1: Substrate Kinetic Parameters of pLDH (Biochemistry 2004, 43(20): 6219-6229); printed column heads substrate | kcat (min-1) | Km (uM) | Kcat/Km (min-1 M-1). Table 1, lactate block, poLDH row; column kcat (min-1) = 1.5 x 10^3; column Km (uM) = 93000; column Kcat/Km (min-1 M-1) = 1.6 x 10^4. captured primary segment: poLDH, recombinant wild-type Plasmodium ovale lactate dehydrogenase | substrate lactate | Km 93000 uM | kcat 1.5 x 10^3 min^-1 | kcat/Km 1.6 x 10^4 min^-1 M^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 93000 uM under the printed column head Km (uM); 1 uM is 1/1000 mM, so 93000 / 1000 = 93.0 mM. kcat: printed Table 1 kcat cell 1.5 x 10^3 min^-1 under the printed column head kcat (min-1); 1 min^-1 is 1/60 s^-1, so 1.5 x 10^3 / 60 = 25.0 s^(-1). kcat/Km: printed Table 1 Kcat/Km cell 1.6 x 10^4 min^-1 M^-1 under the printed column head Kcat/Km (min-1 M-1); 1 min^-1 M^-1 is 1/60000 s^-1 mM^-1, so the printed cell is 0.26666666666666666 s^(-1)*mM^(-1). Quotient of this row's own printed component cells: 25.0 / 93.0 = 0.26881720430107525 s^-1 mM^-1, which is the exported catalytic efficiency; the printed efficiency cell is that quotient written to the two significant figures the column uses.

raw_value_unit_evidence: Table 1, lactate block, poLDH row: kcat (min-1) cell = 1.5 x 10^3; Km (uM) cell = 93000; Kcat/Km (min-1 M-1) cell = 1.6 x 10^4.

row_label: Table 1, lactate block, poLDH row


substrate_name: NAD+

assay_conditions_summary: pH 9.2; 298.15 K; cofactor NAD+

substrate: NAD+


column_label: Table 2: Cofactor Kinetic Parameters of PLDH (Biochemistry 2004, 43(20): 6219-6229); printed column heads cofactor | kcat (min-1) | Km (uM) | Kcat/Km (min-1 M-1). Table 2, NAD block, poLDH row; column kcat (min-1) = 1.5 x 10^3; column Km (uM) = 311; column Kcat/Km (min-1 M-1) = 4.8 x 10^6. captured primary segment: poLDH, recombinant wild-type Plasmodium ovale lactate dehydrogenase | substrate NAD+ | Km 311 uM | kcat 1.5 x 10^3 min^-1 | kcat/Km 4.8 x 10^6 min^-1 M^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 311 uM under the printed column head Km (uM); 1 uM is 1/1000 mM, so 311 / 1000 = 0.311 mM. kcat: printed Table 2 kcat cell 1.5 x 10^3 min^-1 under the printed column head kcat (min-1); 1 min^-1 is 1/60 s^-1, so 1.5 x 10^3 / 60 = 25.0 s^(-1). kcat/Km: printed Table 2 Kcat/Km cell 4.8 x 10^6 min^-1 M^-1 under the printed column head Kcat/Km (min-1 M-1); 1 min^-1 M^-1 is 1/60000 s^-1 mM^-1, so the printed cell is 80.0 s^(-1)*mM^(-1). Quotient of this row's own printed component cells: 25.0 / 0.311 = 80.38585209003216 s^-1 mM^-1, which is the exported catalytic efficiency; the printed efficiency cell is that quotient written to the two significant figures the column uses.

raw_value_unit_evidence: Table 2, NAD block, poLDH row: kcat (min-1) cell = 1.5 x 10^3; Km (uM) cell = 311; Kcat/Km (min-1 M-1) cell = 4.8 x 10^6.

row_label: Table 2, NAD block, poLDH row


substrate_name: NADH

assay_conditions_summary: pH 5.5; 298.15 K; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


sequence_variant_note: Mutation signature S245A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: Oxomalonate

substrate: Oxomalonate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I240R/R171Y with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00344 and applied mutation signature Q102E with inferred residue-numbering offset -16 to reconstruct the assayed variant sequence.

column_label: Table 1, compound row 1g (oxomalonate), Q102E column of each printed group: column kcat (s^-1) = 28; column KM (mM) = 10.2; column kcat/KM (M^-1 s^-1) = 2.8 x 10^3.

normalized_value_unit_evidence: KM: printed Table 1 cell 10.2 mM; the column head prints mM, so no unit conversion applies and the exported value is 10.2 mM. kcat: printed Table 1 cell 28 s^-1; the column head prints s^-1, so no unit conversion applies and the exported value is 28.0 s^(-1). kcat/KM: printed Table 1 cell 2.8 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell converts to 2.8 s^-1 mM^-1. Quotient disclosure for this cell group: 28 / 10.2 = 2.7450980392156863 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell lies outside the last-place rounding interval of that quotient, so this record carries the printed cell as the paper value for kcat_over_km alone.

raw_value_unit_evidence: Table 1, compound row 1g (oxomalonate), Q102E column: kcat = 28 s^-1; KM = 10.2 mM; printed kcat/KM = 2.8 x 10^3 M^-1 s^-1.

row_label: Table 1, compound row 1g (oxomalonate), Q102E column group

table_label: Table 1: Steady State Kinetic Parameters (Biochemistry 1995, volume 34, number 13, pages 4225-4230); printed column groups kcat (s^-1), KM (mM) and kcat/KM (M^-1 s^-1), each printing a WT, a Q102E and a Q102D column


substrate_name: oxaloacetate

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

substrate: oxaloacetate


substrate_name: pyruvate

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

substrate: pyruvate


organism: Anas platyrhynchos


organism: Bos taurus


organism: Gallus gallus


substrate_name: phenylpyruvate

substrate: phenylpyruvate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S163L with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature S163L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Lactobacillus helveticus


organism: Oryctolagus cuniculus


assay_conditions_summary: pH 7.5; 298.15 K; buffer 1 mL of 0.1 M sodium phosphate; cofactor NADH

column_label: Table 1: Substrate Kinetic Parameters of pLDH (Biochemistry 2004, 43(20): 6219-6229); printed column heads substrate | kcat (min-1) | Km (uM) | Kcat/Km (min-1 M-1). Table 1, pyruvate block, pmLDH row; column kcat (min-1) = 7.5 x 10^3; column Km (uM) = 140; column Kcat/Km (min-1 M-1) = 5.4 x 10^7. captured primary segment: pmLDH, recombinant wild-type Plasmodium malariae lactate dehydrogenase | substrate pyruvate | Km 140 uM | kcat 7.5 x 10^3 min^-1 | kcat/Km 5.4 x 10^7 min^-1 M^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 140 uM under the printed column head Km (uM); 1 uM is 1/1000 mM, so 140 / 1000 = 0.14 mM. kcat: printed Table 1 kcat cell 7.5 x 10^3 min^-1 under the printed column head kcat (min-1); 1 min^-1 is 1/60 s^-1, so 7.5 x 10^3 / 60 = 125.0 s^(-1). kcat/Km: printed Table 1 Kcat/Km cell 5.4 x 10^7 min^-1 M^-1 under the printed column head Kcat/Km (min-1 M-1); 1 min^-1 M^-1 is 1/60000 s^-1 mM^-1, so the printed cell is 900.0 s^(-1)*mM^(-1). Quotient of this row's own printed component cells: 125.0 / 0.14 = 892.8571428571428 s^-1 mM^-1, which is the exported catalytic efficiency; the printed efficiency cell is that quotient written to the two significant figures the column uses.

raw_value_unit_evidence: Table 1, pyruvate block, pmLDH row: kcat (min-1) cell = 7.5 x 10^3; Km (uM) cell = 140; Kcat/Km (min-1 M-1) cell = 5.4 x 10^7.

row_label: Table 1, pyruvate block, pmLDH row


organism: Squalus acanthias


organism: Toxoplasma gondii


enzyme_display_name: D-lactate dehydrogenase

organism: Pediococcus acidilactici

assay_conditions_summary: pH 5.5; 303.15 K; cofactor NADH

column_label: Table 2 (Kinetic parameters of the wild-type and engineered paLDH), substrate block '2-Oxo butyrate', column head 'Wild type'; parameter row 'Km (mM)' = 11; parameter row 'kcat (s-1)' = 50.7; parameter row 'kcat/Km (s-1 mM-1)' = 4.40. In the rendering every value on those three lines starts at the same character column as its variant head, which fixes the column reading.

normalized_value_unit_evidence: kcat: printed Table 2 cell 50.7 under the parameter head kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 50.7 s^(-1). Km: printed Table 2 cell 11 under the parameter head Km (mM); mM is already canonical, so no unit conversion applies and the value is 11.0 mM. kcat/Km: printed Table 2 cell 4.40 under the parameter head kcat/Km (s-1 mM-1); 1 s-1 mM-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the printed efficiency is 4.4 s^(-1)*mM^(-1). The catalog carries 4.609090909090909 s^(-1)*mM^(-1), the arithmetic quotient 50.7 / 11 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy replaces it with the printed primary value 4.4 s^(-1)*mM^(-1) and the two component metrics stand.

raw_value_unit_evidence: PMID: 31190286; Table 2, substrate block '2-Oxo butyrate', column 'Wild type': Km = 11 mM; kcat = 50.7 s-1; printed kcat/Km = 4.40 in a parameter row headed kcat/Km (s-1 mM-1).

table_label: Table 2: Kinetic parameters of the wild-type and engineered paLDH (Applied Biochemistry and Biotechnology 2019, 189:1141-1155). Printed column heads: Substrate; Parameter; Wild type; Y51L; Y51M; Y51F; Y51A; Y51S. Printed parameter heads inside each substrate block: Km (mM); kcat (s-1); kcat/Km (s-1 mM-1).

enzyme: D-lactate dehydrogenase


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E0NDE9 and applied mutation signature Y51F to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of the wild-type and engineered paLDH), substrate block '2-Oxo butyrate', column head 'Y51F'; parameter row 'Km (mM)' = 2.7; parameter row 'kcat (s-1)' = 99.4; parameter row 'kcat/Km (s-1 mM-1)' = 37.2. In the rendering every value on those three lines starts at the same character column as its variant head, which fixes the column reading.

normalized_value_unit_evidence: kcat: printed Table 2 cell 99.4 under the parameter head kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 99.4 s^(-1). Km: printed Table 2 cell 2.7 under the parameter head Km (mM); mM is already canonical, so no unit conversion applies and the value is 2.7 mM. kcat/Km: printed Table 2 cell 37.2 under the parameter head kcat/Km (s-1 mM-1); 1 s-1 mM-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the printed efficiency is 37.2 s^(-1)*mM^(-1). The catalog carries 36.81481481481482 s^(-1)*mM^(-1), the arithmetic quotient 99.4 / 2.7 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy replaces it with the printed primary value 37.2 s^(-1)*mM^(-1) and the two component metrics stand.

raw_value_unit_evidence: PMID: 31190286; Table 2, substrate block '2-Oxo butyrate', column 'Y51F': Km = 2.7 mM; kcat = 99.4 s-1; printed kcat/Km = 37.2 in a parameter row headed kcat/Km (s-1 mM-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E0NDE9 and applied mutation signature Y51L to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of the wild-type and engineered paLDH), substrate block '2-Oxo butyrate', column head 'Y51L'; parameter row 'Km (mM)' = 12; parameter row 'kcat (s-1)' = 199; parameter row 'kcat/Km (s-1 mM-1)' = 16.8. In the rendering every value on those three lines starts at the same character column as its variant head, which fixes the column reading.

normalized_value_unit_evidence: kcat: printed Table 2 cell 199 under the parameter head kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 199.0 s^(-1). Km: printed Table 2 cell 12 under the parameter head Km (mM); mM is already canonical, so no unit conversion applies and the value is 12.0 mM. kcat/Km: printed Table 2 cell 16.8 under the parameter head kcat/Km (s-1 mM-1); 1 s-1 mM-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the printed efficiency is 16.8 s^(-1)*mM^(-1). The catalog carries 16.583333333333332 s^(-1)*mM^(-1), the arithmetic quotient 199 / 12 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy replaces it with the printed primary value 16.8 s^(-1)*mM^(-1) and the two component metrics stand.

raw_value_unit_evidence: PMID: 31190286; Table 2, substrate block '2-Oxo butyrate', column 'Y51L': Km = 12 mM; kcat = 199 s-1; printed kcat/Km = 16.8 in a parameter row headed kcat/Km (s-1 mM-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E0NDE9 and applied mutation signature Y51M to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of the wild-type and engineered paLDH), substrate block '2-Oxo butyrate', column head 'Y51M'; parameter row 'Km (mM)' = 7.5; parameter row 'kcat (s-1)' = 152; parameter row 'kcat/Km (s-1 mM-1)' = 20.7. In the rendering every value on those three lines starts at the same character column as its variant head, which fixes the column reading.

normalized_value_unit_evidence: kcat: printed Table 2 cell 152 under the parameter head kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 152.0 s^(-1). Km: printed Table 2 cell 7.5 under the parameter head Km (mM); mM is already canonical, so no unit conversion applies and the value is 7.5 mM. kcat/Km: printed Table 2 cell 20.7 under the parameter head kcat/Km (s-1 mM-1); 1 s-1 mM-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the printed efficiency is 20.7 s^(-1)*mM^(-1). The catalog carries 20.266666666666666 s^(-1)*mM^(-1), the arithmetic quotient 152 / 7.5 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy replaces it with the printed primary value 20.7 s^(-1)*mM^(-1) and the two component metrics stand.

raw_value_unit_evidence: PMID: 31190286; Table 2, substrate block '2-Oxo butyrate', column 'Y51M': Km = 7.5 mM; kcat = 152 s-1; printed kcat/Km = 20.7 in a parameter row headed kcat/Km (s-1 mM-1).


organism: Lactobacillus delbrueckii subsp. bulgaricus

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


organism: Lactobacillus plantarum

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q88VJ2 and applied mutation signature R235K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 303.15 K; cofactor NADH

column_label: Table I, 2-Ketobutyrate block, Lys235 column: row head Km (mM) = 40; row head kcat (s^-1) = 0.1; row head kcat/Km (s^-1 mM^-1) = 0.0025.

normalized_value_unit_evidence: Km: printed Table I cell 40 mM; the printed row head is Km (mM), so no unit conversion applies and the exported value is 40.0 mM. kcat: printed Table I cell 0.1 s^-1; the printed row head is kcat (s^-1), so no unit conversion applies and the exported value is 0.1 s^(-1). kcat/Km: printed Table I cell 0.0025 s^-1 mM^-1; the printed row head is kcat/Km (s^-1 mM^-1), so no unit conversion applies and the exported value is 0.0025 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 0.1 / 40.0 = 0.0025 s^-1 mM^-1, which is the printed efficiency cell.

raw_value_unit_evidence: Table I, 2-Ketobutyrate block, Lys235 column: Km = 40 mM; kcat = 0.1 s^-1; printed kcat/Km = 0.0025 s^-1 mM^-1.

table_label: Table I: Catalytic constants for the wild-type and mutant enzymes (J. Biochem. 1994, volume 115, number 5, pages 930-936); within each substrate block the printed row heads are Km (mM), kcat (s^-1) and kcat/Km (s^-1 mM^-1), and the printed column heads are Wild-type, Lys235 and Gln235


column_label: Table I, 2-Ketobutyrate block, Wild-type column: row head Km (mM) = 25; row head kcat (s^-1) = 700; row head kcat/Km (s^-1 mM^-1) = 28.

normalized_value_unit_evidence: Km: printed Table I cell 25 mM; the printed row head is Km (mM), so no unit conversion applies and the exported value is 25.0 mM. kcat: printed Table I cell 700 s^-1; the printed row head is kcat (s^-1), so no unit conversion applies and the exported value is 700.0 s^(-1). kcat/Km: printed Table I cell 28 s^-1 mM^-1; the printed row head is kcat/Km (s^-1 mM^-1), so no unit conversion applies and the exported value is 28.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 700.0 / 25.0 = 28.0 s^-1 mM^-1, which is the printed efficiency cell.

raw_value_unit_evidence: Table I, 2-Ketobutyrate block, Wild-type column: Km = 25 mM; kcat = 700 s^-1; printed kcat/Km = 28 s^-1 mM^-1.


organism: Fusobacterium nucleatum subsp. nucleatum

smiles: CCCCC(=O)C(=O)[O-]

assay_conditions_summary: pH 7; 303.15 K; buffer containing 0; cofactor NADH

column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block 2-Ketocaproate, enzyme row FNLDH; column k cat (s -1) = 230; column S 0.5 (mM) = 2.6; column kcat/S0.5 (s -1 mM -1) = 87; column K i (mM) = blank for this row; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 230 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 230 s^(-1). Km: printed Table 1 cell 2.6 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 2.6 mM. kcat/Km: printed Table 1 cell 87 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 87 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, 2-Ketocaproate block, FNLDH row: k cat (s -1) cell = 230; S 0.5 (mM) cell = 2.6; kcat/S0.5 (s -1 mM -1) cell = 87.

table_label: Table 1: Kinetic parameters for various 2-ketoacids at pH 7.0 (AMB Express 2014, volume 4, article 76)


organism: Pseudomonas aeruginosa

column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block 2-Ketocaproate, enzyme row PALDH; column k cat (s -1) = 160; column S 0.5 (mM) = 5.8; column kcat/S0.5 (s -1 mM -1) = 27; column K i (mM) = blank for this row; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 160 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 160 s^(-1). Km: printed Table 1 cell 5.8 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 5.8 mM. kcat/Km: printed Table 1 cell 27 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 27 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, 2-Ketocaproate block, PALDH row: k cat (s -1) cell = 160; S 0.5 (mM) cell = 5.8; kcat/S0.5 (s -1 mM -1) cell = 27.


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

column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block 2-Ketoisocaproate, enzyme row FNLDH; column k cat (s -1) = 200; column S 0.5 (mM) = 3.8; column kcat/S0.5 (s -1 mM -1) = 53; column K i (mM) = blank for this row; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 200 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 200 s^(-1). Km: printed Table 1 cell 3.8 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 3.8 mM. kcat/Km: printed Table 1 cell 53 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 53 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, 2-Ketoisocaproate block, FNLDH row: k cat (s -1) cell = 200; S 0.5 (mM) cell = 3.8; kcat/S0.5 (s -1 mM -1) cell = 53.


column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block 2-Ketoisocaproate, enzyme row PALDH; column k cat (s -1) = 39; column S 0.5 (mM) = 12; column kcat/S0.5 (s -1 mM -1) = 3.2; column K i (mM) = blank for this row; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 39 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 39 s^(-1). Km: printed Table 1 cell 12 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 12 mM. kcat/Km: printed Table 1 cell 3.2 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 3.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, 2-Ketoisocaproate block, PALDH row: k cat (s -1) cell = 39; S 0.5 (mM) cell = 12; kcat/S0.5 (s -1 mM -1) cell = 3.2.


column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block 2-Ketoisovalerate, enzyme row FNLDH; column k cat (s -1) = 120; column S 0.5 (mM) = 3.5; column kcat/S0.5 (s -1 mM -1) = 35; column K i (mM) = blank for this row; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 120 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 120 s^(-1). Km: printed Table 1 cell 3.5 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 3.5 mM. kcat/Km: printed Table 1 cell 35 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 35 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, 2-Ketoisovalerate block, FNLDH row: k cat (s -1) cell = 120; S 0.5 (mM) cell = 3.5; kcat/S0.5 (s -1 mM -1) cell = 35.


column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block 2-Ketovalerate, enzyme row FNLDH; column k cat (s -1) = 140; column S 0.5 (mM) = 0.68; column kcat/S0.5 (s -1 mM -1) = 200; column K i (mM) = blank for this row; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 140 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 140 s^(-1). Km: printed Table 1 cell 0.68 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 0.68 mM. kcat/Km: printed Table 1 cell 200 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 200 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, 2-Ketovalerate block, FNLDH row: k cat (s -1) cell = 140; S 0.5 (mM) cell = 0.68; kcat/S0.5 (s -1 mM -1) cell = 200.


column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block 2-Ketovalerate, enzyme row PALDH; column k cat (s -1) = 69; column S 0.5 (mM) = 4.0; column kcat/S0.5 (s -1 mM -1) = 18; column K i (mM) = blank for this row; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 69 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 69 s^(-1). Km: printed Table 1 cell 4.0 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 4 mM. kcat/Km: printed Table 1 cell 18 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 18 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, 2-Ketovalerate block, PALDH row: k cat (s -1) cell = 69; S 0.5 (mM) cell = 4.0; kcat/S0.5 (s -1 mM -1) cell = 18.


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


column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block 2-Ketobutyrate, enzyme row FNLDH; column k cat (s -1) = 140; column S 0.5 (mM) = 0.31; column kcat/S0.5 (s -1 mM -1) = 440; column K i (mM) = blank for this row; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 140 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 140 s^(-1). Km: printed Table 1 cell 0.31 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 0.31 mM. kcat/Km: printed Table 1 cell 440 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 440 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, 2-Ketobutyrate block, FNLDH row: k cat (s -1) cell = 140; S 0.5 (mM) cell = 0.31; kcat/S0.5 (s -1 mM -1) cell = 440.


column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block 2-Ketobutyrate, enzyme row PALDH; column k cat (s -1) = 100; column S 0.5 (mM) = 0.64; column kcat/S0.5 (s -1 mM -1) = 150; column K i (mM) = blank for this row; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 100 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 100 s^(-1). Km: printed Table 1 cell 0.64 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 0.64 mM. kcat/Km: printed Table 1 cell 150 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 150 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, 2-Ketobutyrate block, PALDH row: k cat (s -1) cell = 100; S 0.5 (mM) cell = 0.64; kcat/S0.5 (s -1 mM -1) cell = 150.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R235K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q88VJ2 and applied mutation signature R235Q to reconstruct the assayed variant sequence.

column_label: Table I, Hydroxypyruvate block, Gln235 column: row head Km (mM) = 120; row head kcat (s^-1) = 0.6; row head kcat/Km (s^-1 mM^-1) = 0.005.

normalized_value_unit_evidence: Km: printed Table I cell 120 mM; the printed row head is Km (mM), so no unit conversion applies and the exported value is 120.0 mM. kcat: printed Table I cell 0.6 s^-1; the printed row head is kcat (s^-1), so no unit conversion applies and the exported value is 0.6 s^(-1). kcat/Km: printed Table I cell 0.005 s^-1 mM^-1; the printed row head is kcat/Km (s^-1 mM^-1), so no unit conversion applies and the exported value is 0.005 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 0.6 / 120.0 = 0.005 s^-1 mM^-1, which is the printed efficiency cell.

raw_value_unit_evidence: Table I, Hydroxypyruvate block, Gln235 column: Km = 120 mM; kcat = 0.6 s^-1; printed kcat/Km = 0.005 s^-1 mM^-1.


column_label: Table I, Hydroxypyruvate block, Wild-type column: row head Km (mM) = 2.5; row head kcat (s^-1) = 5,000; row head kcat/Km (s^-1 mM^-1) = 2,000.

normalized_value_unit_evidence: Km: printed Table I cell 2.5 mM; the printed row head is Km (mM), so no unit conversion applies and the exported value is 2.5 mM. kcat: printed Table I cell 5,000 s^-1; the printed row head is kcat (s^-1), so no unit conversion applies and the exported value is 5000.0 s^(-1). kcat/Km: printed Table I cell 2,000 s^-1 mM^-1; the printed row head is kcat/Km (s^-1 mM^-1), so no unit conversion applies and the exported value is 2000.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 5000.0 / 2.5 = 2000.0 s^-1 mM^-1, which is the printed efficiency cell.

raw_value_unit_evidence: Table I, Hydroxypyruvate block, Wild-type column: Km = 2.5 mM; kcat = 5,000 s^-1; printed kcat/Km = 2,000 s^-1 mM^-1.


column_label: Table 2 (Kinetic parameters of the wild-type and engineered paLDH), substrate block '3-Methyl-2-oxo butyrate', column head 'Wild type'; parameter row 'Km (mM)' = 38; parameter row 'kcat (s-1)' = 33.9; parameter row 'kcat/Km (s-1 mM-1)' = 0.892. In the rendering every value on those three lines starts at the same character column as its variant head, which fixes the column reading.

normalized_value_unit_evidence: kcat: printed Table 2 cell 33.9 under the parameter head kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 33.9 s^(-1). Km: printed Table 2 cell 38 under the parameter head Km (mM); mM is already canonical, so no unit conversion applies and the value is 38.0 mM. kcat/Km: printed Table 2 cell 0.892 under the parameter head kcat/Km (s-1 mM-1); 1 s-1 mM-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the printed cell is 0.892 s^(-1)*mM^(-1). The exported ratio 0.8921052631578947 s^(-1)*mM^(-1) is the exact quotient of the same two printed component cells, 33.9 / 38, and the printed cell is that quotient rendered at the precision the paper prints, so the exported value stands and no metric is changed.

raw_value_unit_evidence: PMID: 31190286; Table 2, substrate block '3-Methyl-2-oxo butyrate', column 'Wild type': Km = 38 mM; kcat = 33.9 s-1; printed kcat/Km = 0.892 in a parameter row headed kcat/Km (s-1 mM-1).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y51F to reconstruct the assayed variant sequence.


column_label: Table 2 (Kinetic parameters of the wild-type and engineered paLDH), substrate block '3-Methyl-2-oxo butyrate', column head 'Y51L'; parameter row 'Km (mM)' = 12; parameter row 'kcat (s-1)' = 90.2; parameter row 'kcat/Km (s-1 mM-1)' = 7.41. In the rendering every value on those three lines starts at the same character column as its variant head, which fixes the column reading.

normalized_value_unit_evidence: kcat: printed Table 2 cell 90.2 under the parameter head kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 90.2 s^(-1). Km: printed Table 2 cell 12 under the parameter head Km (mM); mM is already canonical, so no unit conversion applies and the value is 12.0 mM. kcat/Km: printed Table 2 cell 7.41 under the parameter head kcat/Km (s-1 mM-1); 1 s-1 mM-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the printed efficiency is 7.41 s^(-1)*mM^(-1). The catalog carries 7.516666666666667 s^(-1)*mM^(-1), the arithmetic quotient 90.2 / 12 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy replaces it with the printed primary value 7.41 s^(-1)*mM^(-1) and the two component metrics stand.

raw_value_unit_evidence: PMID: 31190286; Table 2, substrate block '3-Methyl-2-oxo butyrate', column 'Y51L': Km = 12 mM; kcat = 90.2 s-1; printed kcat/Km = 7.41 in a parameter row headed kcat/Km (s-1 mM-1).


column_label: Table 2 (Kinetic parameters of the wild-type and engineered paLDH), substrate block '3-Methyl-2-oxo butyrate', column head 'Y51M'; parameter row 'Km (mM)' = 8.6; parameter row 'kcat (s-1)' = 76.2; parameter row 'kcat/Km (s-1 mM-1)' = 8.85. In the rendering every value on those three lines starts at the same character column as its variant head, which fixes the column reading.

normalized_value_unit_evidence: kcat: printed Table 2 cell 76.2 under the parameter head kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 76.2 s^(-1). Km: printed Table 2 cell 8.6 under the parameter head Km (mM); mM is already canonical, so no unit conversion applies and the value is 8.6 mM. kcat/Km: printed Table 2 cell 8.85 under the parameter head kcat/Km (s-1 mM-1); 1 s-1 mM-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the printed efficiency is 8.85 s^(-1)*mM^(-1). The catalog carries 8.860465116279071 s^(-1)*mM^(-1), the arithmetic quotient 76.2 / 8.6 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy replaces it with the printed primary value 8.85 s^(-1)*mM^(-1) and the two component metrics stand.

raw_value_unit_evidence: PMID: 31190286; Table 2, substrate block '3-Methyl-2-oxo butyrate', column 'Y51M': Km = 8.6 mM; kcat = 76.2 s-1; printed kcat/Km = 8.85 in a parameter row headed kcat/Km (s-1 mM-1).


substrate_name: D-Lactate

substrate: D-Lactate


substrate_name: glyoxylate

smiles: O=CC(=O)O

column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block Glyoxylate, enzyme row FNLDH; column k cat (s -1) = 11; column S 0.5 (mM) = 18; column kcat/S0.5 (s -1 mM -1) = 0.70; column K i (mM) = blank for this row; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 11 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 11 s^(-1). Km: printed Table 1 cell 18 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 18 mM. kcat/Km: printed Table 1 cell 0.70 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 0.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Glyoxylate block, FNLDH row: k cat (s -1) cell = 11; S 0.5 (mM) cell = 18; kcat/S0.5 (s -1 mM -1) cell = 0.70.

row_label: Table 1, Glyoxylate block, FNLDH row

substrate: glyoxylate


column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block Glyoxylate, enzyme row PALDH; column k cat (s -1) = 880; column S 0.5 (mM) = 6.8; column kcat/S0.5 (s -1 mM -1) = 130; column K i (mM) = 44; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 880 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 880 s^(-1). Km: printed Table 1 cell 6.8 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 6.8 mM. kcat/Km: printed Table 1 cell 130 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 130 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Glyoxylate block, PALDH row: k cat (s -1) cell = 880; S 0.5 (mM) cell = 6.8; kcat/S0.5 (s -1 mM -1) cell = 130.

row_label: Table 1, Glyoxylate block, PALDH row


substrate_name: Glyoxylate

substrate: Glyoxylate


substrate_name: Hydroxypyruvate

column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block Hydroxypyruvate, enzyme row FNLDH; column k cat (s -1) = 160; column S 0.5 (mM) = 18; column kcat/S0.5 (s -1 mM -1) = 8.7; column K i (mM) = blank for this row; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 160 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 160 s^(-1). Km: printed Table 1 cell 18 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 18 mM. kcat/Km: printed Table 1 cell 8.7 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 8.699999999999999 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Hydroxypyruvate block, FNLDH row: k cat (s -1) cell = 160; S 0.5 (mM) cell = 18; kcat/S0.5 (s -1 mM -1) cell = 8.7.

substrate: Hydroxypyruvate


column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block Hydroxypyruvate, enzyme row PALDH; column k cat (s -1) = 420; column S 0.5 (mM) = 3.0; column kcat/S0.5 (s -1 mM -1) = 140; column K i (mM) = 19; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 420 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 420 s^(-1). Km: printed Table 1 cell 3.0 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 3 mM. kcat/Km: printed Table 1 cell 140 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 140 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Hydroxypyruvate block, PALDH row: k cat (s -1) cell = 420; S 0.5 (mM) cell = 3.0; kcat/S0.5 (s -1 mM -1) cell = 140.


assay_conditions_summary: pH 7; 303.15 K; cofactor NADH


column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block Oxaloacetate, enzyme row FNLDH; column k cat (s -1) = 80; column S 0.5 (mM) = 2.5; column kcat/S0.5 (s -1 mM -1) = 31; column K i (mM) = 140; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 80 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 80 s^(-1). Km: printed Table 1 cell 2.5 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 2.5 mM. kcat/Km: printed Table 1 cell 31 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 31 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Oxaloacetate block, FNLDH row: k cat (s -1) cell = 80; S 0.5 (mM) cell = 2.5; kcat/S0.5 (s -1 mM -1) cell = 31.

row_label: Table 1, Oxaloacetate block, FNLDH row


column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block Oxaloacetate, enzyme row PALDH; column k cat (s -1) = 410; column S 0.5 (mM) = 1.7; column kcat/S0.5 (s -1 mM -1) = 230; column K i (mM) = blank for this row; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 410 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 410 s^(-1). Km: printed Table 1 cell 1.7 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 1.7 mM. kcat/Km: printed Table 1 cell 230 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 230 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Oxaloacetate block, PALDH row: k cat (s -1) cell = 410; S 0.5 (mM) cell = 1.7; kcat/S0.5 (s -1 mM -1) cell = 230.

row_label: Table 1, Oxaloacetate block, PALDH row


column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block Phenylpyruvate, enzyme row FNLDH; column k cat (s -1) = 120; column S 0.5 (mM) = 11; column kcat/S0.5 (s -1 mM -1) = 11; column K i (mM) = 23; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 120 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 120 s^(-1). Km: printed Table 1 cell 11 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 11 mM. kcat/Km: printed Table 1 cell 11 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 11 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Phenylpyruvate block, FNLDH row: k cat (s -1) cell = 120; S 0.5 (mM) cell = 11; kcat/S0.5 (s -1 mM -1) cell = 11.


column_label: Table 2 (Kinetic parameters of the wild-type and engineered paLDH), substrate block 'Phenyl pyruvate', column head 'Wild type'; parameter row 'Km (mM)' = 2.6; parameter row 'kcat (s-1)' = 41.3; parameter row 'kcat/Km (s-1 mM-1)' = 15.9. In the rendering every value on those three lines starts at the same character column as its variant head, which fixes the column reading.

normalized_value_unit_evidence: kcat: printed Table 2 cell 41.3 under the parameter head kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 41.3 s^(-1). Km: printed Table 2 cell 2.6 under the parameter head Km (mM); mM is already canonical, so no unit conversion applies and the value is 2.6 mM. kcat/Km: printed Table 2 cell 15.9 under the parameter head kcat/Km (s-1 mM-1); 1 s-1 mM-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the printed cell is 15.9 s^(-1)*mM^(-1). The exported ratio 15.884615384615383 s^(-1)*mM^(-1) is the exact quotient of the same two printed component cells, 41.3 / 2.6, and the printed cell is that quotient rendered at the precision the paper prints, so the exported value stands and no metric is changed.

raw_value_unit_evidence: PMID: 31190286; Table 2, substrate block 'Phenyl pyruvate', column 'Wild type': Km = 2.6 mM; kcat = 41.3 s-1; printed kcat/Km = 15.9 in a parameter row headed kcat/Km (s-1 mM-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E0NDE9 and applied mutation signature Y51A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of the wild-type and engineered paLDH), substrate block 'Phenyl pyruvate', column head 'Y51A'; parameter row 'Km (mM)' = 0.16; parameter row 'kcat (s-1)' = 269; parameter row 'kcat/Km (s-1 mM-1)' = 1720. In the rendering every value on those three lines starts at the same character column as its variant head, which fixes the column reading.

normalized_value_unit_evidence: kcat: printed Table 2 cell 269 under the parameter head kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 269.0 s^(-1). Km: printed Table 2 cell 0.16 under the parameter head Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.16 mM. kcat/Km: printed Table 2 cell 1720 under the parameter head kcat/Km (s-1 mM-1); 1 s-1 mM-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the printed efficiency is 1720.0 s^(-1)*mM^(-1). The catalog carries 1681.25 s^(-1)*mM^(-1), the arithmetic quotient 269 / 0.16 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy replaces it with the printed primary value 1720.0 s^(-1)*mM^(-1) and the two component metrics stand.

raw_value_unit_evidence: PMID: 31190286; Table 2, substrate block 'Phenyl pyruvate', column 'Y51A': Km = 0.16 mM; kcat = 269 s-1; printed kcat/Km = 1720 in a parameter row headed kcat/Km (s-1 mM-1).


column_label: Table 2 (Kinetic parameters of the wild-type and engineered paLDH), substrate block 'Phenyl pyruvate', column head 'Y51F'; parameter row 'Km (mM)' = 0.22; parameter row 'kcat (s-1)' = 391; parameter row 'kcat/Km (s-1 mM-1)' = 1880. In the rendering every value on those three lines starts at the same character column as its variant head, which fixes the column reading.

normalized_value_unit_evidence: kcat: printed Table 2 cell 391 under the parameter head kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 391.0 s^(-1). Km: printed Table 2 cell 0.22 under the parameter head Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.22 mM. kcat/Km: printed Table 2 cell 1880 under the parameter head kcat/Km (s-1 mM-1); 1 s-1 mM-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the printed efficiency is 1880.0 s^(-1)*mM^(-1). The catalog carries 1777.2727272727273 s^(-1)*mM^(-1), the arithmetic quotient 391 / 0.22 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy replaces it with the printed primary value 1880.0 s^(-1)*mM^(-1) and the two component metrics stand.

raw_value_unit_evidence: PMID: 31190286; Table 2, substrate block 'Phenyl pyruvate', column 'Y51F': Km = 0.22 mM; kcat = 391 s-1; printed kcat/Km = 1880 in a parameter row headed kcat/Km (s-1 mM-1).


column_label: Table 2 (Kinetic parameters of the wild-type and engineered paLDH), substrate block 'Phenyl pyruvate', column head 'Y51L'; parameter row 'Km (mM)' = 0.17; parameter row 'kcat (s-1)' = 376; parameter row 'kcat/Km (s-1 mM-1)' = 2200. In the rendering every value on those three lines starts at the same character column as its variant head, which fixes the column reading.

normalized_value_unit_evidence: kcat: printed Table 2 cell 376 under the parameter head kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 376.0 s^(-1). Km: printed Table 2 cell 0.17 under the parameter head Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.17 mM. kcat/Km: printed Table 2 cell 2200 under the parameter head kcat/Km (s-1 mM-1); 1 s-1 mM-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the printed efficiency is 2200.0 s^(-1)*mM^(-1). The catalog carries 2211.7647058823527 s^(-1)*mM^(-1), the arithmetic quotient 376 / 0.17 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy replaces it with the printed primary value 2200.0 s^(-1)*mM^(-1) and the two component metrics stand.

raw_value_unit_evidence: PMID: 31190286; Table 2, substrate block 'Phenyl pyruvate', column 'Y51L': Km = 0.17 mM; kcat = 376 s-1; printed kcat/Km = 2200 in a parameter row headed kcat/Km (s-1 mM-1).


column_label: Table 2 (Kinetic parameters of the wild-type and engineered paLDH), substrate block 'Phenyl pyruvate', column head 'Y51M'; parameter row 'Km (mM)' = 0.22; parameter row 'kcat (s-1)' = 462; parameter row 'kcat/Km (s-1 mM-1)' = 2130. In the rendering every value on those three lines starts at the same character column as its variant head, which fixes the column reading.

normalized_value_unit_evidence: kcat: printed Table 2 cell 462 under the parameter head kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 462.0 s^(-1). Km: printed Table 2 cell 0.22 under the parameter head Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.22 mM. kcat/Km: printed Table 2 cell 2130 under the parameter head kcat/Km (s-1 mM-1); 1 s-1 mM-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the printed efficiency is 2130.0 s^(-1)*mM^(-1). The catalog carries 2100.0 s^(-1)*mM^(-1), the arithmetic quotient 462 / 0.22 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy replaces it with the printed primary value 2130.0 s^(-1)*mM^(-1) and the two component metrics stand.

raw_value_unit_evidence: PMID: 31190286; Table 2, substrate block 'Phenyl pyruvate', column 'Y51M': Km = 0.22 mM; kcat = 462 s-1; printed kcat/Km = 2130 in a parameter row headed kcat/Km (s-1 mM-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E0NDE9 and applied mutation signature Y51S to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of the wild-type and engineered paLDH), substrate block 'Phenyl pyruvate', column head 'Y51S'; parameter row 'Km (mM)' = 0.40; parameter row 'kcat (s-1)' = 239; parameter row 'kcat/Km (s-1 mM-1)' = 612. In the rendering every value on those three lines starts at the same character column as its variant head, which fixes the column reading.

normalized_value_unit_evidence: kcat: printed Table 2 cell 239 under the parameter head kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 239.0 s^(-1). Km: printed Table 2 cell 0.40 under the parameter head Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.4 mM. kcat/Km: printed Table 2 cell 612 under the parameter head kcat/Km (s-1 mM-1); 1 s-1 mM-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the printed efficiency is 612.0 s^(-1)*mM^(-1). The catalog carries 597.5 s^(-1)*mM^(-1), the arithmetic quotient 239 / 0.40 of the two component cells, which the paper's own printed efficiency cell does not reproduce at the precision it prints, so the ratio policy replaces it with the printed primary value 612.0 s^(-1)*mM^(-1) and the two component metrics stand.

raw_value_unit_evidence: PMID: 31190286; Table 2, substrate block 'Phenyl pyruvate', column 'Y51S': Km = 0.40 mM; kcat = 239 s-1; printed kcat/Km = 612 in a parameter row headed kcat/Km (s-1 mM-1).


column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block Phenylpyruvate, enzyme row PALDH; column k cat (s -1) = 18; column S 0.5 (mM) = 7.1; column kcat/S0.5 (s -1 mM -1) = 2.6; column K i (mM) = blank for this row; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 18 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 18 s^(-1). Km: printed Table 1 cell 7.1 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 7.1 mM. kcat/Km: printed Table 1 cell 2.6 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 2.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Phenylpyruvate block, PALDH row: k cat (s -1) cell = 18; S 0.5 (mM) cell = 7.1; kcat/S0.5 (s -1 mM -1) cell = 2.6.


organism: Lactiplantibacillus plantarum subsp. plantarum


organism: Weizmannia coagulans


substrate_name: (R)-lactate

substrate: (R)-lactate


column_label: Table I, Phenylpyruvate block, Lys235 column: row head Km (mM) = 20; row head kcat (s^-1) = 0.24; row head kcat/Km (s^-1 mM^-1) = 0.012.

normalized_value_unit_evidence: Km: printed Table I cell 20 mM; the printed row head is Km (mM), so no unit conversion applies and the exported value is 20.0 mM. kcat: printed Table I cell 0.24 s^-1; the printed row head is kcat (s^-1), so no unit conversion applies and the exported value is 0.24 s^(-1). kcat/Km: printed Table I cell 0.012 s^-1 mM^-1; the printed row head is kcat/Km (s^-1 mM^-1), so no unit conversion applies and the exported value is 0.012 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 0.24 / 20.0 = 0.012 s^-1 mM^-1, which is the printed efficiency cell.

raw_value_unit_evidence: Table I, Phenylpyruvate block, Lys235 column: Km = 20 mM; kcat = 0.24 s^-1; printed kcat/Km = 0.012 s^-1 mM^-1.


column_label: Table I, Pyruvate block, Lys235 column: row head Km (mM) = 50; row head kcat (s^-1) = 12; row head kcat/Km (s^-1 mM^-1) = 0.24.

normalized_value_unit_evidence: Km: printed Table I cell 50 mM; the printed row head is Km (mM), so no unit conversion applies and the exported value is 50.0 mM. kcat: printed Table I cell 12 s^-1; the printed row head is kcat (s^-1), so no unit conversion applies and the exported value is 12.0 s^(-1). kcat/Km: printed Table I cell 0.24 s^-1 mM^-1; the printed row head is kcat/Km (s^-1 mM^-1), so no unit conversion applies and the exported value is 0.24 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 12.0 / 50.0 = 0.24 s^-1 mM^-1, which is the printed efficiency cell.

raw_value_unit_evidence: Table I, Pyruvate block, Lys235 column: Km = 50 mM; kcat = 12 s^-1; printed kcat/Km = 0.24 s^-1 mM^-1.

row_label: Table I, Pyruvate block, Lys235 column


column_label: Table I, Pyruvate block, Gln235 column: row head Km (mM) = 500; row head kcat (s^-1) = 12; row head kcat/Km (s^-1 mM^-1) = 0.024.

normalized_value_unit_evidence: Km: printed Table I cell 500 mM; the printed row head is Km (mM), so no unit conversion applies and the exported value is 500.0 mM. kcat: printed Table I cell 12 s^-1; the printed row head is kcat (s^-1), so no unit conversion applies and the exported value is 12.0 s^(-1). kcat/Km: printed Table I cell 0.024 s^-1 mM^-1; the printed row head is kcat/Km (s^-1 mM^-1), so no unit conversion applies and the exported value is 0.024 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 12.0 / 500.0 = 0.024 s^-1 mM^-1, which is the printed efficiency cell.

raw_value_unit_evidence: Table I, Pyruvate block, Gln235 column: Km = 500 mM; kcat = 12 s^-1; printed kcat/Km = 0.024 s^-1 mM^-1.

row_label: Table I, Pyruvate block, Gln235 column


enzyme_display_name: 3-hydroxybutyrate dehydrogenase

organism: Alcaligenes faecalis

substrate_name: acetoacetate

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

enzyme: 3-hydroxybutyrate dehydrogenase

substrate: acetoacetate


substrate_name: levulinic acid

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H144A to reconstruct the assayed variant sequence.

smiles: CC(=O)CCC(=O)O

substrate: levulinic acid


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H144F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H144I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H144L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H144L/W187A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H144L/W187F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H144L/W187I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H144L/W187L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H144L/W187V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H144V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W187A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W187F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W187I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W187L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W187V to reconstruct the assayed variant sequence.


organism: Homo sapiens

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


enzyme_display_name: 3-hydroxyisobutyrate dehydrogenase

organism: Mycobacterium tuberculosis

substrate_name: 3-hydroxypropanoic acid

smiles: O=C(O)CCO

enzyme: 3-hydroxyisobutyrate dehydrogenase

substrate: 3-hydroxypropanoic acid


substrate_name: L-serine

substrate: L-serine


organism: Arabidopsis thaliana

assay_conditions_summary: pH 8.5; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 8.5; 303.15 K; cofactor NAD+


substrate_name: NADP+

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADP+

substrate: NADP+


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


source_db: brenda

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W187A to reconstruct the assayed variant sequence.

source: brenda


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W187I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W187V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H144A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H144L/W187A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H144L/W187A, at pH 6.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H144L/W187V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H144L/W187V, at pH 6.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H144L/W187I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H144L/W187I, at pH 6.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W187L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H144V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H144F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H144I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W187F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H144L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H144L/W187L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H144L/W187L, at pH 6.5 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H144L/W187F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H144L/W187F, at pH 6.5 and 30°C


organism: Limosilactobacillus fermentum


substrate_name: NADPH

substrate: NADPH


organism: Sporolactobacillus inulinus

source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


kcat_display: Not reported

kcat_over_km_display: Not reported


organism: Escherichia coli

column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block 2-Ketobutyrate, enzyme row ECLDH; column k cat (s -1) = 31; column S 0.5 (mM) = 30; column kcat/S0.5 (s -1 mM -1) = 1.0; column K i (mM) = blank for this row; column n H = 1.4.

normalized_value_unit_evidence: kcat: printed Table 1 cell 31 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 31 s^(-1). Km: printed Table 1 cell 30 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 30 mM. kcat/Km: printed Table 1 cell 1.0 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, 2-Ketobutyrate block, ECLDH row: k cat (s -1) cell = 31; S 0.5 (mM) cell = 30; kcat/S0.5 (s -1 mM -1) cell = 1.0.


column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block Glyoxylate, enzyme row ECLDH; column k cat (s -1) = 100; column S 0.5 (mM) = 20; column kcat/S0.5 (s -1 mM -1) = 5.3; column K i (mM) = blank for this row; column n H = 1.5.

normalized_value_unit_evidence: kcat: printed Table 1 cell 100 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 100 s^(-1). Km: printed Table 1 cell 20 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 20 mM. kcat/Km: printed Table 1 cell 5.3 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 5.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Glyoxylate block, ECLDH row: k cat (s -1) cell = 100; S 0.5 (mM) cell = 20; kcat/S0.5 (s -1 mM -1) cell = 5.3.

row_label: Table 1, Glyoxylate block, ECLDH row


column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block Hydroxypyruvate, enzyme row ECLDH; column k cat (s -1) = 50; column S 0.5 (mM) = 12; column kcat/S0.5 (s -1 mM -1) = 4.2; column K i (mM) = blank for this row; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 50 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 50 s^(-1). Km: printed Table 1 cell 12 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 12 mM. kcat/Km: printed Table 1 cell 4.2 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 4.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Hydroxypyruvate block, ECLDH row: k cat (s -1) cell = 50; S 0.5 (mM) cell = 12; kcat/S0.5 (s -1 mM -1) cell = 4.2.


column_label: Table 1 (Kinetic parameters for various 2-ketoacids at pH 7.0), substrate block Oxaloacetate, enzyme row ECLDH; column k cat (s -1) = 1,100; column S 0.5 (mM) = 54; column kcat/S0.5 (s -1 mM -1) = 21; column K i (mM) = 5.0; column n H = blank for this row.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1,100 under the column head k cat (s -1); the printed unit is already canonical, so kcat = 1100 s^(-1). Km: printed Table 1 cell 54 under the column head S 0.5 (mM), the paper's half-saturation constant, which the article itself writes as S0.5 (Km); the printed unit is already canonical, so Km = 54 mM. kcat/Km: printed Table 1 cell 21 under the column head kcat/S0.5 (s -1 mM -1); the printed unit is already the canonical per-second per-millimolar unit, so kcat/Km = 21 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Oxaloacetate block, ECLDH row: k cat (s -1) cell = 1,100; S 0.5 (mM) cell = 54; kcat/S0.5 (s -1 mM -1) cell = 21.

row_label: Table 1, Oxaloacetate block, ECLDH row


organism: Furfurilactobacillus rossiae


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

sequence_source: multiple

proof_lines:
pH 7.0, 30°C, recombinant enzyme
Raw SKiD Env: Temp=30°C, pH=7

source_databases_merged: brenda skid


proof_lines: pH 8.0, 30°C, recombinant enzyme, with Mg2+


assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

proof_lines: pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate


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


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


proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=30°C, pH=7


organism: Enterococcus faecium

substrate_name: pyruvate (in the presence of NADPH at pH 5.6)

source_db: uniprot

assay_conditions_summary: pH 5.6; cofactor NADPH

proof_lines: kcat is 40 sec(-1) with pyruvate as substrate (in the presence of NADPH at pH 5.6) (PubMed:1931965). kcat is 10.7 sec(-1) with pyruvate as substrate (in the presence of NADPH at pH 5.6) (PubMed:9605319). kcat is 35 sec(-1) with alpha-ketobu

source: uniprot


substrate_name: alpha-ketobutyrate (in the presence of NADPH at pH 5.6)


substrate_name: alpha-ketovalerate (in the presence of NADPH at pH 5.6)


substrate_name: alpha-ketocaproate (in the presence of NADPH at pH 5.6)


substrate_name: alpha-ketoisocaproate (in the presence of NADPH at pH 5.6)


substrate_name: NADPH (at pH 5.6)

substrate: NADPH (at pH 5.6)


substrate_name: NADH (at pH 5.6)

assay_conditions_summary: pH 5.6; cofactor NADH

substrate: NADH (at pH 5.6)


organism: Pseudomonas fragi

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


sequence_variant_note: Resolved canonical sequence from genbank:AB183516.1 protein_id=BAD86668.1 (uniprotkb:Q5KST5) and applied mutation signature Q196E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from genbank:AB183516.1 protein_id=BAD86668.1 (uniprotkb:Q5KST5) and applied mutation signature L215V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from genbank:AB183516.1 protein_id=BAD86668.1 (uniprotkb:Q5KST5) and applied mutation signature W257F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from genbank:AB183516.1 protein_id=BAD86668.1 (uniprotkb:Q5KST5) and applied mutation signature Q196A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from genbank:AB183516.1 protein_id=BAD86668.1 (uniprotkb:Q5KST5) and applied mutation signature K152R 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 genbank:AB183516.1 protein_id=BAD86668.1 (uniprotkb:Q5KST5) and applied mutation signature T190S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from genbank:AB183516.1 protein_id=BAD86668.1 (uniprotkb:Q5KST5) and applied mutation signature Q94A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from genbank:AB183516.1 protein_id=BAD86668.1 (uniprotkb:Q5KST5) and applied mutation signature W187Y to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from genbank:AB183516.1 protein_id=BAD86668.1 (uniprotkb:Q5KST5) and applied mutation signature W187F to reconstruct the assayed variant sequence.


organism: Lactiplantibacillus pentosus

substrate_name: oxaloacetate

sequence_variant_note: Resolved canonical sequence from uniprotkb:P26298 and applied mutation signature F299S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P26298 and applied mutation signature F299G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P26298 and applied mutation signature Y52L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P26298 and applied mutation signature Y52R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P26298 and applied mutation signature Y52A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P26298 and applied mutation signature Y52V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P26298 and applied mutation signature Y52R/F299G to reconstruct the assayed variant sequence.


substrate_name: pyruvate


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_exact_accession:P26298 and applied mutation signature Y52V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 5.5; cofactor NADH

column_label: Table 2 row 2-Ketocaproate under Y52V reports Km 0.3, kcat 51, and kcat/Km 170.

normalized_value_unit_evidence: Km normalized_value=0.3 normalized_unit=mM; kcat normalized_value=51.0 normalized_unit=s^-1; kcat/Km normalized_value=170.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.3 raw_unit=mM; kcat raw_value=51 raw_unit=s^-1; kcat/Km raw_value=170 raw_unit=s^-1 mM^-1

row_label: Y52V / 2-ketocaproate

table_label: OUP full text Table 2


substrate_name: phenylpyruvate


assay_conditions_summary: pH 5.5; 303.15 K; buffer 100 mM sodium MES [2-(N-morpholino)ethane sulfonic acid]; cofactor NADH

column_label: Table 2, enzyme column group Wild-type, substrate row 2-Ketoglutarate; column Km (mM) = 15.5; column kcat (s-1) = 0.51; column kcat/Km (s-1 mM-1) = 0.03; column kH/kD = 2.6

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.51 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 0.51 s^(-1). Km: printed Table 2 cell 15.5 mM; the Michaelis-constant column of this paper is already in millimolar, so no unit conversion applies and the paper value is 15.5 mM. kcat/Km: printed Table 2 cell 0.03 s-1 mM-1; the efficiency column of this paper is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.03 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme column group Wild-type, substrate row 2-Ketoglutarate: Km = 15.5 mM; kcat = 0.51 s-1; printed kcat/Km = 0.03 s-1 mM-1; printed kH/kD = 2.6.

table_label: Table 2: Kinetic parameters for various substrates for Y52L, Y52V and Y52A L. pentosus D-LDHs (J. Biochem. 138, 741-749, 2005)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P26298 and applied mutation signature Y52A to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme column group Y52A, substrate row 2-Ketocaproate; column Km (mM) = 0.7; column kcat (s-1) = 102; column kcat/Km (s-1 mM-1) = 146; column kH/kD = 2.7

normalized_value_unit_evidence: kcat: printed Table 2 cell 102 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 102.0 s^(-1). Km: printed Table 2 cell 0.7 mM; the Michaelis-constant column of this paper is already in millimolar, so no unit conversion applies and the paper value is 0.7 mM. kcat/Km: printed Table 2 cell 146 s-1 mM-1; the efficiency column of this paper is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 146.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme column group Y52A, substrate row 2-Ketocaproate: Km = 0.7 mM; kcat = 102 s-1; printed kcat/Km = 146 s-1 mM-1; printed kH/kD = 2.7.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P26298 and applied mutation signature Y52T/F299S to reconstruct the assayed variant sequence.


column_label: Table 2, enzyme column group Wild-type, substrate row 2-Ketovalerate; column Km (mM) = 17; column kcat (s-1) = 5.7; column kcat/Km (s-1 mM-1) = 0.34; column kH/kD = 1.9

normalized_value_unit_evidence: kcat: printed Table 2 cell 5.7 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 5.7 s^(-1). Km: printed Table 2 cell 17 mM; the Michaelis-constant column of this paper is already in millimolar, so no unit conversion applies and the paper value is 17.0 mM. kcat/Km: printed Table 2 cell 0.34 s-1 mM-1; the efficiency column of this paper is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.34 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme column group Wild-type, substrate row 2-Ketovalerate: Km = 17 mM; kcat = 5.7 s-1; printed kcat/Km = 0.34 s-1 mM-1; printed kH/kD = 1.9.


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q5KST5 and applied mutation signature L215V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q5KST5 and applied mutation signature T190S to reconstruct the assayed variant sequence.


substrate_name: NADH

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

assay_conditions_summary: cofactor NADH

substrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q5KST5 and applied mutation signature T190A to reconstruct the assayed variant sequence.


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprotkb:Q5KST5 and applied mutation signature K152R to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NAD+

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q5KST5 and applied mutation signature Q196A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q5KST5 and applied mutation signature Q196E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q5KST5 and applied mutation signature Q94A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q5KST5 and applied mutation signature Q196N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q5KST5 and applied mutation signature W187Y to reconstruct the assayed variant sequence.


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


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


substrate: pyruvate


substrate: phenylpyruvate


substrate_name: Hydroxypyruvate


substrate: oxaloacetate


sequence_variant_note: Resolved canonical sequence from uniprot:P26298;mutation:F299S and applied mutation signature F299S with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P26298;mutation:Y52V and applied mutation signature Y52V with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P26298;mutation:Y52A and applied mutation signature Y52A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P26298;mutation:Y52L and applied mutation signature Y52L with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


organism: Haloferax volcanii

assay_conditions_summary: pH 7.3; 310.15 K; cofactor NADPH

proof_lines: pH 7.3, 37°C, cosubstrate: (S)-3-hydroxy-3-methylglutaryl-CoA, first step of the reaction, mutant enzyme H398Q


assay_conditions_summary: pH 7.3; 310.15 K; cofactor CoA

proof_lines: pH 7.3, 37°C, first step of the reaction, mutant enzyme H398Q


proof_lines: pH 7.3, 37°C, cosubstrate: mevaldehyde, second step of the reaction, mutant enzyme 404D/H398Q with Asp is added at position 404


proof_lines: pH 7.3, 37°C, cosubstrate: mevaldehyde, second step of the reaction, mutant enzyme H398Q


proof_lines: pH 7.3, 37°C, cosubstrate: mevaldehyde, second step of the reaction, mutant enzyme 404N with Asp is added at position 404


substrate_name: (R)-mevaldehyde

proof_lines: pH 7.3, 37°C, second step of the reaction, mutant enzyme 404N with Asp is added at position 404

substrate: (R)-mevaldehyde


proof_lines: pH 7.3, 37°C, second step of the reaction, wild-type enzyme


proof_lines: pH 7.3, 37°C, first step of the reaction, wild-type enzyme


proof_lines: pH 7.3, 37°C, cosubstrate: (S)-3-hydroxy-3-methylglutaryl-CoA, first step of the reaction, wild-type enzyme

proof_lines: pH 7.3, 37°C, cosubstrate: mevaldehyde, second step of the reaction, wild-type enzyme


proof_lines: pH 7.3, 37°C, cosubstrate: (S)-3-hydroxy-3-methylglutaryl-CoA, first step of the reaction, mutant enzyme 404D with Asp is added at position 404


proof_lines: pH 7.3, 37°C, cosubstrate: (S)-3-hydroxy-3-methylglutaryl-CoA, first step of the reaction, mutant enzyme 404D/H398Q with Asp is added at position 404


proof_lines: pH 7.3, 37°C, cosubstrate: (S)-3-hydroxy-3-methylglutaryl-CoA, first step of the reaction, mutant enzyme 404N with Asp is added at position 404


proof_lines: pH 7.3, 37°C, first step of the reaction, mutant enzyme 404N with Asp is added at position 404


proof_lines: pH 7.3, 37°C, first step of the reaction, mutant enzyme 404D with Asp is added at position 404


proof_lines: pH 7.3, 37°C, first step of the reaction, mutant enzyme 404D/H398Q with Asp is added at position 404


proof_lines: pH 7.3, 37°C, second step of the reaction, mutant enzyme 404D/H398Q with Asp is added at position 404


proof_lines: pH 7.3, 37°C, second step of the reaction, mutant enzyme H398Q


organism: Saccharolobus solfataricus

substrate_name: CoASH

substrate: CoASH


substrate_name: NADP+

assay_conditions_summary: pH 9; 323.15 K; cofactor NADP+


substrate_name: (R)-mevalonate

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

proof_lines:
pH 9.0, 50°C, wild-type
wild type enzyme, at pH 9.0 and 50°C

substrate: (R)-mevalonate


proof_lines: mutant enzyme L403R/G404R/A406S, at pH 9.0 and 50°C


substrate_name: mevaldehyde

substrate: mevaldehyde


assay_conditions_summary: pH 5.5; 323.15 K; cofactor CoA

proof_lines:
wild type
pH 5.5, 50°C, wild-type


substrate_name: NADPH

assay_conditions_summary: pH 5.5; 323.15 K; cofactor NADPH


assay_conditions_summary: cofactor CoA


substrate_name: HMG-CoA

sequence_variant_note: Resolved canonical sequence from uniprotkb:O08424 and applied mutation signature L403R/G404R/A406S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 5.5; cofactor CoA

substrate: HMG-CoA


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

assay_conditions_summary: cofactor NADPH


organism: Sporolactobacillus laevolacticus


organism: Pediococcus acidilactici


organism: Enterococcus mundtii

proof_lines: pH 7.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate

proof_lines: pH 5.5, temperature not specified in the publication, wild-type and mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate

proof_lines: pH 5.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate


proof_lines: pH 7.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate

proof_lines: pH 5.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate


proof_lines: pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate


assay_conditions_summary: pH 7.5; cofactor NADH


proof_lines: pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate


proof_lines: pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, without fructose-1,6-bisphosphate


km_display: Not reported

proof_lines: pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, without fructose-1,6-bisphosphate


organism: Pseudomonas aeruginosa

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

assay_conditions_summary: pH 7


assay_conditions_summary: pH 8

proof_lines: pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate

proof_lines: pH 8.0, 30°C, recombinant enzyme, with Mg2+


assay_conditions_summary: pH 8; cofactor NADH

proof_lines: pH 8.0, 30°C, recombinant enzyme, with or without fructose 1,6-bisphosphate and Mg2+


substrate: Hydroxypyruvate


substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


enzyme_display_name: glycerate dehydrogenase

assay_conditions_summary: pH 6.2; 298.15 K; cofactor NADH

enzyme: glycerate dehydrogenase


assay_conditions_summary: pH 6.2; 298.15 K; cofactor NADPH


proof_lines: mutant T335D, cosubstrate NADH, pH 6.2, 25°C


proof_lines: wild-type, cosubstrate NADH, pH 6.2, 25°C

proof_lines: wild-type, cosubstrate NADPH, pH 6.2, 25°C


proof_lines: mutant T335A, cosubstrate NADH, pH 6.2, 25°C


proof_lines: mutant T335D, cosubstrate NADPH, pH 6.2, 25°C


proof_lines: mutant T335A, cosubstrate NADPH, pH 6.2, 25°C


organism: Lactobacillus helveticus

proof_lines: mutant V152R/N213E, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant V152R/I177K/N213I, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant V152R/I177K, pH not specified in the publication, temperature not specified in the publication


substrate_name: nicotinamide cytosine dinucleotide

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

substrate: nicotinamide cytosine dinucleotide


proof_lines: mutant V152R, pH not specified in the publication, temperature not specified in the publication


organism: Pseudomonas putida


assay_conditions_summary: pH 8; 296.15 K; cofactor NAD+


organism: Rattus norvegicus


proof_lines:
wild type, NAD as cofactor
wild type, NADP as cofactor


assay_conditions_summary: cofactor NADP+

substrate: NADP+


proof_lines: mutant enzyme D33R, pH and temperature not specified in the publication


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


assay_conditions_summary: cofactor NAD+


proof_lines: pH 8.0, 30°C, recombinant enzyme, with fructose 1,6-bisphosphate


assay_conditions_summary: pH 7; 303.15 K; cofactor NADH

proof_lines: pH 8.0, 30°C, recombinant enzyme, with Mg2+


organism: Cryptosporidium parvum

substrate_name: (S)-lactate

substrate: (S)-lactate


assay_conditions_summary: pH 5.5; 298.15 K; cofactor NAD+


substrate_name: APAD+

assay_conditions_summary: pH 5.5; 298.15 K; cofactor NADH

proof_lines: pH 5.5, 25°C, recombinant enzyme, with NADH and pyruvate

substrate: APAD+


proof_lines:
pH 5.5, 25°C, recombinant enzyme
pH 8.0, 25°C

substrate: NADH


substrate_name: pyruvate


substrate_name: APADH

substrate: APADH


organism: Anas platyrhynchos

substrate_name: epsilon-NAD+

substrate: epsilon-NAD+


substrate_name: nicotinamide hypoxanthine dinucleotide

substrate: nicotinamide hypoxanthine dinucleotide


substrate_name: 3-acetylpyridine adenine dinucleotide

substrate: 3-acetylpyridine adenine dinucleotide


substrate_name: NAD+

substrate: NAD+


substrate: pyruvate


substrate_name: Bromopyruvate

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

substrate: Bromopyruvate


organism: Plasmodium vivax


assay_conditions_summary: pH 9.2; 298.15 K; cofactor NAD+


substrate_name: NADH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


organism: Plasmodium ovale


organism: Plasmodium malariae


assay_conditions_summary: pH 9.2; cofactor NAD+


substrate_name: gossypol lactone

substrate: gossypol lactone


organism: Leuconostoc mesenteroides subsp. mesenteroides

assay_conditions_summary: pH 9; 303.15 K; cofactor NAD+

proof_lines:
pH 9, 30°C
pH 11.0, 20°C, recombinant enzyme


substrate_name: (R)-lactate

proof_lines:
pH 8, , 30°C
pH 11.0, 20°C, recombinant enzyme

substrate: (R)-lactate


substrate_name: oxaloacetate

substrate: oxaloacetate


assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

proof_lines:
pH 8, 30°C
pH 8.0, 30°C, recombinant enzyme


organism: Plasmodium falciparum


substrate_name: phenylpyruvate

substrate: phenylpyruvate


assay_conditions_summary: cofactor NADH


substrate_name: L-lactate

substrate: L-lactate


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+


organism: Geobacillus stearothermophilus

proof_lines: pH 6.0, 25°C, recombinant wild-type enzyme in presence of fructose 1,6-bisphosphate

proof_lines: pH 6.0, 25°C, recombinant wild-type enzyme in absence of fructose 1,6-bisphosphate


proof_lines: pH 6.0, 25°C, recombinant mutant D38R in presence of fructose 1,6-bisphosphate


proof_lines: pH 6.0, 25°C, recombinant mutant D38R in absence of fructose 1,6-bisphosphate


substrate_name: Unknown

substrate: Unknown


organism: Lacticaseibacillus casei

proof_lines: wild-type, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C


proof_lines: mutant I229A, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C


proof_lines: mutant Q88R, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C


organism: Haliotis cracherodii


substrate_name: alpha-Ketobutyrate

substrate: alpha-Ketobutyrate


organism: Methylorubrum extorquens


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: Hydroxypyruvate

substrate: Hydroxypyruvate


substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: glycerate

substrate: glycerate


organism: Mycobacterium tuberculosis


substrate_name: L-serine

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

substrate: L-serine


substrate_name: NADP+

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADP+

proof_lines: with (S)-3-hydroxyisobutyrate as cosubstrate, pH 8.5 and 30°C

substrate: NADP+


assay_conditions_summary: pH 8.5; 303.15 K; cofactor NAD+


substrate_name: 3-hydroxypropanoic acid

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

substrate: 3-hydroxypropanoic acid


organism: Trypanosoma cruzi

sequence_source: uniprotkb:O15888 (GN=Hmgr; EC=1.1.1.34; organism=Trypanosoma cruzi; EC+organism lookup)

assay_conditions_summary: pH 6.8; cofactor CoA


substrate_name: CoA

assay_conditions_summary: pH 8.3; cofactor CoA

substrate: CoA


substrate_name: (R)-mevalonate

substrate: (R)-mevalonate


substrate_name: fluvastatin

proof_lines: pH 6.8, 25°C, versus (S)-3-hydroxy-3-methylglutaryl-CoA

substrate: fluvastatin


organism: Haloferax volcanii

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

assay_conditions_summary: pH 8; cofactor CoA

column_label: Paper prose evidence: abstract kinetic prose segment; row_label=oxidative acylation of mevaldehyde / CoA; column_label=Km for CoA; raw_value=300 raw_unit=microM; normalized_value=0.3 normalized_unit=mM; assay_condition=oxidative acylation of mevaldehyde at pH 8.0; captured paper segment: Kms 350 microM (NADP+), 300 microM (CoA), 470 microM [(R,S)-mevaldehyde].

raw_value_unit_evidence: Km raw_value=300 microM raw_unit=microM raw_cell=Kms 350 microM (NADP+), 300 microM (CoA), 470 microM [(R,S)-mevaldehyde]

table_label: Abstract kinetic prose segment


assay_conditions_summary: pH 6; cofactor NADPH

column_label: PMCID PMC177616 / PMID 8550415 abstract, prose clause for reduction of mevaldehyde, metric Km, substrate NADPH, raw value 32 microM.

normalized_value_unit_evidence: 32 microM NADPH = 0.032 mM, matching the exported Km 0.032 mM.

raw_value_unit_evidence: PMC177616 abstract reports reduction of mevaldehyde with Kms 32 microM (NADPH) and 550 microM [(R,S)-mevaldehyde].

row_label: reduction of mevaldehyde

table_label: PMC article abstract/prose


assay_conditions_summary: pH 8; cofactor NADP+

column_label: Paper prose evidence: abstract kinetic prose segment; row_label=oxidative acylation of mevaldehyde / NADP+; column_label=Km for NADP+; raw_value=350 raw_unit=microM; normalized_value=0.35 normalized_unit=mM; assay_condition=oxidative acylation of mevaldehyde at pH 8.0; captured paper segment: Kms 350 microM (NADP+), 300 microM (CoA), 470 microM [(R,S)-mevaldehyde].

raw_value_unit_evidence: Km raw_value=350 microM raw_unit=microM raw_cell=Kms 350 microM (NADP+), 300 microM (CoA), 470 microM [(R,S)-mevaldehyde]


assay_conditions_summary: pH 7.3; cofactor CoA

column_label: PMID 8550415 / DOI 10.1128/jb.178.1.19-23.1996, Results paragraph, expressed enzyme overall reaction: (S)-HMG-CoA Km = 60 uM.

raw_value_unit_evidence: Results paragraph reports Km for (S)-HMG-CoA = 60 uM for the expressed enzyme overall reaction.

row_label: (S)-HMG-CoA

table_label: Results prose: Reductive deacylation of HMG-CoA


substrate_name: (R,S)-mevaldehyde

column_label: PMCID PMC177616 / PMID 8550415 abstract, prose clause for oxidative acylation of mevaldehyde, metric Km, substrate (R,S)-mevaldehyde, raw value 470 microM.

normalized_value_unit_evidence: 470 microM (R,S)-mevaldehyde = 0.470 mM, matching the exported Km 0.47 mM.

raw_value_unit_evidence: PMC177616 abstract reports oxidative acylation of mevaldehyde with Kms 350 microM (NADP+), 300 microM (CoA), 470 microM [(R,S)-mevaldehyde].

row_label: oxidative acylation of mevaldehyde

substrate: (R,S)-mevaldehyde


organism: Limosilactobacillus fermentum


assay_conditions_summary: pH 6; 298.15 K; cofactor NADPH


substrate_name: pyruvate

substrate: pyruvate


substrate_name: NADH

assay_conditions_summary: pH 6; 298.15 K; cofactor NADH

substrate: NADH


organism: Gallus gallus

substrate_name: nicotinamide hypoxanthine dinucleotide

substrate: nicotinamide hypoxanthine dinucleotide


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

proof_lines:
enzyme from muscle
enzyme from heart

substrate: NAD+


substrate_name: 3-acetylpyridine adenine dinucleotide

substrate: 3-acetylpyridine adenine dinucleotide


substrate_name: Fluoropyruvate

substrate: Fluoropyruvate


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines: 25°C, pH 8, mutant enzyme F16Q/C81S/N85R, activated by fructose 1,6-diphosphate


proof_lines: 25°C, pH 8, mutant enzyme F16Q/I37K/D38SC81S/N85R, activated by fructose 1,6-diphosphate


proof_lines: 25°C, pH 8, wild-type enzyme, activated by fructose 1,6-diphosphate


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


organism: Ipomoea batatas

assay_conditions_summary: pH 7.3; cofactor NADH


proof_lines:
pH 7.3, isoenzyme I
pH 7.3, isoenzyme II
pH 6.5, isoenzyme II


assay_conditions_summary: pH 8.2; cofactor NAD+


substrate_name: (S)-lactate

proof_lines:
pH 8.2, isoenzyme II
pH 8.8, isoenzyme I

substrate: (S)-lactate


organism: Agama stellio stellio


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


organism: Streptococcus uberis

assay_conditions_summary: cofactor NADH


organism: Taenia asiatica


substrate_name: Lactate

substrate: Lactate


organism: Priestia megaterium

proof_lines: measured without D-fructose 1,6-bisphosphate, wild-type enzyme

proof_lines: measured with D-fructose 1,6-bisphosphate, wild-type enzyme


proof_lines: measured without D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)

proof_lines: measured with D-fructose 1,6-bisphosphate


proof_lines: measured with D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)


organism: Molinema dessetae


organism: Solanum tuberosum


substrate_name: Hydroxypyruvate

substrate: Hydroxypyruvate


substrate_name: glyoxylate

substrate: glyoxylate