sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature I54V with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '2,4-Dichloro-cis,cis-muconate', enzyme column group 'I54V'; column 'Km (uM)' = 93; column 'kcat (min^-1)' = 7.2; column 'kcat/Km (min^-1 uM^-1)' = 0.078.

raw_value_unit_evidence: Table 3, substrate row 2,4-Dichloro-cis,cis-muconate, enzyme column I54V: Km = 93 uM; kcat = 7.2 min^-1; printed kcat/Km = 0.078 min^-1 uM^-1.


enzyme_display_name: muconate cycloisomerase

organism: Pseudomonas putida

source_db: oed

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I54V/F329I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

data_origin: experimental

enzyme: muconate cycloisomerase

source: oed


verification_status: unverified

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +3, so it is treated as a source-provided variant sequence.

mutation_type: substitution

status: unverified


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature L333V with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '2,4-Dichloro-cis,cis-muconate', enzyme column group 'L333V'; column 'Km (uM)' = 39; column 'kcat (min^-1)' = 0.88; column 'kcat/Km (min^-1 uM^-1)' = 0.022.

raw_value_unit_evidence: Table 3, substrate row 2,4-Dichloro-cis,cis-muconate, enzyme column L333V: Km = 39 uM; kcat = 0.88 min^-1; printed kcat/Km = 0.022 min^-1 uM^-1.

table_label: Table 3: Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates (Appl. Environ. Microbiol. 1998, 64(9):3290-3299)

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A271S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +11, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature I54V/F329I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '2-Chloro-cis,cis-muconate', enzyme column group 'I54V-F329I'; column 'Km (uM)' = 33; column 'kcat (min^-1)' = 10; column 'kcat/Km (min^-1 uM^-1)' = 0.32.

raw_value_unit_evidence: Table 3, substrate row 2-Chloro-cis,cis-muconate, enzyme column I54V-F329I: Km = 33 uM; kcat = 10 min^-1; printed kcat/Km = 0.32 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature K276N with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '2-Chloro-cis,cis-muconate', enzyme column group 'K276N'; column 'Km (uM)' = 34; column 'kcat (min^-1)' = 3.2; column 'kcat/Km (min^-1 uM^-1)' = 0.095.

raw_value_unit_evidence: Table 3, substrate row 2-Chloro-cis,cis-muconate, enzyme column K276N: Km = 34 uM; kcat = 3.2 min^-1; printed kcat/Km = 0.095 min^-1 uM^-1.


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


verification_status: verified

mutation_signature: Unknown

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

column_label: PMID 9726873 TABLE 3. Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates; row 2-Chloro-cis,cis-muconate / wild-type enzyme column group (TABLE 3); wild-type enzyme column group, sub-columns Km (uM), kcat (min^-1) and kcat/Km (min^-1 uM^-1); printed cells Km 59 ± 5 uM, kcat 49 ± 2 min^-1, kcat/Km 0.83 min^-1 uM^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.817 s^-1 / 0.059 mM = 13.847457627118644 s^-1 mM^-1), not as the paper's rounded printed kcat/Km cell (0.83 min^-1 uM^-1), which agrees with that quotient at the printed cell's precision.

normalized_value_unit_evidence: metric: Km; normalized value: 0.059 mM; metric: kcat; normalized value: 0.817 s^-1; metric: kcat/Km; normalized value: 13.847457627118644 s^-1 mM^-1; assay condition: Kinetic assay at pH 7.5 in 30 mM Tris-HCl with 1 mM MnSO4 at 25 degrees C, followed spectrophotometrically at 260 nm; purified wild-type P. putida PRS2000 muconate cycloisomerase, the TABLE 3 wild-type enzyme column group; kcat computed for a subunit molecular mass of 40 kDa

raw_value_unit_evidence: Table row as printed: Km 59 ± 5 uM; kcat 49 ± 2 min^-1; kcat/Km 0.83 min^-1 uM^-1 (wild-type enzyme column group).

status: verified


enzyme_display_name: carboxy-cis,cis-muconate cyclase

organism: Neurospora crassa

substrate_name: cis,cis-muconate

source_db: brenda

enzyme: carboxy-cis,cis-muconate cyclase

substrate: cis,cis-muconate

source: brenda


sequence_variant_note: Mutation signature I59W could not be applied safely because the resolved sequence does not match the expected reference residue(s).


column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '3-Fluoro-cis,cis-muconate', enzyme column group 'K276N'; column 'Km (uM)' = 230; column 'kcat (min^-1)' = 5,200; column 'kcat/Km (min^-1 uM^-1)' = 22.

raw_value_unit_evidence: Table 3, substrate row 3-Fluoro-cis,cis-muconate, enzyme column K276N: Km = 230 uM; kcat = 5,200 min^-1; printed kcat/Km = 22 min^-1 uM^-1.


column_label: PMID 9726873 TABLE 3. Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates; row 3-Fluoro-cis,cis-muconate / wild-type enzyme column group (TABLE 3); wild-type enzyme column group, sub-columns Km (uM), kcat (min^-1) and kcat/Km (min^-1 uM^-1); printed cells Km 97 ± 21 uM, kcat 8,900 ± 1,000 min^-1, kcat/Km 92 min^-1 uM^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (148.333 s^-1 / 0.097 mM = 1529.2061855670102 s^-1 mM^-1), not as the paper's rounded printed kcat/Km cell (92 min^-1 uM^-1), which agrees with that quotient at the printed cell's precision.

normalized_value_unit_evidence: metric: Km; normalized value: 0.097 mM; metric: kcat; normalized value: 148.333 s^-1; metric: kcat/Km; normalized value: 1529.2061855670102 s^-1 mM^-1; assay condition: Kinetic assay at pH 7.5 in 30 mM Tris-HCl with 1 mM MnSO4 at 25 degrees C, followed spectrophotometrically at 260 nm; purified wild-type P. putida PRS2000 muconate cycloisomerase, the TABLE 3 wild-type enzyme column group; kcat computed for a subunit molecular mass of 40 kDa

raw_value_unit_evidence: Table row as printed: Km 97 ± 21 uM; kcat 8,900 ± 1,000 min^-1; kcat/Km 92 min^-1 uM^-1 (wild-type enzyme column group).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature A271S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '3-Methyl-cis,cis-muconate', enzyme column group 'A271S'; column 'Km (uM)' = 9.7; column 'kcat (min^-1)' = 680; column 'kcat/Km (min^-1 uM^-1)' = 71.

normalized_value_unit_evidence: Km: printed 9.7 uM; 9.7 / 1000 = 0.0097 mM, carried here at the exported precision as 0.01 mM. kcat: printed 680 min^-1; 680 / 60 = 11.333333 s^-1, carried here at the exported precision as 11.333 s^-1. kcat/Km: printed 71 min^-1 uM^-1; one min^-1 uM^-1 is 1000 / 60 = 16.666667 s^-1 mM^-1, so 71 x 1000 / 60 = 1183.333333 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate row 3-Methyl-cis,cis-muconate, enzyme column A271S: Km = 9.7 uM; kcat = 680 min^-1; printed kcat/Km = 71 min^-1 uM^-1.


column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '3-Methyl-cis,cis-muconate', enzyme column group 'I54V'; column 'Km (uM)' = 7.2; column 'kcat (min^-1)' = 740; column 'kcat/Km (min^-1 uM^-1)' = 100.

raw_value_unit_evidence: Table 3, substrate row 3-Methyl-cis,cis-muconate, enzyme column I54V: Km = 7.2 uM; kcat = 740 min^-1; printed kcat/Km = 100 min^-1 uM^-1.


column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '3-Methyl-cis,cis-muconate', enzyme column group 'I54V-F329I'; column 'Km (uM)' = 6.4; column 'kcat (min^-1)' = 310; column 'kcat/Km (min^-1 uM^-1)' = 49.

normalized_value_unit_evidence: Km: printed 6.4 uM; 6.4 / 1000 = 0.0064 mM, carried here at the exported precision as 0.006 mM. kcat: printed 310 min^-1; 310 / 60 = 5.166667 s^-1, carried here at the exported precision as 5.167 s^-1. kcat/Km: printed 49 min^-1 uM^-1; one min^-1 uM^-1 is 1000 / 60 = 16.666667 s^-1 mM^-1, so 49 x 1000 / 60 = 816.666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate row 3-Methyl-cis,cis-muconate, enzyme column I54V-F329I: Km = 6.4 uM; kcat = 310 min^-1; printed kcat/Km = 49 min^-1 uM^-1.


column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '3-Methyl-cis,cis-muconate', enzyme column group 'K276N'; column 'Km (uM)' = 12; column 'kcat (min^-1)' = 95; column 'kcat/Km (min^-1 uM^-1)' = 8.2.

raw_value_unit_evidence: Table 3, substrate row 3-Methyl-cis,cis-muconate, enzyme column K276N: Km = 12 uM; kcat = 95 min^-1; printed kcat/Km = 8.2 min^-1 uM^-1.


organism: Pseudomonas reinekei

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


enzyme_display_name: inositol-3-phosphate synthase

organism: Corynebacterium glutamicum

substrate_name: D-glucose 6-phosphate

sequence_source: multiple

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

proof_lines: recombinant enzyme expressed in Escherichia coli BL21(DE3) cells, at pH 7.5 and 37°C

proof_lines: kcat is 2.24 for D-glucose 6-phosphate (at 37 degrees Celsius and pH 7.5).

source_databases_merged: brenda uniprot

enzyme: inositol-3-phosphate synthase

substrate: D-glucose 6-phosphate


enzyme_display_name: chalcone isomerase

organism: Citrus sinensis

substrate_name: liquiritigenin

kcat_display: Not reported

kcat_over_km_display: Not reported

enzyme: chalcone isomerase

substrate: liquiritigenin


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


column_label: Table 4. Kinetic constant of the following enzyme; row A271S / 2-Methyl-cis,cis-muconate; columns A271S Km (uM), A271S kcat (min^-1), and A271S kcat/Km (min^-1 uM^-1); cells Km=59 +/- 5, kcat=6400 +/- 200, printed kcat/Km=110.

normalized_value_unit_evidence: kcat normalized_value=106.667 normalized_unit=s^-1; Km normalized_value=0.059 normalized_unit=mM; kcat/Km normalized_value=1807.91525423729 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row A271S / 2-Methyl-cis,cis-muconate: Km 59 +/- 5 uM; kcat 6400 +/- 200 min^-1; printed kcat/Km 110 min^-1 uM^-1.

row_label: A271S / 2-Methyl-cis,cis-muconate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature F329I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '2-Methyl-cis,cis-muconate', enzyme column group 'F329I'; column 'Km (uM)' = 68; column 'kcat (min^-1)' = 10,000; column 'kcat/Km (min^-1 uM^-1)' = 150.

raw_value_unit_evidence: Table 3, substrate row 2-Methyl-cis,cis-muconate, enzyme column F329I: Km = 68 uM; kcat = 10,000 min^-1; printed kcat/Km = 150 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I54V with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic constant of the following enzyme; row I54V / 2-Methyl-cis,cis-muconate; columns I54V Km (uM), I54V kcat (min^-1), and I54V kcat/Km (min^-1 uM^-1); cells Km=58 +/- 5, kcat=650 +/- 30, printed kcat/Km=11.

normalized_value_unit_evidence: kcat normalized_value=10.833 normalized_unit=s^-1; Km normalized_value=0.058 normalized_unit=mM; kcat/Km normalized_value=186.775862068966 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row I54V / 2-Methyl-cis,cis-muconate: Km 58 +/- 5 uM; kcat 650 +/- 30 min^-1; printed kcat/Km 11 min^-1 uM^-1.

row_label: I54V / 2-Methyl-cis,cis-muconate


column_label: Table 4. Kinetic constant of the following enzyme; row I54V-F329I / 2-Methyl-cis,cis-muconate; columns I54V-F329I Km (uM), I54V-F329I kcat (min^-1), and I54V-F329I kcat/Km (min^-1 uM^-1); cells Km=57 +/- 4, kcat=1400 +/- 100, printed kcat/Km=24.

normalized_value_unit_evidence: kcat normalized_value=23.333 normalized_unit=s^-1; Km normalized_value=0.057 normalized_unit=mM; kcat/Km normalized_value=409.350877192982 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row I54V-F329I / 2-Methyl-cis,cis-muconate: Km 57 +/- 4 uM; kcat 1400 +/- 100 min^-1; printed kcat/Km 24 min^-1 uM^-1.

row_label: I54V-F329I / 2-Methyl-cis,cis-muconate


column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '2-Methyl-cis,cis-muconate', enzyme column group 'K276N'; column 'Km (uM)' = 180; column 'kcat (min^-1)' = 1,000; column 'kcat/Km (min^-1 uM^-1)' = 5.8.

raw_value_unit_evidence: Table 3, substrate row 2-Methyl-cis,cis-muconate, enzyme column K276N: Km = 180 uM; kcat = 1,000 min^-1; printed kcat/Km = 5.8 min^-1 uM^-1.


column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '2-Methyl-cis,cis-muconate', enzyme column group 'L333V'; column 'Km (uM)' = 110; column 'kcat (min^-1)' = 320; column 'kcat/Km (min^-1 uM^-1)' = 2.8.

raw_value_unit_evidence: Table 3, substrate row 2-Methyl-cis,cis-muconate, enzyme column L333V: Km = 110 uM; kcat = 320 min^-1; printed kcat/Km = 2.8 min^-1 uM^-1.


column_label: Table 4. Kinetic constant of the following enzyme; row Wild type / 2-Methyl-cis,cis-muconate; columns Wild type Km (uM), Wild type kcat (min^-1), and Wild type kcat/Km (min^-1 uM^-1); cells Km=40 +/- 2, kcat=3900 +/- 100, printed kcat/Km=97.

normalized_value_unit_evidence: kcat normalized_value=65 normalized_unit=s^-1; Km normalized_value=0.04 normalized_unit=mM; kcat/Km normalized_value=1625 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row Wild type / 2-Methyl-cis,cis-muconate: Km 40 +/- 2 uM; kcat 3900 +/- 100 min^-1; printed kcat/Km 97 min^-1 uM^-1.

row_label: Wild type / 2-Methyl-cis,cis-muconate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y59W with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic constant of the following enzyme; row Y59W / 2-Methyl-cis,cis-muconate; columns Y59W Km (uM), Y59W kcat (min^-1), and Y59W kcat/Km (min^-1 uM^-1); cells Km=69 +/- 6, kcat=3700 +/- 200, printed kcat/Km=53.

normalized_value_unit_evidence: kcat normalized_value=61.667 normalized_unit=s^-1; Km normalized_value=0.069 normalized_unit=mM; kcat/Km normalized_value=893.724637681159 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row Y59W / 2-Methyl-cis,cis-muconate: Km 69 +/- 6 uM; kcat 3700 +/- 200 min^-1; printed kcat/Km 53 min^-1 uM^-1.

row_label: Y59W / 2-Methyl-cis,cis-muconate


column_label: Table 4. Kinetic constant of the following enzyme; row A271S / 3-Chloro-cis,cis-muconate; columns A271S Km (uM), A271S kcat (min^-1), and A271S kcat/Km (min^-1 uM^-1); cells Km=180 +/- 20, kcat=960 +/- 60, printed kcat/Km=5.400.

normalized_value_unit_evidence: kcat normalized_value=16 normalized_unit=s^-1; Km normalized_value=0.18 normalized_unit=mM; kcat/Km normalized_value=88.8888888888889 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row A271S / 3-Chloro-cis,cis-muconate: Km 180 +/- 20 uM; kcat 960 +/- 60 min^-1; printed kcat/Km 5.400 min^-1 uM^-1.

row_label: A271S / 3-Chloro-cis,cis-muconate


organism: Medicago sativa

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P28012 and applied mutation signature N113A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer HEPES

column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row N113A, 2′,4′-dihydroxychalcone column group; column kcat (min^-1) = 284 ± 42; column Km (uM) = 17.4 ± 3.6; column kcat/Km (M^-1 s^-1) = 272000.

raw_value_unit_evidence: Table 2, enzyme row N113A, 2′,4′-dihydroxychalcone column group: kcat = 284 ± 42 min^-1; Km = 17.4 ± 3.6 uM; printed kcat/Km = 272000 M^-1 s^-1.

row_label: Table 2, row N113A, 2′,4′-dihydroxychalcone column group

table_label: Table 2: Steady-State Kinetic Parameters of Wild-Type and Mutant CHI (Biochemistry 2002, volume 41, issue 16, pages 5168-5176)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P28012 and applied mutation signature T190A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row T190A, 2′,4′-dihydroxychalcone column group; column kcat (min^-1) = 176 ± 20; column Km (uM) = 19.2 ± 2.5; column kcat/Km (M^-1 s^-1) = 153000.

raw_value_unit_evidence: Table 2, enzyme row T190A, 2′,4′-dihydroxychalcone column group: kcat = 176 ± 20 min^-1; Km = 19.2 ± 2.5 uM; printed kcat/Km = 153000 M^-1 s^-1.

row_label: Table 2, row T190A, 2′,4′-dihydroxychalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T48A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P28012 and applied mutation signature T48S to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row T48S, 2′,4′-dihydroxychalcone column group; column kcat (min^-1) = 519 ± 63; column Km (uM) = 41.0 ± 4.2; column kcat/Km (M^-1 s^-1) = 197000.

raw_value_unit_evidence: Table 2, enzyme row T48S, 2′,4′-dihydroxychalcone column group: kcat = 519 ± 63 min^-1; Km = 41.0 ± 4.2 uM; printed kcat/Km = 197000 M^-1 s^-1.

row_label: Table 2, row T48S, 2′,4′-dihydroxychalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P28012 and applied mutation signature Y106F to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row Y106F, 2′,4′-dihydroxychalcone column group; column kcat (min^-1) = 34.1 ± 3.1; column Km (uM) = 34.6 ± 5.9; column kcat/Km (M^-1 s^-1) = 16400.

raw_value_unit_evidence: Table 2, enzyme row Y106F, 2′,4′-dihydroxychalcone column group: kcat = 34.1 ± 3.1 min^-1; Km = 34.6 ± 5.9 uM; printed kcat/Km = 16400 M^-1 s^-1.

row_label: Table 2, row Y106F, 2′,4′-dihydroxychalcone column group


column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row N113A, 4,2′-dihydroxychalcone column group; column kcat (min^-1) = 343 ± 58; column Km (uM) = 52.5 ± 10.6; column kcat/Km (M^-1 s^-1) = 109000.

raw_value_unit_evidence: Table 2, enzyme row N113A, 4,2′-dihydroxychalcone column group: kcat = 343 ± 58 min^-1; Km = 52.5 ± 10.6 uM; printed kcat/Km = 109000 M^-1 s^-1.

row_label: Table 2, row N113A, 4,2′-dihydroxychalcone column group


column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row T190A, 4,2′-dihydroxychalcone column group; column kcat (min^-1) = 225 ± 47; column Km (uM) = 55.9 ± 8.4; column kcat/Km (M^-1 s^-1) = 67100.

raw_value_unit_evidence: Table 2, enzyme row T190A, 4,2′-dihydroxychalcone column group: kcat = 225 ± 47 min^-1; Km = 55.9 ± 8.4 uM; printed kcat/Km = 67100 M^-1 s^-1.

row_label: Table 2, row T190A, 4,2′-dihydroxychalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P28012 and applied mutation signature T48A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row T48A, 4,2′-dihydroxychalcone column group; column kcat (min^-1) = 0.28 ± 0.05; column Km (uM) = 46.4 ± 7.6; column kcat/Km (M^-1 s^-1) = 101.

raw_value_unit_evidence: Table 2, enzyme row T48A, 4,2′-dihydroxychalcone column group: kcat = 0.28 ± 0.05 min^-1; Km = 46.4 ± 7.6 uM; printed kcat/Km = 101 M^-1 s^-1.

row_label: Table 2, row T48A, 4,2′-dihydroxychalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T48S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y106F to reconstruct the assayed variant sequence.


enzyme_display_name: chloromuconate cycloisomerase

organism: Rhodococcus erythropolis

sequence: PDLTVSGVRTTIVDLPILRP

wild_type_sequence: PDLTVSGVRTTIVDLPILRP

enzyme: chloromuconate cycloisomerase


column_label: Table 1 (Substrate specificity of chloromuconate cycloisomerase from R. erythropolis 1CP) carries one substrate label column and four numeric columns, headed 'K_m,app (uM)', 'V_max (U/mg)', 'k_cat (1/min)' and 'k_cat/K_m,app (uM^-1 . min^-1)'. The cited cell set is the substrate row '3-Methyl-cis,cis-muconate': column 'K_m,app (uM)' = 66; column 'V_max (U/mg)' = 1.2; column 'k_cat (1/min)' = 48; column 'k_cat/K_m,app (uM^-1 . min^-1)' = 0.73. The Km,app and Vmax cells are printed with their standard deviations; the kcat and kcat/Km,app cells are printed on their own.

normalized_value_unit_evidence: Km: printed Table 1 cell 66 under the column head 'K_m,app (uM)'; 66 / 1000 = 0.066 mM. kcat: printed Table 1 cell 48 under the column head 'k_cat (1/min)'; 48 / 60 = 0.8 s^-1. kcat/Km: printed Table 1 cell 0.73 under the column head 'k_cat/K_m,app (uM^-1 . min^-1)'; one uM^-1 min^-1 is 1000 / 60 = 16.666667 s^-1 mM^-1, so 0.73 x 1000 / 60 = 12.166666666666668 s^-1 mM^-1, and the same-row quotient of the two printed component cells is 0.8 / 0.066 = 12.121212121212121 s^-1 mM^-1, which the printed efficiency cell reproduces at the two-figure precision Table 1 prints.

raw_value_unit_evidence: Table 1, substrate row '3-Methyl-cis,cis-muconate': Km,app = 66 uM; Vmax = 1.2 U/mg; kcat = 48 min^-1; printed kcat/Km,app = 0.73 uM^-1 min^-1.

table_label: Table 1: Substrate specificity of chloromuconate cycloisomerase from R. erythropolis 1CP (J. Bacteriol. 1995, 177(10):2821-2826)


column_label: Table 1 (Substrate specificity of chloromuconate cycloisomerase from R. erythropolis 1CP) carries one substrate label column and four numeric columns, headed 'K_m,app (uM)', 'V_max (U/mg)', 'k_cat (1/min)' and 'k_cat/K_m,app (uM^-1 . min^-1)'. The cited cell set is the substrate row '2-Chloro-cis,cis-muconate': column 'K_m,app (uM)' = 312; column 'V_max (U/mg)' = 3.3; column 'k_cat (1/min)' = 132; column 'k_cat/K_m,app (uM^-1 . min^-1)' = 0.42. The Km,app and Vmax cells are printed with their standard deviations; the kcat and kcat/Km,app cells are printed on their own.

normalized_value_unit_evidence: Km: printed Table 1 cell 312 under the column head 'K_m,app (uM)'; 312 / 1000 = 0.312 mM. kcat: printed Table 1 cell 132 under the column head 'k_cat (1/min)'; 132 / 60 = 2.2 s^-1. kcat/Km: printed Table 1 cell 0.42 under the column head 'k_cat/K_m,app (uM^-1 . min^-1)'; one uM^-1 min^-1 is 1000 / 60 = 16.666667 s^-1 mM^-1, so 0.42 x 1000 / 60 = 7.0 s^-1 mM^-1, and the same-row quotient of the two printed component cells is 2.2 / 0.312 = 7.051282051282052 s^-1 mM^-1, which the printed efficiency cell reproduces at the two-figure precision Table 1 prints.

raw_value_unit_evidence: Table 1, substrate row '2-Chloro-cis,cis-muconate': Km,app = 312 uM; Vmax = 3.3 U/mg; kcat = 132 min^-1; printed kcat/Km,app = 0.42 uM^-1 min^-1.


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


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +11, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature I54V/F329I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '3-Chloro-cis,cis-muconate', enzyme column group 'I54V-F329I'; column 'Km (uM)' = 210; column 'kcat (min^-1)' = 110; column 'kcat/Km (min^-1 uM^-1)' = 0.54.

raw_value_unit_evidence: Table 3, substrate row 3-Chloro-cis,cis-muconate, enzyme column I54V-F329I: Km = 210 uM; kcat = 110 min^-1; printed kcat/Km = 0.54 min^-1 uM^-1.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +3, so it is treated as a source-provided variant sequence.


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


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

column_label: PMID 9726873 TABLE 3. Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates; row 3-Chloro-cis,cis-muconate^b / wild-type enzyme column group (TABLE 3) (the printed row label carries footnote marker b); wild-type enzyme column group, sub-columns Km (uM), kcat (min^-1) and kcat/Km (min^-1 uM^-1); printed cells Km 320 ± 200 uM, kcat 64 ± 30 min^-1, kcat/Km 0.20 min^-1 uM^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (1.067 s^-1 / 0.32 mM = 3.3343749999999996 s^-1 mM^-1), not as the paper's rounded printed kcat/Km cell (0.20 min^-1 uM^-1), which agrees with that quotient at the printed cell's precision.

normalized_value_unit_evidence: metric: Km; normalized value: 0.32 mM; metric: kcat; normalized value: 1.067 s^-1; metric: kcat/Km; normalized value: 3.3343749999999996 s^-1 mM^-1; assay condition: Kinetic assay at pH 7.5 in 30 mM Tris-HCl with 1 mM MnSO4 at 25 degrees C, followed spectrophotometrically at 260 nm; purified wild-type P. putida PRS2000 muconate cycloisomerase, the TABLE 3 wild-type enzyme column group; kcat computed for a subunit molecular mass of 40 kDa

raw_value_unit_evidence: Table row as printed: Km 320 ± 200 uM; kcat 64 ± 30 min^-1; kcat/Km 0.20 min^-1 uM^-1 (wild-type enzyme column group).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A271S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '3-Fluoro-cis,cis-muconate', enzyme column group 'I54V-F329I'; column 'Km (uM)' = 100; column 'kcat (min^-1)' = 4,900; column 'kcat/Km (min^-1 uM^-1)' = 47.

raw_value_unit_evidence: Table 3, substrate row 3-Fluoro-cis,cis-muconate, enzyme column I54V-F329I: Km = 100 uM; kcat = 4,900 min^-1; printed kcat/Km = 47 min^-1 uM^-1.


substrate_name: Isoliquiritigenin

column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row N113A, 4,2′,4′-trihydroxychalcone column group; column kcat (min^-1) = 304 ± 33; column Km (uM) = 24.3 ± 3.8; column kcat/Km (M^-1 s^-1) = 209000.

raw_value_unit_evidence: Table 2, enzyme row N113A, 4,2′,4′-trihydroxychalcone column group: kcat = 304 ± 33 min^-1; Km = 24.3 ± 3.8 uM; printed kcat/Km = 209000 M^-1 s^-1.

row_label: Table 2, row N113A, 4,2′,4′-trihydroxychalcone column group

substrate: Isoliquiritigenin


column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row T190A, 4,2′,4′-trihydroxychalcone column group; column kcat (min^-1) = 379 ± 54; column Km (uM) = 19.8 ± 2.7; column kcat/Km (M^-1 s^-1) = 319000.

raw_value_unit_evidence: Table 2, enzyme row T190A, 4,2′,4′-trihydroxychalcone column group: kcat = 379 ± 54 min^-1; Km = 19.8 ± 2.7 uM; printed kcat/Km = 319000 M^-1 s^-1.

row_label: Table 2, row T190A, 4,2′,4′-trihydroxychalcone column group


column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row T48A, 4,2′,4′-trihydroxychalcone column group; column kcat (min^-1) = 1.45 ± 0.11; column Km (uM) = 18.9 ± 3.2; column kcat/Km (M^-1 s^-1) = 1280.

raw_value_unit_evidence: Table 2, enzyme row T48A, 4,2′,4′-trihydroxychalcone column group: kcat = 1.45 ± 0.11 min^-1; Km = 18.9 ± 3.2 uM; printed kcat/Km = 1280 M^-1 s^-1.

row_label: Table 2, row T48A, 4,2′,4′-trihydroxychalcone column group


column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row T48S, 4,2′,4′-trihydroxychalcone column group; column kcat (min^-1) = 830 ± 86; column Km (uM) = 21.3 ± 4.1; column kcat/Km (M^-1 s^-1) = 650000.

raw_value_unit_evidence: Table 2, enzyme row T48S, 4,2′,4′-trihydroxychalcone column group: kcat = 830 ± 86 min^-1; Km = 21.3 ± 4.1 uM; printed kcat/Km = 650000 M^-1 s^-1.

row_label: Table 2, row T48S, 4,2′,4′-trihydroxychalcone column group


substrate_name: naringenin chalcone

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N113A to reconstruct the assayed variant sequence.

substrate: naringenin chalcone


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


column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row T48A, 4,2′,4′,6′-tetrahydroxychalcone column group; column kcat (min^-1) = 88.6 ± 13; column Km (uM) = 182 ± 91; column kcat/Km (M^-1 s^-1) = 8110.

raw_value_unit_evidence: Table 2, enzyme row T48A, 4,2′,4′,6′-tetrahydroxychalcone column group: kcat = 88.6 ± 13 min^-1; Km = 182 ± 91 uM; printed kcat/Km = 8110 M^-1 s^-1.

row_label: Table 2, row T48A, 4,2′,4′,6′-tetrahydroxychalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T48S with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


organism: Deschampsia antarctica

substrate_name: isoliquiritigenin

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I190M to reconstruct the assayed variant sequence.

substrate: isoliquiritigenin


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature K108A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 298.15 K; buffer DMSO in 50 mM potassium phosphate

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row K108A, isoliquiritigenin column group; column kcat (min^-1) = 0.2 ± 0.11; column Km (uM) = 11.2 ± 15.9; column kcat/Km (M^-1 s^-1) = 298.

raw_value_unit_evidence: Table 4, enzyme row K108A, isoliquiritigenin column group: kcat = 0.2 ± 0.11 min^-1; Km = 11.2 ± 15.9 uM; printed kcat/Km = 298 M^-1 s^-1.

row_label: Table 4, row K108A, isoliquiritigenin column group

table_label: Table 4: Steady-state kinetic parameters of wild-type and mutant DaCHI1 (PLoS ONE 2018, 13(2): e0192415)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature M36A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row M36A, isoliquiritigenin column group; column kcat (min^-1) = 0.5 ± 0.15; column Km (uM) = 16.4 ± 10.1; column kcat/Km (M^-1 s^-1) = 508.

raw_value_unit_evidence: Table 4, enzyme row M36A, isoliquiritigenin column group: kcat = 0.5 ± 0.15 min^-1; Km = 16.4 ± 10.1 uM; printed kcat/Km = 508 M^-1 s^-1.

row_label: Table 4, row M36A, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature Q104E to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row Q104E, isoliquiritigenin column group; column kcat (min^-1) = 1.4 ± 0.06; column Km (uM) = 22.5 ± 2.3; column kcat/Km (M^-1 s^-1) = 1011.

raw_value_unit_evidence: Table 4, enzyme row Q104E, isoliquiritigenin column group: kcat = 1.4 ± 0.06 min^-1; Km = 22.5 ± 2.3 uM; printed kcat/Km = 1011 M^-1 s^-1.

row_label: Table 4, row Q104E, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature R34A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row R34A, isoliquiritigenin column group; column kcat (min^-1) = 0.1 ± 0.03; column Km (uM) = 5.3 ± 7.8; column kcat/Km (M^-1 s^-1) = 314.

raw_value_unit_evidence: Table 4, enzyme row R34A, isoliquiritigenin column group: kcat = 0.1 ± 0.03 min^-1; Km = 5.3 ± 7.8 uM; printed kcat/Km = 314 M^-1 s^-1.

row_label: Table 4, row R34A, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature R34M to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row R34M, isoliquiritigenin column group; column kcat (min^-1) = 0.1 ± 0.08; column Km (uM) = 24.3 ± 28.2; column kcat/Km (M^-1 s^-1) = 69.

raw_value_unit_evidence: Table 4, enzyme row R34M, isoliquiritigenin column group: kcat = 0.1 ± 0.08 min^-1; Km = 24.3 ± 28.2 uM; printed kcat/Km = 69 M^-1 s^-1.

row_label: Table 4, row R34M, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature S189A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row S189A, isoliquiritigenin column group; column kcat (min^-1) = 0.2 ± 0.03; column Km (uM) = 18.5 ± 6.9; column kcat/Km (M^-1 s^-1) = 180.

raw_value_unit_evidence: Table 4, enzyme row S189A, isoliquiritigenin column group: kcat = 0.2 ± 0.03 min^-1; Km = 18.5 ± 6.9 uM; printed kcat/Km = 180 M^-1 s^-1.

row_label: Table 4, row S189A, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature S189T to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row S189T, isoliquiritigenin column group; column kcat (min^-1) = 1.0 ± 0.04; column Km (uM) = 10.8 ± 1.2; column kcat/Km (M^-1 s^-1) = 1543.

raw_value_unit_evidence: Table 4, enzyme row S189T, isoliquiritigenin column group: kcat = 1.0 ± 0.04 min^-1; Km = 10.8 ± 1.2 uM; printed kcat/Km = 1543 M^-1 s^-1.

row_label: Table 4, row S189T, isoliquiritigenin column group


column_label: Table 4 | Steady-state kinetic parameters of wild-type and mutant DaCHI1; row DaCHI1; Isoliquiritigenin columns kcat (min^-1), Km (uM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 4 | Steady-state kinetic parameters of wild-type and mutant DaCHI1, isoliquiritigenin row DaCHI1: kcat 1.3 ± 0.1 min^-1; Km 15.3 ± 1.5 uM; kcat/Km 1416 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature Y116A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row Y116A, isoliquiritigenin column group; column kcat (min^-1) = 0.4 ± 0.04; column Km (uM) = 27.6 ± 5.4; column kcat/Km (M^-1 s^-1) = 242.

raw_value_unit_evidence: Table 4, enzyme row Y116A, isoliquiritigenin column group: kcat = 0.4 ± 0.04 min^-1; Km = 27.6 ± 5.4 uM; printed kcat/Km = 242 M^-1 s^-1.

row_label: Table 4, row Y116A, isoliquiritigenin column group


organism: Arthrobacter sp.

assay_conditions_summary: pH 8

column_label: Table 2 row '2-Methyl-cis,cis-muconate', column 'Km (uM)': 29 +/- 5.2

raw_value_unit_evidence: Km column reports 29 +/- 5.2 uM

table_label: Table 2: Substrate specificity of the MC from Arthrobacter sp. BA-5-17


column_label: Table 2 row '3-Chloro-cis,cis-muconate', column 'Km (uM)': 46 +/- 5.5

raw_value_unit_evidence: Km column reports 46 +/- 5.5 uM


column_label: Table 2 row '3-Methyl-cis,cis-muconate', column 'Km (uM)': 75 +/- 8.9

raw_value_unit_evidence: Km column reports 75 +/- 8.9 uM


column_label: Table 2 row 'cis,cis-Muconate', column 'Km (uM)': 150 +/- 19

raw_value_unit_evidence: Km column reports 150 +/- 19 uM

row_label: cis,cis-Muconate


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


column_label: PMID 14617643 Table 2, Pseudomonas sp. strain MT1 MCI row for 3-Chloromuconate: Km 410 +/- 75 uM, kcat 7,200 +/- 520 min^-1, kcat/Km 17.6 min^-1 uM^-1.

raw_value_unit_evidence: Table 2 reports 3-Chloromuconate Km = 410 uM, kcat = 7,200 min^-1, and kcat/Km = 17.6 min^-1 uM^-1 for Pseudomonas sp. strain MT1 MCI.

row_label: Pseudomonas sp. strain MT1 / MCI / 3-Chloromuconate

table_label: Table 2. Substrate specificities of chloromuconate cycloisomerase and MCI from different strains and of trans-DLH from Pseudomonas sp. strain MT1


substrate_name: cis,cis-Muconate

column_label: Retained ASM PDF Table 2, Pseudomonas sp. strain MT1 / MCI / Muconate row: Km 1,730 +/- 350; kcat 7,500 +/- 350; kcat/Km 4.3.

normalized_value_unit_evidence: Km 1.73 mM; kcat 125 s^-1; independently printed kcat/Km 71.66666666666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 Pseudomonas sp. strain MT1 / MCI / Muconate row: Km 1,730 +/- 350 uM; kcat 7,500 +/- 350 min^-1; independently printed kcat/Km 4.3 min^-1 uM^-1.

substrate: cis,cis-Muconate


organism: Pseudomonas sp.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature I190M to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row I190M, naringenin chalcone column group; column kcat (min^-1) = 11860 ± 539; column Km (uM) = 8.6 ± 1.2; column kcat/Km (M^-1 s^-1) = 2.292 x 10^7.

raw_value_unit_evidence: Table 4, enzyme row I190M, naringenin chalcone column group: kcat = 11860 ± 539 min^-1; Km = 8.6 ± 1.2 uM; printed kcat/Km = 2.292 x 10^7 M^-1 s^-1.

row_label: Table 4, row I190M, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row K108A, naringenin chalcone column group; column kcat (min^-1) = 3416 ± 234; column Km (uM) = 4.8 ± 1.2; column kcat/Km (M^-1 s^-1) = 1.19 x 10^7.

raw_value_unit_evidence: Table 4, enzyme row K108A, naringenin chalcone column group: kcat = 3416 ± 234 min^-1; Km = 4.8 ± 1.2 uM; printed kcat/Km = 1.19 x 10^7 M^-1 s^-1.

row_label: Table 4, row K108A, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row M36A, naringenin chalcone column group; column kcat (min^-1) = 2112 ± 239; column Km (uM) = 4.8 ± 2.0; column kcat/Km (M^-1 s^-1) = 7.33 x 10^6.

raw_value_unit_evidence: Table 4, enzyme row M36A, naringenin chalcone column group: kcat = 2112 ± 239 min^-1; Km = 4.8 ± 2.0 uM; printed kcat/Km = 7.33 x 10^6 M^-1 s^-1.

row_label: Table 4, row M36A, naringenin chalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature M96K to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row M96K, naringenin chalcone column group; column kcat (min^-1) = 468 ± 51; column Km (uM) = 10.5 ± 3.4; column kcat/Km (M^-1 s^-1) = 7.43 x 10^5.

raw_value_unit_evidence: Table 4, enzyme row M96K, naringenin chalcone column group: kcat = 468 ± 51 min^-1; Km = 10.5 ± 3.4 uM; printed kcat/Km = 7.43 x 10^5 M^-1 s^-1.

row_label: Table 4, row M96K, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row Q104E, naringenin chalcone column group; column kcat (min^-1) = 8082 ± 267; column Km (uM) = 6.1 ± 0.7; column kcat/Km (M^-1 s^-1) = 2.208 x 10^7.

raw_value_unit_evidence: Table 4, enzyme row Q104E, naringenin chalcone column group: kcat = 8082 ± 267 min^-1; Km = 6.1 ± 0.7 uM; printed kcat/Km = 2.208 x 10^7 M^-1 s^-1.

row_label: Table 4, row Q104E, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row S189A, naringenin chalcone column group; column kcat (min^-1) = 299 ± 15; column Km (uM) = 2.4 ± 0.6; column kcat/Km (M^-1 s^-1) = 2.08 x 10^6.

raw_value_unit_evidence: Table 4, enzyme row S189A, naringenin chalcone column group: kcat = 299 ± 15 min^-1; Km = 2.4 ± 0.6 uM; printed kcat/Km = 2.08 x 10^6 M^-1 s^-1.

row_label: Table 4, row S189A, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row S189T, naringenin chalcone column group; column kcat (min^-1) = 13690 ± 556; column Km (uM) = 9.9 ± 1.2; column kcat/Km (M^-1 s^-1) = 2.306 x 10^7.

raw_value_unit_evidence: Table 4, enzyme row S189T, naringenin chalcone column group: kcat = 13690 ± 556 min^-1; Km = 9.9 ± 1.2 uM; printed kcat/Km = 2.306 x 10^7 M^-1 s^-1.

row_label: Table 4, row S189T, naringenin chalcone column group


assay_conditions_summary: pH 7.6; 298.15 K; buffer potassium phosphate

column_label: table label: Table 4. Steady-state kinetic parameters of wild-type and mutant DaCHI1.; row label: DaCHI1; column label: the Naringenin chalcone kcat (min-1) cell and the Naringenin chalcone Km (uM) cell of this one wild-type row; no cell is taken from the Isoliquiritigenin column group of this row, from any mutant row, or from any other table; raw value: kcat 7819 plus-minus 825 min-1, Km 8.5 plus-minus 3.1 uM; raw unit: min-1 for kcat, uM for Km; normalized value: kcat 130.3 s^-1, Km 0.0085 mM, kcat/Km 15329.411764705883 s^-1 mM^-1; normalized unit: s^-1, mM, s^-1 mM^-1; condition label: Table 4 footnote: Km and kcat were calculated using the Michaelis-Menten equation; reactions were performed in potassium phosphate buffer (pH 7.6) as described in Material and Methods; all Km and kcat values are expressed as the mean plus-minus standard deviation of three parallel experiments. Enzymatic activity assay (Materials and Methods, Block RVM0009-METHODS-VERBATIM): the standard reaction was carried out at 25 C using 50 uM substrate in DMSO, 50 mM potassium phosphate buffer (pH 7.6) containing 1 mg bovine serum albumin. The export row carries pH 7.6 and no stored temperature.

normalized_value_unit_evidence: metric: kcat; raw value: 7819 ± 825; raw unit: min–1; normalized value: 130.3 s^-1; normalized unit: s^-1; metric: Km; raw value: 8.5 ± 3.1; raw unit: μM; normalized value: 0.0085 mM; normalized unit: mM; metric: kcat/Km; normalized value: 15329.411764705883 s^-1 mM^-1; normalized unit: s^-1 mM^-1; assay condition: Table 4 footnote: Km and kcat were calculated using the Michaelis-Menten equation; reactions were performed in potassium phosphate buffer (pH 7.6) as described in Material and Methods; all Km and kcat values are expressed as the mean plus-minus standard deviation of three parallel experiments. Enzymatic activity assay (Materials and Methods, Block RVM0009-METHODS-VERBATIM): the standard reaction was carried out at 25 C using 50 uM substrate in DMSO, 50 mM potassium phosphate buffer (pH 7.6) containing 1 mg bovine serum albumin. The export row carries pH 7.6 and no stored temperature. Conversion note: 7819 min-1 divided by 60 is 130.31666666666666 s^-1, stored at the export's one-decimal precision as 130.3 s^-1; 8.5 uM divided by 1000 is 0.0085 mM exactly; kcat/Km is the quotient of this row's own two cells as stored, 130.3 s^-1 divided by 0.0085 mM giving 15329.411764705883 s^-1 mM^-1, which reproduces the printed ratio cell 1.53 x 10^7 M-1 s-1 exactly at that cell's three-significant-figure precision.

raw_value_unit_evidence: Table 4, row DaCHI1, Naringenin chalcone column group: kcat cell 7819 ± 825 min–1; Km cell 8.5 ± 3.1 μM; printed kcat/Km cell 1.53 × 10^7 M–1 s–1 (superscript 7 rendered on the preceding text-layer line).


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row Y116A, naringenin chalcone column group; column kcat (min^-1) = 578 ± 68; column Km (uM) = 7.0 ± 2.8; column kcat/Km (M^-1 s^-1) = 1.38 x 10^6.

raw_value_unit_evidence: Table 4, enzyme row Y116A, naringenin chalcone column group: kcat = 578 ± 68 min^-1; Km = 7.0 ± 2.8 uM; printed kcat/Km = 1.38 x 10^6 M^-1 s^-1.

row_label: Table 4, row Y116A, naringenin chalcone column group


organism: Eubacterium ramulus

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

source_databases_merged: brenda skid


substrate_name: butein

substrate: butein


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=6.4


organism: Hydrogenophaga intermedia


organism: Cupriavidus necator


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


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_accession and applied mutation signature Y106F to reconstruct the assayed variant sequence.


column_label: Table 4. Kinetic constant of the following enzyme; row Wild type / 3-Methyl-cis,cis-muconate; columns Wild type Km (uM), Wild type kcat (min^-1), and Wild type kcat/Km (min^-1 uM^-1); cells Km=6.0 +/- 0.5, kcat=590 +/- 10, printed kcat/Km=99.

normalized_value_unit_evidence: kcat normalized_value=9.833 normalized_unit=s^-1; Km normalized_value=0.006 normalized_unit=mM; kcat/Km normalized_value=1638.83333333333 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row Wild type / 3-Methyl-cis,cis-muconate: Km 6.0 +/- 0.5 uM; kcat 590 +/- 10 min^-1; printed kcat/Km 99 min^-1 uM^-1.

row_label: Wild type / 3-Methyl-cis,cis-muconate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y59W with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic constant of the following enzyme; row Y59W / 3-Methyl-cis,cis-muconate; columns Y59W Km (uM), Y59W kcat (min^-1), and Y59W kcat/Km (min^-1 uM^-1); cells Km=15 +/- 1, kcat=140 +/- 10, printed kcat/Km=9.7.

normalized_value_unit_evidence: kcat normalized_value=2.333 normalized_unit=s^-1; Km normalized_value=0.015 normalized_unit=mM; kcat/Km normalized_value=155.533333333333 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row Y59W / 3-Methyl-cis,cis-muconate: Km 15 +/- 1 uM; kcat 140 +/- 10 min^-1; printed kcat/Km 9.7 min^-1 uM^-1.

row_label: Y59W / 3-Methyl-cis,cis-muconate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A271S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic constant of the following enzyme; row A271S / cis,cis-Muconate; columns A271S Km (uM), A271S kcat (min^-1), and A271S kcat/Km (min^-1 uM^-1); cells Km=35 +/- 3, kcat=7100 +/- 200, printed kcat/Km=200.

normalized_value_unit_evidence: kcat normalized_value=118.333 normalized_unit=s^-1; Km normalized_value=0.035 normalized_unit=mM; kcat/Km normalized_value=3380.94285714286 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row A271S / cis,cis-Muconate: Km 35 +/- 3 uM; kcat 7100 +/- 200 min^-1; printed kcat/Km 200 min^-1 uM^-1.

row_label: A271S / cis,cis-Muconate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature F329I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row 'cis,cis-Muconate', enzyme column group 'F329I'; column 'Km (uM)' = 47; column 'kcat (min^-1)' = 2,600; column 'kcat/Km (min^-1 uM^-1)' = 54.

raw_value_unit_evidence: Table 3, substrate row cis,cis-Muconate, enzyme column F329I: Km = 47 uM; kcat = 2,600 min^-1; printed kcat/Km = 54 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I54V with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic constant of the following enzyme; row I54V / cis,cis-Muconate; columns I54V Km (uM), I54V kcat (min^-1), and I54V kcat/Km (min^-1 uM^-1); cells Km=96 +/- 8, kcat=2500 +/- 100, printed kcat/Km=26.

normalized_value_unit_evidence: kcat normalized_value=41.667 normalized_unit=s^-1; Km normalized_value=0.096 normalized_unit=mM; kcat/Km normalized_value=434.03125 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row I54V / cis,cis-Muconate: Km 96 +/- 8 uM; kcat 2500 +/- 100 min^-1; printed kcat/Km 26 min^-1 uM^-1.

row_label: I54V / cis,cis-Muconate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I54V/F329I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic constant of the following enzyme; row I54V-F329I / cis,cis-Muconate; columns I54V-F329I Km (uM), I54V-F329I kcat (min^-1), and I54V-F329I kcat/Km (min^-1 uM^-1); cells Km=140 +/- 10, kcat=540 +/- 30, printed kcat/Km=3.80.

normalized_value_unit_evidence: kcat normalized_value=9 normalized_unit=s^-1; Km normalized_value=0.14 normalized_unit=mM; kcat/Km normalized_value=64.2857142857143 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row I54V-F329I / cis,cis-Muconate: Km 140 +/- 10 uM; kcat 540 +/- 30 min^-1; printed kcat/Km 3.80 min^-1 uM^-1.

row_label: I54V-F329I / cis,cis-Muconate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature K276N with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row 'cis,cis-Muconate', enzyme column group 'K276N'; column 'Km (uM)' = 74; column 'kcat (min^-1)' = 2,100; column 'kcat/Km (min^-1 uM^-1)' = 29.

raw_value_unit_evidence: Table 3, substrate row cis,cis-Muconate, enzyme column K276N: Km = 74 uM; kcat = 2,100 min^-1; printed kcat/Km = 29 min^-1 uM^-1.


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


column_label: Table 4. Kinetic constant of the following enzyme; row Wild type / cis,cis-Muconate; columns Wild type Km (uM), Wild type kcat (min^-1), and Wild type kcat/Km (min^-1 uM^-1); cells Km=40 +/- 4, kcat=12600 +/- 400, printed kcat/Km=310.

normalized_value_unit_evidence: kcat normalized_value=210 normalized_unit=s^-1; Km normalized_value=0.04 normalized_unit=mM; kcat/Km normalized_value=5250 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row Wild type / cis,cis-Muconate: Km 40 +/- 4 uM; kcat 12600 +/- 400 min^-1; printed kcat/Km 310 min^-1 uM^-1.

row_label: Wild type / cis,cis-Muconate


column_label: Table 4. Kinetic constant of the following enzyme; row Y59W / cis,cis-Muconate; columns Y59W Km (uM), Y59W kcat (min^-1), and Y59W kcat/Km (min^-1 uM^-1); cells Km=47 +/- 3, kcat=1100 +/- 100, printed kcat/Km=24.

normalized_value_unit_evidence: kcat normalized_value=18.333 normalized_unit=s^-1; Km normalized_value=0.047 normalized_unit=mM; kcat/Km normalized_value=390.063829787234 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row Y59W / cis,cis-Muconate: Km 47 +/- 3 uM; kcat 1100 +/- 100 min^-1; printed kcat/Km 24 min^-1 uM^-1.

row_label: Y59W / cis,cis-Muconate


organism: Antrophyum callifolium


organism: Marchantia paleacea


organism: Selaginella moellendorffii


organism: Aspergillus niger


organism: Cutaneotrichosporon cutaneum

column_label: Abstract states the two purified enzyme forms have the same Km value of 25 microM for cis,cis-muconate.

raw_value_unit_evidence: Km raw_value=25 raw_unit=microM

row_label: Trichosporon cutaneum cis,cis-muconate cyclase with cis,cis-muconate

table_label: PubMed/PMC abstract PMID 7193457


organism: Homo sapiens

substrate_name: NAD

source_db: uniprot

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

column_label: Abstract reports K(m) values of 0.57 mm for glucose 6-phosphate and 8 microm for NAD(+).

raw_value_unit_evidence: Km raw_value=8 microm raw_unit=microM

row_label: Recombinant human MIP synthase / NAD+

table_label: PubMed XML abstract PMID 15024000

substrate: NAD

source: uniprot


organism: Saccharomyces cerevisiae

substrate_name: D-Glucose 6-phosphate

substrate: D-Glucose 6-phosphate


organism: Oryza sativa


substrate_name: Naringenin chalcone

substrate: Naringenin chalcone


column_label: Abstract reports the apparent Km was found to be 57 microM at pH 6.0 and 30 degrees C.

raw_value_unit_evidence: Km raw_value=57 microM raw_unit=microM

row_label: Aspergillus niger 3-carboxy-cis,cis-muconate cyclase / 3-carboxy-cis,cis-muconate

table_label: PubMed XML abstract PMID 240704


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

column_label: Table 1 row MIPS1, column kcat/Km (mM^-1 min^-1) for Glc-6-P.

normalized_value_unit_evidence: kcat 0.10666666666666667 s^-1; Km 0.68 mM; explicit kcat/Km 0.15666666666666668 s^-1*mM^-1. Current exported rounded/derived values differ for at least one populated metric.

table_label: Table 1. Steady State Kinetic Parameters for Arabidopsis MIPS


column_label: Table 1 row MIPS2, column kcat/Km (mM^-1 min^-1) for Glc-6-P.

normalized_value_unit_evidence: kcat 0.06666666666666667 s^-1; Km 0.45 mM; explicit kcat/Km 0.14666666666666667 s^-1*mM^-1. Current exported rounded/derived values differ for at least one populated metric.


column_label: Table 1 Steady State Kinetic Parameters for Arabidopsis MIPS: MIPS3 row; columns kcat (min^-1), KmGlc-6-P (mM), kcat/Km (mM^-1 min^-1).

normalized_value_unit_evidence: kcat normalized_value=0.08666666666666667 normalized_unit=s^-1; Km normalized_value=0.31 normalized_unit=mM; explicit kcat/Km normalized_value=0.2833333333333333 normalized_unit=s^-1 mM^-1. CatLog stores derived kcat/Km=0.2806451612903226 from rounded export kcat/Km inputs.

raw_value_unit_evidence: Table 1 row MIPS3 reports kcat=5.2 min^-1, KmGlc-6-P=0.31 mM, kcat/Km=17 mM^-1 min^-1.

row_label: MIPS3 / Glc-6-P

table_label: PMC2861443 Table 1


substrate_name: NAD+

substrate: NAD+


organism: Rattus norvegicus

assay_conditions_summary: cofactor NAD+

column_label: Abstract kinetic summary: glucose 6-phosphate Km 3.8 mM; NAD+ Km 17.9 uM.

normalized_value_unit_evidence: glucose 6-phosphate 3.8 mM; NAD+ 0.0179 mM

raw_value_unit_evidence: Abstract states basal Km values for glucose 6-phosphate and NAD+ were 3.8 mM and 17.9 uM, respectively.

row_label: Glucose-6-phosphate cycloisomerase substrate/cofactor Kms

table_label: Abstract / kinetic summary


organism: Trypanosoma brucei brucei

substrate_name: D-glucose 6-phosphate (at 37 degrees Celsius and pH 8.0)

column_label: PMID 16824097 Results prose/Fig. 2B, recombinant TbINO1 with glucose 6-phosphate: apparent Km = 0.58 mM.

raw_value_unit_evidence: Results prose reports an apparent Km of 0.58 mM and Vmax of 0.25 umol h^-1 for recombinant TbINO1 with glucose 6-phosphate.

row_label: recombinant TbINO1 / glucose 6-phosphate

table_label: Results prose and Fig. 2B


organism: Vigna radiata

substrate_name: 1D-myo-Inositol 3-phosphate

substrate: 1D-myo-Inositol 3-phosphate


substrate_name: (+)-taxifolin

column_label: Results prose reports: The Km for (+)-taxifolin was 4.1 +/- 0.6 uM for recombinant CHI characterization.

raw_value_unit_evidence: Km raw_value=4.1 +/- 0.6 raw_unit=uM

row_label: Recombinant E. ramulus CHI in E. coli pTI2 cell extract / (+)-taxifolin

table_label: Results prose: recombinant chi expression and flavanonol-isomerizing characterization

substrate: (+)-taxifolin


organism: Pseudomonas putida

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


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


km_display: Not reported

proof_lines: pH 7.5, 25°C, mutant enzyme Y59W and A271S


organism: Odontosoria chusana


organism: Lindsaea orbiculata


organism: Acinetobacter calcoaceticus


substrate_name: Unknown

ki_unit: mM

proof_lines: inhibitor of cis,cis-muconate conversion

substrate: Unknown


organism: Rhodococcus erythropolis


proof_lines: pH 7.5, 25°C, mutant enzyme K276N or F329I


proof_lines: pH 7.5, 25°C, mutant enzyme Y59W and F329I


proof_lines: pH 7.5, 25°C, mutant enzyme A271S or I54V/F329


organism: Pseudomonas sp.


organism: Glycine max


proof_lines:
pH 8, 20°C
methanethiolated enzyme
native enzyme


organism: Adiantum capillus-veneris


organism: Agrobacterium tumefaciens


substrate_name: glucose 6-phosphate

substrate: glucose 6-phosphate


substrate_name: cis,cis-muconate


substrate_name: D-glucose 6-phosphate

proof_lines: presence of 0.6 mM valnoctamide, pH 7.6, 37°C


proof_lines:
pH 7.6, 37°C
brain, post mortem


organism: Medicago sativa


proof_lines:
chloroplastic enzyme
cytosolic enzyme


proof_lines:
cytosolic enzyme
chloroplastic enzyme


organism: Oryza coarctata


organism: Oryza sativa Japonica Group

proof_lines: at pH 7.5, temperature not specified in the publication


substrate_name: muconolactone

substrate: muconolactone


substrate: cis,cis-muconate


organism: Archaeoglobus fulgidus

substrate: D-glucose 6-phosphate


assay_conditions_summary: pH 7.5; cofactor NAD+


organism: Oryza sativa


proof_lines: mutant bearing amino acids 174-210 of Porteresia coarctata enzyme, 37°C


organism: Pseudomonas reinekei


enzyme_display_name: dichloromuconate cycloisomerase

organism: Cupriavidus necator

enzyme: dichloromuconate cycloisomerase


enzyme_display_name: (+)-bornyl diphosphate synthase

organism: Tanacetum vulgare

substrate_name: geranyl diphosphate

smiles: CC(=CCCC(=CCOP(=O)(O)OP(=O)(O)O)C)C

enzyme: (+)-bornyl diphosphate synthase

substrate: geranyl diphosphate


substrate_name: (+)-(3S)-linalyl diphosphate

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

substrate: (+)-(3S)-linalyl diphosphate


enzyme_display_name: cycloeucalenol cycloisomerase

organism: Zea mays

substrate_name: cycloeucalenol

enzyme: cycloeucalenol cycloisomerase

substrate: cycloeucalenol


enzyme_display_name: ent-copalyl diphosphate synthase

organism: Cucurbita maxima

substrate_name: geranylgeranyl diphosphate

enzyme: ent-copalyl diphosphate synthase

substrate: geranylgeranyl diphosphate


enzyme_display_name: alpha-pinene-oxide decyclase

organism: Nocardia sp.

substrate_name: alpha-Pinene oxide

enzyme: alpha-pinene-oxide decyclase

substrate: alpha-Pinene oxide


enzyme_display_name: copalyl diphosphate synthase

organism: Abies grandis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T769G to reconstruct the assayed variant sequence.

enzyme: copalyl diphosphate synthase


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


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

proof_lines:
wild-type
wild-type, D405A, Y520A


sequence_variant_note: Resolved canonical sequence from brenda_getSequence_unique_ec_organism and applied mutation signature D405N/Y520A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from brenda_getSequence_unique_ec_organism and applied mutation signature D402N/R365A/R454A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from brenda_getSequence_unique_ec_organism and applied mutation signature R411A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from brenda_getSequence_unique_ec_organism and applied mutation signature W358A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from brenda_getSequence_unique_ec_organism and applied mutation signature D405N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from brenda_getSequence_unique_ec_organism and applied mutation signature D361A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from brenda_getSequence_unique_ec_organism and applied mutation signature E499A/R411A/R365A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from brenda_getSequence_unique_ec_organism and applied mutation signature D404A to reconstruct the assayed variant sequence.


substrate_name: CPP (in presence of magnesium)

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

substrate: CPP (in presence of magnesium)


enzyme_display_name: terpentedienyl-diphosphate synthase

organism: Kitasatospora griseola

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

enzyme: terpentedienyl-diphosphate synthase


organism: Salvia officinalis


organism: Arabidopsis thaliana

substrate_name: (E,E,E)-geranylgeranyl diphosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D503A to reconstruct the assayed variant sequence.

substrate: (E,E,E)-geranylgeranyl diphosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E211A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N425A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N425H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R340A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T421A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T421S to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.8; 295.15 K; buffer of 50 mM HEPES pH 7

column_label: Table 2 (Steady-State Kinetic Parameters for CPS Mutants), enzyme-form row 'Wild-type'; column 'kcat (s^-1)' = 0.9; column 'KM (uM)' = 3; column 'kcat/KM (M^-1 s^-1)' = 3 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.9 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.9 s^(-1). Km: printed Table 2 cell 3 uM; 3 / 1000 = 0.003 mM; the exported value is 0.003 mM. kcat/Km: printed Table 2 cell 3 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 300000 / 1000 = 300.0 s^-1 mM^-1; the exported value is 300.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row Wild-type: kcat = 0.9 s^-1; KM = 3 uM; printed kcat/KM = 3 x 10^5 M^-1 s^-1.

row_label: Table 2, row Wild-type

table_label: Table 2: Steady-State Kinetic Parameters for CPS Mutants (Biochim Biophys Acta 2014, 1840(1))


organism: Phaeosphaeria sp.

substrate_name: copalyl diphosphate

substrate: copalyl diphosphate


organism: Talaromyces verruculosus

substrate_name: DMAPP (for prenyltransferase activity)

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

substrate: DMAPP (for prenyltransferase activity)


substrate_name: IPP (for prenyltransferase activity)

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

substrate: IPP (for prenyltransferase activity)


source_db: skid

source_databases_merged: skid uniprot

source: skid


substrate_name: farnesyl diphosphate

substrate: farnesyl diphosphate


substrate_name: Geranyl diphosphate

substrate: Geranyl diphosphate


organism: Agrobacterium tumefaciens

substrate_name: Unknown

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

substrate: Unknown


proof_lines: pH 7.5, 30°C, periodate assay method, in absence of 1 mM Mg2+

proof_lines: pH 7.5, 30°C, periodate assay method, in presence of 1 mM Mg2+

proof_lines: pH 7.5, 30°C, IMP-coupled assay method, in presence of 1 mM Mg2+


enzyme_display_name: prosolanapyrone-III cycloisomerase

organism: Saccharopolyspora spinosa

proof_lines: pH and temperature not specified in the publication

enzyme: prosolanapyrone-III cycloisomerase


enzyme_display_name: (-)-bornyl diphosphate synthase

organism: Blumea balsamifera

enzyme: (-)-bornyl diphosphate synthase


enzyme_display_name: UniProt P34808

organism: Caenorhabditis elegans

substrate_name: ATP

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P34808

substrate: ATP


enzyme_display_name: aklanonic acid methyl ester cyclase

organism: Streptomyces galilaeus

substrate_name: nogalonic acid methyl ester

proof_lines: kcat is 1 sec(-1) for cyclization with nogalonic acid methyl ester.

enzyme: aklanonic acid methyl ester cyclase

substrate: nogalonic acid methyl ester


substrate_name: (-)-(3R)-linalyl diphosphate

column_label: Table I row (+)-BPP cyclase (sage) / (3R)-LPP, Km column: 0.7 uM.

raw_value_unit_evidence: Table I reports (3R)-LPP Km 0.7 uM for (+)-BPP cyclase from sage.

row_label: (3R)-LPP for (+)-BPP cyclase from sage

table_label: Table I

substrate: (-)-(3R)-linalyl diphosphate


organism: Alternaria solani

substrate_name: Prosolanapyrone II; O2

substrate: Prosolanapyrone II; O2


enzyme_display_name: halimadienyl-diphosphate synthase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

enzyme: halimadienyl-diphosphate synthase


organism: Streptomyces peucetius


enzyme_display_name: lycopene beta-cyclase

organism: Paracoccus haeundaensis

substrate_name: lycopene

assay_conditions_summary: pH 6.5; cofactor NADPH

enzyme: lycopene beta-cyclase

substrate: lycopene


assay_conditions_summary: pH 7.8; 303.15 K; buffer of 50 mM HEPES pH 7


enzyme_display_name: microtubule-severing ATPase

assay_conditions_summary: pH 8; 301.15 K; cofactor ATP

proof_lines: pH 8.0, 28°C, MEI-1 WT/MEI-2 wild-type enzyme

enzyme: microtubule-severing ATPase


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +7, so it is treated as a source-provided variant sequence.

proof_lines: pH 8.0, 28°C, mutant enzyme MEI-1 K293Q/MEI-2


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature K239A with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 28°C, mutant enzyme MEI-1 K239A/MEI-2


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E29D with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: mutant E29D, 30°C, pH not specified in the publication, Vmax: 0.24 nmol/h/mg


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D260H with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: mutant D260H, 30°C, pH not specified in the publication, Vmax: 0.35 nmol/h/mg


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E29H with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: mutant E29H, 30°C, pH not specified in the publication, Vmax: 0.33 nmol/h/mg


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W112L with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

proof_lines: mutant W112L, 30°C, pH not specified in the publication, Vmax: 14.7 nmol/h/mg


proof_lines: wild-type, 30°C, pH not specified in the publication, Vmax: 22 nmol/h/mg


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +1, so it is treated as a source-provided variant sequence.

proof_lines: mutant F111L, 30°C, pH not specified in the publication, Vmax: 4.7 nmol/h/mg


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D260E with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: mutant D260E, 30°C, pH not specified in the publication, Vmax: 44 nmol/h/mg


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T113S with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

proof_lines: mutant T113S, 30°C, pH not specified in the publication, Vmax: 26 nmol/h/mg


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -5, so it is treated as a source-provided variant sequence.

proof_lines: mutant F117L, 30°C, pH not specified in the publication, Vmax: 5.3 nmol/h/mg


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

proof_lines: mutant G108A, 30°C, pH not specified in the publication, Vmax: 11.4 nmol/h/mg


proof_lines: mutant T113A, 30°C, pH not specified in the publication, Vmax: 4.9 nmol/h/mg


organism: Tanacetum vulgare

substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


substrate_name: (+)-(3S)-linalyl diphosphate

substrate: (+)-(3S)-linalyl diphosphate


organism: Streptomyces sp.

substrate_name: geranylgeranyl diphosphate

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

substrate: geranylgeranyl diphosphate


organism: Homo sapiens

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

mutation_type: truncation

assay_conditions_summary: cofactor ATP

proof_lines: Kinetic parameters shown are for full-length enzyme. N-terminally truncated spastin (residues 228-616), which has been shown to exhibit full severing activity, shows a basal ATP turnover rate of 0.78 sec(-1) in the absence of microtubules,


enzyme_display_name: (+)-cis,trans-nepetalactol synthase

organism: Nepeta racemosa

substrate_name: cis-trans-nepetalactol (in the presence of NAD(+) at pH 8.0 and 25 degrees Celsius)

proof_lines: kcat is 0.148 sec(-1) with cis-trans-nepetalactol as substrate (in the presence of NAD(+) at pH 8.0 and 25 degrees Celsius). kcat is 0.32 sec(-1) with cis-cis-nepetalactol as substrate (in the presence of NAD(+) at pH 8.0 and 25 degrees Cel

enzyme: (+)-cis,trans-nepetalactol synthase


substrate_name: NAD(+) (in the presence of cis-trans-nepetalactol at pH 8.0 and 25 degrees Celsius)


substrate_name: H2O; ATP

substrate: H2O; ATP


organism: Mus musculus

substrate_name: ATP; H2O

substrate: ATP; H2O


organism: Citrullus lanatus

substrate_name: Lycopene

substrate: Lycopene


organism: Capsicum annuum

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: Prosolanapyrone II

substrate: Prosolanapyrone II


assay_conditions_summary: pH 6.8; 295.15 K; cofactor ATP


enzyme_display_name: (S)-beta-macrocarpene synthase

organism: Zea mays

substrate_name: farnesyl diphosphate

assay_conditions_summary: pH 7; buffer 100 uL assay

column_label: Table 1; row label: TPS6-B73; column label: FPP / Km column; raw value 2.1 uM; normalized value 0.0021 mM.

normalized_value_unit_evidence: Km=0.0021 mM after converting 2.1 uM from Table 1.

raw_value_unit_evidence: Table 1; TPS6-B73; FPP / Km column = 2.1 uM (footnote a).

row_label: TPS6-B73 table row / FPP / Km column

table_label: Table 1. Kinetic constants for TPS6-B73 heterologously expressed in E. coli

enzyme: (S)-beta-macrocarpene synthase


column_label: Table 1; row label: TPS6-B73; column label: GPP / Km column; raw value 1.1 uM; normalized value 0.0011 mM.

normalized_value_unit_evidence: Km=0.0011 mM after converting 1.1 uM from Table 1.

raw_value_unit_evidence: Table 1; TPS6-B73; GPP / Km column = 1.1 uM (footnote a).

row_label: TPS6-B73 table row / GPP / Km column


substrate_name: magnesium (in the presence of 10 uM farnesyl diphosphate)

smiles: [Mg]

assay_conditions_summary: pH 7; buffer assay

column_label: Table 1; row label: TPS6-B73; column label: Mg2+ / Km column; raw value 130.7 uM; normalized value 0.1307 mM.

normalized_value_unit_evidence: Km=0.1307 mM after converting 130.7 uM from Table 1.

raw_value_unit_evidence: Table 1; TPS6-B73; Mg2+ / Km column = 130.7 uM (footnote b).

row_label: TPS6-B73 table row / Mg2+ / Km column


substrate_name: manganese (in the presence of 10 uM farnesyl diphosphate)

smiles: [Mn]

column_label: Table 1; row label: TPS6-B73; column label: Mn2+ / Km column; raw value 23.4 uM; normalized value 0.0234 mM.

normalized_value_unit_evidence: Km=0.0234 mM after converting 23.4 uM from Table 1.

raw_value_unit_evidence: Table 1; TPS6-B73; Mn2+ / Km column = 23.4 uM (footnote b).

row_label: TPS6-B73 table row / Mn2+ / Km column


organism: Drosophila melanogaster

substrate_name: ATP

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


organism: Mycobacterium tuberculosis

substrate_name: (E,E,E)-geranylgeranyl diphosphate

substrate: (E,E,E)-geranylgeranyl diphosphate


proof_lines:
microtubule-free KSP
microtubule-free KSP + 50 microM KSPA-1
KSP + microtubules + 30 microM KSPA-1


substrate_name: Unknown

proof_lines: inhibition of the microtubule-stimulated ATP activity of the ispinesib resistant mutant KHC-L5


assay_conditions_summary: pH 6.8; cofactor ATP

proof_lines: inhibition of the microtubule-stimulated ATP activity

proof_lines: pH 6.8, temperature not specified in the publication


proof_lines: pH 8.0, 28°C, mutant enzyme MEI-1 K293A/MEI-2


enzyme_display_name: phosphoribosylanthranilate isomerase

organism: Escherichia coli

proof_lines:
pH 7.5
25°C, bifunctional IGPS:PRAI
25°C, monomeric domain PRAI[ML256-452]

enzyme: phosphoribosylanthranilate isomerase


organism: Cinnamomum burmanni


enzyme_display_name: glutamine synthetase

substrate_name: Gln

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

enzyme: glutamine synthetase

substrate: Gln


substrate_name: methyl aklanonate

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

assay_conditions_summary: pH 7

substrate: methyl aklanonate


mutation_signature: Kinetic parameters shown are for full-length enzyme. N-terminally truncated spastin (residues 228-616)


enzyme_display_name: ADP-glyceromanno-heptose 6-epimerase

substrate_name: ADP-D-glycero-D-manno-heptose

assay_conditions_summary: cofactor ADP

enzyme: ADP-glyceromanno-heptose 6-epimerase

substrate: ADP-D-glycero-D-manno-heptose


substrate_name: formate

substrate: formate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R169T to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

substrate: ATP


substrate_name: holo-[aryl-carrier protein EntB]

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

proof_lines: product analog inhibitor, competitive inhibitor, result indicates that the catecholic 2-OH group is critical for tight binding

substrate: holo-[aryl-carrier protein EntB]


enzyme_display_name: isochorismate synthase

substrate_name: chorismate

proof_lines:
in absence of 2-mercaptoethanol
in presence of 2-mercaptoethanol

enzyme: isochorismate synthase

substrate: chorismate


enzyme_display_name: tRNA pseudouridine(38-40) synthase

substrate_name: tRNAHis guanidine36 uridine38 cytidine39

enzyme: tRNA pseudouridine(38-40) synthase


enzyme_display_name: chorismate mutase

assay_conditions_summary: pH 7.8; 310.15 K; cofactor NAD+

proof_lines: genetically engineered enzyme containg the amino acid residues 1-300

proof_lines: genetically engineered enzyme containg the amino acid residues 1-285

enzyme: chorismate mutase


enzyme_display_name: D-alanine--D-alanine ligase

substrate_name: D-serine

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

enzyme: D-alanine--D-alanine ligase

substrate: D-serine


enzyme_display_name: peptidylprolyl isomerase

enzyme: peptidylprolyl isomerase

substrate: Unknown


enzyme_display_name: L-rhamnose isomerase

substrate_name: L-rhamnulose

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

enzyme: L-rhamnose isomerase

substrate: L-rhamnulose


enzyme_display_name: cellobiose epimerase

organism: [Eubacterium] cellulosolvens

substrate_name: lactose

proof_lines: pH and temperature not specified in the publication

enzyme: cellobiose epimerase

substrate: lactose


enzyme_display_name: adenylate cyclase

organism: Euglena gracilis

assay_conditions_summary: 298.15 K; cofactor ATP

proof_lines: 25°C, plasma membrane isolated from glutamate/malate grown cells

proof_lines: 25°C, plasma membrane isolated from lactic acid grown cells

enzyme: adenylate cyclase


organism: Flavobacterium johnsoniae


enzyme_display_name: bisphosphoglycerate mutase

organism: Gallus gallus

proof_lines: presence of activator 2-phosphoglycolate

enzyme: bisphosphoglycerate mutase


enzyme_display_name: aldose 1-epimerase

substrate_name: alpha-D-glucose

enzyme: aldose 1-epimerase

substrate: alpha-D-glucose


organism: Ganoderma lucidum

substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


enzyme_display_name: methionine gamma-lyase

organism: Fusobacterium nucleatum subsp. nucleatum

substrate_name: L-cysteine

sequence_source: UniProtKB/Swiss-Prot Q8RDT4 FASTA

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

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

enzyme: methionine gamma-lyase

substrate: L-cysteine


enzyme_display_name: isopentenyl-diphosphate Delta-isomerase

substrate_name: isopentenyl diphosphate

proof_lines:
isomerase II and III
isomerase I
isomerase IV

enzyme: isopentenyl-diphosphate Delta-isomerase

substrate: isopentenyl diphosphate


enzyme_display_name: myosin ATPase

organism: Oryctolagus cuniculus

substrate_name: CTP

enzyme: myosin ATPase

substrate: CTP


substrate_name: UTP

substrate: UTP


substrate_name: TTP

substrate: TTP


substrate_name: GTP

substrate: GTP


substrate_name: ITP

substrate: ITP


enzyme_display_name: proteasome ATPase

organism: Methanocaldococcus jannaschii

enzyme: proteasome ATPase


substrate_name: ATP

mutation_signature: Δ1

mutation_type: deletion


enzyme_display_name: dynein ATPase

organism: Saccharomyces cerevisiae

proof_lines:
mutant E2488Q, basal activity
mutant E2488Q, microtubule-stimulated

enzyme: dynein ATPase


proof_lines:
mutant E2819Q, basal activity
mutant E2819Q, microtubule-stimulated


proof_lines:
basal activity
microtubule-stimulated


substrate_name: a dynein associated with a microtubule at position n


substrate: a dynein associated with a microtubule at position n


enzyme_display_name: plus-end-directed kinesin ATPase

organism: Dictyostelium discoideum

mutation_signature: truncated Kif3-342

proof_lines: truncated protein Kif3-342, 22°C, pH 6.8

enzyme: plus-end-directed kinesin ATPase

substrate: ATP


mutation_signature: truncated Kif3-592

proof_lines: truncated protein Kif3-592, 22°C, pH 6.8


organism: Schizosaccharomyces pombe

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


mutation_signature: C-terminally truncated enzyme

proof_lines: C-terminally truncated enzyme, at pH 7.5 and 37°C


organism: Neurospora crassa

substrate_name: phosphate

proof_lines: in presence of microtubule the ATP hydrolysis is activated 3fold to 4fold compared to kcat, 125 vs. 34 s-1, while phosphate release is approximately equally fast: 29 s-1, pH and temperature not specified in the publication

substrate: phosphate


substrate_name: ADP

substrate: ADP


organism: Heliocidaris crassispina

proof_lines: 12S sucrose gradient fraction of inner arm dynein

proof_lines: 21S sucrose gradient fraction of outer arm dynein


organism: Bos taurus

proof_lines:
19S sucrose gradient dynein particle
12S sucrose gradient dynein particle


organism: Lytechinus pictus

proof_lines: latent dynein ATPase 1, in the presence of 0.02 mM P1,P5-di(adenosine-5')-pentaphosphate


proof_lines:
in the presence of microtubules
in the absence of microtubules


organism: Tetrahymena pyriformis

proof_lines: 30S dynein, in the absence of tubulin, 1 mM KCl

proof_lines: 30S dynein, in the presence of tubulin, 1 mM KCl


organism: Tetrahymena thermophila

assay_conditions_summary: pH 7; 301.15 K; cofactor ATP

proof_lines: 22S sucrose gradient fraction, per site at pH 7 and 28°C


substrate_name: Formycin triphosphate

substrate: Formycin triphosphate


organism: Hemicentrotus pulcherrimus


organism: Tripneustes gratilla

proof_lines:
21S dynein 1
12S dynein 2


organism: Plasmodium berghei

assay_conditions_summary: pH 7; 299.15 K; cofactor ATP


proof_lines: in 12.5 mM ACES-KOH, 25 mM potassium acetate, 5 mM MgCl2, 0.5 M EGTA, pH 6.8, at 22°C


enzyme_display_name: minus-end-directed kinesin ATPase

organism: Eremothecium gossypii

assay_conditions_summary: pH 6.9; 295.15 K; cofactor ATP

proof_lines: motor domain, 25 mM potassium acetate, Vmax/2 at 0.0007 mM microtubles, pH 6.9, 22°C

proof_lines: motor domain, 0 mM potassium acetate, Vmax/2 at 0.00008 mM microtubles, pH 6.9, 22°C

proof_lines: motor domain, 0 mM potassium acetate, pH 6.9, 22°C

enzyme: minus-end-directed kinesin ATPase


organism: Plasmodium falciparum


organism: Bifidobacterium longum subsp. infantis

assay_conditions_summary: pH 5; 310.15 K; cofactor ATP


organism: Rattus norvegicus

proof_lines:
rSUG1 + 0.001 mg poly(U)
rSUG1 + 0.0005 mg poly(U)
rSUG1 + 0.00025 mg poly(U)


enzyme_display_name: chaperonin ATPase

organism: Pyrococcus furiosus

assay_conditions_summary: pH 7.5; 358.15 K; cofactor ATP

enzyme: chaperonin ATPase


organism: Lathyrus oleraceus

assay_conditions_summary: cofactor ATP


organism: Saccharomyces cerevisiae


organism: Escherichia coli


substrate_name: K48-GREEN-TAIL polypeptide

proof_lines:
at pH 7.6 and 30°C
at pH and ?C

substrate: K48-GREEN-TAIL polypeptide


organism: Dictyostelium sp.

proof_lines: chimeric myosin, Dictyostelium myosin loop 2 replaced by chicken smooth muscle myosin loop 2, actin activated


organism: Caenorhabditis elegans


enzyme_display_name: inositol-3-phosphate synthase

organism: Bos taurus

substrate_name: D-glucose 6-phosphate

proof_lines: with addition of 5% ethanol plus 50 mM KCl

enzyme: inositol-3-phosphate synthase

substrate: D-glucose 6-phosphate


organism: Gallus gallus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: actin-activated, unphosphorylated myosin, pH 7.5, 25°C


organism: Lethocerus griseus

proof_lines: activation with 0.02 mM actin from rabbit skeletal muscle

proof_lines: activation with 0.06 mM actin from rabbit skeletal muscle


organism: Mammalia

proof_lines:
Myo1b1IQ-GAGEGA, pCa 8.9
Myo1b1IQ-WT, pCa 4.6
Myo1b1IQ-WT, pCa 8.9


organism: Oryctolagus cuniculus

substrate_name: ATP; H2O

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

proof_lines:
pH 7.6, 25°C, cosubstrate GTP
pH 7.6, 25°C, cosubstrate ITP
pH 7.6, 25°C, presence of Sr2+ at 2 mM

substrate: ATP; H2O


proof_lines:
Mg-ATPase, 0.6 M KCl
Ca-ATPase, 2.0 mM Ca2+
K+EDTA-ATPase, 1 mM EDTA


assay_conditions_summary: pH 7; 296.15 K; cofactor ATP

proof_lines: enzyme in complex with the calmodulin-like domain of its light chain MLC-B, at pH 7.0 and 23°C


organism: Lethocerus indicus


organism: Sus scrofa

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines: in the presence of 5 mM Zn2+, at pH 7.2 and 37°C

proof_lines: in the absence of Zn2+, at pH 7.2 and 37°C


organism: Homo sapiens

proof_lines: beta-cardiac myosin isoform, at pH 7.0 and 20°C

proof_lines: embryonic myosin isoform, at pH 7.0 and 20°C


organism: Mus musculus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A247C to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.7; 298.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G272C with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A252C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S275C to reconstruct the assayed variant sequence.


substrate_name: Unknown

substrate: Unknown


proof_lines: various isoenzymes of subfragment 1 and heavy-meromyosin, absence of actin


organism: Drosophila melanogaster

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E585D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: mutant NcN-E585D, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C


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

proof_lines: E585D/E585E, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C


proof_lines: mutant E585A/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C

proof_lines: mutant E552A/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C

proof_lines: mutant E552A plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C


organism: Thermoplasma acidophilum

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D94A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 328.15 K; cofactor ATP

proof_lines: mutant enzyme D94A, with rhamnose dehydrogenase as protein substrate, at pH 7.5 and 55°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D93K with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D93K, with rhamnose dehydrogenase as protein substrate, at pH 7.5 and 55°C


proof_lines: Ncd700SG (residue 250-700, residue 671-679 replaced by sequence GGSGGSGGS), microtuble stimulated, Vmax/2 at 0.00014 mM microtubles, pH 7.2, 25°C

proof_lines: Ncd670 (residue 250-670), microtuble stimulated, Vmax/2 at 0.00014 mM microtubles, pH 7.2, 25°C

proof_lines: NcdWT (residue 250-700), microtuble stimulated, Vmax/2 at 0.00022 mM microtubles, pH 7.2, 25°C


proof_lines: mutant Ncd700SG, pH 7.2, 25°C, microtubule-stimulated ATPase activity

proof_lines: mutant Ncd670, pH 7.2, 25°C, microtubule-stimulated ATPase activity

proof_lines: mutant NcN, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M672N to reconstruct the assayed variant sequence.

proof_lines: NcdM672N (residue 250-679, M672N mutation), microtuble stimulated, Vmax/2 at 0.00061 mM microtubles, pH 7.2, 25°C


proof_lines:
asthenozoospermic samples
normozoospermic samples


assay_conditions_summary: pH 7.2; 298.15 K; cofactor ATP

proof_lines: in presence of microtubles, pH 7.2, 25°C

proof_lines: in presence of microtubles, Vmax/2 at 0.0004 mM microtubles, pH 7.2, 25°C


organism: Acetivibrio thermocellus


organism: Schizosaccharomyces pombe

assay_conditions_summary: pH 6.8; cofactor ATP

proof_lines: green fluorescent protein-tagged Pkl1H, in 12 mM PIPES-KOH, 2 mM MgCl2, 1 mM EGTA, pH 6.8, containing 1 mM dithiothreitol, 0.7 mg/ml casein, and 1% (v/v) Tween 20 at 25°C


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: MgATP

proof_lines: kcat is 0.49 sec(-1) with MgATP as substrate (PubMed:17382884). kcat is 2.8 sec(-1) with MgATP as substrate in complex with CIK1 (PubMed:17382884). kcat is 3.7 sec(-1) with MgATP as substrate in complex with VIK1 (PubMed:17382884).

substrate: MgATP


organism: Escherichia coli


organism: Allochromatium vinosum


substrate_name: MgATP in complex with CIK1

substrate: MgATP in complex with CIK1


enzyme_display_name: channel-conductance-controlling ATPase

enzyme: channel-conductance-controlling ATPase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat for ATPase activity is 0.16 min(-1).


proof_lines: kcat for ATPase activity is 0.28 min(-1) (PubMed:15327959). kcat for ATPase activity is 0.18 min(-1) (PubMed:21802426).


organism: Dictyostelium discoideum

proof_lines: ATPase activity of the actomyosin complex


enzyme_display_name: microtubule-severing ATPase

organism: Caenorhabditis elegans

substrate_name: ATP (at 37 degrees Celsius and pH 8.8)

enzyme: microtubule-severing ATPase

substrate: ATP (at 37 degrees Celsius and pH 8.8)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y485W to reconstruct the assayed variant sequence.


substrate_name: glutathione (in the presence of MgAMP-PNP)

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

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

column_label: Figure 1C caption and adjacent results prose report CFTR-mediated GSH flux in the presence of MgAMP-PNP with K_m 0.47 mM.

raw_value_unit_evidence: Km raw_value=0.47 raw_unit=mM

row_label: wild-type CFTR-dependent GSH flux in the presence of MgAMP-PNP

table_label: PMC Fig. 1C caption and results prose PMID 12727866


organism: Danio rerio

column_label: Cell full text reports: Phosphorylated zebrafish CFTR has a KM of 0.22 mM for ATP, comparable to the 0.30 mM value reported for human CFTR.

raw_value_unit_evidence: Km raw_value=0.22 raw_unit=mM

row_label: phosphorylated zebrafish CFTR / ATPase activity

table_label: Results and Discussion / Figure 1 Biochemical Properties of Zebrafish CFTR


organism: Methanococcus maripaludis

column_label: Prose section 'ATPase activity and stability of Mm-cpn as a function of temperature', PDF page 3 / journal page 671; metric label ATPase activity/rate; substrate ATP; raw value 59.4 +/- 2.1 ATP min^-1 at 37 C.

normalized_value_unit_evidence: kcat normalized_value=0.99 normalized_unit=s^-1 from 59.4 ATP min^-1 / 60

raw_value_unit_evidence: Prose states that the Mm-cpn oligomer hydrolyses ATP at a rate of 59.4 +/- 2.1 ATP min^-1 at 37 C.

row_label: Mm-cpn oligomer, ATPase rate at 37 C

table_label: Prose section: ATPase activity and stability of Mm-cpn as a function of temperature


assay_conditions_summary: pH 6.8; 298.15 K; cofactor ATP

proof_lines: in presence of mutant microtubles alpha-E415A, pH 6.8, 25°C


proof_lines: in presence of mutant microtubles alpha-E416A, pH 6.8, 25°C


proof_lines: in presence of mutant microtubles alpha-E418A, pH 6.8, 25°C


proof_lines: in presence of mutant microtubles alpha-E421A, pH 6.8, 25°C


proof_lines: in presence of mutant microtubles beta-E410A, pH 6.8, 25°C


proof_lines:
basal MgATPase activity
Vmax of actin-activated ATPase activity
basal CaATPase activity


substrate_name: actin

substrate: actin


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)


organism: Acanthamoeba castellanii

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S639D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; cofactor ATP

proof_lines: mutant S639D, pH 7.0, 30°C, in presence of F-actin


proof_lines: wild-type S1 fragment, pH 7.0, 30°C, in presence of F-actin

proof_lines: wild-type S1 fragment, pH 7.0, 30°C, hyperbolic fit


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D417A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

proof_lines: in presence of mutant microtubles beta-D417A, pH 6.8, 25°C


proof_lines:
wild-type
wild-type, pH 6.8


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


enzyme_display_name: UniProt P11388

enzyme: UniProt P11388


enzyme_display_name: UniProt P38935

enzyme: UniProt P38935


substrate_name: methylanthraniloyl-ATP

assay_conditions_summary: pH 6.9; 298.15 K; cofactor ATP

proof_lines: basal activity, in absence of tubulin or microtubles, pH 6.9, 25°C

proof_lines: +/-0.022 mM, Vmax: 247 nmol/s, pH and temperature not specified in the publication. The fluorescent ATP analog can fuel kinesin-1'S processsive motion and is a suitable substrate analog, but it alters the motor's kinetic parameters

substrate: methylanthraniloyl-ATP


proof_lines: in presence of unpolymerized tubulin, pH 6.9, 25°C


assay_conditions_summary: 293.15 K; cofactor ATP

proof_lines: Mn2+ concentration variable, ATP concentration fixed, Mn-ATP complexes at 1 mM ATP and 0.8 mM Mn2+

proof_lines: ATP concentration variable, Mn2+ concentration fixed, Mn-ATP complexes at 1 mM ATP and 0.8 mM Mn2+


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


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

proof_lines: wild-type KIF4 enzyme, pH and temperature not specified in the publication

proof_lines: recombinant wild-type K888, pH and temperature not specified in the publication


organism: Saccharomyces cerevisiae

proof_lines: both wild-type and GST-fusion protein, pH 7.2, 25°C


enzyme_display_name: RNA 3'-5' helicase

organism: West Nile virus

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

enzyme: RNA 3'-5' helicase


substrate_name: GTP


proof_lines: pH 7.5, 37°C, wild-type enzyme, inhibition of the ATPase reaction


substrate_name: ITP


substrate_name: ribavirin triphosphate

substrate: ribavirin triphosphate


enzyme_display_name: DNA 5'-3' helicase

organism: Severe acute respiratory syndrome-related coronavirus

enzyme: DNA 5'-3' helicase

substrate: GTP


substrate_name: dGTP

substrate: dGTP


substrate_name: UTP

substrate: UTP


substrate_name: CTP

substrate: CTP


substrate_name: dCTP

substrate: dCTP


substrate_name: dATP

substrate: dATP


substrate_name: dUTP

substrate: dUTP


substrate_name: ATP

assay_conditions_summary: pH 6.6; 298.15 K; cofactor ATP

substrate: ATP


enzyme_display_name: DEAD-box RNA helicase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q169E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor ATP

table_label: Table I. Kinetic parameters for RNA-dependent ATPase activity

enzyme: DEAD-box RNA helicase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F162A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q169A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T166S to reconstruct the assayed variant sequence.