organism: Mycolicibacterium smegmatis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature A124V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.8; 298.15 K; cofactor CoA


substrate_name: Unknown

source_db: brenda

verification_status: unverified

kcat_display: Not reported

km_display: Not reported

kcat_over_km_display: Not reported

source_license: CC BY 4.0

ki_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature M161V to reconstruct the assayed variant sequence.

mutation_type: substitution

substrate: Unknown

status: unverified

source: brenda


organism: Spinacia oleracea

substrate_name: H+; NADH; But-2-enoyl-[acyl-carrier protein]

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

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

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: cofactor NADH


organism: Staphylococcus aureus

substrate_name: H+; NADH; Crotonoyl-CoA

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

assay_conditions_summary: cofactor CoA

substrate: H+; NADH; Crotonoyl-CoA


organism: Streptococcus pneumoniae

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

proof_lines: 30°C, pH 6.5, in the absence of 100 mM NH4+

proof_lines: 30°C, pH 6.5, in the presence of 100 mM NH4+


enzyme_display_name: coproporphyrinogen oxidase

organism: Homo sapiens

substrate_name: mesoporphyrinogen-VI

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R401A to reconstruct the assayed variant sequence.

proof_lines: mutant R401A, monovinyl product, 37°C, pH not specified in the publication

enzyme: coproporphyrinogen oxidase

substrate: mesoporphyrinogen-VI


substrate_name: Coproporphyrinogen-III

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D400A to reconstruct the assayed variant sequence.

proof_lines: mutant D400A, total product, 37°C, pH not specified in the publication

data_origin: experimental

substrate: Coproporphyrinogen-III


enzyme_display_name: protoporphyrinogen oxidase

organism: Bacillus subtilis

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

proof_lines: pH 7.5, 22°C, recombinant wild-type enzyme

enzyme: protoporphyrinogen oxidase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V311M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y366E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y366H to reconstruct the assayed variant sequence.


organism: Yersinia pestis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature T267A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA


enzyme_display_name: acrylyl-CoA reductase (NADH)

organism: Clostridium propionicum

substrate_name: H+; Acryloyl-CoA; NADH

sequence_source: multiple

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: kcat is 4.5 sec(-1), 29 sec(-1), 2 sec(-1) and 3.5 sec(-1) for acryloyl-CoA, 3-buten-2-one, propionyl-CoA and butyryl-CoA, respectively (at pH 7.5 and 25 degrees Celsius).

enzyme: acrylyl-CoA reductase (NADH)

substrate: H+; Acryloyl-CoA; NADH


enzyme_display_name: Botryococcus squalene synthase

organism: Botryococcus braunii

enzyme: Botryococcus squalene synthase


enzyme_display_name: NADPH-dependent curcumin reductase

organism: Escherichia coli (strain K12)

source_db: uniprot

enzyme: NADPH-dependent curcumin reductase

source: uniprot


enzyme_display_name: L-galactonolactone dehydrogenase

organism: Arabidopsis thaliana

substrate_name: cytochrome c

proof_lines: wild type enzyme, in the presence of L-galactono-1,4-lactone, in 50 mM sodium phosphate (pH 8.8), at 25°C

enzyme: L-galactonolactone dehydrogenase

substrate: cytochrome c


proof_lines: in the presence of L-galactono-1,4-lactone, in 50 mM sodium phosphate (pH 8.8), at 25°C

source_databases_merged: sabio_rk brenda uniprot


enzyme_display_name: Succinate dehydrogenase [rhodoquinone] flavoprotein subunit 1, mitochondrial

organism: Ascaris suum

substrate_name: ubquinone-1 (adult complex II, succinate as cosubstrate and at 25 degrees Celsius)

proof_lines: kcat is 6000 min(-1) with fumarate as substrate (adult complex II, at 25 degrees Celsius and in anaerobic conditions).


enzyme_display_name: Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

substrate_name: ubquinone-1 (adult and larval complex II, succinate as cosubstrate and at 25 degrees Celsius)


organism: Bos taurus

enzyme: Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial


enzyme_display_name: Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial


enzyme_display_name: succinate dehydrogenase

organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E49A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

enzyme: succinate dehydrogenase


substrate_name: ubiquinone

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E29L to reconstruct the assayed variant sequence.

substrate: ubiquinone


enzyme_display_name: protoporphyrinogen IX dehydrogenase (menaquinone)

substrate_name: Menadione; Protoporphyrinogen IX

proof_lines: kcat for protoporphyrinogen IX is 17.52 min(-1) and for menadione is 16.86 min(-1).

substrate: Menadione; Protoporphyrinogen IX


enzyme_display_name: fumarate reductase (menaquinone)

organism: Mycobacterium tuberculosis

substrate_name: Reduced acceptor; Fumarate

enzyme: fumarate reductase (menaquinone)

substrate: Reduced acceptor; Fumarate


organism: Oryza sativa subsp. indica


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E29F to reconstruct the assayed variant sequence.


substrate_name: reduced plumbagin

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E101L with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant subunit SDHC mutant E101L

substrate: reduced plumbagin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E101D with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant subunit SDHC mutant E101D


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature G227L with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant subunit SDHB mutant G227L


enzyme_display_name: dihydroorotate dehydrogenase (quinone)

organism: Candida albicans

substrate_name: Decylubiquinone; L-Dihydroorotate

enzyme: dihydroorotate dehydrogenase (quinone)

substrate: Decylubiquinone; L-Dihydroorotate


organism: Enterococcus faecalis

substrate_name: Menadione; L-Dihydroorotate

substrate: Menadione; L-Dihydroorotate


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature Y366A to reconstruct the assayed variant sequence.


substrate_name: protoporphyrinogen-IX

substrate: protoporphyrinogen-IX


enzyme_display_name: bilirubin oxidase

organism: Albifimbria verrucaria

proof_lines: at pH 5.3, about 3fold higher value at pH 2.5

proof_lines: pH 6.5, recombinant enzyme from Pichia pastoris

enzyme: bilirubin oxidase


enzyme_display_name: Laccase

organism: Bacillus subtilis (strain 168)

substrate_name: SGZ

proof_lines: kcat is 16.8 sec(-1) with ABTS as substrate (PubMed:11884407). kcat is 322 sec(-1) with ABTS as substrate (PubMed:18307408). kcat is 144 sec(-1) with ABTS as substrate (PubMed:22481612). kcat is 3.7 sec(-1) with SGZ as substrate (PubMed:118

enzyme: Laccase

substrate: SGZ


enzyme_display_name: Acyl-coenzyme A oxidase acox-1.1

organism: Caenorhabditis elegans

substrate_name: asc-omega-C5-CoA (at 30 degrees Celsius, pH 7.4 and in complex with acox-1.2)

assay_conditions_summary: pH 7.4; cofactor CoA

proof_lines: kcat is 252 sec(-1) with asc-C9-CoA (at 30 degrees Celsius and pH 7.4) (PubMed:25775534). kcat is 144 sec(-1) with asc-C7-CoA (at 30 degrees Celsius, pH 7.4 and in complex with acox-1.3) (PubMed:25775534). kcat is 478 sec(-1) with asc-omega

enzyme: Acyl-coenzyme A oxidase acox-1.1


enzyme_display_name: Peroxisomal acyl-coenzyme A oxidase 1

organism: Phascolarctos cinereus

substrate_name: Unknown

enzyme: Peroxisomal acyl-coenzyme A oxidase 1


enzyme_display_name: 2-alkenal reductase

substrate_name: 4-Hydroxycinnamyl aldehyde; NADPH; H+

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 3.8 sec(-1) for trans-1,3 diphenyl-2-propenone. kcat is 4.9 sec(-1) for trans-1,4-diphenyl-2-butene-1,4-dione. kcat is 10 sec(-1) for traumatin (PubMed:26678323). kcat is 98 sec(-1) for 9,10-phenanthrenequinone. kcat is 1.9 sec(-1)

enzyme: 2-alkenal reductase

substrate: 4-Hydroxycinnamyl aldehyde; NADPH; H+


enzyme_display_name: Prostaglandin reductase 1

organism: Cavia porcellus

enzyme: Prostaglandin reductase 1


organism: Sus scrofa


enzyme_display_name: anthocyanidin reductase

substrate_name: NADP+; Cyanidin

enzyme: anthocyanidin reductase

substrate: NADP+; Cyanidin


enzyme_display_name: arogenate dehydrogenase (NADP+)

substrate_name: L-Arogenate; NADP+

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

proof_lines: pH 7.5, 25°C, with 0.05 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT2

proof_lines: pH 7.5, 25°C, with 0.07 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT2

proof_lines: pH 7.5, 25°C, with 0.1 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT2

enzyme: arogenate dehydrogenase (NADP+)

substrate: L-Arogenate; NADP+


proof_lines: pH 7.5, 25°C, with 0.05 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT1

proof_lines: pH 7.5, 25°C, with 0.07 mM arogenate as fixed substrate and NADP+ as varied substrate, TyrAAT1

proof_lines: pH 7.5, 25°C, with 0.02 mM NADP+ as fixed substrate and arogenate as varied substrate, TyrAAT1


substrate_name: fumarate

source_db: oed

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

substrate: fumarate

source: oed


substrate_name: Fumarate

sequence_variant_note: Mutation signature Q50A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: Fumarate


sequence_variant_note: Mutation signature Q50E could not be applied safely because the resolved sequence does not match the expected reference residue(s).


verification_status: verified

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

column_label: Table 2, row WT SQR, fumarate-reduction columns kcat, Kmfum, and Fum-red kcat/Km.

raw_value_unit_evidence: Table 2 WT SQR fumarate-reduction cells report kcat 2.0 s^-1, Kmfum 0.1 mM, and Fum-red kcat/Km 20 s^-1 mM^-1.

row_label: WT SQR / fumarate reduction

table_label: Table 2. Comparison of catalytic parameters for succinate-oxidase and fumarate-reductase reactions catalyzed by E. coli wild type and mutant SQR enzymes and QFR enzymes

status: verified


substrate_name: succinate

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

substrate: succinate


verification_status: corrected

column_label: JBC DOI 10.1074/jbc.M512544200 Table 2; row WT QFR; Succinate oxidation columns kcat, Km, and catalytic efficiency.

raw_value_unit_evidence: Table 2 row WT QFR Succinate oxidation: Km 0.55 mM after uM-to-mM normalization; kcat 30.0 s^-1; kcat/Km 54 s^-1 mM^-1 as printed in catalytic-efficiency column.

row_label: WT QFR

status: corrected


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +9, so it is treated as a source-provided variant sequence.


substrate_name: L-malate

substrate: L-malate


substrate_name: D-malate

substrate: D-malate


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

enzyme: Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial


enzyme_display_name: 2-methylene-furan-3-one reductase

organism: Fragaria x ananassa

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

column_label: ACS PMID 17636940 Figure 1 row FaEO / BDHMF to BHMF reports kcat 1.43 +/- 0.7 s^-1, Km 0.82 +/- 0.40 mM, and kcat/Km 1.90 +/- 0.95 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=1.43 s^-1; Km normalized_value=0.82 mM; kcat/Km normalized_value=1.90 s^-1*mM^-1; current row stores 1.7439024390243902 s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.43 +/- 0.7 raw_unit=s^-1; Km raw_value=0.82 +/- 0.40 raw_unit=mM; kcat/Km raw_value=1.90 +/- 0.95 raw_unit=mM^-1 s^-1

row_label: FaEO / BDHMF to BHMF

table_label: Figure 1

enzyme: 2-methylene-furan-3-one reductase


column_label: ACS PMID 17636940 Figure 1 row FaEO / HMPDF to HMPF reports kcat 2.69 +/- 0.50 s^-1, Km 1.04 +/- 0.26 mM, and kcat/Km 2.60 +/- 0.50 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=2.69 s^-1; Km normalized_value=1.04 mM; kcat/Km normalized_value=2.60 s^-1*mM^-1; current row stores 2.5865384615384612 s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=2.69 +/- 0.50 raw_unit=s^-1; Km raw_value=1.04 +/- 0.26 raw_unit=mM; kcat/Km raw_value=2.60 +/- 0.50 raw_unit=mM^-1 s^-1

row_label: FaEO / HMPDF to HMPF


column_label: ACS PMID 17636940 Figure 1 row FaEO / EDHMF to EHMF reports kcat 1.94 +/- 0.03 s^-1, Km 2.14 +/- 0.07 mM, and kcat/Km 0.90 +/- 0.03 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=1.94 s^-1; Km normalized_value=2.14 mM; kcat/Km normalized_value=0.90 s^-1*mM^-1; current row stores 0.9065420560747662 s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.94 +/- 0.03 raw_unit=s^-1; Km raw_value=2.14 +/- 0.07 raw_unit=mM; kcat/Km raw_value=0.90 +/- 0.03 raw_unit=mM^-1 s^-1

row_label: FaEO / EDHMF to EHMF


enzyme_display_name: L-galactonolactone dehydrogenase

column_label: Table 2. Steady-state kinetic parameters of AtGALDH row Electron acceptor: 1,4-Benzoquinone: Km 0.280 +/- 0.05 mM | kcat 108 +/- 12 s^-1 | kcat/Km 3.9 x 10^2 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.28 normalized_unit=mM; kcat normalized_value=108.0 normalized_unit=s^-1; kcat/Km ratio normalized_value=385.71428571428567 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=390 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2. Steady-state kinetic parameters of AtGALDH row Electron acceptor: 1,4-Benzoquinone: Km raw_value=0.280 +/- 0.05 raw_unit=mM; kcat raw_value=108 +/- 12 raw_unit=s^-1; kcat/Km printed raw_value=3.9 x 10^2 raw_unit=mM^-1 s^-1.

row_label: Electron acceptor: 1,4-Benzoquinone


substrate_name: Ferricytochrome c

column_label: Table 2. Steady-state kinetic parameters of AtGALDH row Electron acceptor: Cytochrome c: Km 0.034 +/- 0.002 mM | kcat 151 +/- 1 s^-1 | kcat/Km 4.4 x 10^3 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.034 normalized_unit=mM; kcat normalized_value=151.0 normalized_unit=s^-1; kcat/Km ratio normalized_value=4441.176470588235 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=4400 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2. Steady-state kinetic parameters of AtGALDH row Electron acceptor: Cytochrome c: Km raw_value=0.034 +/- 0.002 raw_unit=mM; kcat raw_value=151 +/- 1 raw_unit=s^-1; kcat/Km printed raw_value=4.4 x 10^3 raw_unit=mM^-1 s^-1.

row_label: Electron acceptor: Cytochrome c

substrate: Ferricytochrome c


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L56A with inferred residue-numbering offset -21 to reconstruct the assayed variant sequence.

column_label: Table 3. Steady-state kinetic parameters of AtGALDH variants row L56A: Km 1.7 +/- 0.05 mM | kcat 45 +/- 2 s^-1 | kcat/Km 2.6 x 10^1 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=1.7 normalized_unit=mM; kcat normalized_value=45.0 normalized_unit=s^-1; kcat/Km ratio normalized_value=26.47058823529412 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=26 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 3. Steady-state kinetic parameters of AtGALDH variants row L56A: Km raw_value=1.7 +/- 0.05 raw_unit=mM; kcat raw_value=45 +/- 2 raw_unit=s^-1; kcat/Km printed raw_value=2.6 x 10^1 raw_unit=mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L56C with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

column_label: Table 3. Steady-state kinetic parameters of AtGALDH variants row L56C: Km 0.99 +/- 0.05 mM | kcat 76 +/- 3 s^-1 | kcat/Km 7.8 x 10^1 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.99 normalized_unit=mM; kcat normalized_value=76.0 normalized_unit=s^-1; kcat/Km ratio normalized_value=76.76767676767678 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=78 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 3. Steady-state kinetic parameters of AtGALDH variants row L56C: Km raw_value=0.99 +/- 0.05 raw_unit=mM; kcat raw_value=76 +/- 3 raw_unit=s^-1; kcat/Km printed raw_value=7.8 x 10^1 raw_unit=mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L56F with inferred residue-numbering offset -21 to reconstruct the assayed variant sequence.

column_label: Table 3. Steady-state kinetic parameters of AtGALDH variants row L56F: Km 0.56 +/- 0.02 mM | kcat 126 +/- 1 s^-1 | kcat/Km 2.3 x 10^2 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.56 normalized_unit=mM; kcat normalized_value=126.0 normalized_unit=s^-1; kcat/Km ratio normalized_value=224.99999999999997 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=230 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 3. Steady-state kinetic parameters of AtGALDH variants row L56F: Km raw_value=0.56 +/- 0.02 raw_unit=mM; kcat raw_value=126 +/- 1 raw_unit=s^-1; kcat/Km printed raw_value=2.3 x 10^2 raw_unit=mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L56H with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

column_label: Table 3. Steady-state kinetic parameters of AtGALDH variants row L56H: Km 0.12 +/- 0.01 mM | kcat 32 +/- 1 s^-1 | kcat/Km 2.6 x 10^2 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.12 normalized_unit=mM; kcat normalized_value=32.0 normalized_unit=s^-1; kcat/Km ratio normalized_value=266.6666666666667 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=260 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 3. Steady-state kinetic parameters of AtGALDH variants row L56H: Km raw_value=0.12 +/- 0.01 raw_unit=mM; kcat raw_value=32 +/- 1 raw_unit=s^-1; kcat/Km printed raw_value=2.6 x 10^2 raw_unit=mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L56I with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


column_label: Table 2. Steady-state kinetic parameters of AtGALDH row Substrate: L-Galactono-1,4-lactone: Km 0.17 +/- 0.01 mM | kcat 134 +/- 5 s^-1 | kcat/Km 7.7 x 10^2 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.17 normalized_unit=mM; kcat normalized_value=134.0 normalized_unit=s^-1; kcat/Km ratio normalized_value=788.235294117647 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=770 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2. Steady-state kinetic parameters of AtGALDH row Substrate: L-Galactono-1,4-lactone: Km raw_value=0.17 +/- 0.01 raw_unit=mM; kcat raw_value=134 +/- 5 raw_unit=s^-1; kcat/Km printed raw_value=7.7 x 10^2 raw_unit=mM^-1 s^-1.

row_label: Substrate: L-Galactono-1,4-lactone


column_label: Table 2. Steady-state kinetic parameters of AtGALDH row Substrate: L-Gulono-1,4-lactone: Km 13.1 +/- 2.8 mM | kcat 4.0 +/- 0.2 s^-1 | kcat/Km 3.1 x 10^-1 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=13.1 normalized_unit=mM; kcat normalized_value=4.0 normalized_unit=s^-1; kcat/Km ratio normalized_value=0.3053435114503817 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=0.31 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2. Steady-state kinetic parameters of AtGALDH row Substrate: L-Gulono-1,4-lactone: Km raw_value=13.1 +/- 2.8 raw_unit=mM; kcat raw_value=4.0 +/- 0.2 raw_unit=s^-1; kcat/Km printed raw_value=3.1 x 10^-1 raw_unit=mM^-1 s^-1.

row_label: Substrate: L-Gulono-1,4-lactone


substrate_name: Phenazine methosulfate

column_label: Table 2. Steady-state kinetic parameters of AtGALDH row Electron acceptor: Phenazine methosulfate: Km 0.026 +/- 0.004 mM | kcat 64 +/- 3 s^-1 | kcat/Km 2.4 x 10^3 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.026 normalized_unit=mM; kcat normalized_value=64.0 normalized_unit=s^-1; kcat/Km ratio normalized_value=2461.5384615384614 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=2400 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2. Steady-state kinetic parameters of AtGALDH row Electron acceptor: Phenazine methosulfate: Km raw_value=0.026 +/- 0.004 raw_unit=mM; kcat raw_value=64 +/- 3 raw_unit=s^-1; kcat/Km printed raw_value=2.4 x 10^3 raw_unit=mM^-1 s^-1.

substrate: Phenazine methosulfate


enzyme_display_name: acyl-CoA oxidase

organism: Rattus norvegicus

substrate_name: octanoyl-CoA

assay_conditions_summary: pH 7.4; 303.15 K; cofactor FAD

enzyme: acyl-CoA oxidase

substrate: octanoyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y232F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y232G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y232S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y401F with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


organism: Streptomyces collinus

substrate_name: NADPH

assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: Abstract reports this enzyme exhibits a Km of 1.5 +/- 0.3 microM for NADPH.

raw_value_unit_evidence: Km raw_value=1.5 +/- 0.3 microM raw_unit=microM

row_label: S. collinus enoyl-CoA reductase / NADPH

table_label: PubMed XML abstract PMID 1597409

source_databases_merged: brenda uniprot

substrate: NADPH


proof_lines:
Streptomyces collinus
enoyl-CoA reductase
1-cyclohexenylcarbonyl-CoA


enzyme_display_name: 1-cyclohexenylcarbonyl-CoA reductase

enzyme: 1-cyclohexenylcarbonyl-CoA reductase


enzyme_display_name: protoporphyrinogen oxidase

organism: Myxococcus xanthus

substrate_name: protoporphyrinogen IX

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E39D to reconstruct the assayed variant sequence.

column_label: Table 2 row Glu39Asp, columns KM (uM), kcat (s^-1), and direct kcat/KM (uM^-1 s^-1)

table_label: Table 2. Kinetic parameters of wild type and mutant MxPPOX proteins

enzyme: protoporphyrinogen oxidase

substrate: protoporphyrinogen IX


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N441I to reconstruct the assayed variant sequence.

column_label: Table 2 row Asn441Ile, columns KM (uM), kcat (s^-1), and direct kcat/KM (uM^-1 s^-1)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N441Q to reconstruct the assayed variant sequence.

column_label: Table 2 row Asn441Gln, columns KM (uM), kcat (s^-1), and direct kcat/KM (uM^-1 s^-1)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S20A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

column_label: Table 2 row Ser20Ala, columns KM (uM), kcat (s^-1), and direct kcat/KM (uM^-1 s^-1)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S20T with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

column_label: Table 2 row Ser20Thr, columns KM (uM), kcat (s^-1), and direct kcat/KM (uM^-1 s^-1)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W408L to reconstruct the assayed variant sequence.

column_label: Table 2 row Trp408Leu, columns KM (uM), kcat (s^-1), and direct kcat/KM (uM^-1 s^-1)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W408Y to reconstruct the assayed variant sequence.

column_label: Table 2 row Trp408Tyr, columns KM (uM), kcat (s^-1), and direct kcat/KM (uM^-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, columns KM (uM), kcat (s^-1), and direct kcat/KM (uM^-1 s^-1)

row_label: Wild type


enzyme_display_name: succinate dehydrogenase

organism: Shewanella frigidimarina

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H365A with inferred residue-numbering offset +25 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H365A/H504A with inferred residue-numbering offset +25 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H504A with inferred residue-numbering offset +25 to reconstruct the assayed variant sequence.


enzyme_display_name: tetrahydroberberine oxidase

organism: Berberis wilsoniae

substrate_name: (S)-Tetrahydrojatrorrhizine

enzyme: tetrahydroberberine oxidase

substrate: (S)-Tetrahydrojatrorrhizine


substrate_name: (S)-canadine

assay_conditions_summary: pH 8.9; buffer 0

column_label: The substrate specificity prose reports Km and Vmax values for best substrates using homogeneous enzyme; (R,S)-canadine K=13.3 and Vmax=27.4.

raw_value_unit_evidence: Km raw_value=13.3 raw_unit=umol/l

row_label: (R,S)-canadine

table_label: Wiley PDF reader, Substrate specificity section after Table 3

substrate: (S)-canadine


enzyme_display_name: Tetrahydroberberine oxidase

substrate_name: (S)-scoulerine

column_label: Abstract reports Km values for (S)-scoulerine and (S)-norreticuline were 25 microM and 150 microM, respectively.

raw_value_unit_evidence: Km raw_value=25 microM raw_unit=microM

row_label: (S)-tetrahydroprotoberberine oxidase / (S)-scoulerine

table_label: PubMed XML abstract PMID 3402447

enzyme: Tetrahydroberberine oxidase

substrate: (S)-scoulerine


substrate_name: (S)-tetrahydropalmatine

column_label: The substrate specificity prose reports Km and Vmax values for best substrates using homogeneous enzyme; (R,S)-tetrahydropalmatine K=4.3 and Vmax=20.8.

raw_value_unit_evidence: Km raw_value=4.3 raw_unit=umol/l

row_label: (R,S)-tetrahydropalmatine

substrate: (S)-tetrahydropalmatine


enzyme_display_name: dihydroorotate dehydrogenase (quinone)

organism: Bos taurus

substrate_name: L-Dihydroorotate

substrate: L-Dihydroorotate


substrate_name: menadione

substrate: menadione


substrate_name: ubiquinone

substrate: ubiquinone


enzyme_display_name: Dihydroorotate dehydrogenase (quinone), mitochondrial

substrate_name: (S)-dihydroorotate

column_label: Table II, Dihydroorotate row, Km column: 9.2 +/- 1.3 uM.

raw_value_unit_evidence: Dihydroorotate Km 9.2 +/- 1.3 uM.

row_label: Dihydroorotate

table_label: Table II

substrate: (S)-dihydroorotate


substrate_name: decylplastoquinone (DPQ)

column_label: Table 2 row DPQ | wild type; column KM exp. [mM]

normalized_value_unit_evidence: km=1.3 mM

row_label: DPQ | wild type

table_label: Table 2

substrate: decylplastoquinone (DPQ)


substrate_name: phytoene

column_label: Table 2 row Phytoene | wild type; column KM exp. [mM]

row_label: Phytoene | wild type

substrate: phytoene


substrate_name: phytofluene

column_label: Table 2 row Phytofluene | wild type; column KM exp. [mM]

row_label: Phytofluene | wild type

substrate: phytofluene


enzyme_display_name: Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing]

organism: Mus musculus

column_label: Table I row 2,4-Decadienoyl-CoA; column Km (uM) = 6.

raw_value_unit_evidence: 6 uM

table_label: Table I, Kinetic parameters of recombinant mouse Delta2,Delta4-dienoyl-CoA reductase


enzyme: Peroxisomal 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing]


enzyme: dihydroorotate dehydrogenase (quinone)


substrate_name: Decylubiquinone

column_label: Table 2; full-length Ca row; QD Km, kcat, and QD efficiency columns; QD footnote b.

row_label: Ca (full-length CaDHODH)

substrate: Decylubiquinone


substrate_name: Fumarate

enzyme: succinate dehydrogenase

substrate: Fumarate


substrate_name: succinate

substrate: succinate


enzyme_display_name: Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2, mitochondrial

organism: Ascaris suum

substrate_name: succinate (free larvae complex II, at 25 degrees Celsius)

proof_lines:
succinate dehydrogenase
larval stage
Complex II


substrate_name: fumarate (free larvae complex II, at 25 degrees Celsius)

proof_lines:
fumarate reductase
larval form
adult form

enzyme: Succinate dehydrogenase [ubiquinone] flavoprotein subunit 2, mitochondrial


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A251C/S430C to reconstruct the assayed variant sequence.


organism: Arabidopsis thaliana

substrate_name: dihydroorotate

column_label: ScienceDirect HTML, Table 1, row AT-DHODH / DHO, column Km (uM).

raw_value_unit_evidence: Table 1 AT-DHODH / DHO Km (uM): 40+/-10 uM

row_label: AT-DHODH / DHO

table_label: Table 1

enzyme: Dihydroorotate dehydrogenase (quinone), mitochondrial

substrate: dihydroorotate


substrate_name: decylubiquinone

substrate: decylubiquinone


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -6, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R402Y with inferred residue-numbering offset +25 to reconstruct the assayed variant sequence.


enzyme_display_name: Fumarate reductase (CoM/CoB) subunit B

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

substrate_name: fumarate

column_label: Abstract states the fumarate reductase had an apparent Km of 0.20 mM for fumarate.

raw_value_unit_evidence: Km raw_value=0.20 mM raw_unit=mM

row_label: Fumarate reductase / fumarate

table_label: PMC184214 abstract

enzyme: Fumarate reductase (CoM/CoB) subunit B

substrate: fumarate


enzyme_display_name: Fumarate reductase (CoM/CoB) subunit A

enzyme: Fumarate reductase (CoM/CoB) subunit A


organism: Saccharomyces kluyveri

column_label: PMID 15196933 Table 2. Kinetic constants of the purified full-length and truncated yeast DHODH. Row group Q_D variable + DHO / DHODH SKmt; columns kcat (s^-1), kcat/Km (M^-1 s^-1), Km (uM).

normalized_value_unit_evidence: kcat=0.34 s^-1; kcat_over_km=7.555555555555556 s^-1 mM^-1; same Table 2 row explicitly reports kcat/Km=7.5 x 10^3 M^-1 s^-1; Km=0.045 mM

row_label: Q_D variable + DHO / DHODH SKmt


column_label: PMID 15196933 Table 2. Kinetic constants of the purified full-length and truncated yeast DHODH. Row group DHO variable + Q_D + DCIP / DHODH SKmt; columns kcat (s^-1), kcat/Km (M^-1 s^-1), Km (uM).

normalized_value_unit_evidence: kcat=2.5 s^-1; kcat_over_km=51.0204081632653 s^-1 mM^-1; same Table 2 row explicitly reports kcat/Km=5.1 x 10^4 M^-1 s^-1; Km=0.049 mM

row_label: DHO variable + Q_D + DCIP / DHODH SKmt


enzyme_display_name: protoporphyrinogen IX dehydrogenase (quinone)

organism: Escherichia coli

substrate_name: Protoporphyrinogen IX

substrate: Protoporphyrinogen IX


enzyme: protoporphyrinogen IX dehydrogenase (quinone)


enzyme_display_name: (S)-8-oxocitronellyl enol synthase

organism: Catharanthus roseus

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

enzyme: (S)-8-oxocitronellyl enol synthase


organism: Capsicum annuum

substrate_name: zeta-carotene

substrate: zeta-carotene


substrate_name: neurosporene

substrate: neurosporene


organism: Candida albicans (strain SC5314 / ATCC MYA-2876)

column_label: Table 2; full-length Ca row; Km QD column; footnote b.


column_label: Table 2; full-length Ca row; Km DCIP column; footnote c.


enzyme_display_name: NADPH-dependent curcumin reductase

organism: Escherichia coli (strain K12)

substrate_name: curcumin

enzyme: NADPH-dependent curcumin reductase

substrate: curcumin


enzyme_display_name: UniProt Q16698

organism: Homo sapiens

substrate_name: NADPH

source_db: skid

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

assay_conditions_summary: pH 6; 296.15 K; cofactor NADPH

source_databases_merged: skid uniprot

enzyme: UniProt Q16698

substrate: NADPH

source: skid


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: coproporphyrinogen

column_label: PubMed abstract states: The Km value for coproporphyrinogen was 0.05 microM.

raw_value_unit_evidence: Km raw_value=0.05 raw_unit=microM

row_label: Saccharomyces cerevisiae coproporphyrinogen oxidase with coproporphyrinogen substrate

table_label: PubMed abstract PMID 3516695

substrate: coproporphyrinogen


organism: Schizosaccharomyces pombe

column_label: PMID 15196933 Table 2. Kinetic constants of the purified full-length and truncated yeast DHODH. Row group Q_D variable + DHO / DHODH SPmt; columns kcat (s^-1), kcat/Km (M^-1 s^-1), Km (uM).

normalized_value_unit_evidence: kcat=1.7 s^-1; kcat_over_km=15.596330275229358 s^-1 mM^-1; same Table 2 row explicitly reports kcat/Km=1.6 x 10^4 M^-1 s^-1; Km=0.109 mM

row_label: Q_D variable + DHO / DHODH SPmt


substrate_name: L-Dihydroorotate

column_label: PMID 15196933 Table 2. Kinetic constants of the purified full-length and truncated yeast DHODH. Row group DHO variable + Q_D + DCIP / DHODH SPmt; columns kcat (s^-1), kcat/Km (M^-1 s^-1), Km (uM).

normalized_value_unit_evidence: kcat=1.0 s^-1; kcat_over_km=3.8910505836575875 s^-1 mM^-1; same Table 2 row explicitly reports kcat/Km=3.9 x 10^3 M^-1 s^-1; Km=0.257 mM

row_label: DHO variable + Q_D + DCIP / DHODH SPmt

substrate: L-Dihydroorotate


enzyme_display_name: coproporphyrinogen oxidase

organism: Gallus gallus

substrate_name: Coproporphyrinogen-III

enzyme: coproporphyrinogen oxidase

substrate: Coproporphyrinogen-III


enzyme_display_name: L-galactonolactone dehydrogenase

organism: Brassica oleracea var. botrytis

substrate_name: L-galactono-gamma-lactone

assay_conditions_summary: pH 8

column_label: Abstract states the enzyme showed a pH optimum between pH 8.0 and 8.5, with an apparent Km of 3.3 mM for L-galactono-gamma-lactone.

raw_value_unit_evidence: Km raw_value=3.3 raw_unit=mM

row_label: cauliflower L-galactono-gamma-lactone dehydrogenase with L-galactono-gamma-lactone

table_label: PubMed abstract PMID 9374475

enzyme: L-galactonolactone dehydrogenase

substrate: L-galactono-gamma-lactone


organism: Bacillus subtilis

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


enzyme_display_name: Protoporphyrinogen oxidase

substrate_name: protoporphyrinogen IX

column_label: Abstract states the Michaelis constant (Km) for protoporphyrinogen IX was 0.1 microM.

raw_value_unit_evidence: Km raw_value=0.1 raw_unit=microM

row_label: Saccharomyces cerevisiae protoporphyrinogen oxidase with protoporphyrinogen IX

table_label: PubMed abstract PMID 7798202

enzyme: Protoporphyrinogen oxidase

substrate: protoporphyrinogen IX


organism: Schistosoma mansoni

substrate_name: coenzyme Q0

proof_lines:
pH 8.2, 25°C
Raw SKiD Env: Temp=25°C, pH=8.2

source_databases_merged: brenda skid

substrate: coenzyme Q0


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

substrate_name: (S)-dihydroorotate

column_label: PMID 15196933 Table 2. Kinetic constants of the purified full-length and truncated yeast DHODH. Row group DHO variable + Q_D + DCIP / DHODH SPmt; columns Km (uM).

substrate: (S)-dihydroorotate


column_label: PMID 15196933 Table 2. Kinetic constants of the purified full-length and truncated yeast DHODH. Row group Q_D variable + DHO / DHODH SPmt; columns Km (uM).


enzyme_display_name: Peroxisomal acyl-coenzyme A oxidase 1

substrate_name: hexadecanoyl-CoA (palmitoyl-CoA)

enzyme: Peroxisomal acyl-coenzyme A oxidase 1

substrate: hexadecanoyl-CoA (palmitoyl-CoA)


enzyme_display_name: bilirubin oxidase

organism: Halobacterium volcanii

substrate_name: bilirubin

column_label: Applied and Environmental Microbiology 76(3):733-743 (2010); Results, bilirubin specificity sentence; substrate bilirubin; printed 'kcat, 29 s^-1'; printed 'Km, 236 uM'; printed 'kcat/Km value of 0.12 s^-1 uM^-1'.

normalized_value_unit_evidence: Printed kcat 29 s^-1 is already the catalog unit s^(-1); no conversion needed; catalog kcat = 29.0. Printed Km 236 uM / 1000 = 0.236 mM, matching the catalog km 0.236 mM exactly. The paper prints a ratio for this measurement, kcat/Km value of 0.12 s^-1 uM^-1 = 120.0 s^(-1)*mM^(-1), but that printed value is NOT the catalog value: the catalog kcat_over_km 122.88135593220339 s^(-1)*mM^(-1) is the exact full-precision quotient of this measurement's own printed pair, 29.0 / 0.236. The printed ratio is rounded to two significant figures, so the ratio is typed derived_same_measurement and the printed value is documented in prose only.

raw_value_unit_evidence: Results, bilirubin specificity sentence: printed kcat, 29 s^-1; printed Km, 236 uM; printed kcat/Km value of 0.12 s^-1 uM^-1. In the stored asset the micro sign is U+03BC and every exponent minus is U+2212.

row_label: Results bilirubin specificity sentence; printed kcat, 29 s^-1, printed Km, 236 uM, printed kcat/Km value of 0.12 s^-1 uM^-1

table_label: Results, bilirubin specificity sentence (no table; the paper prints this pair in prose)

enzyme: bilirubin oxidase

substrate: bilirubin


organism: Albifimbria verrucaria

substrate_name: Biliverdin

substrate: Biliverdin


organism: Bacillus pumilus

proof_lines:
Bacillus pumilus
Bilirubin oxidase
2,6-Dimethoxyphenol


organism: Phascolarctos cinereus

column_label: Abstract reports apparent Km values for AOX1 and AOX2 cDNA-expressed enzymes were 28 and 38 microM, respectively.

raw_value_unit_evidence: Km raw_value=28 microM raw_unit=microM

row_label: Koala AOX1 cDNA-expressed acyl-CoA oxidase / palmitoyl-CoA

table_label: PubMed XML abstract PMID 12758125


enzyme_display_name: Acyl-coenzyme A oxidase 4, peroxisomal

organism: Arabidopsis thaliana

substrate_name: hexanoyl-CoA

enzyme: Acyl-coenzyme A oxidase 4, peroxisomal

substrate: hexanoyl-CoA


enzyme_display_name: succinate dehydrogenase

organism: Escherichia coli

substrate_name: succinate

column_label: Table 2, row WT SQR, succinate-oxidation columns kcat, Kmsucc, and Succ-ox kcat/Km.

raw_value_unit_evidence: Table 2 WT SQR succinate-oxidation cells report kcat 110.0 s^-1, Kmsucc 0.11 mM, and Succ-ox kcat/Km 1000 s^-1 mM^-1.

row_label: WT SQR / succinate oxidation

substrate: succinate


enzyme_display_name: 15-cis-phytoene desaturase

organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)

substrate_name: NADP

enzyme: 15-cis-phytoene desaturase

substrate: NADP


enzyme_display_name: UniProt Q9NUI1

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA

enzyme: UniProt Q9NUI1


column_label: Results prose gives the docosaheptaenoyl-CoA Km under absence-of-albumin conditions; Fig. 2C is the matching substrate panel.

raw_value_unit_evidence: Results prose reports docosaheptaenoyl-CoA Km = 102 uM.

row_label: 2,4,7,10,13,16,19-docosaheptaenoyl-CoA; Fig. 2C; Km prose

table_label: PMID 11514237 results prose plus Fig. 2 kinetic analysis


enzyme_display_name: dihydroorotate dehydrogenase (quinone)

organism: Phytophthora infestans

enzyme: dihydroorotate dehydrogenase (quinone)


organism: Plasmodium falciparum

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

smiles: O=O


substrate_name: coenzyme QD

substrate: coenzyme QD


substrate_name: coenzyme Q1

substrate: coenzyme Q1


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


enzyme_display_name: Dihydroorotate dehydrogenase (quinone)

organism: Escherichia coli (strain K12)

substrate_name: dihydroorotate

column_label: Results kinetic mechanism section; E. coli DHOD; metric KM for DHO

normalized_value_unit_evidence: normalized: Km=0.0288 mM

raw_value_unit_evidence: paper text: KM for DHO 28.8 (1.5) uM

row_label: E. coli DHOD / DHO

table_label: Results kinetic mechanism prose

enzyme: Dihydroorotate dehydrogenase (quinone)

substrate: dihydroorotate


organism: Shewanella frigidimarina

substrate_name: Fumarate

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

proof_lines: about 20-fold less active than wild-type

enzyme: succinate dehydrogenase

substrate: Fumarate


proof_lines:
H505Y mutant
catalytically active mutant enzymes
markedly different pH profiles


organism: Solanum tuberosum


substrate_name: ubiquinone

substrate: ubiquinone


substrate_name: menaquinol

proof_lines:
mutant R28E/E29I, pH 8.0, 30°C
mutant R28E/E29I, pH 7.0, 30°C

substrate: menaquinol


proof_lines:
mutant R81A, pH 8.0, 30°C
mutant R81A, pH 7.0, 30°C


proof_lines:
mutant R28L/E29L, pH 8.0, 30°C
mutant R28L/E29L, pH 7.0, 30°C


proof_lines:
mutant R81E, pH 8.0, 30°C
mutant R81E, pH 7.0, 30°C


substrate_name: ferricyanide

substrate: ferricyanide


organism: Synechococcus sp.

substrate_name: Phytoene

substrate: Phytoene


substrate_name: Coproporphyrinogen-III

proof_lines: recombinant O2-dependent enzyme form HemF

substrate: Coproporphyrinogen-III


enzyme_display_name: sanguinarine reductase

organism: Eschscholzia californica

substrate_name: sanguinarine

column_label: PMID 17080644 Results prose/Fig. 12, sanguinarine reductase with sanguinarine: KM = 9.5 uM.

raw_value_unit_evidence: Results prose reports a KM for sanguinarine of 9.5 uM for sanguinarine reductase.

row_label: sanguinarine reductase / sanguinarine

table_label: Results prose and Fig. 12

enzyme: sanguinarine reductase

substrate: sanguinarine


enzyme_display_name: protoporphyrinogen oxidase

organism: Homo sapiens

substrate_name: protoporphyrinogen-IX

enzyme: protoporphyrinogen oxidase

substrate: protoporphyrinogen-IX


substrate_name: Unknown

substrate: Unknown


organism: Nicotiana tabacum

proof_lines: pH 7.4, temperature not specified in the publication, wild-type enzyme


proof_lines: pH 7.4, temperature not specified in the publication, mutant R98A


substrate_name: L-dihydroorotate

proof_lines:
mutant enzyme H185A
pH 8.0, 22°C, mutant H185A

substrate: L-dihydroorotate


substrate_name: decylubiquinone

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

substrate: decylubiquinone


proof_lines:
mutant enzyme R265A
pH 8.0, 22°C, mutant R265A


substrate_name: reduced plumbagin

proof_lines: pH 8.0, 25°C, recombinant subunit SDHC mutant D95L

substrate: reduced plumbagin


proof_lines: pH 8.0, 25°C, recombinant subunit SDHD mutant Q78L


proof_lines: pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95L


proof_lines: pH 8.0, 25°C, recombinant subunit SDHC mutant D95E


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


proof_lines: pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95E


enzyme_display_name: acyl-CoA oxidase

organism: Rattus norvegicus

enzyme: acyl-CoA oxidase


organism: Sulfolobus acidocaldarius

substrate_name: geranylgeranyl diphosphate

substrate: geranylgeranyl diphosphate


enzyme_display_name: chlorophyllide a reductase

organism: Rhodobacter capsulatus

substrate_name: 8-vinyl chlorophyllide a

enzyme: chlorophyllide a reductase

substrate: 8-vinyl chlorophyllide a


enzyme_display_name: short-chain acyl-CoA dehydrogenase

organism: Acidaminococcus fermentans

substrate_name: NADH

proof_lines: pH and temperature not specified in the publication

enzyme: short-chain acyl-CoA dehydrogenase

substrate: NADH


enzyme_display_name: Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial

substrate_name: (2S)-2-methylbutanoyl-CoA (at 32 degrees Celsius)

proof_lines: kcat is 9700 sec(-1) for the dehydrogenation of (2S)-2-methylbutanoyl-CoA (PubMed:12855692). kcat is 7600 sec(-1) for the dehydrogenation of hexanoyl-CoA (PubMed:12855692). kcat is 2900 sec(-1) for the dehydrogenation of hexanoyl-CoA (PubMe


substrate_name: hexanoyl-CoA (at 32 degrees Celsius)

enzyme: Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial

substrate: hexanoyl-CoA (at 32 degrees Celsius)


substrate_name: 2-methylpropanoyl-CoA (at 32 degrees Celsius)


organism: Megasphaera elsdenii

substrate_name: phenazine ethosulfate

proof_lines: phenazine ethosulfate as intermediate electron carrier

substrate: phenazine ethosulfate


substrate_name: phenazine methosulfate

proof_lines: phenazine methosulfate as intermediate electron carrier

substrate: phenazine methosulfate


substrate_name: protoporphyrinogen IX

proof_lines: pH 7.4, temperature not specified in the publication, mutant G169A

substrate: protoporphyrinogen IX


proof_lines: pH 7.4, temperature not specified in the publication, mutant L166N


proof_lines: pH 7.4, temperature not specified in the publication, wild-type enzyme


proof_lines: pH 7.4, temperature not specified in the publication, mutant R168S


proof_lines: pH 7.4, temperature not specified in the publication, mutant F331A


proof_lines: pH 7.4, temperature not specified in the publication, mutant V170T


proof_lines: pH 7.4, temperature not specified in the publication, mutant F331T


proof_lines: pH 7.4, temperature not specified in the publication, mutant M368Q


proof_lines: pH 7.4, temperature not specified in the publication, mutant M368K


proof_lines: pH 7.4, temperature not specified in the publication, mutant L334V


proof_lines: pH 7.4, temperature not specified in the publication, mutant R97G


enzyme_display_name: Broad-specificity linear acyl-CoA dehydrogenase FadE5

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: butanoyl-CoA

proof_lines: kcat is 1.07 sec(-1) with butanoyl-CoA as substrate. kcat is 0.80 sec(-1) with hexanoyl-CoA as substrate. kcat is 0.61 sec(-1) with octadecanoyl-CoA as substrate.

substrate: butanoyl-CoA


substrate_name: hexanoyl-CoA

enzyme: Broad-specificity linear acyl-CoA dehydrogenase FadE5

substrate: hexanoyl-CoA


substrate_name: octadecanoyl-CoA

substrate: octadecanoyl-CoA


proof_lines: kcat is 30000 sec(-1) for the dehydrogenation of (2S)-2-methylbutanoyl-CoA (PubMed:12855692). kcat is 1800 sec(-1) for the dehydrogenation of hexanoyl-CoA (PubMed:12855692). kcat is 8500 sec(-1) for the dehydrogenation of hexanoyl-CoA (PubM


substrate_name: butyryl-CoA

proof_lines: recombinant enzyme, O2 as electron acceptor

substrate: butyryl-CoA


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

proof_lines: kcat is 0.53 sec(-1) with butanoyl-CoA as substrate.


enzyme_display_name: (R)-benzylsuccinyl-CoA dehydrogenase

organism: Thauera aromatica

assay_conditions_summary: pH 6.4; cofactor CoA

proof_lines: forward reaction, recombinant enzyme, pH 6.4, 50°C

enzyme: (R)-benzylsuccinyl-CoA dehydrogenase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E368D with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


substrate_name: octanoyl-CoA

substrate: octanoyl-CoA


enzyme_display_name: red chlorophyll catabolite reductase

organism: Hordeum vulgare

substrate_name: Red chlorophyll catabolite; H+; Reduced ferredoxin

enzyme: red chlorophyll catabolite reductase


enzyme_display_name: butyryl-CoA dehydrogenase

organism: Bos taurus

substrate_name: Butanoyl-CoA; Acceptor

enzyme: butyryl-CoA dehydrogenase

substrate: Butanoyl-CoA; Acceptor


organism: Clostridium kluyveri

substrate_name: N-acetyl-S-acryloyl-cysteamine

substrate: N-acetyl-S-acryloyl-cysteamine


substrate_name: Propanoyl-CoA; FAD

assay_conditions_summary: cofactor FAD

substrate: Propanoyl-CoA; FAD


substrate_name: Butanoyl-CoA; FAD

substrate: Butanoyl-CoA; FAD


enzyme_display_name: 4,4'-diapophytoene desaturase

organism: Staphylococcus aureus

substrate_name: 4,4'-Diapophytoene; FAD

enzyme: 4,4'-diapophytoene desaturase

substrate: 4,4'-Diapophytoene; FAD


substrate_name: 2-methylbutanoyl-CoA (at pH 8.0 and 37 degrees Celsius)

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: kcat is 9700 sec(-1) for the dehydrogenation of (2S)-2-methylbutanoyl-CoA (PubMed:12855692). kcat is 7600 sec(-1) for the dehydrogenation of hexanoyl-CoA (PubMed:12855692). kcat is 2900 sec(-1) for the dehydrogenation of hexanoyl-CoA (PubMe


substrate_name: Unknown

substrate: Unknown


substrate_name: cyclopentanecarboxyl-CoA

substrate: cyclopentanecarboxyl-CoA


enzyme_display_name: UniProt P26440

substrate_name: isovaleryl-CoA

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt P26440

substrate: isovaleryl-CoA


enzyme_display_name: UniProt Q39QF5

organism: Geobacter metallireducens

enzyme: UniProt Q39QF5


assay_conditions_summary: pH 6.4; 323.15 K; cofactor CoA


enzyme_display_name: glutaryl-CoA dehydrogenase (ETF)

substrate_name: glutaryl-CoA

assay_conditions_summary: pH 7.8; 303.15 K; cofactor CoA

enzyme: glutaryl-CoA dehydrogenase (ETF)

substrate: glutaryl-CoA


enzyme_display_name: medium-chain acyl-CoA dehydrogenase

organism: Aspergillus niger

substrate_name: decanoyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: medium-chain acyl-CoA dehydrogenase

substrate: decanoyl-CoA


substrate_name: Hexanoyl-CoA

assay_conditions_summary: pH 8; 305.15 K; cofactor CoA

column_label: Table VII, row 'Hexanoyl-CoA / SCAD', columns Vmax, Vmax/Km, Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

row_label: Hexanoyl-CoA / SCAD

table_label: Table VII

substrate: Hexanoyl-CoA


substrate_name: Phenazine methosulfate

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines:
PMS
electron acceptor
acyl-CoA dehydrogenases

substrate: Phenazine methosulfate


substrate_name: pentanoyl-CoA

column_label: Table VII, row 'Valeryl-CoA / SCAD', columns Vmax, Vmax/Km, Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

row_label: Valeryl-CoA / SCAD

substrate: pentanoyl-CoA


substrate_name: butanoyl-CoA

column_label: Table VII, row 'Butyryl-CoA / SCAD', columns Vmax, Vmax/Km, Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

row_label: Butyryl-CoA / SCAD

substrate: butanoyl-CoA


enzyme_display_name: Short-chain specific acyl-CoA dehydrogenase, mitochondrial

column_label: Table VII, row 'Butyryl-CoA / SCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

raw_value_unit_evidence: Km 10.7 uM


column_label: Table VII, row 'Valeryl-CoA / SCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

raw_value_unit_evidence: Km 32.9 uM

enzyme: Short-chain specific acyl-CoA dehydrogenase, mitochondrial


substrate_name: hexanoyl-CoA

column_label: Table VII, row 'Hexanoyl-CoA / SCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

raw_value_unit_evidence: Km 285 uM

substrate: hexanoyl-CoA


organism: Clostridioides difficile

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


substrate_name: crotonyl-CoA

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH

substrate: crotonyl-CoA


substrate_name: NADH

substrate: NADH


substrate_name: acryloyl-CoA

substrate: acryloyl-CoA


substrate_name: ethyl vinyl ketone

substrate: ethyl vinyl ketone


substrate_name: acrolein

substrate: acrolein


substrate_name: propanoyl-CoA

substrate: propanoyl-CoA


assay_conditions_summary: pH 7.1; cofactor CoA


substrate_name: heptanoyl-CoA

substrate: heptanoyl-CoA


substrate_name: octanoyl-CoA

substrate: octanoyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L222I/A383T with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


substrate_name: isobutyryl-CoA

substrate: isobutyryl-CoA


substrate_name: hexanoyl-CoA (at 32 degrees Celsius)

substrate: hexanoyl-CoA (at 32 degrees Celsius)


substrate_name: octadecanoyl-CoA

substrate: octadecanoyl-CoA


organism: Homo sapiens

proof_lines: kcat is 2.0 sec(-1) for the oxidation of 2-methylpropanoyl-CoA (PubMed:12359132). kcat is 4.1 sec(-1) for the oxidation of (2S)-methylbutanoyl-CoA (PubMed:12359132). kcat is 0.83 sec(-1) for the oxidation of n-propionyl-CoA (PubMed:12359132


substrate_name: n-propionyl-CoA

substrate: n-propionyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K304E to reconstruct the assayed variant sequence.


substrate_name: hexadecanoyl-CoA

substrate: hexadecanoyl-CoA


substrate_name: tetradecanoyl-CoA

substrate: tetradecanoyl-CoA


substrate_name: decanoyl-CoA

substrate: decanoyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


substrate_name: dodecanoyl-CoA

substrate: dodecanoyl-CoA


substrate_name: hexanoyl-CoA

substrate: hexanoyl-CoA


substrate_name: pentanoyl-CoA

column_label: Table 1, row Pentanoyl-CoA, column Apparent Km (microM), value 15.0

raw_value_unit_evidence: 15.0 microM

row_label: Pentanoyl-CoA

table_label: Table 1. Reactivity of butyryl-CoA dehydrogenase with straight and branched-chain acyl-CoA thioesters

substrate: pentanoyl-CoA


column_label: Table 1, row Hexanoyl-CoA, column Apparent Km (microM), value 53

raw_value_unit_evidence: 53 microM

row_label: Hexanoyl-CoA


substrate_name: cyclohexanecarboxyl-CoA

column_label: Table 2, row Cyclohexanecarboxylic acyl-CoA, column Apparent Km (microM), value 82

raw_value_unit_evidence: 82 microM

row_label: Cyclohexanecarboxylic acyl-CoA

table_label: Table 2. Reactivity of butyryl-CoA dehydrogenase with alicyclic acyl-CoA thioesters

substrate: cyclohexanecarboxyl-CoA


proof_lines:
branched-chain acyl thioesters
straight-chain acyl thioesters
alicyclic acyl thioesters


column_label: Table 1, row 2-Methylpropionyl-CoA, column Apparent Km (microM), value 161

raw_value_unit_evidence: 161 microM


substrate_name: Hexanoyl-CoA

column_label: Table VIII row Hexanoyl-CoA; SCAD columns Km, Vmax, and Vmax/Km.

raw_value_unit_evidence: Table VIII row Hexanoyl-CoA, SCAD columns: Km 33.9 uM; Vmax 16.5 s^-1; Vmax/Km 0.49 s^-1*uM^-1.

table_label: Table VIII, Kinetic parameters of SCAD, MCAD, and IVD for various acyl-CoAs

substrate: Hexanoyl-CoA


column_label: Table VIII row Valeryl-CoA; SCAD columns Km, Vmax, and Vmax/Km.

raw_value_unit_evidence: Table VIII row Valeryl-CoA, SCAD columns: Km 33.3 uM; Vmax 40 s^-1; Vmax/Km 1.2 s^-1*uM^-1.

row_label: Valeryl-CoA


column_label: Table VIII row Butyryl-CoA; SCAD columns Km, Vmax, and Vmax/Km.

raw_value_unit_evidence: Table VIII row Butyryl-CoA, SCAD columns: Km 12.9 uM; Vmax 20.7 s^-1; Vmax/Km 1.6 s^-1*uM^-1.

row_label: Butyryl-CoA


substrate_name: glutaryl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A433V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; cofactor CoA

proof_lines: mutant A433V, pH 7.6, 25°C, electron acceptor is electron transfer flavoprotein

substrate: glutaryl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T429M to reconstruct the assayed variant sequence.

proof_lines: mutant T429M, pH 7.6, 25°C, electron acceptor is electron transfer flavoprotein


organism: Syntrophus aciditrophicus

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: Km less than 0.005 mM, at pH 7.0 and 30°C


enzyme_display_name: UniProt Q92947

assay_conditions_summary: pH 8.5; 298.15 K; cofactor CoA

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.8
Raw SKiD Env: Temp=-----, pH=7.6
Raw SKiD Env: Temp=-----, pH=8.5

enzyme: UniProt Q92947


assay_conditions_summary: pH 6.5; 298.15 K; cofactor CoA


substrate_name: glutaryl-CoA (at pH 6.5)

assay_conditions_summary: pH 7.8; 298.15 K; cofactor CoA

substrate: glutaryl-CoA (at pH 6.5)


organism: Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15)

substrate_name: CHeneCoA

substrate: CHeneCoA


enzyme_display_name: cyclohexane-1-carbonyl-CoA dehydrogenase (electron-transfer flavoprotein)

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA


enzyme_display_name: isovaleryl-CoA dehydrogenase

substrate_name: 3-Methylbutanoyl-CoA; FAD

column_label: Table VIII row Isovaleryl-CoA; IVD Vmax column; FAD preincubation described in the table method.

raw_value_unit_evidence: Table VIII row Isovaleryl-CoA, IVD Vmax column: 8.9 s^-1; table method states enzyme was preincubated with FAD before PMS/DCIP assay.

row_label: Isovaleryl-CoA

enzyme: isovaleryl-CoA dehydrogenase

substrate: 3-Methylbutanoyl-CoA; FAD


substrate_name: FAD; 3-Methylbutanoyl-CoA

substrate: FAD; 3-Methylbutanoyl-CoA


organism: Rattus norvegicus


organism: Solanum tuberosum

column_label: Isovaleryl-CoA is the primary table preferred substrate for IVD and corresponds to 3-methylbutanoyl-CoA; the required Vmax has an exact primary Vmax cell.

raw_value_unit_evidence: Table I row IVD / Isovaleryl-CoA: Km 1.3 uM; Vmax 1.25 umol/min; kcat per tetramer 0.98 s^-1.

row_label: IVD; Isovaleryl-CoA

table_label: Table I: Kinetic parameters of IVD and 2MBCD with preferred substrates


substrate_name: 2-methylbutanoyl-CoA (at pH 8.0 and 37 degrees Celsius)


substrate_name: Isovaleryl-CoA

column_label: The Km-only expected row has an exact primary table Km cell for IVD / Isovaleryl-CoA.

raw_value_unit_evidence: Table I row IVD / Isovaleryl-CoA: Km 1.3 uM.

substrate: Isovaleryl-CoA


substrate_name: (2S)-2-methylbutanoyl-CoA (at 32 degrees Celsius)


substrate_name: hexanoyl-CoA (at 32 degrees Celsius)

substrate: hexanoyl-CoA (at 32 degrees Celsius)


substrate_name: 2-methylpropanoyl-CoA (at 32 degrees Celsius)


substrate_name: octanoyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y375K with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; buffer 50 mM potassium phosphate; cofactor CoA

proof_lines: mutant enzyme Y375K, in 50 mM potassium phosphate buffer, pH 7.6

substrate: octanoyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y375A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y375A, in 50 mM potassium phosphate buffer, pH 7.6


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y375F with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y375F, in 50 mM potassium phosphate buffer, pH 7.6


enzyme_display_name: glutaryl-CoA dehydrogenase

substrate_name: Glutaryl-CoA; Acceptor

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

enzyme: glutaryl-CoA dehydrogenase

substrate: Glutaryl-CoA; Acceptor


organism: Sus scrofa


enzyme_display_name: medium-chain-acyl-CoA dehydrogenase

substrate_name: Octanoyl-CoA; Acceptor

enzyme: medium-chain-acyl-CoA dehydrogenase

substrate: Octanoyl-CoA; Acceptor


substrate_name: Glutaramyl-CoA; Acceptor

substrate: Glutaramyl-CoA; Acceptor


substrate_name: Unknown

substrate: Unknown


substrate_name: electron transfer flavoprotein

substrate: electron transfer flavoprotein


enzyme_display_name: long-chain-acyl-CoA dehydrogenase

substrate_name: Lauroyl-CoA; Acceptor

enzyme: long-chain-acyl-CoA dehydrogenase

substrate: Lauroyl-CoA; Acceptor


substrate_name: Lauroyl-CoA; FAD

assay_conditions_summary: cofactor FAD

substrate: Lauroyl-CoA; FAD


substrate_name: FAD; Palmitoyl-CoA

substrate: FAD; Palmitoyl-CoA


assay_conditions_summary: 305.15 K; cofactor CoA

proof_lines: per enzyme tetramer, recombinant enzyme, 32°C

proof_lines: kcat is 1.77 sec(-1) per tetramer for 2-methylbutanoyl-CoA.


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


substrate_name: glutaryl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V400M with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; cofactor CoA

proof_lines: recombinant mutant V400M with ETF, pH 7.8, temperature not specified in the publication

substrate: glutaryl-CoA


substrate_name: isovaleryl-CoA

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -8, so it is treated as a source-provided variant sequence.

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines:
rat SBCAD
rat IVD
rat IBD

substrate: isovaleryl-CoA


substrate_name: Glutaramyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R94G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 298.15 K; cofactor CoA

substrate: Glutaramyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R94Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S98A to reconstruct the assayed variant sequence.


column_label: Table I; wild type GCD; glutaramyl-CoA rows for Km, kcat, and kcat/Km

normalized_value_unit_evidence: not accepted: normalized paper Km=0.0016 mM and kcat/Km=1400 s^-1 mM^-1; export expects Km=0.002 mM and kcat/Km=1100 s^-1 mM^-1

row_label: Wild type GCD / glutaramyl-CoA

table_label: JBC PMID 11024031 Table I


substrate_name: Hexanoyl-CoA

substrate: Hexanoyl-CoA


column_label: Table I; wild type GCD; hexanoyl-CoA rows for Km, kcat, and kcat/Km

normalized_value_unit_evidence: not accepted: normalized paper Km=0.0368 mM, kcat=18.5 s^-1, kcat/Km=500 s^-1 mM^-1; export expects Km=0.037 mM

row_label: Wild type GCD / hexanoyl-CoA


substrate_name: Furylpropionyl-CoA

substrate: Furylpropionyl-CoA


substrate_name: Octanoyl-CoA

substrate: Octanoyl-CoA


substrate_name: decanoyl-CoA

substrate: decanoyl-CoA


assay_conditions_summary: pH 8; 305.15 K; cofactor CoA

column_label: Table VIII row Isovaleryl-CoA; IVD columns Km, Vmax, and Vmax/Km.

raw_value_unit_evidence: Table VIII row Isovaleryl-CoA, IVD columns: Km 14 uM; Vmax 8.9 s^-1; Vmax/Km 0.64 s^-1*uM^-1.


column_label: Table VIII row Hexanoyl-CoA; IVD columns Km, Vmax, and Vmax/Km.

raw_value_unit_evidence: Table VIII row Hexanoyl-CoA, IVD columns: Km 20 uM; Vmax 2.1 s^-1; Vmax/Km 0.105 s^-1*uM^-1.


substrate_name: pentanoyl-CoA

column_label: Table VIII row Valeryl-CoA; IVD columns Km, Vmax, and Vmax/Km.

raw_value_unit_evidence: Table VIII row Valeryl-CoA, IVD columns: Km 16.7 uM; Vmax 3.3 s^-1; Vmax/Km 0.2 s^-1*uM^-1.

substrate: pentanoyl-CoA


column_label: Table VIII row Butyryl-CoA; IVD columns Km, Vmax, and Vmax/Km.

raw_value_unit_evidence: Table VIII row Butyryl-CoA, IVD columns: Km 25 uM; Vmax 2.2 s^-1; Vmax/Km 0.09 s^-1*uM^-1.


column_label: Table VII, row 'Butyryl-CoA / MCAD', columns Vmax, Vmax/Km, Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

row_label: Butyryl-CoA / MCAD


column_label: Table VII, row 'Hexanoyl-CoA / MCAD', columns Vmax, Vmax/Km, Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

row_label: Hexanoyl-CoA / MCAD


column_label: Table VII, row 'Octanoyl-CoA / MCAD', columns Vmax, Vmax/Km, Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

row_label: Octanoyl-CoA / MCAD


substrate_name: Phenazine methosulfate

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

column_label: Table VIII, row 'MCAD, fixed substrate C8-CoA, varied intermediary electron acceptor PMS', columns Vmax, Vmax/Km, Km. Table VIII varies ETF/PMS electron acceptor with fixed acyl-CoA substrate; not a substrate row for Phenazine methosulfate.

table_label: Table VIII

substrate: Phenazine methosulfate


column_label: Table VII, row 'Decanoyl-CoA / MCAD', columns Vmax, Vmax/Km, Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

row_label: Decanoyl-CoA / MCAD


column_label: Table VII, row 'Valeryl-CoA / MCAD', columns Vmax, Vmax/Km, Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

row_label: Valeryl-CoA / MCAD


enzyme_display_name: Long-chain specific acyl-CoA dehydrogenase, mitochondrial

substrate_name: octanoyl-CoA (at 32 degrees Celsius and pH 8.0)

assay_conditions_summary: pH 8; cofactor CoA

column_label: Table VII, row 'Octanoyl-CoA / MCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

raw_value_unit_evidence: Km 4 uM


substrate_name: decanoyl-CoA (at 32 degrees Celsius and pH 8.0)

column_label: Table VII, row 'Decanoyl-CoA / MCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

raw_value_unit_evidence: Km 5.4 uM

enzyme: Long-chain specific acyl-CoA dehydrogenase, mitochondrial


substrate_name: dodecanoyl-CoA (at 32 degrees Celsius and pH 8.0)

column_label: Table VII, row 'Lauroyl-CoA / MCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

raw_value_unit_evidence: Km 5.7 uM

row_label: Lauroyl-CoA / MCAD


substrate_name: tetradecanoyl-CoA (at 32 degrees Celsius and pH 8.0)


enzyme_display_name: short-chain acyl-CoA dehydrogenase

substrate_name: Propanoyl-CoA

enzyme: short-chain acyl-CoA dehydrogenase

substrate: Propanoyl-CoA


organism: Clostridium acetobutylicum

substrate_name: butyryl-CoA

assay_conditions_summary: cofactor CoA

proof_lines:
Clostridium acetobutylicum
butyryl-CoA dehydrogenase
P262

substrate: butyryl-CoA


assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

column_label: ACS Table 1 row 4-nitrobutyryl-CoA, columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1).

table_label: Table 1: Steady-State Kinetic Constants of Human Glutaryl-CoA Dehydrogenase with Glutaryl-CoA and Alternate Substrates


column_label: ACS Table 1 row 5-hexenoyl-CoA, columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1).


column_label: ACS Table 1 row glutaramyl-CoA, columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1).

row_label: glutaramyl-CoA


column_label: ACS Table 1 row hexanoyl-CoA, columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1).

row_label: hexanoyl-CoA


substrate_name: Methylglutaryl-CoA

column_label: ACS Table 1 row methyl-glutaryl-CoA, columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1).

row_label: methyl-glutaryl-CoA

substrate: Methylglutaryl-CoA


column_label: ACS Table 1 row pentanoyl-CoA, columns kcat (s^-1), Km (uM), and kcat/Km (uM^-1 s^-1).

row_label: pentanoyl-CoA


enzyme_display_name: Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

assay_conditions_summary: buffer ferricenium assay; cofactor CoA

column_label: Table 1 MCADH Km [uM] row C4 column = 175.

normalized_value_unit_evidence: Km=0.175 mM converted from 175 uM.

raw_value_unit_evidence: MCADH Km row C4 column reports 175 uM.

row_label: MCADH / Km row / C4

table_label: Table 1 / Kinetic Parameter of Wildtype and Mutant Human MCADH and of Wildtype Human LCADH


substrate_name: hexanoyl-CoA

column_label: Table 1 MCADH Km [uM] row C6 column = 15.

normalized_value_unit_evidence: Km=0.015 mM converted from 15 uM.

raw_value_unit_evidence: MCADH Km row C6 column reports 15 uM.

row_label: MCADH / Km row / C6

enzyme: Medium-chain specific acyl-CoA dehydrogenase, mitochondrial

substrate: hexanoyl-CoA


substrate_name: octanoyl-CoA

column_label: Table 1 MCADH Km [uM] row C8 column = 3.4.

normalized_value_unit_evidence: Km=0.0034 mM converted from 3.4 uM.

raw_value_unit_evidence: MCADH Km row C8 column reports 3.4 uM.

row_label: MCADH / Km row / C8

substrate: octanoyl-CoA


column_label: Table 1 MCADH Km [uM] row C10 column = 2.5.

normalized_value_unit_evidence: Km=0.0025 mM converted from 2.5 uM.

raw_value_unit_evidence: MCADH Km row C10 column reports 2.5 uM.

row_label: MCADH / Km row / C10


substrate_name: dodecanoyl-CoA

column_label: Table 1 MCADH Km [uM] row C12 column = 2.5.

raw_value_unit_evidence: MCADH Km row C12 column reports 2.5 uM.

row_label: MCADH / Km row / C12

substrate: dodecanoyl-CoA


substrate_name: tetradecanoyl-CoA

column_label: Table 1 MCADH Km [uM] row C14 column = 2.3.

normalized_value_unit_evidence: Km=0.0023 mM converted from 2.3 uM.

raw_value_unit_evidence: MCADH Km row C14 column reports 2.3 uM.

row_label: MCADH / Km row / C14

substrate: tetradecanoyl-CoA


substrate_name: hexadecanoyl-CoA

column_label: Table 1 MCADH Km [uM] row C16 column = 1.6.

normalized_value_unit_evidence: Km=0.0016 mM converted from 1.6 uM.

raw_value_unit_evidence: MCADH Km row C16 column reports 1.6 uM.

row_label: MCADH / Km row / C16

substrate: hexadecanoyl-CoA


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


column_label: Table 1 LCADH Km [uM] row C8 column = 8.

normalized_value_unit_evidence: Km=0.008 mM converted from 8 uM.

raw_value_unit_evidence: LCADH Km row C8 column reports 8 uM.

row_label: LCADH / Km row / C8


enzyme_display_name: red chlorophyll catabolite reductase

substrate_name: red chlorophyll catabolite

column_label: Abstract reports RCC reductase exhibited saturation kinetics for RCC, with an apparent Michaelis constant of 0.6 mM.

raw_value_unit_evidence: Km raw_value=0.6 mM raw_unit=mM

row_label: Hordeum vulgare RCC reductase / red chlorophyll catabolite

table_label: PubMed XML abstract PMID 12223836

substrate: red chlorophyll catabolite


enzyme_display_name: Complex I assembly factor ACAD9, mitochondrial


enzyme: Complex I assembly factor ACAD9, mitochondrial


assay_conditions_summary: pH 7.6; 298.15 K; buffer this table | conditions 50 mM phosphate; cofactor CoA

column_label: Table 2 (Comparative Steady-State Kinetic Parameters for the Human Liver and Pig Kidney MCAD-Catalyzed Dehydrogenase and Oxidase Reactions), Dehydrogenase Reaction section, substrate row DPCoA; column 'pig kidney MCAD Km (uM)' = 61.0; column 'pig kidney MCAD kcat (s^-1)' = 0.61; the two human liver MCAD columns of the same row read 42.6 and 4.6 and belong to the other enzyme form; the table carries no ratio column.

normalized_value_unit_evidence: Km: printed Table 2 cell 61.0 uM; 61.0 / 1000 = 0.061 mM; the exported value is 0.061 mM. kcat: printed Table 2 cell 0.61 s^-1; the cell is already in s^-1 and no unit conversion applies; the exported value is 0.61 s^(-1). kcat/Km: Table 2 carries no ratio column, so the exported ratio is typed as the same-measurement quotient of that one row's own two printed cells: 0.61 / 0.061 = 10.0 s^-1 mM^-1, which is the exported value 10.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Dehydrogenase Reaction section, substrate row DPCoA, pig kidney MCAD columns: Km = 61.0 uM; kcat = 0.61 s^-1. The table prints four numeric columns and none of them is a catalytic-efficiency column.

row_label: Table 2, Dehydrogenase Reaction section, substrate row DPCoA, pig kidney MCAD column pair

table_label: Table 2: Comparative Steady-State Kinetic Parameters for the Human Liver and Pig Kidney MCAD-Catalyzed "Dehydrogenase" and "Oxidase" Reactions (Biochemistry 1995, volume 34, number 45, pages 14942-14953)


substrate_name: Furylpropionyl-CoA


substrate_name: butanoyl-CoA

column_label: Table 2 (Comparative Steady-State Kinetic Parameters for the Human Liver and Pig Kidney MCAD-Catalyzed Dehydrogenase and Oxidase Reactions), Dehydrogenase Reaction section, substrate row C4-CoA; column 'pig kidney MCAD Km (uM)' = 264; column 'pig kidney MCAD kcat (s^-1)' = 6.2; the two human liver MCAD columns of the same row read 450 and 11.5 and belong to the other enzyme form; the table carries no ratio column.

normalized_value_unit_evidence: Km: printed Table 2 cell 264 uM; 264 / 1000 = 0.264 mM; the exported value is 0.264 mM. kcat: printed Table 2 cell 6.2 s^-1; the cell is already in s^-1 and no unit conversion applies; the exported value is 6.2 s^(-1). kcat/Km: Table 2 carries no ratio column, so the exported ratio is typed as the same-measurement quotient of that one row's own two printed cells: 6.2 / 0.264 = 23.484848484848484 s^-1 mM^-1, which is the exported value 23.484848484848484 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Dehydrogenase Reaction section, substrate row C4-CoA, pig kidney MCAD columns: Km = 264 uM; kcat = 6.2 s^-1. The table prints four numeric columns and none of them is a catalytic-efficiency column.

row_label: Table 2, Dehydrogenase Reaction section, substrate row C4-CoA, pig kidney MCAD column pair

substrate: butanoyl-CoA


substrate_name: Hexanoyl-CoA


substrate_name: Octanoyl-CoA


substrate_name: decanoyl-CoA


assay_conditions_summary: pH 6.8; cofactor CoA

proof_lines:
Geobacter metallireducens
cyclohexanoyl-CoA
CHeneCoA

enzyme: cyclohexane-1-carbonyl-CoA dehydrogenase (electron-transfer flavoprotein)


substrate_name: Lauroyl-CoA

column_label: Table VII, row 'Lauroyl-CoA / LCAD', columns Vmax, Vmax/Km, Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

row_label: Lauroyl-CoA / LCAD

substrate: Lauroyl-CoA


column_label: Table VII, row 'Octanoyl-CoA / LCAD', columns Vmax, Vmax/Km, Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

row_label: Octanoyl-CoA / LCAD


substrate_name: Oleoyl-CoA

column_label: Table VII, row 'Oleoyl-CoA / LCAD', columns Vmax, Vmax/Km, Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

row_label: Oleoyl-CoA / LCAD

substrate: Oleoyl-CoA


substrate_name: Palmitoyl-CoA

column_label: Table VII, row 'Palmitoyl-CoA / LCAD', columns Vmax, Vmax/Km, Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

row_label: Palmitoyl-CoA / LCAD

substrate: Palmitoyl-CoA


substrate_name: Phenazine methosulfate


substrate_name: stearoyl-CoA

column_label: Table VII, row 'Stearoyl-CoA / LCAD', columns Vmax, Vmax/Km, Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

row_label: Stearoyl-CoA / LCAD

substrate: stearoyl-CoA


column_label: Table VII, row 'Decanoyl-CoA / LCAD', columns Vmax, Vmax/Km, Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

row_label: Decanoyl-CoA / LCAD

substrate: decanoyl-CoA


substrate_name: myristoyl-CoA

column_label: Table VII, row 'Myristoyl-CoA / LCAD', columns Vmax, Vmax/Km, Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

row_label: Myristoyl-CoA / LCAD

substrate: myristoyl-CoA


substrate_name: octanoyl-CoA (at 32 degrees Celsius and pH 8.0)

column_label: Table VII, row 'Octanoyl-CoA / LCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

raw_value_unit_evidence: Km 123 uM


assay_conditions_summary: pH 7; cofactor CoA


assay_conditions_summary: pH 8; 305.15 K; cofactor FAD


organism: Megasphaera elsdenii

substrate_name: butyryl-CoA


substrate_name: hexanoyl-CoA

assay_conditions_summary: pH 7.6; buffer 100 mM KPi pH 7; cofactor CoA

column_label: Table 1; wildtype human LCADH block; C6 Km [uM]g = 29

normalized_value_unit_evidence: normalized: Km=0.029 mM

raw_value_unit_evidence: Table 1 wildtype human LCADH row for C6/hexanoyl-CoA: Km [uM]g = 29

row_label: LCADH C6

table_label: Table 1


substrate_name: octanoyl-CoA

column_label: Table 1; wildtype human LCADH block; C8 Km [uM]g = 8

normalized_value_unit_evidence: normalized: Km=0.008 mM

raw_value_unit_evidence: Table 1 wildtype human LCADH row for C8/octanoyl-CoA: Km [uM]g = 8

row_label: LCADH C8


column_label: Table 1; wildtype human LCADH block; C10 Km [uM]g = 10

normalized_value_unit_evidence: normalized: Km=0.010 mM

raw_value_unit_evidence: Table 1 wildtype human LCADH row for C10/decanoyl-CoA: Km [uM]g = 10

row_label: LCADH C10


substrate_name: dodecanoyl-CoA

column_label: Table 1; wildtype human LCADH block; C12 Km [uM]g = 7

normalized_value_unit_evidence: normalized: Km=0.007 mM

raw_value_unit_evidence: Table 1 wildtype human LCADH row for C12/dodecanoyl-CoA: Km [uM]g = 7

row_label: LCADH C12


substrate_name: tetradecanoyl-CoA

column_label: Table 1; wildtype human LCADH block; C14 Km [uM]g = 10

raw_value_unit_evidence: Table 1 wildtype human LCADH row for C14/tetradecanoyl-CoA: Km [uM]g = 10

row_label: LCADH C14


substrate_name: hexadecanoyl-CoA

column_label: Table 1; wildtype human LCADH block; C16 Km [uM]g = 14

normalized_value_unit_evidence: normalized: Km=0.014 mM

raw_value_unit_evidence: Table 1 wildtype human LCADH row for C16/hexadecanoyl-CoA: Km [uM]g = 14

row_label: LCADH C16


substrate_name: octadecanoyl-CoA

column_label: Table 1; wildtype human LCADH block; C18 Km [uM]g = 8

raw_value_unit_evidence: Table 1 wildtype human LCADH row for C18/octadecanoyl-CoA: Km [uM]g = 8

row_label: LCADH C18

substrate: octadecanoyl-CoA


substrate_name: glutaryl-CoA

substrate: glutaryl-CoA


organism: Cavia porcellus

substrate_name: isovaleryl-CoA

proof_lines:
pig liver isovaleryl-CoA dehydrogenase
rat liver mitochondria
tritium release assays

substrate: isovaleryl-CoA


substrate_name: hexadecanoyl-CoA (at 32 degrees Celsius and pH 8.0)


substrate_name: octadecanoyl-CoA (at 32 degrees Celsius and pH 8.0)


substrate_name: (9Z)-octadecenoyl-CoA (at 32 degrees Celsius and pH 8.0)


substrate_name: butanoyl-CoA

column_label: Table VII, row 'Butyryl-CoA / MCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

raw_value_unit_evidence: Km 135 uM

row_label: Butyryl-CoA / MCAD


substrate_name: pentanoyl-CoA

column_label: Table VII, row 'Valeryl-CoA / MCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

raw_value_unit_evidence: Km 39.6 uM

row_label: Valeryl-CoA / MCAD

substrate: pentanoyl-CoA


column_label: Table VII, row 'Hexanoyl-CoA / MCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

raw_value_unit_evidence: Km 9.4 uM

row_label: Hexanoyl-CoA / MCAD

substrate: hexanoyl-CoA


column_label: Table VII, row 'Octanoyl-CoA / MCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

raw_value_unit_evidence: Km 4 uM

row_label: Octanoyl-CoA / MCAD

substrate: octanoyl-CoA


substrate_name: decanoyl-CoA

column_label: Table VII, row 'Decanoyl-CoA / MCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

raw_value_unit_evidence: Km 5.4 uM

row_label: Decanoyl-CoA / MCAD


column_label: Table VII, row 'Lauroyl-CoA / MCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

raw_value_unit_evidence: Km 5.7 uM

row_label: Lauroyl-CoA / MCAD

substrate: dodecanoyl-CoA


assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


column_label: Table 1 LCADH Km [uM] row C12 column = 7.

normalized_value_unit_evidence: Km=0.007 mM converted from 7 uM.

raw_value_unit_evidence: LCADH Km row C12 column reports 7 uM.

row_label: LCADH / Km row / C12


column_label: Table 1 LCADH Km [uM] row C14 column = 10.

normalized_value_unit_evidence: Km=0.01 mM converted from 10 uM.

raw_value_unit_evidence: LCADH Km row C14 column reports 10 uM.

row_label: LCADH / Km row / C14

substrate: tetradecanoyl-CoA


column_label: Table 1 LCADH Km [uM] row C16 column = 14.

normalized_value_unit_evidence: Km=0.014 mM converted from 14 uM.

raw_value_unit_evidence: LCADH Km row C16 column reports 14 uM.

row_label: LCADH / Km row / C16

substrate: hexadecanoyl-CoA


column_label: Table 1 LCADH Km [uM] row C18 column = 8.

raw_value_unit_evidence: LCADH Km row C18 column reports 8 uM.

row_label: LCADH / Km row / C18


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


enzyme_display_name: Very long-chain acyl-CoA dehydrogenase, mitochondrial


column_label: Table VIII row Valeryl-CoA; MCAD columns Km, Vmax, and Vmax/Km.

raw_value_unit_evidence: Table VIII row Valeryl-CoA, MCAD columns: Km 58.3 uM; Vmax 14.1 s^-1; Vmax/Km 0.25 s^-1*uM^-1.

row_label: Valeryl-CoA


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


substrate_name: isobutyryl-CoA

mutation_signature: deletion mutant M10

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

mutation_type: deletion

substrate: isobutyryl-CoA


substrate: butanoyl-CoA


substrate_name: decanoyl-CoA (at 32 degrees Celsius and pH 8.0)

proof_lines:
acyl-CoA dehydrogenases
decanoyl-CoA
medium-chain specificity


substrate_name: dodecanoyl-CoA (at 32 degrees Celsius and pH 8.0)

column_label: Table VII, row 'Lauroyl-CoA / LCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

raw_value_unit_evidence: Km 9 uM

row_label: Lauroyl-CoA / LCAD


substrate_name: tetradecanoyl-CoA (at 32 degrees Celsius and pH 8.0)


column_label: Table VII, row 'Stearoyl-CoA / LCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

row_label: Stearoyl-CoA / LCAD

substrate: octadecanoyl-CoA (at 32 degrees Celsius and pH 8.0)


column_label: Table VII, row 'Palmitoyl-CoA / LCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

raw_value_unit_evidence: Km 2.5 uM

row_label: Palmitoyl-CoA / LCAD

substrate: hexadecanoyl-CoA (at 32 degrees Celsius and pH 8.0)


column_label: Table VII, row 'Oleoyl-CoA / LCAD', columns Km. Table VII page 1320; Table VII assay: purified holoenzymes, 100 uM FAD, Vmax in s^-1, Km in uM, Vmax/Km in s^-1 uM^-1.

raw_value_unit_evidence: Km 6.5 uM

row_label: Oleoyl-CoA / LCAD

substrate: (9Z)-octadecenoyl-CoA (at 32 degrees Celsius and pH 8.0)


substrate_name: Acceptor; Hexanoyl-CoA

substrate: Acceptor; Hexanoyl-CoA


enzyme_display_name: long-chain acyl-CoA dehydrogenase

enzyme: long-chain acyl-CoA dehydrogenase

substrate: decanoyl-CoA


substrate_name: dodecanoyl-CoA


substrate_name: octanoyl-CoA


substrate_name: stearoyl-CoA

substrate: stearoyl-CoA


substrate_name: tetradecanoyl-CoA


substrate_name: hexanoyl-CoA


substrate_name: hexadecanoyl-CoA

proof_lines:
VLCAD
palmitoyl-CoA
charge transfer complex

enzyme: Very long-chain acyl-CoA dehydrogenase, mitochondrial


substrate_name: valeryl-CoA

substrate: valeryl-CoA


substrate_name: electron transfer flavoprotein

substrate: electron transfer flavoprotein


substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


substrate_name: butyryl-CoA

substrate: butyryl-CoA


substrate_name: tetradecenoyl-CoA

substrate: tetradecenoyl-CoA


substrate_name: decanoyl-CoA


substrate: octanoyl-CoA


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


substrate: hexanoyl-CoA


substrate_name: electron-transfer flavoprotein

substrate: electron-transfer flavoprotein


enzyme_display_name: acyl-CoA oxidase

enzyme: acyl-CoA oxidase


substrate_name: linoleoyl-CoA

substrate: linoleoyl-CoA


substrate_name: myristoyl-CoA

substrate: myristoyl-CoA


substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


substrate_name: lauroyl-CoA

substrate: lauroyl-CoA


substrate_name: octanoyl-CoA


enzyme_display_name: protoporphyrinogen oxidase

substrate_name: protoporphyrinogen IX

enzyme: protoporphyrinogen oxidase

substrate: protoporphyrinogen IX


proof_lines:
mutant enzyme R59K, at pH 7.4 and 25°C
recombinant mutant R59K, pH 8.2


substrate_name: FAD

assay_conditions_summary: cofactor FAD

substrate: FAD


enzyme_display_name: medium-chain acyl-CoA dehydrogenase


enzyme_display_name: succinate dehydrogenase

organism: Saccharomyces cerevisiae

enzyme: succinate dehydrogenase


mutation_type: truncation


substrate_name: propionyl-CoA

substrate: propionyl-CoA


substrate_name: heptanoyl-CoA

substrate: heptanoyl-CoA


substrate_name: hexanoyl-CoA


substrate_name: pentanoyl-CoA

substrate: pentanoyl-CoA


organism: Escherichia coli

substrate_name: succinate

proof_lines: mutant K228R, cosubstrate ubiquinone, pH 7.9, 30°C

substrate: succinate


proof_lines: mutant K228L, cosubstrate ubiquinone, pH 7.9, 30°C


substrate_name: fumarate

proof_lines: mutant K228R, cosubstrate menaquinone, pH 7.0, 30°C

substrate: fumarate


proof_lines: wild-type, cosubstrate menaquinone, pH 7.9, 30°C

proof_lines: wild-type, cosubstrate ubiquinone, pH 7.9, 30°C


proof_lines: wild-type, cosubstrate menaquinone, pH 7.0, 30°C


substrate_name: menaquinone

substrate: menaquinone


organism: Candida tropicalis

substrate_name: decanoyl-CoA

substrate: decanoyl-CoA


substrate_name: arachidoyl-CoA

substrate: arachidoyl-CoA


substrate_name: stearoyl-CoA

substrate: stearoyl-CoA


substrate: octanoyl-CoA


substrate_name: Unknown

substrate: Unknown


substrate_name: tetradecanoyl-CoA

enzyme: medium-chain acyl-CoA dehydrogenase

substrate: tetradecanoyl-CoA


substrate: hexanoyl-CoA


substrate_name: dodecanoyl-CoA

substrate: dodecanoyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


substrate_name: octanoyl-CoA


substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


assay_conditions_summary: pH 6; 295.15 K; cofactor CoA

proof_lines: recombinant His-tagged truncated wild-type enzyme, pH 6.0, 22°C


substrate_name: NADPH

substrate: NADPH


proof_lines: recombinant His-tagged mutant E227A, pH 6.0, 22°C


proof_lines: recombinant His-tagged mutant E154A, pH 6.0, 22°C


substrate_name: electron-transfer flavoprotein

proof_lines: saturating dodecanoyl-CoA, measured with ETF from pig kidney

substrate: electron-transfer flavoprotein


substrate_name: hexanoyl-CoA


enzyme_display_name: dihydroorotate dehydrogenase (quinone)

organism: Toxoplasma gondii

enzyme: dihydroorotate dehydrogenase (quinone)


substrate_name: (S)-dihydroorotate

substrate: (S)-dihydroorotate


substrate_name: decylubiquinone

substrate: decylubiquinone


organism: Thermus thermophilus

substrate_name: menadione

proof_lines: with 2,6-dichlorophenolindophenol, pH 7.6, 30°C

substrate: menadione


substrate_name: oxidized 2,6-dichlorophenolindophenol

substrate: oxidized 2,6-dichlorophenolindophenol


substrate_name: duroquinone

substrate: duroquinone


substrate_name: succinate

substrate: succinate


enzyme_display_name: glutaryl-CoA dehydrogenase (ETF)

substrate_name: glutaryl-CoA

assay_conditions_summary: pH 6.5; cofactor CoA

proof_lines:
oxidase activity
at pH 6.5
at pH 7.6

enzyme: glutaryl-CoA dehydrogenase (ETF)

substrate: glutaryl-CoA


proof_lines:
oxidase activity
recombinant protein


substrate_name: pentanoyl-CoA

substrate: pentanoyl-CoA


substrate_name: butyryl-CoA

substrate: butyryl-CoA


substrate: octanoyl-CoA


substrate: hexanoyl-CoA


assay_conditions_summary: pH 7; 305.15 K; cofactor CoA


proof_lines:
32°C, pH 7.0, R147W mutant
R147W mutant


proof_lines:
32°C, pH 7.0, G185S mutant
G185S mutant


enzyme_display_name: UniProt A1B5Y0

organism: Paracoccus denitrificans

substrate_name: succinyl-CoA

enzyme: UniProt A1B5Y0

substrate: succinyl-CoA


assay_conditions_summary: pH 7.6; 298.15 K; cofactor CoA

proof_lines: mutant A421V, pH 7.6, 25°C, electron acceptor is electron transfer flavoprotein


proof_lines: mutant A421T, pH 7.6, 25°C, electron acceptor is electron transfer flavoprotein


substrate_name: electron transfer flavoprotein

proof_lines: recombinant wild-type enzyme, pH 7.6, 25°C

substrate: electron transfer flavoprotein


organism: Plasmodium falciparum

substrate_name: L-dihydroorotate

mutation_signature: N-terminally truncated protein

proof_lines: pH 8.0, 25°C, cosubstrate Q0, N-terminally truncated protein

proof_lines: pH 8.0, 25°C, cosubstrate vitamin K3, N-terminally truncated protein

proof_lines: pH 8.0, 25°C, cosubstrate Q4, N-terminally truncated protein

substrate: L-dihydroorotate


proof_lines: pH 8.0, 25°C, cosubstrate L-dihydroorotate, N-terminally truncated protein


substrate_name: Unknown

proof_lines: pH 8.0, 25°C, varied substrate L-dihydroorotate, N-terminally truncated protein

proof_lines: pH 8.0, 25°C, varied substrate QD, N-terminally truncated protein

substrate: Unknown


organism: Arabidopsis thaliana

substrate_name: dihydroorotate

substrate: dihydroorotate


mutation_signature: Δ1


organism: Bacillus cereus

substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


organism: Homo sapiens

substrate_name: indolepropionyl-CoA

substrate: indolepropionyl-CoA


substrate_name: decanoyl-CoA

substrate: decanoyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


substrate_name: hexanoyl-CoA


substrate_name: ferrocenium hexafluorophosphate

proof_lines:
substrate indolepropionyl-CoA
substrate octanoyl-CoA

substrate: ferrocenium hexafluorophosphate


enzyme_display_name: dihydroorotate dehydrogenase (fumarate)

organism: Bacillus subtilis

substrate_name: L-Dihydroorotate; Fumarate

enzyme: dihydroorotate dehydrogenase (fumarate)

substrate: L-Dihydroorotate; Fumarate


organism: Enterococcus faecalis

substrate_name: L-Dihydroorotate; Nitroblue tetrazolium

substrate: L-Dihydroorotate; Nitroblue tetrazolium


organism: Lactococcus lactis subsp. lactis

substrate_name: NADH; O2; H+

assay_conditions_summary: cofactor NADH

substrate: NADH; O2; H+


substrate_name: NADH; H+; O2

substrate: NADH; H+; O2


substrate_name: CoQ

substrate: CoQ


organism: Saccharolobus solfataricus


substrate_name: ferricyanide

substrate: ferricyanide


organism: Crithidia fasciculata

assay_conditions_summary: pH 6


proof_lines: at saturating concentration of dihydroorotate


organism: Helicobacter pylori


substrate_name: S-dihydroorotate

substrate: S-dihydroorotate


substrate_name: orotate

substrate: orotate


enzyme_display_name: 2-amino-4-deoxychorismate dehydrogenase

organism: Streptomyces globisporus

assay_conditions_summary: cofactor FMN

proof_lines: kcat is 15 sec(-1) for ADIC. kcat is 17 sec(-1) for FMN.

enzyme: 2-amino-4-deoxychorismate dehydrogenase


substrate_name: FMN

substrate: FMN


organism: Leishmania major

proof_lines:
in the presence of 0.125 mM fumarate
in the presence of 0.25 mM fumarate
in the presence of 0.5 mM fumarate


substrate_name: fumarate

proof_lines: in the presence of 0.02 mM dihydroorotate

proof_lines: in the presence of 0.03 mM dihydroorotate

proof_lines: in the presence of 0.04 mM dihydroorotate

substrate: fumarate


enzyme_display_name: Dihydroorotate dehydrogenase A (fumarate)

organism: Lactococcus lactis subsp. cremoris (strain MG1363)

substrate_name: Unknown

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

substrate: Unknown


enzyme_display_name: Dihydroorotate dehydrogenase (fumarate)

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: (S)-dihydroorotate (at pH 7.5)

column_label: Metric label K m; row DHO varied substrate with 2 mM fumarate; value 8.4 +/- 0.2 microM

row_label: DHO-fumarate substrate pair; with 2 mM fumarate and varied DHO

table_label: PDF page 5; article page 88; Alternate electron acceptors prose

enzyme: Dihydroorotate dehydrogenase (fumarate)

substrate: (S)-dihydroorotate (at pH 7.5)


substrate_name: fumarate (at pH 7.5)

column_label: Metric label K m; row fumarate varied substrate with 1 mM DHO; value 45 +/- 3 microM

raw_value_unit_evidence: K m = 45 +/- 3 microM

row_label: DHO-fumarate substrate pair; with 1 mM DHO and varied fumarate

substrate: fumarate (at pH 7.5)


enzyme_display_name: (2S)-methylsuccinyl-CoA dehydrogenase

organism: Cereibacter sphaeroides

assay_conditions_summary: cofactor CoA

enzyme: (2S)-methylsuccinyl-CoA dehydrogenase


enzyme_display_name: crotonobetainyl-CoA reductase

organism: Escherichia coli

enzyme: crotonobetainyl-CoA reductase


substrate_name: L-Dihydroorotate; Hexacyanoferrate(III)

substrate: L-Dihydroorotate; Hexacyanoferrate(III)


substrate_name: L-Dihydroorotate; O2

substrate: L-Dihydroorotate; O2


enzyme_display_name: UniProt Q8Y5F1

organism: Listeria monocytogenes

smiles: OO

enzyme: UniProt Q8Y5F1


organism: Paracoccus denitrificans

substrate_name: succinyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D3JV03 and applied mutation signature A282V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; buffer pH 7; cofactor CoA

column_label: Table 2. Michaelis-Menten kinetic parameters for the wildtype and mutant RsMCD with either (2S)-methylsuccinyl-CoA or succinyl-CoA as substrate; row RsMCD A282V / Succinyl-CoA; columns kcat s^-1 raw 0.30 +/- 0.04, Km(app) uM raw 57 +/- 20, kcat/Km s^-1 M^-1 raw 5.3 x 10^3 +/- 2.0 x 10^3; normalized kcat 0.3 s^-1, Km 0.057 mM, same-row kcat/Km 5.263157894736842 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.3 normalized_unit=s^-1; Km normalized_value=0.057 normalized_unit=mM from 57 +/- 20 uM / 1000; kcat/Km normalized_value=5.263157894736842 normalized_unit=s^-1*mM^-1 from same-row kcat/Km; printed efficiency=5.3 x 10^3 +/- 2.0 x 10^3 s^-1 M^-1

raw_value_unit_evidence: kcat raw_value=0.30 +/- 0.04 raw_unit=s^-1; Km raw_value=57 +/- 20 raw_unit=uM; kcat/Km raw_value=5.3 x 10^3 +/- 2.0 x 10^3 raw_unit=s^-1 M^-1

row_label: RsMCD A282V / Succinyl-CoA

substrate: succinyl-CoA


column_label: Table 2. Michaelis-Menten kinetic parameters for the wildtype and mutant RsMCD with either (2S)-methylsuccinyl-CoA or succinyl-CoA as substrate; row RsMCD WT / Succinyl-CoA; columns kcat s^-1 raw 0.32 +/- 0.06, Km(app) uM raw 141 +/- 52, kcat/Km s^-1 M^-1 raw 2.3 x 10^3 +/- 0.9 x 10^3; normalized kcat 0.32 s^-1, Km 0.141 mM, same-row kcat/Km 2.269503546099291 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.32 normalized_unit=s^-1; Km normalized_value=0.141 normalized_unit=mM from 141 +/- 52 uM / 1000; kcat/Km normalized_value=2.269503546099291 normalized_unit=s^-1*mM^-1 from same-row kcat/Km; printed efficiency=2.3 x 10^3 +/- 0.9 x 10^3 s^-1 M^-1

raw_value_unit_evidence: kcat raw_value=0.32 +/- 0.06 raw_unit=s^-1; Km raw_value=141 +/- 52 raw_unit=uM; kcat/Km raw_value=2.3 x 10^3 +/- 0.9 x 10^3 raw_unit=s^-1 M^-1

row_label: RsMCD WT / Succinyl-CoA