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'


enzyme_display_name: haloalkane dehalogenase

organism: Rhodococcus rhodochrous

source_db: oed

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_source: UniProtKB:P0A3G2 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: 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.

data_origin: experimental

enzyme: haloalkane dehalogenase

status: verified

source: oed


smiles: CC(Br)CBr

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.


organism: Sphingomonas paucimobilis

verification_status: unverified

kcat_over_km_origin: calculated

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

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

smiles: BrCCBr

mutation_type: substitution

status: unverified


smiles: CCCCCl


organism: Agrobacterium tumefaciens

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

smiles: BrCCCBr


smiles: CCCCCCI


smiles: CCCCCCCl


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


smiles: CCCCCCBr


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 UniProtKB:D4Z2G1; P51698 inactive/demerged replacement selected by UT26 strain context and applied mutation signature L177W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:D4Z2G1; P51698 inactive/demerged replacement selected by UT26 strain context and applied mutation signature L177H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:D4Z2G1; P51698 inactive/demerged replacement selected by UT26 strain context and applied mutation signature L177Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:D4Z2G1; P51698 inactive/demerged replacement selected by UT26 strain context and applied mutation signature L177A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:D4Z2G1; P51698 inactive/demerged replacement selected by UT26 strain context and applied mutation signature L177G to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:D4Z2G1; P51698 inactive/demerged replacement selected by UT26 strain context and applied mutation signature L177D to reconstruct the assayed variant sequence.


organism: Caulobacter vibrioides

sequence_source: UniProtKB:Q9A919 direct accession lookup

smiles: ClCCCCCCl


smiles: CCCCBr


organism: Lyngbya majuscula

sequence_source: UniProtKB:Q6DND9 direct accession lookup

smiles: N#CCCCBr


smiles: CCCI


smiles: CCCCI


organism: Plesiocystis pacifica

sequence_source: UniProtKB:A6G7B1 direct accession lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:D4Z2G1 canonical FASTA; P51698 inactive/demerged replacement selected by UT26/UT26S strain match; mutation reconstructed from PMID 14525993 residue-177 engineering context and applied mutation signature L177H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:D4Z2G1 canonical FASTA; P51698 inactive/demerged replacement selected by UT26/UT26S strain match; mutation reconstructed from PMID 14525993 residue-177 engineering context and applied mutation signature L177M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:D4Z2G1 canonical FASTA; P51698 inactive/demerged replacement selected by UT26/UT26S strain match; mutation reconstructed from PMID 14525993 residue-177 engineering context and applied mutation signature L177D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:D4Z2G1 canonical FASTA; P51698 inactive/demerged replacement selected by UT26/UT26S strain match; mutation reconstructed from PMID 14525993 residue-177 engineering context and applied mutation signature L177S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:D4Z2G1 canonical FASTA; P51698 inactive/demerged replacement selected by UT26/UT26S strain match; mutation reconstructed from PMID 14525993 residue-177 engineering context


sequence_variant_note: Resolved canonical sequence from UniProtKB:D4Z2G1 canonical FASTA; P51698 inactive/demerged replacement selected by UT26/UT26S strain match; mutation reconstructed from PMID 14525993 residue-177 engineering context and applied mutation signature L177F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:D4Z2G1 canonical FASTA; P51698 inactive/demerged replacement selected by UT26/UT26S strain match; mutation reconstructed from PMID 14525993 residue-177 engineering context and applied mutation signature L177K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:D4Z2G1 canonical FASTA; P51698 inactive/demerged replacement selected by UT26/UT26S strain match; mutation reconstructed from PMID 14525993 residue-177 engineering context and applied mutation signature L177W to reconstruct the assayed variant sequence.


sequence_source: UniProt D4Z2G1 canonical sequence, direct REST check on 2026-06-01; source accession P51698 is inactive and listed as a secondary accession on D4Z2G1; L177F reconstructed by replacing residue 177 after confirming canonical residue 177 is L.


sequence_source: UniProt D4Z2G1 canonical sequence, direct REST check on 2026-06-01; source accession P51698 is inactive and listed as a secondary accession on D4Z2G1; L177T reconstructed by replacing residue 177 after confirming canonical residue 177 is L.


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: CCCBr


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.


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.


smiles: BrCCCBr

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.


smiles: BrCCBr

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


verification_status: corrected

smiles: C=C(C)CCl

status: corrected


ki_unit: mM


smiles: CCCCCl


organism: Ancylobacter aquaticus

kcat_display: Not reported

smiles: ClCCCl


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.

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

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


substrate_name: Arsenate; Mycothiol

sequence_source: UniProtKB direct lookup for P0DKS5; matches accession reuse cache accession_2fb3d14c44b4d48b

substrate: Arsenate; Mycothiol


sequence_source: UniProtKB direct lookup for P0DKS7; matches accession reuse cache accession_2293b723b69248b3


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

proof_lines: isoform ArsC1, pH and temperature not specified in the publication

proof_lines: isoform ArsC2, pH and temperature not specified in the publication

source_databases_merged: sabio_rk brenda skid


organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)

assay_conditions_summary: pH 8; buffer 50 mM Hepes; cofactor mycoredoxin 1; mycothiol; mycothione reductase; NADPH


enzyme_display_name: 6-oxocamphor hydrolase

organism: Rhodococcus sp.

sequence_variant_note: Resolved canonical sequence from uniprot_exact_accession:Q93TU6 and applied mutation signature H45A to reconstruct the assayed variant sequence.

enzyme: 6-oxocamphor hydrolase


sequence_variant_note: Resolved canonical sequence from uniprot_exact_accession:Q93TU6 and applied mutation signature H145A to reconstruct the assayed variant sequence.


substrate_name: 6-Oxocamphor; H2O

sequence_variant_note: Resolved canonical sequence from uniprot_exact_accession:Q93TU6 and applied mutation signature D154N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6-oxocamphor hydrolase(Enzyme) mutant D154N

substrate: 6-Oxocamphor; H2O


substrate_name: H2O; 6-Oxocamphor

sequence_variant_note: Resolved canonical sequence from uniprot_exact_accession:Q93TU6 and applied mutation signature H122A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 6-oxocamphor hydrolase(Enzyme) mutant H122A

substrate: H2O; 6-Oxocamphor


proof_lines: SABIO-RK modifier species: 6-oxocamphor hydrolase(Enzyme) mutant H145A


proof_lines: SABIO-RK modifier species: 6-oxocamphor hydrolase(Enzyme) mutant H45A


organism: Rhodococcus sp


sequence_variant_note: Resolved canonical sequence from UniProtKB Q93TU6 canonical sequence checked directly; D154N reconstructed after confirming canonical residue D154. and applied mutation signature D154N to reconstruct the assayed variant sequence.


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

sequence_source: UniProtKB Q93TU6 FASTA checked directly for the canonical wild-type sequence.

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7
Raw SKiD Env: Temp=-----, pH=-----


sequence_variant_note: Resolved canonical sequence from UniProtKB Q93TU6 canonical sequence checked directly; E244Q reconstructed after confirming canonical residue E244. and applied mutation signature E244Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q93TU6 canonical sequence checked directly; E244Q reconstructed after confirming canonical residue E244.

proof_lines: SABIO-RK modifier species: 6-oxocamphor hydrolase(Enzyme) mutant E244Q


organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)


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


organism: Escherichia coli

substrate_name: UDP-GlcUA

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

substrate: UDP-GlcUA


organism: Bos taurus

substrate_name: UDP-N-acetyl-beta-D-galactosamine

substrate: UDP-N-acetyl-beta-D-galactosamine


substrate_name: UDP-N-acetyl-alpha-D-glucosamine

sequence_source: UniProtKB Q8L0V4, direct REST check on 2026-06-01

proof_lines: wild type enzyme, in 25 mM HEPES (pH 7.5), 100 mM NaCl, 20 mM MnCl2, 1 mM CaCl2, at 30°C

substrate: UDP-N-acetyl-alpha-D-glucosamine


organism: Avibacterium paragallinarum

substrate_name: UDP-GalNAc

sequence_source: UniProtKB direct accession lookup for D0QYM5 on 2026-06-01

substrate: UDP-GalNAc


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

sequence_source: UniProtKB direct accession lookup for Q8L0V4 on 2026-06-01

source_databases_merged: brenda skid


organism: Homo sapiens

substrate_name: Chondroitin sulfate; UDPglucuronate

sequence_source: UniProtKB direct accession lookup for Q70JA7 on 2026-06-01

substrate: Chondroitin sulfate; UDPglucuronate


sequence_source: UniProtKB direct accession lookup for Q86X52 on 2026-06-01


organism: Sphingobium sp. (strain NBRC 103272 / SYK-6)

substrate_name: vanillate

proof_lines: kcat is 5.76 sec(-1) with vanillate as substrate.

substrate: vanillate


organism: Neomoorella thermoacetica


organism: Sphingobium sp.

sequence_source: UniProtKB reviewed accession G2IQS7, direct lookup 2026-06-01


organism: Sphingomonas paucimobilis

sequence_source: UniProtKB accession Q60FX1 redirected to reviewed primary accession G2IQS7, direct lookup 2026-06-01


substrate_name: Vanillate; 5,6,7,8-Tetrahydrofolate

substrate: Vanillate; 5,6,7,8-Tetrahydrofolate


proof_lines: substrate tetrahydrofolate, pH 8.0, 30°C


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB reviewed accession P9WKL5 fetched by direct accession lookup

proof_lines:
pH 7.0 30°C
Raw SKiD Env: Temp=30°C, pH=7


organism: Mycobacteroides abscessus

sequence_source: UniProtKB reviewed accession B1MCE2 fetched by direct accession lookup


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: HQNO

proof_lines: kcat is 0.8 sec(-1) with HQNO as substrate (PubMed:33064871). kcat is 0.074 min(-1) with compound 14 as substrate (PubMed:27432954).

substrate: HQNO


organism: Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948)

proof_lines: kcat is 2.0 sec(-1) with HQNO as substrate.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P9WKL5:S140A and applied mutation signature S140A to reconstruct the assayed variant sequence.


organism: Arabidopsis thaliana

substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Humulus lupulus

substrate_name: AMP

substrate: AMP


substrate_name: Dimethylallyl diphosphate; ATP

sequence_source: UniProtKB reviewed direct accession lookup for Q9SB60

substrate: Dimethylallyl diphosphate; ATP


substrate_name: ADP

sequence_source: UniProtKB reviewed direct accession lookup for Q5GHF7

assay_conditions_summary: pH 7; 298.15 K; buffer or raw SKiD pH/temperature notes; cofactor ATP

proof_lines: in HEPES (20mM, pH 7.0; 150 mM NaCl, 3 mM dithiothreitol), at 25°C

substrate: ADP


organism: Morus alba

sequence_source: UniProtKB TrEMBL direct accession lookup for Q08ET4

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP


assay_conditions_summary: pH 7; 298.15 K; buffer 100 mM Tris-HCl; cofactor ATP

proof_lines: in 100 mM Tris-HCl buffer, pH 7.0, containing 50 mM KCl, 2 mM MnCl2, 1 mg/ml bovine serum albumin, and 1 mM dithiohtreitol, at 25°C


substrate_name: dimethylallyl diphosphate

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

substrate: dimethylallyl diphosphate


sequence_source: UniProtKB Q9SB60 reviewed Swiss-Prot entry IPT4_ARATH; PMID 11479373 reference covers catalytic activity and the source cache records sequence_source=source_record with confidence 1.0.

assay_conditions_summary: pH 7.5; 297.15 K; cofactor ATP

proof_lines: in 25 mM Tris-HCl, pH 7.5, 10 mM MgCl2+, 5 mM 2-mercaptoethanol at 24°C


sequence_source: UniProtKB Q5GHF7 reviewed Swiss-Prot entry IPT_HUMLU; PMID 15381407 reference covers catalytic activity and the source cache records sequence_source=source_record with confidence 1.0.

assay_conditions_summary: pH 8; 298.15 K; buffer 100 mM Tris-HCl; cofactor ATP

proof_lines: in 100 mM Tris-HCl buffer, pH 8.0, containing 50 mM KCl, 10 mM MgCl2, 1 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 25°C

proof_lines: in 100 mM Tris–HCl buffer, pH 8.0, containing 50 mM KCl, 10 mM MgCl2, 1 mg/ml bovine serum albumin, 1 mM dithiothreitol, at 25°C


enzyme_display_name: homocysteine S-methyltransferase

organism: Brassica oleracea var. italica

substrate_name: DL-homocysteine

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

enzyme: homocysteine S-methyltransferase

substrate: DL-homocysteine


substrate_name: S-Methyl-L-methionine; L-Homocysteine

proof_lines: pH 7.5, 30°C, cosubstrate: S-adenosyl-L-methionine

proof_lines: pH 7.5, 30°C, cosubstrate: S-methyl-L-methionine

substrate: S-Methyl-L-methionine; L-Homocysteine


substrate_name: L-Homocysteine; S-Methyl-L-methionine

substrate: L-Homocysteine; S-Methyl-L-methionine


proof_lines: pH 7.5, 25°C, cosubstrate: S-methyl-L-methionine

proof_lines: pH 7.5, 25°C, cosubstrate: S-adenosyl-L-methionine


organism: Escherichia coli (strain K12)

substrate_name: L-Homocysteine

substrate: L-Homocysteine


substrate_name: S-Adenosyl-L-methionine; L-Homocysteine

proof_lines: pH 6, 30°C, cosubstrate: S-adenosyl-L-methionine

substrate: S-Adenosyl-L-methionine; L-Homocysteine


substrate_name: S-methyl-L-methionine

proof_lines: final concentrations of S-methyl-L-methionine ranging from 0.1 mM to 9 mM, lower value than obtained for BHMT (EC 2.1.1.5)

substrate: S-methyl-L-methionine


enzyme_display_name: carnosine N-methyltransferase

organism: Gallus gallus

substrate_name: S-adenosyl-L-methionine

enzyme: carnosine N-methyltransferase

substrate: S-adenosyl-L-methionine


organism: Oryctolagus cuniculus

substrate_name: Actin peptide H

substrate: Actin peptide H


substrate_name: carnosine

proof_lines: kcat is 0.034 sec(-1) for carnosine. kcat is 0.519 sec(-1) for S-adenosyl-L-methionine.

substrate: carnosine


proof_lines: kcat is 0.14 min(-1) for carnosine. kcat is 2.51 min(-1) for S-adenosyl-L-methionine.


proof_lines: kcat is 0.09 min(-1) for carnosine. kcat is 3.57 min(-1) for S-adenosyl-L-methionine.


organism: Rattus norvegicus

proof_lines: kcat is 0.15 min(-1) for carnosine. kcat is 4.69 min(-1) for S-adenosyl-L-methionine.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 0.38 min(-1) for carnosine. kcat is 0.74 min(-1) for S-adenosyl-L-methionine.


substrate_name: S-Adenosyl-L-methionine

sequence_source: UniProt REST FASTA accession F1N9S8; matched identity reuse cache accession:F1N9S8

substrate: S-Adenosyl-L-methionine


substrate_name: S-Adenosyl-L-methionine; Carnosine

substrate: S-Adenosyl-L-methionine; Carnosine


organism: Homo sapiens

sequence_source: UniProt REST FASTA accession Q8N4J0; matched identity reuse cache accession:Q8N4J0


proof_lines:
pH 7.5, 30°C
Raw SKiD Env: Temp=30°C, pH=7.5


sequence_source: UniProt REST FASTA accession Q5BJZ6; matched identity reuse cache accession:Q5BJZ6


substrate_name: Carnosine; S-Adenosyl-L-methionine

sequence_source: UniProtKB Q5BJZ6 direct accession lookup; sequence matched the accession reuse cache.

substrate: Carnosine; S-Adenosyl-L-methionine


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB P53934 direct accession lookup; sequence matched the accession reuse cache.


enzyme_display_name: sulfoquinovosidase

organism: Agrobacterium tumefaciens

substrate_name: 4-nitrophenyl alpha-sulfoquinovoside

sequence_source: UniProt A9CEZ0 canonical sequence with K245Q reconstructed during review from PMID 30276262 UniProt mutagenesis evidence.

sequence_variant_note: Mutation signature K245Q matches the mutant residue at offset +0 and the reference residue at offset +11; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: mutant K245Q, pH not specified in the publication, temperature not specified in the publication

enzyme: sulfoquinovosidase

substrate: 4-nitrophenyl alpha-sulfoquinovoside


sequence_source: UniProt A9CEZ0 canonical AtSQase/SmoI sequence linked to PMID 30276262.

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


proof_lines: mutantK245Q/ E270Q, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant E270Q, pH not specified in the publication, temperature not specified in the publication


substrate_name: para-nitrophenyl alpha-sulfoquinovoside

proof_lines: kcat is 14.3 sec(-1) with para-nitrophenyl alpha-sulfoquinovoside as substrate.

substrate: para-nitrophenyl alpha-sulfoquinovoside


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from UniProt P32138 REST direct check; variant sequence reconstructed from the P32138 canonical sequence when mutation_signature is present. and applied mutation signature R301K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: sulfoquinovosidase(Enzyme) mutant R301K His-tagged


sequence_variant_note: Resolved canonical sequence from UniProt P32138 REST direct check; variant sequence reconstructed from the P32138 canonical sequence when mutation_signature is present. and applied mutation signature R301Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: sulfoquinovosidase(Enzyme) mutant R301Q His-tagged


sequence_source: UniProt P32138 REST direct check; variant sequence reconstructed from the P32138 canonical sequence when mutation_signature is present.

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


sequence_variant_note: Resolved canonical sequence from UniProt P32138 REST direct check; variant sequence reconstructed from the P32138 canonical sequence when mutation_signature is present. and applied mutation signature Q288E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: sulfoquinovosidase(Enzyme) mutant Q288E His-tagged

proof_lines: mutant Q288E, pH not specified in the publication, temperature not specified in the publication


substrate_name: p-Nitrophenol alpha-D-glucopyranoside

substrate: p-Nitrophenol alpha-D-glucopyranoside


sequence_variant_note: Resolved canonical sequence from UniProt P32138 REST direct check; variant sequence reconstructed from the P32138 canonical sequence when mutation_signature is present. and applied mutation signature Q262K/Q288E to reconstruct the assayed variant sequence.

proof_lines: mutant Q262K/Q288E, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt P32138 REST direct check; variant sequence reconstructed from the P32138 canonical sequence when mutation_signature is present. and applied mutation signature Q262K to reconstruct the assayed variant sequence.

proof_lines: mutant Q262K, pH not specified in the publication, temperature not specified in the publication


organism: Marinobacter adhaerens (strain DSM 23420 / HP15)

substrate_name: 2-O-(alpha-D-glucopyranosyl)glycerol (at pH 6.5 and 37 degrees Celsius)

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

proof_lines: kcat is 14 sec(-1) towards 2-O-(alpha-D-glucopyranosyl)glycerol for the phosphorolytic direction (at pH 6.5 and 37 degrees Celsius). kcat is 14 sec(-1) towards phosphate for the phosphorolytic direction (at pH 6.5 and 37 degrees Celsius). k


organism: Marinobacter adhaerens


proof_lines:
pH 6.5, 37°C
recombinant enzyme, pH 6.5, 37°C
Raw SKiD Env: Temp=37°C, pH=6.5


substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


substrate_name: glycerol

substrate: glycerol


substrate_name: phosphate

smiles: O=P(O)(O)O

substrate: phosphate


enzyme_display_name: cyanohydrin beta-glucosyltransferase

organism: Sorghum bicolor

substrate_name: mandelonitrile

proof_lines: kcat is 10.6 sec(-1) with mandelonitrile as substrate. kcat is 0.10 sec(-1) with geraniol as substrate. kcat is 0.09 sec(-1) with beta-citronellol as substrate. kcat is 0.06 sec(-1) with nerol as substrate. kcat is 0.06 sec(-1) with 1-hexan

enzyme: cyanohydrin beta-glucosyltransferase

substrate: mandelonitrile


substrate_name: geraniol

substrate: geraniol


substrate_name: Prenol

sequence_source: UniProtKB Q9SBL1 direct lookup; matches accession reuse cache accession_f5a28182a913b775

smiles: CC(C)=CCO

substrate: Prenol


substrate_name: Leaf alcohol

smiles: CCC=CCCO

substrate: Leaf alcohol


substrate_name: Mandelonitrile; UDPglucose

proof_lines: pH 7.5, 30°C, cosubstrate: mandelonitrile

substrate: Mandelonitrile; UDPglucose


organism: Prunus dulcis

substrate_name: benzyl alcohol

substrate: benzyl alcohol


sequence_source: UniProtKB:Q9SBL1 direct accession lookup

smiles: C=C(C)CCO


smiles: CCCCCCO


substrate_name: beta-Citronellol

smiles: CC(C)=CCCC(C)CCO

substrate: beta-Citronellol


substrate_name: Mandelonitrile

substrate: Mandelonitrile


substrate_name: Nerol

smiles: CC(C)=CCC/C(C)=C\CO

substrate: Nerol


substrate_name: Geraniol

smiles: CC(C)=CCC/C(C)=C/CO

substrate: Geraniol


substrate_name: 2-Hydroxy-3-methoxybenzyl alcohol

substrate: 2-Hydroxy-3-methoxybenzyl alcohol


enzyme_display_name: GDP-mannose 4,6-dehydratase

organism: Pseudomonas aeruginosa

substrate_name: GDP-mannose

enzyme: GDP-mannose 4,6-dehydratase

substrate: GDP-mannose


proof_lines:
pH 7.5, 37°C
Raw SKiD Env: Temp=37°C, pH=7.5


substrate_name: GDP-alpha-D-mannose

sequence_source: multiple

source_databases_merged: brenda uniprot

substrate: GDP-alpha-D-mannose


organism: Phaseolus vulgaris


substrate_name: GDPmannose

substrate: GDPmannose


organism: Sus scrofa


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


organism: Burkholderia cenocepacia J2315


sequence_source: UniProtKB O60547; reviewed GMDS_HUMAN; PMID 9525924 citation; REST check 2026-06-02


organism: Mortierella alpina

proof_lines:
pH 8.0, 37°C
recombinant enzyme, pH 8.0, 37°C


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

proof_lines: mutant S156A, 37°C, pH not specified in the publication


proof_lines: wild-type, 37°C, pH not specified in the publication


organism: Burkholderia cepacia

proof_lines: at pH 7.4 and 25°C, in the presence of 1 mol MgCl2 per mol of protein


proof_lines:
pH 8, M-GMD and L-GMD
pH 8, isoenzyme M-GMD
pH 8, isoenzyme L-GMD

source_databases_merged: brenda skid uniprot


substrate_name: GDP-D-mannose

proof_lines: Table 1 reports BceN from B. cenocepacia J2315 using GDP-D-mannose as substrate.

substrate: GDP-D-mannose


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


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


substrate_name: Unknown

substrate: Unknown


organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

substrate_name: UDP-N-acetylbacillosamine

substrate: UDP-N-acetylbacillosamine


organism: Bacillus subtilis (strain 168)


organism: Acinetobacter baumannii

source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Bacillus subtilis

substrate_name: Acetyl-CoA; UDP-N-acetylbacillosamine

sequence_source: UniProtKB P71063 direct lookup; accession reuse cache canonical sequence from source_record

assay_conditions_summary: cofactor CoA

substrate: Acetyl-CoA; UDP-N-acetylbacillosamine


organism: Neisseria gonorrhoeae

sequence_source: UniProtKB Q5FAE1 direct lookup plus validated Q370A substitution reconstruction

sequence_variant_note: Mutation signature Q370A matches the mutant residue at offset +0 and the reference residue at offset -1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB Q5FAE1 direct lookup plus validated Q369A substitution reconstruction

sequence_variant_note: Mutation signature Q369A matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB Q5FAE1 direct lookup plus validated H210F substitution reconstruction


sequence_source: UniProtKB Q5FAE1 direct lookup plus validated D332A substitution reconstruction


sequence_source: UniProtKB Q5FAE1 direct lookup; RCSB 4M98/4M99 SIFTS accession support


sequence_source: UniProtKB reviewed accession Q0P9D1 (PGLD_CAMJE)


enzyme_display_name: ureidoglycolate amidohydrolase

organism: Arabidopsis thaliana

substrate_name: (S)-ureidoglycolate

sequence_source: source_record; UniProt REST direct check Q8VXY9

proof_lines: kcat is 1.43 sec(-1) with (S)-ureidoglycolate as substrate (at pH 8.5 and 30 degrees Celsius) (PubMed:25020232). kcat is 7.9 sec(-1) for (S)-ureidoglycolate (PubMed:19935661).

enzyme: ureidoglycolate amidohydrolase

substrate: (S)-ureidoglycolate


organism: Glycine max

substrate_name: H2O; (-)-Ureidoglycolate

substrate: H2O; (-)-Ureidoglycolate


organism: Oryza sativa


substrate_name: ureidoglycolate

proof_lines:
in presence of Mn2+
in absence of Mn2+

substrate: ureidoglycolate


organism: Oryza sativa subsp. japonica

sequence_source: source_record; UniProt REST accession Q2QMN7 cross-check


sequence_source: UniProt Q8VXY9 canonical sequence; direct UniProt REST check on 2026-06-02 plus RCSB 4PXB/4PXC/4PXE accession anchors from PMID 25020232.


sequence_source: Reconstructed from UniProt Q8VXY9 canonical sequence by applying Y423F; residue check performed on 2026-06-02; RCSB 4PXB/4PXC/4PXE support Q8VXY9 identity from PMID 25020232.


proof_lines:
wild-type enzyme, pH 8.5, 30°C
pH 7.4, 30°C, wild-type enzyme


sequence_source: Reconstructed from UniProt Q8VXY9 canonical sequence by applying H424N; residue check performed on 2026-06-02; RCSB 4PXB/4PXC/4PXE support Q8VXY9 identity from PMID 25020232.

sequence_variant_note: Mutation signature H424N matches the mutant residue at offset +0 and the reference residue at offset -9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: Reconstructed from UniProt Q8VXY9 canonical sequence by applying Q257N; residue check performed on 2026-06-02; RCSB 4PXB/4PXC/4PXE support Q8VXY9 identity from PMID 25020232.


sequence_source: UniProtKB Q8VXY9 direct REST lookup on 2026-06-02; variant reconstructed from the checked Q8VXY9 canonical sequence


sequence_source: UniProtKB Q8VXY9 direct REST lookup on 2026-06-02; canonical sequence matches local accession cache

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8.5
Raw SKiD Env: Temp=30°C, pH=7.4


substrate_name: (-)-Ureidoglycolate; H2O

sequence_source: UniProtKB Q2QMN7 direct REST lookup on 2026-06-02; canonical sequence matches local accession cache

substrate: (-)-Ureidoglycolate; H2O


substrate_name: (-)-Ureidoglycolate

substrate: (-)-Ureidoglycolate


enzyme_display_name: palmitoyl-CoA hydrolase

organism: Homo sapiens

substrate_name: myristoyl-CoA

sequence_source: UniProtKB reviewed accession Q8N1Q8 direct lookup

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

column_label: Figure 2F (PDF page 5 of 13, journal page 2689), decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C14:0`: Km (uM) = 8.6; kcat (s^-1) = 19.7; kcat/Km (M^-1 s^-1) = 2.3x10^6.

normalized_value_unit_evidence: kcat: printed cell 19.7 s^-1 -> 19.7 s^(-1) (already per second, carried unchanged); the exported value is 19.7 s^(-1). Km: printed cell 8.6 uM -> 0.0086 mM (divide by 1000); the exported value is 0.009 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.3x10^6 M^-1 s^-1 for this substrate line -> 2300.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 2188.888888888889 s^(-1)*mM^(-1).

row_label: Figure 2F, decoded plain-numeral transcription, enzyme block `hThem5 WT`, substrate row `C14:0`

table_label: Figure 2F (PDF page 5 of 13, journal page 2689) 'Steady-state kinetic constants for hThem5 catalyzed hydrolysis of selected Acyl-CoA esters'

enzyme: palmitoyl-CoA hydrolase

substrate: myristoyl-CoA


substrate_name: Arachidonyl-CoA

substrate: Arachidonyl-CoA


substrate_name: H2O; Myristoyl-CoA

sequence_source: UniProtKB reviewed accession Q5T1C6 direct lookup plus selected-source N183A mutation reconstruction

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant N183A His6-tagged

substrate: H2O; Myristoyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5T1C6 and applied mutation signature K207A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

column_label: Table 1: Steady-state kinetic constants of wild-type and mutant hHTEM4-catalyzed hydrolysis of myristoyl-CoA at pH 7.5 and 25 C (Biochemistry 2012, 51(33):6490-6492, NIH Public Access author manuscript page 9), printed column heads hTHEM4 | kcat (s-1) | Km (uM) | kcat/Km (M-1 s-1). hTHEM4 row 'K207A': column 'kcat (s-1)' = 1.5 ± 0.1; column 'Km (uM)' = 2.8 ± 0.1; column 'kcat/Km (M-1 s-1)' = 6.7 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.5 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 1.5 s^(-1); the exported value is 1.5 s^(-1). Km: printed Table 1 cell 2.8 uM; 1 uM is 0.001 mM, so 2.8 / 1000 = 0.0028 mM; the paper value is 0.0028 mM; the exported value is 0.003 mM. kcat/Km: printed Table 1 cell 6.7 x 10^5 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 6.7 x 10^5 / 1000 = 670 s^-1 mM^-1; the paper value is 670 s^(-1)*mM^(-1); the exported value is 500 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, hTHEM4 row 'K207A', myristoyl-CoA hydrolysis: kcat = 1.5 s-1; Km = 2.8 uM; printed kcat/Km = 6.7 x 10^5 M-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5T1C6 and applied mutation signature R206A to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-state kinetic constants of wild-type and mutant hHTEM4-catalyzed hydrolysis of myristoyl-CoA at pH 7.5 and 25 C (Biochemistry 2012, 51(33):6490-6492, NIH Public Access author manuscript page 9), printed column heads hTHEM4 | kcat (s-1) | Km (uM) | kcat/Km (M-1 s-1). hTHEM4 row 'R206A': column 'kcat (s-1)' = 1.5 ± 0.1; column 'Km (uM)' = 4.4 ± 0.6; column 'kcat/Km (M-1 s-1)' = 3.6 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.5 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 1.5 s^(-1); the exported value is 1.5 s^(-1). Km: printed Table 1 cell 4.4 uM; 1 uM is 0.001 mM, so 4.4 / 1000 = 0.0044 mM; the paper value is 0.0044 mM; the exported value is 0.004 mM. kcat/Km: printed Table 1 cell 3.6 x 10^5 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 3.6 x 10^5 / 1000 = 360 s^-1 mM^-1; the paper value is 360 s^(-1)*mM^(-1); the exported value is 375 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, hTHEM4 row 'R206A', myristoyl-CoA hydrolysis: kcat = 1.5 s-1; Km = 4.4 uM; printed kcat/Km = 3.6 x 10^5 M-1 s-1.


substrate_name: Myristoyl-CoA; H2O

sequence_source: UniProtKB reviewed accession Q5T1C6 direct lookup plus selected-source D161E mutation reconstruction

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant D161E His6-tagged

substrate: Myristoyl-CoA; H2O


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5T1C6 and applied mutation signature H152A to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-state kinetic constants of wild-type and mutant hHTEM4-catalyzed hydrolysis of myristoyl-CoA at pH 7.5 and 25 C (Biochemistry 2012, 51(33):6490-6492, NIH Public Access author manuscript page 9), printed column heads hTHEM4 | kcat (s-1) | Km (uM) | kcat/Km (M-1 s-1). hTHEM4 row 'H152A': column 'kcat (s-1)' = 0.04 ± 0.01; column 'Km (uM)' = 62 ± 4; column 'kcat/Km (M-1 s-1)' = 6.7 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.04 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.04 s^(-1); the exported value is 0.04 s^(-1). Km: printed Table 1 cell 62 uM; 1 uM is 0.001 mM, so 62 / 1000 = 0.062 mM; the paper value is 0.062 mM; the exported value is 0.062 mM. kcat/Km: printed Table 1 cell 6.7 x 10^2 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 6.7 x 10^2 / 1000 = 0.67 s^-1 mM^-1; the paper value is 0.67 s^(-1)*mM^(-1); the exported value is 0.645161290323 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, hTHEM4 row 'H152A', myristoyl-CoA hydrolysis: kcat = 0.04 s-1; Km = 62 uM; printed kcat/Km = 6.7 x 10^2 M-1 s-1.


organism: Escherichia coli

substrate_name: lauroyl-CoA

substrate: lauroyl-CoA


substrate_name: Octanoyl-CoA; H2O

sequence_source: UniProtKB reviewed direct lookup: O00154, Homo sapiens, cytosolic acyl coenzyme A thioester hydrolase, EC 3.1.2.2.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA

substrate: Octanoyl-CoA; H2O


substrate_name: H2O; Choloyl-CoA

substrate: H2O; Choloyl-CoA


substrate_name: Decanoyl-CoA; H2O

sequence_source: UniProtKB reviewed direct lookup: Q86TX2, Homo sapiens, acyl-coenzyme A thioesterase 1, EC 3.1.2.-.

substrate: Decanoyl-CoA; H2O


sequence_source: UniProtKB reviewed direct lookup: P49753, Homo sapiens, acyl-coenzyme A thioesterase 2 mitochondrial, EC 3.1.2.2.


substrate_name: H2O; Succinyl-CoA

substrate: H2O; Succinyl-CoA


mutation_type: deletion

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant delta99 N-terminal His6-MBP-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB P0ADA1 reviewed sequence plus PMID 16515533 mutagenesis mapping mature G44A to precursor G70A. and applied mutation signature G44A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.


substrate_name: p-Nitrophenyl butyrate

sequence_variant_note: Resolved canonical sequence from UniProtKB P0ADA1 reviewed sequence plus PMID 16515533 mutagenesis mapping mature N73A to precursor N99A. and applied mutation signature N73A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.

substrate: p-Nitrophenyl butyrate


substrate_name: H2O; p-Nitrophenyl butyrate

sequence_source: UniProtKB P0ADA1 reviewed sequence plus PMID 16515533 mutagenesis mapping mature G44A to precursor G70A.

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant G44A

substrate: H2O; p-Nitrophenyl butyrate


sequence_variant_note: Resolved canonical sequence from UniProtKB P0ADA1 reviewed sequence plus PMID 16515533 mutagenesis mapping mature D154A to precursor D180A. and applied mutation signature D154A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant D154A


substrate_name: Lauroyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB P0ADA1 reviewed sequence plus PMID 16515533 mutagenesis mapping mature S10A to precursor S36A. and applied mutation signature S10A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.

substrate: Lauroyl-CoA


sequence_source: UniProtKB P0ADA1 reviewed sequence plus PMID 16515533 mutagenesis mapping mature D154A to precursor D180A.


sequence_source: UniProtKB P0ADA1 reviewed sequence plus PMID 16515533 mutagenesis mapping mature N73A to precursor N99A.


substrate_name: p-Nitrophenyl butyrate; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB P0ADA1 reviewed sequence plus PMID 16515533 mutagenesis mapping mature H157A to precursor H183A. and applied mutation signature H157A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant H157A

substrate: p-Nitrophenyl butyrate; H2O


substrate_name: Lauroyl-CoA; H2O

sequence_source: UniProtKB:F4HU51 reviewed canonical sequence; selected Q8GYW7 resolves as a secondary accession on that live entry.

substrate: Lauroyl-CoA; H2O


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0ADA1 and applied mutation signature S10A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; buffer 0.1 M sodium phosphate

column_label: Table 2 (Kinetic analysis of wild-type and mutants of TAP), substrate stub 'L-NBTNPE', parameter stub rows 'k cat (s-1)', 'K m (mM)' and 'k cat /K m', enzyme-form column head 'S10A': k cat 0.02, K m 0.061, k cat /K m 0.32.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.02 s-1; the value is already in s^-1, so no unit conversion applies, giving 0.02 s^(-1). Km: printed Table 2 cell 0.061 mM; the value is already in mM, so no unit conversion applies, giving 0.061 mM. kcat/Km: the Table 2 k cat /K m stub prints 0.32 in this column; the table's own kcat column unit s^-1 and Km column unit mM make that printed cell 0.32 s^(-1)*mM^(-1), so no unit conversion applies.

raw_value_unit_evidence: Table 2, substrate stub 'L-NBTNPE', enzyme-form column head 'S10A': k cat = 0.02 s-1; K m = 0.061 mM; printed k cat /K m = 0.32.

table_label: Table 2: Kinetic analysis of wild-type and mutants of TAP (Biochem. J. 2006, 397, 69-76)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0ADA1 and applied mutation signature G44A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic analysis of wild-type and mutants of TAP), substrate stub 'NPB', parameter stub rows 'k cat (s-1)', 'K m (mM)' and 'k cat /K m', enzyme-form column head 'G44A': k cat 3.16, K m 1.10, k cat /K m 2.87.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.16 s-1; the value is already in s^-1, so no unit conversion applies, giving 3.16 s^(-1). Km: printed Table 2 cell 1.10 mM; the value is already in mM, so no unit conversion applies, giving 1.1 mM. kcat/Km: the Table 2 k cat /K m stub prints 2.87 in this column; the table's own kcat column unit s^-1 and Km column unit mM make that printed cell 2.87 s^(-1)*mM^(-1), so no unit conversion applies.

raw_value_unit_evidence: Table 2, substrate stub 'NPB', enzyme-form column head 'G44A': k cat = 3.16 s-1; K m = 1.10 mM; printed k cat /K m = 2.87.


sequence_source: UniProtKB:P0ADA1 reviewed canonical precursor sequence.

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

column_label: Table 2 (Kinetic analysis of wild-type and mutants of TAP), substrate stub 'L-NBTNPE', parameter stub rows 'k cat (s-1)', 'K m (mM)' and 'k cat /K m', enzyme-form column head 'Wild-type': k cat 88.99, K m 0.174, k cat /K m 512.40.

normalized_value_unit_evidence: kcat: printed Table 2 cell 88.99 s-1; the value is already in s^-1, so no unit conversion applies, giving 88.99 s^(-1). Km: printed Table 2 cell 0.174 mM; the value is already in mM, so no unit conversion applies, giving 0.174 mM. kcat/Km: the Table 2 k cat /K m stub prints 512.40 in this column; the table's own kcat column unit s^-1 and Km column unit mM make that printed cell 512.4 s^(-1)*mM^(-1), so no unit conversion applies.

raw_value_unit_evidence: Table 2, substrate stub 'L-NBTNPE', enzyme-form column head 'Wild-type': k cat = 88.99 s-1; K m = 0.174 mM; printed k cat /K m = 512.40.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ADA1 reviewed canonical precursor sequence with N73A applied at full precursor residue 99 after UniProt signal peptide residues 1-26. and applied mutation signature N73A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant N73A


sequence_source: UniProtKB:P0ADA1 reviewed canonical precursor sequence with S10A applied at full precursor residue 36 after UniProt signal peptide residues 1-26.

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +26, so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant S10A


column_label: Table 2 (Kinetic analysis of wild-type and mutants of TAP), substrate stub 'NPB', parameter stub rows 'k cat (s-1)', 'K m (mM)' and 'k cat /K m', enzyme-form column head 'Wild-type': k cat 15.29, K m 0.87, k cat /K m 17.75.

normalized_value_unit_evidence: kcat: printed Table 2 cell 15.29 s-1; the value is already in s^-1, so no unit conversion applies, giving 15.29 s^(-1). Km: printed Table 2 cell 0.87 mM; the value is already in mM, so no unit conversion applies, giving 0.87 mM. kcat/Km: the Table 2 k cat /K m stub prints 17.75 in this column; the table's own kcat column unit s^-1 and Km column unit mM make that printed cell 17.75 s^(-1)*mM^(-1), so no unit conversion applies.

raw_value_unit_evidence: Table 2, substrate stub 'NPB', enzyme-form column head 'Wild-type': k cat = 15.29 s-1; K m = 0.87 mM; printed k cat /K m = 17.75.


proof_lines:
native enzyme
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=37°C, pH=7


enzyme_display_name: Thioesterase 1/protease 1/lysophospholipase L1

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ADA1 direct accession lookup and applied mutation signature G44A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ADA1 direct accession lookup and applied mutation signature S10A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.

enzyme: Thioesterase 1/protease 1/lysophospholipase L1


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ADA1 direct accession lookup and applied mutation signature N73A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ADA1 direct accession lookup and applied mutation signature D154A with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0ADA1 direct accession lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ADA1 direct accession lookup and applied mutation signature P110A/L109P with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.


organism: Rattus norvegicus

substrate_name: H2O; Palmitoyl-CoA

sequence_source: UniProtKB Q64559 canonical FASTA

proof_lines:
the induced E. coli enzyme
brain ACT
recombinant enzyme

substrate: H2O; Palmitoyl-CoA


sequence_source: UniProt Q5T1C6 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProt Q5T1C6 canonical sequence; H152F reconstructed after direct residue check and applied mutation signature H152F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q5T1C6 canonical sequence; T177A reconstructed after direct residue check and applied mutation signature T177A to reconstruct the assayed variant sequence.


sequence_source: UniProt Q5T1C6 canonical sequence; T177A reconstructed after direct residue check

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant T177A His6-tagged


sequence_variant_note: Resolved canonical sequence from UniProt Q5T1C6 canonical sequence; D161N reconstructed after direct residue check and applied mutation signature D161N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant D161N His6-tagged


sequence_source: UniProt Q5T1C6 canonical sequence; H152F reconstructed after direct residue check

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant H152F His6-tagged


sequence_source: UniProt Q5T1C6 canonical sequence; D161N reconstructed after direct residue check


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q5T1C6 (THEM4_HUMAN); canonical residue K207 matched and was substituted to A. and applied mutation signature K207A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant K207A His6-tagged


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5T1C6 and applied mutation signature D161E to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-state kinetic constants of wild-type and mutant hHTEM4-catalyzed hydrolysis of myristoyl-CoA at pH 7.5 and 25 C (Biochemistry 2012, 51(33):6490-6492, NIH Public Access author manuscript page 9), printed column heads hTHEM4 | kcat (s-1) | Km (uM) | kcat/Km (M-1 s-1). hTHEM4 row 'D161E': column 'kcat (s-1)' = 0.1 ± 0.01; column 'Km (uM)' = 45 ± 3; column 'kcat/Km (M-1 s-1)' = 2.3 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.1 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.1 s^(-1); the exported value is 0.1 s^(-1). Km: printed Table 1 cell 45 uM; 1 uM is 0.001 mM, so 45 / 1000 = 0.045 mM; the paper value is 0.045 mM; the exported value is 0.045 mM. kcat/Km: printed Table 1 cell 2.3 x 10^3 M-1 s-1; 1 M-1 s-1 is 0.001 s^-1 mM^-1, so 2.3 x 10^3 / 1000 = 2.3 s^-1 mM^-1; the paper value is 2.3 s^(-1)*mM^(-1); the exported value is 2.22222222222 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, hTHEM4 row 'D161E', myristoyl-CoA hydrolysis: kcat = 0.1 s-1; Km = 45 uM; printed kcat/Km = 2.3 x 10^3 M-1 s-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q5T1C6 (THEM4_HUMAN); canonical residue R206 matched and was substituted to A. and applied mutation signature R206A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant R206A His6-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q5T1C6 (THEM4_HUMAN); canonical residue H152 matched and was substituted to A. and applied mutation signature H152A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant H152A His6-tagged


sequence_source: UniProtKB reviewed accession O14734 (ACOT8_HUMAN) canonical sequence.


organism: Mus musculus

substrate_name: palmitoleoyl-CoA

sequence_source: UniProtKB reviewed accession P58137 (ACOT8_MOUSE) canonical sequence.

assay_conditions_summary: pH 7.4; cofactor CoA

substrate: palmitoleoyl-CoA


substrate_name: Palmitoyl-CoA; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O55137 (ACOT1_MOUSE); canonical residue S232 matched and was substituted to A. and applied mutation signature S232A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant S232A His-tagged

substrate: Palmitoyl-CoA; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O55137 (ACOT1_MOUSE); canonical residue D324 matched and was substituted to A. and applied mutation signature D324A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: palmitoyl-CoA hydrolase(Enzyme) mutant D324A His-tagged


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


organism: Bos taurus

substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


substrate_name: S-palmitoyl H-Ras

substrate: S-palmitoyl H-Ras


substrate_name: S-palmitoyl-CoA

substrate: S-palmitoyl-CoA


substrate_name: succinyl-CoA

substrate: succinyl-CoA


sequence_source: UniProtKB O55137 live lookup; source SABIO-RK records cite O55137 for Mus musculus PMID 11694534.