sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H251A to reconstruct the assayed variant sequence.

column_label: Scientific Reports DOI 10.1038/s41598-017-18475-8 Table 1; row H251A; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

raw_value_unit_evidence: Table 1 row H251A: Km 1.69 mM; kcat 8.8 s^-1; kcat/Km 5.2 s^-1 mM^-1.


enzyme_display_name: maleylacetate reductase

organism: Sphingobium chlorophenolicum

source_db: oed

verification_status: verified

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K140A to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7; 296.15 K; cofactor NADPH

column_label: Scientific Reports DOI 10.1038/s41598-017-18475-8 Table 1; row K140A; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

raw_value_unit_evidence: Table 1 row K140A: Km 0.36 mM; kcat 0.9 s^-1; kcat/Km 2.5 s^-1 mM^-1.

table_label: Table 1. Apparent kinetic parameters for recombinant PcpE and its mutants

data_origin: experimental

enzyme: maleylacetate reductase

status: verified

source: oed


verification_status: corrected

mutation_signature: Unknown

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

column_label: Scientific Reports DOI 10.1038/s41598-017-18475-8 Table 1; row Wild type; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

raw_value_unit_evidence: Table 1 row Wild type: Km 0.09 mM; kcat 1.2 s^-1; kcat/Km 13.3 s^-1 mM^-1.

row_label: Wild type

status: corrected


substrate_name: NADH

assay_conditions_summary: pH 7; 296.15 K; cofactor NADH

column_label: Scientific Reports DOI 10.1038/s41598-017-18475-8 Table 2; row 2-CMA / NADH; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

raw_value_unit_evidence: Table 2 row 2-CMA / NADH: Km 0.13 mM; kcat 143.7 s^-1; kcat/Km 1105.4 s^-1 mM^-1.

row_label: 2-CMA / NADH

table_label: Table 2. Apparent kinetic parameters for recombinant PcpE

substrate: NADH


substrate_name: NADPH

column_label: Scientific Reports DOI 10.1038/s41598-017-18475-8 Table 2; row 2-CMA / NADPH; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

raw_value_unit_evidence: Table 2 row 2-CMA / NADPH: Km 0.67 mM; kcat 29.7 s^-1; kcat/Km 44.3 s^-1 mM^-1.

row_label: 2-CMA / NADPH

substrate: NADPH


enzyme_display_name: 2-enoate reductase

organism: Achromobacter sp.

verification_status: unverified

kcat_over_km_origin: calculated

enzyme: 2-enoate reductase

status: unverified


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH


organism: Bacillus subtilis

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH


organism: Klebsiella pneumoniae

column_label: ScienceDirect Table 3 row KpnER / NADH has columns Km (uM)=11.57 +/- 1.81, kcat (min^-1)=16.45 +/- 0.44, kcat/Km (mM^-1 min^-1)=1421.48.

normalized_value_unit_evidence: kcat 0.2741666666666666666666666667 s^-1 from explicit paper cell; kcat_over_km 23.69133333333333333333333333 s^-1 mM^-1 from explicit paper cell; km 0.01157 mM from explicit paper cell

row_label: KpnER; NADH

table_label: Table 3. Kinetic parameters of YqjM and KpnER towards citraconate.


column_label: ScienceDirect Table 3 row KpnER / NADPH has columns Km (uM)=2.59 +/- 1.10, kcat (min^-1)=16.70 +/- 0.43, kcat/Km (mM^-1 min^-1)=6458.89.

normalized_value_unit_evidence: kcat 0.2783333333333333333333333333 s^-1 from explicit paper cell; kcat_over_km 107.6481666666666666666666667 s^-1 mM^-1 from explicit paper cell; km 0.00259 mM from explicit paper cell

row_label: KpnER; NADPH


organism: Cupriavidus necator

source_db: brenda

kcat_display: Not reported

kcat_over_km_display: Not reported

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

source: brenda


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


assay_conditions_summary: cofactor NADH

proof_lines:
2-chloromaleylacetate as substrate
maleylacetate as substrate


substrate_name: maleylacetate

assay_conditions_summary: cofactor NADPH

substrate: maleylacetate


organism: Escherichia coli


organism: Clostridium sp.

substrate_name: cinnamate

substrate: cinnamate


smiles: CC=CC(=O)O


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


substrate_name: NAD+

assay_conditions_summary: pH 8; cofactor NAD+

substrate: NAD+


enzyme_display_name: aldehyde oxidase

organism: Macaca fascicularis

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

proof_lines: chimeric rat/monkey enzyme, high affinity value, pH 6.0, 37°C

proof_lines: chimeric rat/monkey enzyme, low affinity value, pH 6.0, 37°C

enzyme: aldehyde oxidase


proof_lines: high affinity component of the expressed enzyme

proof_lines: low affinity component of the expressed enzyme


assay_conditions_summary: pH 7; cofactor NADH

proof_lines: in 50 mM HEPES, pH 7.0, ionic strength 0.05 M


assay_conditions_summary: pH 7


organism: Mus musculus

substrate_name: retinal

substrate: retinal


proof_lines:
37°C, pH 7.8, strain c129/C57
37°C, pH 7.8, nude mouse tumor bearing
37°C, pH 7.8, nude mouse


enzyme_display_name: geissoschizine dehydrogenase

organism: Catharanthus roseus

substrate_name: NADP+

enzyme: geissoschizine dehydrogenase

substrate: NADP+


substrate_name: Geissoschizine

substrate: Geissoschizine


organism: Oryctolagus cuniculus

substrate_name: phenanthridine

proof_lines:
methanol, pH 7.4, at 35°C
pyridine, pH 7.4, at 35°C
acetonitrile, pH 7.4, at 35°C

substrate: phenanthridine


organism: Pseudomonas putida

assay_conditions_summary: cofactor NAD+


substrate_name: cis-benzene dihydrodiol

substrate: cis-benzene dihydrodiol


enzyme_display_name: protochlorophyllide reductase

organism: Lyngbya majuscula

proof_lines: pH and temperature not specified in the publication

enzyme: protochlorophyllide reductase


substrate_name: protochlorophyllide

substrate: protochlorophyllide


organism: Chlorobaculum tepidum

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: in 100 mM HEPES-NaOH (pH 7.5), 2 mM ATP, 5 mM MgCl2


substrate_name: Dithionite

substrate: Dithionite


organism: Homo sapiens

mutation_signature: recombinant His-tagged truncated enzyme

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

mutation_type: truncation

assay_conditions_summary: pH 6; 295.15 K; cofactor NADPH

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


organism: Rhodobacter capsulatus


enzyme_display_name: enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)

organism: Porphyromonas gingivalis


substrate_name: crotonyl-CoA

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

enzyme: enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific)

substrate: crotonyl-CoA


enzyme_display_name: cis-2-enoyl-CoA reductase (NADPH)

assay_conditions_summary: cofactor CoA

enzyme: cis-2-enoyl-CoA reductase (NADPH)


organism: Thermosynechococcus vestitus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F233L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F233Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P158F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K156N/I157V to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.5; cofactor NADPH

proof_lines: pH 7.5, 25°C, wild-type, co-substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F237Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K156N with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I157V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P158A to reconstruct the assayed variant sequence.


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

assay_conditions_summary: pH 7.4; cofactor CoA

column_label: Results prose gives the apparent 2,4-decadienoyl-CoA Km with 0.1% albumin; Fig. 2B is the matching substrate panel.

raw_value_unit_evidence: Results prose reports apparent 2,4-decadienoyl-CoA Km = 6 uM in 0.1% albumin.

row_label: 2,4-decadienoyl-CoA; Fig. 2B; apparent Km prose

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


assay_conditions_summary: pH 7.4; 293.15 K; cofactor CoA

column_label: Results prose gives the 2,4-hexadienoyl-CoA Km with 0.1% albumin; Fig. 2A is the matching substrate panel.

raw_value_unit_evidence: Results prose reports 2,4-hexadienoyl-CoA Km = 59 uM in 0.1% albumin.

row_label: 2,4-hexadienoyl-CoA; Fig. 2A; Km prose


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


enzyme_display_name: trans-2-enoyl-CoA reductase (NADPH)

organism: Mycobacterium tuberculosis

km_display: Not reported

sequence_variant_note: Resolved canonical sequence from ncbi_protein_accession:NP_216000.1 and applied mutation signature F149A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.8; 298.15 K; cofactor CoA

proof_lines: mutant enzyme F149A, at 25°C in 30 mM PIPES and 150 mM NaCl (pH 6.8)

enzyme: trans-2-enoyl-CoA reductase (NADPH)


assay_conditions_summary: pH 6.8; 298.15 K; cofactor NADH

proof_lines: wild type enzyme, at 25°C in 30 mM PIPES and 150 mM NaCl (pH 6.8)


protein_accession_database: NCBI Protein


assay_conditions_summary: pH 6.8; cofactor NADH

column_label: table Table 1; row wild-type; columns Km; ACS Table 1 wild-type row under KNADH (uM).

row_label: wild-type

table_label: Table 1


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T145A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T145A, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T147F with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T147F, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N149V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N149V, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T230F with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T230F, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N39V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N39V, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T147S with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T147S, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N90A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N90A, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H236A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H236A, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S16C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S16C, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G19A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme G19A, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R38V with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R38V, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K42A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K42A, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S189A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S189A, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T230A with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T230A, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T230S with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T230S, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y94F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y94F, at 25°C, pH not specified in the publication


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


organism: Chlamydomonas reinhardtii

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

proof_lines: pH and temperature not specified in the publication


organism: Marchantia paleacea

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C226S to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, mutant C226S, co-substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C199S/C226S to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, mutant C199S/C226S, co-substrate: NADPH


proof_lines: pH 7.5, 25°C, mutant C199S/C226S, co-substrate: protochlorophyllide


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C37S/C226S to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, mutant C37S/C226S, co-substrate: NADPH


proof_lines: pH 7.5, 25°C, mutant C37S/C226S, co-substrate: protochlorophyllide


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C37S/C199S/C226S to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, mutant C37S/C199S/C226S, co-substrate: NADPH


proof_lines: pH 7.5, 25°C, mutant C37S/C199S/C226S, co-substrate: protochlorophyllide


proof_lines: pH 7.5, 25°C, mutant C226S, co-substrate: protochlorophyllide


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C199S to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, mutant C199S, co-substrate: NADPH


proof_lines: pH 7.5, 25°C, mutant C199S, co-substrate: protochlorophyllide


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C37S/C199S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C37S to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, mutant C37S, co-substrate: NADPH


proof_lines: pH 7.5, 25°C, mutant C37S, co-substrate: protochlorophyllide


proof_lines: pH 7.5, 25°C, wild-type, co-substrate: protochlorophyllide


organism: Escherichia coli (strain K12)

source_db: uniprot

proof_lines: kcat is 16 sec(-1) for the NADPH-reduction of (2E,4E)-decadienoyl-CoA.

source: uniprot


enzyme_display_name: UniProt P42593

organism: Escherichia coli

source_db: skid

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

sequence_source: multiple

assay_conditions_summary: pH 7.4; cofactor NADPH

source_databases_merged: skid uniprot

enzyme: UniProt P42593

source: skid


organism: Cavia porcellus

source_databases_merged: brenda uniprot


organism: Synechocystis sp.


substrate_name: protochlorophyllide a

substrate: protochlorophyllide a


organism: Gloeobacter violaceus

proof_lines:
protochlorophyllide
Gloeobacter violaceus
Synechocystis POR


proof_lines:
NADPH
Gloeobacter violaceus
POR


column_label: AbstractText; NADPH row/prose; K(m) metric; raw value 0.013 uM.

raw_value_unit_evidence: Abstract reports K(m) for NADPH = 0.013 uM.

row_label: NADPH; K(m) prose

table_label: PMID 16307122 PubMed abstract / RSC article abstract


column_label: AbstractText; Pchlide row/prose; K(m) metric; raw value 1.8 uM.

raw_value_unit_evidence: Abstract reports K(m) for Pchlide = 1.8 uM.

row_label: Pchlide / protochlorophyllide; K(m) prose


enzyme_display_name: Fatty acid synthase

substrate_name: acetyl-CoA

column_label: Scanned journal page 8696; Purification and Properties of Human FAS paragraph; apparent K_m values sentence; acetyl-CoA = 8 uM.

raw_value_unit_evidence: The scanned PMID 7567999 page 8696 prose explicitly reports an apparent K_m of 8 uM for acetyl-CoA.

table_label: PMID 7567999, Results and Discussion prose, scanned journal page 8696

enzyme: Fatty acid synthase

substrate: acetyl-CoA


substrate_name: malonyl-CoA

column_label: Scanned journal page 8696; Purification and Properties of Human FAS paragraph; apparent K_m values sentence; malonyl-CoA = 20 uM.

raw_value_unit_evidence: The scanned PMID 7567999 page 8696 prose explicitly reports an apparent K_m of 20 uM for malonyl-CoA.

substrate: malonyl-CoA


column_label: Scanned journal page 8696; Purification and Properties of Human FAS paragraph; apparent K_m values sentence; NADPH = 25 uM.

raw_value_unit_evidence: The scanned PMID 7567999 page 8696 prose explicitly reports an apparent K_m of 25 uM for NADPH.


substrate_name: butanoyl-CoA

column_label: Prose results on scanned p. 8696; acyl primer specificity sentence; butyryl-CoA/butanoyl-CoA Km raw value 4 uM.

raw_value_unit_evidence: Scanned PNAS p. 8696 prose states that human FAS prefers butyryl-CoA (Km = 4 uM) over acetyl-CoA.

row_label: Human FAS acyl primer specificity; butyryl-CoA (synonym of butanoyl-CoA) compared with acetyl-CoA

table_label: PMID 7567999, scanned PNAS p. 8696 prose: Purification and Properties of Human FAS

substrate: butanoyl-CoA


organism: Staphylococcus aureus

substrate_name: But-2-enoyl-[acyl-carrier protein]

smiles: CC=CC(=O)S

substrate: But-2-enoyl-[acyl-carrier protein]


substrate_name: Dodecenoyl-CoA

assay_conditions_summary: pH 7.8; 298.15 K; cofactor CoA

substrate: Dodecenoyl-CoA


substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A95V with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADPH

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F204S to reconstruct the assayed variant sequence.


smiles: CCCCCCCCC/C=C/C(=O)C(CS)NC(C)=O


organism: Leptolyngbya boryana

column_label: Table 1 journal page 135 row Leptolyngbya boryana dg5, column Km for Pchlide (uM), has 7.8 +/- 1.5 and reference This work.

raw_value_unit_evidence: Km raw_value=7.8 +/- 1.5 raw_unit=uM for Pchlide/protochlorophyllide.

row_label: Cyanobacteria; Leptolyngbya boryana dg5

table_label: Table 1, Kinetic parameters of LPOR from various organisms


column_label: Table 1 journal page 135 row Leptolyngbya boryana dg5, column Km for NADPH (uM), has 8.5 +/- 0.7 and reference This work.

raw_value_unit_evidence: Km raw_value=8.5 +/- 0.7 raw_unit=uM for NADPH.


organism: Bos taurus

substrate_name: lithocholic acid

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

substrate: lithocholic acid


substrate_name: chenodeoxycholic acid

substrate: chenodeoxycholic acid


substrate_name: cholic acid

substrate: cholic acid


substrate_name: taurocholic acid

substrate: taurocholic acid


substrate_name: taurolithocholic acid

substrate: taurolithocholic acid


substrate_name: deoxycholic acid

substrate: deoxycholic acid


substrate_name: taurochenodeoxycholic acid

substrate: taurochenodeoxycholic acid


enzyme_display_name: UniProt Q9FEW9

organism: Solanum lycopersicum

source_license: CC BY-NC-ND 4.0

smiles: CCCC=CC=O

enzyme: UniProt Q9FEW9


enzyme_display_name: UniProt Q9FUP0

organism: Arabidopsis thaliana

enzyme: UniProt Q9FUP0


substrate_name: Methyl vinyl ketone

smiles: CC(=O)C=C

substrate: Methyl vinyl ketone


enzyme_display_name: 2'-hydroxyisoflavone reductase

organism: Cicer arietinum

enzyme: 2'-hydroxyisoflavone reductase


organism: Avena sativa


organism: Synechocystis sp. PCC 6803

substrate_name: protochlorophyllide

proof_lines:
PORs
Synechocystis sp. PCC6803
Gloeobacter violaceus PCC7421

substrate: protochlorophyllide


enzyme_display_name: Trans-2-enoyl-CoA reductase

organism: Euglena gracilis

substrate_name: trans-2-hexenoyl-CoA (in the presence of NADH)

assay_conditions_summary: pH 6.2; cofactor NADH

column_label: Results section Catalytic Properties of Recombinant TER; substrate trans-2-hexenoyl-CoA using NADH; Km value = 91 +/- 1.8 uM.

raw_value_unit_evidence: Km 91 +/- 1.8 uM for trans-2-hexenoyl-CoA using NADH.

row_label: trans-2-hexenoyl-CoA using NADH

table_label: Results prose - Catalytic Properties of Recombinant TER

enzyme: Trans-2-enoyl-CoA reductase


enzyme_display_name: Enoyl-[acyl-carrier-protein] reductase [NADPH] FabI

organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: NADPH (with DD-ACP at 25 degrees Celsius and pH 7.8)

assay_conditions_summary: cofactor NADPH


enzyme_display_name: arogenate dehydrogenase

organism: Stutzerimonas stutzeri

substrate_name: prephenate

enzyme: arogenate dehydrogenase

substrate: prephenate


substrate_name: NAD+

substrate: NAD+


substrate_name: L-arogenate

substrate: L-arogenate


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Mus musculus

substrate_name: malonyl-CoA

proof_lines:
murine FAS
malonyl-CoA
MAT

substrate: malonyl-CoA


substrate_name: acetyl-CoA

proof_lines:
murine FAS
acetyl-CoA
MAT

substrate: acetyl-CoA


enzyme_display_name: 12-oxophytodienoate reductase

organism: Zea mays

substrate_name: NADPH

enzyme: 12-oxophytodienoate reductase


substrate_name: 12-oxophytodienoic acid

substrate: 12-oxophytodienoic acid


substrate_name: NADH

substrate: NADH


organism: Thermosynechococcus vestitus

substrate_name: monovinyl protochlorophyllide a

column_label: PMC article Results prose states that the Km for MV Pchlide was calculated to be 1.36 +/- 0.34 microM; MV means monovinyl Pchlide.

raw_value_unit_evidence: Km raw_value=1.36 +/- 0.34 microM raw_unit=microM

row_label: Thermosynecoccus elongatus BP-1 POR / MV Pchlide

table_label: PMC full text PMID 16274361 steady-state kinetic parameters prose

substrate: monovinyl protochlorophyllide a


organism: Homo sapiens

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADPH

column_label: Official JBC fulltext/PDF results prose; HsNrbf-1p C10 values

normalized_value_unit_evidence: Km 0.0071 mM; kcat 0.93 s^-1; catalytic efficiency 131 s^-1*mM^-1.

row_label: HsNrbf-1p; trans-2-decenoyl-CoA

table_label: Results prose


column_label: Official JBC fulltext/PDF results prose; HsNrbf-1p C6 values

normalized_value_unit_evidence: Km 0.037 mM; kcat 0.53 s^-1; kcat_over_km 14.324324324324326 s^-1 mM^-1 from same row-level kcat and Km cells; explicit paper efficiency rounds nearby at 14.4

row_label: HsNrbf-1p; trans-2-hexenoyl-CoA


assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA

column_label: Official JBC fulltext/PDF results prose; BtNrbf-1p C10 values

normalized_value_unit_evidence: kcat 0.52 s^-1; Km 0.0045 mM; explicit kcat/Km 115 s^-1 mM^-1; exported kcat_over_km 104.0 s^-1 mM^-1

row_label: BtNrbf-1p; trans-2-decenoyl-CoA


enzyme_display_name: trans-2-enoyl-CoA reductase (NAD+)

organism: Mycolicibacterium smegmatis

assay_conditions_summary: cofactor NADH

enzyme: trans-2-enoyl-CoA reductase (NAD+)


substrate_name: hexadecenoyl-CoA

substrate: hexadecenoyl-CoA


assay_conditions_summary: cofactor NAD+


organism: Pseudomonas aeruginosa


organism: Lathyrus oleraceus


organism: Phenylobacterium immobile


organism: Pseudomonas flexibilis


organism: Streptomyces phaeochromogenes


substrate_name: NAD+; L-Arogenate

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

proof_lines: with L-arogenate as variable substrate, competitive inhibition

proof_lines: with prephenate as variable substrate, competitive inhibition

substrate: NAD+; L-Arogenate


enzyme_display_name: biochanin-A reductase

organism: Fusarium solani-melongenae

substrate_name: Biochanin A

enzyme: biochanin-A reductase

substrate: Biochanin A


substrate: NADPH


organism: Actinoplanes missouriensis


enzyme_display_name: alpha-santonin 1,2-reductase

organism: Pseudomonas cichorii

enzyme: alpha-santonin 1,2-reductase


substrate_name: alpha-santonin

substrate: alpha-santonin


enzyme_display_name: xanthommatin reductase

organism: Drosophila melanogaster

substrate_name: Xanthommatin

enzyme: xanthommatin reductase

substrate: Xanthommatin


organism: Medicago sativa

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y272A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D285G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y169A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R97G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H164A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Δ39 to reconstruct the assayed variant sequence.

mutation_type: deletion


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


enzyme_display_name: Prostaglandin reductase-3

proof_lines: kcat is 8.6 min(-1) for 15-keto-PGE2, 4.37 min(-1) for 15-keto-PGE1, 11.55 for min(-1) for 15-keto-PGF2-alpha, 11.45 min(-1) for 15-keto-PGF1-alpha.

enzyme: Prostaglandin reductase-3


enzyme_display_name: Trans-2-enoyl-CoA reductase [NADH]

organism: Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104)

substrate_name: NAD

assay_conditions_summary: pH 6.2; cofactor CoA

proof_lines: kcat is 385.9 sec(-1) for reductase activity (at pH 6.2 and 25 degrees Celsius) (PubMed:23050861). kcat is 112 sec(-1) for reductase activity with hexenoyl-CoA as substrate (PubMed:22906002). kcat is 91 sec(-1) for reductase activity with c

enzyme: Trans-2-enoyl-CoA reductase [NADH]

substrate: NAD


substrate_name: dodecenoyl-CoA

substrate: dodecenoyl-CoA


substrate_name: hexenoyl-CoA

substrate: hexenoyl-CoA


substrate_name: NADP

substrate: NADP


enzyme_display_name: 12-oxophytodienoate reductase 2

organism: Arabidopsis thaliana

proof_lines: kcat is 0.819 sec(-1) with 4,5-didehydrojasmonate as substrate.

enzyme: 12-oxophytodienoate reductase 2


substrate_name: crotonyl-CoA (at pH 6.2 and 30 degrees Celsius)


organism: Clostridium acetobutylicum

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K245A to reconstruct the assayed variant sequence.

proof_lines:
pH 6.2, 25°C, mutant K245A
mutant enzyme K245A, at pH 6.2 and 25°C


organism: Burkholderia mallei (strain ATCC 23344)

substrate_name: DD-CoA (with His tag)

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

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 1728 min(-1) for reductase activity with DD-CoA as substrate (without His tag). kcat is 1242 min(-1) for reductase activity with DD-CoA as substrate (with His tag).

substrate: DD-CoA (with His tag)


organism: Euglena gracilis

substrate_name: crotonyl-CoA

column_label: Results section Catalytic Properties of Recombinant TER; substrate crotonyl-CoA using NADH; Km value = 68 +/- 3.9 uM.

raw_value_unit_evidence: Km 68 +/- 3.9 uM for crotonyl-CoA using NADH.

row_label: crotonyl-CoA using NADH

substrate: crotonyl-CoA


proof_lines: recombinant enzyme, pH 6.2, 30°C, with crotonyl-CoA as substrate


assay_conditions_summary: pH 6.2; cofactor NADPH


enzyme_display_name: Cyclohexadienyl dehydrogenase

organism: Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)

substrate_name: L-arogenate (at pH 6.6 and 37 degrees Celsius)

column_label: PubMed abstract reports Km values of 0.25 mM and 0.18 mM for prephenate and L-arogenate, respectively.

raw_value_unit_evidence: Km raw_value=0.18 raw_unit=mM

row_label: Z. mobilis cyclohexadienyl dehydrogenase with L-arogenate

table_label: PubMed abstract PMID 7916685

enzyme: Cyclohexadienyl dehydrogenase


substrate_name: prephenate (at pH 6.6 and 37 degrees Celsius)

raw_value_unit_evidence: Km raw_value=0.25 raw_unit=mM

row_label: Z. mobilis cyclohexadienyl dehydrogenase with prephenate


substrate_name: NAD(+) (at pH 6.6 and 37 degrees Celsius)

assay_conditions_summary: pH 6.6; cofactor NAD+

column_label: PubMed abstract reports that the Km value for NAD+ was 0.09 mM and unchanged between arogenate- and prephenate-dehydrogenase assays.

raw_value_unit_evidence: Km raw_value=0.09 raw_unit=mM

row_label: Z. mobilis cyclohexadienyl dehydrogenase with NAD(+)


organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)

substrate_name: NAD (at pH 6.2 and 25 degrees Celsius)

proof_lines: kcat is 28.2 sec(-1) for reductase activity (at pH 6.2 and 25 degrees Celsius).

substrate: NAD (at pH 6.2 and 25 degrees Celsius)


organism: Xanthomonas oryzae pv. oryzae (strain MAFF 311018)

substrate_name: NADH

proof_lines: kcat is 1335 sec(-1) for reductase activity.


enzyme_display_name: 12-oxophytodienoate reductase 1

organism: Solanum lycopersicum

substrate_name: N-ethylmaleimide (at pH 7.0 and 25 degrees Celsius)

assay_conditions_summary: pH 7

proof_lines: The highest catalytic efficiency was observed with N-ethylmaleimide.

enzyme: 12-oxophytodienoate reductase 1


substrate_name: maleic acid (at pH 7.0 and 25 degrees Celsius)


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

substrate: OPDA (at pH 7.0 and 25 degrees Celsius)


enzyme_display_name: 15-oxoprostaglandin 13-reductase

organism: Mus musculus

substrate_name: 15-Keto-prostaglandin E1

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

column_label: Required metric is kcat_over_km; the explicit primary Table 2 Kcat/Km cell for 15-Keto-PGE1 is 215.1 mM^-1 min^-1. Expected row value is 3.617647058823529 s^-1*mM^-1.

raw_value_unit_evidence: Table 2 row 15-Keto-PGE1: Km 34.4 +/- reported SD uM; Kcat 7.4 +/- reported SD min^-1; Kcat/Km 215.1 mM^-1 min^-1.

table_label: Table 2: Enzymatic substrates and kinetic parameters for mouse PGR-2

enzyme: 15-oxoprostaglandin 13-reductase

substrate: 15-Keto-prostaglandin E1


substrate_name: 15-Keto-prostaglandin F1alpha

column_label: Required metric is kcat_over_km; the explicit primary Table 2 Kcat/Km cell for 15-Keto-PGF1alpha is 222.9 mM^-1 min^-1. Expected row value is 3.728813559322034 s^-1*mM^-1.

normalized_value_unit_evidence: Required Kcat/Km 222.9 mM^-1 min^-1 = 3.715 s^-1*mM^-1; context Km 0.0592 mM; context Kcat 0.22 s^-1.

raw_value_unit_evidence: Table 2 row 15-Keto-PGF1alpha: Km 59.2 +/- reported SD uM; Kcat 13.2 +/- reported SD min^-1; Kcat/Km 222.9 mM^-1 min^-1.

substrate: 15-Keto-prostaglandin F1alpha


substrate_name: 15-Keto-prostaglandin F2alpha

column_label: Required metric is kcat_over_km; the explicit primary Table 2 Kcat/Km cell for 15-Keto-PGF2alpha is 136.0 mM^-1 min^-1. Expected row value is 2.2660550458715596 s^-1*mM^-1.

raw_value_unit_evidence: Table 2 row 15-Keto-PGF2alpha: Km 108.8 +/- reported SD uM; Kcat 14.8 +/- reported SD min^-1; Kcat/Km 136.0 mM^-1 min^-1.

substrate: 15-Keto-prostaglandin F2alpha


column_label: Required metric is kcat_over_km; the explicit primary Table 2 Kcat/Km cell for 15-Keto-PGE2 is 229.8 mM^-1 min^-1. Expected row value is 3.8 s^-1*mM^-1.

normalized_value_unit_evidence: Required Kcat/Km 229.8 mM^-1 min^-1 = 3.83 s^-1*mM^-1; context Km 0.0496 mM; context Kcat 0.19 s^-1.

raw_value_unit_evidence: Table 2 row 15-Keto-PGE2: Km 49.6 +/- reported SD uM; Kcat 11.4 +/- reported SD min^-1; Kcat/Km 229.8 mM^-1 min^-1.


substrate_name: NADPH

column_label: Required metric is kcat_over_km; the explicit primary Table 2 Kcat/Km cell for NADPH is 98.3 mM^-1 min^-1. Expected row value is 1.6842105263157894 s^-1*mM^-1.

raw_value_unit_evidence: Table 2 row NADPH: Km 94.6 +/- reported SD uM; Kcat 9.3 +/- reported SD min^-1; Kcat/Km 98.3 mM^-1 min^-1.

row_label: NADPH


enzyme_display_name: Prostaglandin reductase 2

column_label: Table 2 Km column maps 15-Keto-PGE2 to 49.6 uM

raw_value_unit_evidence: Km raw_value=49.6 raw_unit=uM

table_label: PMID 17449869 PDF Table 2

enzyme: Prostaglandin reductase 2


column_label: Table 2 Km column maps 15-Keto-PGE1 to 34.4 uM

raw_value_unit_evidence: Km raw_value=34.4 raw_unit=uM


column_label: Table 2 Km column maps NADPH to 94.6 uM

raw_value_unit_evidence: Km raw_value=94.6 raw_unit=uM


enzyme_display_name: Prostaglandin reductase 1

organism: Homo sapiens

enzyme: Prostaglandin reductase 1


smiles: CCCCCC=CC=O


smiles: CCCCCCCC=CC=O

assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 5, row Trans-2-decenal, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 5, row Trans-2-decenal: Km 6 +/- 2.3 uM

table_label: Table 5


smiles: CCCCCCCCCC=O


smiles: CC=CC(=O)C


smiles: CCCCCC=CC(=O)C

column_label: Table 5, row Trans-3-nonen-2-one, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 5, row Trans-3-nonen-2-one: Km 6.5 +/- 0.5 uM


substrate_name: 15-oxoprostaglandin E1

substrate: 15-oxoprostaglandin E1


substrate_name: 15-oxoprostaglandin E2

column_label: Table 6, row 15-keto-PGE2, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 6, row 15-keto-PGE2: Km 0.6 +/- 0.2 uM

table_label: Table 6

substrate: 15-oxoprostaglandin E2


substrate_name: 15-oxoprostaglandin F1alpha

substrate: 15-oxoprostaglandin F1alpha


organism: Sus scrofa


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


substrate: NADH


substrate: NADPH


enzyme_display_name: trans-2-enoyl-CoA reductase (NAD(+))

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F11K with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.2; 298.15 K; cofactor NADH

enzyme: trans-2-enoyl-CoA reductase (NAD(+))


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K245A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y225A to reconstruct the assayed variant sequence.


enzyme_display_name: 12-oxophytodienoate reductase 3

column_label: Abstract reports OPR3 effectively converts natural (9S,13S)-12-oxophytodienoic acid [Km = 35 microM, Vmax 53.7 nkat (mg protein)-1].

raw_value_unit_evidence: Km raw_value=35 microM raw_unit=microM

row_label: Arabidopsis thaliana OPR3 / natural (9S,13S)-12-oxophytodienoic acid

table_label: PubMed XML abstract PMID 10872231

enzyme: 12-oxophytodienoate reductase 3


substrate_name: cyclohexenone

substrate: cyclohexenone


organism: Cavia porcellus


assay_conditions_summary: pH 7.4; cofactor NADH

column_label: Results paragraph; substrate 15-keto-PGE2; metric Km; raw cell/prose value 35 uM; uncertainty 8.5 uM.

normalized_value_unit_evidence: Km=0.035 mM for 15-keto-PGE2.

raw_value_unit_evidence: Results paragraph reports recombinant gpLTB4 12-HD/PGR Km for 15-keto-PGE2 = 35 +/- 8.5 uM.

row_label: 15-keto-PGE2 / PGR activity

table_label: Wiley full-text results paragraph and Fig. 2 kinetic profiles


column_label: Table 2 row Wild-type, 15-Keto-PGE2 KM (uM) column = 11.21 +/- 0.14.

raw_value_unit_evidence: Km raw_value=11.21 +/- 0.14 uM raw_unit=uM

row_label: Wild-type hPTGR2 row

table_label: ScienceDirect PMID 19000823 Table 2


column_label: Table 2 row Wild-type, NADPH KM (uM) column = 15.87 +/- 1.71.

raw_value_unit_evidence: Km raw_value=15.87 +/- 1.71 uM raw_unit=uM


enzyme_display_name: Isoflavone reductase

enzyme: Isoflavone reductase


substrate_name: NADP(+)

assay_conditions_summary: cofactor NADP+

proof_lines:
PTGR1
LTB4 12-hydroxydehydrogenase
NADP+ as a cofactor

substrate: NADP(+)


substrate_name: 15-oxoprostaglandin F2alpha

column_label: Table 6, row 15-keto-PGF2alpha, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 6, row 15-keto-PGF2alpha: Km 3.2 +/- 0.9 uM

substrate: 15-oxoprostaglandin F2alpha


substrate_name: leukotriene B4

assay_conditions_summary: pH 7; cofactor NADP+

column_label: Table 6, row LTB4, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 6, row LTB4: Km 5.2 +/- 1.4 uM

substrate: leukotriene B4


column_label: PMID 25619643 article preview states NADPH Km 14 uM for PGR1, matching 0.014 mM.

normalized_value_unit_evidence: Km normalized_value=0.014 mM.

raw_value_unit_evidence: ScienceDirect preview reports NADPH Km=14 uM.

row_label: PGR1 / NADPH

table_label: ScienceDirect article preview / Table 1 cofactor specificity statement


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: crotonyl-CoA

column_label: Table 4 row Crotonyl-CoA reports Km 704.3 uM under the FabV column.

normalized_value_unit_evidence: Km normalized 0.7043 mM.

raw_value_unit_evidence: Km raw 704.3 uM for FabV/crotonyl-CoA.

row_label: Crotonyl-CoA row

table_label: Table 4 kinetic parameters of P. aeruginosa FabV and FabI


organism: Treponema denticola


substrate_name: 15-ketoprostaglandin E1

substrate: 15-ketoprostaglandin E1


substrate_name: 15-ketoprostaglandin A1

substrate: 15-ketoprostaglandin A1


substrate_name: 15-ketoprostaglandin F2alpha

substrate: 15-ketoprostaglandin F2alpha


substrate_name: 15-ketoprostaglandin B1

substrate: 15-ketoprostaglandin B1


substrate_name: 15-ketoprostaglandin E2

substrate: 15-ketoprostaglandin E2


substrate_name: NADH


substrate_name: nicotinamide hypoxanthine dinucleotide

substrate: nicotinamide hypoxanthine dinucleotide


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


substrate_name: 15-ketoprostaglandin F1alpha

substrate: 15-ketoprostaglandin F1alpha


organism: Escherichia coli

substrate_name: NADPH

assay_conditions_summary: pH 7.4; buffer 50 mM potassium phosphate; cofactor NADPH

proof_lines: mutant enzyme C337A, in 50 mM potassium phosphate buffer (pH 7.4)


proof_lines: mutant enzyme H252A, in 50 mM potassium phosphate buffer (pH 7.4)


proof_lines: mutant enzyme E164A, in 50 mM potassium phosphate buffer (pH 7.4)


proof_lines: mutant enzyme H252A/Y166F, in 50 mM potassium phosphate buffer (pH 7.4)


proof_lines: mutant enzyme Y166F, in 50 mM potassium phosphate buffer (pH 7.4)


proof_lines: wild type enzyme, in 50 mM potassium phosphate buffer (pH 7.4)


assay_conditions_summary: cofactor NADPH

proof_lines:
cofactor NADH
cofactor NADPH
recombinant enzyme


organism: Rattus norvegicus

substrate_name: acrolein

smiles: C=CC=O

substrate: acrolein


substrate_name: crotonaldehyde

smiles: CC=CC=O

substrate: crotonaldehyde


substrate_name: alpha-methylcinnamaldehyde

substrate: alpha-methylcinnamaldehyde


smiles: CCC(C=CC=O)O


substrate_name: cinnamaldehyde

assay_conditions_summary: pH 7.4; 298.15 K; buffer 100 mM phosphate

proof_lines: in 100 mM phosphate buffer (pH 7.4), at 25°C

substrate: cinnamaldehyde


smiles: CCC=CC=O


smiles: CCCCC=CC=CC=O


substrate_name: chalcone

substrate: chalcone


substrate_name: benzylidene acetone

substrate: benzylidene acetone


smiles: CCCCCCCCCC=CC=O


smiles: CCCCCC(C=CC=O)O


smiles: CCCCCCC=CC=O


substrate_name: methylvinylketone

substrate: methylvinylketone


substrate_name: ethylvinylketone

smiles: CCC(=O)C=C

substrate: ethylvinylketone


enzyme_display_name: dihydropyrimidine dehydrogenase (NADP+)

organism: Bos taurus

enzyme: dihydropyrimidine dehydrogenase (NADP+)


substrate_name: Uracil

substrate: Uracil


proof_lines:
in presence of 5-fluorouracil
in presence of uracil

substrate: NADPH


substrate_name: NADP+

substrate: NADP+


substrate_name: crotonyl-CoA

proof_lines: pH and temperature not specified in the publication, mutant Y240F

proof_lines: mutant Y240F, pH not specified in the publication, temperature not specified in the publication

substrate: crotonyl-CoA


proof_lines: pH and temperature not specified in the publication, mutant I287A

proof_lines: mutant I287A, pH not specified in the publication, temperature not specified in the publication

proof_lines: pH and temperature not specified in the publication, 0.0001 mM inhibitor, mutant I287A


substrate_name: hexanoyl-CoA

substrate: hexanoyl-CoA


proof_lines: pH and temperature not specified in the publication, mutant L276A/V277A

proof_lines: mutant L276A/V277A, pH not specified in the publication, temperature not specified in the publication


proof_lines: pH and temperature not specified in the publication, mutant L276A/V277A/F295A

proof_lines: mutant L276A/V277A/F295A, pH not specified in the publication, temperature not specified in the publication


proof_lines: pH and temperature not specified in the publication, mutant L291A

proof_lines: mutant L291A, pH not specified in the publication, temperature not specified in the publication


proof_lines: pH and temperature not specified in the publication, mutant Y370A


proof_lines: mutant Y370A, pH not specified in the publication, temperature not specified in the publication


proof_lines: pH and temperature not specified in the publication, mutant F295A


proof_lines: mutant F295A, pH not specified in the publication, temperature not specified in the publication


substrate_name: 15-ketoprostaglandin E2


substrate_name: 6,15-diketo-prostaglandin F1alpha

substrate: 6,15-diketo-prostaglandin F1alpha


enzyme_display_name: Enoyl-[acyl-carrier-protein] reductase [NADH] 1

organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)

column_label: Table 1 row FabV Native column Km Crotonyl-CoA reports 1178 +/- 471 uM

raw_value_unit_evidence: Km raw_value=1178 +/- 471 raw_unit=uM

row_label: Native FabV

table_label: JBC PDF Table 1


organism: Alcaligenes faecalis


substrate_name: NAD+

substrate: NAD+


organism: Comamonas testosteroni


enzyme_display_name: UniProt Q46381

enzyme: UniProt Q46381


proof_lines: in 100 mM phosphate buffer (pH 7.4), at 25°C

substrate: 15-ketoprostaglandin E2


substrate_name: phenyl propenyl ketone

substrate: phenyl propenyl ketone


substrate_name: cinnamoylthiophene

substrate: cinnamoylthiophene


enzyme_display_name: protochlorophyllide reductase

organism: Hordeum vulgare

substrate_name: NADPH

enzyme: protochlorophyllide reductase


substrate_name: protochlorophyllide

substrate: protochlorophyllide


substrate_name: 15-ketoprostaglandin E

substrate: 15-ketoprostaglandin E


substrate_name: NADH

substrate: NADH


enzyme_display_name: trans-2-enoyl-CoA reductase (NAD+)

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

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

proof_lines: pH and temperature not specified in the publication, 0.0015 mM inhibitor, wild-type

enzyme: trans-2-enoyl-CoA reductase (NAD+)


enzyme_display_name: precorrin-6A reductase

organism: Pseudomonas denitrificans (nom. rej.)

enzyme: precorrin-6A reductase


enzyme_display_name: zeatin reductase

organism: Phaseolus vulgaris

substrate_name: trans-zeatin

proof_lines: low molecular weight isoenzyme, instability of the isoenzyme after gel filtration may contibute to the variation between experiments

enzyme: zeatin reductase

substrate: trans-zeatin


enzyme_display_name: 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH)

organism: Rhodobacter capsulatus

substrate_name: 3,8-divinyl chlorophyllide a

substrate: 3,8-divinyl chlorophyllide a


substrate_name: 3,8-divinyl protochlorophyllide a

enzyme: 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (NADPH)

substrate: 3,8-divinyl protochlorophyllide a


enzyme_display_name: DELTA14-sterol reductase

organism: Zea mays

enzyme: DELTA14-sterol reductase


proof_lines:
membrane-bound enzyme, Lineweaver-Burk
soluble enzyme
microsomal-bound enzyme


substrate_name: 15-keto-prostaglandin E2

substrate: 15-keto-prostaglandin E2


enzyme_display_name: prephenate dehydrogenase

organism: Bacillus subtilis

substrate_name: prephenate

enzyme: prephenate dehydrogenase

substrate: prephenate


enzyme_display_name: 2'-hydroxydaidzein reductase

organism: Glycine max

enzyme: 2'-hydroxydaidzein reductase


substrate: NADPH


organism: Vitis bellula

substrate_name: cyanidin

substrate: cyanidin


substrate_name: pelargonidin

substrate: pelargonidin


substrate_name: delphinidin

substrate: delphinidin


assay_conditions_summary: pH 4; 313.15 K; cofactor NADPH


organism: Camellia sinensis

proof_lines: pH 6.5, temperature not specified in the publication


assay_conditions_summary: pH 6.5; cofactor NADPH

proof_lines: co-substrate: cyanidin, pH 6.5, temperature not specified in the publication


enzyme_display_name: arogenate dehydrogenase (NADP+)

organism: Synechocystis sp. PCC 6803

substrate_name: NADP+

assay_conditions_summary: pH 8.6; 298.15 K; cofactor NADP+

enzyme: arogenate dehydrogenase (NADP+)

substrate: NADP+


substrate_name: L-arogenate

substrate: L-arogenate


substrate_name: Unknown

proof_lines:
pH 8.6, 25°C, versus NADP+
pH 8.6, 25°C, versus L-arogenate

substrate: Unknown


enzyme_display_name: 2-alkenal reductase [NAD(P)+]

organism: Artemisia annua

enzyme: 2-alkenal reductase [NAD(P)+]


substrate_name: artemisinic aldehyde

substrate: artemisinic aldehyde


organism: Sorghum bicolor


organism: Euglena gracilis


enzyme_display_name: 2-alkenal reductase [NAD(P)(+)]

organism: Cucumis sativus

smiles: C=CC(=O)CC

enzyme: 2-alkenal reductase [NAD(P)(+)]


smiles: C=CC(C)=O


smiles: CC=CC(C)=O


assay_conditions_summary: pH 7; 298.15 K; cofactor NADH


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH


substrate_name: propenal

substrate: propenal


organism: Mangifera indica


organism: Nicotiana sylvestris


substrate_name: crotonaldehyde

substrate: crotonaldehyde


smiles: CCC(=O)C=CC


smiles: CC(=O)C=C


substrate_name: NADPH


organism: Synechocystis sp.


enzyme_display_name: arogenate dehydrogenase [NAD(P)+]

organism: Sediminispirochaeta smaragdinae

proof_lines: mutant D208N, pH 7.6, temperature not specified in the publication

enzyme: arogenate dehydrogenase [NAD(P)+]


proof_lines: wild-type, pH 7.6, temperature not specified in the publication


organism: Acinetobacter calcoaceticus


enzyme_display_name: NADPH-dependent oxidoreductase 2-alkenal reductase

organism: Arabidopsis thaliana

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)


smiles: CCCC=CC=O

enzyme: NADPH-dependent oxidoreductase 2-alkenal reductase


smiles: CC=CC(=O)C


organism: Vigna radiata

substrate_name: L-Arogenate; NADP+

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

substrate: L-Arogenate; NADP+


assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH


assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: PDF page 3, Table 1, Arabidopsis P1-ZCr row 9,10-Phenanthrenequinone (PAQ), column Km (microM): 0.65; 0.65 microM = 0.00065 mM.

raw_value_unit_evidence: Km raw_value=0.65 raw_unit=microM

row_label: 9,10-Phenanthrenequinone (PAQ)

table_label: Table 1: Comparison of substrate specificity of Arabidopsis P1-ZCr and guinea-pig ZCr


column_label: PDF page 3, Table 1, Arabidopsis P1-ZCr row 5-Hydroxy-1,4-naphtoquinone (juglone), column Km (microM): 11; 11 microM = 0.011 mM.

raw_value_unit_evidence: Km raw_value=11 raw_unit=microM

row_label: 5-Hydroxy-1,4-naphtoquinone (juglone)


column_label: PDF page 3, Table 1, Arabidopsis P1-ZCr row 1,4-Benzoquinone, column Km (microM): 152; 152 microM = 0.152 mM.

raw_value_unit_evidence: Km raw_value=152 raw_unit=microM


substrate_name: decyl-plastoquinone

column_label: PDF page 3, Table 1, Arabidopsis P1-ZCr row Decyl-plastoquinone (DPQ), column Km (microM): 25; 25 microM = 0.025 mM.

raw_value_unit_evidence: Km raw_value=25 raw_unit=microM

row_label: Decyl-plastoquinone (DPQ)

substrate: decyl-plastoquinone


column_label: PDF page 8, Nucleotide specificity prose: NADPH Km in the PAQ-reduction was 2.5 microM at 5 microM PAQ; 2.5 microM = 0.0025 mM.

raw_value_unit_evidence: Km raw_value=2.5 raw_unit=microM

row_label: NADPH in PAQ-reducing reaction

table_label: Nucleotide specificity prose


organism: Zea mays


enzyme_display_name: 1,2-dihydrovomilenine 19,20-reductase

organism: Rauvolfia serpentina

substrate_name: Vomilenine

mutation_signature: N-terminally truncated enzyme

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

proof_lines: N-terminally truncated enzyme, at pH 7.5 and 30°C

enzyme: 1,2-dihydrovomilenine 19,20-reductase

substrate: Vomilenine


enzyme_display_name: 1,2-Dihydrovomilenine reductase

proof_lines: kcat is 0.2 sec(-1) with vomilenine as substrate (PubMed:38212296). kcat is 10.4 sec(-1) with 1,2-dihydrovomilenine as substrate (PubMed:38212296).

enzyme: 1,2-Dihydrovomilenine reductase


substrate_name: 9-oxo-10(E),12(Z)-octadecadienoic acid

smiles: CCCCCC=CC=CC(=O)CCCCCCCC(=O)O

substrate: 9-oxo-10(E),12(Z)-octadecadienoic acid


substrate_name: 13-oxo-9(Z),11(E)-octadecadienoic acid

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

substrate: 13-oxo-9(Z),11(E)-octadecadienoic acid


smiles: CCCCCC=CC(=O)C


substrate_name: vomilenine

substrate: vomilenine


substrate_name: traumatin

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

substrate: traumatin


enzyme_display_name: Prostaglandin reductase 1

organism: Sus scrofa

assay_conditions_summary: cofactor NADH

column_label: Table 2 is labelled Apparent Km and Vmax values for pig lung PGR; the 15-oxo-PGE1 row reports Native Km 7.7 in the Km (uM) column.

normalized_value_unit_evidence: Km central normalized_value=0.0077 normalized_unit=mM.

raw_value_unit_evidence: Table 2 reports the 15-oxo-PGE1 row under Km (uM), Native as raw_value=7.7 raw_unit=uM.

row_label: Native pig lung PGR / 15-oxo-PGE1

table_label: Biochem. J. 1998 Table 2

enzyme: Prostaglandin reductase 1


column_label: Table 2 is labelled Apparent Km and Vmax values for pig lung PGR; the 15-oxo-PGE2 row reports Native Km 19.0 in the Km (uM) column.

normalized_value_unit_evidence: Km central normalized_value=0.019 normalized_unit=mM.

raw_value_unit_evidence: Table 2 reports the 15-oxo-PGE2 row under Km (uM), Native as raw_value=19.0 raw_unit=uM.

row_label: Native pig lung PGR / 15-oxo-PGE2


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

column_label: Table 2 row LTB4, recombinant enzyme Km column: 10.0 uM.

raw_value_unit_evidence: Table 2 reports recombinant enzyme LTB4 Km 10.0 uM.

row_label: LTB4 for recombinant pig lung PGR

table_label: Table 2


substrate_name: NADH

column_label: Table 2 is labelled Apparent Km and Vmax values for pig lung PGR; the NADH row reports Native Km 153.0 in the Km (uM) column.

normalized_value_unit_evidence: Km central normalized_value=0.153 normalized_unit=mM.

raw_value_unit_evidence: Table 2 reports the NADH row under Km (uM), Native as raw_value=153.0 raw_unit=uM.

row_label: Native pig lung PGR / NADH

substrate: NADH


column_label: Table 2 is labelled Apparent Km and Vmax values for pig lung PGR; the NADPH row reports Native Km 15.0 in the Km (uM) column.

normalized_value_unit_evidence: Km central normalized_value=0.015 normalized_unit=mM.

raw_value_unit_evidence: Table 2 reports the NADPH row under Km (uM), Native as raw_value=15.0 raw_unit=uM.

row_label: Native pig lung PGR / NADPH

substrate: NADPH


substrate_name: p-coumaryl aldehyde

substrate: p-coumaryl aldehyde


substrate_name: coniferyl aldehyde

substrate: coniferyl aldehyde


substrate_name: arogenate

proof_lines: NADP increases the apparent affinity for arogenate. The two active domains have the same KM values for arogenate.

substrate: arogenate


substrate_name: NADP+

assay_conditions_summary: pH 7.5; cofactor NADP+

substrate: NADP+


proof_lines: NADP increases the apparent affinity for arogenate.


substrate_name: prephenate

proof_lines: pH 7.5, 25°C, with 0.1 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

substrate: prephenate


enzyme_display_name: Arogenate dehydrogenase 2, chloroplastic


organism: Homo sapiens

assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 5, row Trans-2-hexenal, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 5, row Trans-2-hexenal: Km 33 +/- 6 uM


smiles: CCCCCC=CC=O

column_label: Table 5, row Trans-2-octenal, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 5, row Trans-2-octenal: Km 14 +/- 3 uM


smiles: CCCCCCCC=CC=O

column_label: Table 5, row Trans-2-decenal, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 5, row Trans-2-decenal: Km 6 +/- 2.3 uM


smiles: CCCCCCCCCC=CC=O

column_label: Table 5, row Trans-2-dodecenal, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 5, row Trans-2-dodecenal: Km 12 +/- 2.5 uM


column_label: Table 5, row Trans-3-buten-2-one, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 5, row Trans-3-buten-2-one: Km 12 +/- 1.7 uM


column_label: Table 5, row Trans-3-penten-2-one, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 5, row Trans-3-penten-2-one: Km 7.3 +/- 1 uM


column_label: Table 5, row Trans-3-nonen-2-one, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 5, row Trans-3-nonen-2-one: Km 6.5 +/- 0.5 uM


substrate_name: 15-oxoprostaglandin E1

column_label: Table 6, row 15-keto-PGE1, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 6, row 15-keto-PGE1: Km 1.4 +/- 0.3 uM

substrate: 15-oxoprostaglandin E1


substrate_name: 15-oxoprostaglandin E2

column_label: Table 6, row 15-keto-PGE2, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 6, row 15-keto-PGE2: Km 0.6 +/- 0.2 uM

substrate: 15-oxoprostaglandin E2


substrate_name: 15-oxoprostaglandin F1alpha

column_label: Table 6, row 15-keto-PGF1alpha, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 6, row 15-keto-PGF1alpha: Km 1.1 +/- 0.3 uM

substrate: 15-oxoprostaglandin F1alpha


substrate_name: delphinidin

assay_conditions_summary: pH 8; cofactor NADH

proof_lines:
pH 8.0
cannot use NADH as cosubstrate.

substrate: delphinidin


substrate_name: cyanidin

substrate: cyanidin


substrate_name: pelargonidin

substrate: pelargonidin


organism: Vitis bellula


smiles: CCC=CC=O

assay_conditions_summary: pH 6


substrate_name: propenal

smiles: C=CC=O

substrate: propenal


proof_lines:
pH 6
pH 6.0


smiles: CCCCCCC=CC=O


substrate_name: Diamide

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

substrate: Diamide


organism: Rauvolfia tetraphylla

substrate: vomilenine


organism: Cavia porcellus


assay_conditions_summary: pH 7.4; cofactor NADH

column_label: Results paragraph; substrate 15-keto-PGE2; metric Km; raw value 35 uM; uncertainty 8.5 uM.

normalized_value_unit_evidence: Km=0.035 mM for 15-keto-PGE2; paper uncertainty is 0.0085 mM.

raw_value_unit_evidence: Results paragraph reports recombinant gpLTB4 12-HD/PGR Km for 15-keto-PGE2 = 35 +/- 8.5 uM; 8.5 uM is the uncertainty term, not the Km.


substrate_name: 15-oxoprostaglandin F2alpha

column_label: Table 6, row 15-keto-PGF2alpha, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 6, row 15-keto-PGF2alpha: Km 3.2 +/- 0.9 uM

substrate: 15-oxoprostaglandin F2alpha


substrate_name: leukotriene B4

assay_conditions_summary: pH 7; cofactor NADP+

column_label: Table 6, row LTB4, column Km; unit header Km (uM)

raw_value_unit_evidence: Table 6, row LTB4: Km 5.2 +/- 1.4 uM

substrate: leukotriene B4


substrate_name: NADPH

column_label: ScienceDirect article preview, cofactor specificity section, Table 1 statement for NADPH Km.

normalized_value_unit_evidence: Km=0.014 mM converted from 14 uM.

raw_value_unit_evidence: ScienceDirect preview reports NADPH Km=14 uM.

table_label: Table 1 / Cofactor specificity of human PGR1 and quaternary structure

substrate: NADPH


substrate_name: NADH

substrate: NADH


substrate_name: Cyanidin

column_label: Table 1 AtANR row Cyanidin reports Km 73.9 +/- 5.9 uM, kcat 62.7 min^-1, and kcat/Km 1.4 x 10^4 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.074 normalized_unit=mM; kcat normalized_value=1.045 normalized_unit=s^-1; kcat/Km normalized_value=14.0 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=73.9 +/- 5.9 raw_unit=uM; kcat raw_value=62.7 raw_unit=min^-1; kcat/Km raw_value=1.4 x 10^4 raw_unit=M^-1 s^-1

row_label: AtANR / Cyanidin

table_label: Table 1 - Kinetic properties of MtANR and AtANR

substrate: Cyanidin


column_label: Table 1 AtANR row Delphinidin reports Km 17.8 +/- 1.5 uM, kcat 3.5 min^-1, and kcat/Km 0.3 x 10^4 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.018 normalized_unit=mM; kcat normalized_value=0.058 normalized_unit=s^-1; kcat/Km normalized_value=3.0 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=17.8 +/- 1.5 raw_unit=uM; kcat raw_value=3.5 raw_unit=min^-1; kcat/Km raw_value=0.3 x 10^4 raw_unit=M^-1 s^-1

row_label: AtANR / Delphinidin


enzyme_display_name: arogenate dehydrogenase (NADP(+))

substrate_name: L-Arogenate

enzyme: arogenate dehydrogenase (NADP(+))

substrate: L-Arogenate


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

substrate: NADP+


substrate_name: Prephenate

substrate: Prephenate


substrate_name: NADP(+)

assay_conditions_summary: cofactor NADP+

proof_lines:
PTGR1
LTB4 12-hydroxydehydrogenase
NADP+ as a cofactor

substrate: NADP(+)


smiles: CCC=CCCC=CC=O


organism: Medicago truncatula

assay_conditions_summary: pH 7; 318.15 K; cofactor NADPH

column_label: Table 1 MtANR row Cyanidin gives Km 12.9 uM, kcat 10.8 min^-1, kcat/Km 1.4 x 10^4 M^-1 s^-1.

row_label: MtANR / Cyanidin

table_label: Table 1. Kinetic properties of MtANR and AtANR


column_label: Table 1 MtANR row Delphinidin gives Km 49.8 uM, kcat 80.3 min^-1, kcat/Km 2.7 x 10^4 M^-1 s^-1.

row_label: MtANR / Delphinidin


organism: Bos taurus


substrate_name: pyruvate

substrate: pyruvate


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


enzyme_display_name: UniProt E4N096

organism: Kitasatospora setae

enzyme: UniProt E4N096


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


organism: Brassica napus

substrate_name: crotonyl-[acyl-carrier protein]

substrate: crotonyl-[acyl-carrier protein]


enzyme_display_name: aldehyde oxidase

substrate_name: benzaldehyde

proof_lines: pH 7.8, determined according to Eadie-Hofstee

proof_lines: pH 7.8, determined according to Lineweaver-Burk

enzyme: aldehyde oxidase

substrate: benzaldehyde


substrate_name: phenanthridine

substrate: phenanthridine


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


enzyme_display_name: crotonyl-CoA reductase

organism: Clostridioides difficile

substrate_name: butyryl-CoA

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: crotonyl-CoA reductase

substrate: butyryl-CoA


assay_conditions_summary: pH 7.5; cofactor NADH


substrate_name: Ferredoxin

substrate: Ferredoxin


enzyme_display_name: crotonyl-CoA carboxylase/reductase

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

enzyme: crotonyl-CoA carboxylase/reductase


assay_conditions_summary: pH 8; 303.15 K; cofactor CoA


enzyme_display_name: (+)-pulegone reductase

organism: Mentha x piperita

substrate_name: Unknown

enzyme: (+)-pulegone reductase

substrate: Unknown


enzyme_display_name: Crotonyl-CoA carboxylase/reductase

organism: Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.)

substrate_name: NADPH (in the reductive carboxylation assay)

proof_lines: kcat is 104 sec(-1) for the reductive carboxylation of (2E)-butenoyl-CoA (PubMed:17548827). Acryloyl-CoA is accepted as an alternative substrate analog by the enzyme with 40% relative activity (compared with Vmax of crotonyl-CoA carboxylati

enzyme: Crotonyl-CoA carboxylase/reductase


substrate_name: ethylmalonyl-CoA (in the oxidative decarboxylation assay)


substrate_name: trans-crotonyl-CoA

assay_conditions_summary: pH 6.8; 299.15 K; buffer 200 mM potassium phosphate; cofactor CoA

proof_lines: in 200 mM potassium phosphate buffer, pH 6.8, at 26°C

proof_lines: pH and temperature not specified in the publication

substrate: trans-crotonyl-CoA


substrate_name: NADPH

assay_conditions_summary: pH 6.8; 299.15 K; buffer 200 mM potassium phosphate; cofactor NADPH


organism: Streptomyces sp.

assay_conditions_summary: cofactor CoA

proof_lines: mutant enzyme V350G, pH and temperature not specified in the publication


proof_lines: mutant enzyme V350A, pH and temperature not specified in the publication


substrate_name: cinnamoyl-CoA

substrate: cinnamoyl-CoA


proof_lines: mutant enzyme V350F, pH and temperature not specified in the publication


proof_lines: mutant enzyme A182L, pH and temperature not specified in the publication


substrate_name: acryloyl-CoA (in the reductive carboxylation assay)


substrate_name: (+)-pulegone

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

assay_conditions_summary: pH 5

proof_lines:
pH 5.0, recombinant enzyme
pH 6.6

substrate: (+)-pulegone


assay_conditions_summary: pH 5; cofactor NADPH

substrate: NADPH


enzyme_display_name: acrylyl-CoA reductase (NADPH)

organism: Sulfolobus tokodaii

assay_conditions_summary: pH 6; 338.15 K; cofactor NADPH

column_label: Table 3. Molecular and catalytic properties of recombinant acryloyl-CoA reductase from S. tokodaii and 3-hydroxypropionyl-CoA dehydratase from M. sedula.; row S. tokodaii acryloyl-CoA reductase / NADPH apparent Km; column Turnover (s^-1); metric kcat; normalized value 13 s^-1 | Table 3. Molecular and catalytic properties of recombinant acryloyl-CoA reductase from S. tokodaii and 3-hydroxypropionyl-CoA dehydratase from M. sedula.; row S. tokodaii acryloyl-CoA reductase / NADPH apparent Km; column Apparent Km (uM); Turnover (s^-1); metric km; normalized value 0.036 mM | Table 3. Molecular and catalytic properties of recombinant acryloyl-CoA reductase from S. tokodaii and 3-hydroxypropionyl-CoA dehydratase from M. sedula.; row S. tokodaii acryloyl-CoA reductase / NADPH apparent Km; column Computed from exact turnover and Km cells; metric kcat_over_km; normalized value 361.11111111111114 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=13 normalized_unit=s^-1; km normalized_value=0.036 normalized_unit=mM; kcat_over_km normalized_value=361.11111111111114 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=13 raw_unit=s^-1; km raw_value=36 raw_unit=uM; converted to mM for export comparison; kcat_over_km raw_value=13/0.036 raw_unit=s^-1*mM^-1; computed from explicit turnover and apparent Km cells

enzyme: acrylyl-CoA reductase (NADPH)


substrate_name: acryloyl-CoA

assay_conditions_summary: pH 6; 338.15 K; cofactor CoA

substrate: acryloyl-CoA


enzyme_display_name: Trans-2-enoyl-CoA reductase

organism: Euglena gracilis

substrate_name: trans-2-hexenoyl-CoA (in the presence of NADH)

assay_conditions_summary: pH 6.2; cofactor NADH

column_label: Results section Catalytic Properties of Recombinant TER; substrate trans-2-hexenoyl-CoA using NADH; Km value = 91 +/- 1.8 uM.

raw_value_unit_evidence: Km 91 +/- 1.8 uM for trans-2-hexenoyl-CoA using NADH.

row_label: trans-2-hexenoyl-CoA using NADH

table_label: Results prose - Catalytic Properties of Recombinant TER

enzyme: Trans-2-enoyl-CoA reductase


enzyme_display_name: Crotonyl-CoA reductase

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

substrate_name: NADP (at 30 degrees Celsius and at pH 7.5)

assay_conditions_summary: pH 7.5; cofactor NADPH

proof_lines:
crotonyl-CoA reductase
Streptomyces collinus
NADPH

enzyme: Crotonyl-CoA reductase


substrate_name: crotonyl-CoA (at 30 degrees Celsius and at pH 7.5)

proof_lines:
crotonyl-CoA reductase
crotonyl-CoA
Streptomyces collinus


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


substrate_name: crotonyl-CoA


enzyme_display_name: (-)-isopiperitenone reductase

substrate_name: (-)-isopiperitenone

enzyme: (-)-isopiperitenone reductase

substrate: (-)-isopiperitenone


assay_conditions_summary: pH 5.5; cofactor NADPH


organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 6; cofactor NADPH

row_label: S. tokodaii acryloyl-CoA reductase / NADPH apparent Km

table_label: Table 3. Molecular and catalytic properties of recombinant acryloyl-CoA reductase from S. tokodaii and 3-hydroxypropionyl-CoA dehydratase from M. sedula.


organism: Streptomyces collinus

substrate_name: crotonyl-CoA (with NADP at pH 7.5)

column_label: PubMed abstract metric sentence gives Km for crotonyl-CoA as 18 microM, normalized to 0.018 mM

normalized_value_unit_evidence: PubMed abstract Km normalized_value=0.018 normalized_unit=mM

raw_value_unit_evidence: PubMed abstract: This enzyme exhibits a Km = 18 microM for crotonyl-CoA and 15 microM for NADPH

row_label: crotonyl-CoA reductase Km sentence

table_label: PubMed abstract

substrate: crotonyl-CoA (with NADP at pH 7.5)


organism: Escherichia coli

substrate_name: crotonyl CoA

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

proof_lines:
25°C, pH 8.0
at pH 7.5 and 30°C
pH 7.5, 22°C

substrate: crotonyl CoA


enzyme_display_name: prephenate dehydrogenase

enzyme: prephenate dehydrogenase


substrate_name: NAD+; Pyruvate; Coenzyme A

assay_conditions_summary: cofactor NAD+

substrate: NAD+; Pyruvate; Coenzyme A


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH


substrate_name: NAD+

substrate: NAD+


substrate_name: prephenate

substrate: prephenate


organism: Mentha piperita

column_label: PubMed abstract kinetic prose; metric K(m); (+)-pulegone reductase; (+)-pulegone; first value in respectively pair; K(m) values of 2.3 and 6.9 microM for (+)-pulegone and NADPH, respectively.

normalized_value_unit_evidence: Km=0.0023 mM after microM -> mM conversion from raw 2.3 microM.

raw_value_unit_evidence: PubMed abstract reports K(m) values of 2.3 and 6.9 microM for (+)-pulegone and NADPH, respectively.

table_label: PubMed abstract kinetic prose for recombinant peppermint monoterpene double-bond reductases


column_label: PubMed abstract kinetic prose; metric K(m); (+)-pulegone reductase; NADPH; second value in respectively pair; K(m) values of 2.3 and 6.9 microM for (+)-pulegone and NADPH, respectively.

normalized_value_unit_evidence: Km=0.0069 mM after microM -> mM conversion from raw 6.9 microM.


enzyme_display_name: acrylyl-CoA reductase (NADH)

organism: Clostridium kluyveri

assay_conditions_summary: pH 6.4; 295.15 K; buffer pH 6; cofactor CoA

proof_lines: in 0.1 M phosphate buffer pH 6.4, at 22°C

enzyme: acrylyl-CoA reductase (NADH)


substrate_name: ethyl vinyl ketone

smiles: CCC(=O)C=C

substrate: ethyl vinyl ketone


substrate_name: acrolein

substrate: acrolein


substrate_name: N-acetyl-S-acryloylcysteamine

substrate: N-acetyl-S-acryloylcysteamine


organism: Cereibacter sphaeroides

substrate_name: acrylyl-CoA

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: pH 7.0, 30°C, recombinant His-tagged enzyme

substrate: acrylyl-CoA


substrate_name: NADPH


column_label: PubMed abstract kinetic prose; metric K(m); (-)-isopiperitenone reductase; (-)-isopiperitenone; first value in respectively pair; K(m) values of 1.0 and 2.2 microM for (-)-isopiperitenone and NADPH, respectively.

normalized_value_unit_evidence: Km=0.001 mM after microM -> mM conversion from raw 1.0 microM.

raw_value_unit_evidence: PubMed abstract reports K(m) values of 1.0 and 2.2 microM for (-)-isopiperitenone and NADPH, respectively.


column_label: PubMed abstract kinetic prose; metric K(m); (-)-isopiperitenone reductase; NADPH; second value in respectively pair; K(m) values of 1.0 and 2.2 microM for (-)-isopiperitenone and NADPH, respectively.

normalized_value_unit_evidence: Km=0.0022 mM after microM -> mM conversion from raw 2.2 microM.


enzyme_display_name: Acryloyl-CoA reductase (NADH)

organism: Anaerotignum propionicum

substrate_name: acryloyl-CoA (with NADH as electron acceptor at pH 7.5 and 25 degrees Celsius)

assay_conditions_summary: pH 7.5; cofactor NADH

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: Acryloyl-CoA reductase (NADH)


substrate_name: NADH (at pH 7.5 and 25 degrees Celsius)

substrate: NADH (at pH 7.5 and 25 degrees Celsius)


substrate_name: propionyl-CoA (with of ferricenium hexafluorophosphate as electron acceptor at pH 7.5 and 25 degrees Celsius)

assay_conditions_summary: pH 7.5; cofactor CoA


substrate_name: butyryl-CoA (with of ferricenium hexafluorophosphate as electron acceptor at pH 7.5 and 25 degrees Celsius)


substrate_name: 3-buten-2-one (with NADH as electron acceptor at pH 7.5 and 25 degrees Celsius)

smiles: CC(=O)C=C


enzyme_display_name: dihydrolipoyl dehydrogenase

organism: Homo sapiens

substrate_name: Pyruvate; NAD+; Coenzyme A

enzyme: dihydrolipoyl dehydrogenase

substrate: Pyruvate; NAD+; Coenzyme A


substrate_name: Unknown

proof_lines:
wild-type, 30 min reaction time
wild-type, 10 min reaction time

substrate: Unknown


organism: Metallosphaera sedula

substrate_name: acryloyl-CoA

proof_lines: apparent value, recombinant enzyme, at pH 7.5 and 22°C

proof_lines: apparent value, Km less than 0.01 mM, recombinant enzyme, at pH 7.5 and 22°C


organism: Ruegeria pomeroyi


column_label: Official PMC full text Table 2 lists Ruegeria pomeroyi DSS-3 / SPO_1914 with apparent Km for NADPH (uM) = 18.

raw_value_unit_evidence: Table 2 row Ruegeria pomeroyi DSS-3 / SPO_1914 reports apparent Km for NADPH raw_value=18 raw_unit=uM.

row_label: Ruegeria pomeroyi DSS-3 / SPO_1914

table_label: PMC3807440 Table 2


organism: Artemisia annua

substrate_name: (+)-carvone

column_label: Table 1. Apparent kinetic parameters for Dbr2 row (+)-Carvone: Km 650 uM | kcat 0.86 s^-1 | kcat/Km 1.3 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.65 normalized_unit=mM; kcat normalized_value=0.86 normalized_unit=s^-1; kcat/Km ratio normalized_value=1.323076923076923 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=1.3 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1. Apparent kinetic parameters for Dbr2 row (+)-Carvone: Km raw_value=650 raw_unit=uM; kcat raw_value=0.86 raw_unit=s^-1; kcat/Km printed raw_value=1.3 raw_unit=mM^-1 s^-1.

row_label: Substrate/cofactor: (+)-Carvone

source_databases_merged: brenda skid uniprot

substrate: (+)-carvone


substrate_name: NADH

column_label: Table 1. Apparent kinetic parameters for Dbr2 row NADH: Km 770 uM | kcat 1.3 s^-1 | kcat/Km 1.7 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.77 normalized_unit=mM; kcat normalized_value=1.3 normalized_unit=s^-1; kcat/Km ratio normalized_value=1.688311688311688 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=1.7 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1. Apparent kinetic parameters for Dbr2 row NADH: Km raw_value=770 raw_unit=uM; kcat raw_value=1.3 raw_unit=s^-1; kcat/Km printed raw_value=1.7 raw_unit=mM^-1 s^-1.

row_label: Substrate/cofactor: NADH

substrate: NADH


column_label: Table 1. Apparent kinetic parameters for Dbr2 row 2-Cyclohexen-1-one: Km 790 uM | kcat 1.8 s^-1 | kcat/Km 2.3 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.79 normalized_unit=mM; kcat normalized_value=1.8 normalized_unit=s^-1; kcat/Km ratio normalized_value=2.278481012658228 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=2.3 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1. Apparent kinetic parameters for Dbr2 row 2-Cyclohexen-1-one: Km raw_value=790 raw_unit=uM; kcat raw_value=1.8 raw_unit=s^-1; kcat/Km printed raw_value=2.3 raw_unit=mM^-1 s^-1.

row_label: Substrate/cofactor: 2-Cyclohexen-1-one


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

column_label: Table 1. Apparent kinetic parameters for Dbr2 row NADPH: Km 95 uM | kcat 2.5 s^-1 | kcat/Km 26 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.095 normalized_unit=mM; kcat normalized_value=2.5 normalized_unit=s^-1; kcat/Km ratio normalized_value=26.31578947368421 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=26 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1. Apparent kinetic parameters for Dbr2 row NADPH: Km raw_value=95 raw_unit=uM; kcat raw_value=2.5 raw_unit=s^-1; kcat/Km printed raw_value=26 raw_unit=mM^-1 s^-1.

row_label: Substrate/cofactor: NADPH

substrate: NADPH


substrate_name: artemisinic aldehyde

column_label: Table 1. Apparent kinetic parameters for Dbr2 row Artemisinic aldehyde: Km 19 uM | kcat 2.6 s^-1 | kcat/Km 140 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.019 normalized_unit=mM; kcat normalized_value=2.6 normalized_unit=s^-1; kcat/Km ratio normalized_value=136.8421052631579 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=140 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1. Apparent kinetic parameters for Dbr2 row Artemisinic aldehyde: Km raw_value=19 raw_unit=uM; kcat raw_value=2.6 raw_unit=s^-1; kcat/Km printed raw_value=140 raw_unit=mM^-1 s^-1.

substrate: artemisinic aldehyde


enzyme_display_name: UniProt P61431

organism: Staphylococcus aureus

enzyme: UniProt P61431


enzyme_display_name: acryloyl-CoA reductase (NADH)

organism: Clostridium propionicum

smiles: C=CC(C)=O

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

column_label: PubMed abstract metric prose for 3-buten-2-one: Km 1800 uM and kcat 29 s^-1 at 300 uM NADH.

normalized_value_unit_evidence: Km normalized_value=1.8 normalized_unit=mM; kcat normalized_value=29.0 normalized_unit=s^-1; kcat/Km normalized_value=16.11111111111111 normalized_unit=s^-1*mM^-1 calculated from same-prose kcat 29.0 s^-1 / Km 1.8 mM

raw_value_unit_evidence: Km raw_value=1800 raw_unit=uM; kcat raw_value=29 raw_unit=s^-1; kcat/Km calculated from same-prose kcat and Km

row_label: 3-buten-2-one (methyl vinyl ketone)

table_label: PubMed abstract metric-labeled prose

enzyme: acryloyl-CoA reductase (NADH)


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


substrate_name: Propanoyl-CoA

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

column_label: PubMed abstract metric prose for propionyl-CoA: Km 50 uM and kcat 2.0 s^-1 with ferricenium acceptor.

normalized_value_unit_evidence: Km normalized_value=0.05 normalized_unit=mM; kcat normalized_value=2.0 normalized_unit=s^-1; kcat/Km normalized_value=40.0 normalized_unit=s^-1*mM^-1 calculated from same-prose kcat 2.0 s^-1 / Km 0.05 mM

raw_value_unit_evidence: Km raw_value=50 raw_unit=uM; kcat raw_value=2.0 raw_unit=s^-1; kcat/Km calculated from same-prose kcat and Km

row_label: propionyl-CoA (expected sheet synonym: propanoyl-CoA)

substrate: Propanoyl-CoA


assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

column_label: PubMed abstract metric prose for acryloyl-CoA: Km 2 +/- 1 uM and kcat 4.5 s^-1 at 100 uM NADH.

normalized_value_unit_evidence: Km normalized_value=0.002 normalized_unit=mM; kcat normalized_value=4.5 normalized_unit=s^-1; kcat/Km normalized_value=2250.0 normalized_unit=s^-1*mM^-1 calculated from same-prose kcat 4.5 s^-1 / Km 0.002 mM

raw_value_unit_evidence: Km raw_value=2 raw_unit=uM; kcat raw_value=4.5 raw_unit=s^-1; kcat/Km calculated from same-prose kcat and Km

row_label: acryloyl-CoA

substrate: acryloyl-CoA


substrate_name: butanoyl-CoA

column_label: PubMed abstract metric prose for butyryl-CoA: Km 100 uM and kcat 3.5 s^-1 with ferricenium acceptor.

normalized_value_unit_evidence: Km normalized_value=0.1 normalized_unit=mM; kcat normalized_value=3.5 normalized_unit=s^-1; kcat/Km normalized_value=35.0 normalized_unit=s^-1*mM^-1 calculated from same-prose kcat 3.5 s^-1 / Km 0.1 mM

raw_value_unit_evidence: Km raw_value=100 raw_unit=uM; kcat raw_value=3.5 raw_unit=s^-1; kcat/Km calculated from same-prose kcat and Km

row_label: butyryl-CoA (expected sheet synonym: butanoyl-CoA)

substrate: butanoyl-CoA


enzyme_display_name: oxalate oxidase

organism: Hordeum vulgare

substrate_name: oxalic acid

assay_conditions_summary: pH 4

enzyme: oxalate oxidase

substrate: oxalic acid


substrate_name: oxalate

proof_lines: oxalate oxidase activity is measured by oxygen uptake assay with a Clark oxygen electrode in a thermostated cell (25°C). The Km evalutated from initial velocity data exhibits a strong pH dependence with limiting slopes (versus pH) of 0.9 (b

substrate: oxalate


enzyme_display_name: artemisinic aldehyde Delta(11(13)) reductase

table_label: Table 1. Apparent kinetic parameters for Dbr2


enzyme: artemisinic aldehyde Delta(11(13)) reductase


enzyme_display_name: 2-alkenal reductase (NADP+)

organism: Plagiochasma appendiculatum

substrate_name: 4-coumaryl aldehyde

proof_lines: pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56V

enzyme: 2-alkenal reductase (NADP+)

substrate: 4-coumaryl aldehyde


substrate_name: caffeoyl aldehyde

substrate: caffeoyl aldehyde


proof_lines: pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR1

proof_lines: pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR2


substrate_name: coniferyl aldehyde

substrate: coniferyl aldehyde


proof_lines: pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56Y


substrate_name: 5-hydroxyconiferyl aldehyde

substrate: 5-hydroxyconiferyl aldehyde


assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA


substrate_name: crotonyl-N-acetylcysteamine

substrate: crotonyl-N-acetylcysteamine


substrate_name: acrylyl-CoA

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

column_label: Results prose adjacent to Table 2 explicitly states kcat 80 s^-1 and apparent acrylyl-CoA Km 1.5 uM for the Rhodobacter sphaeroides AcuI acrylyl-CoA measurement.

raw_value_unit_evidence: Results prose: kcat (turnover) 80 s^-1 and apparent acrylyl-CoA Km 1.5 uM; no independently printed kcat/Km cell.

row_label: Rhodobacter sphaeroides 2.4.1 RSP_1434 (AcuI)

table_label: Results prose adjacent to Table 2

substrate: acrylyl-CoA


organism: Rattus norvegicus

substrate_name: NADPH

assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADPH

proof_lines: with trans-2-nonenal as cosubstrate, in 100 mM Tris (pH 7.2), at 25°C

proof_lines: with trans-3-nonen-2-one as cosubstrate, in 100 mM Tris (pH 7.2), at 25°C


organism: Nicotiana tabacum

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines:
dehydrogenation, pH 8.0, 35°C, NADP+
pH 8.0, 35°C, NADP+


assay_conditions_summary: pH 7.4; cofactor NADP+

proof_lines: hydrogenation to (1R,2S,4S)-neoisodihydrocarveol, pH 7.4, 35°C, NADP+


substrate_name: (S)-carvone

proof_lines: hydrogenation to (2R,4S)-carveol, pH 7.4, 35°C, NADP+

proof_lines: hydrogenation to (2R,4R)-carveol, pH 7.4, 35°C, NADP+

proof_lines: hydrogenation to (2S,4S)-carveol, pH 7.4, 35°C, NADP+

substrate: (S)-carvone


enzyme_display_name: chanoclavine-I aldehyde reductase

organism: Aspergillus fumigatus

substrate_name: chanoclavine-I aldehyde

proof_lines: pH and temperature not specified in the publication

enzyme: chanoclavine-I aldehyde reductase

substrate: chanoclavine-I aldehyde


assay_conditions_summary: cofactor NADPH


substrate_name: Unknown

substrate: Unknown


smiles: CCCCCC(=O)C=C

proof_lines:
app. Kcat, pH 7.3 and 25°C
app. Kcat, pH 5.4 and 25°C


smiles: CCC(=CC=O)C

proof_lines:
app. Kcat, pH 7.3 and 25°C
app. Kcat, pH 5.4 and 25°C
app. Km value, pH 7.3 and 25°C


substrate_name: trans-cinnamaldehyde

proof_lines:
app. Kcat, pH 7.3 and 25°C
value above, app. Kcat, pH 5.4 and 25°C
app. Km value, pH 7.3 and 25°C

substrate: trans-cinnamaldehyde


assay_conditions_summary: pH 7.3; cofactor NADPH

proof_lines: app. Kcat, pH 7.3 and 25°C, with 1-nitrocyclohexene

proof_lines: app. Km value, pH 5.4 and 25°C, with 1-nitrocyclohexene

proof_lines: kcat is 3.3 sec(-1) for (R)-pulegone at pH 7.0. kcat is 2.8 sec(-1) for (S)-pulegone at pH 7.0. kcat is 1.3 sec(-1) for NADPH at pH 7.3. kcat is 1.46 sec(-1) for 1-nitrocyclohexene at pH 7.3. kcat is 9.2 sec(-1) for 2-methylpentenal at pH 5

substrate: NADPH


substrate_name: (S)-pulegone

substrate: (S)-pulegone


enzyme_display_name: 2-alkenal reductase (NADP(+)-dependent)

substrate_name: 2-methylpentenal (at pH 5.4)

smiles: CCC=C(C)C=O

assay_conditions_summary: pH 5; cofactor NADPH

enzyme: 2-alkenal reductase (NADP(+)-dependent)

substrate: 2-methylpentenal (at pH 5.4)


organism: uncultured bacterium pBF1

substrate_name: crotonyl-CoA

sequence_source: paper_backed_accession:AOR51268.1 (PMID:29891603; FabL2 ENR protein sequence)

assay_conditions_summary: pH 7; cofactor CoA

substrate: crotonyl-CoA


assay_conditions_summary: pH 7; cofactor NADPH


enzyme_display_name: 2-haloacrylate reductase

organism: Burkholderia sp.

assay_conditions_summary: pH 8; cofactor NADPH

proof_lines:
NADPH-dependent reduction
Burkholderia sp. WS
2-chloroacrylate

enzyme: 2-haloacrylate reductase


assay_conditions_summary: pH 8

proof_lines:
2-bromoacrylate
NADPH-dependent reduction
Burkholderia sp. WS


proof_lines:
2-chloroacrylate
NADPH-dependent reduction
Burkholderia sp. WS


enzyme_display_name: UDP-N-acetylmuramate dehydrogenase

organism: Escherichia coli

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

column_label: Table 3 row 3'-NADPH gives Km 250 +/- 50 uM and kcat 49 +/- 6 s^-1, matching row after unit conversion and derived kcat/Km.

raw_value_unit_evidence: Table 3 row 3'-NADPH reports Km 250 +/- 50 uM and kcat 49 +/- 6 s^-1.

table_label: Table 3: Kinetic Constants for Analogs of NADPH as Alternate Substrates

enzyme: UDP-N-acetylmuramate dehydrogenase


substrate_name: alpha-NADPH

column_label: Table 3 row a-NADPH gives Km 780 +/- 120 uM and kcat 42 +/- 3 s^-1, matching row alpha-NADPH after unit conversion and derived kcat/Km.

raw_value_unit_evidence: Table 3 row a-NADPH reports Km 780 +/- 120 uM and kcat 42 +/- 3 s^-1.

row_label: a-NADPH

substrate: alpha-NADPH


assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH

column_label: Table 4 pH 8.0 row gives Km.NADPH 17 +/- 3 uM, matching expected 0.017 mM.

raw_value_unit_evidence: Table 4 pH 8.0 row reports Km.NADPH 17 +/- 3 uM.

row_label: pH 8.0 / NADPH

table_label: Table 4: Kinetic Constants for Ping Pong Bi Bi Mechanism with Double Substrate Inhibition


enzyme_display_name: Enoyl-[acyl-carrier-protein] reductase [NADPH] FabL

organism: Bacillus subtilis (strain 168)

column_label: Primary-paper page 3 states YgaA had a Km of 16 uM for NADPH.

raw_value_unit_evidence: YgaA had a Km of 16 uM for NADPH

row_label: YgaA/FabL NADPH Km sentence

table_label: Characterization of the Reductases prose and Figure 2 cofactor utilization


enzyme_display_name: 2-alkenal reductase (NADP(+))

substrate_name: (R)-pulegone

enzyme: 2-alkenal reductase (NADP(+))

substrate: (R)-pulegone


assay_conditions_summary: pH 7.3; 298.15 K; cofactor NADPH

column_label: Official PMC Table 1 image row 1a pH 7.3 columns App. kcat, App. Km, and kcat/Km.

normalized_value_unit_evidence: Central values normalize to kcat 1.46 s^-1; Km 0.057 mM; kcat/Km 25.6 s^-1 mM^-1; all match the exported row.

table_label: Table 1. Steady-State Kinetic Parameters of NtDBR with a Variety of Substrates


substrate_name: UDP-N-acetylenolpyruvylglucosamine

proof_lines: 10 mM Mg2+, 50 mM Tris-HCl, at pH 8.0, temperature not specified in the publication

proof_lines: 10 mM Mg2+, 50 mM Tris-HCl, at pH 8.0 temperature not specified in the publication

substrate: UDP-N-acetylenolpyruvylglucosamine


proof_lines: in 10 mM PIPES-NaOH (pH 7.0), 3 mM KCl, 2 mM dithiothreitol, 1 mM MgCl, temperature not specified in the publication


organism: Mycobacterium tuberculosis


organism: Streptococcus pneumoniae


organism: Enterobacter cloacae


enzyme_display_name: pyruvate oxidase

organism: Lactiplantibacillus plantarum

substrate_name: pyruvate

assay_conditions_summary: buffer phosphate

enzyme: pyruvate oxidase

substrate: pyruvate


substrate_name: arsenate

substrate: arsenate


organism: Lathyrus oleraceus


enzyme_display_name: indole-3-acetaldehyde oxidase

enzyme: indole-3-acetaldehyde oxidase


enzyme_display_name: formylmethanofuran dehydrogenase

organism: Methanosarcina barkeri

substrate_name: formylmethanofuran

proof_lines: value below, methylviologen, molybdenum enzyme

enzyme: formylmethanofuran dehydrogenase

substrate: formylmethanofuran


substrate_name: N-Furfurylformamide

proof_lines:
furfurylformamide
molybdenum enzyme

substrate: N-Furfurylformamide


enzyme_display_name: enoyl-[acyl-carrier-protein] reductase

organism: Homo sapiens

column_label: Table 2. Kinetic parameters of the wild-type MECR/ETR1; row (2E)-Dodecenoyl-CoA (C12); columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: Km normalized_value=0.0036 normalized_unit=mM; kcat normalized_value=3.6 normalized_unit=s^-1; kcat/Km normalized_value=990 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: (2E)-Dodecenoyl-CoA (C12): Km raw_value=3.6 raw_unit=uM; kcat raw_value=3.6 raw_unit=s^-1; kcat/Km raw_value=9.9 x 10^5 raw_unit=M^-1 s^-1

row_label: (2E)-Dodecenoyl-CoA (C12)

enzyme: enoyl-[acyl-carrier-protein] reductase


column_label: Table 2. Kinetic parameters of the wild-type MECR/ETR1; row (2E)-Decenoyl-CoA (C10); columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: Km normalized_value=0.0104 normalized_unit=mM; kcat normalized_value=1.7 normalized_unit=s^-1; kcat/Km normalized_value=160 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: (2E)-Decenoyl-CoA (C10): Km raw_value=10.4 raw_unit=uM; kcat raw_value=1.7 raw_unit=s^-1; kcat/Km raw_value=1.6 x 10^5 raw_unit=M^-1 s^-1

row_label: (2E)-Decenoyl-CoA (C10)


column_label: Table 2 row Wild type, C6 columns: Km = 63.5 +/- 2.5 uM, kcat = 2.2 +/- 0.04 s^-1, kcat/Km = 0.4 x 10^5 M^-1 s^-1; exported Km is 0.064 mM and exported kcat/Km is 34.375 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.0635 mM; kcat normalized_value=2.2 s^-1; kcat/Km normalized_value=40 s^-1*mM^-1

row_label: Wild type / (2E)-Hexenoyl-CoA C6

table_label: ScienceDirect PMID 18479707 Table 2


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F324Y with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G165S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADPH

column_label: Table 4 row G165S / (2E)-Hexadecenoyl-CoA (C16); columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 4 row G165S / (2E)-Hexadecenoyl-CoA (C16): Km 7.5 uM, kcat 0.4 s^-1, catalytic efficiency 5.3 x 10^4 M^-1 s^-1.

row_label: G165S / (2E)-Hexadecenoyl-CoA (C16)

table_label: Table 4. Kinetic parameters of the wild type and the pocket variants having mutations lining the substrate binding pocket


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I129M to reconstruct the assayed variant sequence.

column_label: Table 4 row I129M / (2E)-Hexadecenoyl-CoA (C16); columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 4 row I129M / (2E)-Hexadecenoyl-CoA (C16): Km 4.9 uM, kcat 1.2 s^-1, catalytic efficiency 2.4 x 10^5 M^-1 s^-1.

row_label: I129M / (2E)-Hexadecenoyl-CoA (C16)


assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA

column_label: Table 2. Kinetic parameters of the wild-type MECR/ETR1; row (2E)-Hexadecenoyl-CoA (C16); columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: Km normalized_value=0.0066 normalized_unit=mM; kcat normalized_value=2.0 normalized_unit=s^-1; kcat/Km normalized_value=300 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: (2E)-Hexadecenoyl-CoA (C16): Km raw_value=6.6 raw_unit=uM; kcat raw_value=2.0 raw_unit=s^-1; kcat/Km raw_value=3.0 x 10^5 raw_unit=M^-1 s^-1

row_label: (2E)-Hexadecenoyl-CoA (C16)


column_label: Table 4 row G165S / (2E)-Octenoyl-CoA (C8); columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 4 row G165S / (2E)-Octenoyl-CoA (C8): Km 2.4 uM, kcat 1.5 s^-1, catalytic efficiency 6.3 x 10^5 M^-1 s^-1.

row_label: G165S / (2E)-Octenoyl-CoA (C8)


column_label: Table 4 row I129M / (2E)-Octenoyl-CoA (C8); columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 4 row I129M / (2E)-Octenoyl-CoA (C8): Km 14.1 uM, kcat 8.7 s^-1, catalytic efficiency 6.2 x 10^5 M^-1 s^-1.

row_label: I129M / (2E)-Octenoyl-CoA (C8)


organism: Methanothermobacter thermautotrophicus

substrate_name: methylviologen

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

substrate: methylviologen


organism: Staphylococcus aureus

assay_conditions_summary: pH 8; 295.15 K; cofactor NADPH


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


organism: Methanothermobacter wolfeii

substrate_name: formate

substrate: formate


enzyme_display_name: butanoyl-CoA dehydrogenase complex (NAD(+), ferredoxin)

organism: Clostridioides difficile

substrate_name: butanoyl-CoA

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

substrate: butanoyl-CoA


enzyme_display_name: butanoyl-CoA dehydrogenase complex (NAD+, ferredoxin)


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

organism: Fragaria x ananassa

assay_conditions_summary: pH 7; 303.15 K; cofactor NADH

proof_lines: 0.1 M Na2HPO4/NaH2PO4, pH 7, 30°C, cofactor NADH

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


enzyme_display_name: anaerobic carbon monoxide dehydrogenase

organism: Methanosarcina thermophila

substrate_name: Trichloroethylene

smiles: C(=C(Cl)Cl)Cl

enzyme: anaerobic carbon monoxide dehydrogenase

substrate: Trichloroethylene


enzyme_display_name: UniProt P9WGR1

enzyme: UniProt P9WGR1


substrate_name: NADH

substrate: NADH


organism: Streptomyces collinus


organism: Acidaminococcus fermentans

assay_conditions_summary: pH 7; cofactor NADH

proof_lines: pH 7, temperature not specified in the publication

enzyme: butanoyl-CoA dehydrogenase complex (NAD+, ferredoxin)


organism: Fragaria ananassa

assay_conditions_summary: cofactor NADH


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH


organism: Fragaria vesca

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

assay_conditions_summary: pH 5; 303.15 K; cofactor NADPH


assay_conditions_summary: pH 5; 303.15 K; cofactor NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S85A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

column_label: Table 3 row S85A / (2E)-Octenoyl-CoA; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 3 row S85A / (2E)-Octenoyl-CoA: Km 22.3 uM, kcat 2.1 s^-1, catalytic efficiency 9.4 x 10^4 M^-1 s^-1.

row_label: S85A / (2E)-Octenoyl-CoA

table_label: Table 3. Kinetic parameters of the wild type and MECR/ETR1 variants, with mutations near the catalytic cavity


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T170A with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.

column_label: Table 3 row T170A / (2E)-Octenoyl-CoA; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 3 row T170A / (2E)-Octenoyl-CoA: Km 16.3 uM, kcat 1.5 s^-1, catalytic efficiency 9.1 x 10^4 M^-1 s^-1.

row_label: T170A / (2E)-Octenoyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W311A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W311L with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 3 row W311L / (2E)-Octenoyl-CoA; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 3 row W311L / (2E)-Octenoyl-CoA: Km 34.1 uM, kcat 1.4 s^-1, catalytic efficiency 4.0 x 10^4 M^-1 s^-1.

row_label: W311L / (2E)-Octenoyl-CoA


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

column_label: Table 2. Kinetic parameters of the wild-type MECR/ETR1; row (2E)-Octenoyl-CoA (C8); columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: Km normalized_value=0.0102 normalized_unit=mM; kcat normalized_value=3.0 normalized_unit=s^-1; kcat/Km normalized_value=290 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: (2E)-Octenoyl-CoA (C8): Km raw_value=10.2 raw_unit=uM; kcat raw_value=3.0 raw_unit=s^-1; kcat/Km raw_value=2.9 x 10^5 raw_unit=M^-1 s^-1

row_label: (2E)-Octenoyl-CoA (C8)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y94F to reconstruct the assayed variant sequence.

column_label: Table 3 row Y94F / (2E)-Octenoyl-CoA; columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 3 row Y94F / (2E)-Octenoyl-CoA: Km 78.5 uM, kcat 0.011 s^-1, catalytic efficiency 1.4 x 10^2 M^-1 s^-1.

row_label: Y94F / (2E)-Octenoyl-CoA


column_label: Table 4 row G165S / (2E)-Tetradecenoyl-CoA (C14); columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 4 row G165S / (2E)-Tetradecenoyl-CoA (C14): Km 6.4 uM, kcat 0.6 s^-1, catalytic efficiency 9.3 x 10^4 M^-1 s^-1.

row_label: G165S / (2E)-Tetradecenoyl-CoA (C14)


column_label: Table 4 row I129M / (2E)-Tetradecenoyl-CoA (C14); columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 4 row I129M / (2E)-Tetradecenoyl-CoA (C14): Km 12.0 uM, kcat 4.3 s^-1, catalytic efficiency 3.6 x 10^5 M^-1 s^-1.

row_label: I129M / (2E)-Tetradecenoyl-CoA (C14)


column_label: Table 2. Kinetic parameters of the wild-type MECR/ETR1; row (2E)-Tetradecenoyl-CoA (C14); columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: Km normalized_value=0.0043 normalized_unit=mM; kcat normalized_value=1.4 normalized_unit=s^-1; kcat/Km normalized_value=340 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: (2E)-Tetradecenoyl-CoA (C14): Km raw_value=4.3 raw_unit=uM; kcat raw_value=1.4 raw_unit=s^-1; kcat/Km raw_value=3.4 x 10^5 raw_unit=M^-1 s^-1

row_label: (2E)-Tetradecenoyl-CoA (C14)


enzyme_display_name: meromycolic acid enoyl-[acyl-carrier-protein] reductase

organism: Mycobacterium tuberculosis

substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

proof_lines: pH 7.0, temperature not specified in the publication

substrate: Unknown