enzyme_display_name: xylan 1,4-beta-xylosidase; gene bxtw1; UniProtKB unreviewed entry A0A0H3W535_TALAM

sequence_source: UniProtKB REST A0A0H3W535.json/fasta; PMID 26150469; GenBank/EMBL AKJ79184.1; organism Talaromyces amestolkiae; EC 3.2.1.37


organism: Talaromyces amestolkiae

substrate_name: xylobiose

source_db: oed

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

data_origin: experimental

enzyme: xylan 1,4-beta-xylosidase; gene bxtw1; UniProtKB unreviewed entry A0A0H3W535_TALAM

substrate: xylobiose

status: unverified

source: oed


enzyme_display_name: xylan 1,4-beta-xylosidase; gene bxl1; UniProtKB unreviewed entry Q8X212_RASEM

organism: Talaromyces emersonii

substrate_name: p-Nitrophenyl-beta-D-xylopyranoside

sequence_source: UniProtKB REST Q8X212.json/fasta; PMID 12763033 sequence reference; selected PMID 16752410 kinetics; organism Rasamsonia emersonii with synonym Talaromyces emersonii; EC 3.2.1.37

substrate: p-Nitrophenyl-beta-D-xylopyranoside


substrate_name: xylotriose

enzyme: xylan 1,4-beta-xylosidase; gene bxl1; UniProtKB unreviewed entry Q8X212_RASEM

substrate: xylotriose


substrate_name: Xylotetraose

substrate: Xylotetraose


substrate_name: xylopentaose

substrate: xylopentaose


substrate_name: Xylohexaose

substrate: Xylohexaose


enzyme_display_name: versatile peroxidase

organism: Pleurotus eryngii

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from official_uniprot_json:O94753 and applied mutation signature K176G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

mutation_type: substitution

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 2; measurement identity label: K176G; 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid); low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 2, K176G; 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid); low-efficiency site: Km 0.383 ± 0.014 mM; kcat 259 ± 3 s^-1; kcat/Km 676 ± 18 s^-1 mM^-1.

table_label: Table 2

enzyme: versatile peroxidase

status: corrected


sequence_variant_note: Resolved canonical sequence from official_uniprot_json:O94753 and applied mutation signature P76G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: P76G; 2,6-dimethoxyphenol; DMP high-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, P76G; 2,6-dimethoxyphenol; DMP high-efficiency site: Km 0.036 ± 0.003 mM; kcat 6.2 ± 0.1 s^-1; kcat/Km 171 ± 12 s^-1 mM^-1.

table_label: Table 3


substrate_name: guaiacol

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O94753 and applied mutation signature E140G/P141G/K176G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants of native VP, and multiple variants; Km in uM, kcat in s^-1, kcat/Km in s^-1 mM^-1), block head 'Guaiacol', column head 'E140G/P141G/K176G'; the block's Km line reads 14,200, its kcat line reads 19.3, and its kcat/Km line reads 1.4 in that column.

normalized_value_unit_evidence: Km: printed Table 4 cell 14,200 uM; 14200 / 1000 = 14.2 mM. kcat: printed Table 4 cell 19.3 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 19.3 s^(-1). kcat/Km: printed Table 4 cell 1.4 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the normalized value is 1.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Guaiacol block, column E140G/P141G/K176G: Km = 14,200 uM; kcat = 19.3 s^-1; printed kcat/Km = 1.4 s^-1 mM^-1.

row_label: Table 4, Guaiacol block, E140G/P141G/K176G column

table_label: Table 4: Steady-state kinetic constants of native VP, and multiple variants (Km in uM, kcat in s^-1, and kcat/Km in s^-1 mM^-1) for oxidation of catechol, guaiacol, HQ, and DMP, the last two ones at high and low efficiency sites (J. Biol. Chem. 2012, 287(49):41053-41067)

substrate: guaiacol


substrate_name: catechol

sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 canonical precursor; PMID 23071108 mature-chain mutation reconstructed with +30 offset and applied mutation signature K215Q with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

substrate: catechol


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O94753 and applied mutation signature E140G/W164S/K176G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants of native VP, and multiple variants; Km in uM, kcat in s^-1, kcat/Km in s^-1 mM^-1), block head 'Guaiacol', column head 'E140G/W164S/K176G'; the block's Km line reads 5,850, its kcat line reads 54.2, and its kcat/Km line reads 9.3 in that column.

normalized_value_unit_evidence: Km: printed Table 4 cell 5,850 uM; 5850 / 1000 = 5.85 mM. kcat: printed Table 4 cell 54.2 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 54.2 s^(-1). kcat/Km: printed Table 4 cell 9.3 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the normalized value is 9.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Guaiacol block, column E140G/W164S/K176G: Km = 5,850 uM; kcat = 54.2 s^-1; printed kcat/Km = 9.3 s^-1 mM^-1.

row_label: Table 4, Guaiacol block, E140G/W164S/K176G column


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 canonical precursor; PMID 23071108 mature-chain mutation reconstructed with +30 offset and applied mutation signature E140G/P141G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from official_uniprot_json:O94753 and applied mutation signature F142G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: F142G; guaiacol; guaiacol; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, F142G; guaiacol; guaiacol: Km 10.800 ± 0.400 mM; kcat 17.5 ± 0.2 s^-1; kcat/Km 1.6 ± 0.0 s^-1 mM^-1.

row_label: F142G; guaiacol; guaiacol


column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: K176G; 4-hydroquinone; HQ low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, K176G; 4-hydroquinone; HQ low-efficiency site: Km 1.050 ± 0.080 mM; kcat 70.6 ± 1.9 s^-1; kcat/Km 67.0 ± 3.8 s^-1 mM^-1.


sequence_source: UniProtKB O94753 FASTA direct accession lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB O94753 FASTA direct accession lookup and applied mutation signature K215G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: F142G; 4-hydroquinone; HQ low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, F142G; 4-hydroquinone; HQ low-efficiency site: Km 0.380 ± 0.017 mM; kcat 19.2 ± 0.2 s^-1; kcat/Km 50.6 ± 1.8 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from official_uniprot_json:O94753 and applied mutation signature E140G/K176G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 4; measurement identity label: E140G/K176G; 4-hydroquinone; HQ low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 4, E140G/K176G; 4-hydroquinone; HQ low-efficiency site: Km 0.618 ± 0.036 mM; kcat 82.1 ± 1.3 s^-1; kcat/Km 132.8 ± 1.0 s^-1 mM^-1.

table_label: Table 4


sequence_variant_note: Resolved canonical sequence from official_uniprot_json:O94753 and applied mutation signature P141G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 2; measurement identity label: P141G; 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid); low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 2, P141G; 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid); low-efficiency site: Km 0.461 ± 0.022 mM; kcat 93 ± 2 s^-1; kcat/Km 201 ± 7 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from official_uniprot_json:O94753 and applied mutation signature E140G/W164S/K176G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 4; measurement identity label: E140G/W164S/K176G; 4-hydroquinone; HQ low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 4, E140G/W164S/K176G; 4-hydroquinone; HQ low-efficiency site: Km 0.884 ± 0.071 mM; kcat 85.6 ± 2.3 s^-1; kcat/Km 96.8 ± 5.8 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from official_uniprot_json:O94753 and applied mutation signature E140G/P141G/K176G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 4; measurement identity label: E140G/P141G/K176G; 2,6-dimethoxyphenol; DMP low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 4, E140G/P141G/K176G; 2,6-dimethoxyphenol; DMP low-efficiency site: Km 2.380 ± 0.200 mM; kcat 56.6 ± 1.3 s^-1; kcat/Km 23.8 ± 1.6 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from official_uniprot_json:O94753 and applied mutation signature K215Q with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 2; measurement identity label: K215Q; 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid); low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 2, K215Q; 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid); low-efficiency site: Km 1.660 ± 0.130 mM; kcat 165 ± 5 s^-1; kcat/Km 99 ± 10 s^-1 mM^-1.


sequence_source: UniProtKB:O94753 reviewed Swiss-Prot VPL2_PLEER sequence retrieved by direct UniProt REST check on 2026-06-01

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: native VP; catechol; catechol; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, native VP; catechol; catechol: Km 5.040 ± 0.200 mM; kcat 185 ± 3 s^-1; kcat/Km 36.7 ± 1 s^-1 mM^-1.

row_label: native VP; catechol; catechol


column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 4; measurement identity label: E140G/K176G; 2,6-dimethoxyphenol; DMP low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 4, E140G/K176G; 2,6-dimethoxyphenol; DMP low-efficiency site: Km 2.970 ± 0.130 mM; kcat 67.0 ± 0.9 s^-1; kcat/Km 22.6 ± 0.8 s^-1 mM^-1.


column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: P141G; 4-hydroquinone; HQ low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, P141G; 4-hydroquinone; HQ low-efficiency site: Km 1.114 ± 0.059 mM; kcat 108.0 ± 2.1 s^-1; kcat/Km 97.0 ± 3.0 s^-1 mM^-1.


column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: K176G; guaiacol; guaiacol; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, K176G; guaiacol; guaiacol: Km 16.200 ± 0.700 mM; kcat 33.3 ± 0.7 s^-1; kcat/Km 2.0 ± 0.0 s^-1 mM^-1.

row_label: K176G; guaiacol; guaiacol


sequence_variant_note: Resolved canonical sequence from official_uniprot_json:O94753 and applied mutation signature E140G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: E140G; catechol; catechol; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, E140G; catechol; catechol: Km 4.260 ± 0.200 mM; kcat 164 ± 3 s^-1; kcat/Km 38.4 ± 0.7 s^-1 mM^-1.

row_label: E140G; catechol; catechol


column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: native VP; guaiacol; guaiacol; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, native VP; guaiacol; guaiacol: Km 11.100 ± 0.600 mM; kcat 22.7 ± 0.5 s^-1; kcat/Km 2.0 ± 0.0 s^-1 mM^-1.

row_label: native VP; guaiacol; guaiacol


column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: F142G; catechol; catechol; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, F142G; catechol; catechol: Km 5.150 ± 0.290 mM; kcat 75 ± 1 s^-1; kcat/Km 14.5 ± 0.6 s^-1 mM^-1.

row_label: F142G; catechol; catechol


organism: Amycolatopsis sp.


substrate_name: Reactive black 5

substrate: Reactive black 5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:O94753 and applied mutation signature D175A with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


substrate_name: Veratryl alcohol

substrate: Veratryl alcohol


sequence_variant_note: Resolved canonical sequence from UniProt O94753 FASTA plus mature-chain mutation reconstruction and applied mutation signature K215G with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 4; measurement identity label: E140G/P141G/K176G; catechol; catechol; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 4, E140G/P141G/K176G; catechol; catechol: Km 4.720 ± 0.320 mM; kcat 135.7 ± 3.7 s^-1; kcat/Km 28.8 ± 1.3 s^-1 mM^-1.

row_label: E140G/P141G/K176G; catechol; catechol


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O94753 and applied mutation signature E140G/P141G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants of native VP, and multiple variants; Km in uM, kcat in s^-1, kcat/Km in s^-1 mM^-1), block head 'Guaiacol', column head 'E140G/P141G'; the block's Km line reads 5,100, its kcat line reads 3.1, and its kcat/Km line reads 0.6 in that column.

normalized_value_unit_evidence: Km: printed Table 4 cell 5,100 uM; 5100 / 1000 = 5.1 mM. kcat: printed Table 4 cell 3.1 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 3.1 s^(-1). kcat/Km: printed Table 4 cell 0.6 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the normalized value is 0.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Guaiacol block, column E140G/P141G: Km = 5,100 uM; kcat = 3.1 s^-1; printed kcat/Km = 0.6 s^-1 mM^-1.

row_label: Table 4, Guaiacol block, E140G/P141G column


sequence_source: UniProt O94753 FASTA plus mature-chain mutation reconstruction

sequence_variant_note: Mutation signature K215Q matches the mutant residue at offset +30 and the reference residue at offset -9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


verification_status: verified

sequence_variant_note: Resolved canonical sequence from official_uniprot_json:O94753 and applied mutation signature K176D with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 2; measurement identity label: K176D; 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid); low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 2, K176D; 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid); low-efficiency site: Km 2.230 ± 0.170 mM; kcat 223 ± 8 s^-1; kcat/Km 100 ± 0 s^-1 mM^-1.

status: verified


column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: E140G; guaiacol; guaiacol; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, E140G; guaiacol; guaiacol: Km 1.970 ± 0.150 mM; kcat 34.8 ± 0.5 s^-1; kcat/Km 17.6 ± 1.1 s^-1 mM^-1.

row_label: E140G; guaiacol; guaiacol


column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: K176D; 4-hydroquinone; HQ low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, K176D; 4-hydroquinone; HQ low-efficiency site: Km 0.420 ± 0.006 mM; kcat 25.2 ± 0.1 s^-1; kcat/Km 59.9 ± 0.6 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from official_uniprot_json:O94753 and applied mutation signature W164S with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 2; measurement identity label: W164S; 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid); low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 2, W164S; 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid); low-efficiency site: Km 1.000 ± 0.010 mM; kcat 205 ± 8 s^-1; kcat/Km 200 ± 10 s^-1 mM^-1.


kcat_over_km_display: Not reported

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 2; measurement identity label: E140G; 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid); low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 2, E140G; 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid); low-efficiency site: Km 0.305 ± 0.023 mM; kcat 216 ± 6 s^-1; kcat/Km 710 ± 40 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from official_uniprot_json:O94753 and applied mutation signature P76G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: P76G; catechol; catechol; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, P76G; catechol; catechol: Km 4.790 ± 0.180 mM; kcat 99 ± 1 s^-1; kcat/Km 20.7 ± 0.6 s^-1 mM^-1.

row_label: P76G; catechol; catechol


column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 4; measurement identity label: E140G/W164S/K176G; 2,6-dimethoxyphenol; DMP low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 4, E140G/W164S/K176G; 2,6-dimethoxyphenol; DMP low-efficiency site: Km 3.330 ± 0.260 mM; kcat 50.2 ± 1.7 s^-1; kcat/Km 15.1 ± 0.7 s^-1 mM^-1.


column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 4; measurement identity label: E140G/K176G; catechol; catechol; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 4, E140G/K176G; catechol; catechol: Km 2.630 ± 0.070 mM; kcat 185.6 ± 1.3 s^-1; kcat/Km 70.7 ± 1.5 s^-1 mM^-1.

row_label: E140G/K176G; catechol; catechol


column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: P76G; guaiacol; guaiacol; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, P76G; guaiacol; guaiacol: Km 16.300 ± 0.900 mM; kcat 26.2 ± 0.7 s^-1; kcat/Km 1.6 ± 0.0 s^-1 mM^-1.

row_label: P76G; guaiacol; guaiacol


column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: W164S; catechol; catechol; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, W164S; catechol; catechol: Km 7.760 ± 0.320 mM; kcat 8 ± 0 s^-1; kcat/Km 1.0 ± 0.0 s^-1 mM^-1.

normalized_value_unit_evidence: Km=7.760 mM; kcat=8 s^-1; printed kcat/Km=1.0 s^-1 mM^-1.

row_label: W164S; catechol; catechol


sequence_source: UniProtKB O94753 reviewed canonical precursor FASTA fetched via UniProt REST on 2026-06-01.

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 O94753 canonical precursor sequence; mutation signature applied after mature-chain coordinate mapping (+30 from UniProt chain start at residue 31) and applied mutation signature P141G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O94753 canonical precursor sequence; mutation signature applied after mature-chain coordinate mapping (+30 from UniProt chain start at residue 31) and applied mutation signature E140G/P141G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O94753 canonical precursor sequence; mutation signature applied after mature-chain coordinate mapping (+30 from UniProt chain start at residue 31) and applied mutation signature K176G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O94753 canonical precursor sequence; mutation signature applied after mature-chain coordinate mapping (+30 from UniProt chain start at residue 31) and applied mutation signature F142G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O94753 canonical precursor sequence; mutation signature applied after mature-chain coordinate mapping (+30 from UniProt chain start at residue 31) and applied mutation signature W164S with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O94753 canonical precursor sequence; mutation signature applied after mature-chain coordinate mapping (+30 from UniProt chain start at residue 31) and applied mutation signature K215G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_source: UniProt O94753 canonical precursor sequence; mutation signature applied after mature-chain coordinate mapping (+30 from UniProt chain start at residue 31)


sequence_variant_note: Resolved canonical sequence from official_uniprot_json:O94753 and applied mutation signature P141G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: P141G; catechol; catechol; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, P141G; catechol; catechol: Km 5.110 ± 0.320 mM; kcat 78 ± 2 s^-1; kcat/Km 15 ± 1 s^-1 mM^-1.

normalized_value_unit_evidence: Km=5.110 mM; kcat=78 s^-1; printed kcat/Km=15 s^-1 mM^-1.

row_label: P141G; catechol; catechol


sequence_variant_note: Resolved canonical sequence from official_uniprot_json:O94753 and applied mutation signature E140G/P141G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 4; measurement identity label: E140G/P141G; catechol; catechol; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 4, E140G/P141G; catechol; catechol: Km 10.500 ± 0.800 mM; kcat 105.6 ± 4.0 s^-1; kcat/Km 10.1 ± 0.4 s^-1 mM^-1.

row_label: E140G/P141G; catechol; catechol


organism: Rhodococcus jostii

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q0SE24 and applied mutation signature N246A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 5; 298.15 K; buffer 50 mM sodium malonate

column_label: Table 1 (Kinetic parameters of recombinant Rh_DypB peroxidase on Mn2+, ABTS, and 2,6-DMP), row (B) In presence of 0.3 mM H2O2, ABTS column group; column kcat (s^-1) = 15.4 ± 0.73; column Km (mM) = 15.6 ± 1.3; column kcat/Km (head prints no unit; decoded unit s^-1 mM^-1 from the kcat and Km column heads) = 0.98 ± 0.1.

normalized_value_unit_evidence: kcat: printed Table 1 row (B) ABTS cell 15.4 s^-1; already in s^-1, no unit conversion applies; the exported value is 15.4 s^(-1). Km: printed Table 1 row (B) ABTS cell 15.6 mM; already in mM, no unit conversion applies; the exported value is 15.6 mM. kcat/Km: printed Table 1 row (B) ABTS cell 0.98 in the kcat/Km column, whose unit is s^-1 mM^-1 because kcat is printed in s^-1 and Km in mM; already in s^-1 mM^-1, no unit conversion applies, so the paper value is 0.98 s^(-1)*mM^(-1); the exported value is 0.9871794871794872 s^(-1)*mM^(-1), which is the full-precision quotient 15.4 / 15.6.

raw_value_unit_evidence: Table 1, row (B) In presence of 0.3 mM H2O2, ABTS column group: kcat = 15.4 ± 0.73 s^-1; Km = 15.6 ± 1.3 mM; printed kcat/Km = 0.98 ± 0.1 in the kcat/Km column, whose head prints no unit and whose unit is s^-1 mM^-1 (the kcat column unit s^-1 over the Km column unit mM).

row_label: Table 1, row (B) In presence of 0.3 mM H2O2, ABTS column group (recombinant Rh_DypB, the N246A variant of R. jostii RHA1 DypB)

table_label: Table 1: Kinetic parameters of recombinant Rh_DypB peroxidase on Mn2+, ABTS, and 2,6-DMP (Appl Microbiol Biotechnol 2018, 102:10579-10588)


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q0SE24 FASTA retrieved 2026-06-01; N246A reconstructed after direct residue check showed canonical residue 246 is N. and applied mutation signature N246A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST Q0SE24 FASTA retrieved 2026-06-01; N246A reconstructed after direct residue check showed canonical residue 246 is N.

smiles: OO


sequence_variant_note: Resolved canonical sequence from UniProt REST O94753 exact accession; variant sequence reconstructed from the selected mutation signature using mature-enzyme residue numbering offset +30. and applied mutation signature K176D with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_source: UniProt REST O94753 exact accession; variant sequence reconstructed from the selected mutation signature using mature-enzyme residue numbering offset +30.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O94753 and applied mutation signature E140G/W164S/K176G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants of native VP, and multiple variants; Km in uM, kcat in s^-1, kcat/Km in s^-1 mM^-1), block head 'Catechol', column head 'E140G/W164S/K176G'; the block's Km line reads 34,10, its kcat line reads 164.8, and its kcat/Km line reads 48.4 in that column.

normalized_value_unit_evidence: Km: printed Table 4 cell 34,10 uM; that cell sets its digit-group comma one place too early, and reading the digit group as 3,410 gives 3410 uM, the only value that closes with the same column's printed kcat 164.8 s^-1 and printed kcat/Km 48.4 s^-1 mM^-1 (164.8 divided by 3.41 is 48.3) and the only value in line with the neighbouring catechol Km cells 10,500, 2,630 and 4,720 uM; 3410 / 1000 = 3.41 mM. kcat: printed Table 4 cell 164.8 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 164.8 s^(-1). kcat/Km: printed Table 4 cell 48.4 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the normalized value is 48.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Catechol block, column E140G/W164S/K176G: Km = 34,10 uM; kcat = 164.8 s^-1; printed kcat/Km = 48.4 s^-1 mM^-1.

row_label: Table 4, Catechol block, E140G/W164S/K176G column


sequence_variant_note: Resolved canonical sequence from UniProt REST Q0SE24 exact accession; variant sequence reconstructed from selected mutation signature against canonical UniProt coordinates. and applied mutation signature D153A/N246A to reconstruct the assayed variant sequence.


sequence_source: UniProt REST Q0SE24 exact accession canonical sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST Q0SE24 exact accession; variant sequence reconstructed from selected mutation signature against canonical UniProt coordinates. and applied mutation signature D153A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST Q0SE24 exact accession; variant sequence reconstructed from selected mutation signature against canonical UniProt coordinates. and applied mutation signature D153H to reconstruct the assayed variant sequence.


substrate_name: Mn(II)

sequence_variant_note: Resolved canonical sequence from UniProt REST Q0SE24 exact accession; variant sequence reconstructed from selected mutation signature against canonical UniProt coordinates. and applied mutation signature N246A to reconstruct the assayed variant sequence.

substrate: Mn(II)


sequence_variant_note: Resolved canonical sequence from UniProtKB O94753 annotated mature chain (residues 31-361); K215G reconstructed at mature residue 215 from PMID 23071108 Table 3 context. and applied mutation signature K215G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from official_uniprot_json:O94753 and applied mutation signature E140G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: E140G; 2,6-dimethoxyphenol; DMP low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, E140G; 2,6-dimethoxyphenol; DMP low-efficiency site: Km 37.400 ± 3.600 mM; kcat 293.0 ± 16.9 s^-1; kcat/Km 7.8 ± 0.3 s^-1 mM^-1.


sequence_source: UniProtKB O94753 annotated mature chain (residues 31-361); K215G reconstructed at mature residue 215 from PMID 23071108 Table 3 context.


sequence_variant_note: Resolved canonical sequence from official_uniprot_json:O94753 and applied mutation signature P76G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: Primary measurement evidence: evidence location type: table; evidence location label: Table 3; measurement identity label: P76G; 4-hydroquinone; HQ low-efficiency site; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 25 °C; 0.1 M sodium tartrate buffer; pH 3.5; printed uncertainty is the 95% confidence limit.; captured primary segment: Table 3, P76G; 4-hydroquinone; HQ low-efficiency site: Km 1.026 ± 0.062 mM; kcat 29.9 ± 0.6 s^-1; kcat/Km 29.2 ± 1.3 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB O94753 annotated mature chain (residues 31-361); W164S reconstructed at mature residue 164 from PMID 23071108 Table 3 context. and applied mutation signature W164S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O94753 annotated mature chain (residues 31-361); P141G reconstructed at mature residue 141 from PMID 23071108 Table 3 context. and applied mutation signature P141G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O94753 annotated mature chain (residues 31-361); K176D reconstructed at mature residue 176 from PMID 23071108 Table 3 context. and applied mutation signature K176D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB O94753 annotated mature chain (residues 31-361); K215Q reconstructed at mature residue 215 from PMID 23071108 Table 3 context. and applied mutation signature K215Q to reconstruct the assayed variant sequence.


enzyme_display_name: L-allo-threonine aldolase

organism: Aeromonas jandaei

substrate_name: L-allo-threonine

source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB reviewed accession O07051 direct REST/FASTA lookup on 2026-06-01

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

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=-----, pH=7.4

enzyme: L-allo-threonine aldolase

substrate: L-allo-threonine

source: skid


organism: Rattus norvegicus

substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature T130S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'T130S'; column 'KATP (mM)' = 0.03; column 'Vmax/Et (s^-1)' = 0.046; column 'V/KATP Et (M^-1 s^-1)' = 1500.

normalized_value_unit_evidence: Km: printed Table II KATP cell 0.03 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 0.03 mM. kcat: printed Table II Vmax/Et cell 0.046 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.046 s^(-1). kcat/Km: printed Table II V/KATP Et cell 1500 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1500 / 1000 = 1.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'T130S': KATP = 0.03 mM; Vmax/Et = 0.046 s^-1; printed V/KATP Et = 1500 M^-1 s^-1.

row_label: Table II, enzyme row T130S, ATP-varied column group

table_label: Table II: Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes (The Journal of Biological Chemistry 1997, volume 272, number 12, pages 7867-7872); Fru 6-P,2-kinase column heads KATP (mM) | KFru 6-P (mM) | Vmax/Et (s^-1) | V/KATP Et (M^-1 s^-1) | V/KFru 6-P Et (M^-1 s^-1)

substrate: ATP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature D128S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'D128S'; column 'KATP (mM)' = 7.5; column 'Vmax/Et (s^-1)' = 0.0092; column 'V/KATP Et (M^-1 s^-1)' = 1.2.

normalized_value_unit_evidence: Km: printed Table II KATP cell 7.5 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 7.5 mM. kcat: printed Table II Vmax/Et cell 0.0092 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.0092 s^(-1). kcat/Km: printed Table II V/KATP Et cell 1.2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 / 1000 = 0.0012 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'D128S': KATP = 7.5 mM; Vmax/Et = 0.0092 s^-1; printed V/KATP Et = 1.2 M^-1 s^-1.

row_label: Table II, enzyme row D128S, ATP-varied column group


substrate_name: D-Fructose 6-phosphate

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'D128S'; column 'KFru 6-P (mM)' = 8.0; column 'Vmax/Et (s^-1)' = 0.0092; column 'V/KFru 6-P Et (M^-1 s^-1)' = 1.2.

normalized_value_unit_evidence: Km: printed Table II KFru 6-P cell 8.0 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 8.0 mM. kcat: printed Table II Vmax/Et cell 0.0092 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.0092 s^(-1). kcat/Km: printed Table II V/KFru 6-P Et cell 1.2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 / 1000 = 0.0012 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'D128S': KFru 6-P = 8.0 mM; Vmax/Et = 0.0092 s^-1; printed V/KFru 6-P Et = 1.2 M^-1 s^-1.

row_label: Table II, enzyme row D128S, Fru 6-P-varied column group

substrate: D-Fructose 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature D128K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'D128K'; column 'KATP (mM)' = 2.2; column 'Vmax/Et (s^-1)' = 0.00061; column 'V/KATP Et (M^-1 s^-1)' = 0.28.

normalized_value_unit_evidence: Km: printed Table II KATP cell 2.2 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 2.2 mM. kcat: printed Table II Vmax/Et cell 0.00061 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.00061 s^(-1). kcat/Km: printed Table II V/KATP Et cell 0.28 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.28 / 1000 = 0.00028000000000000003 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'D128K': KATP = 2.2 mM; Vmax/Et = 0.00061 s^-1; printed V/KATP Et = 0.28 M^-1 s^-1.

row_label: Table II, enzyme row D128K, ATP-varied column group


column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'WT'; column 'KFru 6-P (mM)' = 0.04; column 'Vmax/Et (s^-1)' = 0.073; column 'V/KFru 6-P Et (M^-1 s^-1)' = 1800.

normalized_value_unit_evidence: Km: printed Table II KFru 6-P cell 0.04 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 0.04 mM. kcat: printed Table II Vmax/Et cell 0.073 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.073 s^(-1). kcat/Km: printed Table II V/KFru 6-P Et cell 1800 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1800 / 1000 = 1.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'WT': KFru 6-P = 0.04 mM; Vmax/Et = 0.073 s^-1; printed V/KFru 6-P Et = 1800 M^-1 s^-1.

row_label: Table II, enzyme row WT, Fru 6-P-varied column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature T52S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'T52S'; column 'KATP (mM)' = 0.19; column 'Vmax/Et (s^-1)' = 0.15; column 'V/KATP Et (M^-1 s^-1)' = 790.

normalized_value_unit_evidence: Km: printed Table II KATP cell 0.19 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 0.19 mM. kcat: printed Table II Vmax/Et cell 0.15 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.15 s^(-1). kcat/Km: printed Table II V/KATP Et cell 790 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 790 / 1000 = 0.79 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'T52S': KATP = 0.19 mM; Vmax/Et = 0.15 s^-1; printed V/KATP Et = 790 M^-1 s^-1.

row_label: Table II, enzyme row T52S, ATP-varied column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature T130V with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'T130V'; column 'KFru 6-P (mM)' = 14; column 'Vmax/Et (s^-1)' = 0.092; column 'V/KFru 6-P Et (M^-1 s^-1)' = 6.6.

normalized_value_unit_evidence: Km: printed Table II KFru 6-P cell 14 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 14.0 mM. kcat: printed Table II Vmax/Et cell 0.092 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.092 s^(-1). kcat/Km: printed Table II V/KFru 6-P Et cell 6.6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.6 / 1000 = 0.0066 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'T130V': KFru 6-P = 14 mM; Vmax/Et = 0.092 s^-1; printed V/KFru 6-P Et = 6.6 M^-1 s^-1.

row_label: Table II, enzyme row T130V, Fru 6-P-varied column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature D128E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'D128E'; column 'KFru 6-P (mM)' = 8.4; column 'Vmax/Et (s^-1)' = 0.14; column 'V/KFru 6-P Et (M^-1 s^-1)' = 17.

normalized_value_unit_evidence: Km: printed Table II KFru 6-P cell 8.4 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 8.4 mM. kcat: printed Table II Vmax/Et cell 0.14 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.14 s^(-1). kcat/Km: printed Table II V/KFru 6-P Et cell 17 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 17 / 1000 = 0.017 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'D128E': KFru 6-P = 8.4 mM; Vmax/Et = 0.14 s^-1; printed V/KFru 6-P Et = 17 M^-1 s^-1.

row_label: Table II, enzyme row D128E, Fru 6-P-varied column group


organism: Homo sapiens

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

assay_conditions_summary: pH 8.5; 298.15 K; cofactor ATP


substrate_name: beta-D-Fructose 6-phosphate

substrate: beta-D-Fructose 6-phosphate


sequence_source: UniProtKB:P25114 direct FASTA/API lookup on 2026-06-01

column_label: Table 2 (Summary of Kinetic Data for Wild Type and Mutant Enzymes Measured at pH 7.5), body row 'wild type'; column 'KFru 6-P (mM)' = 0.04; column 'KMgATP (mM)' = 0.1; column 'V/Et (s-1)' = 0.092; column 'V/KFru 6PEt (M-1 s-1)' = 2300; column 'V/KMgATPEt (M-1 s-1)' = 920; the two fold-decrease columns are blank on this row.

normalized_value_unit_evidence: Km: printed cell 0.04 mM; mM is already the canonical Km unit, so no unit conversion applies and the value is 0.04 mM. kcat: printed cell 0.092 s^-1; s^-1 is already the canonical kcat unit, so no unit conversion applies and the value is 0.092 s^(-1). kcat/Km: printed cell 2300 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2300 / 1000 = 2.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 body row 'wild type': Km printed in the 'KFru 6-P (mM)' column as 0.04; kcat printed in the 'V/Et (s-1)' column as 0.092; kcat/Km printed in the 'V/KFru 6PEt (M-1 s-1)' column as 2300.

row_label: Table 2 body row 'wild type'

table_label: Table 2: Summary of Kinetic Data for Wild Type and Mutant Enzymes Measured at pH 7.5 (Biochemistry 1997, volume 36, number 29, pages 8775-8784)


sequence_source: UniProtKB:P25114 reviewed canonical sequence; variant rows reconstructed from source mutation signature with +1 UniProt residue-numbering offset

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'WT'; column 'KATP (mM)' = 0.1; column 'Vmax/Et (s^-1)' = 0.073; column 'V/KATP Et (M^-1 s^-1)' = 730.

normalized_value_unit_evidence: Km: printed Table II KATP cell 0.1 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 0.1 mM. kcat: printed Table II Vmax/Et cell 0.073 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.073 s^(-1). kcat/Km: printed Table II V/KATP Et cell 730 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 730 / 1000 = 0.73 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'WT': KATP = 0.1 mM; Vmax/Et = 0.073 s^-1; printed V/KATP Et = 730 M^-1 s^-1.

row_label: Table II, enzyme row WT, ATP-varied column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature N73A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'N73A'; column 'KATP (mM)' = 0.4; column 'Vmax/Et (s^-1)' = 0.037; column 'V/KATP Et (M^-1 s^-1)' = 93.

normalized_value_unit_evidence: Km: printed Table II KATP cell 0.4 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 0.4 mM. kcat: printed Table II Vmax/Et cell 0.037 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.037 s^(-1). kcat/Km: printed Table II V/KATP Et cell 93 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 93 / 1000 = 0.093 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'N73A': KATP = 0.4 mM; Vmax/Et = 0.037 s^-1; printed V/KATP Et = 93 M^-1 s^-1.

row_label: Table II, enzyme row N73A, ATP-varied column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature D128N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'D128N'; column 'KFru 6-P (mM)' = 1.3; column 'Vmax/Et (s^-1)' = 0.0031; column 'V/KFru 6-P Et (M^-1 s^-1)' = 2.4.

normalized_value_unit_evidence: Km: printed Table II KFru 6-P cell 1.3 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 1.3 mM. kcat: printed Table II Vmax/Et cell 0.0031 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.0031 s^(-1). kcat/Km: printed Table II V/KFru 6-P Et cell 2.4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.4 / 1000 = 0.0024 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'D128N': KFru 6-P = 1.3 mM; Vmax/Et = 0.0031 s^-1; printed V/KFru 6-P Et = 2.4 M^-1 s^-1.

row_label: Table II, enzyme row D128N, Fru 6-P-varied column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature N73D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'N73D'; column 'KFru 6-P (mM)' = 24; column 'Vmax/Et (s^-1)' = 0.0082; column 'V/KFru 6-P Et (M^-1 s^-1)' = 0.34.

normalized_value_unit_evidence: Km: printed Table II KFru 6-P cell 24 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 24.0 mM. kcat: printed Table II Vmax/Et cell 0.0082 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.0082 s^(-1). kcat/Km: printed Table II V/KFru 6-P Et cell 0.34 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.34 / 1000 = 0.00034 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'N73D': KFru 6-P = 24 mM; Vmax/Et = 0.0082 s^-1; printed V/KFru 6-P Et = 0.34 M^-1 s^-1.

row_label: Table II, enzyme row N73D, Fru 6-P-varied column group


column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'N73A'; column 'KFru 6-P (mM)' = 5.3; column 'Vmax/Et (s^-1)' = 0.037; column 'V/KFru 6-P Et (M^-1 s^-1)' = 7.0.

normalized_value_unit_evidence: Km: printed Table II KFru 6-P cell 5.3 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 5.3 mM. kcat: printed Table II Vmax/Et cell 0.037 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.037 s^(-1). kcat/Km: printed Table II V/KFru 6-P Et cell 7.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.0 / 1000 = 0.007 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'N73A': KFru 6-P = 5.3 mM; Vmax/Et = 0.037 s^-1; printed V/KFru 6-P Et = 7.0 M^-1 s^-1.

row_label: Table II, enzyme row N73A, Fru 6-P-varied column group


column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'T130V'; column 'KATP (mM)' = 1.4; column 'Vmax/Et (s^-1)' = 0.092; column 'V/KATP Et (M^-1 s^-1)' = 66.

normalized_value_unit_evidence: Km: printed Table II KATP cell 1.4 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 1.4 mM. kcat: printed Table II Vmax/Et cell 0.092 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.092 s^(-1). kcat/Km: printed Table II V/KATP Et cell 66 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 66 / 1000 = 0.066 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'T130V': KATP = 1.4 mM; Vmax/Et = 0.092 s^-1; printed V/KATP Et = 66 M^-1 s^-1.

row_label: Table II, enzyme row T130V, ATP-varied column group


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25114 reviewed canonical sequence; variant rows reconstructed from source mutation signature with +1 UniProt residue-numbering offset and applied mutation signature K172A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature R193L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Summary of Kinetic Data for Wild Type and Mutant Enzymes Measured at pH 7.5), body row 'R193L'; column 'KMgATP (mM)' = 0.43; column 'V/Et (s-1)' = 0.010; column 'V/KMgATPEt (M-1 s-1)' = 23; column 'KFru 6-P (mM)' = 25; column 'V/KFru 6PEt (M-1 s-1)' = 0.40; column 'V (fold decrease)' = 9; column 'V/K (fold decrease)' = 5800 and 40.

normalized_value_unit_evidence: Km: printed cell 0.43 mM; mM is already the canonical Km unit, so no unit conversion applies and the value is 0.43 mM. kcat: printed cell 0.010 s^-1; s^-1 is already the canonical kcat unit, so no unit conversion applies and the value is 0.01 s^(-1). kcat/Km: printed cell 23 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 23 / 1000 = 0.023 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 body row 'R193L': Km printed in the 'KMgATP (mM)' column as 0.43; kcat printed in the 'V/Et (s-1)' column as 0.010; kcat/Km printed in the 'V/KMgATPEt (M-1 s-1)' column as 23.

row_label: Table 2 body row 'R193L'


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25114 sequenceVersion 3; PMID:9220964 mutation signature K51A and applied mutation signature K51A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P25114 sequenceVersion 3; PMID:9220964 mutation signature R79H

sequence_variant_note: Mutation signature R79H matches the mutant residue at offset +1 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature R78L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Summary of Kinetic Data for Wild Type and Mutant Enzymes Measured at pH 7.5), body row 'R78L'; column 'KMgATP (mM)' = 2.7; column 'V/Et (s-1)' = 0.050; column 'V/KMgATPEt (M-1 s-1)' = 19; column 'KFru 6-P (mM)' = 9; column 'V/KFru 6PEt (M-1 s-1)' = 5.60; column 'V (fold decrease)' = 2; column 'V/K (fold decrease)' = 400 and 50.

normalized_value_unit_evidence: Km: printed cell 2.7 mM; mM is already the canonical Km unit, so no unit conversion applies and the value is 2.7 mM. kcat: printed cell 0.050 s^-1; s^-1 is already the canonical kcat unit, so no unit conversion applies and the value is 0.05 s^(-1). kcat/Km: printed cell 19 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 19 / 1000 = 0.019 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 body row 'R78L': Km printed in the 'KMgATP (mM)' column as 2.7; kcat printed in the 'V/Et (s-1)' column as 0.050; kcat/Km printed in the 'V/KMgATPEt (M-1 s-1)' column as 19.

row_label: Table 2 body row 'R78L'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature R78H with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Summary of Kinetic Data for Wild Type and Mutant Enzymes Measured at pH 7.5), body row 'R78H'; column 'KFru 6-P (mM)' = 8; column 'V/Et (s-1)' = 0.010; column 'V/KFru 6PEt (M-1 s-1)' = 1.3; column 'KMgATP (mM)' = 2.8; column 'V/KMgATPEt (M-1 s-1)' = 3.6; column 'V (fold decrease)' = 9; column 'V/K (fold decrease)' = 1800 and 250.

normalized_value_unit_evidence: Km: printed cell 8 mM; mM is already the canonical Km unit, so no unit conversion applies and the value is 8.0 mM. kcat: printed cell 0.010 s^-1; s^-1 is already the canonical kcat unit, so no unit conversion applies and the value is 0.01 s^(-1). kcat/Km: printed cell 1.3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 / 1000 = 0.0013 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 body row 'R78H': Km printed in the 'KFru 6-P (mM)' column as 8; kcat printed in the 'V/Et (s-1)' column as 0.010; kcat/Km printed in the 'V/KFru 6PEt (M-1 s-1)' column as 1.3.

row_label: Table 2 body row 'R78H'


column_label: Table 2 (Summary of Kinetic Data for Wild Type and Mutant Enzymes Measured at pH 7.5), body row 'R78H'; column 'KMgATP (mM)' = 2.8; column 'V/Et (s-1)' = 0.010; column 'V/KMgATPEt (M-1 s-1)' = 3.6; column 'KFru 6-P (mM)' = 8; column 'V/KFru 6PEt (M-1 s-1)' = 1.3; column 'V (fold decrease)' = 9; column 'V/K (fold decrease)' = 1800 and 250.

normalized_value_unit_evidence: Km: printed cell 2.8 mM; mM is already the canonical Km unit, so no unit conversion applies and the value is 2.8 mM. kcat: printed cell 0.010 s^-1; s^-1 is already the canonical kcat unit, so no unit conversion applies and the value is 0.01 s^(-1). kcat/Km: printed cell 3.6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.6 / 1000 = 0.0036 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 body row 'R78H': Km printed in the 'KMgATP (mM)' column as 2.8; kcat printed in the 'V/Et (s-1)' column as 0.010; kcat/Km printed in the 'V/KMgATPEt (M-1 s-1)' column as 3.6.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25114 sequenceVersion 3; PMID:9220964 mutation signature K172R and applied mutation signature K172R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25114 sequenceVersion 3; PMID:9220964 mutation signature R79L and applied mutation signature R79L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25114 canonical sequence with selected OED mutation applied at paper-to-UniProt offset +1 and applied mutation signature Y178S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25114 canonical sequence with selected OED mutation applied at paper-to-UniProt offset +1 and applied mutation signature Y178K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25114 canonical sequence with selected OED mutation applied at paper-to-UniProt offset +1 and applied mutation signature D177N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'D128E'; column 'KATP (mM)' = 1.3; column 'Vmax/Et (s^-1)' = 0.14; column 'V/KATP Et (M^-1 s^-1)' = 110.

normalized_value_unit_evidence: Km: printed Table II KATP cell 1.3 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 1.3 mM. kcat: printed Table II Vmax/Et cell 0.14 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.14 s^(-1). kcat/Km: printed Table II V/KATP Et cell 110 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 110 / 1000 = 0.11 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'D128E': KATP = 1.3 mM; Vmax/Et = 0.14 s^-1; printed V/KATP Et = 110 M^-1 s^-1.

row_label: Table II, enzyme row D128E, ATP-varied column group


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25114 canonical sequence with selected OED mutation applied at paper-to-UniProt offset +1 and applied mutation signature T130S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'D128N'; column 'KATP (mM)' = 25; column 'Vmax/Et (s^-1)' = 0.0031; column 'V/KATP Et (M^-1 s^-1)' = 0.12.

normalized_value_unit_evidence: Km: printed Table II KATP cell 25 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 25.0 mM. kcat: printed Table II Vmax/Et cell 0.0031 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.0031 s^(-1). kcat/Km: printed Table II V/KATP Et cell 0.12 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.12 / 1000 = 0.00011999999999999999 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'D128N': KATP = 25 mM; Vmax/Et = 0.0031 s^-1; printed V/KATP Et = 0.12 M^-1 s^-1.

row_label: Table II, enzyme row D128N, ATP-varied column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature D128A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'D128A'; column 'KATP (mM)' = 2.9; column 'Vmax/Et (s^-1)' = 0.0037; column 'V/KATP Et (M^-1 s^-1)' = 1.3.

normalized_value_unit_evidence: Km: printed Table II KATP cell 2.9 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 2.9 mM. kcat: printed Table II Vmax/Et cell 0.0037 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.0037 s^(-1). kcat/Km: printed Table II V/KATP Et cell 1.3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 / 1000 = 0.0013 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'D128A': KATP = 2.9 mM; Vmax/Et = 0.0037 s^-1; printed V/KATP Et = 1.3 M^-1 s^-1.

row_label: Table II, enzyme row D128A, ATP-varied column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature D128K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'D128K'; column 'KFru 6-P (mM)' = 4.5; column 'Vmax/Et (s^-1)' = 0.00061; column 'V/KFru 6-P Et (M^-1 s^-1)' = 0.14.

normalized_value_unit_evidence: Km: printed Table II KFru 6-P cell 4.5 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 4.5 mM. kcat: printed Table II Vmax/Et cell 0.00061 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.00061 s^(-1). kcat/Km: printed Table II V/KFru 6-P Et cell 0.14 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.14 / 1000 = 0.00014000000000000001 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'D128K': KFru 6-P = 4.5 mM; Vmax/Et = 0.00061 s^-1; printed V/KFru 6-P Et = 0.14 M^-1 s^-1.

row_label: Table II, enzyme row D128K, Fru 6-P-varied column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature Y197F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'Y197F'; column 'KFru 6-P (mM)' = 2.8; column 'Vmax/Et (s^-1)' = 0.083; column 'V/KFru 6-P Et (M^-1 s^-1)' = 30.

normalized_value_unit_evidence: Km: printed Table II KFru 6-P cell 2.8 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 2.8 mM. kcat: printed Table II Vmax/Et cell 0.083 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.083 s^(-1). kcat/Km: printed Table II V/KFru 6-P Et cell 30 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 30 / 1000 = 0.03 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'Y197F': KFru 6-P = 2.8 mM; Vmax/Et = 0.083 s^-1; printed V/KFru 6-P Et = 30 M^-1 s^-1.

row_label: Table II, enzyme row Y197F, Fru 6-P-varied column group


column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'D128A'; column 'KFru 6-P (mM)' = 5.0; column 'Vmax/Et (s^-1)' = 0.0037; column 'V/KFru 6-P Et (M^-1 s^-1)' = 0.74.

normalized_value_unit_evidence: Km: printed Table II KFru 6-P cell 5.0 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 5.0 mM. kcat: printed Table II Vmax/Et cell 0.0037 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.0037 s^(-1). kcat/Km: printed Table II V/KFru 6-P Et cell 0.74 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.74 / 1000 = 0.00074 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'D128A': KFru 6-P = 5.0 mM; Vmax/Et = 0.0037 s^-1; printed V/KFru 6-P Et = 0.74 M^-1 s^-1.

row_label: Table II, enzyme row D128A, Fru 6-P-varied column group


column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'N73D'; column 'KATP (mM)' = 0.09; column 'Vmax/Et (s^-1)' = 0.0082; column 'V/KATP Et (M^-1 s^-1)' = 91.

normalized_value_unit_evidence: Km: printed Table II KATP cell 0.09 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 0.09 mM. kcat: printed Table II Vmax/Et cell 0.0082 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.0082 s^(-1). kcat/Km: printed Table II V/KATP Et cell 91 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 91 / 1000 = 0.091 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'N73D': KATP = 0.09 mM; Vmax/Et = 0.0082 s^-1; printed V/KATP Et = 91 M^-1 s^-1.

row_label: Table II, enzyme row N73D, ATP-varied column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature T52S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'T52S'; column 'KFru 6-P (mM)' = 0.11; column 'Vmax/Et (s^-1)' = 0.15; column 'V/KFru 6-P Et (M^-1 s^-1)' = 1400.

normalized_value_unit_evidence: Km: printed Table II KFru 6-P cell 0.11 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 0.11 mM. kcat: printed Table II Vmax/Et cell 0.15 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.15 s^(-1). kcat/Km: printed Table II V/KFru 6-P Et cell 1400 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1400 / 1000 = 1.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'T52S': KFru 6-P = 0.11 mM; Vmax/Et = 0.15 s^-1; printed V/KFru 6-P Et = 1400 M^-1 s^-1.

row_label: Table II, enzyme row T52S, Fru 6-P-varied column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature T130A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'T130A'; column 'KATP (mM)' = 0.16; column 'Vmax/Et (s^-1)' = 0.070; column 'V/KATP Et (M^-1 s^-1)' = 440.

normalized_value_unit_evidence: Km: printed Table II KATP cell 0.16 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 0.16 mM. kcat: printed Table II Vmax/Et cell 0.070 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.07 s^(-1). kcat/Km: printed Table II V/KATP Et cell 440 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 440 / 1000 = 0.44 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'T130A': KATP = 0.16 mM; Vmax/Et = 0.070 s^-1; printed V/KATP Et = 440 M^-1 s^-1.

row_label: Table II, enzyme row T130A, ATP-varied column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P25114 and applied mutation signature Y197S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'Y197S'; column 'KATP (mM)' = 1.9; column 'Vmax/Et (s^-1)' = 0.023; column 'V/KATP Et (M^-1 s^-1)' = 12.

normalized_value_unit_evidence: Km: printed Table II KATP cell 1.9 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 1.9 mM. kcat: printed Table II Vmax/Et cell 0.023 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.023 s^(-1). kcat/Km: printed Table II V/KATP Et cell 12 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 12 / 1000 = 0.012 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'Y197S': KATP = 1.9 mM; Vmax/Et = 0.023 s^-1; printed V/KATP Et = 12 M^-1 s^-1.

row_label: Table II, enzyme row Y197S, ATP-varied column group


sequence_variant_note: Resolved canonical sequence from UniProtKB:P25114 canonical sequence retrieved via UniProt REST; selected OED/PMID 9065453 mutation signature applied with inferred +1 paper-to-UniProt residue-numbering offset. and applied mutation signature T130A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


column_label: Table II (Kinetic constants of rat testis Fru 6-P,2-kinase: Fru-2,6-Pase and the mutant enzymes), Enzyme row 'Y197F'; column 'KATP (mM)' = 0.6; column 'Vmax/Et (s^-1)' = 0.083; column 'V/KATP Et (M^-1 s^-1)' = 140.

normalized_value_unit_evidence: Km: printed Table II KATP cell 0.6 mM; the column is already millimolar, so no conversion is applied and the exported unit value is 0.6 mM. kcat: printed Table II Vmax/Et cell 0.083 s^-1; the column is maximal velocity per total enzyme and is already per second, so no conversion is applied and the value is 0.083 s^(-1). kcat/Km: printed Table II V/KATP Et cell 140 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 140 / 1000 = 0.14 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, Enzyme row 'Y197F': KATP = 0.6 mM; Vmax/Et = 0.083 s^-1; printed V/KATP Et = 140 M^-1 s^-1.

row_label: Table II, enzyme row Y197F, ATP-varied column group


sequence_source: UniProtKB:P25114 canonical sequence checked; K172R variant sequence not accepted from selected evidence.

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.


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


enzyme_display_name: flavin-containing monooxygenase

substrate_name: methyl 4-tolyl sulfide

sequence_source: UniProtKB P31513 canonical FASTA with N61S reconstructed after confirming residue 61 is N.

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

enzyme: flavin-containing monooxygenase

substrate: methyl 4-tolyl sulfide


substrate_name: trimethylamine

smiles: CN(C)C

substrate: trimethylamine


sequence_source: UniProtKB P31513 canonical FASTA with E158K reconstructed after confirming residue 158 is E.


sequence_source: UniProtKB P31513 canonical FASTA with V257M reconstructed after confirming residue 257 is V.


sequence_source: UniProtKB P31513 canonical FASTA with E308G reconstructed after confirming residue 308 is E.


substrate_name: Benzydamine

substrate: Benzydamine


sequence_source: UniProtKB P31513 canonical FASTA sequence.

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


organism: Sus scrofa

sequence_source: UniProtKB:P16549 reviewed FASTA/REST direct lookup


substrate_name: NADPH

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from UniProt P31513 canonical sequence with V257M reconstructed after confirming V257 in the canonical sequence. and applied mutation signature V257M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P31513 canonical sequence with P153L reconstructed after confirming P153 in the canonical sequence. and applied mutation signature P153L to reconstruct the assayed variant sequence.


substrate_name: methyl p-tolyl sulfide

sequence_source: UniProt Q99518 exact accession canonical sequence.

substrate: methyl p-tolyl sulfide


sequence_variant_note: Resolved canonical sequence from UniProt Q99518 canonical sequence with N413K reconstructed after confirming N413 in the canonical sequence. and applied mutation signature N413K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q99518 canonical sequence with S195L reconstructed after confirming S195 in the canonical sequence. and applied mutation signature S195L to reconstruct the assayed variant sequence.


sequence_source: UniProt Q99518 canonical sequence with S195L reconstructed after confirming S195 in the canonical sequence.

assay_conditions_summary: pH 9; 310.15 K; cofactor NADPH


sequence_source: UniProt Q99518 canonical sequence with N413K reconstructed after confirming N413 in the canonical sequence.


substrate_name: clomiphene

sequence_variant_note: Resolved canonical sequence from uniprot_accession:P31513 and applied mutation signature E308G to reconstruct the assayed variant sequence.

substrate: clomiphene


substrate_name: tamoxifen

sequence_variant_note: Resolved canonical sequence from uniprot_accession:P31513 and applied mutation signature E158K to reconstruct the assayed variant sequence.

substrate: tamoxifen


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P31513 and applied mutation signature V257M to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P31513 canonical FMO3 sequence; P153L reconstructed by replacing residue P153 with L after direct residue check.


sequence_source: UniProtKB P31513 canonical FMO3 sequence; E308G reconstructed by replacing residue E308 with G after direct residue check.


sequence_source: UniProtKB P31513 canonical FMO3 sequence from direct REST FASTA lookup.


sequence_source: UniProtKB P31513 canonical FMO3 sequence; N61S reconstructed by replacing residue N61 with S after direct residue check.


sequence_source: UniProtKB P31513 canonical FMO3 sequence; V257M reconstructed by replacing residue V257 with M after direct residue check.


sequence_variant_note: Resolved canonical sequence from UniProt:P31513 direct REST lookup; variant reconstructed from canonical sequence and applied mutation signature V257M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P31513 direct REST lookup; variant reconstructed from canonical sequence and applied mutation signature E158K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P31513 direct REST lookup; variant reconstructed from canonical sequence and applied mutation signature E308G to reconstruct the assayed variant sequence.


sequence_source: UniProt:P31513 direct REST lookup canonical sequence


enzyme_display_name: dye decolorizing peroxidase

organism: Auricularia auricula-judae

substrate_name: Reactive Blue 19

sequence_source: UniProtKB:I2DBY1 FASTA direct lookup 2026-06-01

enzyme: dye decolorizing peroxidase

substrate: Reactive Blue 19


substrate_name: veratrylglycerol-beta-guaiacyl ether

substrate: veratrylglycerol-beta-guaiacyl ether


organism: Bacillus subtilis

substrate_name: Reactive Black 5

sequence_source: UniProtKB:P39597 FASTA direct lookup 2026-06-01

substrate: Reactive Black 5


substrate_name: malachite green

substrate: malachite green


substrate_name: Methyl Violet

substrate: Methyl Violet


organism: Dictyostelium discoideum

sequence_source: UniProtKB:Q556V8 FASTA direct lookup 2026-06-01


substrate_name: veratryl alcohol

substrate: veratryl alcohol


organism: Anabaena sp.

substrate_name: Reactive Blue 5

sequence_source: UniProtKB A0ACD6B9A9 FASTA; Q8YWM0 direct lookup returned inactive DEMERGED to A0ACD6B9A9

substrate: Reactive Blue 5


sequence_source: UniProtKB I2DBY1 FASTA; reviewed Swiss-Prot DYP_AURAJ


sequence_variant_note: Resolved canonical sequence from UniProtKB I2DBY1 FASTA plus UniProt mutagenesis feature at full-sequence residue 438 for mature-chain W377S and applied mutation signature W377S with inferred residue-numbering offset +61 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB I2DBY1 FASTA plus UniProt mutagenesis feature at full-sequence residue 438 for mature-chain W377S


sequence_source: UniProtKB:K7N5M8 reviewed Swiss-Prot entry DYP2_AMYS7, accessed 2026-06-01


organism: Amycolatopsis sp. ATCC 39116

substrate_name: guaiacylglycerol-beta-guaiacyl ether

substrate: guaiacylglycerol-beta-guaiacyl ether


column_label: Table 1. Steady-state kinetic parameters −Km (µM), kcat (s−1) and kcat/Km (s−1·mM−1)−for ABTS, DMP, RB19, Mn2+, VA and H2O2 reactions of the bacterial AspDyP2 and TcuDyP, obtained here, compared with fungal AauDyP, PerVPL and PchLiPA from previous work. Enzyme block 'AspDyP2'; substrate column 'RB19'; row 'K m' = 20 (caption unit uM); row 'k cat' = 26.0 (caption unit s^-1); row 'k cat /K m' = 1300 (caption unit s^-1 mM^-1).

normalized_value_unit_evidence: Km: printed Table 1 cell 20, caption unit uM; 20 / 1000 = 0.02 mM; the exported value is 0.02 mM. kcat: printed Table 1 cell 26.0, caption unit s^-1; no conversion; the exported value is 26.0 s^(-1). kcat/Km: printed Table 1 cell 1300, caption unit s^-1 mM^-1; no conversion; the exported value is 1300.0 s^(-1)*mM^(-1). All three agree exactly.

raw_value_unit_evidence: Table 1, enzyme block 'AspDyP2', substrate column 'RB19': Km = 20 (caption unit uM); kcat = 26.0 (caption unit s^-1); printed kcat/Km = 1300 (caption unit s^-1 mM^-1).


sequence_source: UniProtKB:A0ACD6B9A9 live TrEMBL entry, secondary accession Q8YWM0, accessed 2026-06-01


organism: Irpex lacteus

sequence_variant_note: Resolved canonical sequence from RCSB/PDB 7D8M chain A sequence mapped to UniProtKB:A0A2P1C6N4 residues 31-480; PMID 34059116 mutation W264F applied directly to the paper-numbered chain sequence and applied mutation signature W264F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from RCSB/PDB 7D8M chain A sequence mapped to UniProtKB:A0A2P1C6N4 residues 31-480; PMID 34059116 mutation W212F applied directly to the paper-numbered chain sequence and applied mutation signature W212F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A0A2P1C6N4 canonical sequence retrieved by direct accession lookup

assay_conditions_summary: pH 3.5; 308.15 K; buffer ABTS oxidation in 10 mM sodium tartrate


sequence_source: RCSB/PDB 7D8M chain A sequence mapped to UniProtKB:A0A2P1C6N4 residues 31-480; PMID 34059116 mutation W212F applied directly to the paper-numbered chain sequence


sequence_variant_note: Resolved canonical sequence from RCSB/PDB 7D8M chain A sequence mapped to UniProtKB:A0A2P1C6N4 residues 31-480; PMID 34059116 mutation W109F applied directly to the paper-numbered chain sequence and applied mutation signature W109F to reconstruct the assayed variant sequence.


organism: Pleurotus sapidus

sequence_source: UniProtKB:A0A0F7VJ89 canonical sequence retrieved by direct accession lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB A0A2P1C6N4 canonical sequence with row-specific substitution reconstructed using RCSB 7D8M/PMID 34059116 residue numbering offset +30 and applied mutation signature W264H with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 3.5; 308.15 K; buffer 10 mM sodium tartrate


sequence_variant_note: Resolved canonical sequence from UniProtKB A0A2P1C6N4 canonical sequence with row-specific substitution reconstructed using RCSB 7D8M/PMID 34059116 residue numbering offset +30 and applied mutation signature W380F with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A0A2P1C6N4 canonical sequence with row-specific substitution reconstructed using RCSB 7D8M/PMID 34059116 residue numbering offset +30 and applied mutation signature W147F with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A0A2P1C6N4 canonical sequence with row-specific substitution reconstructed using RCSB 7D8M/PMID 34059116 residue numbering offset +30 and applied mutation signature W264R with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A0A2P1C6N4 canonical sequence with row-specific substitution reconstructed using RCSB 7D8M/PMID 34059116 residue numbering offset +30 and applied mutation signature W109F with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB A0A2P1C6N4 canonical sequence with row-specific substitution reconstructed using RCSB 7D8M/PMID 34059116 residue numbering offset +30


organism: Thermomonospora curvata

substrate_name: catechol

sequence_source: UniProtKB:D1A807 direct REST lookup on 2026-06-01; EMBL ACY98529.1 / RefSeq WP_012853313.1; PDB cross-references 5JXU, 7RMU, 8FJQ, and 8FJR.

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

substrate: catechol


organism: Vibrio cholerae

sequence_source: UniProtKB:Q9KQ59 direct REST lookup on 2026-06-01, cross-checked to RCSB PDB 5DE0 primary citation PMID 26431465.


substrate_name: guaiacol

substrate: guaiacol


organism: Pseudomonas aeruginosa


organism: Thermobifida fusca YX


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A2P1C6N4 plus mature-residue mutation reconstruction and applied mutation signature W380Y with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A2P1C6N4 plus mature-residue mutation reconstruction and applied mutation signature W264H with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A2P1C6N4 plus mature-residue mutation reconstruction and applied mutation signature W264F with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A0A2P1C6N4 plus mature-residue mutation reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A2P1C6N4 plus mature-residue mutation reconstruction and applied mutation signature W147F with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


substrate_name: pyrogallol

substrate: pyrogallol


substrate_name: Reactive Blue 4

substrate: Reactive Blue 4


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A2P1C6N4 residues 31-480 (paper mature Il-DyP4 construct) and applied mutation signature W264H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A2P1C6N4 residues 31-480 (paper mature Il-DyP4 construct) and applied mutation signature W264Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A2P1C6N4 residues 31-480 (paper mature Il-DyP4 construct) and applied mutation signature W212F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A0A2P1C6N4 residues 31-480 (paper mature Il-DyP4 construct)


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A2P1C6N4 residues 31-480 (paper mature Il-DyP4 construct) and applied mutation signature W264F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt D1A807 canonical FASTA; D220A reconstructed after confirming the canonical residue at that position. and applied mutation signature D220A to reconstruct the assayed variant sequence.


sequence_source: UniProt D1A807 FASTA canonical wild-type sequence.


sequence_variant_note: Resolved canonical sequence from UniProt D1A807 canonical FASTA; H312C reconstructed after confirming the canonical residue at that position. and applied mutation signature H312C to reconstruct the assayed variant sequence.


sequence_source: UniProt D1A807 canonical FASTA; D220A reconstructed after confirming the canonical residue at that position.


sequence_source: UniProt D1A807 canonical FASTA; H312C reconstructed after confirming the canonical residue at that position.


substrate_name: hydroquinone

substrate: hydroquinone


enzyme_display_name: 1-deoxy-D-xylulose-5-phosphate synthase

organism: Deinococcus radiodurans

substrate_name: D-glyceraldehyde 3-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9RUB5 canonical FASTA; residue-validated in-place substitution applied for the selected mutation. and applied mutation signature H304A to reconstruct the assayed variant sequence.

enzyme: 1-deoxy-D-xylulose-5-phosphate synthase

substrate: D-glyceraldehyde 3-phosphate


substrate_name: pyruvate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9RUB5 canonical FASTA; residue-validated in-place substitution applied for the selected mutation. and applied mutation signature D430A to reconstruct the assayed variant sequence.

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

substrate: pyruvate


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9RUB5 canonical FASTA; residue-validated in-place substitution applied for the selected mutation. and applied mutation signature H82A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9RUB5 canonical FASTA; residue-validated in-place substitution applied for the selected mutation. and applied mutation signature H434A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9RUB5 canonical FASTA; residue-validated in-place substitution applied for the selected mutation.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9RUB5 and applied mutation signature H434A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

column_label: Table 2. DXS Steady-State Kinetics Data (Wild-Type and Mutants) for Both Pyruvate and G3P, The Journal of Physical Chemistry B 2016, 120(37), pages 9922-9934. Pyruvate block; enzyme row H434A; KM cell = 1.7 +/- 0.1 mM; kcat/KM cell = 5.9 x 10^3 s^-1 M^-1; kcat cell = 9.9 +/- 0.2 s^-1; % WT cell = 133.8.

normalized_value_unit_evidence: kcat: printed Table 2 cell 9.9 +/- 0.2 under the column head kcat (s^-1); the printed turnover column is already per second, so the canonical value is 9.9 s^-1 and the export value 9.9 s^-1 already agrees. Km: printed Table 2 cell 1.7 +/- 0.1 under the column head KM (mM); the printed Michaelis column is already millimolar, so the canonical value is 1.7 mM and the export value 1.7 mM already agrees. kcat/Km: printed Table 2 cell 5.9 x 10^3 under the column head kcat/KM (s^-1 M^-1), that is 5900 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 5900 / 1000 = 5.9 s^-1 mM^-1; the exported value is 5900.0 s^-1 mM^-1, which is the printed per-molar cell carrying the per-millimolar label without that division.

raw_value_unit_evidence: Table 2, Pyruvate block, enzyme row H434A: KM = 1.7 +/- 0.1 mM; kcat/KM = 5.9 x 10^3 s^-1 M^-1; kcat = 9.9 +/- 0.2 s^-1; % WT = 133.8. The printed column heads are KM (mM), kcat/KM (s^-1 M^-1), kcat (s^-1) and % WT, and the printed table footnote reads: % WT was determined by comparing the mutant kcat to the wild-type kcat.


sequence_source: UniProtKB Q9RUB5 canonical FASTA.


organism: Escherichia coli


enzyme_display_name: haloalkane dehalogenase

organism: Sphingomonas paucimobilis

substrate_name: bromocyclohexane

sequence_source: UniProtKB:D4Z2G1 canonical LinB sequence; P51698 is inactive and demerged, and D4Z2G1 is the UT26/UT26S replacement aligned to the selected paper context.

enzyme: haloalkane dehalogenase

substrate: bromocyclohexane


smiles: CCCCCCCl


substrate_name: Chlorocyclohexane

substrate: Chlorocyclohexane


sequence_source: Reconstructed from UniProtKB:D4Z2G1 canonical LinB sequence by applying L177A; direct check confirmed D4Z2G1 has L at residue 177.

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

smiles: CCCCCl


sequence_source: Reconstructed from UniProtKB:D4Z2G1 canonical LinB sequence by applying L177R; direct check confirmed D4Z2G1 has L at residue 177.

smiles: BrCCBr


sequence_source: Reconstructed from UniProtKB:D4Z2G1 canonical LinB sequence by applying L177Y; direct check confirmed D4Z2G1 has L at residue 177.


sequence_source: Reconstructed from UniProtKB:D4Z2G1 canonical LinB sequence by applying L177Q; direct check confirmed D4Z2G1 has L at residue 177.


sequence_source: Reconstructed from UniProtKB:D4Z2G1 canonical LinB sequence by applying L177V; direct check confirmed D4Z2G1 has L at residue 177.


organism: Plesiocystis pacifica

sequence_source: UniProtKB:A6G7B1 FASTA retrieved 2026-06-01

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

smiles: CCCCCCBr

assay_conditions_summary: pH 8.2; 308.15 K; buffer 50 mM HEPES

column_label: Table 2: Kinetic parameters of DppA for a set of substrates (Appl Microbiol Biotechnol 2011, 91:1049-1060); printed column heads Substrate | Km [mM] | kcat [sec-1] | kcat/Km [mM-1 x sec-1]. Table 2, substrate row '1-Bromohexane'; column Km [mM] = 1.70; column kcat [sec-1] = 2.69; column kcat/Km [mM-1 x sec-1] = 1.58. captured primary segment: 1-Bromohexane | Km 1.70 mM | kcat 2.69 s^-1 | kcat/Km 1.58 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 1.70 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper-side value is 1.7 mM. kcat: printed Table 2 cell 2.69 sec^-1; sec^-1 is the export unit s^(-1) (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper-side value is 2.69 s^(-1). kcat/Km: printed Table 2 cell 1.58 mM^-1 sec^-1; mM^-1 sec^-1 is the canonical s^(-1)*mM^(-1) written in the printed order, so no unit conversion applies and the printed efficiency is 1.58 s^(-1)*mM^(-1). Quotient disclosure for this row: 2.69 / 1.70 = 1.5823529411764705 s^-1 mM^-1, which the table prints as 1.58 at its own two-decimal precision.

raw_value_unit_evidence: Table 2, substrate row '1-Bromohexane': Km = 1.70 mM; kcat = 2.69 sec^-1; printed kcat/Km = 1.58 mM^-1 sec^-1.

row_label: Table 2, substrate row '1-Bromohexane'


smiles: CCCCBr

column_label: Table 2: Kinetic parameters of DppA for a set of substrates (Appl Microbiol Biotechnol 2011, 91:1049-1060); printed column heads Substrate | Km [mM] | kcat [sec-1] | kcat/Km [mM-1 x sec-1]. Table 2, substrate row '1-Bromobutane'; column Km [mM] = 24.0; column kcat [sec-1] = 8.08; column kcat/Km [mM-1 x sec-1] = 0.34. captured primary segment: 1-Bromobutane | Km 24.0 mM | kcat 8.08 s^-1 | kcat/Km 0.34 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 24.0 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper-side value is 24.0 mM. kcat: printed Table 2 cell 8.08 sec^-1; sec^-1 is the export unit s^(-1) (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper-side value is 8.08 s^(-1). kcat/Km: printed Table 2 cell 0.34 mM^-1 sec^-1; mM^-1 sec^-1 is the canonical s^(-1)*mM^(-1) written in the printed order, so no unit conversion applies and the printed efficiency is 0.34 s^(-1)*mM^(-1). Quotient disclosure for this row: 8.08 / 24.0 = 0.33666666666666667 s^-1 mM^-1, which the table prints as 0.34 at its own two-decimal precision.

raw_value_unit_evidence: Table 2, substrate row '1-Bromobutane': Km = 24.0 mM; kcat = 8.08 sec^-1; printed kcat/Km = 0.34 mM^-1 sec^-1.

row_label: Table 2, substrate row '1-Bromobutane'


smiles: CC(Br)CBr


smiles: CCCCCBr

column_label: Table 2: Kinetic parameters of DppA for a set of substrates (Appl Microbiol Biotechnol 2011, 91:1049-1060); printed column heads Substrate | Km [mM] | kcat [sec-1] | kcat/Km [mM-1 x sec-1]. Table 2, substrate row '1-Bromopentane'; column Km [mM] = 2.51; column kcat [sec-1] = 9.94; column kcat/Km [mM-1 x sec-1] = 3.96. captured primary segment: 1-Bromopentane | Km 2.51 mM | kcat 9.94 s^-1 | kcat/Km 3.96 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 2.51 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper-side value is 2.51 mM. kcat: printed Table 2 cell 9.94 sec^-1; sec^-1 is the export unit s^(-1) (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper-side value is 9.94 s^(-1). kcat/Km: printed Table 2 cell 3.96 mM^-1 sec^-1; mM^-1 sec^-1 is the canonical s^(-1)*mM^(-1) written in the printed order, so no unit conversion applies and the printed efficiency is 3.96 s^(-1)*mM^(-1). Quotient disclosure for this row: 9.94 / 2.51 = 3.960159362549801 s^-1 mM^-1, which the table prints as 3.96 at its own two-decimal precision.

raw_value_unit_evidence: Table 2, substrate row '1-Bromopentane': Km = 2.51 mM; kcat = 9.94 sec^-1; printed kcat/Km = 3.96 mM^-1 sec^-1.

row_label: Table 2, substrate row '1-Bromopentane'


smiles: CCCBr

column_label: Table 2: Kinetic parameters of DppA for a set of substrates (Appl Microbiol Biotechnol 2011, 91:1049-1060); printed column heads Substrate | Km [mM] | kcat [sec-1] | kcat/Km [mM-1 x sec-1]. Table 2, substrate row '1-Bromopropane'; column Km [mM] = 45.2; column kcat [sec-1] = 5.85; column kcat/Km [mM-1 x sec-1] = 0.13. captured primary segment: 1-Bromopropane | Km 45.2 mM | kcat 5.85 s^-1 | kcat/Km 0.13 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 45.2 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper-side value is 45.2 mM. kcat: printed Table 2 cell 5.85 sec^-1; sec^-1 is the export unit s^(-1) (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper-side value is 5.85 s^(-1). kcat/Km: printed Table 2 cell 0.13 mM^-1 sec^-1; mM^-1 sec^-1 is the canonical s^(-1)*mM^(-1) written in the printed order, so no unit conversion applies and the printed efficiency is 0.13 s^(-1)*mM^(-1). Quotient disclosure for this row: 5.85 / 45.2 = 0.12942477876106193 s^-1 mM^-1, which the table prints as 0.13 at its own two-decimal precision.

raw_value_unit_evidence: Table 2, substrate row '1-Bromopropane': Km = 45.2 mM; kcat = 5.85 sec^-1; printed kcat/Km = 0.13 mM^-1 sec^-1.

row_label: Table 2, substrate row '1-Bromopropane'