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.


enzyme_display_name: dye decolorizing peroxidase

organism: Irpex lacteus

substrate_name: Reactive Blue 19

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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.

mutation_type: substitution

data_origin: experimental

enzyme: dye decolorizing peroxidase

substrate: Reactive Blue 19

status: corrected

source: oed


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.


mutation_signature: Unknown

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


sequence_source: UniProtKB:A0A2P1C6N4 plus mature-residue mutation reconstruction

smiles: OO


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.


organism: Dictyostelium discoideum

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.


organism: Thermomonospora curvata

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.


substrate_name: guaiacol

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.

substrate: guaiacol


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.


verification_status: unverified

kcat_over_km_origin: calculated

status: unverified


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


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D4Z2G1 and applied mutation signature L177A to reconstruct the assayed variant sequence.

smiles: CCCCCl

assay_conditions_summary: pH 8.6; 310.15 K; buffer EZ-Fit version 1.1. The

column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); first-set enzyme column 'L177A', substrate block '1-Chlorobutane'; row 'Km (mM)' = 3.34; row 'kcat (s^-1)' = 2.67; row 'kcat/Km (mM^-1 . s^-1)' = 0.80.

normalized_value_unit_evidence: Km: printed Table II cell 3.34 mM; mM is already the canonical unit, so no unit conversion applies and the value is 3.34 mM. kcat: printed Table II cell 2.67 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 2.67 s^(-1). kcat/Km: printed Table II cell 0.80 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 0.8 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 2.67 / 3.34 = 0.7994011976047904 s^-1 mM^-1.

raw_value_unit_evidence: Table II, first-set column 'L177A', 1-Chlorobutane block: Km = 3.34 mM; kcat = 2.67 s^-1; printed kcat/Km = 0.80 mM^-1 s^-1.

status: verified


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D4Z2G1 and applied mutation signature L177R to reconstruct the assayed variant sequence.

smiles: BrCCBr

column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); second-set enzyme column 'L177R', substrate block '1,2-Dibromoethane'; row 'Km (mM)' = 10.36; row 'Ksi (mM)' = 0.82; row 'kcat (s^-1)' = 41.73; row 'kcat/Km (mM^-1 . s^-1)' = 4.03.

normalized_value_unit_evidence: Km: printed Table II cell 10.36 mM; mM is already the canonical unit, so no unit conversion applies and the value is 10.36 mM. kcat: printed Table II cell 41.73 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 41.73 s^(-1). kcat/Km: printed Table II cell 4.03 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 4.03 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 41.73 / 10.36 = 4.027992277992278 s^-1 mM^-1.

raw_value_unit_evidence: Table II, second-set column 'L177R', 1,2-Dibromoethane block: Km = 10.36 mM; kcat = 41.73 s^-1; printed kcat/Km = 4.03 mM^-1 s^-1; printed Ksi = 0.82 mM.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D4Z2G1 and applied mutation signature L177Y to reconstruct the assayed variant sequence.

column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); second-set enzyme column 'L177Y', substrate block '1-Chlorobutane'; row 'Km (mM)' = 0.92; row 'kcat (s^-1)' = 0.88; row 'kcat/Km (mM^-1 . s^-1)' = 0.96.

normalized_value_unit_evidence: Km: printed Table II cell 0.92 mM; mM is already the canonical unit, so no unit conversion applies and the value is 0.92 mM. kcat: printed Table II cell 0.88 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 0.88 s^(-1). kcat/Km: printed Table II cell 0.96 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 0.96 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 0.88 / 0.92 = 0.9565217391304347 s^-1 mM^-1.

raw_value_unit_evidence: Table II, second-set column 'L177Y', 1-Chlorobutane block: Km = 0.92 mM; kcat = 0.88 s^-1; printed kcat/Km = 0.96 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D4Z2G1 and applied mutation signature L177Q to reconstruct the assayed variant sequence.

column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); second-set enzyme column 'L177Q', substrate block '1-Chlorobutane'; row 'Km (mM)' = 4.40; row 'kcat (s^-1)' = 2.25; row 'kcat/Km (mM^-1 . s^-1)' = 0.51.

normalized_value_unit_evidence: Km: printed Table II cell 4.40 mM; mM is already the canonical unit, so no unit conversion applies and the value is 4.4 mM. kcat: printed Table II cell 2.25 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 2.25 s^(-1). kcat/Km: printed Table II cell 0.51 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 0.51 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 2.25 / 4.40 = 0.5113636363636364 s^-1 mM^-1.

raw_value_unit_evidence: Table II, second-set column 'L177Q', 1-Chlorobutane block: Km = 4.40 mM; kcat = 2.25 s^-1; printed kcat/Km = 0.51 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D4Z2G1 and applied mutation signature L177V to reconstruct the assayed variant sequence.

column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); second-set enzyme column 'L177V', substrate block '1-Chlorobutane'; row 'Km (mM)' = 0.06; row 'kcat (s^-1)' = 0.57; row 'kcat/Km (mM^-1 . s^-1)' = 8.87.

normalized_value_unit_evidence: Km: printed Table II cell 0.06 mM; mM is already the canonical unit, so no unit conversion applies and the value is 0.06 mM. kcat: printed Table II cell 0.57 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 0.57 s^(-1). kcat/Km: printed Table II cell 8.87 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 8.87 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 0.57 / 0.06 = 9.5 s^-1 mM^-1.

raw_value_unit_evidence: Table II, second-set column 'L177V', 1-Chlorobutane block: Km = 0.06 mM; kcat = 0.57 s^-1; printed kcat/Km = 8.87 mM^-1 s^-1.


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

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 '1,2-Dibromopropane'; column Km [mM] = 1.96; column kcat [sec-1] = 1.97; column kcat/Km [mM-1 x sec-1] = 1.00. captured primary segment: 1,2-Dibromopropane | Km 1.96 mM | kcat 1.97 s^-1 | kcat/Km 1.00 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 1.96 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 1.96 mM; the exported value is 1.96 mM. kcat: printed Table 2 cell 1.97 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 value is 1.97 s^(-1); the exported value is 1.97 s^(-1). kcat/Km: printed Table 2 cell 1.00 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 paper value is 1.0 s^(-1)*mM^(-1); the exported value is 1.0051020408163265 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 2, substrate row '1,2-Dibromopropane': Km = 1.96 mM; kcat = 1.97 sec^-1; printed kcat/Km = 1.00 mM^-1 sec^-1.


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'


smiles: CCCCCCCBr

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-Bromoheptane'; column Km [mM] = 0.75; column kcat [sec-1] = 1.39; column kcat/Km [mM-1 x sec-1] = 1.84. captured primary segment: 1-Bromoheptane | Km 0.75 mM | kcat 1.39 s^-1 | kcat/Km 1.84 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 0.75 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.75 mM; the exported value is 0.75 mM. kcat: printed Table 2 cell 1.39 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 value is 1.39 s^(-1); the exported value is 1.39 s^(-1). kcat/Km: printed Table 2 cell 1.84 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 paper value is 1.84 s^(-1)*mM^(-1); the exported value is 1.8533333333333333 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 2, substrate row '1-Bromoheptane': Km = 0.75 mM; kcat = 1.39 sec^-1; printed kcat/Km = 1.84 mM^-1 sec^-1.

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


organism: Rhodococcus rhodochrous

sequence_source: UniProtKB:P0A3G2 FASTA retrieved 2026-06-01

smiles: BrCC(Br)CBr

assay_conditions_summary: pH 9.4; 303.15 K; buffer 50 mM NaHCO3/NaOH

column_label: Table label: Table 1: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Evidence location type: table. Row label: 1,2,3-tribromopropane. Column labels read: kcat (s-1) cell 3.6, Km (mM) cell 0.3, kcat/Km (M-1 s-1) cell 12000. captured primary segment: 1,2,3-tribromopropane       3.6          0.3             12000. The printed kcat cell 3.6 s-1 decimal-matches the exported kcat 3.6 s^(-1); the printed Km cell 0.3 mM decimal-matches the exported km 0.3 mM; the exported kcat_over_km 12.0 s^(-1)*mM^(-1) is this row's own printed kcat/Km cell 12000 M-1 s-1 converted to s^-1 mM^-1, and it is also the exact quotient of this same row's printed kcat and Km cells. Every value in this record comes from the single printed row 1,2,3-tribromopropane of Table 1; no value is taken from another row, another column, another table or another paper. assay condition: Purified haloalkane dehalogenase DhaA of Rhodococcus rhodochrous; Table 1 title as printed: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Materials and Methods, Steady-State Kinetics section of this same paper states that dehalogenase assays were carried out at 30 °C in 50 mM NaHCO3/NaOH buffer (pH 9.4) using colorimetric detection of halide release from halogenated substrates, and that the Km and Vmax values were calculated from the initial rate of (halo)alcohol production, determined by gas chromatography, or from halide production rates, determined colorimetrically; in the two-column PDF text layer that sentence is interleaved line by line with the left column, so it is deliberately not reproduced here as a single contiguous quote. The export row carries pH 9.4 for the same measurement, matching the printed table title. The 1 mM dithiothreitol named in the paper belongs to the separate Rapid-Quench-Flow Measurements section and is not part of this steady-state Table 1 condition.

normalized_value_unit_evidence: metric: kcat; raw value: 3.6; raw unit: s-1; normalized value: 3.6 s^(-1); metric: Km; raw value: 0.3; raw unit: mM; normalized value: 0.3 mM; metric: kcat/Km; raw value: 12000; raw unit: M-1 s-1; normalized value: 12.0 s^-1 mM^-1; assay condition: Purified haloalkane dehalogenase DhaA of Rhodococcus rhodochrous; Table 1 title as printed: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Materials and Methods, Steady-State Kinetics section of this same paper states that dehalogenase assays were carried out at 30 °C in 50 mM NaHCO3/NaOH buffer (pH 9.4) using colorimetric detection of halide release from halogenated substrates, and that the Km and Vmax values were calculated from the initial rate of (halo)alcohol production, determined by gas chromatography, or from halide production rates, determined colorimetrically; in the two-column PDF text layer that sentence is interleaved line by line with the left column, so it is deliberately not reproduced here as a single contiguous quote. The export row carries pH 9.4 for the same measurement, matching the printed table title. The 1 mM dithiothreitol named in the paper belongs to the separate Rapid-Quench-Flow Measurements section and is not part of this steady-state Table 1 condition. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 3.6 s-1 is already in s^-1, so the normalized kcat is 3.6 s^(-1). Km 0.3 mM is already in mM, so the normalized Km is 0.3 mM. kcat/Km is read from this row's own printed kcat/Km cell 12000 M-1 s-1: 12000 M^-1 s^-1 / 1000 = 12.0 s^(-1)*mM^(-1). Cross-check against the quotient of this row's own two other printed cells: 3.6 s^-1 / 0.3 mM = 12.0 s^-1 mM^-1, which decimal-matches the printed ratio cell after the M^-1 to mM^-1 conversion. Two-sided round-trip: the quotient re-expressed in the printed column's unit is 12000.0 M-1 s-1 and rounds to the printed cell 12000 M-1 s-1 exactly; the printed cell converted back is 12.0 s^(-1)*mM^(-1), which equals the exported value. No disagreement survives rounding to either side's precision, so this is an exact match and not a correction. In this PDF text layer the superscript minus-one exponents render inline, so the printed headers appear as kcat (s-1), Km (mM) and kcat/Km (M-1 s-1).

raw_value_unit_evidence: Table 1: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C | printed column header line: substrate           kcat (s-1)   Km (mM)      kcat/Km (M-1 s-1) | printed row: 1,2,3-tribromopropane       3.6          0.3             12000 | kcat cell as printed for this row: 3.6, printed unit s-1 | Km cell as printed for this row: 0.3, printed unit mM | kcat/Km cell as printed for this row: 12000, printed unit M-1 s-1.


column_label: Table label: Table 1: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Evidence location type: table. Row label: 1,2-dibromopropane. Column labels read: kcat (s-1) cell 2.3, Km (mM) cell 1.0, kcat/Km (M-1 s-1) cell 2300. captured primary segment: 1,2-dibromopropane          2.3          1.0              2300. The printed kcat cell 2.3 s-1 decimal-matches the exported kcat 2.3 s^(-1); the printed Km cell 1.0 mM decimal-matches the exported km 1.0 mM; the exported kcat_over_km 2.3 s^(-1)*mM^(-1) is this row's own printed kcat/Km cell 2300 M-1 s-1 converted to s^-1 mM^-1, and it is also the exact quotient of this same row's printed kcat and Km cells. Every value in this record comes from the single printed row 1,2-dibromopropane of Table 1; no value is taken from another row, another column, another table or another paper. assay condition: Purified haloalkane dehalogenase DhaA of Rhodococcus rhodochrous; Table 1 title as printed: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Materials and Methods, Steady-State Kinetics section of this same paper states that dehalogenase assays were carried out at 30 °C in 50 mM NaHCO3/NaOH buffer (pH 9.4) using colorimetric detection of halide release from halogenated substrates, and that the Km and Vmax values were calculated from the initial rate of (halo)alcohol production, determined by gas chromatography, or from halide production rates, determined colorimetrically; in the two-column PDF text layer that sentence is interleaved line by line with the left column, so it is deliberately not reproduced here as a single contiguous quote. The export row carries pH 9.4 for the same measurement, matching the printed table title. The 1 mM dithiothreitol named in the paper belongs to the separate Rapid-Quench-Flow Measurements section and is not part of this steady-state Table 1 condition.

normalized_value_unit_evidence: metric: kcat; raw value: 2.3; raw unit: s-1; normalized value: 2.3 s^(-1); metric: Km; raw value: 1.0; raw unit: mM; normalized value: 1.0 mM; metric: kcat/Km; raw value: 2300; raw unit: M-1 s-1; normalized value: 2.3 s^-1 mM^-1; assay condition: Purified haloalkane dehalogenase DhaA of Rhodococcus rhodochrous; Table 1 title as printed: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Materials and Methods, Steady-State Kinetics section of this same paper states that dehalogenase assays were carried out at 30 °C in 50 mM NaHCO3/NaOH buffer (pH 9.4) using colorimetric detection of halide release from halogenated substrates, and that the Km and Vmax values were calculated from the initial rate of (halo)alcohol production, determined by gas chromatography, or from halide production rates, determined colorimetrically; in the two-column PDF text layer that sentence is interleaved line by line with the left column, so it is deliberately not reproduced here as a single contiguous quote. The export row carries pH 9.4 for the same measurement, matching the printed table title. The 1 mM dithiothreitol named in the paper belongs to the separate Rapid-Quench-Flow Measurements section and is not part of this steady-state Table 1 condition. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 2.3 s-1 is already in s^-1, so the normalized kcat is 2.3 s^(-1). Km 1.0 mM is already in mM, so the normalized Km is 1.0 mM. kcat/Km is read from this row's own printed kcat/Km cell 2300 M-1 s-1: 2300 M^-1 s^-1 / 1000 = 2.3 s^(-1)*mM^(-1). Cross-check against the quotient of this row's own two other printed cells: 2.3 s^-1 / 1.0 mM = 2.3 s^-1 mM^-1, which decimal-matches the printed ratio cell after the M^-1 to mM^-1 conversion. Two-sided round-trip: the quotient re-expressed in the printed column's unit is 2300.0 M-1 s-1 and rounds to the printed cell 2300 M-1 s-1 exactly; the printed cell converted back is 2.3 s^(-1)*mM^(-1), which equals the exported value. No disagreement survives rounding to either side's precision, so this is an exact match and not a correction. In this PDF text layer the superscript minus-one exponents render inline, so the printed headers appear as kcat (s-1), Km (mM) and kcat/Km (M-1 s-1).

raw_value_unit_evidence: Table 1: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C | printed column header line: substrate           kcat (s-1)   Km (mM)      kcat/Km (M-1 s-1) | printed row: 1,2-dibromopropane          2.3          1.0              2300 | kcat cell as printed for this row: 2.3, printed unit s-1 | Km cell as printed for this row: 1.0, printed unit mM | kcat/Km cell as printed for this row: 2300, printed unit M-1 s-1.


column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); second-set enzyme column 'L177V', substrate block '1,2-Dibromoethane'; row 'Km (mM)' = 9.32; row 'Ksi (mM)' = 1.91; row 'kcat (s^-1)' = 28.27; row 'kcat/Km (mM^-1 . s^-1)' = 3.03.

normalized_value_unit_evidence: Km: printed Table II cell 9.32 mM; mM is already the canonical unit, so no unit conversion applies and the value is 9.32 mM. kcat: printed Table II cell 28.27 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 28.27 s^(-1). kcat/Km: printed Table II cell 3.03 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 3.03 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 28.27 / 9.32 = 3.0332618025751072 s^-1 mM^-1.

raw_value_unit_evidence: Table II, second-set column 'L177V', 1,2-Dibromoethane block: Km = 9.32 mM; kcat = 28.27 s^-1; printed kcat/Km = 3.03 mM^-1 s^-1; printed Ksi = 1.91 mM.


column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); second-set enzyme column 'L177R', substrate block '1-Chlorobutane'; row 'Km (mM)' = 7.90; row 'kcat (s^-1)' = 1.89; row 'kcat/Km (mM^-1 . s^-1)' = 0.24.

normalized_value_unit_evidence: Km: printed Table II cell 7.90 mM; mM is already the canonical unit, so no unit conversion applies and the value is 7.9 mM. kcat: printed Table II cell 1.89 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 1.89 s^(-1). kcat/Km: printed Table II cell 0.24 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 0.24 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 1.89 / 7.90 = 0.2392405063291139 s^-1 mM^-1.

raw_value_unit_evidence: Table II, second-set column 'L177R', 1-Chlorobutane block: Km = 7.90 mM; kcat = 1.89 s^-1; printed kcat/Km = 0.24 mM^-1 s^-1.


column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); second-set enzyme column 'L177Y', substrate block '1,2-Dibromoethane'; row 'Km (mM)' = 4.62; row 'Ksi (mM)' = 0.34; row 'kcat (s^-1)' = 31.60; row 'kcat/Km (mM^-1 . s^-1)' = 6.83.

normalized_value_unit_evidence: Km: printed Table II cell 4.62 mM; mM is already the canonical unit, so no unit conversion applies and the value is 4.62 mM. kcat: printed Table II cell 31.60 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 31.6 s^(-1). kcat/Km: printed Table II cell 6.83 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 6.83 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 31.60 / 4.62 = 6.83982683982684 s^-1 mM^-1.

raw_value_unit_evidence: Table II, second-set column 'L177Y', 1,2-Dibromoethane block: Km = 4.62 mM; kcat = 31.60 s^-1; printed kcat/Km = 6.83 mM^-1 s^-1; printed Ksi = 0.34 mM.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D4Z2G1 and applied mutation signature L177C to reconstruct the assayed variant sequence.

column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); first-set enzyme column 'L177C', substrate block '1,2-Dibromoethane'; row 'Km (mM)' = 3.82; row 'Ksi (mM)' = 1.28; row 'kcat (s^-1)' = 14.00; row 'kcat/Km (mM^-1 . s^-1)' = 3.66.

normalized_value_unit_evidence: Km: printed Table II cell 3.82 mM; mM is already the canonical unit, so no unit conversion applies and the value is 3.82 mM. kcat: printed Table II cell 14.00 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 14.0 s^(-1). kcat/Km: printed Table II cell 3.66 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 3.66 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 14.00 / 3.82 = 3.6649214659685865 s^-1 mM^-1.

raw_value_unit_evidence: Table II, first-set column 'L177C', 1,2-Dibromoethane block: Km = 3.82 mM; kcat = 14.00 s^-1; printed kcat/Km = 3.66 mM^-1 s^-1; printed Ksi = 1.28 mM.


sequence_source: UniProtKB D4Z2G1 direct lookup; P51698 inactive demerge target matching UT26 context


column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); first-set enzyme column 'L177C', substrate block '1-Chlorobutane'; row 'Km (mM)' = 0.60; row 'kcat (s^-1)' = 0.49; row 'kcat/Km (mM^-1 . s^-1)' = 0.82.

normalized_value_unit_evidence: Km: printed Table II cell 0.60 mM; mM is already the canonical unit, so no unit conversion applies and the value is 0.6 mM. kcat: printed Table II cell 0.49 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 0.49 s^(-1). kcat/Km: printed Table II cell 0.82 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 0.82 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 0.49 / 0.60 = 0.8166666666666667 s^-1 mM^-1.

raw_value_unit_evidence: Table II, first-set column 'L177C', 1-Chlorobutane block: Km = 0.60 mM; kcat = 0.49 s^-1; printed kcat/Km = 0.82 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D4Z2G1 and applied mutation signature L177K to reconstruct the assayed variant sequence.

column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); first-set enzyme column 'L177K', substrate block '1,2-Dibromoethane'; row 'Km (mM)' = 6.23; row 'Ksi (mM)' = 0.90; row 'kcat (s^-1)' = 16.67; row 'kcat/Km (mM^-1 . s^-1)' = 2.68.

normalized_value_unit_evidence: Km: printed Table II cell 6.23 mM; mM is already the canonical unit, so no unit conversion applies and the value is 6.23 mM. kcat: printed Table II cell 16.67 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 16.67 s^(-1). kcat/Km: printed Table II cell 2.68 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 2.68 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 16.67 / 6.23 = 2.6757624398073836 s^-1 mM^-1.

raw_value_unit_evidence: Table II, first-set column 'L177K', 1,2-Dibromoethane block: Km = 6.23 mM; kcat = 16.67 s^-1; printed kcat/Km = 2.68 mM^-1 s^-1; printed Ksi = 0.90 mM.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D4Z2G1 and applied mutation signature L177S to reconstruct the assayed variant sequence.

column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); second-set enzyme column 'L177S', substrate block '1-Chlorobutane'; row 'Km (mM)' = 7.60; row 'kcat (s^-1)' = 2.87; row 'kcat/Km (mM^-1 . s^-1)' = 0.38.

normalized_value_unit_evidence: Km: printed Table II cell 7.60 mM; mM is already the canonical unit, so no unit conversion applies and the value is 7.6 mM. kcat: printed Table II cell 2.87 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 2.87 s^(-1). kcat/Km: printed Table II cell 0.38 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 0.38 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 2.87 / 7.60 = 0.37763157894736843 s^-1 mM^-1.

raw_value_unit_evidence: Table II, second-set column 'L177S', 1-Chlorobutane block: Km = 7.60 mM; kcat = 2.87 s^-1; printed kcat/Km = 0.38 mM^-1 s^-1.


organism: Agrobacterium tumefaciens

sequence_source: UniProtKB:E2RV69 canonical sequence; primaryAccession E2RV69; sequenceVersion 1

smiles: BrCCCBr


smiles: CCCCCCI


smiles: ICCCI

column_label: Table label: Table 1. Kinetic characteristics of DatA with six halogenated substrates. Row: 1,3-Diiodopropane. Enzyme: DatA haloalkane dehalogenase from Agrobacterium tumefaciens C58. Columns read: K0.5 (mM) cell 0.20, kcat (s^-1) cell 1.2, kcat/K0.5 (s^-1 mM^-1) cell 6.0. metric: kcat; raw value: 1.2; raw unit: s^-1; normalized value: 1.2 s^(-1); metric: Km; raw value: 0.20; raw unit: mM; normalized value: 0.2 mM; metric: kcat/Km; raw value: 6.0; raw unit: s^-1 mM^-1; normalized value: 5.999999999999999 s^-1 mM^-1; assay condition: Purified haloalkane dehalogenase DatA from Agrobacterium tumefaciens C58; Table 1 footnote a: all measurements used 100 mM glycine buffer, pH 8.6, at 37 C. Export row conditions: pH 8.6; 310.15 K.

normalized_value_unit_evidence: Table 1 row 1,3-Diiodopropane of the DatA kinetics table: kcat 1.2 s^-1 is already the export unit s^(-1), so it normalizes to 1.2 s^(-1) with no conversion. The Hill-equation half-saturation constant K0.5 is the Km-role parameter of this table and is printed in mM, the export unit, so K0.5 0.20 mM normalizes to 0.2 mM with no conversion. kcat/K0.5 is printed as 6.0 in s^-1 mM^-1, the export unit; the export stores the full-precision quotient of the same row's own printed cells, 1.2 s^-1 / 0.2 mM = 5.999999999999999 s^-1 mM^-1 in binary floating point, which is the printed 6.0 cell at that cell's own precision. Rendering quirks: in the Europe PMC PDF text extract the superscript minus one is flattened to a substitution glyph, so the header cell reads `kcat (s⫺1)`, and the plus-or-minus sign is substituted by `⫾`, so the same data row reads `1,3-Diiodopropanec 0.20 ⫾ 0.03 1.2 ⫾ 0.1 6.0 3.5 ⫾ 1.6` The trailing `c` on the row label is footnote marker c, not part of the substrate name.

raw_value_unit_evidence: Table 1 label: Kinetic characteristics of DatA with six halogenated substrates. Column header row of Table 1: Substrate | K0.5 (mM) | kcat (s^-1) | kcat/K0.5 (s^-1 mM^-1) | nH | mH | Ksi (mM).; kcat=1.2 +/- 0.1 s^-1; kcat/K0.5=6.0 s^-1 mM^-1; nH=3.5 +/- 1.6. The cells read: K0.5 = 0.20 mM (standard error of the fit 0.03 mM); kcat = 1.2 s^-1 (standard error of the fit 0.1 s^-1); kcat/K0.5 = 6.0 s^-1 mM^-1; Hill coefficient nH = 3.5; mH and Ksi are not reported for this row.


smiles: ClCCCCl


organism: Alcanivorax dieselolei

sequence_source: UniProtKB:K0CAI2 canonical sequence; primaryAccession K0CAI2; sequenceVersion 1


smiles: C=C(Cl)CCl


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D4Z2G1 and applied mutation signature L177W to reconstruct the assayed variant sequence.

column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); first-set enzyme column 'L177W', substrate block '1-Chlorobutane'; row 'Km (mM)' = 2.22; row 'kcat (s^-1)' = 2.52; row 'kcat/Km (mM^-1 . s^-1)' = 1.14.

normalized_value_unit_evidence: Km: printed Table II cell 2.22 mM; mM is already the canonical unit, so no unit conversion applies and the value is 2.22 mM. kcat: printed Table II cell 2.52 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 2.52 s^(-1). kcat/Km: printed Table II cell 1.14 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 1.14 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 2.52 / 2.22 = 1.135135135135135 s^-1 mM^-1.

raw_value_unit_evidence: Table II, first-set column 'L177W', 1-Chlorobutane block: Km = 2.22 mM; kcat = 2.52 s^-1; printed kcat/Km = 1.14 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D4Z2G1 and applied mutation signature L177H to reconstruct the assayed variant sequence.

column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); second-set enzyme column 'L177H', substrate block '1,2-Dibromoethane'; row 'Km (mM)' = 5.49; row 'Ksi (mM)' = 0.98; row 'kcat (s^-1)' = 26.53; row 'kcat/Km (mM^-1 . s^-1)' = 4.47.

normalized_value_unit_evidence: Km: printed Table II cell 5.49 mM; mM is already the canonical unit, so no unit conversion applies and the value is 5.49 mM. kcat: printed Table II cell 26.53 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 26.53 s^(-1). kcat/Km: printed Table II cell 4.47 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 4.47 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 26.53 / 5.49 = 4.832422586520948 s^-1 mM^-1.

raw_value_unit_evidence: Table II, second-set column 'L177H', 1,2-Dibromoethane block: Km = 5.49 mM; kcat = 26.53 s^-1; printed kcat/Km = 4.47 mM^-1 s^-1; printed Ksi = 0.98 mM.


column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); second-set enzyme column 'L177Q', substrate block '1,2-Dibromoethane'; row 'Km (mM)' = 10.37; row 'Ksi (mM)' = 1.12; row 'kcat (s^-1)' = 48.80; row 'kcat/Km (mM^-1 . s^-1)' = 4.71.

normalized_value_unit_evidence: Km: printed Table II cell 10.37 mM; mM is already the canonical unit, so no unit conversion applies and the value is 10.37 mM. kcat: printed Table II cell 48.80 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 48.8 s^(-1). kcat/Km: printed Table II cell 4.71 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 4.71 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 48.80 / 10.37 = 4.705882352941177 s^-1 mM^-1.

raw_value_unit_evidence: Table II, second-set column 'L177Q', 1,2-Dibromoethane block: Km = 10.37 mM; kcat = 48.80 s^-1; printed kcat/Km = 4.71 mM^-1 s^-1; printed Ksi = 1.12 mM.


column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); first-set enzyme column 'L177A', substrate block '1,2-Dibromoethane'; row 'Km (mM)' = 8.75; row 'Ksi (mM)' = 3.70; row 'kcat (s^-1)' = 47.20; row 'kcat/Km (mM^-1 . s^-1)' = 5.39.

normalized_value_unit_evidence: Km: printed Table II cell 8.75 mM; mM is already the canonical unit, so no unit conversion applies and the value is 8.75 mM. kcat: printed Table II cell 47.20 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 47.2 s^(-1). kcat/Km: printed Table II cell 5.39 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 5.39 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 47.20 / 8.75 = 5.394285714285715 s^-1 mM^-1.

raw_value_unit_evidence: Table II, first-set column 'L177A', 1,2-Dibromoethane block: Km = 8.75 mM; kcat = 47.20 s^-1; printed kcat/Km = 5.39 mM^-1 s^-1; printed Ksi = 3.70 mM.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D4Z2G1 and applied mutation signature L177G to reconstruct the assayed variant sequence.

column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); first-set enzyme column 'L177G', substrate block '1,2-Dibromoethane'; row 'Km (mM)' = 4.03; row 'Ksi (mM)' = 14.27; row 'kcat (s^-1)' = 12.35; row 'kcat/Km (mM^-1 . s^-1)' = 3.06.

normalized_value_unit_evidence: Km: printed Table II cell 4.03 mM; mM is already the canonical unit, so no unit conversion applies and the value is 4.03 mM. kcat: printed Table II cell 12.35 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 12.35 s^(-1). kcat/Km: printed Table II cell 3.06 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 3.06 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 12.35 / 4.03 = 3.064516129032258 s^-1 mM^-1.

raw_value_unit_evidence: Table II, first-set column 'L177G', 1,2-Dibromoethane block: Km = 4.03 mM; kcat = 12.35 s^-1; printed kcat/Km = 3.06 mM^-1 s^-1; printed Ksi = 14.27 mM.


column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); first-set enzyme column 'L177G', substrate block '1-Chlorobutane'; row 'Km (mM)' = 0.81; row 'kcat (s^-1)' = 1.28; row 'kcat/Km (mM^-1 . s^-1)' = 1.58.

normalized_value_unit_evidence: Km: printed Table II cell 0.81 mM; mM is already the canonical unit, so no unit conversion applies and the value is 0.81 mM. kcat: printed Table II cell 1.28 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 1.28 s^(-1). kcat/Km: printed Table II cell 1.58 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 1.58 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 1.28 / 0.81 = 1.5802469135802468 s^-1 mM^-1.

raw_value_unit_evidence: Table II, first-set column 'L177G', 1-Chlorobutane block: Km = 0.81 mM; kcat = 1.28 s^-1; printed kcat/Km = 1.58 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D4Z2G1 and applied mutation signature L177D to reconstruct the assayed variant sequence.

column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); second-set enzyme column 'L177D', substrate block '1,2-Dibromoethane'; row 'Km (mM)' = 14.00; row 'Ksi (mM)' = 5.32; row 'kcat (s^-1)' = 18.67; row 'kcat/Km (mM^-1 . s^-1)' = 1.33.

normalized_value_unit_evidence: Km: printed Table II cell 14.00 mM; mM is already the canonical unit, so no unit conversion applies and the value is 14.0 mM. kcat: printed Table II cell 18.67 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 18.67 s^(-1). kcat/Km: printed Table II cell 1.33 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 1.33 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 18.67 / 14.00 = 1.3335714285714286 s^-1 mM^-1.

raw_value_unit_evidence: Table II, second-set column 'L177D', 1,2-Dibromoethane block: Km = 14.00 mM; kcat = 18.67 s^-1; printed kcat/Km = 1.33 mM^-1 s^-1; printed Ksi = 5.32 mM.


sequence_source: UniProtKB:D4Z2G1; P51698 inactive/demerged replacement selected by UT26 strain context


organism: Caulobacter vibrioides

sequence_source: UniProtKB:Q9A919 direct accession lookup

smiles: ClCCCCCCl


organism: Lyngbya majuscula

sequence_source: UniProtKB:Q6DND9 direct accession lookup

smiles: N#CCCCBr


smiles: CCCI


smiles: CCCCI


sequence_source: UniProtKB:A6G7B1 direct accession lookup

smiles: BrCCBr

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 '1,2-Dibromoethane'; column Km [mM] = 1.57; column kcat [sec-1] = 0.38; column kcat/Km [mM-1 x sec-1] = 0.24. captured primary segment: 1,2-Dibromoethane | Km 1.57 mM | kcat 0.38 s^-1 | kcat/Km 0.24 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 1.57 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper-side value is 1.57 mM. kcat: printed Table 2 cell 0.38 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 0.38 s^(-1). kcat/Km: printed Table 2 cell 0.24 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 0.24 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.38 / 1.57 = 0.24203821656050956 s^-1 mM^-1, which the table prints as 0.24 at its own two-decimal precision.

raw_value_unit_evidence: Table 2, substrate row '1,2-Dibromoethane': Km = 1.57 mM; kcat = 0.38 sec^-1; printed kcat/Km = 0.24 mM^-1 sec^-1.


smiles: CCCCCl

column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); second-set enzyme column 'L177H', substrate block '1-Chlorobutane'; row 'Km (mM)' = 1.70; row 'kcat (s^-1)' = 1.06; row 'kcat/Km (mM^-1 . s^-1)' = 0.62.

normalized_value_unit_evidence: Km: printed Table II cell 1.70 mM; mM is already the canonical unit, so no unit conversion applies and the value is 1.7 mM. kcat: printed Table II cell 1.06 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 1.06 s^(-1). kcat/Km: printed Table II cell 0.62 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 0.62 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 1.06 / 1.70 = 0.6235294117647059 s^-1 mM^-1.

raw_value_unit_evidence: Table II, second-set column 'L177H', 1-Chlorobutane block: Km = 1.70 mM; kcat = 1.06 s^-1; printed kcat/Km = 0.62 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D4Z2G1 and applied mutation signature L177M to reconstruct the assayed variant sequence.

column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); second-set enzyme column 'L177M', substrate block '1-Chlorobutane'; row 'Km (mM)' = 0.34; row 'kcat (s^-1)' = 1.49; row 'kcat/Km (mM^-1 . s^-1)' = 4.36.

normalized_value_unit_evidence: Km: printed Table II cell 0.34 mM; mM is already the canonical unit, so no unit conversion applies and the value is 0.34 mM. kcat: printed Table II cell 1.49 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 1.49 s^(-1). kcat/Km: printed Table II cell 4.36 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 4.36 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 1.49 / 0.34 = 4.38235294117647 s^-1 mM^-1.

raw_value_unit_evidence: Table II, second-set column 'L177M', 1-Chlorobutane block: Km = 0.34 mM; kcat = 1.49 s^-1; printed kcat/Km = 4.36 mM^-1 s^-1.


column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); second-set enzyme column 'L177D', substrate block '1-Chlorobutane'; row 'Km (mM)' = 21.90; row 'kcat (s^-1)' = 0.94; row 'kcat/Km (mM^-1 . s^-1)' = 0.04.

normalized_value_unit_evidence: Km: printed Table II cell 21.90 mM; mM is already the canonical unit, so no unit conversion applies and the value is 21.9 mM. kcat: printed Table II cell 0.94 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 0.94 s^(-1). kcat/Km: printed Table II cell 0.04 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 0.04 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 0.94 / 21.90 = 0.042922374429223746 s^-1 mM^-1.

raw_value_unit_evidence: Table II, second-set column 'L177D', 1-Chlorobutane block: Km = 21.90 mM; kcat = 0.94 s^-1; printed kcat/Km = 0.04 mM^-1 s^-1.


column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); second-set enzyme column 'L177S', substrate block '1,2-Dibromoethane'; row 'Km (mM)' = 13.20; row 'Ksi (mM)' = 1.04; row 'kcat (s^-1)' = 45.33; row 'kcat/Km (mM^-1 . s^-1)' = 3.43.

normalized_value_unit_evidence: Km: printed Table II cell 13.20 mM; mM is already the canonical unit, so no unit conversion applies and the value is 13.2 mM. kcat: printed Table II cell 45.33 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 45.33 s^(-1). kcat/Km: printed Table II cell 3.43 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 3.43 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 45.33 / 13.20 = 3.434090909090909 s^-1 mM^-1.

raw_value_unit_evidence: Table II, second-set column 'L177S', 1,2-Dibromoethane block: Km = 13.20 mM; kcat = 45.33 s^-1; printed kcat/Km = 3.43 mM^-1 s^-1; printed Ksi = 1.04 mM.


column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); second-set enzyme column 'L177M', substrate block '1,2-Dibromoethane'; row 'Km (mM)' = 8.36; row 'Ksi (mM)' = 1.68; row 'kcat (s^-1)' = 39.33; row 'kcat/Km (mM^-1 . s^-1)' = 4.70.

normalized_value_unit_evidence: Km: printed Table II cell 8.36 mM; mM is already the canonical unit, so no unit conversion applies and the value is 8.36 mM. kcat: printed Table II cell 39.33 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 39.33 s^(-1). kcat/Km: printed Table II cell 4.70 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 4.7 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 39.33 / 8.36 = 4.704545454545455 s^-1 mM^-1.

raw_value_unit_evidence: Table II, second-set column 'L177M', 1,2-Dibromoethane block: Km = 8.36 mM; kcat = 39.33 s^-1; printed kcat/Km = 4.70 mM^-1 s^-1; printed Ksi = 1.68 mM.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D4Z2G1 and applied mutation signature L177F to reconstruct the assayed variant sequence.

column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); first-set enzyme column 'L177F', substrate block '1-Chlorobutane'; row 'Km (mM)' = 0.78; row 'kcat (s^-1)' = 3.23; row 'kcat/Km (mM^-1 . s^-1)' = 4.14.

normalized_value_unit_evidence: Km: printed Table II cell 0.78 mM; mM is already the canonical unit, so no unit conversion applies and the value is 0.78 mM. kcat: printed Table II cell 3.23 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 3.23 s^(-1). kcat/Km: printed Table II cell 4.14 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 4.14 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 3.23 / 0.78 = 4.1410256410256405 s^-1 mM^-1.

raw_value_unit_evidence: Table II, first-set column 'L177F', 1-Chlorobutane block: Km = 0.78 mM; kcat = 3.23 s^-1; printed kcat/Km = 4.14 mM^-1 s^-1.


column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); first-set enzyme column 'L177K', substrate block '1-Chlorobutane'; row 'Km (mM)' = 0.99; row 'kcat (s^-1)' = 0.98; row 'kcat/Km (mM^-1 . s^-1)' = 0.99.

normalized_value_unit_evidence: Km: printed Table II cell 0.99 mM; mM is already the canonical unit, so no unit conversion applies and the value is 0.99 mM. kcat: printed Table II cell 0.98 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 0.98 s^(-1). kcat/Km: printed Table II cell 0.99 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 0.99 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 0.98 / 0.99 = 0.98989898989899 s^-1 mM^-1.

raw_value_unit_evidence: Table II, first-set column 'L177K', 1-Chlorobutane block: Km = 0.99 mM; kcat = 0.98 s^-1; printed kcat/Km = 0.99 mM^-1 s^-1.


column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); first-set enzyme column 'L177W', substrate block '1,2-Dibromoethane'; row 'Km (mM)' = 0.12; row 'Ksi (mM)' = 2.34; row 'kcat (s^-1)' = 0.61; row 'kcat/Km (mM^-1 . s^-1)' = 5.08.

normalized_value_unit_evidence: Km: printed Table II cell 0.12 mM; mM is already the canonical unit, so no unit conversion applies and the value is 0.12 mM. kcat: printed Table II cell 0.61 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 0.61 s^(-1). kcat/Km: printed Table II cell 5.08 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 5.08 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 0.61 / 0.12 = 5.083333333333333 s^-1 mM^-1.

raw_value_unit_evidence: Table II, first-set column 'L177W', 1,2-Dibromoethane block: Km = 0.12 mM; kcat = 0.61 s^-1; printed kcat/Km = 5.08 mM^-1 s^-1; printed Ksi = 2.34 mM.


column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); first-set enzyme column 'L177F', substrate block '1,2-Dibromoethane'; row 'Km (mM)' = 5.03; row 'Ksi (mM)' = 0.90; row 'kcat (s^-1)' = 39.60; row 'kcat/Km (mM^-1 . s^-1)' = 7.87.

normalized_value_unit_evidence: Km: printed Table II cell 5.03 mM; mM is already the canonical unit, so no unit conversion applies and the value is 5.03 mM. kcat: printed Table II cell 39.60 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 39.6 s^(-1). kcat/Km: printed Table II cell 7.87 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 7.87 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 39.60 / 5.03 = 7.8727634194831015 s^-1 mM^-1.

raw_value_unit_evidence: Table II, first-set column 'L177F', 1,2-Dibromoethane block: Km = 5.03 mM; kcat = 39.60 s^-1; printed kcat/Km = 7.87 mM^-1 s^-1; printed Ksi = 0.90 mM.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:D4Z2G1 and applied mutation signature L177T to reconstruct the assayed variant sequence.

column_label: Table II: Steady-state kinetic parameters of purified wild type and mutant haloalkane dehalogenases (J. Biol. Chem. 2003, 278(52):52622-52628, journal page 52627); first-set enzyme column 'L177T', substrate block '1,2-Dibromoethane'; row 'Km (mM)' = 18.30; row 'Ksi (mM)' = 0.87; row 'kcat (s^-1)' = 38.67; row 'kcat/Km (mM^-1 . s^-1)' = 2.11.

normalized_value_unit_evidence: Km: printed Table II cell 18.30 mM; mM is already the canonical unit, so no unit conversion applies and the value is 18.3 mM. kcat: printed Table II cell 38.67 s^-1; s^-1 is already the canonical unit, so no unit conversion applies and the value is 38.67 s^(-1). kcat/Km: printed Table II cell 2.11 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1, so no unit conversion applies and the printed cell reads 2.11 s^(-1)*mM^(-1). The quotient of the paper's own two printed component cells is 38.67 / 18.30 = 2.1131147540983606 s^-1 mM^-1.

raw_value_unit_evidence: Table II, first-set column 'L177T', 1,2-Dibromoethane block: Km = 18.30 mM; kcat = 38.67 s^-1; printed kcat/Km = 2.11 mM^-1 s^-1; printed Ksi = 0.87 mM.


organism: Yarrowia lipolytica

sequence_source: UniProt Q6C598 canonical sequence, direct REST check on 2026-06-01; Q6C598 cross-references RefSeq XP_504164.1 and BRENDA EC 3.8.1.5.


smiles: CCCCCCCCCCCCBr


smiles: CCCCCCCCCCBr


smiles: OCCCBr

column_label: Table label: Table 1: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Evidence location type: table. Row label: 3-bromo-1-propanol. Column labels read: kcat (s-1) cell 3.0, Km (mM) cell 3.3, kcat/Km (M-1 s-1) cell 910. captured primary segment: 3-bromo-1-propanol          3.0          3.3               910. The printed kcat cell 3.0 s-1 decimal-matches the exported kcat 3.0 s^(-1); the printed Km cell 3.3 mM decimal-matches the exported km 3.3 mM; the exported kcat_over_km 0.9090909090909092 s^(-1)*mM^(-1) is the exact quotient of those same two printed cells of this same row. Every value in this record comes from the single printed row 3-bromo-1-propanol of Table 1; no value is taken from another row, another column, another table or another paper. assay condition: Purified haloalkane dehalogenase DhaA of Rhodococcus rhodochrous; Table 1 title as printed: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Materials and Methods, Steady-State Kinetics section of this same paper states that dehalogenase assays were carried out at 30 °C in 50 mM NaHCO3/NaOH buffer (pH 9.4) using colorimetric detection of halide release from halogenated substrates, and that the Km and Vmax values were calculated from the initial rate of (halo)alcohol production, determined by gas chromatography, or from halide production rates, determined colorimetrically; in the two-column PDF text layer that sentence is interleaved line by line with the left column, so it is deliberately not reproduced here as a single contiguous quote. The export row carries pH 9.4 for the same measurement, matching the printed table title. The 1 mM dithiothreitol named in the paper belongs to the separate Rapid-Quench-Flow Measurements section and is not part of this steady-state Table 1 condition.

normalized_value_unit_evidence: metric: kcat; raw value: 3.0; raw unit: s-1; normalized value: 3.0 s^(-1); metric: Km; raw value: 3.3; raw unit: mM; normalized value: 3.3 mM; metric: kcat/Km; derived from this row's own printed cells 3.0 s^-1 / 3.3 mM; normalized value: 0.9090909090909092 s^-1 mM^-1; assay condition: Purified haloalkane dehalogenase DhaA of Rhodococcus rhodochrous; Table 1 title as printed: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Materials and Methods, Steady-State Kinetics section of this same paper states that dehalogenase assays were carried out at 30 °C in 50 mM NaHCO3/NaOH buffer (pH 9.4) using colorimetric detection of halide release from halogenated substrates, and that the Km and Vmax values were calculated from the initial rate of (halo)alcohol production, determined by gas chromatography, or from halide production rates, determined colorimetrically; in the two-column PDF text layer that sentence is interleaved line by line with the left column, so it is deliberately not reproduced here as a single contiguous quote. The export row carries pH 9.4 for the same measurement, matching the printed table title. The 1 mM dithiothreitol named in the paper belongs to the separate Rapid-Quench-Flow Measurements section and is not part of this steady-state Table 1 condition. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 3.0 s-1 is already in s^-1, so the normalized kcat is 3.0 s^(-1). Km 3.3 mM is already in mM, so the normalized Km is 3.3 mM. kcat/Km is NOT read from the table's separately rounded kcat/Km cell 910 M-1 s-1; it is this row's own printed kcat divided by this row's own printed Km: 3.0 s^-1 / 3.3 mM = 0.9090909090909092 s^(-1)*mM^(-1). Two-sided round-trip against that separately printed cell: the whole kcat/Km column of Table 1 is printed at two significant figures (480, 2000, 36, 4500, 2300, 540000, 12000, 3600, 910), so the cell 910 M-1 s-1 stands for the interval [905.0, 915.0) M-1 s-1; the quotient of this row's own two printed cells re-expressed in that unit is 909.0909090909091 M-1 s-1, which falls inside that interval, and rounding it to the printed cell's granularity returns 910 exactly. Converted the other way, the printed cell is 0.91 s^(-1)*mM^(-1) and the exported 0.9090909090909092 s^(-1)*mM^(-1) rounds to it at that printed precision. No disagreement survives rounding to either side's precision, so this is an exact match and not a correction. In this PDF text layer the superscript minus-one exponents render inline, so the printed headers appear as kcat (s-1), Km (mM) and kcat/Km (M-1 s-1).

raw_value_unit_evidence: Table 1: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C | printed column header line: substrate           kcat (s-1)   Km (mM)      kcat/Km (M-1 s-1) | printed row: 3-bromo-1-propanol          3.0          3.3               910 | kcat cell as printed for this row: 3.0, printed unit s-1 | Km cell as printed for this row: 3.3, printed unit mM | kcat/Km cell as printed for this row: 910, printed unit M-1 s-1, retained as rounded corroboration only and not used as the exported ratio.


smiles: ClCC(Cl)CCl

column_label: Table label: Table 1: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Evidence location type: table. Row label: 1,2,3-trichloropropane. Column labels read: kcat (s-1) cell 0.08, Km (mM) cell 2.2, kcat/Km (M-1 s-1) cell 36. captured primary segment: 1,2,3-trichloropropane      0.08         2.2                36. The printed kcat cell 0.08 s-1 decimal-matches the exported kcat 0.08 s^(-1); the printed Km cell 2.2 mM decimal-matches the exported km 2.2 mM; the exported kcat_over_km 0.03636363636363636 s^(-1)*mM^(-1) is the exact quotient of those same two printed cells of this same row. Every value in this record comes from the single printed row 1,2,3-trichloropropane of Table 1; no value is taken from another row, another column, another table or another paper. assay condition: Purified haloalkane dehalogenase DhaA of Rhodococcus rhodochrous; Table 1 title as printed: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Materials and Methods, Steady-State Kinetics section of this same paper states that dehalogenase assays were carried out at 30 °C in 50 mM NaHCO3/NaOH buffer (pH 9.4) using colorimetric detection of halide release from halogenated substrates, and that the Km and Vmax values were calculated from the initial rate of (halo)alcohol production, determined by gas chromatography, or from halide production rates, determined colorimetrically; in the two-column PDF text layer that sentence is interleaved line by line with the left column, so it is deliberately not reproduced here as a single contiguous quote. The export row carries pH 9.4 for the same measurement, matching the printed table title. The 1 mM dithiothreitol named in the paper belongs to the separate Rapid-Quench-Flow Measurements section and is not part of this steady-state Table 1 condition.

normalized_value_unit_evidence: metric: kcat; raw value: 0.08; raw unit: s-1; normalized value: 0.08 s^(-1); metric: Km; raw value: 2.2; raw unit: mM; normalized value: 2.2 mM; metric: kcat/Km; derived from this row's own printed cells 0.08 s^-1 / 2.2 mM; normalized value: 0.03636363636363636 s^-1 mM^-1; assay condition: Purified haloalkane dehalogenase DhaA of Rhodococcus rhodochrous; Table 1 title as printed: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Materials and Methods, Steady-State Kinetics section of this same paper states that dehalogenase assays were carried out at 30 °C in 50 mM NaHCO3/NaOH buffer (pH 9.4) using colorimetric detection of halide release from halogenated substrates, and that the Km and Vmax values were calculated from the initial rate of (halo)alcohol production, determined by gas chromatography, or from halide production rates, determined colorimetrically; in the two-column PDF text layer that sentence is interleaved line by line with the left column, so it is deliberately not reproduced here as a single contiguous quote. The export row carries pH 9.4 for the same measurement, matching the printed table title. The 1 mM dithiothreitol named in the paper belongs to the separate Rapid-Quench-Flow Measurements section and is not part of this steady-state Table 1 condition. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 0.08 s-1 is already in s^-1, so the normalized kcat is 0.08 s^(-1). Km 2.2 mM is already in mM, so the normalized Km is 2.2 mM. kcat/Km is NOT read from the table's separately rounded kcat/Km cell 36 M-1 s-1; it is this row's own printed kcat divided by this row's own printed Km: 0.08 s^-1 / 2.2 mM = 0.03636363636363636 s^(-1)*mM^(-1). Two-sided round-trip against that separately printed cell: the whole kcat/Km column of Table 1 is printed at two significant figures (480, 2000, 36, 4500, 2300, 540000, 12000, 3600, 910), so the cell 36 M-1 s-1 stands for the interval [35.5, 36.5) M-1 s-1; the quotient of this row's own two printed cells re-expressed in that unit is 36.36363636363636 M-1 s-1, which falls inside that interval, and rounding it to the printed cell's granularity returns 36 exactly. Converted the other way, the printed cell is 0.036 s^(-1)*mM^(-1) and the exported 0.03636363636363636 s^(-1)*mM^(-1) rounds to it at that printed precision. No disagreement survives rounding to either side's precision, so this is an exact match and not a correction. In this PDF text layer the superscript minus-one exponents render inline, so the printed headers appear as kcat (s-1), Km (mM) and kcat/Km (M-1 s-1).

raw_value_unit_evidence: Table 1: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C | printed column header line: substrate           kcat (s-1)   Km (mM)      kcat/Km (M-1 s-1) | printed row: 1,2,3-trichloropropane      0.08         2.2                36 | kcat cell as printed for this row: 0.08, printed unit s-1 | Km cell as printed for this row: 2.2, printed unit mM | kcat/Km cell as printed for this row: 36, printed unit M-1 s-1, retained as rounded corroboration only and not used as the exported ratio.


smiles: CCCBr

column_label: Table label: Table 1: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Evidence location type: table. Row label: 1-bromopropane. Column labels read: kcat (s-1) cell 2.7, Km (mM) cell 0.6, kcat/Km (M-1 s-1) cell 4500. captured primary segment: 1-bromopropane              2.7          0.6              4500. The printed kcat cell 2.7 s-1 decimal-matches the exported kcat 2.7 s^(-1); the printed Km cell 0.6 mM decimal-matches the exported km 0.6 mM; the exported kcat_over_km 4.500000000000001 s^(-1)*mM^(-1) is the exact quotient of those same two printed cells of this same row. Every value in this record comes from the single printed row 1-bromopropane of Table 1; no value is taken from another row, another column, another table or another paper. assay condition: Purified haloalkane dehalogenase DhaA of Rhodococcus rhodochrous; Table 1 title as printed: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Materials and Methods, Steady-State Kinetics section of this same paper states that dehalogenase assays were carried out at 30 °C in 50 mM NaHCO3/NaOH buffer (pH 9.4) using colorimetric detection of halide release from halogenated substrates, and that the Km and Vmax values were calculated from the initial rate of (halo)alcohol production, determined by gas chromatography, or from halide production rates, determined colorimetrically; in the two-column PDF text layer that sentence is interleaved line by line with the left column, so it is deliberately not reproduced here as a single contiguous quote. The export row carries pH 9.4 for the same measurement, matching the printed table title. The 1 mM dithiothreitol named in the paper belongs to the separate Rapid-Quench-Flow Measurements section and is not part of this steady-state Table 1 condition.

normalized_value_unit_evidence: metric: kcat; raw value: 2.7; raw unit: s-1; normalized value: 2.7 s^(-1); metric: Km; raw value: 0.6; raw unit: mM; normalized value: 0.6 mM; metric: kcat/Km; derived from this row's own printed cells 2.7 s^-1 / 0.6 mM; normalized value: 4.500000000000001 s^-1 mM^-1; assay condition: Purified haloalkane dehalogenase DhaA of Rhodococcus rhodochrous; Table 1 title as printed: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Materials and Methods, Steady-State Kinetics section of this same paper states that dehalogenase assays were carried out at 30 °C in 50 mM NaHCO3/NaOH buffer (pH 9.4) using colorimetric detection of halide release from halogenated substrates, and that the Km and Vmax values were calculated from the initial rate of (halo)alcohol production, determined by gas chromatography, or from halide production rates, determined colorimetrically; in the two-column PDF text layer that sentence is interleaved line by line with the left column, so it is deliberately not reproduced here as a single contiguous quote. The export row carries pH 9.4 for the same measurement, matching the printed table title. The 1 mM dithiothreitol named in the paper belongs to the separate Rapid-Quench-Flow Measurements section and is not part of this steady-state Table 1 condition. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 2.7 s-1 is already in s^-1, so the normalized kcat is 2.7 s^(-1). Km 0.6 mM is already in mM, so the normalized Km is 0.6 mM. kcat/Km is NOT read from the table's separately rounded kcat/Km cell 4500 M-1 s-1; it is this row's own printed kcat divided by this row's own printed Km: 2.7 s^-1 / 0.6 mM = 4.500000000000001 s^(-1)*mM^(-1). Two-sided round-trip against that separately printed cell: the whole kcat/Km column of Table 1 is printed at two significant figures (480, 2000, 36, 4500, 2300, 540000, 12000, 3600, 910), so the cell 4500 M-1 s-1 stands for the interval [4450.0, 4550.0) M-1 s-1; the quotient of this row's own two printed cells re-expressed in that unit is 4500.000000000001 M-1 s-1, which falls inside that interval, and rounding it to the printed cell's granularity returns 4500 exactly. Converted the other way, the printed cell is 4.5 s^(-1)*mM^(-1) and the exported 4.500000000000001 s^(-1)*mM^(-1) rounds to it at that printed precision. No disagreement survives rounding to either side's precision, so this is an exact match and not a correction. In this PDF text layer the superscript minus-one exponents render inline, so the printed headers appear as kcat (s-1), Km (mM) and kcat/Km (M-1 s-1).

raw_value_unit_evidence: Table 1: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C | printed column header line: substrate           kcat (s-1)   Km (mM)      kcat/Km (M-1 s-1) | printed row: 1-bromopropane              2.7          0.6              4500 | kcat cell as printed for this row: 2.7, printed unit s-1 | Km cell as printed for this row: 0.6, printed unit mM | kcat/Km cell as printed for this row: 4500, printed unit M-1 s-1, retained as rounded corroboration only and not used as the exported ratio.


column_label: Table label: Table 1: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Evidence location type: table. Row label: 1,3-dibromopropane. Column labels read: kcat (s-1) cell 2.7, Km (mM) cell 0.005, kcat/Km (M-1 s-1) cell 540000. captured primary segment: 1,3-dibromopropane          2.7          0.005          540000. The printed kcat cell 2.7 s-1 decimal-matches the exported kcat 2.7 s^(-1); the printed Km cell 0.005 mM decimal-matches the exported km 0.005 mM; the exported kcat_over_km 540.0 s^(-1)*mM^(-1) is this row's own printed kcat/Km cell 540000 M-1 s-1 converted to s^-1 mM^-1, and it is also the exact quotient of this same row's printed kcat and Km cells. Every value in this record comes from the single printed row 1,3-dibromopropane of Table 1; no value is taken from another row, another column, another table or another paper. assay condition: Purified haloalkane dehalogenase DhaA of Rhodococcus rhodochrous; Table 1 title as printed: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Materials and Methods, Steady-State Kinetics section of this same paper states that dehalogenase assays were carried out at 30 °C in 50 mM NaHCO3/NaOH buffer (pH 9.4) using colorimetric detection of halide release from halogenated substrates, and that the Km and Vmax values were calculated from the initial rate of (halo)alcohol production, determined by gas chromatography, or from halide production rates, determined colorimetrically; in the two-column PDF text layer that sentence is interleaved line by line with the left column, so it is deliberately not reproduced here as a single contiguous quote. The export row carries pH 9.4 for the same measurement, matching the printed table title. The 1 mM dithiothreitol named in the paper belongs to the separate Rapid-Quench-Flow Measurements section and is not part of this steady-state Table 1 condition.

normalized_value_unit_evidence: metric: kcat; raw value: 2.7; raw unit: s-1; normalized value: 2.7 s^(-1); metric: Km; raw value: 0.005; raw unit: mM; normalized value: 0.005 mM; metric: kcat/Km; raw value: 540000; raw unit: M-1 s-1; normalized value: 540.0 s^-1 mM^-1; assay condition: Purified haloalkane dehalogenase DhaA of Rhodococcus rhodochrous; Table 1 title as printed: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Materials and Methods, Steady-State Kinetics section of this same paper states that dehalogenase assays were carried out at 30 °C in 50 mM NaHCO3/NaOH buffer (pH 9.4) using colorimetric detection of halide release from halogenated substrates, and that the Km and Vmax values were calculated from the initial rate of (halo)alcohol production, determined by gas chromatography, or from halide production rates, determined colorimetrically; in the two-column PDF text layer that sentence is interleaved line by line with the left column, so it is deliberately not reproduced here as a single contiguous quote. The export row carries pH 9.4 for the same measurement, matching the printed table title. The 1 mM dithiothreitol named in the paper belongs to the separate Rapid-Quench-Flow Measurements section and is not part of this steady-state Table 1 condition. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 2.7 s-1 is already in s^-1, so the normalized kcat is 2.7 s^(-1). Km 0.005 mM is already in mM, so the normalized Km is 0.005 mM. kcat/Km is read from this row's own printed kcat/Km cell 540000 M-1 s-1: 540000 M^-1 s^-1 / 1000 = 540.0 s^(-1)*mM^(-1). Cross-check against the quotient of this row's own two other printed cells: 2.7 s^-1 / 0.005 mM = 540.0 s^-1 mM^-1, which decimal-matches the printed ratio cell after the M^-1 to mM^-1 conversion. Two-sided round-trip: the quotient re-expressed in the printed column's unit is 540000.0 M-1 s-1 and rounds to the printed cell 540000 M-1 s-1 exactly; the printed cell converted back is 540.0 s^(-1)*mM^(-1), which equals the exported value. No disagreement survives rounding to either side's precision, so this is an exact match and not a correction. In this PDF text layer the superscript minus-one exponents render inline, so the printed headers appear as kcat (s-1), Km (mM) and kcat/Km (M-1 s-1).

raw_value_unit_evidence: Table 1: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C | printed column header line: substrate           kcat (s-1)   Km (mM)      kcat/Km (M-1 s-1) | printed row: 1,3-dibromopropane          2.7          0.005          540000 | kcat cell as printed for this row: 2.7, printed unit s-1 | Km cell as printed for this row: 0.005, printed unit mM | kcat/Km cell as printed for this row: 540000, printed unit M-1 s-1.


column_label: Table label: Table 1: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Evidence location type: table. Row label: 1,2-dibromoethane. Column labels read: kcat (s-1) cell 14.3, Km (mM) cell 4.0, kcat/Km (M-1 s-1) cell 3600. captured primary segment: 1,2-dibromoethane          14.3          4.0              3600. The printed kcat cell 14.3 s-1 decimal-matches the exported kcat 14.3 s^(-1); the printed Km cell 4.0 mM decimal-matches the exported km 4.0 mM; the exported kcat_over_km 3.575 s^(-1)*mM^(-1) is the exact quotient of those same two printed cells of this same row. Every value in this record comes from the single printed row 1,2-dibromoethane of Table 1; no value is taken from another row, another column, another table or another paper. assay condition: Purified haloalkane dehalogenase DhaA of Rhodococcus rhodochrous; Table 1 title as printed: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Materials and Methods, Steady-State Kinetics section of this same paper states that dehalogenase assays were carried out at 30 °C in 50 mM NaHCO3/NaOH buffer (pH 9.4) using colorimetric detection of halide release from halogenated substrates, and that the Km and Vmax values were calculated from the initial rate of (halo)alcohol production, determined by gas chromatography, or from halide production rates, determined colorimetrically; in the two-column PDF text layer that sentence is interleaved line by line with the left column, so it is deliberately not reproduced here as a single contiguous quote. The export row carries pH 9.4 for the same measurement, matching the printed table title. The 1 mM dithiothreitol named in the paper belongs to the separate Rapid-Quench-Flow Measurements section and is not part of this steady-state Table 1 condition.

normalized_value_unit_evidence: metric: kcat; raw value: 14.3; raw unit: s-1; normalized value: 14.3 s^(-1); metric: Km; raw value: 4.0; raw unit: mM; normalized value: 4.0 mM; metric: kcat/Km; derived from this row's own printed cells 14.3 s^-1 / 4.0 mM; normalized value: 3.575 s^-1 mM^-1; assay condition: Purified haloalkane dehalogenase DhaA of Rhodococcus rhodochrous; Table 1 title as printed: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Materials and Methods, Steady-State Kinetics section of this same paper states that dehalogenase assays were carried out at 30 °C in 50 mM NaHCO3/NaOH buffer (pH 9.4) using colorimetric detection of halide release from halogenated substrates, and that the Km and Vmax values were calculated from the initial rate of (halo)alcohol production, determined by gas chromatography, or from halide production rates, determined colorimetrically; in the two-column PDF text layer that sentence is interleaved line by line with the left column, so it is deliberately not reproduced here as a single contiguous quote. The export row carries pH 9.4 for the same measurement, matching the printed table title. The 1 mM dithiothreitol named in the paper belongs to the separate Rapid-Quench-Flow Measurements section and is not part of this steady-state Table 1 condition. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 14.3 s-1 is already in s^-1, so the normalized kcat is 14.3 s^(-1). Km 4.0 mM is already in mM, so the normalized Km is 4.0 mM. kcat/Km is NOT read from the table's separately rounded kcat/Km cell 3600 M-1 s-1; it is this row's own printed kcat divided by this row's own printed Km: 14.3 s^-1 / 4.0 mM = 3.575 s^(-1)*mM^(-1). Two-sided round-trip against that separately printed cell: the whole kcat/Km column of Table 1 is printed at two significant figures (480, 2000, 36, 4500, 2300, 540000, 12000, 3600, 910), so the cell 3600 M-1 s-1 stands for the interval [3550.0, 3650.0) M-1 s-1; the quotient of this row's own two printed cells re-expressed in that unit is 3575.0 M-1 s-1, which falls inside that interval, and rounding it to the printed cell's granularity returns 3600 exactly. Converted the other way, the printed cell is 3.6 s^(-1)*mM^(-1) and the exported 3.575 s^(-1)*mM^(-1) rounds to it at that printed precision. No disagreement survives rounding to either side's precision, so this is an exact match and not a correction. In this PDF text layer the superscript minus-one exponents render inline, so the printed headers appear as kcat (s-1), Km (mM) and kcat/Km (M-1 s-1).

raw_value_unit_evidence: Table 1: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C | printed column header line: substrate           kcat (s-1)   Km (mM)      kcat/Km (M-1 s-1) | printed row: 1,2-dibromoethane          14.3          4.0              3600 | kcat cell as printed for this row: 14.3, printed unit s-1 | Km cell as printed for this row: 4.0, printed unit mM | kcat/Km cell as printed for this row: 3600, printed unit M-1 s-1, retained as rounded corroboration only and not used as the exported ratio.


smiles: CCCCl

column_label: Table label: Table 1: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Evidence location type: table. Row label: 1-chloropropane. Column labels read: kcat (s-1) cell 0.48, Km (mM) cell 1.0, kcat/Km (M-1 s-1) cell 480. captured primary segment: 1-chloropropane             0.48          1.0               480. The printed kcat cell 0.48 s-1 decimal-matches the exported kcat 0.48 s^(-1); the printed Km cell 1.0 mM decimal-matches the exported km 1.0 mM; the exported kcat_over_km 0.48 s^(-1)*mM^(-1) is this row's own printed kcat/Km cell 480 M-1 s-1 converted to s^-1 mM^-1, and it is also the exact quotient of this same row's printed kcat and Km cells. Every value in this record comes from the single printed row 1-chloropropane of Table 1; no value is taken from another row, another column, another table or another paper. assay condition: Purified haloalkane dehalogenase DhaA of Rhodococcus rhodochrous; Table 1 title as printed: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Materials and Methods, Steady-State Kinetics section of this same paper states that dehalogenase assays were carried out at 30 °C in 50 mM NaHCO3/NaOH buffer (pH 9.4) using colorimetric detection of halide release from halogenated substrates, and that the Km and Vmax values were calculated from the initial rate of (halo)alcohol production, determined by gas chromatography, or from halide production rates, determined colorimetrically; in the two-column PDF text layer that sentence is interleaved line by line with the left column, so it is deliberately not reproduced here as a single contiguous quote. The export row carries pH 9.4 for the same measurement, matching the printed table title. The 1 mM dithiothreitol named in the paper belongs to the separate Rapid-Quench-Flow Measurements section and is not part of this steady-state Table 1 condition.

normalized_value_unit_evidence: metric: kcat; raw value: 0.48; raw unit: s-1; normalized value: 0.48 s^(-1); metric: Km; raw value: 1.0; raw unit: mM; normalized value: 1.0 mM; metric: kcat/Km; raw value: 480; raw unit: M-1 s-1; normalized value: 0.48 s^-1 mM^-1; assay condition: Purified haloalkane dehalogenase DhaA of Rhodococcus rhodochrous; Table 1 title as printed: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C. Materials and Methods, Steady-State Kinetics section of this same paper states that dehalogenase assays were carried out at 30 °C in 50 mM NaHCO3/NaOH buffer (pH 9.4) using colorimetric detection of halide release from halogenated substrates, and that the Km and Vmax values were calculated from the initial rate of (halo)alcohol production, determined by gas chromatography, or from halide production rates, determined colorimetrically; in the two-column PDF text layer that sentence is interleaved line by line with the left column, so it is deliberately not reproduced here as a single contiguous quote. The export row carries pH 9.4 for the same measurement, matching the printed table title. The 1 mM dithiothreitol named in the paper belongs to the separate Rapid-Quench-Flow Measurements section and is not part of this steady-state Table 1 condition. Conversion arithmetic (disclosed separately from the stated normalized values): kcat 0.48 s-1 is already in s^-1, so the normalized kcat is 0.48 s^(-1). Km 1.0 mM is already in mM, so the normalized Km is 1.0 mM. kcat/Km is read from this row's own printed kcat/Km cell 480 M-1 s-1: 480 M^-1 s^-1 / 1000 = 0.48 s^(-1)*mM^(-1). Cross-check against the quotient of this row's own two other printed cells: 0.48 s^-1 / 1.0 mM = 0.48 s^-1 mM^-1, which decimal-matches the printed ratio cell after the M^-1 to mM^-1 conversion. Two-sided round-trip: the quotient re-expressed in the printed column's unit is 480.0 M-1 s-1 and rounds to the printed cell 480 M-1 s-1 exactly; the printed cell converted back is 0.48 s^(-1)*mM^(-1), which equals the exported value. No disagreement survives rounding to either side's precision, so this is an exact match and not a correction. In this PDF text layer the superscript minus-one exponents render inline, so the printed headers appear as kcat (s-1), Km (mM) and kcat/Km (M-1 s-1).

raw_value_unit_evidence: Table 1: Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 °C | printed column header line: substrate           kcat (s-1)   Km (mM)      kcat/Km (M-1 s-1) | printed row: 1-chloropropane             0.48          1.0               480 | kcat cell as printed for this row: 0.48, printed unit s-1 | Km cell as printed for this row: 1.0, printed unit mM | kcat/Km cell as printed for this row: 480, printed unit M-1 s-1.


substrate_name: bis(2-chloroethyl) ether

smiles: ClCCOCCCl

substrate: bis(2-chloroethyl) ether


smiles: C=C(C)CCl


ki_unit: mM


organism: Ancylobacter aquaticus

kcat_display: Not reported

smiles: ClCCCl


smiles: BrCCCBr


smiles: CCCCCCCl


smiles: CCCCCCBr


enzyme_display_name: 4-hydroxyacetophenone monooxygenase

organism: Pseudomonas fluorescens

sequence_source: UniProtKB Q93TJ5 REST/FASTA direct check; reviewed Swiss-Prot HAPMO_PSEFL canonical sequence.

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

enzyme: 4-hydroxyacetophenone monooxygenase


substrate_name: NADH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

substrate: NADH


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q93TJ5 canonical sequence by applying R339A; canonical residue R at position 339 confirmed; PMID 15153101 supports the mutated HAPMO position. and applied mutation signature R339A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q93TJ5 canonical sequence by applying K439A; canonical residue K at position 439 confirmed; PMID 15153101 supports the mutated HAPMO position. and applied mutation signature K439A to reconstruct the assayed variant sequence.


enzyme_name_source: UniProtKB B7T912 and PMID 19251889

organism: Pseudomonas putida

substrate_name: acetophenone

sequence_source: UniProtKB B7T912 FASTA; TrEMBL entry B7T912_PSEPU, gene hapE, cited to PMID 19251889 and EMBL/GenBank protein ACJ37423.1 from nucleotide accession FJ010625.

assay_conditions_summary: pH 8; 303.15 K; buffer 50 mM Tris-HCl; cofactor NADPH

substrate: acetophenone


substrate_name: propiophenone

substrate: propiophenone


substrate_name: butyrophenone

substrate: butyrophenone


substrate_name: methyl-4-tolyl sulfide

sequence_source: UniProtKB:B7T912 FASTA; cross-referenced to EMBL FJ010625 / protein ACJ37423.1

assay_conditions_summary: pH 8; 303.15 K; buffer pH 8; cofactor NADPH

substrate: methyl-4-tolyl sulfide


substrate_name: trifluoroacetophenone

substrate: trifluoroacetophenone


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


enzyme_name_source: UniProtKB Q93TJ5 and PMID 12514023

substrate_name: 2-Pyrrole carboxaldehyde

substrate: 2-Pyrrole carboxaldehyde


substrate_name: methylphenyl sulfide

substrate: methylphenyl sulfide


substrate_name: cyclohexane carboxaldehyde

substrate: cyclohexane carboxaldehyde


substrate_name: Isobutyrophenone

substrate: Isobutyrophenone


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

proof_lines: Substrate Specificity and Enantioselectivity of 4-Hydroxyacetophenone Monooxygenase


substrate_name: Hydroxyacetone

smiles: CC(=O)CO

substrate: Hydroxyacetone


substrate_name: Acetylcyclohexane

substrate: Acetylcyclohexane


enzyme_display_name: polynucleotide adenylyltransferase

organism: Homo sapiens

kcat_over_km_display: Not reported

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

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

enzyme: polynucleotide adenylyltransferase


sequence_source: UniProtKB Q8NDF8 canonical FASTA fetched 2026-06-01


enzyme_display_name: methylglyoxal reductase (NADPH)

organism: Aspergillus niger

substrate_name: NADPH; H+; Methylglyoxal

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

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

assay_conditions_summary: cofactor NADPH

proof_lines:
enzyme MGR II
enzyme MGR I

enzyme: methylglyoxal reductase (NADPH)

substrate: NADPH; H+; Methylglyoxal


organism: Cyberlindnera mrakii

substrate_name: NADPH

source_db: brenda

substrate: NADPH

source: brenda


organism: Methanocaldococcus jannaschii

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: pH 7, temperature not specified in the publication


organism: Synechococcus sp.

substrate_name: DL-glyceraldehyde

proof_lines:
1 mM
50 mM

substrate: DL-glyceraldehyde


organism: Kluyveromyces marxianus

substrate_name: methyl glyoxal

sequence_source: UniProtKB A0A0E4AY21 REST lookup on 2026-06-01; accession was source-provided by BRENDA in the selected batch.

assay_conditions_summary: pH 6; cofactor NADPH

substrate: methyl glyoxal


organism: Saccharomyces cerevisiae

substrate_name: Methylglyoxal

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

sequence_source: UniProtKB Q12068 REST lookup on 2026-06-01; accession was source-provided by SABIO-RK in the selected batch.

substrate: Methylglyoxal


enzyme_display_name: D-arabinitol dehydrogenase (NADP(+))

organism: Uromyces fabae

substrate_name: D-arabinitol

source_db: uniprot

enzyme: D-arabinitol dehydrogenase (NADP(+))

substrate: D-arabinitol

source: uniprot


substrate_name: NADP+; D-Arabitol

km_display: Not reported

sequence_source: UniProtKB:Q4R0J7 reviewed entry and FASTA, cross-checked against the accession reuse cache.

substrate: NADP+; D-Arabitol


organism: Uromyces viciae-fabae

sequence_source: UniProtKB:Q4R0J7 reviewed entry and FASTA; ENA:AJ809335 CDS translation cross-references UniProtKB/Swiss-Prot:Q4R0J7.

assay_conditions_summary: pH 6

proof_lines:
pH 6.0, with D-fructose
pH 6.0, with D-xylulose
pH 9.0, with D-mannitol


organism: Gluconobacter oxydans

substrate_name: meso-erythritol

substrate: meso-erythritol


substrate_name: D-sorbitol

substrate: D-sorbitol


substrate_name: D-Arabitol

substrate: D-Arabitol


substrate_name: D-mannitol

substrate: D-mannitol


substrate_name: glycerol

smiles: OCC(O)CO

substrate: glycerol


substrate_name: D-ribitol

substrate: D-ribitol


substrate_name: xylitol

substrate: xylitol


enzyme_display_name: arsenate-mycothiol transferase

organism: Corynebacterium glutamicum

substrate_name: arsenate

assay_conditions_summary: pH 8

proof_lines: isoform ArsC2, pH 8.0, presence of phosphate

proof_lines: isoform ArsC1, pH 8.0, presence of phosphate

proof_lines: isoform ArsC2, pH 8.0, presence of sulfate

enzyme: arsenate-mycothiol transferase

substrate: arsenate