sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5JGC7 and applied mutation signature R221G/K228R/I310V to reconstruct the assayed variant sequence.

column_label: Table 2 (Specific activities and kinetic parameters of the wild type and mutant enzymes), body row 'R221G/K228R/I310V', cofactor column NAD+; column 'Km (mM)' = 1.54; column 'kcat (s-1)' = 21.3; column 'kcat/Km (mM-1 s-1)' = 13.8. The value printed after the plus/minus sign beside the Km and kcat cells of this line is the printed uncertainty and is not an exported metric; the specific-activity column of the same line prints 22.9 umol min-1 mg-1 for this cofactor.

normalized_value_unit_evidence: kcat: printed Table 2 cell 21.3 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 21.3 s^(-1). Km: printed Table 2 cell 1.54 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 1.54 mM. kcat/Km: printed Table 2 cell 13.8 in a column headed kcat/Km (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 13.8 s^(-1)*mM^(-1). The exported values are kcat 21.3 s^(-1), Km 1.54 mM and kcat_over_km 13.831168831168831 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'R221G/K228R/I310V', cofactor column NAD+: Km = 1.54 mM; kcat = 21.3 s-1; printed kcat/Km = 13.8 in a column headed kcat/Km (mM-1 s-1).

row_label: Table 2, row R221G/K228R/I310V, cofactor NAD+


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

organism: Thermococcus kodakarensis

substrate_name: NAD+

source_db: oed

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

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.

assay_conditions_summary: pH 8; 343.15 K; cofactor NAD+

column_label: Table 2 (Specific activities and kinetic parameters of the wild type and mutant enzymes), body row 'Wild type', cofactor column NAD+; column 'Km (mM)' = 2.06; column 'kcat (s-1)' = 4.69; column 'kcat/Km (mM-1 s-1)' = 2.27. The value printed after the plus/minus sign beside the Km and kcat cells of this line is the printed uncertainty and is not an exported metric; the specific-activity column of the same line prints 5.77 umol min-1 mg-1 for this cofactor.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4.69 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 4.69 s^(-1). Km: printed Table 2 cell 2.06 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 2.06 mM. kcat/Km: printed Table 2 cell 2.27 in a column headed kcat/Km (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 2.27 s^(-1)*mM^(-1). The exported values are kcat 4.69 s^(-1), Km 2.06 mM and kcat_over_km 2.2766990291262137 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'Wild type', cofactor column NAD+: Km = 2.06 mM; kcat = 4.69 s-1; printed kcat/Km = 2.27 in a column headed kcat/Km (mM-1 s-1).

row_label: Table 2, row Wild type, cofactor NAD+

table_label: Table 2: Specific activities and kinetic parameters of the wild type and mutant enzymes (J. Biosci. Bioeng. 2014, 117(2):147-152). Printed column heads: Enzyme; Specific activity (umol min-1 mg-1); Km (mM); kcat (s-1); kcat/Km (mM-1 s-1); each metric head prints one value column for NAD+ and one for NADP+.

data_origin: experimental

substrate: NAD+

status: corrected

source: oed


substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5JGC7 and applied mutation signature I310V to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 8; 343.15 K; cofactor NADP+

column_label: Table 2 (Specific activities and kinetic parameters of the wild type and mutant enzymes), body row 'I310V', cofactor column NADP+; column 'Km (mM)' = 0.021; column 'kcat (s-1)' = 43.4; column 'kcat/Km (mM-1 s-1)' = 2070. The value printed after the plus/minus sign beside the Km and kcat cells of this line is the printed uncertainty and is not an exported metric; the specific-activity column of the same line prints 5.23 umol min-1 mg-1 for this cofactor.

normalized_value_unit_evidence: kcat: printed Table 2 cell 43.4 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 43.4 s^(-1). Km: printed Table 2 cell 0.021 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.021 mM. kcat/Km: printed Table 2 cell 2070 in a column headed kcat/Km (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 2070.0 s^(-1)*mM^(-1). The exported values are kcat 43.4 s^(-1), Km 0.021 mM and kcat_over_km 2066.6666666666665 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'I310V', cofactor column NADP+: Km = 0.021 mM; kcat = 43.4 s-1; printed kcat/Km = 2070 in a column headed kcat/Km (mM-1 s-1).

row_label: Table 2, row I310V, cofactor NADP+

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

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5JGC7 and applied mutation signature K228R to reconstruct the assayed variant sequence.

column_label: Table 2 (Specific activities and kinetic parameters of the wild type and mutant enzymes), body row 'K228R', cofactor column NADP+; column 'Km (mM)' = 0.019; column 'kcat (s-1)' = 2.97; column 'kcat/Km (mM-1 s-1)' = 156. The value printed after the plus/minus sign beside the Km and kcat cells of this line is the printed uncertainty and is not an exported metric; the specific-activity column of the same line prints 3.57 umol min-1 mg-1 for this cofactor.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.97 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 2.97 s^(-1). Km: printed Table 2 cell 0.019 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.019 mM. kcat/Km: printed Table 2 cell 156 in a column headed kcat/Km (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 156.0 s^(-1)*mM^(-1). The exported values are kcat 2.97 s^(-1), Km 0.019 mM and kcat_over_km 156.31578947368422 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'K228R', cofactor column NADP+: Km = 0.019 mM; kcat = 2.97 s-1; printed kcat/Km = 156 in a column headed kcat/Km (mM-1 s-1).

row_label: Table 2, row K228R, cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5JGC7 and applied mutation signature R221G to reconstruct the assayed variant sequence.

column_label: Table 2 (Specific activities and kinetic parameters of the wild type and mutant enzymes), body row 'R221G', cofactor column NADP+; column 'Km (mM)' = 0.025; column 'kcat (s-1)' = 42.6; column 'kcat/Km (mM-1 s-1)' = 1700. The value printed after the plus/minus sign beside the Km and kcat cells of this line is the printed uncertainty and is not an exported metric; the specific-activity column of the same line prints 52.1 umol min-1 mg-1 for this cofactor.

normalized_value_unit_evidence: kcat: printed Table 2 cell 42.6 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 42.6 s^(-1). Km: printed Table 2 cell 0.025 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.025 mM. kcat/Km: printed Table 2 cell 1700 in a column headed kcat/Km (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 1700.0 s^(-1)*mM^(-1). The exported values are kcat 42.6 s^(-1), Km 0.025 mM and kcat_over_km 1704.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'R221G', cofactor column NADP+: Km = 0.025 mM; kcat = 42.6 s-1; printed kcat/Km = 1700 in a column headed kcat/Km (mM-1 s-1).

row_label: Table 2, row R221G, cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5JGC7 and applied mutation signature R221G/K228R to reconstruct the assayed variant sequence.

column_label: Table 2 (Specific activities and kinetic parameters of the wild type and mutant enzymes), body row 'R221G/K228R', cofactor column NADP+; column 'Km (mM)' = 0.244; column 'kcat (s-1)' = 6.48; column 'kcat/Km (mM-1 s-1)' = 27.5. The value printed after the plus/minus sign beside the Km and kcat cells of this line is the printed uncertainty and is not an exported metric; the specific-activity column of the same line prints 4.89 umol min-1 mg-1 for this cofactor.

normalized_value_unit_evidence: kcat: printed Table 2 cell 6.48 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 6.48 s^(-1). Km: printed Table 2 cell 0.244 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.244 mM. kcat/Km: printed Table 2 cell 27.5 in a column headed kcat/Km (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 27.5 s^(-1)*mM^(-1). The exported values are kcat 6.48 s^(-1), Km 0.244 mM and kcat_over_km 26.55737704918033 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'R221G/K228R', cofactor column NADP+: Km = 0.244 mM; kcat = 6.48 s-1; printed kcat/Km = 27.5 in a column headed kcat/Km (mM-1 s-1).

row_label: Table 2, row R221G/K228R, cofactor NADP+


enzyme_display_name: aldose reductase

organism: Rattus norvegicus

source_db: brenda

verification_status: unverified

kcat_over_km_display: Not reported

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

smiles: CCCCCCCC=CC=O

enzyme: aldose reductase

status: unverified

source: brenda


smiles: CCCCCCC=CC=O


smiles: CCCCCC(C=CC=O)O


smiles: CCCCCC=CC=CC=O


smiles: CCCCC=CC=CC=O


substrate_name: glycoaldehyde

smiles: C(C=O)O

substrate: glycoaldehyde


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


substrate_name: Glyoxal

smiles: C(=O)C=O

substrate: Glyoxal


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


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


enzyme_display_name: malate dehydrogenase (decarboxylating)

organism: Solanum tuberosum

substrate_name: NAD+; L-Malate

kcat_display: Not reported

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

ki_unit: mM

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

assay_conditions_summary: cofactor NADP+

enzyme: malate dehydrogenase (decarboxylating)

substrate: NAD+; L-Malate


assay_conditions_summary: pH 7.4; buffer note ("in 0


smiles: CCCCCCCC=O


smiles: CCCCCC=O


km_display: Not reported


smiles: CCCCCCCCCCO


substrate_name: benzyl alcohol

substrate: benzyl alcohol


smiles: CCCCCCCCCO


smiles: CCCCCCO


smiles: CCC=O


smiles: CCCCO


smiles: CCCCCCCC=CC=O

assay_conditions_summary: pH 7.4; buffer unstructured


smiles: CCCCCCC=CC=O


smiles: CCCCCC(C=CC=O)O


smiles: CCCCCC=CC=CC=O


smiles: CCCCC=CC=CC=O


smiles: C(C=O)O


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


smiles: C(=O)C=O


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


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


smiles: CCCCCCCCC=O

assay_conditions_summary: pH 7.4; buffer note: 'in 0


substrate_name: DL-glyceraldehyde

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

assay_conditions_summary: pH 7.4; 298.15 K; buffer note: 'in 0

proof_lines:
in 0.1 M potassium phosphate, pH 7.4
pH 6.0, 25°C, healthy heart
pH 6.0, 25°C, ischemic heart

substrate: DL-glyceraldehyde


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


smiles: CCCC=O


smiles: CCCC=CC=O


smiles: CCCCCCCC=O

assay_conditions_summary: pH 7.4; buffer conditions and the numeric literature id


smiles: CCCCCC=O


smiles: CCCCCCCCCCO


smiles: CCCCCCCCCO


smiles: CCCCCCO


smiles: CCC=O


smiles: CCCCO


substrate_name: acrolein

smiles: C=CC=O

substrate: acrolein


substrate_name: D-lactoaldehyde

proof_lines:
in 0.1 M potassium phosphate, pH 7.4
pH 6.2, 30°C, isoform ALR2
pH 6.2, 37°C

substrate: D-lactoaldehyde


substrate_name: isatin

substrate: isatin


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


smiles: CCCCCCCCCC=O


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


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


smiles: CCCCCCCCC=O

assay_conditions_summary: pH 7.4; buffer pH 7


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

assay_conditions_summary: pH 6.2; buffer note: 'in 0


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


smiles: CCCC=O


smiles: CCCC=CC=O


smiles: CCCCCCCC=CC=O

assay_conditions_summary: pH 7.4; buffer context ("in 0


smiles: CCCCCCC=CC=O


smiles: CCCCCC(C=CC=O)O


smiles: CCCCCC=CC=CC=O


smiles: CCCCC=CC=CC=O


smiles: C(C=O)O


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


smiles: C(=O)C=O


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


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


enzyme_display_name: alcohol dehydrogenase

organism: Saccharolobus solfataricus

substrate_name: trans-cinnamaldehyde

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

assay_conditions_summary: pH 10.5; buffer 0.1 M glycine-NaOH

enzyme: alcohol dehydrogenase

substrate: trans-cinnamaldehyde


substrate_name: Butyraldehyde

substrate: Butyraldehyde


substrate_name: 4-methoxybenzyl alcohol

substrate: 4-methoxybenzyl alcohol


substrate_name: NADH

assay_conditions_summary: pH 10.5; buffer 0.1 M glycine-NaOH; cofactor NADH

substrate: NADH


smiles: CCCCCCO


smiles: CCCCCCCO


substrate_name: NAD+

assay_conditions_summary: pH 10.5; buffer 0.1 M glycine-NaOH; cofactor NAD+

substrate: NAD+


smiles: CCCCCO


substrate_name: Isobutyraldehyde

smiles: CC(C)C=O

substrate: Isobutyraldehyde


smiles: CCC(C)O


enzyme_display_name: L-lactate dehydrogenase

organism: Lactiplantibacillus plantarum

assay_conditions_summary: cofactor NADH

enzyme: L-lactate dehydrogenase


substrate_name: (S)-lactate

substrate: (S)-lactate


organism: Enterococcus faecalis

assay_conditions_summary: pH 6.5; 310.15 K; cofactor CoA


substrate_name: NADPH

assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADPH

proof_lines: pH 6.5, 37°C, (S)-3-hydroxy-3-methylglutaryl-CoA reduction

substrate: NADPH


substrate_name: CoA

proof_lines:
pH 6.5, 37°C, mevaldehyde oxidation
pH 6.5, 37°C, mevalonate oxidation

substrate: CoA


substrate_name: NADP+

assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADP+

proof_lines:
pH 6.5, 37°C, mevalonate oxidation
pH 6.5, 37°C, mevaldehyde oxidation

substrate: NADP+


substrate_name: mevaldehyde

proof_lines:
pH 6.5, 37°C, oxidation
pH 6.5, 37°C, reduction

substrate: mevaldehyde


substrate_name: (R)-mevalonate

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

substrate: (R)-mevalonate


organism: Rhizopus oryzae ATCC 9363

substrate_name: pyruvate

proof_lines:
LDHB, in the presence of 0.125 mM NADH
LDHB, in the presence of 0.15 mM NADH
LDHB, in the presence of 0.2 mM NADH

substrate: pyruvate


substrate_name: Lactate

assay_conditions_summary: cofactor NAD+

substrate: Lactate


substrate_name: Unknown

proof_lines: LDHA LDHB

substrate: Unknown


enzyme_display_name: 3-hydroxyisobutyrate dehydrogenase

organism: Pseudomonas denitrificans (nom. rej.)

substrate_name: L-serine

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

proof_lines:
at 37°C and pH 9.0
at 30°C and pH 9.0

enzyme: 3-hydroxyisobutyrate dehydrogenase

substrate: L-serine


enzyme_display_name: L-iditol 2-dehydrogenase

organism: Bos taurus

substrate_name: D-sorbitol (at pH 8.0)

source_db: uniprot

verification_status: verified

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

assay_conditions_summary: pH 8

column_label: Primary-paper Table II reports D-sorbitol KM 18 +/- 0.4 mM.

raw_value_unit_evidence: D-sorbitol KM 18 +/- 0.4 mM

row_label: D-sorbitol row

table_label: Table II: Kinetic Constants and Substrate Specificity of Bovine Lens SDH

enzyme: L-iditol 2-dehydrogenase

substrate: D-sorbitol (at pH 8.0)

status: verified

source: uniprot


substrate_name: xylitol (at pH 8.0)

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

column_label: Primary-paper Table II reports xylitol KM 3.2 +/- 0.2 mM.

raw_value_unit_evidence: Xylitol KM 3.2 +/- 0.2 mM

row_label: Xylitol row

substrate: xylitol (at pH 8.0)


substrate_name: L-threitol (at pH 8.0)

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

column_label: Primary-paper Table II reports L-threitol KM 268 +/- 14 mM.

raw_value_unit_evidence: L-threitol KM 268 +/- 14 mM

row_label: L-threitol row

substrate: L-threitol (at pH 8.0)


assay_conditions_summary: pH 8; cofactor NAD+

column_label: Primary-paper Table II reports NAD+ KM 0.089 +/- 0.002 mM.

row_label: NAD+ row


enzyme_display_name: 3-hydroxybutyrate dehydrogenase

organism: Alcaligenes faecalis

substrate_name: levulinic acid

kcat_over_km_origin: calculated

sequence_source: multiple

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

proof_lines: recombinant wild type enzyme with N-terminal His-tag, at pH 6.5 and 30°C

source_databases_merged: brenda oed

enzyme: 3-hydroxybutyrate dehydrogenase

substrate: levulinic acid


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

proof_lines: recombinant mutant enzyme W187F with N-terminal His-tag, at pH 6.5 and 30°C


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

proof_lines: recombinant mutant enzyme H144L with C-terminal His-tag, at pH 6.5 and 30°C


proof_lines: recombinant mutant enzyme H144L with N-terminal His-tag, 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: recombinant mutant enzyme H144L/W187F with C-terminal His-tag, at pH 6.5 and 30°C


proof_lines: recombinant mutant enzyme H144L/W187F with N-terminal His-tag, at pH 6.5 and 30°C


substrate_name: acetoacetate

proof_lines: recombinant enzyme with C-terminal His-tag, at pH 6.5 and 30°C

proof_lines: recombinant enzyme with N-terminal His-tag, at pH 6.5 and 30°C

substrate: acetoacetate


enzyme_display_name: L-xylulose reductase

organism: Trichoderma reesei

substrate_name: xylitol

assay_conditions_summary: pH 7; cofactor NADPH

source_databases_merged: brenda uniprot

enzyme: L-xylulose reductase

substrate: xylitol


substrate_name: D-sorbitol

substrate: D-sorbitol


substrate_name: D-ribulose

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

substrate: D-ribulose


substrate_name: sorbitol

proof_lines: kcat is 8 sec(-1) for sorbitol oxidation and 190 sec(-1) for D-fructose reduction.

substrate: sorbitol


substrate_name: NAD(+)

substrate: NAD(+)


substrate_name: D-fructose

substrate: D-fructose


organism: Homo sapiens

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


enzyme_display_name: mannitol-1-phosphate 5-dehydrogenase

organism: Acinetobacter baumannii

substrate_name: D-fructose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R620A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

enzyme: mannitol-1-phosphate 5-dehydrogenase

substrate: D-fructose 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D602A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R609A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R613A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y427C with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y469C with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M417A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W531A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A466C with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D16A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H434C/Y469C with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A466C/Y427C with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


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

organism: Beggiatoa leptomitoformis

substrate_name: NADH

assay_conditions_summary: 298.15 K; cofactor NADH

substrate: NADH


substrate_name: oxaloacetate

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

substrate: oxaloacetate


substrate_name: NAD+

assay_conditions_summary: 298.15 K; cofactor NAD+

substrate: NAD+


substrate_name: L-malate

substrate: L-malate


enzyme_display_name: NAD-dependent malic enzyme 1, mitochondrial

organism: Arabidopsis thaliana

substrate_name: L-malate (homodimer)

assay_conditions_summary: cofactor CoA

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

substrate: L-malate (homodimer)


enzyme_display_name: NAD-dependent malic enzyme 2, mitochondrial

substrate_name: NAD (homodimer)

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

substrate: NAD (homodimer)


enzyme: NAD-dependent malic enzyme 2, mitochondrial


organism: Caenorhabditis elegans

substrate_name: L-ribulose

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication

proof_lines: The KM value for isatin is approximate as substrate saturation was not reached.

substrate: L-ribulose


substrate_name: D-erythrose

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

substrate: D-erythrose


substrate_name: L-erythrulose

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

substrate: L-erythrulose


organism: Brochothrix thermosphacta

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


substrate_name: D-mannitol 1-phosphate

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

substrate: D-mannitol 1-phosphate


assay_conditions_summary: pH 7.1; cofactor NADH


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

organism: Sus scrofa

substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

proof_lines:
cytosolic enzyme
mitochondrial enzyme

substrate: NADP+


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


substrate_name: pyruvate

substrate: pyruvate


substrate_name: 1,4-dibromo-2,3-butanedione (at 25 degrees Celsius)

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


substrate_name: 2,3-heptanedione (at 25 degrees Celsius)

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


enzyme_display_name: galactitol 2-dehydrogenase

organism: Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841)

substrate_name: galactitol

enzyme: galactitol 2-dehydrogenase

substrate: galactitol


substrate_name: NAD(+)


organism: Ovis aries

substrate_name: D-sorbitol (at pH 7.4)

proof_lines: kcat is 19.6 sec(-1) for D-sorbitol oxidation (at pH 7.4). kcat is 18.2 sec(-1) for xylitol oxidation (at pH 7.4). kcat is 20.4 sec(-1) for L-iditol oxidation (at pH 7.4). kcat is 20 sec(-1) for ribitol oxidation (at pH 7.4). kcat is 18.2 s

substrate: D-sorbitol (at pH 7.4)


substrate_name: xylitol (at pH 7.4)

substrate: xylitol (at pH 7.4)


organism: Sphyraena idiastes

substrate_name: oxaloacetate

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

proof_lines: pH 7.5, 20°C, recombinant cytosolic isoenzyme cMDH-L

proof_lines: pH 7.5, 20°C, mitochondrial isoenzyme mMDH


substrate_name: NADH

assay_conditions_summary: pH 7.5; cofactor NADH

proof_lines: pH 7.5, 20°C, recombinant cytosolic isoenzyme cMDH-S


organism: Ascaris suum

proof_lines:
in the presence of NAD+, 20 mM Mn2+
in the absence of NAD+, 20 mM Mn2+


proof_lines:
in the absence of NAD+, 20 mM Mn2+
in the presence of NAD+, 20 mM Mn2+


enzyme_display_name: NAD-dependent malic enzyme

organism: Escherichia coli (strain K12)

substrate_name: L-malate

enzyme: NAD-dependent malic enzyme


enzyme_display_name: UniProt P16243

organism: Zea mays

substrate_name: (S)-malate

source_db: skid

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

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

source_databases_merged: skid uniprot

enzyme: UniProt P16243

substrate: (S)-malate

source: skid


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=-----, pH=7
Raw SKiD Env: Temp=30°C, pH=7


organism: Aspergillus niger

substrate_name: L-xylulose

substrate: L-xylulose


substrate_name: isatin (at 25 degrees Celsius)

substrate: isatin (at 25 degrees Celsius)


organism: Gluconobacter oxydans

substrate_name: D-sorbitol

source_license: CC BY-NC-ND 4.0

substrate: D-sorbitol


organism: Rattus norvegicus

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


substrate_name: D-fructose 6-phosphate

proof_lines:
pH 7.0, 37°C
Raw SKiD Env: Temp=37°C, pH=7

source_databases_merged: brenda skid

substrate: D-fructose 6-phosphate


organism: Agrobacterium fabrum (strain C58 / ATCC 33970)

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


organism: Thermus thermophilus

proof_lines: kcat is 676 sec(-1) for pyruvate as substrate.


organism: Thermotoga maritima

proof_lines:
octameric enzyme form
tetrameric enzyme form


organism: Haloarcula marismortui

assay_conditions_summary: pH 8; cofactor NADH

proof_lines: pH 8.0, 25°C, recombinant wild-type enzyme and mutant K205A

substrate: NADH


enzyme_display_name: D-lactate dehydrogenase

organism: Lactobacillus helveticus

substrate_name: NAD+

enzyme: D-lactate dehydrogenase

substrate: NAD+


assay_conditions_summary: pH 8; 333.15 K; cofactor NADH

column_label: PDF page 297, Table 1, Hm MalDH column, Enzymatic activity/Coenzyme row reports Km of NADH independent on salt concentration (24 microM).

row_label: Hm MalDH; Enzymatic activity; Coenzyme NADH

table_label: Table 1, Summing-up of the molecular properties from S. ruber and H. marismortui MalDHs


enzyme_display_name: Malate dehydrogenase

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

substrate_name: malate (at pH 10.5 in the presence of NAD)

assay_conditions_summary: pH 10.5; cofactor NADPH

proof_lines: kcat is 360 sec(-1) for NADH-dependent reduction of oxaloacetate. kcat is 150 sec(-1) for NADPH-dependent reduction of oxaloacetate. kcat is 140 sec(-1) for NAD(+)-dependent oxidation of malate.

enzyme: Malate dehydrogenase


assay_conditions_summary: pH 9; cofactor NAD+

proof_lines:
pH 9.0
native enzyme
pH 7.3


enzyme_display_name: malate dehydrogenase (decarboxylating)

organism: Homo sapiens

substrate_name: L-Malate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23368 and applied mutation signature D102A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NAD+

column_label: PMCID PMC1317662 Table 1; row D102A (+), fumarate Yes; columns Km,Malate (mM) and kcat (s^-1); kcat/Km is locked from the same row for L-Malate.

row_label: D102A (+), fumarate Yes

table_label: Table 1. Kinetic parameters for the WT and D102 mutant human m-NAD-MDHs

substrate: L-Malate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23368 and applied mutation signature D102E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: PMCID PMC1317662 Table 1; row D102E (+), fumarate Yes; columns Km,Malate (mM) and kcat (s^-1); kcat/Km is locked from the same row for L-Malate.

row_label: D102E (+), fumarate Yes


column_label: PMCID PMC1317662 Table 1; row WT (+), fumarate Yes; columns Km,Malate (mM) and kcat (s^-1); kcat/Km is locked from the same row for L-Malate.

row_label: WT (+), fumarate Yes


column_label: PMCID PMC1317662 Table 1; row D102A (+), fumarate Yes; columns Km,Mg (mM) and kcat (s^-1); kcat/Km is locked from the same row for Mg2+.


column_label: PMCID PMC1317662 Table 1; row D102E (+), fumarate Yes; columns Km,Mg (mM) and kcat (s^-1); kcat/Km is locked from the same row for Mg2+.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23368 and applied mutation signature D102K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: PMCID PMC1317662 Table 1; row D102K (+), fumarate Yes; columns Km,Mg (mM) and kcat (s^-1); kcat/Km is locked from the same row for Mg2+.

row_label: D102K (+), fumarate Yes


column_label: PMCID PMC1317662 Table 1; row WT (+), fumarate Yes; columns Km,Mg (mM) and kcat (s^-1); kcat/Km is locked from the same row for Mg2+.


column_label: PMCID PMC1317662 Table 1; row D102A (+), fumarate Yes; columns Km,NAD (mM) and kcat (s^-1); kcat/Km is locked from the same row for NAD+.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D102K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: PMCID PMC1317662 Table 1; row D102K (+), fumarate Yes; columns Km,NAD (mM) and kcat (s^-1); kcat/Km is locked from the same row for NAD+.


column_label: PMCID PMC1317662 Table 1; row WT (+), fumarate Yes; columns Km,NAD (mM) and kcat (s^-1); kcat/Km is locked from the same row for NAD+.


organism: Arabidopsis thaliana

substrate_name: Oxaloacetate

substrate: Oxaloacetate


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

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9LYG3 and applied mutation signature R115A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic properties of truncated and mutated AtNADP-ME2 proteins), block heading 'Malate oxidative decarboxylation; pH 7.5', protein column 'ME2-R115A'; parameter row 'kcat (s-1)' = 234.0; parameter row 'KmL-malate (mM)' = 2.4; parameter row 'KmNADP (lM)' = 50.0. The table is printed transposed, so the three NADP-ME2 protein forms are the columns and the kinetic parameters are the rows; the cells above are the 'ME2-R115A' column of the malate oxidative decarboxylation block, read at the constant character offset of that column. This block prints no catalytic-efficiency row.

normalized_value_unit_evidence: Km: the printed Table 2 cell is 2.4 mM; the printed unit is already mM, so no unit conversion applies, and the exported value is 2.4 mM. kcat: the printed Table 2 cell is 234.0 s^-1; the printed unit is already s^-1, so no unit conversion applies, and the exported value is 234.0 s^(-1). kcat/Km: the malate oxidative decarboxylation block of Table 2 prints no catalytic-efficiency cell, so the exported ratio 97.5 s^(-1)*mM^(-1) is carried as the exact quotient of that same column's own two printed cells, 234.0 / 2.4 = 97.5.

raw_value_unit_evidence: Table 2, protein column 'ME2-R115A', malate oxidative decarboxylation block: KmL-malate = 2.4 mM; kcat = 234.0 s^-1. This block of Table 2 prints no catalytic-efficiency cell.

row_label: Table 2, malate oxidative decarboxylation block (pH 7.5), protein column 'ME2-R115A'

table_label: Table 2: Kinetic properties of truncated and mutated AtNADP-ME2 proteins (Plant Mol Biol (2008) 67:231-242)


substrate_name: pyruvate

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

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

column_label: Table 1 (Kinetic properties of the recombinant AtNADP-ME isoforms), block heading 'Pyruvate reductive carboxylation; pH 7.0', isoform column 'NADP-ME1'; parameter row 'kcat (s-1)' = 16.5; parameter row 'Kmpyruvate (mM)' = 16.9; parameter row 'kcat/Kmpyruvate' = 0.98. The table is printed transposed, so the four isoforms are the columns and the kinetic parameters are the rows; the cells above are the 'NADP-ME1' column of the pyruvate reductive carboxylation block, read at the constant character offset of that column.

normalized_value_unit_evidence: Km: the printed Table 1 cell is 16.9 mM; the printed unit is already mM, so no unit conversion applies, and the exported value is 16.9 mM. kcat: the printed Table 1 cell is 16.5 s^-1; the printed unit is already s^-1, so no unit conversion applies, and the exported value is 16.5 s^(-1). kcat/Km: the printed Table 1 cell is 0.98 in the unit s^-1 mM^-1 that the table's own 'kcat (s-1)' and 'Kmpyruvate (mM)' rows fix, so no unit conversion applies. The exported ratio 0.9763313609467457 is the full-precision quotient of those same two printed cells, 16.5 / 16.9 = 0.9763313609467457, and rounding that quotient to the precision the paper printed returns 0.98, the printed cell itself.

raw_value_unit_evidence: Table 1, isoform column 'NADP-ME1', pyruvate reductive carboxylation block: Kmpyruvate = 16.9 mM; kcat = 16.5 s^-1; printed kcat/Kmpyruvate = 0.98.

row_label: Table 1, pyruvate reductive carboxylation block (pH 7.0), isoform column 'NADP-ME1'

table_label: Table 1: Kinetic properties of the recombinant AtNADP-ME isoforms (Plant Mol Biol (2008) 67:231-242)

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


column_label: Table 1 (Kinetic properties of the recombinant AtNADP-ME isoforms), block heading 'Pyruvate reductive carboxylation; pH 7.0', isoform column 'NADP-ME4'; parameter row 'kcat (s-1)' = 284.1; parameter row 'Kmpyruvate (mM)' = 10.8; parameter row 'kcat/Kmpyruvate' = 26.3. The table is printed transposed, so the four isoforms are the columns and the kinetic parameters are the rows; the cells above are the 'NADP-ME4' column of the pyruvate reductive carboxylation block, read at the constant character offset of that column.

normalized_value_unit_evidence: Km: the printed Table 1 cell is 10.8 mM; the printed unit is already mM, so no unit conversion applies, and the exported value is 10.8 mM. kcat: the printed Table 1 cell is 284.1 s^-1; the printed unit is already s^-1, so no unit conversion applies, and the exported value is 284.1 s^(-1). kcat/Km: the printed Table 1 cell is 26.3 in the unit s^-1 mM^-1 that the table's own 'kcat (s-1)' and 'Kmpyruvate (mM)' rows fix, so no unit conversion applies. The exported ratio 26.305555555555557 is the full-precision quotient of those same two printed cells, 284.1 / 10.8 = 26.305555555555557, and rounding that quotient to the precision the paper printed returns 26.3, the printed cell itself.

raw_value_unit_evidence: Table 1, isoform column 'NADP-ME4', pyruvate reductive carboxylation block: Kmpyruvate = 10.8 mM; kcat = 284.1 s^-1; printed kcat/Kmpyruvate = 26.3.

row_label: Table 1, pyruvate reductive carboxylation block (pH 7.0), isoform column 'NADP-ME4'


column_label: Table 2 (Kinetic properties of truncated and mutated AtNADP-ME2 proteins), block heading 'Pyruvate reductive carboxylation; pH 7.0', protein column 'ME2-R115A'; parameter row 'kcat (s-1)' = 64.1; parameter row 'Kmpyruvate (mM)' = 0.8; parameter row 'kcat/Kmpyruvate' = 82. The table is printed transposed, so the three NADP-ME2 protein forms are the columns and the kinetic parameters are the rows; the cells above are the 'ME2-R115A' column of the pyruvate reductive carboxylation block, read at the constant character offset of that column.

normalized_value_unit_evidence: Km: the printed Table 2 cell is 0.8 mM; the printed unit is already mM, so no unit conversion applies, and the exported value is 0.8 mM. kcat: the printed Table 2 cell is 64.1 s^-1; the printed unit is already s^-1, so no unit conversion applies, and the exported value is 64.1 s^(-1). kcat/Km: the printed Table 2 cell is 82 in the unit s^-1 mM^-1 that the table's own 'kcat (s-1)' and 'Kmpyruvate (mM)' rows fix, so no unit conversion applies, and that printed cell carries into the export unit as 82.0 s^(-1)*mM^(-1). The authors' own fitted efficiency cell is adopted here in place of a recomputed quotient.

raw_value_unit_evidence: Table 2, protein column 'ME2-R115A', pyruvate reductive carboxylation block: Kmpyruvate = 0.8 mM; kcat = 64.1 s^-1; printed kcat/Kmpyruvate = 82.

row_label: Table 2, pyruvate reductive carboxylation block (pH 7.0), protein column 'ME2-R115A'


column_label: Table 1 (Kinetic properties of the recombinant AtNADP-ME isoforms), block heading 'Pyruvate reductive carboxylation; pH 7.0', isoform column 'NADP-ME2'; parameter row 'kcat (s-1)' = 75.0; parameter row 'Kmpyruvate (mM)' = 0.54; parameter row 'kcat/Kmpyruvate' = 138.9. The table is printed transposed, so the four isoforms are the columns and the kinetic parameters are the rows; the cells above are the 'NADP-ME2' column of the pyruvate reductive carboxylation block, read at the constant character offset of that column.

normalized_value_unit_evidence: Km: the printed Table 1 cell is 0.54 mM; the printed unit is already mM, so no unit conversion applies, and the exported value is 0.54 mM. kcat: the printed Table 1 cell is 75.0 s^-1; the printed unit is already s^-1, so no unit conversion applies, and the exported value is 75.0 s^(-1). kcat/Km: the printed Table 1 cell is 138.9 in the unit s^-1 mM^-1 that the table's own 'kcat (s-1)' and 'Kmpyruvate (mM)' rows fix, so no unit conversion applies. The exported ratio 138.88888888888889 is the full-precision quotient of those same two printed cells, 75.0 / 0.54 = 138.88888888888889, and rounding that quotient to the precision the paper printed returns 138.9, the printed cell itself.

raw_value_unit_evidence: Table 1, isoform column 'NADP-ME2', pyruvate reductive carboxylation block: Kmpyruvate = 0.54 mM; kcat = 75.0 s^-1; printed kcat/Kmpyruvate = 138.9.

row_label: Table 1, pyruvate reductive carboxylation block (pH 7.0), isoform column 'NADP-ME2'


column_label: Table 1 (Kinetic properties of the recombinant AtNADP-ME isoforms), block heading 'Pyruvate reductive carboxylation; pH 7.0', isoform column 'NADP-ME3'; parameter row 'kcat (s-1)' = 237.0; parameter row 'Kmpyruvate (mM)' = 4.92; parameter row 'kcat/Kmpyruvate' = 48.2. The table is printed transposed, so the four isoforms are the columns and the kinetic parameters are the rows; the cells above are the 'NADP-ME3' column of the pyruvate reductive carboxylation block, read at the constant character offset of that column.

normalized_value_unit_evidence: Km: the printed Table 1 cell is 4.92 mM; the printed unit is already mM, so no unit conversion applies, and the exported value is 4.92 mM. kcat: the printed Table 1 cell is 237.0 s^-1; the printed unit is already s^-1, so no unit conversion applies, and the exported value is 237.0 s^(-1). kcat/Km: the printed Table 1 cell is 48.2 in the unit s^-1 mM^-1 that the table's own 'kcat (s-1)' and 'Kmpyruvate (mM)' rows fix, so no unit conversion applies. The exported ratio 48.170731707317074 is the full-precision quotient of those same two printed cells, 237.0 / 4.92 = 48.170731707317074, and rounding that quotient to the precision the paper printed returns 48.2, the printed cell itself.

raw_value_unit_evidence: Table 1, isoform column 'NADP-ME3', pyruvate reductive carboxylation block: Kmpyruvate = 4.92 mM; kcat = 237.0 s^-1; printed kcat/Kmpyruvate = 48.2.

row_label: Table 1, pyruvate reductive carboxylation block (pH 7.0), isoform column 'NADP-ME3'


organism: Columba livia

sequence_variant_note: Resolved canonical sequence from uniprot_accession:P40927 and applied mutation signature D464N to reconstruct the assayed variant sequence.

column_label: Table 1, row D464N, columns kcat (s^-1) and Km,Mal (uM); uM-to-mM normalization and kcat/Km division use the printed mean values, with uncertainties retained only as uncertainty evidence.

normalized_value_unit_evidence: kcat 157 s^-1; Km,Mal 0.115 mM; derived kcat/Km 1365.21739130435 s^-1 mM^-1 from the printed mean cells.

raw_value_unit_evidence: Table 1 row D464N: kcat 157 +/- 1.2 s^-1; Km,Mal 115 +/- 11 uM. Footnote a: values were obtained by fitting experimental data to Equation 4.

table_label: Table 1. Kinetic parameters of the recombinant malic enzymes


column_label: Table 1, row WT, columns kcat (s^-1) and Km,Mal (uM); uM-to-mM normalization and kcat/Km division use the printed mean values, with uncertainties retained only as uncertainty evidence.

normalized_value_unit_evidence: kcat 369 s^-1; Km,Mal 0.0854 mM; derived kcat/Km 4320.84309133489 s^-1 mM^-1 from the printed mean cells.

raw_value_unit_evidence: Table 1 row WT: kcat 369 +/- 5 s^-1; Km,Mal 85.4 +/- 15 uM. Footnote a: values were obtained by fitting experimental data to Equation 4.

row_label: WT


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P40927 and applied mutation signature D141N to reconstruct the assayed variant sequence.

column_label: Table 1, row D141N, columns kcat (s^-1) and Km,Mn (uM); uM-to-mM normalization and kcat/Km division use the printed mean values, with uncertainties retained only as uncertainty evidence.

normalized_value_unit_evidence: kcat 84.3 s^-1; Km,Mn 0.0168 mM; derived kcat/Km 5017.85714285714 s^-1 mM^-1 from the printed mean cells.

raw_value_unit_evidence: Table 1 row D141N: kcat 84.3 +/- 4 s^-1; Km,Mn 16.8 +/- 2.4 uM. Footnote a: values were obtained by fitting experimental data to Equation 4.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P40927 and applied mutation signature D141N/D464N to reconstruct the assayed variant sequence.

column_label: Table 1, row D(141,464)N, columns kcat (s^-1) and Km,Mn (uM); uM-to-mM normalization and kcat/Km division use the printed mean values, with uncertainties retained only as uncertainty evidence.

normalized_value_unit_evidence: kcat 65.1 s^-1; Km,Mn 0.012 mM; derived kcat/Km 5425 s^-1 mM^-1 from the printed mean cells.

raw_value_unit_evidence: Table 1 row D(141,464)N: kcat 65.1 +/- 1.6 s^-1; Km,Mn 12 +/- 3 uM. Footnote a: values were obtained by fitting experimental data to Equation 4.


substrate_name: NADP+

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADP+

column_label: Table 1, row D141N, columns kcat (s^-1) and Km,NADP(app) (uM); uM-to-mM normalization and kcat/Km division use the printed mean values, with uncertainties retained only as uncertainty evidence.

normalized_value_unit_evidence: kcat 84.3 s^-1; Km,NADP(app) 0.0061 mM; derived kcat/Km 13819.6721311475 s^-1 mM^-1 from the printed mean cells.

raw_value_unit_evidence: Table 1 row D141N: kcat 84.3 +/- 4 s^-1; Km,NADP(app) 6.1 +/- 0.7 uM. Footnote a: values were obtained by fitting experimental data to Equation 4.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P40927 and applied mutation signature D141N/D194N to reconstruct the assayed variant sequence.

column_label: Table 1, row D(141,194)N, columns kcat (s^-1) and Km,NADP(app) (uM); uM-to-mM normalization and kcat/Km division use the printed mean values, with uncertainties retained only as uncertainty evidence.

normalized_value_unit_evidence: kcat 28.3 s^-1; Km,NADP(app) 0.0108 mM; derived kcat/Km 2620.37037037037 s^-1 mM^-1 from the printed mean cells.

raw_value_unit_evidence: Table 1 row D(141,194)N: kcat 28.3 +/- 1 s^-1; Km,NADP(app) 10.8 +/- 0.8 uM. Footnote a: values were obtained by fitting experimental data to Equation 4.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P40927 and applied mutation signature D141N/D194N/D464N to reconstruct the assayed variant sequence.

column_label: Table 1, row D(141,194,464)N, columns kcat (s^-1) and Km,NADP(app) (uM); uM-to-mM normalization and kcat/Km division use the printed mean values, with uncertainties retained only as uncertainty evidence.

normalized_value_unit_evidence: kcat 91.1 s^-1; Km,NADP(app) 0.0026 mM; derived kcat/Km 35038.4615384615 s^-1 mM^-1 from the printed mean cells.

raw_value_unit_evidence: Table 1 row D(141,194,464)N: kcat 91.1 +/- 2 s^-1; Km,NADP(app) 2.6 +/- 0.2 uM. Footnote a: values were obtained by fitting experimental data to Equation 4.


column_label: Table 1, row D(141,464)N, columns kcat (s^-1) and Km,NADP(app) (uM); uM-to-mM normalization and kcat/Km division use the printed mean values, with uncertainties retained only as uncertainty evidence.

normalized_value_unit_evidence: kcat 65.1 s^-1; Km,NADP(app) 0.0028 mM; derived kcat/Km 23250 s^-1 mM^-1 from the printed mean cells.

raw_value_unit_evidence: Table 1 row D(141,464)N: kcat 65.1 +/- 1.6 s^-1; Km,NADP(app) 2.8 +/- 0.2 uM. Footnote a: values were obtained by fitting experimental data to Equation 4.


column_label: Table 1, row D464N, columns kcat (s^-1) and Km,NADP(app) (uM); uM-to-mM normalization and kcat/Km division use the printed mean values, with uncertainties retained only as uncertainty evidence.

normalized_value_unit_evidence: kcat 157 s^-1; Km,NADP(app) 0.0019 mM; derived kcat/Km 82631.5789473684 s^-1 mM^-1 from the printed mean cells.

raw_value_unit_evidence: Table 1 row D464N: kcat 157 +/- 1.2 s^-1; Km,NADP(app) 1.9 +/- 0.4 uM. Footnote a: values were obtained by fitting experimental data to Equation 4.


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

column_label: Table 1, row WT, columns kcat (s^-1) and Km,NADP(app) (uM); uM-to-mM normalization and kcat/Km division use the printed mean values, with uncertainties retained only as uncertainty evidence.

normalized_value_unit_evidence: kcat 369 s^-1; Km,NADP(app) 0.0038 mM; derived kcat/Km 97105.2631578947 s^-1 mM^-1 from the printed mean cells.

raw_value_unit_evidence: Table 1 row WT: kcat 369 +/- 5 s^-1; Km,NADP(app) 3.8 +/- 0.4 uM. Footnote a: values were obtained by fitting experimental data to Equation 4.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P16243 and applied mutation signature C192A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

column_label: Table 2: Kinetic parameters of the recombinant wild-type NADP-ME and site-directed mutants (Plant Cell Physiol. 53(6): 1144-1153 (2012)); printed column heads kcat (s^-1) | Km NADP (uM) | kcat/Km NADP | Km malate (mM) | kcat/Km malate. Table 2, NADP block, enzyme row C192A; column kcat (s^-1) = 5.6; column Km NADP (uM) = 15.4; column kcat/Km NADP = 0.36 (column head carries no printed unit). captured primary segment: C192A | kcat 5.6 s^-1 | Km NADP 15.4 uM | kcat/Km NADP 0.36 (printed ratio cell; the kcat/Km NADP column head carries no printed unit, and the cell is in uM^-1 s^-1 on this row's own printed kcat (s^-1) and Km NADP (uM) columns)

normalized_value_unit_evidence: kcat: printed Table 2 cell 5.6 s^-1; already in s^-1, so no unit conversion applies; the exported value is 5.6 s^(-1). Km: printed Table 2 cell 15.4 uM; 1 uM is 1/1000 mM, so 15.4 / 1000 = 0.0154 mM; the exported value is 0.0154 mM. kcat/Km: printed Table 2 cell 0.36 in the unprinted-unit efficiency column; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so the printed cell 0.36 x 1000 = 360.0 s^-1 mM^-1. The exported kcat_over_km 363.6363636363636 s^(-1)*mM^(-1) is the full-precision quotient of this row's own two printed cells, 5.6 / 0.0154 = 363.6363636363636, and the printed efficiency cell is that quotient written to the precision the column prints.

raw_value_unit_evidence: Table 2, NADP block, enzyme row C192A: kcat = 5.6 s^-1; Km NADP = 15.4 uM; printed kcat/Km NADP = 0.36, in a column whose head carries no printed unit and whose cell is in uM^-1 s^-1 on this row's own printed kcat and Km columns.

row_label: Table 2, NADP block, enzyme row C192A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P16243 and applied mutation signature C231A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of the recombinant wild-type NADP-ME and site-directed mutants (Plant Cell Physiol. 53(6): 1144-1153 (2012)); printed column heads kcat (s^-1) | Km NADP (uM) | kcat/Km NADP | Km malate (mM) | kcat/Km malate. Table 2, NADP block, enzyme row C231A; column kcat (s^-1) = 23.2; column Km NADP (uM) = 15; column kcat/Km NADP = 1.5 (column head carries no printed unit). captured primary segment: C231A | kcat 23.2 s^-1 | Km NADP 15 uM | kcat/Km NADP 1.5 (printed ratio cell; the kcat/Km NADP column head carries no printed unit, and the cell is in uM^-1 s^-1 on this row's own printed kcat (s^-1) and Km NADP (uM) columns)

normalized_value_unit_evidence: kcat: printed Table 2 cell 23.2 s^-1; already in s^-1, so no unit conversion applies; the exported value is 23.2 s^(-1). Km: printed Table 2 cell 15 uM; 1 uM is 1/1000 mM, so 15 / 1000 = 0.015 mM; the exported value is 0.015 mM. kcat/Km: printed Table 2 cell 1.5 in the unprinted-unit efficiency column; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so the printed cell 1.5 x 1000 = 1500.0 s^-1 mM^-1. The exported kcat_over_km 1546.6666666666667 s^(-1)*mM^(-1) is the full-precision quotient of this row's own two printed cells, 23.2 / 0.015 = 1546.6666666666667, and the printed efficiency cell is that quotient written to the precision the column prints.

raw_value_unit_evidence: Table 2, NADP block, enzyme row C231A: kcat = 23.2 s^-1; Km NADP = 15 uM; printed kcat/Km NADP = 1.5, in a column whose head carries no printed unit and whose cell is in uM^-1 s^-1 on this row's own printed kcat and Km columns.

row_label: Table 2, NADP block, enzyme row C231A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P16243 and applied mutation signature C246A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of the recombinant wild-type NADP-ME and site-directed mutants (Plant Cell Physiol. 53(6): 1144-1153 (2012)); printed column heads kcat (s^-1) | Km NADP (uM) | kcat/Km NADP | Km malate (mM) | kcat/Km malate. Table 2, NADP block, enzyme row C246A; column kcat (s^-1) = 1.1; column Km NADP (uM) = 5.3; column kcat/Km NADP = 0.21 (column head carries no printed unit). captured primary segment: C246A | kcat 1.1 s^-1 | Km NADP 5.3 uM | kcat/Km NADP 0.21 (printed ratio cell; the kcat/Km NADP column head carries no printed unit, and the cell is in uM^-1 s^-1 on this row's own printed kcat (s^-1) and Km NADP (uM) columns)

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.1 s^-1; already in s^-1, so no unit conversion applies; the exported value is 1.1 s^(-1). Km: printed Table 2 cell 5.3 uM; 1 uM is 1/1000 mM, so 5.3 / 1000 = 0.0053 mM; the exported value is 0.0053 mM. kcat/Km: printed Table 2 cell 0.21 in the unprinted-unit efficiency column; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so the printed cell 0.21 x 1000 = 210.0 s^-1 mM^-1. The exported kcat_over_km 207.54716981132077 s^(-1)*mM^(-1) is the full-precision quotient of this row's own two printed cells, 1.1 / 0.0053 = 207.54716981132077, and the printed efficiency cell is that quotient written to the precision the column prints.

raw_value_unit_evidence: Table 2, NADP block, enzyme row C246A: kcat = 1.1 s^-1; Km NADP = 5.3 uM; printed kcat/Km NADP = 0.21, in a column whose head carries no printed unit and whose cell is in uM^-1 s^-1 on this row's own printed kcat and Km columns.

row_label: Table 2, NADP block, enzyme row C246A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P16243 and applied mutation signature C270A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of the recombinant wild-type NADP-ME and site-directed mutants (Plant Cell Physiol. 53(6): 1144-1153 (2012)); printed column heads kcat (s^-1) | Km NADP (uM) | kcat/Km NADP | Km malate (mM) | kcat/Km malate. Table 2, NADP block, enzyme row C270A; column kcat (s^-1) = 1.6; column Km NADP (uM) = 13.5; column kcat/Km NADP = 0.12 (column head carries no printed unit). captured primary segment: C270A | kcat 1.6 s^-1 | Km NADP 13.5 uM | kcat/Km NADP 0.12 (printed ratio cell; the kcat/Km NADP column head carries no printed unit, and the cell is in uM^-1 s^-1 on this row's own printed kcat (s^-1) and Km NADP (uM) columns)

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.6 s^-1; already in s^-1, so no unit conversion applies; the exported value is 1.6 s^(-1). Km: printed Table 2 cell 13.5 uM; 1 uM is 1/1000 mM, so 13.5 / 1000 = 0.0135 mM; the exported value is 0.0135 mM. kcat/Km: printed Table 2 cell 0.12 in the unprinted-unit efficiency column; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so the printed cell 0.12 x 1000 = 120.0 s^-1 mM^-1. The exported kcat_over_km 118.51851851851853 s^(-1)*mM^(-1) is the full-precision quotient of this row's own two printed cells, 1.6 / 0.0135 = 118.51851851851853, and the printed efficiency cell is that quotient written to the precision the column prints.

raw_value_unit_evidence: Table 2, NADP block, enzyme row C270A: kcat = 1.6 s^-1; Km NADP = 13.5 uM; printed kcat/Km NADP = 0.12, in a column whose head carries no printed unit and whose cell is in uM^-1 s^-1 on this row's own printed kcat and Km columns.

row_label: Table 2, NADP block, enzyme row C270A


assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

column_label: Table 2: Kinetic parameters of the recombinant wild-type NADP-ME and site-directed mutants (Plant Cell Physiol. 53(6): 1144-1153 (2012)); printed column heads kcat (s^-1) | Km NADP (uM) | kcat/Km NADP | Km malate (mM) | kcat/Km malate. Table 2, malate block, enzyme row C192A; column kcat (s^-1) = 5.6; column Km malate (mM) = 3.0; column kcat/Km malate = 1.9 (column head carries no printed unit). captured primary segment: C192A | kcat 5.6 s^-1 | Km malate 3.0 mM | kcat/Km malate 1.9 (printed ratio cell; the kcat/Km malate column head carries no printed unit, and the cell is in mM^-1 s^-1 on this row's own printed kcat (s^-1) and Km malate (mM) columns)

normalized_value_unit_evidence: kcat: printed Table 2 cell 5.6 s^-1; already in s^-1, so no unit conversion applies; the exported value is 5.6 s^(-1). Km: printed Table 2 cell 3.0 mM; already in mM, so no unit conversion applies (3.0 mM); the exported value is 3.0 mM. kcat/Km: printed Table 2 cell 1.9 in the unprinted-unit efficiency column; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell 1.9 carries over as 1.9 s^-1 mM^-1. The exported kcat_over_km 1.8666666666666665 s^(-1)*mM^(-1) is the full-precision quotient of this row's own two printed cells, 5.6 / 3.0 = 1.8666666666666665, and the printed efficiency cell is that quotient written to the precision the column prints.

raw_value_unit_evidence: Table 2, malate block, enzyme row C192A: kcat = 5.6 s^-1; Km malate = 3.0 mM; printed kcat/Km malate = 1.9, in a column whose head carries no printed unit and whose cell is in mM^-1 s^-1 on this row's own printed kcat and Km columns.

row_label: Table 2, malate block, enzyme row C192A


column_label: Table 2: Kinetic parameters of the recombinant wild-type NADP-ME and site-directed mutants (Plant Cell Physiol. 53(6): 1144-1153 (2012)); printed column heads kcat (s^-1) | Km NADP (uM) | kcat/Km NADP | Km malate (mM) | kcat/Km malate. Table 2, malate block, enzyme row C231A; column kcat (s^-1) = 23.2; column Km malate (mM) = 1.70; column kcat/Km malate = 13.6 (column head carries no printed unit). captured primary segment: C231A | kcat 23.2 s^-1 | Km malate 1.70 mM | kcat/Km malate 13.6 (printed ratio cell; the kcat/Km malate column head carries no printed unit, and the cell is in mM^-1 s^-1 on this row's own printed kcat (s^-1) and Km malate (mM) columns)

normalized_value_unit_evidence: kcat: printed Table 2 cell 23.2 s^-1; already in s^-1, so no unit conversion applies; the exported value is 23.2 s^(-1). Km: printed Table 2 cell 1.70 mM; already in mM, so no unit conversion applies (1.70 mM); the exported value is 1.7 mM. kcat/Km: printed Table 2 cell 13.6 in the unprinted-unit efficiency column; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell 13.6 carries over as 13.6 s^-1 mM^-1. The exported kcat_over_km 13.647058823529411 s^(-1)*mM^(-1) is the full-precision quotient of this row's own two printed cells, 23.2 / 1.7 = 13.647058823529411, and the printed efficiency cell is that quotient written to the precision the column prints.

raw_value_unit_evidence: Table 2, malate block, enzyme row C231A: kcat = 23.2 s^-1; Km malate = 1.70 mM; printed kcat/Km malate = 13.6, in a column whose head carries no printed unit and whose cell is in mM^-1 s^-1 on this row's own printed kcat and Km columns.

row_label: Table 2, malate block, enzyme row C231A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C246A with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


column_label: Table 2: Kinetic parameters of the recombinant wild-type NADP-ME and site-directed mutants (Plant Cell Physiol. 53(6): 1144-1153 (2012)); printed column heads kcat (s^-1) | Km NADP (uM) | kcat/Km NADP | Km malate (mM) | kcat/Km malate. Table 2, malate block, enzyme row C270A; column kcat (s^-1) = 1.6; column Km malate (mM) = 4.30; column kcat/Km malate = 0.37 (column head carries no printed unit). captured primary segment: C270A | kcat 1.6 s^-1 | Km malate 4.30 mM | kcat/Km malate 0.37 (printed ratio cell; the kcat/Km malate column head carries no printed unit, and the cell is in mM^-1 s^-1 on this row's own printed kcat (s^-1) and Km malate (mM) columns)

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.6 s^-1; already in s^-1, so no unit conversion applies; the exported value is 1.6 s^(-1). Km: printed Table 2 cell 4.30 mM; already in mM, so no unit conversion applies (4.30 mM); the exported value is 4.3 mM. kcat/Km: printed Table 2 cell 0.37 in the unprinted-unit efficiency column; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell 0.37 carries over as 0.37 s^-1 mM^-1. The exported kcat_over_km 0.372093023255814 s^(-1)*mM^(-1) is the full-precision quotient of this row's own two printed cells, 1.6 / 4.3 = 0.372093023255814, and the printed efficiency cell is that quotient written to the precision the column prints.

raw_value_unit_evidence: Table 2, malate block, enzyme row C270A: kcat = 1.6 s^-1; Km malate = 4.30 mM; printed kcat/Km malate = 0.37, in a column whose head carries no printed unit and whose cell is in mM^-1 s^-1 on this row's own printed kcat and Km columns.

row_label: Table 2, malate block, enzyme row C270A


organism: Corynebacterium glutamicum

substrate_name: NADPH

assay_conditions_summary: pH 7; buffer 100 mM pH 7; cofactor NADP+

column_label: PMID 10877795 / PMCID PMC92100 / DOI 10.1128/aem.66.7.2981-2987.2000, section sec17 Kinetic parameters, prose Km entry for NADPH = 0.06 +/- 0.015 mM (normalized 0.06 mM).

raw_value_unit_evidence: section sec17: Km for NADPH = 0.06 +/- 0.015 mM

row_label: NADPH

table_label: Prose section: Biochemical characteristics of malic enzyme, (iii) Kinetic parameters

substrate: NADPH


assay_conditions_summary: pH 7.8; buffer 100 mM pH 7; cofactor NADP+

column_label: PMID 10877795 / PMCID PMC92100 / DOI 10.1128/aem.66.7.2981-2987.2000, section sec17 Kinetic parameters, prose Km entry for NADP+ = 0.083 +/- 0.017 mM (normalized 0.083 mM).

raw_value_unit_evidence: section sec17: Km for NADP+ = 0.083 +/- 0.017 mM

row_label: NADP+


column_label: PMID 10877795 / PMCID PMC92100 / DOI 10.1128/aem.66.7.2981-2987.2000, section sec17 Kinetic parameters, prose Km entry for L-malate = 3.8 +/- 0.6 mM (normalized 3.8 mM).

normalized_value_unit_evidence: km=3.8 mM

raw_value_unit_evidence: section sec17: Km for L-malate = 3.8 +/- 0.6 mM

row_label: L-malate

substrate: L-malate


assay_conditions_summary: pH 7; buffer 100 mM pH 7; cofactor NADPH

column_label: PMID 10877795 / PMCID PMC92100 / DOI 10.1128/aem.66.7.2981-2987.2000, section sec17 Kinetic parameters, prose Km entry for pyruvate = 13.8 +/- 3.5 mM (normalized 13.8 mM).

raw_value_unit_evidence: section sec17: Km for pyruvate = 13.8 +/- 3.5 mM

row_label: pyruvate


enzyme_display_name: Bifunctional malic/malolactic enzyme

organism: Bacillus subtilis (strain 168)

substrate_name: malate

assay_conditions_summary: pH 8; cofactor NADP+

column_label: TABLE 2. Enzymatic parameters of purified YtsJ, MleA, MalS, and MaeA; row label: YtsJ; column label: Malate / Km (mM); raw value 1.55 mM; normalized value 1.55 mM.

normalized_value_unit_evidence: Km=1.55 mM as reported in Table 2.

raw_value_unit_evidence: TABLE 2. Enzymatic parameters of purified YtsJ, MleA, MalS, and MaeA; YtsJ row; Malate / Km (mM) = 1.55 mM.

row_label: YtsJ row / Malate / Km (mM) column

enzyme: Bifunctional malic/malolactic enzyme

substrate: malate


substrate_name: NAD

column_label: TABLE 2. Enzymatic parameters of purified YtsJ, MleA, MalS, and MaeA; row label: YtsJ; column label: NAD / Km (mM); raw value 2.8 mM; normalized value 2.8 mM.

normalized_value_unit_evidence: Km=2.8 mM as reported in Table 2.

raw_value_unit_evidence: TABLE 2. Enzymatic parameters of purified YtsJ, MleA, MalS, and MaeA; YtsJ row; NAD / Km (mM) = 2.8 mM.

row_label: YtsJ row / NAD / Km (mM) column

substrate: NAD


substrate_name: NADP

column_label: TABLE 2. Enzymatic parameters of purified YtsJ, MleA, MalS, and MaeA; row label: YtsJ; column label: NADP / Km (mM); raw value 0.055 mM; normalized value 0.055 mM.

normalized_value_unit_evidence: Km=0.055 mM as reported in Table 2.

raw_value_unit_evidence: TABLE 2. Enzymatic parameters of purified YtsJ, MleA, MalS, and MaeA; YtsJ row; NADP / Km (mM) = 0.055 mM.

row_label: YtsJ row / NADP / Km (mM) column

substrate: NADP


assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K255I to reconstruct the assayed variant sequence.

substrate: NADP+


enzyme_display_name: NADP-dependent malic enzyme

column_label: Table 1 MaeB column maps Km,malate to 3.41 +/- 0.25 mM

raw_value_unit_evidence: Km raw_value=3.41 +/- 0.25 raw_unit=mM

row_label: Km,malate / MaeB

table_label: PMID 17557829 PMC Table 1

enzyme: NADP-dependent malic enzyme


column_label: Table 1 MaeB column maps Km,NADP to 41.5 +/- 1.5 uM

raw_value_unit_evidence: Km raw_value=41.5 +/- 1.5 raw_unit=uM

row_label: Km,NADP / MaeB


assay_conditions_summary: pH 7

column_label: Table 1 MaeB column maps Km,pyruvate to 6.21 +/- 0.4 mM

raw_value_unit_evidence: Km raw_value=6.21 +/- 0.4 raw_unit=mM

row_label: Km,pyruvate / MaeB

substrate: pyruvate


organism: Sinorhizobium meliloti

assay_conditions_summary: cofactor NAD+

proof_lines: Michaelis-Menten type behavior with respect to the co-factors NAD(+) or NADP(+)

enzyme: malate dehydrogenase (decarboxylating)


assay_conditions_summary: cofactor NADP+


organism: Rhodopseudomonas palustris

assay_conditions_summary: pH 7.2; 303.15 K; cofactor NADP+


organism: Mesembryanthemum crystallinum

proof_lines:
NADP+
S0.5
9.9 μM


proof_lines:
L-malate
0.35 mM
Mesembryanthemum crystallinum


assay_conditions_summary: cofactor NADPH

column_label: Results prose referring to Table S2 states: pyruvate Km 5.3 +/- 1.3 mM for YtsJ reverse reductive pyruvate carboxylation.

normalized_value_unit_evidence: Pyruvate Km normalized 5.3 mM; CatLog Km = 5.3 mM.

raw_value_unit_evidence: The Results prose states the YtsJ Km value for pyruvate as 5.3 +/- 1.3 mM.

row_label: YtsJ reverse reductive pyruvate carboxylation with pyruvate

table_label: Results prose; Table S2 key kinetic parameters for YtsJ


column_label: Results prose referring to Table S2 states: NADPH Km 0.8 +/- 0.5 mM for YtsJ reverse reductive pyruvate carboxylation.

normalized_value_unit_evidence: NADPH Km normalized 0.8 mM; CatLog Km = 0.8 mM.

raw_value_unit_evidence: The Results prose states the YtsJ Km value for NADPH as 0.8 +/- 0.5 mM.

row_label: YtsJ reverse reductive pyruvate carboxylation with NADPH


organism: Anas platyrhynchos

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R70Q to reconstruct the assayed variant sequence.


column_label: Table 3, Reductive carboxylation row Km [pyruvate] mM, Cytosolic enzyme column: 7.2 +/- 2.1.

raw_value_unit_evidence: Table 3 reports reductive carboxylation Km [pyruvate] 7.2 +/- 2.1 mM for the cytosolic enzyme.

row_label: Reductive carboxylation, cytosolic enzyme, pyruvate

table_label: Table 3


column_label: Abstract states the Km value for Mn2+ for the natural enzyme is 0.12 +/- 0.02 microM.

raw_value_unit_evidence: Km raw_value=0.12 +/- 0.02 raw_unit=microM

row_label: natural human breast cancer cell cytosolic NADP(+)-dependent malic enzyme with Mn2+

table_label: PubMed abstract PMID 8804575


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature S346K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature K362Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature K362H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature E314A with inferred residue-numbering offset +25 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.4; cofactor NADP+

proof_lines: wild type enzyme, in 50 mMTris-HCl (pH 7.4), at 30°C


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature S346K to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature S346I/K347D/K362H could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P48163 and applied mutation signature K362Q with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; buffer of saturating L-malate; cofactor NADP+

column_label: Table 1, c-NADP-ME row 'K362Q'; column 'K m,NADP (mM)' = 0.7±0.1; column 'k cat,NADP (s-1)' = 132±3; Table 1 carries no k cat/K m column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 132 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 132.0 s^(-1). Km: printed Table 1 cell 0.7 mM; already in mM, no conversion; the paper value is 0.7 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 188.57142857142858 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 132 / 0.7 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, c-NADP-ME row 'K362Q': K m,NADP = 0.7±0.1 mM; k cat,NADP = 132±3 s-1; Table 1 prints no k cat/K m cell for this row.

row_label: Table 1, c-NADP-ME row 'K362Q'

table_label: Table 1: Kinetic parameters for human wild-type and nucleotide-binding mutant variants of c-NADP-ME (PLoS ONE 2011, 6(9):e25312)


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature E314A/S346K with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P48163 and applied mutation signature K362H with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

column_label: Table 1, c-NADP-ME row 'K362H'; column 'K m,NADP (mM)' = 0.3±0.02; column 'k cat,NADP (s-1)' = 149±2; Table 1 carries no k cat/K m column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 149 s-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 149.0 s^(-1). Km: printed Table 1 cell 0.3 mM; already in mM, no conversion; the paper value is 0.3 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 496.6666666666667 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 149 / 0.3 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, c-NADP-ME row 'K362H': K m,NADP = 0.3±0.02 mM; k cat,NADP = 149±2 s-1; Table 1 prints no k cat/K m cell for this row.

row_label: Table 1, c-NADP-ME row 'K362H'


sequence_variant_note: Mutation signature E314A/S346I/K347D/K362H could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature E314A/S346K/K347Y/K362Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature S346K/K347Y/K362H could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature E314A/S346K/K347Y/K362H could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature E314A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

column_label: Table 1, E314A row, Km,mal(NADP) column; adjacent fold-increase cell is 0.4.

normalized_value_unit_evidence: Km=0.4 mM

row_label: E314A c-NADP-ME

table_label: PLOS ONE / PMC3183043 Table 1


sequence_variant_note: Mutation context was captured, but conflicting substitutions targeted the same residue position.


column_label: Table 1, S346K row: Km,mal(NADP)=0.8 +/- 0.1 mM; 0.9 is the adjacent fold-increase value.

normalized_value_unit_evidence: correct Km=0.8 mM; current value=0.9 mM

raw_value_unit_evidence: 0.8 +/- 0.1 mM; adjacent fold-increase cell=0.9

row_label: S346K c-NADP-ME


proof_lines: mutant E314A/S346K/K347Y/K362H, with NAD+, pH 7.4, 30°C


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature S346K/K347Y with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

column_label: Table 1, S346K/K347Y row, Km,mal(NADP) column; adjacent fold-increase cell is 1.0.

normalized_value_unit_evidence: Km=1.0 mM

row_label: S346K/K347Y c-NADP-ME


column_label: Table 1, E314A/S346K row: Km,mal(NADP)=1.0 +/- 0.1 mM; 1.2 is the adjacent fold-increase value.

normalized_value_unit_evidence: correct Km=1.0 mM; current value=1.2 mM

raw_value_unit_evidence: 1.0 +/- 0.1 mM; adjacent fold-increase cell=1.2

row_label: E314A/S346K c-NADP-ME


sequence_variant_note: Mutation signature K347Y/K362Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutants K347Y and K362Q, with NADP+, pH 7.4, 30°C


proof_lines: mutant E314A/S346K/K347Y/K362Q, with NAD+, pH 7.4, 30°C


proof_lines: mutant E314A/S346I/K347D/K362H, with NAD+, pH 7.4, 30°C


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature N59E/E73K with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N59E/E73K, at pH 7.4 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature N59E/E73K/S102D with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N59E/E73K/S102D, at pH 7.4 and 30°C


proof_lines: pH 7.4, 30°C, recombinant mutant N59E/E73K


proof_lines: pH 7.4, 30°C, recombinant mutant N59E/E73K/S102D


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

proof_lines: pH 7.4, 30°C, recombinant mutant [51-105]_c-NADP-ME


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/D90E/K106S/Q121S/L125H with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/D90E/K106S/Q121S/L125H, at pH 7.4 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G, at pH 7.4 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature N59E/E73K/S102D/H74K/D78P/D80E/D87G with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 30°C, recombinant mutant 57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/K106S/Q121S/L125H with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/K106S/Q121S/L125H, at pH 7.4 and 30°C


proof_lines: pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/K106S/Q121S/L125H


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature N59E with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature S102D with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


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

proof_lines: pH 7.4, 30°C, recombinant wild-type enzyme

proof_lines: wild type enzyme, in 50 mM Tris-HCl, pH 7.4, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature E73K with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature S57K/N59E/E73K with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S57K/N59E/E73K, at pH 7.4 and 30°C


proof_lines: pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature S346K/K362Q to reconstruct the assayed variant sequence.

proof_lines: mutant S346K/K362Q, with NADP+, pH 7.4, 30°C


sequence_variant_note: Mutation signature E314A/S346K/K362Q/K347Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature K362H to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature K347Y/K362Q/S346K could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutants K347Y, K362Q, and S346K/K347Y, with NAD+, pH 7.4, 30°C


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature S347Y/K362Q with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant S347Y/K362Q, with NADP+, pH 7.4, 30°C


sequence_variant_note: Mutation signature E314A/S346K/K347Y/K362Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant E314A/S346K/K347Y/K362Q, with NADP+, pH 7.4, 30°C


sequence_variant_note: Mutation signature S346K/K347Y/K362H could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutants S346K/K347Y/K362H, with NAD+, pH 7.4, 30°C


sequence_variant_note: Mutation signature S346I/K347D/K362H could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant S346I/K347D/K362H, with NAD+, pH 7.4, 30°C


sequence_variant_note: Mutation signature E314A/S346K/K347Y/K362H could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant E314A/S346K/K347Y/K362H, with NADP+, pH 7.4, 30°C


sequence_variant_note: Mutation context was captured, but conflicting substitutions targeted the same residue position.

proof_lines: mutants K362H and S347Y/K362Q, with NAD+, pH 7.4, 30°C


sequence_variant_note: Mutation signature S346K/K347Y/K362Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant S346K/K347Y/K362Q, with NADP+, pH 7.4, 30°C


proof_lines: mutant S346K/K347Y/K362H, with NADP+, pH 7.4, 30°C


sequence_variant_note: Mutation signature E314A/S346I/K347D/K362H could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant E314A/S346I/K347D/K362H, with NADP+, pH 7.4, 30°C


proof_lines: mutant S346I/K347D/K362H, with NADP+, pH 7.4, 30°C


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature E314A/S346K with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutants E314A and E314A/S346K, in presence of NAD+, pH 7.4, 30°C

substrate: Unknown


proof_lines: mutant E314A/S346K/K347Y/K362Q, in presence of NAD+, pH 7.4, 30°C


proof_lines: mutant E314A/S346K/K347Y/K362Q, in presence of NADP+, pH 7.4, 30°C


proof_lines: mutant E314A/S346K, in presence of NAPD+, pH 7.4, 30°C


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature E314A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant E314A, in presence of NAPD+, pH 7.4, 30°C


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature S57K/N59E/E73K/S102D with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S57K/N59E/E73K/S102D, at pH 7.4 and 30°C

substrate: (S)-malate


proof_lines: pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K/S102D


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature S57K with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/D90E/K106S/Q121S/L125H with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

column_label: Table 3 row [S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/D90E] + [K106S/Q121S/L125H] (ME1_12 Mutant); Fumarate (-); Km,NADP (uM) column.

normalized_value_unit_evidence: 1.8 uM = 0.0018 mM for the Km,NADP column.

raw_value_unit_evidence: Table 3 row [S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/D90E] + [K106S/Q121S/L125H] (ME1_12 Mutant): Km,NADP = 1.8 +/- 0.2 uM without fumarate.

table_label: Table 3: Kinetic parameters of c-NADP-ME multiple mutants


assay_conditions_summary: pH 7.4; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

column_label: Table 3 row S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G (ME1_8 Mutant); Fumarate (-); Km,NADP (uM) column.

normalized_value_unit_evidence: 1.9 uM = 0.0019 mM for the Km,NADP column.

raw_value_unit_evidence: Table 3 row S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G (ME1_8 Mutant): Km,NADP = 1.9 +/- 0.6 uM without fumarate.


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

proof_lines: pH 7.4, 30°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature N59E/E73K/S102D/H74K/D78P/D80E/D87G with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 30°C, recombinant mutant 57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/K106S/Q121S/L125H with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

column_label: Table 3 row [S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G] + [K106S/Q121S/L125H] (ME1_11 Mutant); Fumarate (-); Km,NADP (uM) column.

normalized_value_unit_evidence: 2.3 uM = 0.0023 mM for the Km,NADP column.

raw_value_unit_evidence: Table 3 row [S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G] + [K106S/Q121S/L125H] (ME1_11 Mutant): Km,NADP = 2.3 +/- 0.3 uM without fumarate.


proof_lines: pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K/S102D/H74K/D78P/D80E/D87G/K106S/Q121S/L125H


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

column_label: Table 2 row c-NADP-ME_WT; Fumarate (-); Km,NADP (uM) column.

raw_value_unit_evidence: Table 2 row c-NADP-ME_WT: Km,NADP = 1.9 +/- 0.2 uM without fumarate and 2.2 +/- 0.3 uM with fumarate.

table_label: Table 2: Kinetic parameters of c-NADP-ME and m-NAD(P)-ME


column_label: Table 2 row S57K/N59E/E73K/S102D (ME1_4 Mutant); Fumarate (-); Km,NADP (uM) column.

normalized_value_unit_evidence: 3.1 uM = 0.0031 mM for the Km,NADP column.

raw_value_unit_evidence: Table 2 row S57K/N59E/E73K/S102D (ME1_4 Mutant): Km,NADP = 3.1 +/- 0.4 uM without fumarate.


column_label: Table 2 row S57K; Fumarate (-); Km,NADP (uM) column.

normalized_value_unit_evidence: 4.5 uM = 0.0045 mM for the Km,NADP column.

raw_value_unit_evidence: Table 2 row S57K: Km,NADP = 4.5 +/- 0.8 uM without fumarate.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature N59E/E73K/S102D with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

column_label: Table 2 row N59E/E73K/S102D; Fumarate (-); Km,NADP (uM) column.

raw_value_unit_evidence: Table 2 row N59E/E73K/S102D: Km,NADP = 4.5 +/- 0.9 uM without fumarate.


proof_lines: pH 7.4, 30°C, recombinant mutant N59E/E73K/S102D


sequence_variant_note: Resolved canonical sequence from uniprotkb:P48163 and applied mutation signature N59E/E73K with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

column_label: Table 2 row N59E/E73K; Fumarate (-); Km,NADP (uM) column.

normalized_value_unit_evidence: 4.6 uM = 0.0046 mM for the Km,NADP column.

raw_value_unit_evidence: Table 2 row N59E/E73K: Km,NADP = 4.6 +/- 0.9 uM without fumarate.


proof_lines: pH 7.4, 30°C, recombinant mutant N59E/E73K


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature S102D to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature S57K/N59E/E73K with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADP+

proof_lines: mutant enzyme S57K/N59E/E73K, at pH 7.4 and 30°C


proof_lines: pH 7.4, 30°C, recombinant mutant S57K/N59E/E73K


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature D139A with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D139A, in 50 mM Tris-HCl, pH 7.4, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature H51A/D139A with inferred residue-numbering offset +25 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H51A/D139A, in 50 mM Tris-HCl, pH 7.4, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature W572A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W572A, in 50 mM Tris-HCl, pH 7.4, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature H51A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H51A, in 50 mM Tris-HCl, pH 7.4, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature H142A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H142A, in 50 mM Tris-HCl, pH 7.4, at 30°C


organism: Zea mays

sequence_variant_note: Resolved canonical sequence from uniprot:P16243 and applied mutation signature F140I to reconstruct the assayed variant sequence.

proof_lines: mutant F140I of isoform C4-NADP-ME, at pH 7.0 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot:A0A1D6M261 and applied mutation signature A339E with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines: mutant DelN/A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C


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

proof_lines: mutant DelN of isoform nonC4-NADP-ME, at pH 7.0 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot:P16243 and applied mutation signature L544F to reconstruct the assayed variant sequence.

proof_lines: mutant L544F of isoform C4-NADP-ME, at pH 7.0 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot:P16243 and applied mutation signature E339A to reconstruct the assayed variant sequence.

proof_lines: mutant E339A of isoform C4-NADP-ME, at pH 7.0 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot:P16243 and applied mutation signature Q503E to reconstruct the assayed variant sequence.

proof_lines: mutant Q503E of isoform C4-NADP-ME, at pH 7.0 and 25°C


proof_lines: mutant A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot:A0A1D6M261 and applied mutation signature I140F/A339E with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines: mutant I140F/A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot:A0A1D6M261 and applied mutation signature I140F with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines: mutant I140F of isoform nonC4-NADP-ME, at pH 7.0 and 25°C


proof_lines: mutant DelN/I140F/A339E of isoform nonC4-NADP-ME, at pH 7.0 and 25°C


assay_conditions_summary: pH 7; cofactor NADP+

column_label: Fig. 3f row Km NADP under ZmC4-NADP-ME F140I gives 8.2 +/- 2.8 uM.

normalized_value_unit_evidence: Km NADP=0.0082 mM converted from 8.2 +/- 2.8 uM

raw_value_unit_evidence: Km NADP raw=8.2 +/- 2.8 uM

row_label: ZmC4-NADP-ME F140I

table_label: Fig. 3f: Kinetic parameters of recombinant ZmC4-NADP-ME WT and mutated versions


column_label: Fig. 3f row Km NADP under ZmC4-NADP-ME Q503E gives 12.8 +/- 3.4 uM.

normalized_value_unit_evidence: Km NADP=0.0128 mM converted from 12.8 +/- 3.4 uM

raw_value_unit_evidence: Km NADP raw=12.8 +/- 3.4 uM

row_label: ZmC4-NADP-ME Q503E


assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+


column_label: Fig. 4a row Km NADP under ZmnonC4-NADP-ME A339E gives 15.0 +/- 3.0 uM.

normalized_value_unit_evidence: Km NADP=0.015 mM converted from 15.0 +/- 3.0 uM

raw_value_unit_evidence: Km NADP raw=15.0 +/- 3.0 uM

row_label: ZmnonC4-NADP-ME A339E

table_label: Fig. 4a: Kinetic parameters of recombinant ZmnonC4-NADP-ME WT and mutant variants


column_label: Fig. 3f row Km NADP under ZmC4-NADP-ME E339A gives 15.9 +/- 2.2 uM.

normalized_value_unit_evidence: Km NADP=0.0159 mM converted from 15.9 +/- 2.2 uM

raw_value_unit_evidence: Km NADP raw=15.9 +/- 2.2 uM

row_label: ZmC4-NADP-ME E339A


column_label: Fig. 3f row Km NADP under ZmC4-NADP-ME L544F gives 15.9 +/- 2.8 uM.

normalized_value_unit_evidence: Km NADP=0.0159 mM converted from 15.9 +/- 2.8 uM

raw_value_unit_evidence: Km NADP raw=15.9 +/- 2.8 uM

row_label: ZmC4-NADP-ME L544F


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

column_label: Fig. 4a row Km NADP under ZmnonC4-NADP-ME WT gives 23.0 +/- 3.0 uM.

normalized_value_unit_evidence: Km NADP=0.023 mM converted from 23.0 +/- 3.0 uM

raw_value_unit_evidence: Km NADP raw=23.0 +/- 3.0 uM

row_label: ZmnonC4-NADP-ME WT


column_label: Fig. 4a row Km NADP under ZmnonC4-NADP-ME I140F gives 38.0 +/- 4.6 uM.

normalized_value_unit_evidence: Km NADP=0.038 mM converted from 38.0 +/- 4.6 uM

raw_value_unit_evidence: Km NADP raw=38.0 +/- 4.6 uM

row_label: ZmnonC4-NADP-ME I140F


column_label: Fig. 4a row Km NADP under ZmnonC4-NADP-ME I140F/A339E gives 41.2 +/- 7.2 uM.

normalized_value_unit_evidence: Km NADP=0.0412 mM converted from 41.2 +/- 7.2 uM

raw_value_unit_evidence: Km NADP raw=41.2 +/- 7.2 uM

row_label: ZmnonC4-NADP-ME I140F/A339E


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

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K225I with inferred residue-numbering offset -3 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.

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

proof_lines:
wild-type enzyme, pH 8.0, 30°C
wild-type enzyme, pH 7.0


substrate_name: L-malate


substrate_name: (S)-malate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature D235A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature E234A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature D258A to reconstruct the assayed variant sequence.


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

proof_lines: pH 7.4, 25°C, Mg2+-activated, wild-type enzyme

proof_lines: pH 7.4, 25°C, Mn2+-activated, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature D257A to reconstruct the assayed variant sequence.


column_label: Table 1. Kinetic parameters for wild-type and mutant pigeon cytosolic NADP+-dependent malic enzymes; row Table 1 row D235A; column KmNADP(app) (uM).

raw_value_unit_evidence: Table 1 Table 1 row D235A reports KmNADP(app) 1.79 +/- 0.10 uM.

row_label: Table 1 row D235A


column_label: Table 1. Kinetic parameters for wild-type and mutant pigeon cytosolic NADP+-dependent malic enzymes; row Table 1 row E234A; column KmNADP(app) (uM).

raw_value_unit_evidence: Table 1 Table 1 row E234A reports KmNADP(app) 1.80 +/- 0.08 uM.

row_label: Table 1 row E234A


column_label: Table 1. Kinetic parameters for wild-type and mutant pigeon cytosolic NADP+-dependent malic enzymes; row Table 1 row Wild-type (Mn2+); column KmNADP(app) (uM).

raw_value_unit_evidence: Table 1 Table 1 row Wild-type (Mn2+) reports KmNADP(app) 2.07 +/- 0.15 uM.

row_label: Table 1 row Wild-type (Mn2+)


column_label: Table 1. Kinetic parameters for wild-type and mutant pigeon cytosolic NADP+-dependent malic enzymes; row Table 1 row D257A; column KmNADP(app) (uM).

raw_value_unit_evidence: Table 1 Table 1 row D257A reports KmNADP(app) 2.83 +/- 0.17 uM.

row_label: Table 1 row D257A


column_label: Table 1. Kinetic parameters for wild-type and mutant pigeon cytosolic NADP+-dependent malic enzymes; row Table 1 row D258A; column KmNADP(app) (uM).

raw_value_unit_evidence: Table 1 Table 1 row D258A reports KmNADP(app) 2.96 +/- 0.07 uM.

row_label: Table 1 row D258A


sequence_source: uniprotkb:P16243 (cites PMID 12562758)

sequence_variant_note: Resolved canonical sequence from uniprotkb:P16243 (cites PMID 12562758) and applied mutation signature R237L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P16243 (cites PMID 12562758) and applied mutation signature A387G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P16243 (cites PMID 12562758) and applied mutation signature A392G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; cofactor NAD+


substrate_name: NADH

assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADH

proof_lines:
isoform ME1, at pH 6.5 and 37°C
isoform ME2, at pH 6.5 and 37°C


assay_conditions_summary: pH 6.5; 310.15 K; cofactor NAD+


proof_lines:
isoform ME2, at pH 6.5 and 37°C
isoform ME1, at pH 6.5 and 37°C


organism: Sinorhizobium sp. strain NGR234

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

assay_conditions_summary: pH 7.8; cofactor NAD+


assay_conditions_summary: pH 7.8; cofactor CoA

proof_lines: pH 7.8, 30°C, AZC3656, in presence of 1 mM fumarate

proof_lines: pH 7.8, 30°C, AZC3656, in presence of 10 mM succinate


assay_conditions_summary: pH 7.8; cofactor NADP+


assay_conditions_summary: cofactor NADP+


assay_conditions_summary: pH 7.4; cofactor NADP+

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


assay_conditions_summary: cofactor NADPH


proof_lines:
recombinant enzyme, pH 7.0
pH 8.0, 30°C, light
pH 8.0, 30°C, dark


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


organism: Sus scrofa


assay_conditions_summary: cofactor NAD+


organism: Spinacia oleracea

assay_conditions_summary: cofactor NADH

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


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

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

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


substrate_name: oxaloacetate

substrate: oxaloacetate


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


organism: Escherichia coli K-12


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NAD+


organism: Saccharomyces cerevisiae


organism: Escherichia coli W

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


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

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


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


organism: Escherichia coli

assay_conditions_summary: pH 7.5; cofactor NADP+


organism: Oryza sativa

assay_conditions_summary: pH 8; cofactor NADP+


assay_conditions_summary: pH 8


organism: Flaveria floridana


organism: Sorghum bicolor


organism: Triticum aestivum


organism: Solanum lycopersicum


organism: Pigeon


organism: Pseudomonas aeruginosa


organism: Vigna mungo


assay_conditions_summary: pH 7.4; cofactor ATP


organism: Citrobacter freundii


organism: Escherichia coli B


organism: Brassica oleracea


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


organism: Sinorhizobium meliloti

proof_lines: assuming an octameric oligomerization state


organism: Zea mays

substrate_name: NADP+; L-Malate

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

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

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

substrate: NADP+; L-Malate


organism: Homo sapiens

sequence_source: uniprotkb


organism: Streptomyces avermitilis


enzyme_display_name: malate dehydrogenase

organism: Methanocaldococcus jannaschii

substrate_name: Oxaloacetate; NADH

enzyme: malate dehydrogenase

substrate: Oxaloacetate; NADH


organism: Methanothermus fervidus

substrate_name: NADH; Oxaloacetate

substrate: NADH; Oxaloacetate


organism: Talaromyces emersonii

substrate_name: H+; Oxaloacetate; NADH

substrate: H+; Oxaloacetate; NADH