assay_conditions_summary: pH 6; cofactor NADPH

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

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

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

row_label: reduction of mevaldehyde

table_label: PMC article abstract/prose


organism: Haloferax volcanii

substrate_name: NADP+

source_db: brenda

verification_status: corrected

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_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; cofactor NADP+

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

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

table_label: Abstract kinetic prose segment

data_origin: experimental

substrate: NADP+

status: corrected

source: brenda


verification_status: verified

assay_conditions_summary: pH 7.3; cofactor CoA

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

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

row_label: (S)-HMG-CoA

table_label: Results prose: Reductive deacylation of HMG-CoA

status: verified


substrate_name: (R,S)-mevaldehyde

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

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

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

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

row_label: oxidative acylation of mevaldehyde

substrate: (R,S)-mevaldehyde


enzyme_display_name: L-lactate dehydrogenase

organism: Limosilactobacillus fermentum

verification_status: unverified

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

enzyme: L-lactate dehydrogenase

status: unverified


substrate_name: NADPH

assay_conditions_summary: pH 6; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: pyruvate

substrate: pyruvate


substrate_name: NADH

assay_conditions_summary: pH 6; 298.15 K; cofactor NADH

substrate: NADH


organism: Gallus gallus

substrate_name: nicotinamide hypoxanthine dinucleotide

km_display: Not reported

substrate: nicotinamide hypoxanthine dinucleotide


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

proof_lines:
enzyme from muscle
enzyme from heart

substrate: NAD+


substrate_name: 3-acetylpyridine adenine dinucleotide

substrate: 3-acetylpyridine adenine dinucleotide


substrate_name: Fluoropyruvate

substrate: Fluoropyruvate


organism: Geobacillus stearothermophilus

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

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

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


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


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


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


organism: Ipomoea batatas

assay_conditions_summary: pH 7.3; cofactor NADH


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


assay_conditions_summary: pH 8.2; cofactor NAD+


substrate_name: (S)-lactate

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

substrate: (S)-lactate


organism: Agama stellio stellio


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


organism: Streptococcus uberis

assay_conditions_summary: cofactor NADH


organism: Taenia asiatica


substrate_name: Lactate

substrate: Lactate


organism: Priestia megaterium

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

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


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

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


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


organism: Molinema dessetae


organism: Solanum tuberosum


substrate_name: Hydroxypyruvate

substrate: Hydroxypyruvate


substrate_name: glyoxylate

substrate: glyoxylate


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


enzyme_display_name: D-lactate dehydrogenase

organism: Lactobacillus delbrueckii subsp. bulgaricus

substrate_name: phenylpyruvate

kcat_over_km_origin: calculated

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADH

column_label: Table 2 row Wild-type, PPA (8a), columns Km, kcat, and kcat/Km give 11.4 mM, 11.3 s-1, and 1.0 x 10^3 M-1 s-1 respectively.

normalized_value_unit_evidence: Km normalized_value=11.4 normalized_unit=mM; kcat normalized_value=11.3 normalized_unit=s^-1; the same Table 2 central values give kcat/Km 11.3/11.4 = 0.9912280701754387 s^-1 mM^-1. The paper also prints the rounded catalytic-efficiency column as 1.0 x 10^3 M^-1 s^-1.

raw_value_unit_evidence: Table 2 reports wild-type D-nLDH for PPA (8a): Km 11.4 mM, Vmax 17.1 U mg-1, kcat 11.3 s-1, and kcat/Km 1.0 x 10^3 M-1 s-1.

row_label: Wild-type D-nLDH / PPA (8a; phenylpyruvic acid)

table_label: Table 2: Kinetic parameters of D-nLDH wild-type and D-nLDH mutants for PPA (8a)

enzyme: D-lactate dehydrogenase

substrate: phenylpyruvate


sequence_variant_note: Resolved canonical sequence from manual_literature_uniprot_resolution and applied mutation signature Y53L to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: pH 7.4, 37°C, recombinant His-taged mutant Y52L


sequence_variant_note: Resolved canonical sequence from manual_literature_uniprot_resolution and applied mutation signature Y53L/F300Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 310.15 K; buffer 1 ml of 50 mM Tris-HCl; cofactor NADH

proof_lines: pH 7.4, 37°C, recombinant His-taged mutant Y52L/F299Y


sequence_variant_note: Resolved canonical sequence from manual_literature_uniprot_resolution and applied mutation signature F300Y to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, recombinant His-taged mutant F299Y


organism: Leuconostoc mesenteroides subsp. cremoris


substrate_name: (R)-lactate

substrate: (R)-lactate


organism: Staphylococcus sp.


enzyme_display_name: 3-hydroxybutyrate dehydrogenase

organism: Pseudomonas putida

enzyme: 3-hydroxybutyrate dehydrogenase


proof_lines:
wild type enzyme
23°C, pH 8.0, wild-type enzyme


organism: Ralstonia pickettii

assay_conditions_summary: 303.15 K; cofactor NADH


assay_conditions_summary: 303.15 K; cofactor NAD+


substrate_name: acetoacetate

substrate: acetoacetate


organism: Staphylococcus xylosus


organism: Rattus norvegicus

proof_lines:
liver, soluble enzyme
heart, soluble enzyme


proof_lines:
heart, soluble enzyme
liver, soluble enzyme
liver 3-hydroxybutyrate dehydrogenase


proof_lines: liver-soluble enzyme, at pH 8.1 and 30°C


organism: Zoogloea ramigera I-16-M


organism: Acidovorax sp.

assay_conditions_summary: pH 5; 328.15 K; cofactor NADH


assay_conditions_summary: pH 8.5; 328.15 K; cofactor NAD+


organism: Pseudomonas fragi


assay_conditions_summary: cofactor NADP+


substrate_name: L-threonine

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

substrate: L-threonine


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Camelus dromedarius

assay_conditions_summary: pH 8.1; 310.15 K; cofactor NAD+


assay_conditions_summary: pH 7; 310.15 K; cofactor NADH


enzyme_display_name: 3-hydroxyisobutyrate dehydrogenase

organism: Pseudomonas denitrificans (nom. rej.)

substrate_name: methyl DL-serine

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

enzyme: 3-hydroxyisobutyrate dehydrogenase

substrate: methyl DL-serine


assay_conditions_summary: pH 9; 303.15 K; cofactor NAD+

proof_lines: with 3-hydroxypropionic acid as cosubstrate, at 30°C and pH 9.0


substrate_name: 3-hydroxypropionic acid

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

substrate: 3-hydroxypropionic acid


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


assay_conditions_summary: cofactor NAD+


substrate_name: L-serine

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

substrate: L-serine


organism: Plasmodium berghei

substrate_name: pyruvate

substrate: pyruvate


substrate_name: NADH

assay_conditions_summary: pH 7.5; cofactor NADH

substrate: NADH


organism: Rhizopus delemar

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


organism: Sus scrofa

proof_lines:
pH 8.5, 25°C, isozyme H4
pH 8.5, 25°C, isozyme H2M2
pH 8.5, 25°C, isozyme M4


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NADH

proof_lines:
pH 8.5, 25°C, isozyme H2M2
pH 8.5, 25°C, isozyme H4
pH 8.5, 25°C, isozyme M4


organism: Pediococcus pentosaceus

assay_conditions_summary: pH 5.4; cofactor NADH


substrate_name: NAD+

substrate: NAD+


organism: Geobacillus stearothermophilus

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


organism: Lactococcus cremoris

assay_conditions_summary: pH 7; 303.15 K; cofactor NADH

proof_lines: pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate


assay_conditions_summary: pH 7; 303.15 K; cofactor NAD+


organism: Faxonius virilis

proof_lines:
aerobic control enzyme, pH 6.7, 25°C
anoxic enzyme, pH 6.7, 25°C
anoxic enzyme, pH 7.2, 25°C


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NAD+

proof_lines:
anoxic enzyme, pH 8.5, 25°C
aerobic control enzyme, pH 8.5, 25°C


proof_lines:
anoxic enzyme, pH 6.7, 25°C
aerobic control enzyme, pH 8.5, 25°C
anoxic enzyme, pH 8.5, 25°C


organism: Enterococcus faecium

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


assay_conditions_summary: cofactor NADH


organism: Cornu aspersum


substrate_name: alpha-Ketobutyrate

substrate: alpha-Ketobutyrate


organism: Lactobacillus delbrueckii subsp. bulgaricus

substrate_name: oxaloacetate

substrate: oxaloacetate


substrate_name: Bromopyruvate

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

substrate: Bromopyruvate


organism: Bos taurus


proof_lines: 240 mM Na+, purified enzyme, reconstituted with total mitochondrial phospholipids


organism: Homo sapiens

assay_conditions_summary: pH 9

proof_lines:
enzyme expressed in SF9 cells
30°C, pH 9.0
25°C, pH 9.0


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

proof_lines: enzyme expressed in SF9 cells, C242S mutant


proof_lines: enzyme expressed in SF9 cells, C242S mutant, C242 important for substrate binding


assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: pH 7.5, temperature not specified in the publication


proof_lines: pH and temperature not specified in the publication


organism: Oryctolagus cuniculus

proof_lines: immobiized recombinant enzyme, pH 7.0, 25°C

proof_lines: soluble recombinant enzyme, pH 7.0, 25°C

proof_lines: immobilized recombinant enzyme, pH 7.0, 25°C


organism: Lacticaseibacillus casei


proof_lines: in presence of 0.02 mM fructose 1,6-diphosphate


organism: Sphyraena ensis


organism: Sphyraena barracuda


organism: Epidalea calamita


substrate_name: (S)-lactate

substrate: (S)-lactate


organism: Pelophylax perezi


organism: [Bacillus] caldolyticus


organism: Lactococcus lactis

assay_conditions_summary: pH 6; 303.15 K; cofactor NADH

proof_lines:
pH 6.0, 30°C, isozyme LDH
pH 7.0, 30°C, isozyme LDH
pH 6.0, 30°C, isozyme LDHB


proof_lines: pH 6.9, 90 mM Tris-maleate buffer, pH 6.9, 0.5 mM fructose 1,6-diphosphate


organism: Lactobacillus acidophilus


organism: Saduria entomon


organism: Gadus morhua


organism: Capsella bursa-pastoris


organism: Lactobacillus sp.


assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: pH 8.0, temperature not specified in the publication, healthy breast tissue enzyme

proof_lines: pH 8.0, temperature not specified in the publication, breast cancer tissue enzyme


assay_conditions_summary: pH 8


organism: Bacillus subtilis


organism: Rattus norvegicus


organism: Heyndrickxia coagulans


organism: Lactobacillus jensenii

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines:
isozyme D-LDH3, pH 8.0, 25°C
isozyme D-LDH2, pH 8.0, 25°C
isozyme D-LDH1, pH 8.0, 25°C


assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

proof_lines:
isozyme D-LDH3, pH 8.0, 25°C
isozyme D-LDH1, pH 8.0, 25°C
isozyme D-LDH2, pH 8.0, 25°C


organism: Limosilactobacillus fermentum

assay_conditions_summary: pH 8; 323.15 K; cofactor NADH


organism: Pediococcus pentosaceus


organism: Pediococcus acidilactici


organism: Cornu aspersum

assay_conditions_summary: cofactor NAD+


organism: Rhodopseudomonas palustris

substrate_name: D-lactate

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

substrate: D-lactate


organism: Lactobacillus delbrueckii subsp. bulgaricus


enzyme_display_name: glycerate dehydrogenase

organism: Petroselinum crispum

enzyme: glycerate dehydrogenase


substrate_name: Hydroxypyruvate

substrate: Hydroxypyruvate


organism: Mycolicibacterium phlei


organism: Bacillus cereus


proof_lines: pH 8.5, 37°C, KM-value for 3-hydroxyisobutyrate is approximately 20fold lower


substrate_name: NADP+

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NADP+

substrate: NADP+


organism: Arabidopsis thaliana

assay_conditions_summary: pH 8.5; 313.15 K; cofactor NAD+

proof_lines:
at pH 8.5 and 40°C
25°C, pH 8.5
at pH 8.5 and 25°C


assay_conditions_summary: pH 10; 310.15 K; cofactor NAD+

proof_lines: at pH 10.0, temperature not specified in the publication


assay_conditions_summary: pH 10


organism: Cereibacter sphaeroides


organism: Oryctolagus cuniculus


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


organism: Homo sapiens

substrate_name: 3-hydroxyisobutyric acid

substrate: 3-hydroxyisobutyric acid


organism: Sus scrofa


organism: Rattus norvegicus

substrate_name: hydroxymethylglutaryl-CoA

assay_conditions_summary: cofactor CoA

substrate: hydroxymethylglutaryl-CoA


substrate_name: Unknown

substrate: Unknown


organism: Schistosoma mansoni


organism: Streptomyces sp.


organism: Saccharolobus solfataricus

assay_conditions_summary: pH 5.5; 323.15 K; cofactor CoA


assay_conditions_summary: pH 5.5; 323.15 K; cofactor NADPH


organism: Unknown

substrate_name: SPC_39_Cell; SPC_33_Cell; SPC_38_Cell

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

substrate: SPC_39_Cell; SPC_33_Cell; SPC_38_Cell


organism: Leishmania donovani

assay_conditions_summary: pH 7.2; 310.15 K; cofactor CoA


assay_conditions_summary: pH 7.2; 310.15 K; cofactor NADPH


organism: Escherichia coli

proof_lines: pH 7.5, 25°C, recombinant mutant I12V/R81Q/M85E/G210A/V214I


organism: Sporolactobacillus inulinus

proof_lines:
isoform LDHL2, pH 7, 40°C
isoform LDHL1, pH 7, 45°C


organism: Plasmodium falciparum

sequence_source: uniprot_manual_search:Q76NM3 (PF3D7_1324900, isolate 3D7)


organism: Champsocephalus gunnari

sequence_source: uniprotkb:O93541 (PDB:2V65; paper PMID:17936781)

assay_conditions_summary: pH 7


organism: Lactobacillus helveticus


substrate_name: 3-acetylpyridine adenine dinucleotide

substrate: 3-acetylpyridine adenine dinucleotide


organism: Sphyraena helleri


organism: Thermus thermophilus


organism: Nocardia asteroides


organism: Latilactobacillus curvatus

assay_conditions_summary: cofactor NADH


organism: Streptococcus mutans


organism: Oligosoma polychroma


organism: Clupea harengus

proof_lines:
pH 7.2, 25°C, isoenzyme LDH-A2B2
pH 7.6, 25°C, isoenzyme LDH-B4
pH 7.1, 25°C, isoenzyme LDH-A4


organism: Woodworthia maculata


organism: Woodworthia chrysosiretica


organism: Oligosoma macgregori


organism: Oligosoma zelandicum


organism: Lactuca sativa


organism: Aggregatibacter actinomycetemcomitans

substrate_name: L-lactate

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

substrate: L-lactate


organism: Heyndrickxia coagulans

substrate_name: pyruvate

substrate: pyruvate


organism: Lactococcus cremoris

proof_lines: pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate


organism: Lactococcus lactis

proof_lines: in presence of 1 mM fructose 1,6-diphosphate


proof_lines: in presence of 1.0 mM fructose 1,6-diphosphate


organism: Lacticaseibacillus casei


organism: Plasmodium falciparum


organism: Homo sapiens

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH

proof_lines: LDH-A, pH not specified in the publication, temperature not specified in the publication

proof_lines: pH 7.5, 37°C, recombinant His-tagged enzyme, pyruvate reduction, competitive versus NADH


organism: Unknown

substrate_name: SPC_39_Cell; SPC_1262_Cell; SPC_33_Cell

substrate: SPC_39_Cell; SPC_1262_Cell; SPC_33_Cell


organism: Limosilactobacillus reuteri

substrate_name: 3,4-dihydroxyphenylpyruvic acid

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines:
cosubstrate NADPH, pH 8.0, 25°C
cosubstrate NADH, pH 8.0, 25°C

substrate: 3,4-dihydroxyphenylpyruvic acid


organism: Furfurilactobacillus rossiae

substrate_name: phenylpyruvate

substrate: phenylpyruvate


organism: Sporolactobacillus inulinus

proof_lines:
isoform LDHD3, pH 5.5, 35°C
isoform LDHD2, pH 7.5, 35°C
isoform LDHD1, pH 6, 35°C


organism: Lactiplantibacillus plantarum subsp. plantarum


organism: Lactobacillus delbrueckii subsp. bulgaricus


substrate_name: NADH

substrate: NADH


organism: Lactiplantibacillus plantarum


organism: Neisseria meningitidis

substrate_name: (R)-lactate

substrate: (R)-lactate


organism: Pediococcus pentosaceus

substrate_name: NAD+

substrate: NAD+


organism: Leuconostoc mesenteroides


organism: Leuconostoc lactis


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


organism: Limosilactobacillus fermentum


organism: Lactobacillus jensenii


organism: Lactobacillus leichmannii


organism: Zea mays


assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+

proof_lines:
25°C, pH 9.0
enzyme expressed in SF9 cells


organism: Bos taurus


proof_lines: 240 mM Na+, purified enzyme, reconstituted with total mitochondrial phospholipids


enzyme_display_name: Transferred entry: 1.1.1.1

substrate_name: SPC_39_Cell; SPC_38_Cell; SPC_5227_Cell

enzyme: Transferred entry: 1.1.1.1

substrate: SPC_39_Cell; SPC_38_Cell; SPC_5227_Cell


organism: Oryctolagus cuniculus


organism: Mus musculus

proof_lines: reductase from liver and reductase from tumor


organism: Unknown


organism: Trypanosoma cruzi

substrate_name: NADPH

assay_conditions_summary: pH 6.8; 298.15 K; cofactor NADPH

substrate: NADPH


organism: Fusarium oxysporum


organism: Hevea brasiliensis


organism: Homarus americanus


organism: Saccharolobus solfataricus


organism: Sus scrofa

substrate_name: (S)-lactate

source_db: skid

source_license: CC BY-NC-ND 4.0

substrate: (S)-lactate

source: skid


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NADH


organism: Plasmodium falciparum

assay_conditions_summary: pH 9.2; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


organism: Pseudomonas fragi

substrate_name: acetoacetate

substrate: acetoacetate


assay_conditions_summary: cofactor NAD+


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


substrate_name: L-threonine

substrate: L-threonine


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADP+


substrate_name: 3-hydroxypropanoic acid

substrate: 3-hydroxypropanoic acid


substrate_name: L-serine

substrate: L-serine


assay_conditions_summary: pH 8.5; 303.15 K; cofactor NAD+


organism: Jaculus orientalis

proof_lines:
euthermic state, brain
euthermic state, liver


proof_lines:
euthermic state, liver
isoenzyme from heavy mitochondria
pH 8.0, 25°C


organism: Thermoanaerobacter ethanolicus

proof_lines:
pH 5.8, 60°C, recombinant enzyme
with 1.0 mM fructose 1,6-diphosphate
in absence of fructose 1,6-diphosphate


organism: Geobacillus stearothermophilus


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


organism: Homo sapiens

source_db: uniprot

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

source: uniprot


assay_conditions_summary: pH 8; cofactor NAD+


assay_conditions_summary: pH 8


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.


assay_conditions_summary: cofactor NADPH


assay_conditions_summary: cofactor CoA


organism: Deinococcus radiodurans

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

assay_conditions_summary: pH 7

proof_lines: kcat is 884 sec(-1) for pyruvate as substrate.

source_databases_merged: brenda skid uniprot


organism: Oryctolagus cuniculus


organism: Lactobacillus helveticus

proof_lines: kcat is 643 sec(-1) for pyruvate as substrate.


proof_lines:
isoenzyme from heavy mitochondria
pH 8.0, 25°C
euthermic state, liver


organism: Alcaligenes faecalis

substrate_name: levulinic acid

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

substrate: levulinic acid


organism: Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)

substrate_name: (S)-HMG-CoA

proof_lines: KCl concentrations greater than 2 M are required for maximum reductase activity.

substrate: (S)-HMG-CoA


substrate_name: NAD

assay_conditions_summary: cofactor NADH

substrate: NAD


organism: Limulus polyphemus


substrate_name: pyruvate

substrate: pyruvate


organism: Homarus americanus


organism: Vitis vinifera

substrate_name: 2-keto-L-gulonate (in presence of NADPH)

assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: Table 2 columns Substrate, Coenzyme, Km (mM), Vmax (units/mg), Kcat (s^-1); row 2KLG / NADPH has Km 0.700 mM

raw_value_unit_evidence: Table 2 row 2KLG with coenzyme NADPH reports Km 0.700 mM, Vmax 7.544 units/mg, Kcat 4.178 s^-1

row_label: 2KLG / NADPH

table_label: Table 2


substrate_name: hydroxypyruvate (in presence of NADPH)

column_label: Table 2 columns Substrate, Coenzyme, Km (mM), Vmax (units/mg), Kcat (s^-1); row Hydroxypyruvate / NADPH has Km 0.096 mM

raw_value_unit_evidence: Table 2 row Hydroxypyruvate with coenzyme NADPH reports Km 0.096 mM, Vmax 6.295 units/mg, Kcat 6.973 s^-1; NADH row reports no activity

row_label: Hydroxypyruvate / NADPH

substrate: hydroxypyruvate (in presence of NADPH)


substrate_name: glyoxylate (in presence of NADPH)

column_label: Table 2 columns Substrate, Coenzyme, Km (mM), Vmax (units/mg), Kcat (s^-1); row d-Glyoxylate / NADPH has Km 0.044 mM

raw_value_unit_evidence: Table 2 row d-Glyoxylate with coenzyme NADPH reports Km 0.044 mM, Vmax 13.820 units/mg, Kcat 38.26 s^-1

row_label: d-Glyoxylate / NADPH

substrate: glyoxylate (in presence of NADPH)


substrate_name: pyruvate (in presence of NADPH)

substrate: pyruvate (in presence of NADPH)


organism: Hyphomicrobium methylovorum

substrate_name: NADH

substrate: NADH


substrate_name: Hydroxypyruvate

column_label: The abstract reports Km values of 0.175 mM for hydroxypyruvate and 10.8 mM for glyoxylate.

raw_value_unit_evidence: Km raw_value=0.175 mM raw_unit=mM

row_label: Prose segment: hydroxypyruvate Km

table_label: PubMed PMID 2114287 abstract

substrate: Hydroxypyruvate


substrate_name: glyoxylate

raw_value_unit_evidence: Km raw_value=10.8 mM raw_unit=mM

row_label: Prose segment: glyoxylate Km

substrate: glyoxylate


organism: Sphyraena idiastes


organism: Sphyraena lucasana

verification_status: disputed

status: disputed


organism: Sphyraena argentea


organism: Plasmodium berghei (strain Anka)


organism: Lactobacillus acidophilus

proof_lines:
Bacterial lactate dehydrogenases
Lactobacillus acidophilus
L-lactate dehydrogenase


substrate_name: (R)-lactate

proof_lines:
Bacterial lactate dehydrogenases
Lactobacillus acidophilus
D-lactate dehydrogenase

substrate: (R)-lactate


organism: Leishmania major

column_label: PubMed abstract reports (R,S)-HMG-CoA K(m)=40.3+/-5.8 microM for the overall reaction.

raw_value_unit_evidence: K(m) values for the overall reaction: 40.3+/-5.8 microM for (R,S)-HMG-CoA and 81.4+/-5.3 microM for NADPH

row_label: Leishmania major HMG-CoA reductase overall reaction with (R,S)-HMG-CoA

table_label: PubMed abstract PMID 10861207


substrate_name: NADPH

column_label: PubMed abstract reports NADPH K(m)=81.4+/-5.3 microM for the overall reaction.

row_label: Leishmania major HMG-CoA reductase overall reaction with NADPH

substrate: NADPH


organism: Babesia bovis


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

assay_conditions_summary: pH 7.3; cofactor NADPH

column_label: Paper prose evidence: abstract kinetic prose segment; row_label=HMG-CoA reductase direction / (S)-HMG-CoA; column_label=Km for (S)-HMG-CoA; raw_value=60 raw_unit=microM; normalized_value=0.06 normalized_unit=mM; assay_condition=HMG-CoA reductase activity optimal at pH 7.3; captured paper segment: Kms were 66 microM (NADPH) and 60 microM [(S)-HMG-CoA].

raw_value_unit_evidence: Km raw_value=60 microM raw_unit=microM raw_cell=Kms were 66 microM (NADPH) and 60 microM [(S)-HMG-CoA]


column_label: Paper prose evidence: abstract kinetic prose segment; row_label=HMG-CoA reductase direction / NADPH; column_label=Km for NADPH; raw_value=66 raw_unit=microM; normalized_value=0.066 normalized_unit=mM; assay_condition=HMG-CoA reductase activity optimal at pH 7.3; captured paper segment: Kms were 66 microM (NADPH) and 60 microM [(S)-HMG-CoA].

raw_value_unit_evidence: Km raw_value=66 microM raw_unit=microM raw_cell=Kms were 66 microM (NADPH) and 60 microM [(S)-HMG-CoA]

row_label: HMG-CoA reductase direction / NADPH


organism: Acinetobacter calcoaceticus

substrate_name: (S)-lactate

substrate: (S)-lactate


organism: Lactiplantibacillus pentosus

substrate_name: pyruvate (at pH 5)

assay_conditions_summary: pH 5

substrate: pyruvate (at pH 5)


organism: Lacticaseibacillus casei

substrate_name: pyruvate (at pH 4.8)

assay_conditions_summary: pH 4.8; cofactor NADH

proof_lines:
L(+)-lactate dehydrogenase
NADH
pyruvate

substrate: pyruvate (at pH 4.8)


organism: Lactobacillus delbrueckii subsp. lactis


organism: Diutina rugosa

substrate_name: NAD+

column_label: Kinetic studies section, NAD+ Km line: 5.00 x 10^-5 M.

raw_value_unit_evidence: Km value for NAD+ was 5.00 x 10^-5 M.

row_label: NAD+ for beta-HIBA dehydrogenase from Candida rugosa IFO 0750

table_label: Kinetic studies section and abstract

substrate: NAD+


organism: Thermoanaerobacter ethanolicus

substrate_name: Unknown

substrate: Unknown


organism: Unknown

source_db: strenda

source_license: see source

proof_lines: Raw STRENDA Extraction: 8.00		37.0 ℃	0.12 µg ml⁻¹

source: strenda


organism: Cryptosporidium parvum

source_db: oed

source: oed


organism: Thermus caldophilus

proof_lines: kcat is 745 sec(-1) for pyruvate (in the presence of fructose 1,6-bisphosphate (FBP)). kcat is 131 sec(-1) for pyruvate (in the absence of fructose 1,6-bisphosphate (FBP)).


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

substrate_name: NADH (at 55 degrees Celsius and in the absence of fructose 1,6-bisphosphate (FBP))


organism: Thermus aquaticus


organism: Fusobacterium nucleatum subsp. nucleatum


organism: Lactobacillus helveticus

substrate_name: nicotinamide cytosine dinucleotide

substrate: nicotinamide cytosine dinucleotide


organism: Vitis vinifera


organism: Jaculus orientalis

proof_lines: pH 8.0, 25°C, versus (R)-3-hydroxybutanoate


organism: Homo sapiens


organism: Rattus norvegicus


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


proof_lines: Allosteric and kinetic properties of L-lactate dehydrogenase from Thermus caldophilus GK24, an extremely thermophilic bacterium


assay_conditions_summary: pH 6; cofactor NADH


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

organism: Thermus thermophilus

substrate_name: Deamino-NADH

substrate: Deamino-NADH


organism: Talaromyces emersonii

substrate_name: L-Malate

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

column_label: PDF page 10/article page 3124, Table 2, Recombinant m-MDH Malate ([NAD+] = 1 mM) row reports kcat/Km 2.44 x 10^3 s^-1 mM^-1, not the exported 3500 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=1.0 normalized_unit=mM; kcat normalized_value=3500 normalized_unit=s^-1; kcat_over_km normalized_value=2440 normalized_unit=s^-1*mM^-1

row_label: Recombinant m-MDH; Malate ([NAD+] = 1 mM)

table_label: Table 2, kinetic constants of recombinant m-MDH

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

substrate: L-Malate


organism: Streptomyces coelicolor

column_label: Table 1, NAD+ row, Km column 0.150 mM, kcat column 3.66 s^-1, and kcat/Km column 24.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 NAD+ row: Km 0.150 mM; kcat 3.66 s^-1; kcat/Km 24.4 s^-1 mM^-1.

row_label: NAD+

table_label: Table 1. Kinetic Parameters of Recombinant ScMDH


assay_conditions_summary: pH 7.6; 310.15 K; cofactor NADH

column_label: Table 1, reaction column 'oxaloacetate → malate': row 'Kcat (1/min)' cell = 10.6 (printed as '10.6 ± ...'), row 'Km, NADH (mM)' cell = 0.004. Table 1 prints no kcat/Km column; the kcat/Km entry is the quotient of those two cells, 10.6 (1/min) / 0.004 (mM).

normalized_value_unit_evidence: kcat raw 10.6 1/min normalizes to 0.17666666666666667 s^-1 (divide by 60); km raw 0.004 mM normalizes to 0.004 mM; kcat/Km = 0.17666666666666667 s^-1 / 0.004 mM = 44.166666666666664 s^-1 mM^-1 (quotient of the two printed Table 1 cells; the paper prints no kcat/Km column).

raw_value_unit_evidence: Table 1; reaction column oxaloacetate → malate; column 'Kcat (1/min)'; raw value 10.6 1/min | Table 1; reaction column oxaloacetate → malate; column 'Km, NADH (mM)'; raw value 0.004 mM

row_label: oxaloacetate → malate | Km, NADH (mM)

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


assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADH

column_label: Table 1, NADH row, Km column 0.083 mM, kcat column 5.42 x 10^2 s^-1, and kcat/Km column 6.56 x 10^3 s^-1 mM^-1.

row_label: NADH


assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH


organism: Ignicoccus islandicus

substrate_name: oxaloacetate

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

assay_conditions_summary: pH 7; 343.15 K; buffer 50 mM phosphate; cofactor NADH

column_label: Table 1 rows kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1), Oxaloacetate column cells 444, 0.38, and 1.2 x 10^6.

normalized_value_unit_evidence: kcat=444 s^-1; Km=0.38 mM; kcat/Km=1200 s^-1 mM^-1 from printed 1.2 x 10^6 M^-1 s^-1, matching expected 1168.421052631579 within table precision.

raw_value_unit_evidence: Oxaloacetate column: kcat 444 s^-1; Km 0.38 mM; kcat/Km 1.2 x 10^6 M^-1 s^-1.

row_label: Oxaloacetate

table_label: ScienceDirect HTML Table 1, Kinetic properties of I. isl MalDH

substrate: oxaloacetate


organism: Malus domestica


column_label: Table 1, oxaloacetate row, Km column 0.189 mM, kcat column 1.87 x 10^3 s^-1, and kcat/Km column 1.0 x 10^4 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 oxaloacetate row: Km 0.189 mM; kcat 1.87 x 10^3 s^-1; kcat/Km 1.0 x 10^4 s^-1 mM^-1.


organism: Taenia solium

assay_conditions_summary: pH 8; 295.15 K; cofactor NADH

column_label: Table 2, oxaloacetate row, kcat 665.34 s^-1, Km 0.044 mM, and kcat/Km 1.51 x 10^7 M^-1 s^-1.

raw_value_unit_evidence: Table 2 oxaloacetate row: kcat 665.34 s^-1; Km 0.044 mM; kcat/Km 1.51 x 10^7 M^-1 s^-1.

table_label: Table 2. Kinetic constants of recombinant TscMDH


substrate_name: (S)-malate

assay_conditions_summary: pH 9.6; 295.15 K; cofactor NADH

column_label: Table 2, L-malate row, kcat 47.4 s^-1, Km 0.1 mM, and kcat/Km 4.74 x 10^5 M^-1 s^-1.

raw_value_unit_evidence: Table 2 L-malate row: kcat 47.4 s^-1; Km 0.1 mM; kcat/Km 4.74 x 10^5 M^-1 s^-1.

row_label: L-malate

substrate: (S)-malate


column_label: Table 1, reaction column 'oxaloacetate → malate': row 'Kcat (1/min)' cell = 10.6 (printed as '10.6 ± ...'), row 'Km, oxaloacetate (mM)' cell = 6.5. Table 1 prints no kcat/Km column; the kcat/Km entry is the quotient of those two cells, 10.6 (1/min) / 6.5 (mM).

normalized_value_unit_evidence: kcat raw 10.6 1/min normalizes to 0.17666666666666667 s^-1 (divide by 60); km raw 6.5 mM normalizes to 6.5 mM; kcat/Km = 0.17666666666666667 s^-1 / 6.5 mM = 0.02717948717948718 s^-1 mM^-1 (quotient of the two printed Table 1 cells; the paper prints no kcat/Km column).

raw_value_unit_evidence: Table 1; reaction column oxaloacetate → malate; column 'Kcat (1/min)'; raw value 10.6 1/min | Table 1; reaction column oxaloacetate → malate; column 'Km, oxaloacetate (mM)'; raw value 6.5 mM

row_label: oxaloacetate → malate | Km, oxaloacetate (mM)


enzyme_display_name: Malate dehydrogenase 1, mitochondrial

organism: Arabidopsis thaliana

substrate_name: oxaloacetate (at pH 7.5)

assay_conditions_summary: cofactor NAD+

enzyme: Malate dehydrogenase 1, mitochondrial

substrate: oxaloacetate (at pH 7.5)


enzyme_display_name: Malate dehydrogenase, glyoxysomal

organism: Citrullus lanatus

substrate_name: NADH

enzyme: Malate dehydrogenase, glyoxysomal


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N259A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R542A with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R197E with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R542E with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q362A to reconstruct the assayed variant sequence.

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q362K to reconstruct the assayed variant sequence.


organism: Escherichia coli

sequence_source: uniprotkb:P61889 (identical to P61890/P61891)

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 7.5; 283.15 K; cofactor NADH


assay_conditions_summary: pH 7.5; 277.15 K; cofactor NADH


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

organism: Plasmodium falciparum

substrate_name: 3-acetylpyridine-adenine dinucleotide

sequence_variant_note: Resolved canonical sequence from uniprot:Q6VVP7 and applied mutation signature R183A to reconstruct the assayed variant sequence.

substrate: 3-acetylpyridine-adenine dinucleotide


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


sequence_variant_note: Resolved canonical sequence from uniprot:Q6VVP7 and applied mutation signature R214G to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 10.2; cofactor NAD+


substrate_name: reduced acetylpyridine adenine dinucleotide


substrate_name: malate

substrate: malate


assay_conditions_summary: pH 7.5; cofactor NADH


substrate_name: acetylpyridine adenine dinucleotide

substrate: acetylpyridine adenine dinucleotide


organism: Euglena gracilis

proof_lines: m-MDH s-MDH


assay_conditions_summary: cofactor NADH


proof_lines: s-MDH m-MDH


substrate_name: L-malate

substrate: L-malate


organism: Macromonas bipunctata

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADH


assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+


organism: Trichomonas vaginalis

assay_conditions_summary: pH 7.8; cofactor NADH


assay_conditions_summary: pH 7.8; cofactor NAD+


organism: Methanothermobacter thermautotrophicus

proof_lines: pH and temperature not specified in the publication


organism: Stutzerimonas stutzeri


proof_lines: at 0.08-0.18 mM, pH and temperature not specified in the publication

proof_lines: at 0.18-10.0 mM, pH and temperature not specified in the publication


organism: Leishmania major

proof_lines:
cytosolic isoenzyme
mitochondrial isoenzyme
glycosomal isoenzyme


proof_lines:
mitochondrial isoenzyme
glycosomal isoenzyme
cytosolic isoenzyme


proof_lines:
glycosomal isoenzyme
cytosolic isoenzyme
mitochondrial isoenzyme


organism: Coccochloris peniocystis


assay_conditions_summary: cofactor NADP+


organism: Helicobacter pylori


organism: Mesembryanthemum cordifolium

assay_conditions_summary: pH 6.9; 303.15 K; cofactor NADH


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+


organism: Heliocidaris crassispina


organism: Vulcanithermus mediatlanticus

sequence_source: ncbi_protein:WP_464884684.1 (identical to BGR20347.1)


assay_conditions_summary: pH 9; cofactor NAD+


assay_conditions_summary: pH 9


organism: Physarum polycephalum


assay_conditions_summary: cofactor NAD+


organism: Ignicoccus islandicus

substrate_name: pyruvate

sequence_source: pdb|6QSS|A (NCBI protein efetch; linked via PMID 31301348)

assay_conditions_summary: pH 7; cofactor NADH

column_label: Table 1 row kcat (s^-1), Pyruvate column cell 8.

normalized_value_unit_evidence: kcat=8 s^-1. No Km was populated in the expected row, and Table 1 leaves Km blank for pyruvate.

row_label: Pyruvate

substrate: pyruvate


assay_conditions_summary: pH 7; buffer 50 mM phosphate; cofactor NADH


organism: Leishmania mexicana


organism: Eleusine indica

substrate_name: NAD+


organism: Aeropyrum pernix

sequence_source: UniProt:Q9YEA1 (SIFTS via PDB:2D4A)

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


organism: Panicum miliaceum


organism: Digitaria sanguinalis


organism: Sinorhizobium meliloti

sequence_source: uniprot:O30807 (GN=dme; NAD-dependent malic enzyme; Rhizobium/Sinorhizobium meliloti)

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


organism: Geophagus brasiliensis

proof_lines:
isoform B2, at 20°C
isoform B1, at 20°C


organism: Sus scrofa

assay_conditions_summary: pH 7.5; 293.15 K; cofactor NADH

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


organism: Megathyrsus maximus


organism: Zea mays


proof_lines:
pH 8.1, 22°C
pH 7.5, 20°C, cytosolic isoenzyme cMDH
cytoplasmic isoenzyme


enzyme_display_name: malate dehydrogenase

organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)

substrate_name: Oxaloacetate

sequence_source: uniprotkb:D9PVI7 (lit_pubmed=9639601)

enzyme: malate dehydrogenase

substrate: Oxaloacetate


organism: Erwinia aroidea


organism: Drosophila virilis

proof_lines:
cytoplasmic isoenzyme
mitochondrial isoenzyme


organism: Hoplias malabaricus


organism: Eriochloa borumensis


organism: Agrobacterium tumefaciens


organism: Haloarcula marismortui

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature R100Q with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication, 4 M NaCl, mutant enzyme R100Q


proof_lines: pH 7.0, temperature not specified in the publication, 2 M NaCl, mutant enzyme R100Q


proof_lines: pH 7.0, temperature not specified in the publication, 4 M NaCl, wild-type enzyme

proof_lines: pH 7.0, temperature not specified in the publication, 2 M NaCl, wild-type enzyme

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


proof_lines: pH 7.0, temperature not specified in the publication, 0.15 M NaCl, mutant enzyme R100Q


organism: Taenia solium

proof_lines: pH 8.0, temperature not specified in the publication


assay_conditions_summary: pH 9.6; cofactor NAD+

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

source_databases_merged: brenda uniprot


assay_conditions_summary: pH 8; cofactor NADH


enzyme_display_name: Malate dehydrogenase, cytoplasmic

substrate_name: L-malate (at pH 9.6)

assay_conditions_summary: pH 9.6; cofactor NADH

enzyme: Malate dehydrogenase, cytoplasmic

substrate: L-malate (at pH 9.6)


enzyme_display_name: D-3-phosphoglycerate dehydrogenase

organism: Homo sapiens

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

enzyme: D-3-phosphoglycerate dehydrogenase


substrate_name: NAD(+)

substrate: NAD(+)


assay_conditions_summary: cofactor NADH


enzyme_display_name: UniProt Q6VVP7

organism: Plasmodium falciparum

enzyme: UniProt Q6VVP7


assay_conditions_summary: pH 10.2; cofactor NAD+

substrate: NAD+


assay_conditions_summary: pH 7.5; cofactor NADH


enzyme_display_name: Malate dehydrogenase

organism: Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)

substrate_name: oxaloacetate (in the presence of NADH)

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 1181.6 sec(-1) for NADH-dependent reduction of oxaloacetate. kcat is 67.4 sec(-1) for NADPH-dependent reduction of oxaloacetate. kcat is 4.88 sec(-1) for NAD(+)-dependent oxidation of malate.

enzyme: Malate dehydrogenase

substrate: oxaloacetate (in the presence of NADH)


substrate_name: NADPH

substrate: NADPH


organism: Synechocystis sp. PCC 6803

assay_conditions_summary: pH 8; 318.15 K; cofactor NAD+

column_label: Table 1 row NAD+ lists kcat=0.21 s^-1 and kcat/Km=0.357 s^-1 mM^-1; Table 2 Synechocystis sp. PCC 6803 row lists NAD+ Km=580 uM.

normalized_value_unit_evidence: kcat normalized_value=0.21 normalized_unit=s^-1; Km normalized_value=0.58 normalized_unit=mM; kcat/Km table value=0.357 s^-1 mM^-1; export kcat/Km=0.3620689655172414 from paired rounded kcat and Km cells

raw_value_unit_evidence: Table 1 kcat raw_value=0.21 raw_unit=s^-1; Table 1 kcat/Km raw_value=0.357 raw_unit=s^-1 mM^-1; Table 2 Km raw_value=580 raw_unit=uM

table_label: Table 1: Kinetic parameters of SyMDH; Table 2: Comparison of Km-values of MDHs


assay_conditions_summary: pH 8; 323.15 K; cofactor NAD+

column_label: Table 1 row Malate lists kcat=0.43 s^-1 and kcat/Km=0.165 s^-1 mM^-1; Table 2 Synechocystis sp. PCC 6803 row lists Malate Km=2600 uM.

normalized_value_unit_evidence: kcat normalized_value=0.43 normalized_unit=s^-1; Km normalized_value=2.6 normalized_unit=mM; kcat/Km table value=0.165 s^-1 mM^-1; export kcat/Km=0.16538461538461538 from paired rounded kcat and Km cells

raw_value_unit_evidence: Table 1 kcat raw_value=0.43 raw_unit=s^-1; Table 1 kcat/Km raw_value=0.165 raw_unit=s^-1 mM^-1; Table 2 Km raw_value=2600 raw_unit=uM

row_label: Malate


substrate_name: oxaloacetate

assay_conditions_summary: pH 6.5; 323.15 K; cofactor NADH

column_label: Table 1 row OAA lists kcat=0.71 s^-1 and kcat/Km=59.5 s^-1 mM^-1; Table 2 Synechocystis sp. PCC 6803 row lists OAA Km=12 uM.

normalized_value_unit_evidence: kcat normalized_value=0.71 normalized_unit=s^-1; Km normalized_value=0.012 normalized_unit=mM; kcat/Km table value=59.5 s^-1 mM^-1; export kcat/Km=59.166666666666664 from paired rounded kcat and Km cells

raw_value_unit_evidence: Table 1 kcat raw_value=0.71 raw_unit=s^-1; Table 1 kcat/Km raw_value=59.5 raw_unit=s^-1 mM^-1; Table 2 Km raw_value=12 raw_unit=uM

row_label: OAA / oxaloacetate


assay_conditions_summary: pH 6.5; 318.15 K; cofactor NADH

column_label: Table 1 row NADH lists kcat=0.97 s^-1 and kcat/Km=32.3 s^-1 mM^-1; Table 2 Synechocystis sp. PCC 6803 row lists NADH Km=30 uM.

normalized_value_unit_evidence: kcat normalized_value=0.97 normalized_unit=s^-1; Km normalized_value=0.03 normalized_unit=mM; kcat/Km table value=32.3 s^-1 mM^-1; export kcat/Km=32.333333333333336 from paired rounded kcat and Km cells

raw_value_unit_evidence: Table 1 kcat raw_value=0.97 raw_unit=s^-1; Table 1 kcat/Km raw_value=32.3 raw_unit=s^-1 mM^-1; Table 2 Km raw_value=30 raw_unit=uM


organism: Streptomyces coelicolor

sequence_source: multiple

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NAD+

proof_lines: pH and temperature not specified in the publication

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


substrate_name: (S)-malate


assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADH


assay_conditions_summary: pH 8.5; cofactor NADH


organism: Methylosinus trichosporium

assay_conditions_summary: pH 9.5; 303.15 K; cofactor NAD+


assay_conditions_summary: pH 9.5; 303.15 K; cofactor NADH


organism: Methylotuvimicrobium alcaliphilum

proof_lines:
recombinant enzyme, pH 9.5, 30°C
recombinant enzyme, pH 10.0, 30°C


assay_conditions_summary: pH 10; 303.15 K; cofactor NADH


assay_conditions_summary: pH 10; 303.15 K; cofactor NAD+


organism: Kitasatospora aureofaciens

assay_conditions_summary: cofactor NAD+

proof_lines: pH and temperature not specified in the publication with NAD+


organism: Pyrobaculum islandicum

assay_conditions_summary: pH 8; cofactor NADH

column_label: Springer abstract and public author-uploaded full-text Results prose report Km for OAA and NADH as 15 uM and 86 uM respectively at 80 C and pH 8.0.

raw_value_unit_evidence: Results prose page 743 reports Km for OAA = 15 uM.

row_label: recombinant P. islandicum MDH

table_label: Results prose page 743


assay_conditions_summary: pH 8; cofactor NAD+

column_label: Public author-uploaded full-text Results prose page 743 reports Km for malate and NAD+ as 500 uM and 28 uM respectively.

raw_value_unit_evidence: Results prose page 743 reports Km for NAD+ = 28 uM.


raw_value_unit_evidence: Results prose page 743 reports Km for NADH = 86 uM.


raw_value_unit_evidence: Results prose page 743 reports Km for malate = 500 uM.


organism: Mesembryanthemum crystallinum

assay_conditions_summary: pH 6.8; 303.15 K; cofactor NAD+


assay_conditions_summary: pH 8.2; 303.15 K; cofactor NAD+


organism: Nitrosomonas europaea


assay_conditions_summary: cofactor NADH


organism: Rhodovulum steppense

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


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NAD+

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


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NADH


enzyme_display_name: UniProt P9WK13

organism: Mycobacterium tuberculosis

enzyme: UniProt P9WK13


enzyme_display_name: UniProt P61889

organism: Escherichia coli

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P61889


enzyme_display_name: UniProt Q8NN33

organism: Corynebacterium glutamicum

assay_conditions_summary: pH 6.5; 296.15 K; cofactor NADH

proof_lines:
Raw SKiD Env: Temp=20-23°C, pH=9.5
Raw SKiD Env: Temp=20-23°C, pH=6.5
Raw SKiD Env: Temp=20-23°C, pH=8

source_databases_merged: skid uniprot

enzyme: UniProt Q8NN33


assay_conditions_summary: pH 6.5; 296.15 K; cofactor NADPH

proof_lines:
Raw SKiD Env: Temp=20.23°C, pH=6.5
Raw SKiD Env: Temp=20-23°C, pH=6.5
Raw SKiD Env: Temp=20-23°C, pH=9.5


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.


assay_conditions_summary: pH 10.5; 296.15 K; cofactor NADPH


organism: Metallosphaera sedula

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

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: at pH 7.0, temperature not specified in the publication


assay_conditions_summary: pH 7; cofactor NADH


enzyme_display_name: UniProt P10584

organism: Thermus thermophilus

enzyme: UniProt P10584


assay_conditions_summary: pH 7; 303.15 K; cofactor NADH


assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH


enzyme_display_name: Malate dehydrogenase, mitochondrial

organism: Caenorhabditis elegans

substrate_name: oxaloacetate (at 24 degrees Celsius and pH 7.5)

assay_conditions_summary: pH 7.5; cofactor NADH

proof_lines: kcat is 460 sec(-1) with NADH as substrate (at 24 degrees Celsius and pH 7.5).

enzyme: Malate dehydrogenase, mitochondrial


substrate_name: NADH (at 24 degrees Celsius and pH 7.5)

substrate: NADH (at 24 degrees Celsius and pH 7.5)


proof_lines: kcat is 350 sec(-1) with NADH as substrate (at 24 degrees Celsius and pH 7.5).

substrate: oxaloacetate (at 24 degrees Celsius and pH 7.5)


organism: Leuconostoc mesenteroides subsp. mesenteroides

substrate: oxaloacetate


organism: Sulfolobus acidocaldarius


substrate_name: NADH

assay_conditions_summary: pH 5.8; 313.15 K; cofactor NADH


enzyme_display_name: UniProt A0A088E2H7

enzyme: UniProt A0A088E2H7


enzyme_display_name: UniProt A0A0U3FQH7

organism: Ignicoccus islandicus

enzyme: UniProt A0A0U3FQH7


enzyme_display_name: UniProt O08349

organism: Archaeoglobus fulgidus

assay_conditions_summary: pH 8; 338.15 K; cofactor NADH

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=65°C, pH=8

enzyme: UniProt O08349


organism: Flavobacterium frigidimaris

substrate_name: L-malate (at 40 degrees Celsius)

substrate: L-malate (at 40 degrees Celsius)


substrate_name: NAD(+) (at 40 degrees Celsius)

substrate: NAD(+) (at 40 degrees Celsius)


enzyme_display_name: UniProt P23368

organism: Homo sapiens

enzyme: UniProt P23368

substrate: (S)-malate


assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADH

substrate: NADH


organism: Pyrobaculum calidifontis


organism: Methylorubrum extorquens


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

assay_conditions_summary: cofactor NAD+


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

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


organism: Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)

substrate_name: oxaloacetate (in the presence of 2 M NaCl)

proof_lines: kcat is 197 sec(-1) with oxaloacetate as substrate (in the presence of 2 M NaCl). kcat is 69 sec(-1) with oxaloacetate as substrate (in the presence of 4 M NaCl).


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

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


organism: Rattus norvegicus

assay_conditions_summary: cofactor ATP

proof_lines:
in the presence of 0.5 mM ATP
in the presence of 1.0 mM ATP


enzyme_display_name: UniProt P26616

organism: Escherichia coli

assay_conditions_summary: pH 7.2; cofactor NAD+

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

enzyme: UniProt P26616


assay_conditions_summary: pH 7.4; 303.15 K; cofactor NAD+


substrate_name: L-Malate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R197A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

substrate: L-Malate


proof_lines: ATP NAD+


proof_lines: ATP NAD+ Arg542


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

organism: Corynebacterium glutamicum


assay_conditions_summary: pH 10.5; 293.15 K; cofactor NAD+

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


assay_conditions_summary: pH 6.5; 293.15 K; cofactor NADH


assay_conditions_summary: pH 6.5; 293.15 K; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E314A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R165A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q362N to reconstruct the assayed variant sequence.


substrate_name: NADP+

substrate: NADP+


enzyme_display_name: NAD-dependent malic enzyme 1

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: MleA; column label: Malate / Km (mM); raw value 1.56 mM; normalized value 1.56 mM.

normalized_value_unit_evidence: Km=1.56 mM as reported in Table 2.

raw_value_unit_evidence: TABLE 2. Enzymatic parameters of purified YtsJ, MleA, MalS, and MaeA; MleA row; Malate / Km (mM) = 1.56 mM.

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

enzyme: NAD-dependent malic enzyme 1

substrate: malate


substrate_name: NAD

column_label: TABLE 2. Enzymatic parameters of purified YtsJ, MleA, MalS, and MaeA; row label: MleA; column label: NAD / Km (mM); raw value 1 mM; normalized value 1 mM.

normalized_value_unit_evidence: Km=1 mM as reported in Table 2.

raw_value_unit_evidence: TABLE 2. Enzymatic parameters of purified YtsJ, MleA, MalS, and MaeA; MleA row; NAD / Km (mM) = 1 mM.

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

substrate: NAD


enzyme_display_name: NAD-dependent malic enzyme 3

column_label: TABLE 2. Enzymatic parameters of purified YtsJ, MleA, MalS, and MaeA; row label: MalS; column label: Malate / Km (mM); raw value 3.52 mM; normalized value 3.52 mM.

normalized_value_unit_evidence: Km=3.52 mM as reported in Table 2.

raw_value_unit_evidence: TABLE 2. Enzymatic parameters of purified YtsJ, MleA, MalS, and MaeA; MalS row; Malate / Km (mM) = 3.52 mM.

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

enzyme: NAD-dependent malic enzyme 3


assay_conditions_summary: pH 8

column_label: TABLE 2. Enzymatic parameters of purified YtsJ, MleA, MalS, and MaeA; row label: MalS; column label: NAD / Km (mM); raw value 5.5 mM; normalized value 5.5 mM.

normalized_value_unit_evidence: Km=5.5 mM as reported in Table 2.

raw_value_unit_evidence: TABLE 2. Enzymatic parameters of purified YtsJ, MleA, MalS, and MaeA; MalS row; NAD / Km (mM) = 5.5 mM.

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


substrate_name: NADP

column_label: TABLE 2. Enzymatic parameters of purified YtsJ, MleA, MalS, and MaeA; row label: MalS; column label: NADP / Km (mM); raw value 7.3 mM; normalized value 7.3 mM.

normalized_value_unit_evidence: Km=7.3 mM as reported in Table 2.

raw_value_unit_evidence: TABLE 2. Enzymatic parameters of purified YtsJ, MleA, MalS, and MaeA; MalS row; NADP / Km (mM) = 7.3 mM.

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

substrate: NADP


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

organism: Mycolicibacterium phlei

proof_lines:
Mycobacterium phlei
malate dehydrogenase
EC 1.1.1.37


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


substrate_name: NAD+


substrate_name: L-malate

substrate: L-malate


organism: Syntrophobacter fumaroxidans

assay_conditions_summary: pH 8.5; 333.15 K; cofactor NADH

proof_lines: Full-text kinetic excerpt recovered from Wageningen University eDepot thesis PDF (edepot.wur.nl/210623) reproducing van Kuijk & Stams (FEMS Microbiol. Lett. 1996) catalytic properties section.


assay_conditions_summary: pH 8.5; 333.15 K; cofactor NAD+

column_label: Primary-paper abstract reports NAD Km as 1.1 mM; NAD maps to NAD+ in the malate dehydrogenase reaction context.

raw_value_unit_evidence: NAD Km 1.1 mM

row_label: NAD Km statement

table_label: PubMed primary-paper abstract for PMID 8900056


column_label: Primary-paper abstract reports L-malate Km as 4 mM.

raw_value_unit_evidence: L-malate Km 4 mM

row_label: L-malate Km statement


organism: Trypanosoma cruzi

proof_lines: NAD-linked aromatic alpha-hydroxy acid dehydrogenase


assay_conditions_summary: pH 9.6; 310.15 K; cofactor NAD+


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH


organism: Triticum aestivum


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH


organism: Talaromyces emersonii

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

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

normalized_value_unit_evidence: kcat=2900 s^-1; Km=1.25 mM; current same-row quotient=2320 s^-1 mM^-1; printed efficiency=2320 s^-1 mM^-1.

raw_value_unit_evidence: Native Malate row: Km 1.25 mM; kcat 2.9 x 10^3 s^-1; printed kcat/Km 2.32 x 10^3 s^-1 mM^-1.

row_label: Native m-MDH / Malate ([NAD+] = 1 mM)

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


column_label: The literal Native m-MDH NAD+ row binds substrate, native enzyme block, fixed malate condition, Km, kcat, and printed efficiency. The current quotient differs from the two-significant-digit printed efficiency by 0.36% and is supported by the same row's exact kcat and Km cells.

raw_value_unit_evidence: Native NAD+ row: Km 0.12 mM; kcat 2.77 x 10^3 s^-1; printed kcat/Km 2.3 x 10^4 s^-1 mM^-1.

row_label: Native m-MDH / NAD+ ([malate] = 10 mM)


organism: Malus domestica


assay_conditions_summary: pH 7.8; 303.15 K; cofactor NADH


enzyme_display_name: Malate dehydrogenase 1, mitochondrial

organism: Arabidopsis thaliana

substrate_name: malate (at pH 7.5)

column_label: Primary paper Table 1 row Control, substrate Malate, column Km (mM), value 0.81 +/- 0.14.

normalized_value_unit_evidence: Malate Km paper value 0.81 mM; CatLog stores 0.8 mM, consistent as a rounded value but not exact equality.

raw_value_unit_evidence: Table 1 row Control under substrate Malate reports Km 0.81 +/- 0.14 mM.

row_label: Malate, Control

table_label: Table 1: Kinetic parameters of the enzyme activities of mMDH1 under reducing and oxidizing conditions

enzyme: Malate dehydrogenase 1, mitochondrial

substrate: malate (at pH 7.5)


assay_conditions_summary: pH 7.5; cofactor NAD+

column_label: Primary paper Table 1 row Control, substrate NAD+, column Km (mM), value 0.60 +/- 0.04.

normalized_value_unit_evidence: NAD+ Km normalized 0.60 mM = 0.6 mM; CatLog Km = 0.6 mM.

raw_value_unit_evidence: Table 1 row Control under substrate NAD+ reports Km 0.60 +/- 0.04 mM.

row_label: NAD+, Control


substrate_name: NADH (at pH 7.5)

assay_conditions_summary: pH 7.5; cofactor NADH

proof_lines: mMDH1 NADH Km

substrate: NADH (at pH 7.5)


enzyme_display_name: Malate dehydrogenase 2, mitochondrial

substrate_name: oxaloacetate

assay_conditions_summary: pH 7.4; cofactor NADH

column_label: Downloaded PDF text lines 172-180 show Table 2, with the mMDH2 OAA column reporting Km (mM) = 1.02 +/- 0.31.

normalized_value_unit_evidence: Km normalized_value=1.02 normalized_unit=mM; raw table value is already reported in mM.

raw_value_unit_evidence: Table 2 reports Km = 1.02 +/- 0.31 mM for mMDH2 with OAA.

row_label: A. thaliana recombinant mitochondrial MDH2 (Q9LKA3), OAA substrate

enzyme: Malate dehydrogenase 2, mitochondrial


column_label: Downloaded PDF text lines 172-180 show Table 2, with the mMDH2 2-KG column reporting Km (mM) = 6.97 +/- 2.98.

normalized_value_unit_evidence: Km normalized_value=6.97 normalized_unit=mM; the exported value is 7.0 mM, matching the paper central value rounded to one decimal place.

raw_value_unit_evidence: Table 2 reports Km = 6.97 +/- 2.98 mM for mMDH2 with 2-KG.

row_label: A. thaliana recombinant mitochondrial MDH2 (Q9LKA3), 2-KG substrate


substrate_name: 2-ketoglutarate (at pH 7.4)

column_label: Downloaded PDF text lines 172-180 show Table 2, with the mMDH1 2-KG column reporting Km (mM) = 40.91 +/- 3.77.

normalized_value_unit_evidence: Km normalized_value=40.91 normalized_unit=mM; the exported value is 41.0 mM, matching the paper central value rounded to one decimal place.

raw_value_unit_evidence: Table 2 reports Km = 40.91 +/- 3.77 mM for mMDH1 with 2-KG.

row_label: A. thaliana recombinant mitochondrial MDH1 (Q9ZP06), 2-KG substrate

substrate: 2-ketoglutarate (at pH 7.4)


enzyme_display_name: Malate dehydrogenase, cytoplasmic

organism: Zea mays

substrate_name: NADH for the native enzyme

assay_conditions_summary: cofactor NADH

enzyme: Malate dehydrogenase, cytoplasmic

substrate: NADH for the native enzyme


substrate_name: oxaloacetate for the native enzyme

substrate: oxaloacetate for the native enzyme


substrate_name: malate for the native enzyme

substrate: malate for the native enzyme


organism: Lactiplantibacillus plantarum

assay_conditions_summary: cofactor NAD+

substrate: NAD+


organism: Thermoplasma acidophilum

substrate: oxaloacetate


substrate_name: NADH

column_label: PubMed abstract states that at pH 7.4 the Km for oxaloacetate is 5.6 microM while for NADH a value of 11.7 microM is found.

raw_value_unit_evidence: Km raw_value=11.7 raw_unit=microM

row_label: Thermoplasma acidophilum malate dehydrogenase with NADH coenzyme

table_label: PubMed abstract PMID 3741624


enzyme_display_name: NAD-dependent malic enzyme 2

column_label: Table 2; row label MaeA; column group Malate; column label Km (mM); raw value 3.95 mM; normalized value 3.95 mM.

normalized_value_unit_evidence: Km=3.95 mM as reported in Table 2.

raw_value_unit_evidence: Table 2 MaeA row; Malate / Km (mM) = 3.95 mM.

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

table_label: Table 2. Enzymatic parameters of purified YtsJ, MleA, MalS, and MaeA

enzyme: NAD-dependent malic enzyme 2


column_label: PMID 12949160 PDF section reports Km/kcat/kcat/Km values were 1.1 mM, 112 s^-1, and 102 s^-1 mM^-1 respectively for NAD.

raw_value_unit_evidence: Prose reports Km=1.1 mM for NAD; same sentence reports kcat=112 s^-1 and kcat/Km=102 s^-1 mM^-1.

row_label: YwkA/MaeA NAD kinetic parameter prose

table_label: Section YwkA exhibits a malic enzyme activity and preferentially utilizes NAD


column_label: Table 2; row label MaeA; column group NADP; column label Km (mM); raw value 6.7 mM; normalized value 6.7 mM.

normalized_value_unit_evidence: Km=6.7 mM as reported in Table 2.

raw_value_unit_evidence: Table 2 MaeA row; NADP / Km (mM) = 6.7 mM.

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


organism: Sus scrofa

proof_lines:
L-malate
malate dehydrogenase
pig heart


organism: Taenia solium

assay_conditions_summary: pH 9.6; 295.15 K; cofactor NAD+


assay_conditions_summary: pH 8; 295.15 K; cofactor NADH

column_label: Table 2 row NADH, co-substrate oxaloacetate 0.2 mM gives KM=0.167 mM, Kcat=962.66 s^-1, Kcat/KM=5.76 x 10^6 s^-1 M^-1.

normalized_value_unit_evidence: Km normalized_value=0.167 mM; kcat paper value=962.66 s^-1; kcat/Km 5760000 s^-1 M^-1 converts to 5760 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row NADH / oxaloacetate 0.2 reports Km 0.167 mM, Kcat 962.66 s^-1, Kcat/KM 5.76 x 10^6 s^-1 M^-1.

row_label: NADH substrate row with oxaloacetate co-substrate

table_label: Experimental Parasitology PDF p.222 Table 2


assay_conditions_summary: pH 7.5; 298.15 K; buffer in Methods: 50 mM Tris–HCl pH 7; cofactor NADH


assay_conditions_summary: pH 7.5; 298.15 K; buffer in Methods: 50 mM Tris–HCl pH 7


organism: Thermus thermophilus

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH


organism: Sulfolobus acidocaldarius

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines:
NADPH
oxaloacetate
malate dehydrogenase

substrate: NADPH


organism: Aquaspirillum arcticum

assay_conditions_summary: pH 7.5; 283.15 K; cofactor NADH

proof_lines:
Aa MDH
NADH
oxaloacetate


organism: Methylorubrum extorquens


organism: Streptomyces coelicolor

substrate_name: (S)-malate

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NAD+

column_label: Kinetic constants table row L-malate gives columns Km=0.494 mM, kcat=4.71 s^-1, kcat/Km=9.53 s^-1 mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.494 mM; kcat normalized_value=4.71 s^-1; kcat/Km paper value=9.53 s^-1 mM^-1.

raw_value_unit_evidence: L-malate row reports Km 0.494 mM, kcat 4.71 s^-1, and kcat/Km 9.53 s^-1 mM^-1.

row_label: ScMDH / L-malate substrate

table_label: Biosci. Biotechnol. Biochem. PDF p.2197 kinetic constants table

substrate: (S)-malate


enzyme_display_name: Malate dehydrogenase

organism: Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)

assay_conditions_summary: pH 8; 353.15 K; cofactor NADH

enzyme: Malate dehydrogenase


organism: Klebsiella aerogenes


organism: Ascaris suum

substrate_name: L-Malate

sequence_variant_note: Mutation signature Y126F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
Ascaris suum NAD-malic enzyme
Y126F mutant
V/K(malate)


organism: Escherichia coli

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

proof_lines: mutant enzyme L310R/R346D/Q401C, pH and temperature not specified in the publication


proof_lines: mutant enzyme L310R/R346A/Q401C, pH and temperature not specified in the publication


proof_lines: mutant enzyme L310R/R346F/Q401C, pH and temperature not specified in the publication


proof_lines: mutant enzyme L310R/R346Y/Q401C, pH and temperature not specified in the publication


substrate_name: nicotinamide cytosine dinucleotide

substrate: nicotinamide cytosine dinucleotide


proof_lines: mutant enzyme L310R/R346K/Q401C, pH and temperature not specified in the publication


proof_lines: mutant enzyme L310R, pH and temperature not specified in the publication


proof_lines: mutant enzyme L310R/Q401C, pH and temperature not specified in the publication


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

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


organism: Homo sapiens

proof_lines: pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S with or without 5 mM fumarate


proof_lines: pH 7.4, 30°C, recombinant wild-type enzyme with 5 mM fumarate


assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADH

proof_lines: pH 7.4, 30°C, recombinant wild-type with 5 mM fumarate

substrate: NADH


proof_lines: pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S


proof_lines: pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S with 5 mM fumarate


organism: Triticum aestivum

substrate_name: malate


assay_conditions_summary: 303.15 K; cofactor NADH


assay_conditions_summary: 303.15 K; cofactor NAD+


organism: Clonorchis sinensis

assay_conditions_summary: pH 8.5; cofactor NADH

column_label: Table 1 column Apparent Km (mM) reports 0.007 +/- 0.0004

table_label: ScienceDirect Table 1: Apparent Km and Vmax values for the recombinant cMDH of C. sinensis


column_label: Table 1 column Apparent Km (mM) reports 0.0096 +/- 0.0009


column_label: Table 1 column Apparent Km (mM) reports 0.056 +/- 0.006


assay_conditions_summary: pH 9.6; cofactor NAD+

column_label: Table 1 column Apparent Km (mM) reports 0.094 +/- 0.013


organism: Trichomonas vaginalis


organism: Trypanosoma brucei


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH

proof_lines:
glycosomal enzyme
pH 7.5, 37°C, glycosomal enzyme
glacosomal enzyme


proof_lines:
pH 7.5, 37°C, mitochondrial enzyme
pH 7.5, 37°C, glycosomal enzyme


substrate_name: p-hydroxyphenylpyruvate

substrate: p-hydroxyphenylpyruvate


organism: Dictyostelium discoideum

assay_conditions_summary: cofactor NADH

column_label: Table 2 first K_m NADH row; column Whole cell MDH double-dagger (mM)

raw_value_unit_evidence: K_m NADH = 0.03 mM in whole-cell MDH column

row_label: first K_m NADH row

table_label: Table 2


assay_conditions_summary: cofactor NAD+

column_label: Table 2 first K_m NAD row; column Mitochondrial MDH dagger (mM)

raw_value_unit_evidence: K_m NAD = 0.10 mM in mitochondrial MDH column

row_label: first K_m NAD row


column_label: Table 2 row K_m oxaloacetate; column Whole cell MDH double-dagger (mM)

raw_value_unit_evidence: K_m oxaloacetate = 0.17 mM in whole-cell MDH column

row_label: K_m oxaloacetate


column_label: Table 2 row K_m malate; column Mitochondrial MDH dagger (mM)

raw_value_unit_evidence: K_m malate = 1.33 mM in mitochondrial MDH column

row_label: K_m malate


organism: uncultured bacterium

proof_lines: pH and temperature not specified in the publication


assay_conditions_summary: pH 7; 303.15 K; cofactor NADH


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

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


proof_lines:
reduction of oxaloacetate
decarboxylation of oxaloacetate


organism: Escherichia coli W


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


enzyme_display_name: malate dehydrogenase (decarboxylating)

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.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NAD+

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

raw_value_unit_evidence: Table 1 row D102K (+), fumarate Yes: Km,Malate 5.47+/-0.30 mM; Km,Mg 0.53+/-0.03 mM; Km,NAD 0.31+/-0.04 mM; kcat 111.09+/-1.17 s^-1. Current export mixed condition context: Table 1 row D102K (-), fumarate No: Km,Malate 7.86+/-0.25 mM; kcat 99.06+/-0.59 s^-1.

row_label: D102K (+), fumarate Yes

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

enzyme: malate dehydrogenase (decarboxylating)

substrate: L-Malate


organism: Lipomyces starkeyi


substrate_name: NAD+

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


assay_conditions_summary: pH 7.3; 301.15 K; cofactor NAD+


organism: Rhodopseudomonas palustris


assay_conditions_summary: pH 7.3; 301.15 K; cofactor NADP+


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

organism: Arabidopsis thaliana

substrate_name: Oxaloacetate

substrate: Oxaloacetate


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


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

organism: Anas platyrhynchos

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C99S to reconstruct the assayed variant sequence.


organism: Columba livia

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,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 91.1 s^-1; Km,Mal 0.0826 mM; derived kcat/Km 1102.90556900726 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,Mal 82.6 +/- 7.8 uM. Footnote a: values were obtained by fitting experimental data to Equation 4.

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

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


organism: Zea mays

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

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession: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,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 28.3 s^-1; Km,Mn 0.118 mM; derived kcat/Km 239.830508474576 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,Mn 118 +/- 22 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 D194N to reconstruct the assayed variant sequence.

column_label: Table 1, row D194N, 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 36.8 s^-1; Km,Mn 0.0015 mM; derived kcat/Km 24533.3333333333 s^-1 mM^-1 from the printed mean cells.

raw_value_unit_evidence: Table 1 row D194N: kcat 36.8 +/- 4 s^-1; Km,Mn 1.5 +/- 0.2 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 D194N/D464N to reconstruct the assayed variant sequence.

column_label: Table 1, row D(194,464)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 105 s^-1; Km,Mn 0.0077 mM; derived kcat/Km 13636.3636363636 s^-1 mM^-1 from the printed mean cells.

raw_value_unit_evidence: Table 1 row D(194,464)N: kcat 105 +/- 6 s^-1; Km,Mn 7.7 +/- 0.8 uM. Footnote a: values were obtained by fitting experimental data to Equation 4.


column_label: Table 1, row D194N, 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 36.8 s^-1; Km,NADP(app) 0.0008 mM; derived kcat/Km 46000 s^-1 mM^-1 from the printed mean cells.

raw_value_unit_evidence: Table 1 row D194N: kcat 36.8 +/- 4 s^-1; Km,NADP(app) 0.8 +/- 0.1 uM. Footnote a: values were obtained by fitting experimental data to Equation 4.


column_label: Table 1, row D(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 105 s^-1; Km,NADP(app) 0.0066 mM; derived kcat/Km 15909.0909090909 s^-1 mM^-1 from the printed mean cells.

raw_value_unit_evidence: Table 1 row D(194,464)N: kcat 105 +/- 6 s^-1; Km,NADP(app) 6.6 +/- 0.5 uM. Footnote a: values were obtained by fitting experimental data to Equation 4.


proof_lines: pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C246A


proof_lines: pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C270A


proof_lines: pH 7.0, 30°C, oxidized isozyme ZmC4-NADP-ME

proof_lines: pH 7.0, 30°C, reduced isozyme ZmC4-NADP-ME

proof_lines: pH 8.0, 30°C, oxidized isozyme ZmC4-NADP-ME


assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+


proof_lines: pH 7.0, 30°C, wild-type, treated with diamide

proof_lines: pH 7.0, 30°C, wild-type, treated with dithiothreitol


proof_lines: pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C192A


proof_lines: pH 8.0, 30°C, reduced isozyme ZmC4-NADP-ME, mutant C231A


organism: Thermococcus kodakarensis

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

assay_conditions_summary: pH 8; cofactor NADP+

column_label: Table 2 columns Km (mM) NADP+, kcat (s^-1) NADP+, and kcat/Km (mM^-1 s^-1) NADP+.

raw_value_unit_evidence: Table 2 row K228R reports NADP+ Km 0.019 +/- 0.004 mM, NADP+ kcat 2.97 +/- 0.20 s^-1, and NADP+ kcat/Km 156 mM^-1 s^-1.

table_label: Table 2: Specific activities and kinetic parameters of the wild type and mutant enzymes


assay_conditions_summary: pH 8; cofactor NAD+

column_label: Table 2 columns Km (mM) NAD+, kcat (s^-1) NAD+, and kcat/Km (mM^-1 s^-1) NAD+.

raw_value_unit_evidence: Table 2 row K228R reports NAD+ Km 1.28 +/- 0.09 mM, NAD+ kcat 3.37 +/- 0.20 s^-1, and NAD+ kcat/Km 2.64 mM^-1 s^-1.


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

column_label: Table 2 row Wild type under NAD+ columns reports Km, kcat, and kcat/Km values matching this row's enzyme/cofactor context.

normalized_value_unit_evidence: kcat normalized_value=4.69 normalized_unit=s^-1; Km normalized_value=2.06 normalized_unit=mM; kcat/Km normalized_value=2.27 normalized_unit=mM^-1 s^-1

raw_value_unit_evidence: Table 2 row Wild type; NAD+ columns: Km=2.06 mM, kcat=4.69 s^-1, kcat/Km=2.27 mM^-1 s^-1

row_label: Wild type

table_label: Table 2. Specific activities and kinetic parameters of the wild type and mutant enzymes


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

raw_value_unit_evidence: Table 2 row R221G/K228R reports NADP+ Km 0.244 +/- 0.007 mM, NADP+ kcat 6.48 +/- 0.25 s^-1, and NADP+ kcat/Km 27.5 mM^-1 s^-1.


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

raw_value_unit_evidence: Table 2 row R221G reports NAD+ Km 2.29 +/- 0.28 mM, NAD+ kcat 12.7 +/- 0.32 s^-1, and NAD+ kcat/Km 5.57 mM^-1 s^-1.


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


column_label: Table 2 row Wild type under NADP+ columns reports Km, kcat, and kcat/Km values matching this row's enzyme/cofactor context.

normalized_value_unit_evidence: kcat normalized_value=31.1 normalized_unit=s^-1; Km normalized_value=0.008 normalized_unit=mM; kcat/Km normalized_value=3760.0 normalized_unit=mM^-1 s^-1

raw_value_unit_evidence: Table 2 row Wild type; NADP+ columns: Km=0.008 mM, kcat=31.1 s^-1, kcat/Km=3760.0 mM^-1 s^-1


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

raw_value_unit_evidence: Table 2 row I310V reports NAD+ Km 6.55 +/- 0.25 mM, NAD+ kcat 37.7 +/- 1.5 s^-1, and NAD+ kcat/Km 5.76 mM^-1 s^-1.


sequence_variant_note: Mutation signature R221G/K22P/I310V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 8; 343.15 K; cofactor NADP+

proof_lines: pH 8.0, 70°C, recombinant mutant R221G/K22P8R/I310V


raw_value_unit_evidence: Table 2 row R221G reports NADP+ Km 0.025 +/- 0.007 mM, NADP+ kcat 42.6 +/- 2.9 s^-1, and NADP+ kcat/Km 1700 mM^-1 s^-1.


raw_value_unit_evidence: Table 2 row I310V reports NADP+ Km 0.021 +/- 0.003 mM, NADP+ kcat 43.4 +/- 1.8 s^-1, and NADP+ kcat/Km 2070 mM^-1 s^-1.


organism: Ascaris suum

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N434A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 25°C, mutant N434A, in presence of Mn2+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S433A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N479S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N479Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N434M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N434Q to reconstruct the assayed variant sequence.


substrate_name: L-Malate; NADP+

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

substrate: L-Malate; NADP+


organism: Clupea harengus

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

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+


substrate_name: pyruvate

substrate: pyruvate


organism: Crassula argentea


proof_lines:
activation by Mn2+
activation by Mg2+


organism: Tritrichomonas suis


proof_lines:
with NAD+ as cofactor
with NADP+ as cofactor


sequence_source: PDB:1LLQ_A (Ascaris suum NAD-dependent malic enzyme; matches UniProt P27443 chain 39-643)

assay_conditions_summary: pH 8.5; cofactor NAD+

proof_lines: pH 8.5, 25°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from PDB:1LLQ_A (Ascaris suum NAD-dependent malic enzyme; matches UniProt P27443 chain 39-643) and applied mutation signature R181Q to reconstruct the assayed variant sequence.


proof_lines: pH 8.5, 25°C, recombinant mutant R181Q in presence of 60 mM guanidinium


proof_lines: pH 8.5, 25°C, recombinant mutant R181Q, in presence of 60 mM NH4+


sequence_variant_note: Resolved canonical sequence from PDB:1LLQ_A (Ascaris suum NAD-dependent malic enzyme; matches UniProt P27443 chain 39-643) and applied mutation signature R181K to reconstruct the assayed variant sequence.


substrate_name: Unknown

proof_lines: pH 7.0, 25°C, recombinant wild-type enzyme

substrate: Unknown


organism: Oryctolagus cuniculus


proof_lines: with NAD+ as coenzyme, activation by Mn2+

proof_lines: with NADP+ as coenzyme, activation by Mn2+

proof_lines: with NAD+ as coenzyme, activation by Mg2+


proof_lines:
25°C
pH 8.4, 25°C, versus malate
pH 7.0, 25°C, versus malate


assay_conditions_summary: pH 7.4; cofactor NADPH

proof_lines: isozyme ME2, with NADPH and CO2, pH 7.4, temperature not specified in the publication

proof_lines: pH and temperature not specified in the publication, recombinant isozyme ME2, in presence of 0.5 mM Mn2+

proof_lines: isozyme ME1, with NADPH and CO2, pH 7.4, temperature not specified in the publication


proof_lines: isozyme ME2, pH 7.4, temperature not specified in the publication

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


assay_conditions_summary: pH 7.4; cofactor NADP+


organism: Trypanosoma cruzi

sequence_source: Candidate RefSeq proteins for T. cruzi NADP-dependent malic enzymes include XP_818258/XP_814409 (Tc00.1047053508647.270/Tc00.1047053505183.20; 573 aa) and XP_818259/XP_814410 (Tc00.1047053508647.280/Tc00.1047053505183.30; 565 aa). Mapping of BRENDA ME1 vs ME2 to these accessions is not explicit in the staged evidence.

proof_lines: pH and temperature not specified in the publication, recombinant isozyme ME1, in presence of 0.5 mM Mn2+


sequence_source: Candidate RefSeq proteins for T. cruzi NADP-dependent malic enzymes include XP_818258/XP_814409 (Tc00.1047053508647.270/Tc00.1047053505183.20; 573 aa) and XP_818259/XP_814410 (Tc00.1047053508647.280/Tc00.1047053505183.30; 565 aa). The staged BRENDA evidence does not identify which accession corresponds to ME1 vs ME2 for this cofactor entry.


sequence_source: Candidate RefSeq proteins for T. cruzi NADP-dependent malic enzymes include XP_818258/XP_814409 (Tc00.1047053508647.270/Tc00.1047053505183.20; 573 aa) and XP_818259/XP_814410 (Tc00.1047053508647.280/Tc00.1047053505183.30; 565 aa). Mapping of malate-kinetics ME1 vs ME2 to these accessions is unresolved.


organism: Nicotiana tabacum

assay_conditions_summary: pH 7

proof_lines:
pH 7.0, isozyme NADP-ME2
pH 7.0, isozyme NADP-ME1


proof_lines:
pH 7.3, isozyme NADP-ME1
pH 7.0, isozyme NADP-ME2


assay_conditions_summary: pH 7.3; cofactor NADP+


organism: Saccharolobus solfataricus

proof_lines:
pH 8.0, 60°C
60°C, pH 8.0, presence of Mn2+
60°C, pH 8.0, presence of Mg2+


assay_conditions_summary: pH 8; 333.15 K; cofactor NADP+


assay_conditions_summary: pH 8; 333.15 K; cofactor NAD+


organism: Glossina morsitans

assay_conditions_summary: cofactor NAD+


organism: Streptomyces coelicolor

protein_accession_database: NCBI Protein

sequence_source: NCBI Protein (GenPept) CAC05958.1; gene= SCO5261; organism=Streptomyces coelicolor A3(2)


assay_conditions_summary: pH 8


organism: Mortierella alpina

assay_conditions_summary: pH 7.5; 306.15 K; cofactor NADP+


organism: Populus trichocarpa

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADP+

proof_lines: recombinant isozyme PtNADP-ME1, pH 7.5, 30°C

proof_lines: recombinant isozyme PtNADP-ME2, pH 7.5, 30°C

proof_lines: recombinant isozyme PtNADP-ME3, pH 7.5, 30°C


organism: Cenchrus purpureus

assay_conditions_summary: cofactor NADP+


substrate_name: L-malate

substrate: L-malate


organism: Haloxylon persicum


organism: Leishmania mexicana


organism: Trichomonas vaginalis

sequence_source: GenBank AAQ01174.1 (nucleotide AF545470.1), cytosolic NADP-dependent malic enzyme; linked to PMID 15033531

assay_conditions_summary: pH 7.6; cofactor NADP+


organism: Mesembryanthemum cordifolium

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

assay_conditions_summary: pH 7.3; 303.15 K; cofactor NADP+


organism: Mangifera indica


proof_lines:
at 1.0 mM Mn2+
at 5.0 mM Mn2+


proof_lines:
activation by Mn2+
activation by Mg2+


proof_lines: in the presence of 10 mM Mn2+, at pH 7.4 and 25°C


organism: Kitasatospora aureofaciens


organism: Egeria densa


organism: Ascaris suum

substrate_name: L-Malate; NAD+

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

assay_conditions_summary: 298.15 K; cofactor NAD+

substrate: L-Malate; NAD+


organism: Lactobacillus plantarum


organism: Homo sapiens

substrate_name: NAD+; L-Malate

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

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADP+

proof_lines:
isomerized enzyme form, pH 7.4, 30°C
native enzyme form, pH 7.4, 30°C

substrate: NAD+; L-Malate


organism: Pseudomonas aeruginosa


organism: Atriplex spongiosa


organism: Brevundimonas diminuta

proof_lines:
with NAD+ as coenzyme
with NADP+ as coenzyme


organism: Digitaria sanguinalis


organism: Sulfolobus solfataricus

substrate_name: NADP+; L-Malate

substrate: NADP+; L-Malate


organism: Miscanthus sinensis


organism: Portulaca oleracea


organism: Amaranthus retroflexus


organism: Eleusine indica


organism: Sedum spectabile


organism: Zea mays

proof_lines: wild type isoform nonC4-NADP-ME, at pH 7.0 and 25°C

proof_lines: wild type isoform C4-NADP-ME, at pH 7.0 and 25°C


organism: Aspergillus niger

proof_lines:
pH 7.4, 30°C, with Mg2+
pH 7.4, 30°C, with Mn2+


organism: Hydrilla verticillata

column_label: Abstract reports Km (malate) of 0.6 mM for rHVME1.

raw_value_unit_evidence: Km raw_value=0.6 mM raw_unit=mM

row_label: rHVME1m / malate

table_label: PubMed XML abstract PMID 17638114


enzyme_display_name: NADP-dependent malic enzyme 4, chloroplastic

organism: Arabidopsis thaliana

substrate_name: NADP (at pH 7.5)

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

column_label: Table I; column label: NADP-ME4; row labels: kcat,NADP (s^-1) and Km NADP (uM); raw values 151.3 +/- 12.1 s^-1 and 10.2 +/- 1.2 uM; normalized kcat 151.3 s^-1 and Km 0.0102 mM.

normalized_value_unit_evidence: kcat=151.3 s^-1; Km=0.0102 mM after converting Table I Km NADP from uM to mM.

row_label: NADP-ME4 column / kcat,NADP and Km NADP rows

table_label: Table I. Kinetic properties of recombinant Arabidopsis NADP-ME isoforms

substrate: NADP (at pH 7.5)


substrate_name: malate (at pH 7.5)

column_label: Table I; column label: NADP-ME4; row labels: kcat,NADP (s^-1) and Km malate (mM); raw values 151.3 +/- 12.1 s^-1 and 0.23 +/- 0.025 mM; normalized kcat 151.3 s^-1 and Km 0.23 mM.

normalized_value_unit_evidence: kcat=151.3 s^-1; Km=0.23 mM as reported in Table I.

row_label: NADP-ME4 column / kcat,NADP and Km malate rows

enzyme: NADP-dependent malic enzyme 4, chloroplastic

substrate: malate (at pH 7.5)


enzyme_display_name: NADP-dependent malic enzyme 3

column_label: Table I; column label: NADP-ME3; row labels: kcat,NADP (s^-1) and Km NADP (uM); raw values 268.1 +/- 24.1 s^-1 and 6.5 +/- 0.62 uM; normalized kcat 268.1 s^-1 and Km 0.0065 mM.

normalized_value_unit_evidence: kcat=268.1 s^-1; Km=0.0065 mM after converting Table I Km NADP from uM to mM.

row_label: NADP-ME3 column / kcat,NADP and Km NADP rows

enzyme: NADP-dependent malic enzyme 3


column_label: Table I; column label: NADP-ME3; row labels: kcat,NADP (s^-1) and Km malate (mM); raw values 268.1 +/- 24.1 s^-1 and 0.83 +/- 0.09 mM; normalized kcat 268.1 s^-1 and Km 0.83 mM.

normalized_value_unit_evidence: kcat=268.1 s^-1; Km=0.83 mM as reported in Table I.

row_label: NADP-ME3 column / kcat,NADP and Km malate rows


substrate_name: pyruvate (at pH 7)

proof_lines: kcat is 268.1 sec(-1) with NADP and malate as substrates (at pH 7.5). kcat is 237 sec(-1) with pyruvate as substrate (at pH 7).

substrate: pyruvate (at pH 7)


enzyme_display_name: NADP-dependent malic enzyme 2

column_label: Table I; column label: NADP-ME2; row labels: kcat,NADP (s^-1) and Km NADP (uM); raw values 324.1 +/- 29.2 s^-1 and 72.1 +/- 7.2 uM; normalized kcat 324.1 s^-1 and Km 0.0721 mM.

normalized_value_unit_evidence: kcat=324.1 s^-1; Km=0.0721 mM after converting Table I Km NADP from uM to mM.

row_label: NADP-ME2 column / kcat,NADP and Km NADP rows

enzyme: NADP-dependent malic enzyme 2


column_label: Table I; column label: NADP-ME2; row labels: kcat,NADP (s^-1) and Km malate (mM); raw values 324.1 +/- 29.2 s^-1 and 3.33 +/- 0.37 mM; normalized kcat 324.1 s^-1 and Km 3.33 mM.

normalized_value_unit_evidence: kcat=324.1 s^-1; Km=3.33 mM as reported in Table I.

row_label: NADP-ME2 column / kcat,NADP and Km malate rows


proof_lines: kcat is 324.1 sec(-1) with NADP and malate as substrates (at pH 7.5). kcat is 75 sec(-1) with pyruvate as substrate (at pH 7).


organism: Methylosinus trichosporium

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

column_label: PDF page 8, Table 2, ME column: Pyruvate Km; kcat_pyruvate; kcat/Km_pyruvate

row_label: ME (full-length), pyruvate -> malate

table_label: PMID 31228930 Table 2. Kinetic parameters of the M. trichosporium malic enzyme and its N-terminal fragment


substrate_name: (S)-malate

assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+

column_label: PDF page 8, Table 2, ME column: Malate Km; kcat_malate; kcat/Km_malate; PDF page 7 preserves the conflicting prose Km 2.7 +/- 0.3 mM

raw_value_unit_evidence: Table 2: Km 3.0 +/- 0.3 mM; kcat 18 min^-1; kcat/Km 7 mM^-1 min^-1. Adjacent Results prose reports apparent Km 2.7 +/- 0.3 mM.

row_label: ME (full-length), malate -> pyruvate

substrate: (S)-malate


substrate_name: NADPH

column_label: PDF page 7 Results prose and PDF page 8 Table 2, NADPH Km, ME column

normalized_value_unit_evidence: NADPH Km 0.047 mM

raw_value_unit_evidence: NADPH apparent Km 47 +/- 4 uM

row_label: ME (full-length), NADPH

table_label: PMID 31228930 Results prose and Table 2

substrate: NADPH


column_label: PDF page 7 Results prose and PDF page 8 Table 2, NADP+ Km, ME column

normalized_value_unit_evidence: NADP+ Km 0.064 mM

raw_value_unit_evidence: NADP+ apparent Km 64 +/- 9 uM

row_label: ME (full-length), NADP+


organism: Rhodopseudomonas palustris

assay_conditions_summary: pH 7.2; 303.15 K; cofactor NADP+

proof_lines:
pH 7.2, 30°C, with NADP+
pH 7.2, 30°C, with NAD+


assay_conditions_summary: pH 7.2; 303.15 K; cofactor NAD+

substrate: NAD+


enzyme_display_name: UniProt P16243

enzyme: UniProt P16243


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


assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

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


organism: Leishmania major


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADP+


enzyme_display_name: UniProt Q16798

organism: Homo sapiens

assay_conditions_summary: pH 7.4; cofactor NADP+

enzyme: UniProt Q16798


enzyme_display_name: UniProt P48163

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADPH

enzyme: UniProt P48163


enzyme_display_name: UniProt P40927

organism: Columba livia

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

enzyme: UniProt P40927


organism: Thermococcus kodakarensis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R221G/K22P/I310V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 343.15 K; cofactor NADP+

proof_lines:
Thermococcus kodakarensis
malic enzyme
NADP(H)-dependent malic enzyme


column_label: Table 2, Wild type row, NADP+ columns: Km 0.008 mM; kcat 31.1 s^-1; kcat/Km 3760 mM^-1 s^-1.

raw_value_unit_evidence: Table 2; measurement Wild type; construct wild-type TkME; substrate/cofactor NADP+; condition pH 8.0; 70 degrees C; 0.5 mM NADP+; 30 mM L-malate; Km raw_value=0.008 raw_unit=mM; kcat raw_value=31.1 raw_unit=s^-1; kcat/Km raw_value=3760 raw_unit=mM^-1*s^-1.

row_label: Wild type / NADP+


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

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 'I310V', cofactor column NAD+; column 'Km (mM)' = 6.55; column 'kcat (s-1)' = 37.7; column 'kcat/Km (mM-1 s-1)' = 5.76. 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 22.7 umol min-1 mg-1 for this cofactor.

normalized_value_unit_evidence: kcat: printed Table 2 cell 37.7 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 37.7 s^(-1). Km: printed Table 2 cell 6.55 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 6.55 mM. kcat/Km: printed Table 2 cell 5.76 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 5.76 s^(-1)*mM^(-1). The exported values are kcat 37.7 s^(-1), Km 6.55 mM and kcat_over_km 5.755725190839695 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'I310V', cofactor column NAD+: Km = 6.55 mM; kcat = 37.7 s-1; printed kcat/Km = 5.76 in a column headed kcat/Km (mM-1 s-1).

row_label: Table 2, row I310V, 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+.


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 NAD+; column 'Km (mM)' = 1.28; column 'kcat (s-1)' = 3.37; column 'kcat/Km (mM-1 s-1)' = 2.64. 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 4.47 umol min-1 mg-1 for this cofactor.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.37 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 3.37 s^(-1). Km: printed Table 2 cell 1.28 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 1.28 mM. kcat/Km: printed Table 2 cell 2.64 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 2.64 s^(-1)*mM^(-1). The exported values are kcat 3.37 s^(-1), Km 1.28 mM and kcat_over_km 2.6328125 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'K228R', cofactor column NAD+: Km = 1.28 mM; kcat = 3.37 s-1; printed kcat/Km = 2.64 in a column headed kcat/Km (mM-1 s-1).

row_label: Table 2, row K228R, cofactor NAD+