sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8KSC8 and applied mutation signature F171Q to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), RdpA block measured with (R)-mecoprop, variant row 'F171Q'; column 'Range (uM)' = 62.5-4000; column 'Km (uM)' = 438 +/- 34; column 'kcat (min^-1)' = 203 +/- 4; column 'kcat/Km (min^-1*uM^-1)' = 0.46.

normalized_value_unit_evidence: Km: printed Table 2 cell 438 under the column head Km (uM); one uM is 0.001 mM, so 438 / 1000 = 0.438 mM; the exported value is 0.438 mM. kcat: printed Table 2 cell 203 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 203 / 60 = 3.3833333333333333 s^-1; the exported value is 3.38 s^(-1). kcat/Km: printed Table 2 cell 0.46 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.46 * 1000 / 60 = 7.666666666666668 s^-1 mM^-1; the exported value is 7.716894977168949 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, RdpA block, (R)-mecoprop columns, variant row F171Q: Km = 438 uM (printed with its tolerance +/- 34); kcat = 203 min^-1 (printed with its tolerance +/- 4); kcat/Km = 0.46 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


organism: Sphingobium herbicidovorans

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8KSC8 and applied mutation signature I106A to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 6.8; 303.15 K; buffer 100 mM imidazole

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), RdpA block measured with (R)-mecoprop, variant row 'I106A'; column 'Range (uM)' = 500-4000; column 'Km (uM)' = 8900 +/- 2100; column 'kcat (min^-1)' = 238 +/- 42; column 'kcat/Km (min^-1*uM^-1)' = 0.03.

normalized_value_unit_evidence: Km: printed Table 2 cell 8900 under the column head Km (uM); one uM is 0.001 mM, so 8900 / 1000 = 8.9 mM; the exported value is 8.9 mM. kcat: printed Table 2 cell 238 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 238 / 60 = 3.966666666666667 s^-1; the exported value is 4.0 s^(-1). kcat/Km: printed Table 2 cell 0.03 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.03 * 1000 / 60 = 0.5 s^-1 mM^-1; the exported value is 0.449438202247191 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, RdpA block, (R)-mecoprop columns, variant row I106A: Km = 8900 uM (printed with its tolerance +/- 2100); kcat = 238 min^-1 (printed with its tolerance +/- 42); kcat/Km = 0.03 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).

table_label: Table 2: Kinetic parameters of selected variant forms of RdpA and SdpA (Protein Science 2006, 15(6):1356-1368)

data_origin: experimental

status: corrected

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8KSC8 and applied mutation signature Q93A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), RdpA block measured with (R)-mecoprop, variant row 'Q93A'; column 'Range (uM)' = 200-4000; column 'Km (uM)' = 2800 +/- 400; column 'kcat (min^-1)' = 260 +/- 21; column 'kcat/Km (min^-1*uM^-1)' = 0.09.

normalized_value_unit_evidence: Km: printed Table 2 cell 2800 under the column head Km (uM); one uM is 0.001 mM, so 2800 / 1000 = 2.8000000000000003 mM; the exported value is 2.8 mM. kcat: printed Table 2 cell 260 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 260 / 60 = 4.333333333333333 s^-1; the exported value is 4.33 s^(-1). kcat/Km: printed Table 2 cell 0.09 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.09 * 1000 / 60 = 1.5 s^-1 mM^-1; the exported value is 1.5464285714285715 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, RdpA block, (R)-mecoprop columns, variant row Q93A: Km = 2800 uM (printed with its tolerance +/- 400); kcat = 260 min^-1 (printed with its tolerance +/- 21); kcat/Km = 0.09 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8KSC8 and applied mutation signature R285A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), RdpA block measured with (R)-mecoprop, variant row 'R285A'; column 'Range (uM)' = 200-4000; column 'Km (uM)' = 1550 +/- 220; column 'kcat (min^-1)' = 52 +/- 4; column 'kcat/Km (min^-1*uM^-1)' = 0.03.

normalized_value_unit_evidence: Km: printed Table 2 cell 1550 under the column head Km (uM); one uM is 0.001 mM, so 1550 / 1000 = 1.55 mM; the exported value is 1.55 mM. kcat: printed Table 2 cell 52 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 52 / 60 = 0.8666666666666667 s^-1; the exported value is 0.87 s^(-1). kcat/Km: printed Table 2 cell 0.03 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.03 * 1000 / 60 = 0.5 s^-1 mM^-1; the exported value is 0.5612903225806452 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, RdpA block, (R)-mecoprop columns, variant row R285A: Km = 1550 uM (printed with its tolerance +/- 220); kcat = 52 min^-1 (printed with its tolerance +/- 4); kcat/Km = 0.03 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8KSC8 and applied mutation signature V80A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), RdpA block measured with (R)-mecoprop, variant row 'V80A'; column 'Range (uM)' = 200-4000; column 'Km (uM)' = 2300 +/- 1100; column 'kcat (min^-1)' = 248 +/- 56; column 'kcat/Km (min^-1*uM^-1)' = 0.11.

normalized_value_unit_evidence: Km: printed Table 2 cell 2300 under the column head Km (uM); one uM is 0.001 mM, so 2300 / 1000 = 2.3000000000000003 mM; the exported value is 2.3 mM. kcat: printed Table 2 cell 248 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 248 / 60 = 4.133333333333333 s^-1; the exported value is 4.13 s^(-1). kcat/Km: printed Table 2 cell 0.11 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.11 * 1000 / 60 = 1.8333333333333335 s^-1 mM^-1; the exported value is 1.7956521739130435 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, RdpA block, (R)-mecoprop columns, variant row V80A: Km = 2300 uM (printed with its tolerance +/- 1100); kcat = 248 min^-1 (printed with its tolerance +/- 56); kcat/Km = 0.11 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


mutation_signature: Unknown

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

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), RdpA block measured with (R)-mecoprop, Wild type row; column 'Range (uM)' = 100-4000; column 'Km (uM)' = 380 +/- 28; column 'kcat (min^-1)' = 252 +/- 5; column 'kcat/Km (min^-1*uM^-1)' = 0.66.

normalized_value_unit_evidence: Km: printed Table 2 cell 380 under the column head Km (uM); one uM is 0.001 mM, so 380 / 1000 = 0.38 mM; the exported value is 0.38 mM. kcat: printed Table 2 cell 252 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 252 / 60 = 4.2 s^-1; the exported value is 4.2 s^(-1). kcat/Km: printed Table 2 cell 0.66 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.66 * 1000 / 60 = 11.000000000000002 s^-1 mM^-1; the exported value is 11.052631578947368 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, RdpA block, (R)-mecoprop columns, Wild type row: Km = 380 uM (printed with its tolerance +/- 28); kcat = 252 min^-1 (printed with its tolerance +/- 5); kcat/Km = 0.66 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q700X4 and applied mutation signature E69A to reconstruct the assayed variant sequence.

column_label: PMCID PMC2242530 Table 2 image 1356tbl2.jpg; row SdpA E69A; columns Km, kcat, and kcat/Km for the matching mecoprop enantiomer.

raw_value_unit_evidence: Table 2 SdpA E69A with (S)-mecoprop: Km 91 +/- 14 uM, kcat 241 +/- 8 min^-1, kcat/Km 2.65 min^-1 uM^-1.

row_label: SdpA E69A with (S)-2-(4-chloro-2-methylphenoxy)propanoate

table_label: Table 2. Kinetic parameters of selected variant forms of RdpA and SdpA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q700X4 and applied mutation signature G97I/N98G to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), SdpA block measured with (S)-mecoprop, variant row 'G97I/N98G'; column 'Range (uM)' = 250-4000; column 'Km (uM)' = 1100 +/- 270; column 'kcat (min^-1)' = 42 +/- 4.4; column 'kcat/Km (min^-1*uM^-1)' = 0.04.

normalized_value_unit_evidence: Km: printed Table 2 cell 1100 under the column head Km (uM); one uM is 0.001 mM, so 1100 / 1000 = 1.1 mM; the exported value is 1.1 mM. kcat: printed Table 2 cell 42 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 42 / 60 = 0.7 s^-1; the exported value is 0.7 s^(-1). kcat/Km: printed Table 2 cell 0.04 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.04 * 1000 / 60 = 0.6666666666666667 s^-1 mM^-1; the exported value is 0.6363636363636362 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, SdpA block, (S)-mecoprop columns, variant row G97I/N98G: Km = 1100 uM (printed with its tolerance +/- 270); kcat = 42 min^-1 (printed with its tolerance +/- 4.4); kcat/Km = 0.04 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q700X4 and applied mutation signature H208A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), SdpA block measured with (S)-mecoprop, variant row 'H208A'; column 'Range (uM)' = 500-4000; column 'Km (uM)' = 2900 +/- 960; column 'kcat (min^-1)' = 21 +/- 4; column 'kcat/Km (min^-1*uM^-1)' = 0.007.

normalized_value_unit_evidence: Km: printed Table 2 cell 2900 under the column head Km (uM); one uM is 0.001 mM, so 2900 / 1000 = 2.9 mM; the exported value is 2.9 mM. kcat: printed Table 2 cell 21 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 21 / 60 = 0.35 s^-1; the exported value is 0.35 s^(-1). kcat/Km: printed Table 2 cell 0.007 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.007 * 1000 / 60 = 0.11666666666666668 s^-1 mM^-1; the exported value is 0.12068965517241378 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, SdpA block, (S)-mecoprop columns, variant row H208A: Km = 2900 uM (printed with its tolerance +/- 960); kcat = 21 min^-1 (printed with its tolerance +/- 4); kcat/Km = 0.007 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q700X4 and applied mutation signature R207A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), SdpA block measured with (S)-mecoprop, variant row 'R207A'; column 'Range (uM)' = 250-4000; column 'Km (uM)' = 2500 +/- 400; column 'kcat (min^-1)' = 238 +/- 20; column 'kcat/Km (min^-1*uM^-1)' = 0.1.

normalized_value_unit_evidence: Km: printed Table 2 cell 2500 under the column head Km (uM); one uM is 0.001 mM, so 2500 / 1000 = 2.5 mM; the exported value is 2.5 mM. kcat: printed Table 2 cell 238 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 238 / 60 = 3.966666666666667 s^-1; the exported value is 3.97 s^(-1). kcat/Km: printed Table 2 cell 0.1 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 0.1 * 1000 / 60 = 1.666666666666667 s^-1 mM^-1; the exported value is 1.588 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, SdpA block, (S)-mecoprop columns, variant row R207A: Km = 2500 uM (printed with its tolerance +/- 400); kcat = 238 min^-1 (printed with its tolerance +/- 20); kcat/Km = 0.1 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


column_label: Table 2 (Kinetic parameters of selected variant forms of RdpA and SdpA), SdpA block measured with (S)-mecoprop, Wild type row; column 'Range (uM)' = 31-4000; column 'Km (uM)' = 161 +/- 20; column 'kcat (min^-1)' = 1010 +/- 44; column 'kcat/Km (min^-1*uM^-1)' = 6.24.

normalized_value_unit_evidence: Km: printed Table 2 cell 161 under the column head Km (uM); one uM is 0.001 mM, so 161 / 1000 = 0.161 mM; the exported value is 0.161 mM. kcat: printed Table 2 cell 1010 under the column head kcat (min^-1); one min^-1 is 1/60 s^-1, so 1010 / 60 = 16.833333333333332 s^-1; the exported value is 16.83 s^(-1). kcat/Km: printed Table 2 cell 6.24 under the column head kcat/Km (min^-1*uM^-1); one min^-1*uM^-1 is 1000/60 s^-1 mM^-1, so 6.24 * 1000 / 60 = 104.00000000000001 s^-1 mM^-1; the exported value is 104.53416149068322 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, SdpA block, (S)-mecoprop columns, Wild type row: Km = 161 uM (printed with its tolerance +/- 20); kcat = 1010 min^-1 (printed with its tolerance +/- 44); kcat/Km = 6.24 min^-1*uM^-1. The printed column heads are Range (uM), Km (uM), kcat (min^-1) and kcat/Km (min^-1*uM^-1).


enzyme_display_name: xanthine dioxygenase

organism: Aspergillus nidulans

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C357A to reconstruct the assayed variant sequence.

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

assay_conditions_summary: pH 7.4; 298.15 K; buffer 50 mM MOPS

column_label: Table 2; XanA sample row C357A; substrate column group 2-Oxoglutarate; checked metric(s): kcat, kcat_over_km, km; Assays at 25 C in 50 mM MOPS buffer, pH 7.4, with 40 uM FeII; except for the analyzed compound, solutions contained 1 mM alphaKG and 200 uM xanthine. Xanthine varied 0-250 uM except N358A 0-400 uM; alphaKG varied 0-500 uM; 9-methylxanthine varied 0-1.0 mM.

table_label: Table 2

enzyme: xanthine dioxygenase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D138A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row D138A; substrate column group 2-Oxoglutarate; checked metric(s): kcat, kcat_over_km, km; Assays at 25 C in 50 mM MOPS buffer, pH 7.4, with 40 uM FeII; except for the analyzed compound, solutions contained 1 mM alphaKG and 200 uM xanthine. Xanthine varied 0-250 uM except N358A 0-400 uM; alphaKG varied 0-500 uM; 9-methylxanthine varied 0-1.0 mM.


sequence_variant_note: Resolved canonical sequence from uniprotkb:C8VSZ2 and applied mutation signature C357A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row C357A; substrate column group 9-methylxanthine; columns Km, kcat, kcat/Km; required metrics checked: kcat, kcat_over_km, km.

table_label: Table 2: Substrate, cosubstrate, and substrate analog kinetic parameters of XanA and selected variants


sequence_variant_note: Resolved canonical sequence from uniprotkb:C8VSZ2 and applied mutation signature D138A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row D138A; substrate column group 9-methylxanthine; columns Km, kcat, kcat/Km; required metrics checked: kcat, kcat_over_km, km.


sequence_variant_note: Resolved canonical sequence from uniprotkb:C8VSZ2 and applied mutation signature E137A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row E137A; substrate column group 9-methylxanthine; columns Km, kcat, kcat/Km; required metrics checked: kcat, kcat_over_km, km.


sequence_variant_note: Resolved canonical sequence from uniprotkb:C8VSZ2 and applied mutation signature K122A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row K122A; substrate column group 9-methylxanthine; columns Km, kcat, kcat/Km; required metrics checked: kcat, kcat_over_km, km.


verification_status: unverified

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N358A to reconstruct the assayed variant sequence.

status: unverified


sequence_variant_note: Resolved canonical sequence from uniprotkb:C8VSZ2 and applied mutation signature Q101A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row Q101A; substrate column group 9-methylxanthine; columns Km, kcat, kcat/Km; required metrics checked: kcat, kcat_over_km, km.


sequence_variant_note: Resolved canonical sequence from uniprotkb:C8VSZ2 and applied mutation signature Q356A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row Q356A; substrate column group 9-methylxanthine; columns Km, kcat, kcat/Km; required metrics checked: kcat, kcat_over_km, km.


column_label: Table 2; XanA sample row WT; substrate column group 9-methylxanthine; checked metric(s): kcat, kcat_over_km, km; Assays at 25 C in 50 mM MOPS buffer, pH 7.4, with 40 uM FeII; except for the analyzed compound, solutions contained 1 mM alphaKG and 200 uM xanthine. Xanthine varied 0-250 uM except N358A 0-400 uM; alphaKG varied 0-500 uM; 9-methylxanthine varied 0-1.0 mM.

row_label: WT


source_db: brenda

kcat_display: Not reported

kcat_over_km_display: Not reported

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

sequence_source: multiple

column_label: PMID 16820480 Table 5, RdpA alpha-Ketoglutarate row, Km (uM) = 2.8 +/- 0.8.

normalized_value_unit_evidence: Km normalized_value=0.0028 mM; exported 0.003 mM is rounded from the printed cell.

raw_value_unit_evidence: Table 5 row RdpA / alpha-Ketoglutarate, Km column: 2.8 +/- 0.8 uM.

row_label: alpha-ketoglutarate-dependent (R)-dichlorprop dioxygenase / alpha-Ketoglutarate (7-1,900 uM)

table_label: Table 5. Kinetic parameters of alpha-ketoglutarate-dependent (R)-dichlorprop dioxygenase and alpha-ketoglutarate-dependent (S)-dichlorprop dioxygenase

source_databases_merged: brenda skid

source: brenda


proof_lines:
pH 6.8, 30°C
Raw SKiD Env: Temp=30°C, pH=6.8


column_label: PMID 16820480 Table 5, RdpA (R)-Dichlorprop row, Km (uM) = 163.7 +/- 13.5.

normalized_value_unit_evidence: Km normalized_value=0.1637 mM; exported 0.164 mM is rounded from the printed cell.

raw_value_unit_evidence: Table 5 row RdpA / (R)-Dichlorprop, Km column: 163.7 +/- 13.5 uM.

row_label: alpha-ketoglutarate-dependent (R)-dichlorprop dioxygenase / (R)-Dichlorprop (50-2,000 uM)


substrate_name: xanthine

column_label: Table 2; XanA sample row C357A; substrate column group xanthine; checked metric(s): kcat, kcat_over_km, km; Assays at 25 C in 50 mM MOPS buffer, pH 7.4, with 40 uM FeII; except for the analyzed compound, solutions contained 1 mM alphaKG and 200 uM xanthine. Xanthine varied 0-250 uM except N358A 0-400 uM; alphaKG varied 0-500 uM; 9-methylxanthine varied 0-1.0 mM.

substrate: xanthine


column_label: Table 2; XanA sample row D138A; substrate column group xanthine; checked metric(s): kcat, kcat_over_km, km; Assays at 25 C in 50 mM MOPS buffer, pH 7.4, with 40 uM FeII; except for the analyzed compound, solutions contained 1 mM alphaKG and 200 uM xanthine. Xanthine varied 0-250 uM except N358A 0-400 uM; alphaKG varied 0-500 uM; 9-methylxanthine varied 0-1.0 mM.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E137A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row E137A; substrate column group xanthine; checked metric(s): kcat, kcat_over_km, km; Assays at 25 C in 50 mM MOPS buffer, pH 7.4, with 40 uM FeII; except for the analyzed compound, solutions contained 1 mM alphaKG and 200 uM xanthine. Xanthine varied 0-250 uM except N358A 0-400 uM; alphaKG varied 0-500 uM; 9-methylxanthine varied 0-1.0 mM.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K122A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row K122A; substrate column group xanthine; checked metric(s): kcat, kcat_over_km, km; Assays at 25 C in 50 mM MOPS buffer, pH 7.4, with 40 uM FeII; except for the analyzed compound, solutions contained 1 mM alphaKG and 200 uM xanthine. Xanthine varied 0-250 uM except N358A 0-400 uM; alphaKG varied 0-500 uM; 9-methylxanthine varied 0-1.0 mM.


column_label: Table 2; XanA sample row N358A; substrate column group xanthine; checked metric(s): kcat, kcat_over_km, km; Assays at 25 C in 50 mM MOPS buffer, pH 7.4, with 40 uM FeII; except for the analyzed compound, solutions contained 1 mM alphaKG and 200 uM xanthine. Xanthine varied 0-250 uM except N358A 0-400 uM; alphaKG varied 0-500 uM; 9-methylxanthine varied 0-1.0 mM.


column_label: Table 2; XanA sample row Q101A; substrate column group xanthine; columns Km, kcat, kcat/Km; required metrics checked: kcat, kcat_over_km, km.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q356A to reconstruct the assayed variant sequence.

column_label: Table 2; XanA sample row Q356A; substrate column group xanthine; checked metric(s): kcat, kcat_over_km, km; Assays at 25 C in 50 mM MOPS buffer, pH 7.4, with 40 uM FeII; except for the analyzed compound, solutions contained 1 mM alphaKG and 200 uM xanthine. Xanthine varied 0-250 uM except N358A 0-400 uM; alphaKG varied 0-500 uM; 9-methylxanthine varied 0-1.0 mM.


verification_status: verified

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

column_label: Table 2; XanA sample row WT; substrate column group xanthine; checked metric(s): kcat, kcat_over_km, km; Assays at 25 C in 50 mM MOPS buffer, pH 7.4, with 40 uM FeII; except for the analyzed compound, solutions contained 1 mM alphaKG and 200 uM xanthine. Xanthine varied 0-250 uM except N358A 0-400 uM; alphaKG varied 0-500 uM; 9-methylxanthine varied 0-1.0 mM.

status: verified


column_label: Table 2; XanA sample row E137A; substrate column group 2-Oxoglutarate; checked metric(s): kcat, kcat_over_km, km; Assays at 25 C in 50 mM MOPS buffer, pH 7.4, with 40 uM FeII; except for the analyzed compound, solutions contained 1 mM alphaKG and 200 uM xanthine. Xanthine varied 0-250 uM except N358A 0-400 uM; alphaKG varied 0-500 uM; 9-methylxanthine varied 0-1.0 mM.


column_label: Table 2; XanA sample row K122A; substrate column group 2-Oxoglutarate; checked metric(s): kcat, kcat_over_km, km; Assays at 25 C in 50 mM MOPS buffer, pH 7.4, with 40 uM FeII; except for the analyzed compound, solutions contained 1 mM alphaKG and 200 uM xanthine. Xanthine varied 0-250 uM except N358A 0-400 uM; alphaKG varied 0-500 uM; 9-methylxanthine varied 0-1.0 mM.


enzyme_display_name: L-isoleucine 4-hydroxylase

organism: Bacillus thuringiensis

substrate_name: L-leucine

column_label: PMID 22448874 PDF page 7, printed page 102, Table 2, L-Leu row, IDO column: Km 2.3 +/- 0.4 mM; kcat 7.5 +/- 0.3 min^-1; kcat/Km 3.2 +/- 0.4 mM^-1 min^-1.

normalized_value_unit_evidence: Table 2 L-Leu/IDO: Km normalized_value=2.3 normalized_unit=mM; kcat normalized_value=0.125 normalized_unit=s^-1; printed kcat/Km normalized_value=0.05333333333333334 normalized_unit=s^-1*mM^-1. The paper's min^-1 footnote requires division by 60.

raw_value_unit_evidence: L-Leu/IDO: Km raw_value=2.3 +/- 0.4 raw_unit=mM; kcat raw_value=7.5 +/- 0.3 raw_unit=min^-1; kcat/Km raw_value=3.2 +/- 0.4 raw_unit=mM^-1*min^-1.

row_label: L-Leu; IDO column

table_label: Table 2. Kinetic parameters of L-amino acid hydroxylation (PDF page 7 of 9; printed page 102)

enzyme: L-isoleucine 4-hydroxylase

substrate: L-leucine


substrate_name: L-Methionine

column_label: PMID 22448874 PDF page 7, printed page 102, Table 2, L-Met row, IDO column: Km 3.2 +/- 0.3 mM; kcat 33 +/- 1 min^-1; kcat/Km 10 +/- 1 mM^-1 min^-1.

normalized_value_unit_evidence: Table 2 L-Met/IDO: Km normalized_value=3.2 normalized_unit=mM; kcat normalized_value=0.55 normalized_unit=s^-1; printed kcat/Km normalized_value=0.16666666666666666 normalized_unit=s^-1*mM^-1. The paper's min^-1 footnote requires division by 60.

raw_value_unit_evidence: L-Met/IDO: Km raw_value=3.2 +/- 0.3 raw_unit=mM; kcat raw_value=33 +/- 1 raw_unit=min^-1; kcat/Km raw_value=10 +/- 1 raw_unit=mM^-1*min^-1.

row_label: L-Met; IDO column

substrate: L-Methionine


substrate_name: L-Isoleucine

substrate: L-Isoleucine


organism: Delftia acidovorans

substrate_name: (RS)-2-(m-chlorophenoxy)propionate (at pH 6 and 25 degrees Celsius)

source_db: uniprot

assay_conditions_summary: pH 6

proof_lines: kcat is 50 min(-1) for dioxygenase activity with S-2,4-DP (at pH 6 and 25 degrees Celsius). kcat is 46 min(-1) for dioxygenase activity with S-2,4-MCPP (at pH 6 and 25 degrees Celsius). kcat is 36 min(-1) for dioxygenase activity with 2,4-D

source: uniprot


organism: Sphingobium herbicidovorans (strain ATCC 700291 / DSM 11019 / CCUG 56400 / KCTC 2939 / LMG 18315 / NBRC 16415 / MH)

substrate_name: S-2,4-MCPP (at pH 6.75 and 30 degrees Celsius)

column_label: PMID 16820480 Table 5, SdpA (S)-Mecoprop row, Km (uM) = 132 +/- 17.7.

normalized_value_unit_evidence: Km normalized_value=0.132 mM.

raw_value_unit_evidence: Table 5 row SdpA / (S)-Mecoprop, Km column: 132 +/- 17.7 uM.

row_label: alpha-ketoglutarate-dependent (S)-dichlorprop dioxygenase / (S)-Mecoprop (50-2,000 uM)


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

proof_lines: kcat is 65.2 min(-1) for dioxygenase activity with (RS)-2-(4-chlorophenoxy)propionate (at pH 6 and 30 degrees Celsius). kcat is 55.2 min(-1) for dioxygenase activity with R-2,4-DP (at pH 6 and 30 degrees Celsius). kcat is 50 min(-1) for dio

proof_lines: kcat is 114.2 min(-1) for dioxygenase activity with R-2,4-MCPP (at pH 6.75 and 30 degrees Celsius). kcat is 135.6 min(-1) for dioxygenase activity with alpha-ketoglutarate (at pH 6.75 and 30 degrees Celsius). kcat is 170.1 min(-1) for dioxy


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


enzyme_display_name: 3-mercaptopropionate dioxygenase

organism: Cupriavidus necator

smiles: O=C([O-])CCS

column_label: Primary article prose immediately before Figure 4 gives the 3MP row; Figure 4 caption gives CdoA 3MP substrate concentration range and assay conditions.

normalized_value_unit_evidence: CSV values match after unit normalization: kcat 0.82 s^-1, Km 5.7 mM, kcat/Km 0.143859649122807 s^-1 mM^-1, matching rounded paper 0.144.

raw_value_unit_evidence: Paper reports CdoA with 3MP: maximal specific activity 2.2 umol 3SP/mg protein/min, Km 5.7 mM, kcat 0.82 s^-1, kcat/Km 0.144 s^-1 mM^-1.

row_label: CdoA with 3MP

table_label: PMC article prose, Results: Characterization of CdoA

enzyme: 3-mercaptopropionate dioxygenase


enzyme_display_name: UniProt Q9GZT9

organism: Homo sapiens

source_db: skid

source_databases_merged: skid uniprot

enzyme: UniProt Q9GZT9

source: skid


smiles: O=O


sequence_variant_note: Mutation signature L27I/E80D/G169H/S182D could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: Prolyl hydroxylase EGLN2

substrate_name: L-ascorbate (at pH 7.5 and 37 degrees Celsius)

enzyme: Prolyl hydroxylase EGLN2


substrate_name: Fe(2+) (at pH 7.5 and 37 degrees Celsius)


organism: Pseudomonas aeruginosa


enzyme_display_name: mRNA N1-methyladenine demethylase

organism: Escherichia coli

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

proof_lines: mutant enzyme D135I, pH and temperature not specified in the publication

enzyme: mRNA N1-methyladenine demethylase


proof_lines: mutant enzyme D135N, pH and temperature not specified in the publication


proof_lines: mutant enzyme E136L, pH and temperature not specified in the publication


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

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


enzyme_display_name: ectoine hydroxylase

organism: Virgibacillus salexigens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A163C/S244C with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

enzyme: ectoine hydroxylase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N261A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A163C with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S244C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S205A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S167A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P198A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F263Y with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V265T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V265A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S165A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F242Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V265L to reconstruct the assayed variant sequence.


enzyme_display_name: isoeugenol monooxygenase

organism: Pseudomonas putida

substrate_name: isoeugenol

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

enzyme: isoeugenol monooxygenase

substrate: isoeugenol


enzyme_display_name: validamycin A dioxygenase

organism: Streptomyces hygroscopicus subsp. limoneus

proof_lines: pH 7.2, 30°C, obtained from Hanes-Woolf plot

proof_lines: kcat is 0.97 min(-1) for validamycin A as substrate (at pH 7.2).

source_databases_merged: brenda uniprot

enzyme: validamycin A dioxygenase


substrate_name: validamycin A

substrate: validamycin A


organism: Streptomyces coelicolor

substrate_name: ectoine

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

substrate: ectoine


enzyme_display_name: L-proline cis-4-hydroxylase

organism: Sinorhizobium meliloti

substrate_name: L-homophenylalanine

proof_lines: 20°C, pH not specified in the publication, wild-type enzyme

enzyme: L-proline cis-4-hydroxylase

substrate: L-homophenylalanine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W40M to reconstruct the assayed variant sequence.

proof_lines: 20°C, pH not specified in the publication, mutant enzyme W40M


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W40M/I103L to reconstruct the assayed variant sequence.

proof_lines: 20°C, pH not specified in the publication, mutant enzyme W40M/I103L


organism: Sphingopyxis alaskensis

source_databases_merged: brenda skid uniprot


column_label: Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row S. alaskensis | column Km [mM 2-oxoglutarate] = 2.7 mM 2-oxoglutarate

normalized_value_unit_evidence: km 2.7 mM

raw_value_unit_evidence: km 2.7 mM 2-oxoglutarate

row_label: S. alaskensis


proof_lines: kcat is 7.7 sec(-1) for ectoin as substrate (at pH 7.5 and 32 degrees Celsius).


organism: Halomonas elongata

proof_lines: kcat is 2.8 sec(-1) for ectoin as substrate (at pH 8 and 32 degrees Celsius).


organism: Mesorhizobium loti

proof_lines:
pH 7.5, 25°C
Raw SKiD Env: Temp=25°C, pH=7.5
kcat is 24 sec(-1).


proof_lines:
pH 7.5, 25°C
kcat is 25 sec(-1).


enzyme_display_name: Ectoine dioxygenase

organism: Stutzerimonas stutzeri (strain A1501)

substrate_name: 2-oxoglutarate (at pH 7.5 and 35 degrees Celsius)

proof_lines: kcat is 8.9 sec(-1) for ectoin as substrate (at pH 7.5 and 35 degrees Celsius).

enzyme: Ectoine dioxygenase


substrate_name: ectoine (at pH 7.5 and 35 degrees Celsius)


enzyme_display_name: Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3

substrate_name: N(1)-methyl-2'-deoxyadenosine in single-stranded DNA


organism: Streptantibioticus cattleyicolor

substrate_name: L-proline

column_label: Official Springer Table 2 row ScaEctD / L-Pro gives Km (mM)=17 +/- 2.2 and kcat (s^-1)=1.1 x 10^-1 +/- 0.1 x 10^-1.

normalized_value_unit_evidence: Km normalized_value=17.0 normalized_unit=mM; kcat normalized_value=0.11 normalized_unit=s^-1.

raw_value_unit_evidence: Km raw_value=17 +/- 2.2 raw_unit=mM; kcat raw_value=1.1 x 10^-1 +/- 0.1 x 10^-1 raw_unit=s^-1

row_label: ScaEctD / L-Pro

table_label: Table 2, Kinetic parameters of hydroxylases for ectoine and l-Pro hydroxylation

substrate: L-proline


enzyme_display_name: L-proline trans-4-hydroxylase

organism: Streptomyces griseoviridis

enzyme: L-proline trans-4-hydroxylase


enzyme_display_name: mRNA N6-methyladenine demethylase

substrate_name: 3-Methyluracil in RNA; 2-Oxoglutarate; O2

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

proof_lines: kcat is 8.78 min(-1) for m(7)Gppp(m6A(m))CA mRNA. kcat is 7.77 min(-1) for m(7)Gppp(m6A)CA mRNA. kcat is 0.54 min(-1) for GG(m6A)CU mRNA. kcat is 0.46 min(-1) for m(7)GpppAC(m6) mRNA.

enzyme: mRNA N6-methyladenine demethylase


substrate_name: L-homoectoine

proof_lines: kcat is 1.2 sec(-1) for ectoin as substrate (at pH 8 and 40 degrees Celsius).

substrate: L-homoectoine


organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)


organism: Alkalilimnicola ehrlichii

column_label: Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row A. ehrlichii | column kcat [s^-1] = 1.2 s^-1; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row A. ehrlichii | column Km [mM ectoine] = 9.0 mM ectoine; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row A. ehrlichii | column kcat/Km [mM^-1 s^-1] = 0.13 mM^-1 s^-1

raw_value_unit_evidence: kcat 1.2 s^-1; km 9.0 mM ectoine; kcat_over_km 0.13 mM^-1 s^-1

row_label: A. ehrlichii


column_label: Table 2 row A. ehrlichii, column K_m [mM 2-oxoglutarate], reports 5.0+/-0.3.

raw_value_unit_evidence: Km raw_value=5.0 uncertainty=+/-0.3 raw_unit=mM

table_label: PMC3979721 Table 2, Kinetic parameters of the analyzed ectoine hydroxylases


table_label: Table 2. Kinetic parameters of the analyzed ectoine hydroxylases


enzyme_display_name: fatty acid alpha-dioxygenase

organism: Lathyrus oleraceus

substrate_name: lauric acid

smiles: CCCCCCCCCCCC(=O)O

enzyme: fatty acid alpha-dioxygenase

substrate: lauric acid


organism: Acidiphilium cryptum

column_label: Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row A. cryptum | column kcat [s^-1] = 3.4 s^-1; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row A. cryptum | column Km [mM ectoine] = 10.0 mM ectoine; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row A. cryptum | column kcat/Km [mM^-1 s^-1] = 0.34 mM^-1 s^-1

raw_value_unit_evidence: kcat 3.4 s^-1; km 10.0 mM ectoine; kcat_over_km 0.34 mM^-1 s^-1

row_label: A. cryptum


column_label: Table 2 row A. cryptum, column K_m [mM 2-oxoglutarate], reports 4.1+/-0.4.

raw_value_unit_evidence: Km raw_value=4.1 uncertainty=+/-0.4 raw_unit=mM


organism: Oryza sativa subsp. japonica

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

column_label: Full text reports the FLO7 homolog displayed Km 0.55 mM and Vmax 0.89 mM/min/uM enzyme for 2OA.

raw_value_unit_evidence: Km raw_value=0.55 mM raw_unit=mM

row_label: Oryza sativa FLO7 homolog / 2-oxoadipate

table_label: PMC full text kinetic prose PMID 32523014


column_label: Official Springer Table 2 row HeEctD / L-Pro gives Km (mM)=5.5 +/- 0.6, kcat (s^-1)=2.9 x 10^-2 +/- 0.1 x 10^-2, and kcat/Km (s^-1 mM^-1)=5.3 x 10^-3.

normalized_value_unit_evidence: Km normalized_value=5.5 normalized_unit=mM; kcat normalized_value=0.029 normalized_unit=s^-1; kcat_over_km paper_normalized_value=0.0053 normalized_unit=s^-1*mM^-1; exported derived value=0.005272727272727273 is rounding-consistent with the printed table values.

raw_value_unit_evidence: Km raw_value=5.5 +/- 0.6 raw_unit=mM; kcat raw_value=2.9 x 10^-2 +/- 0.1 x 10^-2 raw_unit=s^-1; kcat_over_km raw_value=5.3 x 10^-3 raw_unit=s^-1 mM^-1

row_label: HeEctD / L-Pro


enzyme_display_name: 2-oxoethane-1-sulfonamide synthase

organism: Streptomyces sp

substrate_name: L-cysteine

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

enzyme: 2-oxoethane-1-sulfonamide synthase

substrate: L-cysteine


enzyme_display_name: UniProt O75164

organism: Homo sapiens

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt O75164


enzyme_display_name: Gibberellin 2-beta-dioxygenase 1

organism: Pisum sativum

column_label: Abstract reports PsGA2OX1 displayed a Km of 0.024 microM and Vmax of 4.4 pkat/mg toward GA20.

raw_value_unit_evidence: Km raw_value=0.024 microM raw_unit=microM

row_label: Recombinant Pisum sativum PsGA2OX1 / GA20

table_label: PubMed XML abstract PMID 16181493

enzyme: Gibberellin 2-beta-dioxygenase 1


organism: Streptomyces cattleya

column_label: Official Springer Table 2 row ScaEctD / Ectoine gives Km (mM)=1.7 +/- 0.1, kcat (s^-1)=5.5 x 10^-1 +/- 0.1 x 10^-1, and kcat/Km (s^-1 mM^-1)=3.3 x 10^-1.

normalized_value_unit_evidence: Km normalized_value=1.7 normalized_unit=mM; kcat normalized_value=0.55 normalized_unit=s^-1; kcat_over_km paper_normalized_value=0.33 normalized_unit=s^-1*mM^-1; exported derived value=0.3235294117647059 is rounding-consistent with the printed table values.

raw_value_unit_evidence: Km raw_value=1.7 +/- 0.1 raw_unit=mM; kcat raw_value=5.5 x 10^-1 +/- 0.1 x 10^-1 raw_unit=s^-1; kcat_over_km raw_value=3.3 x 10^-1 raw_unit=s^-1 mM^-1

row_label: ScaEctD / Ectoine


enzyme_display_name: hyoscyamine (6S)-dioxygenase

organism: Hyoscyamus niger

substrate_name: L-hyoscyamine

enzyme: hyoscyamine (6S)-dioxygenase

substrate: L-hyoscyamine


enzyme_display_name: Phytanoyl-CoA dioxygenase, peroxisomal

assay_conditions_summary: cofactor CoA

enzyme: Phytanoyl-CoA dioxygenase, peroxisomal


enzyme_display_name: Gibberellin 3-beta-dioxygenase 4

organism: Arabidopsis thaliana

enzyme: Gibberellin 3-beta-dioxygenase 4


organism: Sphingopyxis alaskensis

column_label: Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row S. alaskensis | column kcat [s^-1] = 1.2 s^-1; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row S. alaskensis | column Km [mM ectoine] = 9.8 mM ectoine; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row S. alaskensis | column kcat/Km [mM^-1 s^-1] = 0.12 mM^-1 s^-1

raw_value_unit_evidence: kcat 1.2 s^-1; km 9.8 mM ectoine; kcat_over_km 0.12 mM^-1 s^-1


organism: Paenibacillus lautus

column_label: Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row P. lautus | column kcat [s^-1] = 1.6 s^-1; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row P. lautus | column Km [mM ectoine] = 9.5 mM ectoine; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row P. lautus | column kcat/Km [mM^-1 s^-1] = 0.17 mM^-1 s^-1

raw_value_unit_evidence: kcat 1.6 s^-1; km 9.5 mM ectoine; kcat_over_km 0.17 mM^-1 s^-1

row_label: P. lautus


enzyme_display_name: Alpha-ketoglutarate-dependent xanthine dioxygenase xanA

organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)

substrate_name: 9-methylxanthine (at 25 degrees Celsius)

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


organism: Virgibacillus salexigens

column_label: Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row V. salexigens | column kcat [s^-1] = 7.7 s^-1; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row V. salexigens | column Km [mM ectoine] = 5.9 mM ectoine; Table 2. Kinetic parameters of the analyzed ectoine hydroxylases | row V. salexigens | column kcat/Km [mM^-1 s^-1] = 1.31 mM^-1 s^-1

raw_value_unit_evidence: kcat 7.7 s^-1; km 5.9 mM ectoine; kcat_over_km 1.31 mM^-1 s^-1

row_label: V. salexigens


organism: Mesorhizobium loti

proof_lines:
Mesorhizobium loti
L-proline cis-4-hydroxylase
L-proline


enzyme_display_name: 4-chlorophenylacetate 3,4-dioxygenase

organism: Pseudomonas sp.

substrate_name: ferrocytochrome c

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

assay_conditions_summary: cofactor NADH

enzyme: 4-chlorophenylacetate 3,4-dioxygenase

substrate: ferrocytochrome c


substrate_name: reduced 2,6-dichlorophenolindophenol

substrate: reduced 2,6-dichlorophenolindophenol


substrate_name: NADH

substrate: NADH


organism: Sinorhizobium meliloti


enzyme_display_name: alkyl sulfatase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: alpha-ketoglutarate (at pH 7 and 25 degrees Celsius)

assay_conditions_summary: pH 7

proof_lines: kcat is 21.8 min(-1) with alpha-ketoglutarate and 2-EHS as substrates (at pH 7 and 25 degrees Celsius).

enzyme: alkyl sulfatase


enzyme_display_name: 4-sulfobenzoate 3,4-dioxygenase

organism: Comamonas testosteroni

enzyme: 4-sulfobenzoate 3,4-dioxygenase


enzyme_display_name: naphthalene 1,2-dioxygenase

organism: Corynebacterium renale

enzyme: naphthalene 1,2-dioxygenase


substrate_name: Naphthalene

substrate: Naphthalene


enzyme_display_name: phthalate 4,5-dioxygenase

substrate_name: terephthalate

assay_conditions_summary: pH 8

column_label: Table 1 columns substrate, kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1), and coupling; row Terephthalate.

normalized_value_unit_evidence: Km 90 uM = 0.09 mM; kcat 2.0 s^-1; same-row central-value ratio 2.0/0.09 = 22.22222222222222 s^-1*mM^-1, matching table-rounded 22 mM^-1 s^-1.

raw_value_unit_evidence: Table 1 row Terephthalate reports kcat 2.0 +/- 0.1 s^-1, Km 90 +/- 12 uM, kcat/Km 22 +/- 4 mM^-1 s^-1, coupling 5.0 +/- 0.2.

row_label: Terephthalate

table_label: Table 1: Apparent steady-state kinetic parameters of PDOKF1 for different substrates

enzyme: phthalate 4,5-dioxygenase

substrate: terephthalate


substrate_name: Phthalate

column_label: Table 1 columns substrate, kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1), and coupling; row Phthalate.

raw_value_unit_evidence: Table 1 row Phthalate reports kcat 2.1 +/- 0.1 s^-1, Km 3.6 +/- 0.4 uM, kcat/Km 583 +/- 87 mM^-1 s^-1, coupling 1.0 +/- 0.4.

row_label: Phthalate

substrate: Phthalate


organism: Streptomyces griseoviridis


enzyme_display_name: taurine dioxygenase

organism: Escherichia coli

enzyme: taurine dioxygenase


substrate_name: taurine

substrate: taurine


substrate_name: MOPS

substrate: MOPS


substrate_name: pentanesulfonic acid

smiles: CCCCCS(=O)(=O)[O-]

substrate: pentanesulfonic acid


substrate_name: butanesulfonic acid

smiles: CCCCS(=O)(=O)O

substrate: butanesulfonic acid


substrate_name: hexanesulfonic acid

smiles: CCCCCCS(=O)(=O)O

substrate: hexanesulfonic acid


enzyme_display_name: peptide-aspartate beta-dioxygenase

organism: Bos taurus

enzyme: peptide-aspartate beta-dioxygenase


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


organism: Sphingomonas sp.

substrate_name: biphenyl

assay_conditions_summary: pH 7; 303.15 K; buffer 50 mM potassium phosphate; cofactor NADH

proof_lines: at 30°C in reaction mixtures containing 0.00013 mM ht-PhnI and 0.5 mM NADH in 50 mM potassium phosphate buffer, pH 7.0

substrate: biphenyl


enzyme_display_name: UniProt P39662

organism: Cupriavidus necator

enzyme: UniProt P39662


enzyme_display_name: Flavohemoprotein

organism: Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)

substrate_name: NO

smiles: [No]

enzyme: Flavohemoprotein

substrate: NO


enzyme_display_name: tryptophan 2-monooxygenase

organism: Pseudomonas savastanoi

substrate_name: L-tryptophan

enzyme: tryptophan 2-monooxygenase

substrate: L-tryptophan


proof_lines: pH 8.3, 25°C, cosubstrate: O2, wild-type


substrate_name: Unknown

substrate: Unknown


organism: Homo sapiens

substrate_name: DLDLEALAPYIPADDDFQL

substrate: DLDLEALAPYIPADDDFQL


proof_lines: wild type isoform PHD2, at pH 7.0 and 37°C


substrate_name: tryptophan

substrate: tryptophan


enzyme_display_name: persulfide dioxygenase

substrate_name: S-sulfanylglutathione

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

enzyme: persulfide dioxygenase

substrate: S-sulfanylglutathione


enzyme_display_name: cytochrome-c3 hydrogenase

organism: Nitratidesulfovibrio vulgaris

substrate_name: ferricytochrome c

enzyme: cytochrome-c3 hydrogenase

substrate: ferricytochrome c


substrate_name: mutant cytochrome c3 Y65A

substrate: mutant cytochrome c3 Y65A


substrate_name: mutant cytochrome c3 K10M

substrate: mutant cytochrome c3 K10M


substrate_name: mutant cytochrome c3 K26M

substrate: mutant cytochrome c3 K26M


substrate_name: mutant cytochrome c3 Y66L

substrate: mutant cytochrome c3 Y66L


enzyme_display_name: protocatechuate 3,4-dioxygenase

proof_lines: apparent Ki, inhibition is not freely reversible

enzyme: protocatechuate 3,4-dioxygenase


enzyme_display_name: 2,3-dihydroxybenzoate 3,4-dioxygenase

enzyme: 2,3-dihydroxybenzoate 3,4-dioxygenase


substrate_name: D,L-3-phenyl-2-hydrazinopropanoic acid

substrate: D,L-3-phenyl-2-hydrazinopropanoic acid


substrate_name: L-alanine

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

substrate: L-alanine


substrate_name: L-methionine

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

substrate: L-methionine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


enzyme_display_name: 3-carboxyethylcatechol 2,3-dioxygenase

enzyme: 3-carboxyethylcatechol 2,3-dioxygenase


substrate_name: 2,3-dihydroxycinnamic acid

substrate: 2,3-dihydroxycinnamic acid


enzyme_display_name: UniProt P20586

organism: Pseudomonas aeruginosa

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=30°C, pH=7.5

enzyme: UniProt P20586


proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=8


enzyme_display_name: UniProt Q83XK4

organism: Methylophaga aminisulfidivorans

substrate_name: indole

enzyme: UniProt Q83XK4

substrate: indole


enzyme_display_name: UniProt O15229

substrate_name: NADPH

enzyme: UniProt O15229

substrate: NADPH


enzyme_display_name: catechol 1,2-dioxygenase

organism: Acinetobacter radioresistens

substrate_name: catechol

enzyme: catechol 1,2-dioxygenase

substrate: catechol


proof_lines: mutant enzyme A72G, in100 mM Tris-HCl pH 8.5, temperature not specified in the publication


proof_lines:
pH 8.0, 35°C, mutant A72S
mutant A72S


enzyme_display_name: coenzyme F420 hydrogenase

organism: Methanobacterium formicicum

substrate_name: coenzyme F420

enzyme: coenzyme F420 hydrogenase

substrate: coenzyme F420


substrate_name: coenzyme F0

substrate: coenzyme F0


substrate_name: FAD

assay_conditions_summary: cofactor FAD

substrate: FAD


substrate_name: methyl viologen

substrate: methyl viologen


enzyme_display_name: gibberellin 2beta-dioxygenase

organism: Phaseolus vulgaris

substrate_name: alpha-ketoglutarate

enzyme: gibberellin 2beta-dioxygenase

substrate: alpha-ketoglutarate


enzyme_display_name: cyclohexanone monooxygenase

organism: Acinetobacter sp.

substrate_name: cis-hex-2-enyl phenyl selenide

enzyme: cyclohexanone monooxygenase

substrate: cis-hex-2-enyl phenyl selenide


substrate_name: 2-methylcyclohexyl boronic acid

substrate: 2-methylcyclohexyl boronic acid


substrate_name: phenyl propargyl selenide

substrate: phenyl propargyl selenide


substrate_name: n-Octylboronic acid

smiles: B(CCCCCCCC)(O)O

substrate: n-Octylboronic acid


substrate_name: n-Butylboronic acid

smiles: B(CCCC)(O)O

substrate: n-Butylboronic acid


substrate_name: Butanal

smiles: CCCC=O

substrate: Butanal


substrate_name: phenylboronic acid

substrate: phenylboronic acid


substrate_name: Phenyl methyl selenide

substrate: Phenyl methyl selenide


substrate_name: Phenyl allyl sulfide

substrate: Phenyl allyl sulfide


substrate_name: Thiane sulfoxide

substrate: Thiane sulfoxide


substrate_name: ethyl p-tolyl sulfide

substrate: ethyl p-tolyl sulfide


substrate_name: triethyl phosphite

smiles: CCOP(OCC)OCC

substrate: triethyl phosphite


substrate_name: Iodide

substrate: Iodide


enzyme_display_name: UniProt C0STX7

organism: Rhodococcus sp. HI-31

substrate_name: cyclohexanone

enzyme: UniProt C0STX7

substrate: cyclohexanone


substrate_name: NADPH

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A245G/A288V with inferred residue-numbering offset +25 to reconstruct the assayed variant sequence.


enzyme_display_name: 3-hydroxybenzoate 4-monooxygenase

organism: Comamonas testosteroni

substrate_name: m-Hydroxybenzoate

enzyme: 3-hydroxybenzoate 4-monooxygenase

substrate: m-Hydroxybenzoate


enzyme_display_name: UniProt Q0SFK6

organism: Rhodococcus jostii

enzyme: UniProt Q0SFK6


substrate_name: NADH

substrate: NADH


organism: Methanothermobacter thermautotrophicus

substrate_name: coenzyme F420

substrate: coenzyme F420


substrate_name: coenzyme F0

proof_lines: equal turnover in reverse reaction under anaerobic conditions

substrate: coenzyme F0


substrate_name: methyl viologen

proof_lines:
pH 7.2
pH 9

substrate: methyl viologen


smiles: [HH]

assay_conditions_summary: pH 9

proof_lines:
+ methyl viologen, pH 9
+ coenzyme F0, pH 7.2


enzyme_display_name: catechol 2,3-dioxygenase

organism: Pseudomonas sp.

proof_lines:
strain 1YB2, pH 7.5, 25°C
strain 1YdBTEX2, pH 7.5, 25°C

enzyme: catechol 2,3-dioxygenase


substrate_name: catechol

proof_lines:
strain 1YB2, pH 7.5, 25°C
strain 1YdBTEX2, pH 7.5, 25°C
hybrid enzyme, pH 7.5, 25°C

substrate: catechol


enzyme_display_name: UniProt P29477

organism: Mus musculus

substrate_name: L-arginine

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

enzyme: UniProt P29477

substrate: L-arginine


substrate_name: tetrahydrobiopterin

substrate: tetrahydrobiopterin


enzyme_display_name: arachidonate 12-lipoxygenase

organism: Sus scrofa

substrate_name: arachidonic acid

smiles: CCCCCC=CCC=CCC=CCC=CCCCC(=O)O

enzyme: arachidonate 12-lipoxygenase

substrate: arachidonic acid


proof_lines: wild type enzyme and mutant enzyme M338L


enzyme_display_name: UniProt O06647

organism: Pseudomonas nitroreducens

enzyme: UniProt O06647


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


enzyme_display_name: protocatechuate 3,4-dioxygenase

organism: Agrobacterium tumefaciens

enzyme: protocatechuate 3,4-dioxygenase


substrate_name: protocatechuate

proof_lines:
protocatechuate 3,4-dioxygenase type II
protocatechuate 3,4-dioxygenase type I

substrate: protocatechuate


enzyme_display_name: nitric-oxide synthase (NADPH)

organism: Nicotiana tabacum

assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH

enzyme: nitric-oxide synthase (NADPH)


substrate_name: Unknown

substrate: Unknown


organism: Aspergillus niger

substrate_name: anthranilic acid

assay_conditions_summary: pH 8.2; cofactor NADPH

substrate: anthranilic acid


enzyme_display_name: 2-hydroxybiphenyl 3-monooxygenase

substrate_name: indole

enzyme: 2-hydroxybiphenyl 3-monooxygenase

substrate: indole


proof_lines: pH 7.5, temperature not specified in the publication, mutant enzyme H48A


proof_lines: pH 7.5, temperature not specified in the publication R242A


proof_lines: pH 7.5, temperature not specified in the publication, mutant enzyme D117A


substrate_name: guaiacol

substrate: guaiacol


assay_conditions_summary: cofactor NADPH

proof_lines:
reaction with NADH and O2
reaction with NADPH and O2


proof_lines: reaction with 2,2'-dihydroxybiphenyl and O2


proof_lines:
reaction with NADPH and O2
reaction with NADH and O2
reaction with NADH or NADPH and O2


smiles: O=O

proof_lines: reaction with 2-hydroxybiphenyl and NADH


enzyme_display_name: anhydrotetracycline 6-monooxygenase

organism: Kitasatospora aureofaciens

substrate_name: anhydrotetracycline

enzyme: anhydrotetracycline 6-monooxygenase

substrate: anhydrotetracycline


enzyme_display_name: nitric-oxide synthase

organism: Aiptasia pallida

substrate_name: NADPH; L-Arginine; O2

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

enzyme: nitric-oxide synthase

substrate: NADPH; L-Arginine; O2


proof_lines: turnover rate refers to the enzyme monomer and not to the tetramer


enzyme_display_name: leukotriene-E4 20-monooxygenase

organism: Rattus norvegicus

enzyme: leukotriene-E4 20-monooxygenase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R242A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R242E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R242Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W225A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G255F to reconstruct the assayed variant sequence.


proof_lines: recombinant wild-type enzyme, pH 7.5, 30°C


assay_conditions_summary: pH 7.5; buffer 50 mM phosphate; cofactor NADH

column_label: Table 2. Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH.; row WT / NADH; 2-Hydroxybiphenyl/NADH metric block; columns Km (uM), kcat (sec^-1), kcat/Km (sec^-1 uM^-1); cells Km=149 +/- 22 uM, kcat=3.16 sec^-1, kcat/Km=0.02 sec^-1 uM^-1

normalized_value_unit_evidence: Km normalized_value=0.149 normalized_unit=mM; kcat normalized_value=3.16 normalized_unit=s^-1; kcat/Km normalized_value=20 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=149 +/- 22 raw_unit=uM; kcat raw_value=3.16 raw_unit=sec^-1; kcat/Km raw_value=0.02 raw_unit=sec^-1 uM^-1

row_label: WT / NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W225Y to reconstruct the assayed variant sequence.


enzyme_display_name: 2-hydroxycyclohexanone 2-monooxygenase

substrate_name: NADPH

enzyme: 2-hydroxycyclohexanone 2-monooxygenase

substrate: NADPH


organism: Oncorhynchus mykiss

substrate_name: H+; O2; NADPH; L-Arginine

assay_conditions_summary: cofactor NADP+

unit: lswedgeone

substrate: H+; O2; NADPH; L-Arginine


substrate_name: L-Arginine; O2; H+; NADPH

substrate: L-Arginine; O2; H+; NADPH


substrate_name: L-Arginine; NADPH; O2

substrate: L-Arginine; NADPH; O2


enzyme_display_name: alkene monooxygenase

organism: Gordonia rubripertincta

substrate_name: Propene

smiles: CC=C

enzyme: alkene monooxygenase

substrate: Propene


substrate_name: trichlorethene

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

substrate: trichlorethene


enzyme_display_name: phenylacetone monooxygenase

organism: Thermobifida fusca

substrate_name: cyclohexanone

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I67A/P440F to reconstruct the assayed variant sequence.

enzyme: phenylacetone monooxygenase

substrate: cyclohexanone


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I67C/P440F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I67G/P440F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I67Y/P440F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P440F to reconstruct the assayed variant sequence.


organism: Drosophila melanogaster

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

proof_lines:
CaM-bound recombinant eNOS
CaM-free recombinant eNOS


substrate_name: O2; H+; NADH; 4,4-Dimethyl-5alpha-cholest-7-en-3beta-ol


enzyme_display_name: cyclopentanone monooxygenase

proof_lines: recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C

enzyme: cyclopentanone monooxygenase


substrate_name: Cyclopentanone

substrate: Cyclopentanone


smiles: CCCCCCC(=O)C


substrate_name: L-arginine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W457A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

substrate: L-arginine


substrate_name: tetrahydrobiopterin

substrate: tetrahydrobiopterin


substrate_name: NADH

assay_conditions_summary: pH 7.5; 303.15 K; buffer 50 mM phosphate; cofactor NADH

table_label: Table 2. Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH.

substrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O06647 and applied mutation signature G255F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer absorption at 340 nm in 50 mM phosphate; cofactor NADH

column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'G255F', 2-Hydroxybiphenyl column group; column 'Km (uM)' = 26.6; column 'kcat (sec-1)' = 0.71; column 'kcat/Km (sec-1 uM-1)' = 0.03. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.71 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 0.71 s^(-1). Km: printed Table 2 cell 26.6 in a column headed Km (uM); 26.6 / 1000 = 0.0266 mM. kcat/Km: printed Table 2 cell 0.03 in a column headed kcat/Km (sec-1 uM-1), that is 0.03 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.03 x 1000 = 30.0 s^-1 mM^-1. The exported values are kcat 0.71 s^(-1), Km 0.0266 mM and kcat_over_km 26.69172932330827 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'G255F', 2-Hydroxybiphenyl column group: Km = 26.6 uM; kcat = 0.71 sec-1; printed kcat/Km = 0.03 in a column headed (sec-1 uM-1), that is 0.03 s^(-1)*uM^(-1).

row_label: Table 2, row G255F, 2-Hydroxybiphenyl column group

table_label: Table 2: Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH (Biochimica et Biophysica Acta 1854 (2015) 1906-1913). Printed column heads: Variant; 2-Hydroxybiphenyl Km (uM), kcat (sec-1), kcat/Km (sec-1 uM-1); NADH Km (uM), kcat (sec-1), kcat/Km (sec-1 uM-1)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O06647 and applied mutation signature W225A to reconstruct the assayed variant sequence.

column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'W225A', 2-Hydroxybiphenyl column group; column 'Km (uM)' = 29.5; column 'kcat (sec-1)' = 0.46; column 'kcat/Km (sec-1 uM-1)' = 0.02. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.46 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 0.46 s^(-1). Km: printed Table 2 cell 29.5 in a column headed Km (uM); 29.5 / 1000 = 0.0295 mM. kcat/Km: printed Table 2 cell 0.02 in a column headed kcat/Km (sec-1 uM-1), that is 0.02 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.02 x 1000 = 20.0 s^-1 mM^-1. The exported values are kcat 0.46 s^(-1), Km 0.0295 mM and kcat_over_km 15.593220338983052 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'W225A', 2-Hydroxybiphenyl column group: Km = 29.5 uM; kcat = 0.46 sec-1; printed kcat/Km = 0.02 in a column headed (sec-1 uM-1), that is 0.02 s^(-1)*uM^(-1).

row_label: Table 2, row W225A, 2-Hydroxybiphenyl column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O06647 and applied mutation signature W225Y to reconstruct the assayed variant sequence.

column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'W225Y', 2-Hydroxybiphenyl column group; column 'Km (uM)' = 22.8; column 'kcat (sec-1)' = 4.51; column 'kcat/Km (sec-1 uM-1)' = 0.2. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4.51 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 4.51 s^(-1). Km: printed Table 2 cell 22.8 in a column headed Km (uM); 22.8 / 1000 = 0.0228 mM. kcat/Km: printed Table 2 cell 0.2 in a column headed kcat/Km (sec-1 uM-1), that is 0.2 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.2 x 1000 = 200.0 s^-1 mM^-1. The exported values are kcat 4.51 s^(-1), Km 0.0228 mM and kcat_over_km 197.80701754385964 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'W225Y', 2-Hydroxybiphenyl column group: Km = 22.8 uM; kcat = 4.51 sec-1; printed kcat/Km = 0.2 in a column headed (sec-1 uM-1), that is 0.2 s^(-1)*uM^(-1).

row_label: Table 2, row W225Y, 2-Hydroxybiphenyl column group


column_label: Table 2. Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH.; row WT / 2-Hydroxybiphenyl; 2-Hydroxybiphenyl/NADH metric block; columns Km (uM), kcat (sec^-1), kcat/Km (sec^-1 uM^-1); cells Km=3.1 +/- 0.3 uM, kcat=2.26 sec^-1, kcat/Km=0.73 sec^-1 uM^-1

normalized_value_unit_evidence: Km normalized_value=0.0031 normalized_unit=mM; kcat normalized_value=2.26 normalized_unit=s^-1; kcat/Km normalized_value=730 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=3.1 +/- 0.3 raw_unit=uM; kcat raw_value=2.26 raw_unit=sec^-1; kcat/Km raw_value=0.73 raw_unit=sec^-1 uM^-1

row_label: WT / 2-Hydroxybiphenyl


column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'G255F', NADH column group; column 'Km (uM)' = 531; column 'kcat (sec-1)' = 1.34; column 'kcat/Km (sec-1 uM-1)' = 2.53 x 10^-3. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.34 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 1.34 s^(-1). Km: printed Table 2 cell 531 in a column headed Km (uM); 531 / 1000 = 0.531 mM. kcat/Km: printed Table 2 cell 2.53 x 10^-3 in a column headed kcat/Km (sec-1 uM-1), that is 0.00253 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.00253 x 1000 = 2.53 s^-1 mM^-1. The exported values are kcat 1.34 s^(-1), Km 0.531 mM and kcat_over_km 2.5235404896421847 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'G255F', NADH column group: Km = 531 uM; kcat = 1.34 sec-1; printed kcat/Km = 2.53 x 10^-3 in a column headed (sec-1 uM-1), that is 0.00253 s^(-1)*uM^(-1).

row_label: Table 2, row G255F, NADH column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O06647 and applied mutation signature R242A to reconstruct the assayed variant sequence.

column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'R242A', NADH column group; column 'Km (uM)' = 446; column 'kcat (sec-1)' = 0.14; column 'kcat/Km (sec-1 uM-1)' = 3.14 x 10^-4. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.14 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 0.14 s^(-1). Km: printed Table 2 cell 446 in a column headed Km (uM); 446 / 1000 = 0.446 mM. kcat/Km: printed Table 2 cell 3.14 x 10^-4 in a column headed kcat/Km (sec-1 uM-1), that is 0.000314 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.000314 x 1000 = 0.314 s^-1 mM^-1. The exported values are kcat 0.14 s^(-1), Km 0.336 mM and kcat_over_km 0.4166666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'R242A', NADH column group: Km = 446 uM; kcat = 0.14 sec-1; printed kcat/Km = 3.14 x 10^-4 in a column headed (sec-1 uM-1), that is 0.000314 s^(-1)*uM^(-1).

row_label: Table 2, row R242A, NADH column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O06647 and applied mutation signature R242E to reconstruct the assayed variant sequence.

column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'R242E', NADH column group; column 'Km (uM)' = 427; column 'kcat (sec-1)' = 0.15; column 'kcat/Km (sec-1 uM-1)' = 3.51 x 10^-4. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.15 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 0.15 s^(-1). Km: printed Table 2 cell 427 in a column headed Km (uM); 427 / 1000 = 0.427 mM. kcat/Km: printed Table 2 cell 3.51 x 10^-4 in a column headed kcat/Km (sec-1 uM-1), that is 0.000351 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.000351 x 1000 = 0.351 s^-1 mM^-1. The exported values are kcat 0.15 s^(-1), Km 0.427 mM and kcat_over_km 0.351288056206089 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'R242E', NADH column group: Km = 427 uM; kcat = 0.15 sec-1; printed kcat/Km = 3.51 x 10^-4 in a column headed (sec-1 uM-1), that is 0.000351 s^(-1)*uM^(-1).

row_label: Table 2, row R242E, NADH column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O06647 and applied mutation signature R242Q to reconstruct the assayed variant sequence.

column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'R242Q', NADH column group; column 'Km (uM)' = 222; column 'kcat (sec-1)' = 0.24; column 'kcat/Km (sec-1 uM-1)' = 1.08 x 10^-3. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.24 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 0.24 s^(-1). Km: printed Table 2 cell 222 in a column headed Km (uM); 222 / 1000 = 0.222 mM. kcat/Km: printed Table 2 cell 1.08 x 10^-3 in a column headed kcat/Km (sec-1 uM-1), that is 0.00108 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.00108 x 1000 = 1.08 s^-1 mM^-1. The exported values are kcat 0.24 s^(-1), Km 0.222 mM and kcat_over_km 1.081081081081081 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'R242Q', NADH column group: Km = 222 uM; kcat = 0.24 sec-1; printed kcat/Km = 1.08 x 10^-3 in a column headed (sec-1 uM-1), that is 0.00108 s^(-1)*uM^(-1).

row_label: Table 2, row R242Q, NADH column group


column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'W225A', NADH column group; column 'Km (uM)' = 253; column 'kcat (sec-1)' = 3.45; column 'kcat/Km (sec-1 uM-1)' = 0.014. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.45 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 3.45 s^(-1). Km: printed Table 2 cell 253 in a column headed Km (uM); 253 / 1000 = 0.253 mM. kcat/Km: printed Table 2 cell 0.014 in a column headed kcat/Km (sec-1 uM-1), that is 0.014 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.014 x 1000 = 14.0 s^-1 mM^-1. The exported values are kcat 3.45 s^(-1), Km 0.253 mM and kcat_over_km 13.636363636363637 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'W225A', NADH column group: Km = 253 uM; kcat = 3.45 sec-1; printed kcat/Km = 0.014 in a column headed (sec-1 uM-1), that is 0.014 s^(-1)*uM^(-1).

row_label: Table 2, row W225A, NADH column group


column_label: Table 2 (Km and kcat values of HbpA and engineered variants on 2-hydroxybiphenyl and NADH), body row 'W225Y', NADH column group; column 'Km (uM)' = 102; column 'kcat (sec-1)' = 5.8; column 'kcat/Km (sec-1 uM-1)' = 0.057. The uncertainty printed beside the Km cell of this row is the fit error and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 2 cell 5.8 in a column headed kcat (sec-1); sec-1 is the canonical s^-1, so no conversion applies and the value is 5.8 s^(-1). Km: printed Table 2 cell 102 in a column headed Km (uM); 102 / 1000 = 0.102 mM. kcat/Km: printed Table 2 cell 0.057 in a column headed kcat/Km (sec-1 uM-1), that is 0.057 s^(-1)*uM^(-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.057 x 1000 = 57.0 s^-1 mM^-1. The exported values are kcat 5.8 s^(-1), Km 0.102 mM and kcat_over_km 56.86274509803922 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'W225Y', NADH column group: Km = 102 uM; kcat = 5.8 sec-1; printed kcat/Km = 0.057 in a column headed (sec-1 uM-1), that is 0.057 s^(-1)*uM^(-1).

row_label: Table 2, row W225Y, NADH column group


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I67Y/P440F to reconstruct the assayed variant sequence.


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


sequence_variant_note: Mutation signature I67G/P440F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature I67A/P440F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature I67C/P440F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: phenylacetone

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

proof_lines:
mutant P3
mutant P1
mutant P2

substrate: phenylacetone


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R217L with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220Q/K336N to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant H220Q/K336N


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K336H with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K336N with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220Q/K336H to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant H220Q/K336H


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R217A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220T to reconstruct the assayed variant sequence.


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

proof_lines: pH 8.0, 30°C, recombinant wild-type PAMO


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H220N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T218A to reconstruct the assayed variant sequence.


smiles: CCCCCCCCCCC(=O)C

assay_conditions_summary: pH 7.5; cofactor NADPH


substrate_name: benzylacetone

substrate: benzylacetone


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S441G/A442P/L443T/S444Q to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant S441G/A442P/L443T/S444Q


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A442P/L443V with inferred residue-numbering offset -34 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant A442P/L443V


organism: Mycobacterium tuberculosis

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

proof_lines: 25°C, pH 8.5, in the presence of 0.006 mM bovine serum albumin


proof_lines: recombinant wild-type enzyme, pH 7.4, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P253F/G254A/R258M/L443F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C


enzyme_display_name: senecionine N-oxygenase

organism: Arctia caja

substrate_name: senecionine

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

enzyme: senecionine N-oxygenase

substrate: senecionine


substrate_name: monocrotaline

substrate: monocrotaline


substrate_name: heliotrine

substrate: heliotrine


organism: Creatonotos transiens


organism: Comamonas sp. NCIMB 9872

substrate_name: Cyclopentanone; O2; NADPH; H+

substrate: Cyclopentanone; O2; NADPH; H+


substrate_name: H+; NADPH; Ethionamide; O2

substrate: H+; NADPH; Ethionamide; O2


organism: Zonocerus variegatus

assay_conditions_summary: pH 9; 310.15 K; buffer 100 mM glycine/NaOH

proof_lines: in 100 mM glycine/NaOH buffer pH 9.0, at 37°C


substrate_name: phalaenopsine

substrate: phalaenopsine


substrate_name: atropine

substrate: atropine


enzyme_display_name: UniProt A6T923

organism: Klebsiella pneumoniae

enzyme: UniProt A6T923


enzyme_display_name: monocyclic monoterpene ketone monooxygenase

organism: Rhodococcus erythropolis

sequence: MQTIPSTTETAADFDAVIXGAGFXGLYALHR

proof_lines: kcat is 3.9 sec(-1) with (4R)-dihydrocarvone as substrate. kcat is 4.9 sec(-1) with (1R,4S)-1-hydroxy-2-oxolimonene as substrate. kcat is 3.9 sec(-1) with (1S,4R)-1-hydroxy-2-oxolimonene as substrate. kcat is 3.6 sec(-1) with (1R,4S)-mentho


enzyme: monocyclic monoterpene ketone monooxygenase


substrate_name: NADPH

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q47PU3 and applied mutation signature R258M to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH

column_label: Table 1 carries a substrate-block column, a PAMO construct column and three kinetic columns headed K_M [mM], k_cat [s^-1] and k_cat/K_M [M^-1 s^-1]. The cited cell set is the 2-Octanone block, PAMO row R258M: K_M [mM] = 0.3; k_cat [s^-1] = 0.067; k_cat/K_M [M^-1 s^-1] = 2.3 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.067 in the 2-Octanone block of PAMO row R258M under the column head k_cat [s^-1]; the column is already per second, so no unit conversion applies and the paper value is 0.067 s^(-1). Km: printed Table 1 cell 0.3 under the column head K_M [mM]; the column is already in mM, so no unit conversion applies and the paper value is 0.3 mM. kcat/Km: printed Table 1 cell 2.3 x 10^2 under the column head k_cat/K_M [M^-1 s^-1], that is 230.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 230.0 / 1000 = 0.23 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, 2-Octanone block, PAMO row R258M: K_M = 0.3 mM; k_cat = 0.067 s^-1; printed k_cat/K_M = 2.3 x 10^2 M^-1 s^-1.

table_label: Table 1: Steady-state kinetic parameters of PAMO WT and variants R258A, R258M and P253F/G254A/R258M/L443F for the conversion of 2-octanone (Phys. Chem. Chem. Phys., 2018, 20, 2558-2570)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q47PU3 and applied mutation signature R258A to reconstruct the assayed variant sequence.

column_label: Table 1 carries a substrate-block column, a PAMO construct column and three kinetic columns headed K_M [mM], k_cat [s^-1] and k_cat/K_M [M^-1 s^-1]. The cited cell set is the 2-Octanone block, PAMO row R258A: K_M [mM] = 2.1; k_cat [s^-1] = 0.091; k_cat/K_M [M^-1 s^-1] = 43.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.091 in the 2-Octanone block of PAMO row R258A under the column head k_cat [s^-1]; the column is already per second, so no unit conversion applies and the paper value is 0.091 s^(-1). Km: printed Table 1 cell 2.1 under the column head K_M [mM]; the column is already in mM, so no unit conversion applies and the paper value is 2.1 mM. kcat/Km: printed Table 1 cell 43 under the column head k_cat/K_M [M^-1 s^-1], that is 43.0 M^-1 s^-1, a value the paper also restates in prose as the catalytic efficiency of R258A; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 43.0 / 1000 = 0.043 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, 2-Octanone block, PAMO row R258A: K_M = 2.1 mM; k_cat = 0.091 s^-1; printed k_cat/K_M = 43 M^-1 s^-1.


column_label: Table 1 (printed page 2563, PDF page 6), wave-12 decoded plain-numeral transcription, substrate block `2-Octanone`, PAMO sub-row `WT^17`: column `KM [mM]` = 3.2; column `kcat [s^-1]` = 0.22; column `kcat/KM [M^-1 s^-1]` = 66.

normalized_value_unit_evidence: kcat: printed cell 0.22 s^-1 -> 0.22 s^(-1); no unit conversion applies because the column is printed in s^-1. Km: printed cell 3.2 mM -> 3.2 mM; no unit conversion applies because the column is printed in mM. kcat/Km: the paper PRINTS the kcat/KM cell 66 M^-1 s^-1 for this row, and that printed cell is the kcat_over_km value reported here; 66 M^-1 s^-1 divided by 1000 gives 0.066 s^(-1)*mM^(-1). The live export row holds kcat 1.0 s^(-1), km 2.0 mM and kcat_over_km 0.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Raw printed cells for `2-Octanone` `WT^17`: KM = 3.2 mM; kcat = 0.22 s^-1; kcat/KM = 66 M^-1 s^-1.

table_label: Table 1 (printed page 2563, PDF page 6), wave-12 decoded plain-numeral transcription of the steady-state kinetic parameters of PAMO


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R258A to reconstruct the assayed variant sequence.


substrate_name: NADPH; (4R)-Dihydrocarvone; O2; H+

substrate: NADPH; (4R)-Dihydrocarvone; O2; H+


enzyme_display_name: Methanesulfonate monooxygenase ferredoxin subunit

organism: Methylosulfonomonas methylovora

assay_conditions_summary: cofactor NADH

proof_lines: Cell-free extracts of MSA-grown strain M2 have been used. Vmax of a cytoplasmic fraction has shown to be lower as was that of a reconstituted enzyme from partially purified fractions which was increased by addition of FAD and Fe(2+).


substrate_name: ethane sulfonic acid

smiles: CCS(=O)(=O)O

enzyme: Methanesulfonate monooxygenase ferredoxin subunit

substrate: ethane sulfonic acid


enzyme_display_name: Putative methanesulfonate monooxygenase ferredoxin reductase subunit


enzyme: Putative methanesulfonate monooxygenase ferredoxin reductase subunit


enzyme_display_name: Methanesulfonate monooxygenase hydroxylase subunit alpha


enzyme: Methanesulfonate monooxygenase hydroxylase subunit alpha


enzyme_display_name: Methanesulfonate monooxygenase hydroxylase subunit beta


enzyme: Methanesulfonate monooxygenase hydroxylase subunit beta


enzyme_display_name: 2,6-dihydroxypyridine 3-monooxygenase

organism: Arthrobacter nicotinovorans

enzyme: 2,6-dihydroxypyridine 3-monooxygenase


assay_conditions_summary: cofactor NAD+


enzyme_display_name: NO-associated protein 1, chloroplastic/mitochondrial

organism: Arabidopsis thaliana

substrate_name: Unknown

substrate: Unknown


substrate_name: methyl 4-tolylsulfide

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

substrate: methyl 4-tolylsulfide


enzyme_display_name: FAD-dependent urate hydroxylase

organism: Xanthomonas campestris

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

assay_conditions_summary: pH 8; 298.15 K; buffer context; cofactor NADH

proof_lines: in 50 mM K2HPO4/NaH2PO4, pH 8.0, at 25°C

enzyme: FAD-dependent urate hydroxylase


substrate_name: Urate

assay_conditions_summary: pH 8; buffer context; cofactor FAD

substrate: Urate


assay_conditions_summary: pH 8; 298.15 K; buffer context; cofactor NADPH


organism: Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / PYR-1)

substrate_name: urate

proof_lines: kcat is 56.0 sec(-1) for the NADH-dependent oxidation of urate. Exhibits a Michaelian behavior only toward urate and a cooperative behavior toward NADH and NADPH.

substrate: urate


proof_lines:
Raw SKiD Env: Temp=-----, pH=8
Raw SKiD Env: Temp=25°C, pH=8
kcat is 42 sec(-1).


assay_conditions_summary: cofactor FAD


enzyme_display_name: 2-hydroxybiphenyl 3-monooxygenase

organism: Pseudomonas nitroreducens

sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M223A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer pH 7; cofactor NADH

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M223A.

table_label: Table 1, Km and kcat values of engineered HbpA variants on 2HBP

enzyme: 2-hydroxybiphenyl 3-monooxygenase


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M223E to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M223E.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M223I to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M223I.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M223K to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M223K.

raw_value_unit_evidence: Table 1 row M223K: Km 6.5 uM; kcat 1.97 s^-1; kcat/Km 0.3 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M223Q to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M223Q.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M321A to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M321A.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M321F to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M321F.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M321L to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M321L.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature M321V to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant M321V.


sequence_variant_note: Resolved canonical sequence from uniprotkb:O06647;genbank:AAB57640.1;rcsb:5BRT and applied mutation signature W97A to reconstruct the assayed variant sequence.

column_label: Table 1 columns Variant, Km, kcat, and kcat/Km; row matched by engineered variant W97A.

raw_value_unit_evidence: Table 1 row W97A: Km 6 uM; kcat 0.48 s^-1; kcat/Km 0.08 s^-1 uM^-1.


organism: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)

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

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 1.06 sec(-1) for the NADPH-dependent oxidation of urate.


substrate_name: NADH

substrate: NADH


organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)

proof_lines: kcat is 23.6 sec(-1) for the NADH-dependent oxidation of urate. Exhibits a Michaelian behavior toward urate and NADPH and a cooperative behavior toward NADH.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W97Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH

proof_lines:
2-hydroxybiphenyl 3-monooxygenase
2-substituted phenols
M321A


enzyme_display_name: 6-hydroxynicotinate 3-monooxygenase

organism: Bordetella bronchiseptica

assay_conditions_summary: pH 7.5; cofactor NADH

column_label: Table 3 columns KM^6-HNA (uM), kcat (s^-1), and kcat/KM^6-HNA (M^-1 s^-1) for row B. bronchiseptica RB50.

normalized_value_unit_evidence: KM^6-HNA 0.085 mM; kcat 4.2 s^-1; kcat/KM^6-HNA 50 s^-1 mM^-1 table rounded, consistent with csv ratio 49.4117647.

row_label: B. bronchiseptica RB50

table_label: Table 3

enzyme: 6-hydroxynicotinate 3-monooxygenase


assay_conditions_summary: pH 7.5; cofactor NAD+

proof_lines: kcat is 4.2 sec(-1) with 6-hydroxynicotinate as substrate (at pH 7.5 and 25 degrees Celsius) (PubMed:27218267). kcat is 5.1 sec(-1) with 6-hydroxynicotinate as substrate. kcat is 0.074 sec(-1) with 4-hydroxybenzoate as substrate. kcat is 2.


proof_lines: pH 7.5, 25°C, recombinant wild-type enzyme


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

proof_lines:
pH 7.5, 25°C, recombinant mutant C202A
mutant enzyme C202A, at pH 7.5 and 25°C


proof_lines:
pH 7.5, 25°C, recombinant mutant H302A
mutant enzyme H302A, at pH 7.5 and 25°C


proof_lines:
pH 7.5, 25°C, recombinant mutant Y225F
mutant enzyme Y225F, at pH 7.5 and 25°C


proof_lines:
pH 7.5, 25°C, recombinant mutant H211A
mutant enzyme H211A, at pH 7.5 and 25°C


proof_lines:
pH 7.5, 25°C, recombinant mutant Y215F
mutant enzyme Y215F, at pH 7.5 and 25°C


organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

substrate_name: 6-hydroxynicotinate (at pH 7.5 and 25 degrees Celsius)

proof_lines: kcat is 2.2 sec(-1) with 6-hydroxynicotinate as substrate (at pH 7.5 and 25 degrees Celsius).


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

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


organism: Thermobifida fusca

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q47PU3 and applied mutation signature P253F/G254A/R258M/L443F to reconstruct the assayed variant sequence.

smiles: CCCCCCC(C)=O

column_label: Table 1; row 2-Octanone / P253F/G254A/R258M/L443F, columns KM [mM], kcat [s^-1], and kcat/KM [M^-1 s^-1].

normalized_value_unit_evidence: current kcat 2.3 s^-1; paper kcat 2.3 s^-1; current Km 0.25 mM; paper Km 0.25 mM; current kcat/Km 9.2 s^-1 mM^-1; paper kcat/Km 9.2 s^-1 mM^-1

raw_value_unit_evidence: current kcat 2.3 s^-1; paper kcat 2.3 s^-1; current Km 0.25 mM; paper Km 0.25 mM; current kcat/Km 9.2 s^-1 mM^-1; paper kcat/Km 9.2 x 10^3 M^-1 s^-1

table_label: Table 1. Steady-state kinetic parameters of PAMO WT and variants R258A, R258M and P253F/G254A/R258M/L443F


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q47PU3 and applied mutation signature R258A to reconstruct the assayed variant sequence.

column_label: Table 1; row 2-Octanone / R258A, columns KM [mM], kcat [s^-1], and kcat/KM [M^-1 s^-1].

normalized_value_unit_evidence: current kcat 0.091 s^-1; paper kcat 0.091 s^-1; current Km 2.1 mM; paper Km 2.1 mM; current kcat/Km 0.0433333333333 s^-1 mM^-1; paper kcat/Km 0.043 s^-1 mM^-1

raw_value_unit_evidence: current kcat 0.091 s^-1; paper kcat 0.091 s^-1; current Km 2.1 mM; paper Km 2.1 mM; current kcat/Km 0.0433333333333 s^-1 mM^-1; paper kcat/Km 43 M^-1 s^-1

row_label: 2-Octanone / R258A


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q47PU3 and applied mutation signature R258M to reconstruct the assayed variant sequence.

column_label: Table 1; row 2-Octanone / R258M, columns KM [mM], kcat [s^-1], and kcat/KM [M^-1 s^-1].

normalized_value_unit_evidence: current kcat 0.067 s^-1; paper kcat 0.067 s^-1; current Km 0.3 mM; paper Km 0.3 mM; current kcat/Km 0.223333333333 s^-1 mM^-1; paper kcat/Km 0.23 s^-1 mM^-1

raw_value_unit_evidence: current kcat 0.067 s^-1; paper kcat 0.067 s^-1; current Km 0.3 mM; paper Km 0.3 mM; current kcat/Km 0.223333333333 s^-1 mM^-1; paper kcat/Km 2.3 x 10^2 M^-1 s^-1

row_label: 2-Octanone / R258M


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P253F/G254A/R258M/L443F to reconstruct the assayed variant sequence.

column_label: Table 1; row 2-Octanone / WT, columns KM [mM], kcat [s^-1], and kcat/KM [M^-1 s^-1].

normalized_value_unit_evidence: current kcat 0.22 s^-1; paper kcat 0.22 s^-1; current Km 3.2 mM; paper Km 3.2 mM; current kcat/Km 0.06875 s^-1 mM^-1; paper kcat/Km 0.066 s^-1 mM^-1

raw_value_unit_evidence: current kcat 0.22 s^-1; paper kcat 0.22 s^-1; current Km 3.2 mM; paper Km 3.2 mM; current kcat/Km 0.06875 s^-1 mM^-1; paper kcat/Km 66 M^-1 s^-1

row_label: 2-Octanone / WT


column_label: Table 1; row 2-Phenylcyclohexanone / P253F/G254A/R258M/L443F, columns KM [mM], kcat [s^-1], and kcat/KM [M^-1 s^-1].

normalized_value_unit_evidence: current kcat 0.3 s^-1; paper kcat 0.3 s^-1; current Km 0.8 mM; paper Km 0.8 mM; current kcat/Km 0.375 s^-1 mM^-1; paper kcat/Km 0.37 s^-1 mM^-1

raw_value_unit_evidence: current kcat 0.3 s^-1; paper kcat 0.3 s^-1; current Km 0.8 mM; paper Km 0.8 mM; current kcat/Km 0.375 s^-1 mM^-1; paper kcat/Km 3.7 x 10^2 M^-1 s^-1


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


substrate_name: Cyclopentanone

column_label: Table 1; row Cyclopentanone / P253F/G254A/R258M/L443F, columns KM [mM], kcat [s^-1], and kcat/KM [M^-1 s^-1].

normalized_value_unit_evidence: current kcat 1.6 s^-1; paper kcat 1.6 s^-1; current Km 1000 mM; paper Km 1000 mM; current kcat/Km 0.0016 s^-1 mM^-1; paper kcat/Km 0.0016 s^-1 mM^-1

raw_value_unit_evidence: current kcat 1.6 s^-1; paper kcat 1.6 s^-1; current Km 1000 mM; paper Km 1000 mM; current kcat/Km 0.0016 s^-1 mM^-1; paper kcat/Km 1.6 M^-1 s^-1

substrate: Cyclopentanone


substrate_name: phenylacetone

column_label: Table 1; row Phenylacetone / P253F/G254A/R258M/L443F, columns KM [mM], kcat [s^-1], and kcat/KM [M^-1 s^-1].

normalized_value_unit_evidence: current kcat 0.04 s^-1; paper kcat 0.04 s^-1; current Km 1.4 mM; paper Km 1.4 mM; current kcat/Km 0.0285714285714 s^-1 mM^-1; paper kcat/Km 35 s^-1 mM^-1

raw_value_unit_evidence: current kcat 0.04 s^-1; paper kcat 0.04 s^-1; current Km 1.4 mM; paper Km 1.4 mM; current kcat/Km 0.0285714285714 s^-1 mM^-1; paper kcat/Km 3.5 x 10^4 M^-1 s^-1

row_label: Phenylacetone / P253F/G254A/R258M/L443F

substrate: phenylacetone


column_label: Table 1; row Phenylacetone / R258A, columns KM [mM], kcat [s^-1], and kcat/KM [M^-1 s^-1].

normalized_value_unit_evidence: current kcat 2.1 s^-1; paper kcat 2.1 s^-1; current Km 0.17 mM; paper Km 0.17 mM; current kcat/Km 12.3529411765 s^-1 mM^-1; paper kcat/Km 0.012 s^-1 mM^-1

raw_value_unit_evidence: current kcat 2.1 s^-1; paper kcat 2.1 s^-1; current Km 0.17 mM; paper Km 0.17 mM; current kcat/Km 12.3529411765 s^-1 mM^-1; paper kcat/Km 12 M^-1 s^-1

row_label: Phenylacetone / R258A


substrate_name: 6-Hydroxynicotinate; H+; NADH; O2

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

source_databases_merged: sabio_rk brenda uniprot

substrate: 6-Hydroxynicotinate; H+; NADH; O2


organism: Pseudomonas fluorescens


organism: Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)

substrate_name: 4-hydroxybenzoate (at pH 7.5 and 25 degrees Celsius)

column_label: Table 1 row 4-HBA; column KSM; footnote states pH 7.5 and 25 C.

normalized_value_unit_evidence: Km 0.6 mM.

raw_value_unit_evidence: Table 1 row 4-HBA reports KSM 600 +/- 100 uM.

table_label: Table 1. Comparison of reactions catalyzed by wild-type NicC with 6-HNA and analogues


enzyme_display_name: UniProt H9N289

organism: Pseudomonas putida

substrate_name: Caffeine

enzyme: UniProt H9N289

substrate: Caffeine


column_label: Table 1 carries a substrate-block column, a PAMO construct column and three kinetic columns headed K_M [mM], k_cat [s^-1] and k_cat/K_M [M^-1 s^-1]. The cited cell set is the Phenylacetone block, PAMO row WT: K_M [mM] = 0.06; k_cat [s^-1] = 2.4; the efficiency cell = 40, read on the per second per mM scale that the Phenylacetone block's own printed cells follow.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.4 in the Phenylacetone block of PAMO row WT under the column head k_cat [s^-1]; the column is already per second, so no unit conversion applies and the paper value is 2.4 s^(-1). Km: printed Table 1 cell 0.06 under the column head K_M [mM]; the column is already in mM, so no unit conversion applies and the paper value is 0.06 mM. kcat/Km: printed Table 1 cell 40. Printed Table 1 efficiency cell 40 for the Phenylacetone block, PAMO row WT. The printed head of that column is k_cat/K_M [M^-1 s^-1], and the printed efficiency cells of the Phenylacetone block sit on the per second per mM scale: this line prints k_cat 2.4 s^-1 and K_M 0.06 mM, and 2.4 / 0.06 = 40 per second per mM, while the second line of the same block prints k_cat 2.1 s^-1 and K_M 0.17 mM with the efficiency cell 12, and 2.1 / 0.17 = 12.35 per second per mM; the paper's prose gives the step between those two lines as 3.2-fold, which is 40 / 12.35. The cell is therefore read as 40 s^-1 mM^-1 and no unit conversion applies to it. The paper value is 40.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Phenylacetone block, PAMO row WT: K_M = 0.06 mM; k_cat = 2.4 s^-1; printed efficiency cell = 40.

table_label: Table 1: Steady-state kinetic parameters of PAMO WT and variants for the conversion of 2-octanone (Phys. Chem. Chem. Phys., 2018, 20, 2558-2570)


organism: Mycobacterium tuberculosis

substrate_name: benzylacetone

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

substrate: benzylacetone


substrate_name: Ethionamide

substrate: Ethionamide


smiles: CCCCCCCCCCC(C)=O

assay_conditions_summary: pH 8.5; 298.15 K; cofactor NADPH

column_label: Table II 2-Dodecanone row, Km column 200 uM and kcat column 0.023 s^-1; Table II has no separate kcat/Km column, so the current ratio is the exact same-row quotient.

raw_value_unit_evidence: Table II 2-Dodecanone row: Km 200 uM; kcat 0.023 s^-1; FMT 94%.

table_label: Table II. Steady-state kinetic parameters of EtaA