substrate_name: cis-permethrin

column_label: TABLE 1: Kinetic constants determined for the purified recombinant PytH (Appl. Environ. Microbiol. 2009, 75(17):5496-5500). Column heads, in printed order: 'Substrate'; 'Sp act (umol/min/mg)'; 'kcat (s^-1)'; 'Km (uM)'; 'kcat/Km (uM^-1 . s^-1)', all under the banner head 'Mean +/- SD'. The line read here is the one whose substrate label is 'cis-Permethrin': its Sp act cell, its kcat cell 3.00, its Km cell 0.065 and its kcat/Km cell 46.15 sit at the four fixed character columns of the rendering, so each number belongs to the head above it.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.00 s^-1; the printed unit is already the canonical one, so no unit conversion applies; normalized 3.0 s^(-1). Km: printed Table 1 cell 0.065 uM; 0.065 / 1000 = 0.00006500000000000001 mM. kcat/Km: printed Table 1 cell 46.15 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 46.15 x 1000 = 46150.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, line 'cis-Permethrin': kcat column (s^-1) = 3.00; Km column (uM) = 0.065; printed kcat/Km column (uM^-1 s^-1) = 46.15.

row_label: Table 1 line 'cis-Permethrin'

substrate: cis-permethrin


enzyme_display_name: pyrethroid hydrolase

organism: Sphingobium sp.

substrate_name: 4-nitrophenyl hexanoate

source_db: brenda

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_source: multiple

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

proof_lines: kcat is 3.03 sec(-1) with trans-Permethrin acetate as substrate. kcat is 3.00 sec(-1) with cis-Permethrin acetate as substrate. kcat is 2.61 sec(-1) with Fenpropathrin acetate as substrate. kcat is 2.53 sec(-1) with trans-Cypermethrin aceta

data_origin: experimental

source_databases_merged: brenda uniprot

enzyme: pyrethroid hydrolase

substrate: 4-nitrophenyl hexanoate

status: unverified

source: brenda


substrate_name: 4-nitrophenyl butanoate

substrate: 4-nitrophenyl butanoate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


organism: Chryseobacterium sp. StRB126

substrate_name: N-dodecanoyl-L-homoserine lactone

kcat_over_km_origin: calculated

proof_lines: pH 7.5, temperature not specified in the publication

substrate: N-dodecanoyl-L-homoserine lactone


substrate_name: N-decanoyl-L-homoserine lactone

substrate: N-decanoyl-L-homoserine lactone


substrate_name: N-butyryl-L-homoserine lactone

substrate: N-butyryl-L-homoserine lactone


substrate_name: N-octanoyl-L-homoserine lactone

substrate: N-octanoyl-L-homoserine lactone


substrate_name: N-pentanoyl-L-homoserine lactone

substrate: N-pentanoyl-L-homoserine lactone


substrate_name: N-hexanoyl-L-homoserine lactone

substrate: N-hexanoyl-L-homoserine lactone


substrate_name: N-heptanoyl-L-homoserine lactone

substrate: N-heptanoyl-L-homoserine lactone


enzyme_display_name: cutinase

organism: Marinactinospora thermotolerans

verification_status: corrected

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

assay_conditions_summary: pH 8

column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C2 / MtCut, column MtCut; Km mM, raw cell 0.55 +/- 0.04, normalized 0.55 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C2 / MtCut, column MtCut; kcat s^-1, raw cell 4.47 +/- 0.28, normalized 4.47 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C2 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (8.19 +/- 0.34) x 10^3, normalized 8.19 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.55 normalized_unit=mM; kcat normalized_value=4.47 normalized_unit=s^-1; kcat/Km normalized_value=8.19 normalized_unit=s^-1*mM^-1

row_label: pNP-C2 / MtCut

enzyme: cutinase

status: corrected


substrate_name: 4-nitrophenyl palmitate

column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C16 / MtCut, column MtCut; Km mM, raw cell 0.15 +/- 0.01, normalized 0.15 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C16 / MtCut, column MtCut; kcat s^-1, raw cell 4.79 +/- 0.12, normalized 4.79 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C16 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (3.25 +/- 0.10) x 10^4, normalized 32.5 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.15 normalized_unit=mM; kcat normalized_value=4.79 normalized_unit=s^-1; kcat/Km normalized_value=32.5 normalized_unit=s^-1*mM^-1

row_label: pNP-C16 / MtCut

substrate: 4-nitrophenyl palmitate


substrate_name: 4-nitrophenyl myristate

column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C14 / MtCut, column MtCut; Km mM, raw cell 0.19 +/- 0.04, normalized 0.19 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C14 / MtCut, column MtCut; kcat s^-1, raw cell 9.87 +/- 1.52, normalized 9.87 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C14 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (5.14 +/- 0.29) x 10^4, normalized 51.4 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.19 normalized_unit=mM; kcat normalized_value=9.87 normalized_unit=s^-1; kcat/Km normalized_value=51.4 normalized_unit=s^-1*mM^-1

row_label: pNP-C14 / MtCut

substrate: 4-nitrophenyl myristate


substrate_name: 4-nitrophenyl butyrate

column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C4 / MtCut, column MtCut; Km mM, raw cell 1.33 +/- 0.15, normalized 1.33 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C4 / MtCut, column MtCut; kcat s^-1, raw cell 14.10 +/- 1.51, normalized 14.1 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C4 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (1.06 +/- 0.01) x 10^4, normalized 10.6 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=1.33 normalized_unit=mM; kcat normalized_value=14.1 normalized_unit=s^-1; kcat/Km normalized_value=10.6 normalized_unit=s^-1*mM^-1

row_label: pNP-C4 / MtCut

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl octadecanoate

verification_status: verified

column_label: TABLE 1 | MtCut kinetic parameters toward pNP esters; row pNP-C18; columns Km (mM), kcat (s^-1), kcat/Km (M^-1 s^-1); normalized kcat/Km to s^-1 mM^-1.

normalized_value_unit_evidence: kcat paper=14.31 s^-1; km paper=0.45 mM; kcat_over_km paper=31.8 s^-1 mM^-1

raw_value_unit_evidence: TABLE 1 | MtCut kinetic parameters toward pNP esters, row pNP-C18: Km 0.45 mM; kcat 14.31 s^-1; kcat/Km 31.8 s^-1 mM^-1 after converting the printed M^-1 s^-1 value by dividing by 1000.

substrate: 4-nitrophenyl octadecanoate

status: verified


substrate_name: 4-nitrophenyl dodecanoate

column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C12 / MtCut, column MtCut; Km mM, raw cell 1.68 +/- 0.12, normalized 1.68 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C12 / MtCut, column MtCut; kcat s^-1, raw cell 30.52 +/- 3.63, normalized 30.52 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C12 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (1.81 +/- 0.12) x 10^4, normalized 18.1 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=1.68 normalized_unit=mM; kcat normalized_value=30.52 normalized_unit=s^-1; kcat/Km normalized_value=18.1 normalized_unit=s^-1*mM^-1

row_label: pNP-C12 / MtCut

substrate: 4-nitrophenyl dodecanoate


column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C6 / MtCut, column MtCut; Km mM, raw cell 4.61 +/- 1.04, normalized 4.61 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C6 / MtCut, column MtCut; kcat s^-1, raw cell 41.72 +/- 6.35, normalized 41.72 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C6 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (9.23 +/- 0.90) x 10^3, normalized 9.23 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=4.61 normalized_unit=mM; kcat normalized_value=41.72 normalized_unit=s^-1; kcat/Km normalized_value=9.23 normalized_unit=s^-1*mM^-1

row_label: pNP-C6 / MtCut


substrate_name: 4-nitrophenyl decanoate

column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C10 / MtCut, column MtCut; Km mM, raw cell 4.93 +/- 0.53, normalized 4.93 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C10 / MtCut, column MtCut; kcat s^-1, raw cell 69.85 +/- 5.15, normalized 69.85 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C10 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (1.42 +/- 0.05) x 10^4, normalized 14.2 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=4.93 normalized_unit=mM; kcat normalized_value=69.85 normalized_unit=s^-1; kcat/Km normalized_value=14.2 normalized_unit=s^-1*mM^-1

row_label: pNP-C10 / MtCut

substrate: 4-nitrophenyl decanoate


substrate_name: 4-nitrophenyl octanoate

column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C8 / MtCut, column MtCut; Km mM, raw cell 2.55 +/- 0.28, normalized 2.55 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C8 / MtCut, column MtCut; kcat s^-1, raw cell 79.39 +/- 8.75, normalized 79.39 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C8 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (3.11 +/- 0.005) x 10^4, normalized 31.1 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=2.55 normalized_unit=mM; kcat normalized_value=79.39 normalized_unit=s^-1; kcat/Km normalized_value=31.1 normalized_unit=s^-1*mM^-1

row_label: pNP-C8 / MtCut

substrate: 4-nitrophenyl octanoate


enzyme_display_name: cocaine esterase

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

substrate_name: cocaine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9L9D7 and applied mutation signature S117C to reconstruct the assayed variant sequence.

mutation_type: substitution

column_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'S117C'; column 'kcat (s^-1)' = 0.046; column 'KM (uM)' = 46; column 'kcat/KM (s^-1 M^-1)' = 1.0 x 10^3.

normalized_value_unit_evidence: kcat: printed cell 0.046 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 0.046 s^(-1). KM: printed cell 46 uM; 1 uM is 0.001 mM, so 46 / 1000 = 0.046 mM. kcat/KM: printed cell 1.0 x 10^3 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 1.0 x 10^3 / 1000 = 1.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 0.046 / 0.046 = 1.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'S117C' measured on cocaine: kcat = 0.046 s^-1; KM = 46 uM; printed kcat/KM = 1.0 x 10^3 s^-1 M^-1.

row_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'S117C', measured on cocaine

table_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE (Biochemistry 2002, volume 41, pages 12297-12307); printed column heads CocE mutant, kcat (s^-1), KM (uM) and kcat/KM (s^-1 M^-1)

enzyme: cocaine esterase

substrate: cocaine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9L9D7 and applied mutation signature F408A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'F408A'; column 'kcat (s^-1)' = 0.057; column 'KM (uM)' = 5.1; column 'kcat/KM (s^-1 M^-1)' = 1.1 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 0.057 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 0.057 s^(-1). KM: printed cell 5.1 uM; 1 uM is 0.001 mM, so 5.1 / 1000 = 0.0051 mM. kcat/KM: printed cell 1.1 x 10^4 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^4 / 1000 = 11.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 0.057 / 0.0051 = 11.176470588235293 s^-1 mM^-1.

raw_value_unit_evidence: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'F408A' measured on cocaine: kcat = 0.057 s^-1; KM = 5.1 uM; printed kcat/KM = 1.1 x 10^4 s^-1 M^-1.

row_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'F408A', measured on cocaine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9L9D7 and applied mutation signature L407A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'L407A'; column 'kcat (s^-1)' = 0.067; column 'KM (uM)' = 1.2; column 'kcat/KM (s^-1 M^-1)' = 5.6 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 0.067 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 0.067 s^(-1). KM: printed cell 1.2 uM; 1 uM is 0.001 mM, so 1.2 / 1000 = 0.0012 mM. kcat/KM: printed cell 5.6 x 10^4 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 5.6 x 10^4 / 1000 = 56.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 0.067 / 0.0012 = 55.83333333333334 s^-1 mM^-1.

raw_value_unit_evidence: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'L407A' measured on cocaine: kcat = 0.067 s^-1; KM = 1.2 uM; printed kcat/KM = 5.6 x 10^4 s^-1 M^-1.

row_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'L407A', measured on cocaine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9L9D7 and applied mutation signature W151A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'W151A'; column 'kcat (s^-1)' = 0.10; column 'KM (uM)' = 51; column 'kcat/KM (s^-1 M^-1)' = 2.0 x 10^3.

normalized_value_unit_evidence: kcat: printed cell 0.10 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 0.1 s^(-1). KM: printed cell 51 uM; 1 uM is 0.001 mM, so 51 / 1000 = 0.051 mM. kcat/KM: printed cell 2.0 x 10^3 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 2.0 x 10^3 / 1000 = 2.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 0.1 / 0.051 = 1.9607843137254903 s^-1 mM^-1.

raw_value_unit_evidence: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'W151A' measured on cocaine: kcat = 0.10 s^-1; KM = 51 uM; printed kcat/KM = 2.0 x 10^3 s^-1 M^-1.

row_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'W151A', measured on cocaine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9L9D7 and applied mutation signature F261A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'F261A'; column 'kcat (s^-1)' = 0.27; column 'KM (uM)' = 9.6; column 'kcat/KM (s^-1 M^-1)' = 2.8 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 0.27 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 0.27 s^(-1). KM: printed cell 9.6 uM; 1 uM is 0.001 mM, so 9.6 / 1000 = 0.0096 mM. kcat/KM: printed cell 2.8 x 10^4 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 2.8 x 10^4 / 1000 = 28.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 0.27 / 0.0096 = 28.125000000000004 s^-1 mM^-1.

raw_value_unit_evidence: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'F261A' measured on cocaine: kcat = 0.27 s^-1; KM = 9.6 uM; printed kcat/KM = 2.8 x 10^4 s^-1 M^-1.

row_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'F261A', measured on cocaine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9L9D7 and applied mutation signature W166A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'W166A'; column 'kcat (s^-1)' = 0.27; column 'KM (uM)' = 3.6; column 'kcat/KM (s^-1 M^-1)' = 7.5 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 0.27 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 0.27 s^(-1). KM: printed cell 3.6 uM; 1 uM is 0.001 mM, so 3.6 / 1000 = 0.0036 mM. kcat/KM: printed cell 7.5 x 10^4 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 7.5 x 10^4 / 1000 = 75.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 0.27 / 0.0036 = 75.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'W166A' measured on cocaine: kcat = 0.27 s^-1; KM = 3.6 uM; printed kcat/KM = 7.5 x 10^4 s^-1 M^-1.

row_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'W166A', measured on cocaine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9L9D7 and applied mutation signature Q55E to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'Q55E'; column 'kcat (s^-1)' = 0.55; column 'KM (uM)' = 0.27; column 'kcat/KM (s^-1 M^-1)' = 2.0 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 0.55 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 0.55 s^(-1). KM: printed cell 0.27 uM; 1 uM is 0.001 mM, so 0.27 / 1000 = 0.00027 mM. kcat/KM: printed cell 2.0 x 10^6 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 2.0 x 10^6 / 1000 = 2000.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 0.55 / 0.00027 = 2037.0370370370372 s^-1 mM^-1.

raw_value_unit_evidence: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'Q55E' measured on cocaine: kcat = 0.55 s^-1; KM = 0.27 uM; printed kcat/KM = 2.0 x 10^6 s^-1 M^-1.

row_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'Q55E', measured on cocaine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9L9D7 and applied mutation signature Q55A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'Q55A'; column 'kcat (s^-1)' = 1.7; column 'KM (uM)' = 0.75; column 'kcat/KM (s^-1 M^-1)' = 2.3 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 1.7 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 1.7 s^(-1). KM: printed cell 0.75 uM; 1 uM is 0.001 mM, so 0.75 / 1000 = 0.00075 mM. kcat/KM: printed cell 2.3 x 10^6 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 2.3 x 10^6 / 1000 = 2300.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 1.7 / 0.00075 = 2266.6666666666665 s^-1 mM^-1.

raw_value_unit_evidence: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'Q55A' measured on cocaine: kcat = 1.7 s^-1; KM = 0.75 uM; printed kcat/KM = 2.3 x 10^6 s^-1 M^-1.

row_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'Q55A', measured on cocaine


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


substrate_name: cocaethylene

column_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'wild-type with 4 (cocaethylene)'; column 'kcat (s^-1)' = 9.4; column 'KM (uM)' = 1.6; column 'kcat/KM (s^-1 M^-1)' = 5.9 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 9.4 s^-1; the printed column head is kcat (s^-1), so no unit conversion applies and the paper value is 9.4 s^(-1). KM: printed cell 1.6 uM; 1 uM is 0.001 mM, so 1.6 / 1000 = 0.0016 mM. kcat/KM: printed cell 5.9 x 10^6 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 5.9 x 10^6 / 1000 = 5900.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 9.4 / 0.0016 = 5875.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'wild-type with 4 (cocaethylene)' measured on cocaethylene: kcat = 9.4 s^-1; KM = 1.6 uM; printed kcat/KM = 5.9 x 10^6 s^-1 M^-1.

row_label: Table 2: Kinetics of Cocaine Hydrolysis by Wild-Type and Mutant CocE, CocE mutant row 'wild-type with 4 (cocaethylene)', measured on cocaethylene

substrate: cocaethylene


organism: Pyrenopeziza brassicae

substrate_name: 4-nitrophenyl hexadecanoate

proof_lines: pH and temperature not specified in the publication

substrate: 4-nitrophenyl hexadecanoate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


organism: Alicyclobacillus acidoterrestris

substrate_name: gamma-heptanolide

proof_lines: in 2.5 mM Bicine pH 8.3, 150 mM NaCl, 0.2 mM cresol purple, 0.5% (v/v) DMSO and 0.2 mM CoCl2, at 25°C

substrate: gamma-heptanolide


substrate_name: delta-valerolactone

substrate: delta-valerolactone


substrate_name: delta-decalactone

substrate: delta-decalactone


substrate_name: N-butyryl-L-homoserine lactone

substrate: N-butyryl-L-homoserine lactone


substrate_name: gamma-butyrolactone

substrate: gamma-butyrolactone


enzyme_display_name: acetylxylan esterase

organism: Aspergillus nidulans

enzyme: acetylxylan esterase


substrate_name: 4-methylumbelliferyl acetate

substrate: 4-methylumbelliferyl acetate


enzyme_display_name: feruloyl esterase

organism: Bacillus pumilus

substrate_name: methyl sinapate

enzyme: feruloyl esterase

substrate: methyl sinapate


substrate_name: methyl caffeate

substrate: methyl caffeate


substrate_name: methyl ferulate

substrate: methyl ferulate


substrate_name: methyl 4-coumarate

substrate: methyl 4-coumarate


organism: Thermobifida cellulosilytica

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L183A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7


substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


enzyme_display_name: UniProt E9LVH9

source_db: skid

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

proof_lines: kcat is 2.4 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (Ref.1). kcat is 17 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (PubMed:23592055). kcat is 5.3 sec(-1) with pNP-butanoate as subst

source_databases_merged: skid uniprot

enzyme: UniProt E9LVH9

source: skid


organism: uncultured microorganism

proof_lines:
pH 6.5, 18°C, immobilized enzyme
pH 6.5, 18°C, soluble enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G173Q to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme G173Q, at pH 7.4 and 37°C
ph 7.4, 37°C, mutant enzyme G173Q


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T172R with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme T172R, at pH 7.4 and 37°C
ph 7.4, 37°C, mutant enzyme T172R


sequence_variant_note: Mutation signature T172R/G13Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme T172R/G13Q, at pH 7.4 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L169K to reconstruct the assayed variant sequence.


organism: Klebsiella sp.

substrate_name: deltamethrin

proof_lines: kcat is 1.05 sec(-1) with cis-permethrin as substrate. kcat is 1.14 sec(-1) with trans-permethrin as substrate. kcat is 0.288 sec(-1) with cypermethrin as substrate. kcat is 0.103 sec(-1) with fenvalerate as substrate. kcat is 0.016 sec(-1)

substrate: deltamethrin


substrate_name: fenvalerate

substrate: fenvalerate


substrate_name: malathion

smiles: CCOC(=O)CC(C(=O)OCC)SP(=S)(OC)OC

substrate: malathion


substrate_name: cypermethrin

substrate: cypermethrin


substrate_name: cis-permethrin

substrate: cis-permethrin


enzyme_display_name: Cutinase 1

organism: Fusarium vanettenii

substrate_name: p-nitrophenyl acetate (at pH 7.5)

source_db: uniprot

assay_conditions_summary: pH 9

proof_lines: kcat is 1800 sec(-1) with p-nitrophenyl butyrate as substrate (at pH 9 and 30 degrees Celsius).

enzyme: Cutinase 1

substrate: p-nitrophenyl acetate (at pH 7.5)

source: uniprot


substrate_name: p-nitrophenyl valerate (at pH 7.5)

substrate: p-nitrophenyl valerate (at pH 7.5)


substrate_name: p-nitrophenyl hexanoate (at pH 7.5)

substrate: p-nitrophenyl hexanoate (at pH 7.5)


enzyme_display_name: Cocaine esterase

organism: Homo sapiens

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

proof_lines: kcat is 43 min(-1), 49 min(-1), 150 min(-1) with 2-arachidonoylglycerol, prostaglandin F2alpha 1-glyceryl ester and prostaglandin E2 1-glyceryl ester as substrates, respectively.

enzyme: Cocaine esterase


substrate_name: prostaglandin E2 1-glyceryl ester

substrate: prostaglandin E2 1-glyceryl ester


substrate_name: prostaglandin F2alpha 1-glyceryl ester

substrate: prostaglandin F2alpha 1-glyceryl ester


substrate_name: heroin

substrate: heroin


substrate_name: (-)-cocaine

substrate: (-)-cocaine


enzyme_display_name: pheophorbidase

organism: Raphanus sativus

substrate_name: pheophorbide a

assay_conditions_summary: pH 7; buffer 20 mM phosphate

column_label: Results prose gives exact Type 1 value 14.1 uM and Table II row Pheid a anchors the Type 1/Type 2 columns under uM units.

normalized_value_unit_evidence: 14.1 uM normalizes to 0.0141 mM.

raw_value_unit_evidence: Results prose reports Pheid a Km values 14.1 and 15.1 uM for types 1 and 2; Table II rounds Type 1 to 14 uM.

row_label: Pheid a; Type 1 Km

table_label: Results prose and Table II, Substrate specificity of PPD types 1 and 2 from cotyledons of radish

enzyme: pheophorbidase

substrate: pheophorbide a


substrate_name: bacteriopheophorbide a

column_label: Table II row Bacterio-Pheid a, Type 2 Km column; unit line is uM.

normalized_value_unit_evidence: 37 uM normalizes to 0.037 mM.

raw_value_unit_evidence: Table II reports Bacterio-Pheid a Type 2 Km 37 uM.

row_label: Bacterio-Pheid a; Type 2 Km column

table_label: Table II, Substrate specificity of PPD types 1 and 2 from cotyledons of radish

substrate: bacteriopheophorbide a


substrate_name: pheophorbide b

column_label: Table II row Pheid b, Type 2 Km column; unit line is uM.

normalized_value_unit_evidence: 232 uM normalizes to 0.232 mM.

raw_value_unit_evidence: Table II reports Pheid b Type 2 Km 232 uM.

row_label: Pheid b; Type 2 Km column

substrate: pheophorbide b


enzyme_display_name: Pimeloyl-[acyl-carrier protein] methyl ester esterase

organism: Escherichia coli (strain K12)

substrate_name: DMB-S-MMP (at Ph 7.9 and at room temperature)

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

proof_lines: The highest catalytic efficiency was observed with pNP-acetate, then with pNP-propionate, pNP-butyrate and pNP-caproate.


substrate_name: pNP-acetate

enzyme: Pimeloyl-[acyl-carrier protein] methyl ester esterase

substrate: pNP-acetate


substrate_name: pNP-propionate

substrate: pNP-propionate


substrate_name: pNP-butyrate

substrate: pNP-butyrate


enzyme_display_name: Pyrethroid hydrolase Ces2e

organism: Mus musculus

substrate_name: p-Nitrophenyl acetate

proof_lines: kcat is 94 sec(-1) with p-Nitrophenyl acetate as substrate. kcat is 0.12 sec(-1) with cypermethrin as substrate. kcat is 0.11 sec(-1) with (R/S)-alpha-cyano(6-methoxy-2-naphthyl)-methyl-(R/S)-trans/cis-3-(2,2-dichlorovinyl)-2,2-dimethylcycl

enzyme: Pyrethroid hydrolase Ces2e

substrate: p-Nitrophenyl acetate


substrate_name: cypermethrin


substrate_name: chrysanthemic acid

substrate: chrysanthemic acid


enzyme_display_name: Acetylxylan esterase

organism: Geobacillus stearothermophilus

substrate_name: phenyl acetate (at pH 6.0 and 30 degrees Celsius)

assay_conditions_summary: pH 6

proof_lines: kcat is 77 sec(-1) with phenyl acetate as substrate. kcat is 190 sec(-1) with 2-naphtyl acetate as substrate. kcat is 123 sec(-1) with 4-methylumbelliferyl acetate as substrate. kcat is 31 sec(-1) with 4-nitrophenyl acetate as substrate (at

enzyme: Acetylxylan esterase


substrate_name: 4-methylumbelliferyl acetate (at pH 6.0 and 30 degrees Celsius)


substrate_name: 4-nitrophenyl acetate (at pH 6.0 and 30 degrees Celsius)


proof_lines: wild type enzyme, pH not specified in the publication, at 25°C

proof_lines: wild type enzyme, at 25°C, in 0.1 M potassium phosphate, pH 7.5


sequence_variant_note: Mutation signature A199S/F227A/S287G/A328W/E441D could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme A199S/F227A/S287G/A328W/E441D, pH not specified in the publication, at 25°C


sequence_variant_note: Mutation signature A199S/F227A/S287G/A328W/Y332G/E441D could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme A199S/F227A/S287G/A328W/Y332G/E441D, pH not specified in the publication, at 25°C


organism: Aspergillus oryzae

substrate_name: 2-naphthyl acetate

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

substrate: 2-naphthyl acetate


substrate_name: 2-naphthyl propionate

substrate: 2-naphthyl propionate


organism: Aspergillus awamori

substrate_name: 1-naphthyl acetate

km_display: Not reported

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S146A to reconstruct the assayed variant sequence.

proof_lines: substrate: alpha-naphthylacetate, mutant enzyme S146A

substrate: 1-naphthyl acetate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D168A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

proof_lines: substrate: alpha-naphthylacetate, mutant enzyme D168A


organism: Caulobacter vibrioides

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

proof_lines: pH and temperature not specified in the publication


organism: Volvariella volvacea

substrate_name: 4-methylumbelliferyl acetate

proof_lines:
wild-type, 50°C, pH 8.0
wild-type lacking CBM1, 50°C, pH 8.0

substrate: 4-methylumbelliferyl acetate


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

proof_lines: mutant carrying a replacement of CBM1 with CBM6, pH 8.0, 50°C

proof_lines: mutant carrying a replacement of CBM1 with CBM22-2, pH 8.0, 50°C

proof_lines: mutant carrying a replacement of CBM1 with CBM4-2, pH 8.0, 50°C


organism: Evansstolkia leycettana

substrate_name: 4-nitrophenyl acetate

column_label: Table 2 columns Protein, Km (mM), Vmax (umol min^-1 mg^-1), kcat (s^-1), and kcat/Km (s^-1 mM^-1); row AXE + CBM1.

normalized_value_unit_evidence: kcat 306 s^-1, Km 0.5 mM, and kcat/Km 612 s^-1*mM^-1 match the export.

row_label: AXE + CBM1

table_label: Table 2: Kinetic values of acetyl xylan esterase and xylanase

substrate: 4-nitrophenyl acetate


column_label: Table 2 columns Protein, Km (mM), Vmax (umol min^-1 mg^-1), kcat (s^-1), and kcat/Km (s^-1 mM^-1); row AXE.

normalized_value_unit_evidence: kcat 326 s^-1 and Km 0.72 mM match the export; explicit table kcat/Km is 453 s^-1*mM^-1, matching the exported 452.77777777777777 as the table-rounded 326/0.72 ratio.

row_label: AXE


enzyme_display_name: Acetylxylan esterase / glucomannan deacetylase

organism: Cellvibrio japonicus (strain Ueda107)

column_label: Table 1; row CjCE2B; column KM (uM)

raw_value_unit_evidence: Table 1 row CjCE2B column KM (uM) raw value 262 uM

table_label: Table 1 Catalytic Activity of CE2 Enzymes against 4-Nitrophenyl Acetate (4-NPAc)


column_label: Table 1; row CjCE2A; column KM (uM)

raw_value_unit_evidence: Table 1 row CjCE2A column KM (uM) raw value 339 uM

enzyme: Acetylxylan esterase / glucomannan deacetylase


enzyme_display_name: UniProt P52956

substrate_name: 4-nitrophenyl valerate

proof_lines: kcat is 11 sec(-1) with p-nitrophenyl propionate as substrate (at pH 8.0 and 37 degrees Celsius) (PubMed:15968570). kcat is 18 sec(-1) with p-nitrophenyl butyrate as substrate (at pH 8.0 and 37 degrees Celsius) (PubMed:15968570). kcat is 14

enzyme: UniProt P52956

substrate: 4-nitrophenyl valerate


substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40)

substrate_name: p-nitrophenyl acetate (at pH 7.5)

column_label: Official PMC full text PMID 19810726, Table 1 Kinetic and Thermodynamic Parameters and kinetic analysis prose

raw_value_unit_evidence: A. oryzae pNPA Km = 4.96 +/- 0.11 uM

row_label: A. oryzae cutinase; pNPA column

table_label: Official PMC full text Table 1 Kinetic and Thermodynamic Parameters

substrate: p-nitrophenyl acetate (at pH 7.5)


substrate_name: p-nitrophenyl hexanoate (at pH 7.5)

raw_value_unit_evidence: A. oryzae pNPH Km = 0.29 +/- 0.09 uM

row_label: A. oryzae cutinase; pNPH column

substrate: p-nitrophenyl hexanoate (at pH 7.5)


organism: Coprinopsis cinerea


enzyme_display_name: fatty-acyl-ethyl-ester synthase

organism: Rattus norvegicus

substrate_name: oleic acid

smiles: CCCCCCCCC=CCCCCCCCC(=O)O

proof_lines: kcat is 0.22 min(-1) with retinyl palmitate as substrate.

enzyme: fatty-acyl-ethyl-ester synthase

substrate: oleic acid


substrate_name: ethanol

smiles: CCO

substrate: ethanol


enzyme_display_name: Cutinase est2

organism: Thermobifida alba

substrate_name: pNP-acetate (at 37 degrees Celsius and pH 7)

proof_lines: kcat is 2.06 sec(-1) with pNP-acetate as substrate (at 37 degrees Celsius and pH 7) (PubMed:22183084). kcat is 4.48 sec(-1) with pNP-butyrate as substrate (at 37 degrees Celsius and pH 7) (PubMed:22183084). kcat is 3.28 sec(-1) with pNP-hex

enzyme: Cutinase est2


substrate_name: pNP-butyrate (at 37 degrees Celsius and pH 7)

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


substrate_name: oleate

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

proof_lines: pH 7.4, 37°C, 180 kDa high molecular weight protein from liver microsomes

substrate: oleate


organism: Thermobifida cellulosilytica

substrate_name: 4-nitrophenyl butanoate

proof_lines:
fusion protein Cut1-HFB9b, pH 7.0, 25°C
fusion protein Cut1-HFB4, pH 7.0, 25°C
fusion protein Cut1-HFB7, pH 7.0, 25°C

source_databases_merged: brenda skid

substrate: 4-nitrophenyl butanoate


proof_lines:
fusion protein Cut1-HFB4, pH 7.0, 25°C
fusion protein Cut1-HFB9b, pH 7.0, 25°C
fusion protein Cut1-HFB7, pH 7.0, 25°C

source_databases_merged: brenda skid uniprot


organism: Haloferax volcanii

proof_lines:
pH 7.5, 42°C, recombinant enzyme
pH 7.5, 42°C


enzyme_display_name: Carboxylesterase 1D

substrate_name: retinyl palmitate

column_label: PMID 12230550 Table 5, ES10 row, retinyl palmitate Km = 1.16 +/- 0.12 uM.

raw_value_unit_evidence: Table 5 reports ES10 Km = 1.16 +/- 0.12 uM for retinyl palmitate hydrolysis.

row_label: ES10 retinyl palmitate hydrolysis

table_label: Table 5. Kinetic constants for retinyl palmitate hydrolysis by rat liver carboxylesterases

enzyme: Carboxylesterase 1D

substrate: retinyl palmitate


enzyme_display_name: Cellulase/esterase CelE

organism: Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)

column_label: Table 1; row CtCE2; column KM (uM)

raw_value_unit_evidence: Table 1 row CtCE2 column KM (uM) raw value 165 uM

enzyme: Cellulase/esterase CelE


organism: Alicyclobacillus acidoterrestris

substrate_name: N-decanoyl-L-homoserine lactone

assay_conditions_summary: pH 8.3; buffer setup

proof_lines: in 2.5 mM Bicine pH 8.3, 150 mM NaCl, 0.2 mM cresol purple, 0.5% (v/v) DMSO and 0.2 mM CoCl2, at 25°C

substrate: N-decanoyl-L-homoserine lactone


substrate_name: N-hexanoyl-L-homoserine lactone

substrate: N-hexanoyl-L-homoserine lactone


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


organism: Fibrobacter succinogenes

substrate_name: Alpha-naphthyl acetate

proof_lines: pH 6.5, 37°C, acetylxylan esterase Axe6B

proof_lines: pH 6.5, 37°C, acetylxylan esterase Axe6A

substrate: Alpha-naphthyl acetate


organism: Thermobacillus xylanilyticus

substrate_name: ethyl ferulate

substrate: ethyl ferulate


enzyme_display_name: Cutinase 2

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

substrate_name: p-nitrophenyl acetate (at pH 9 and 37 degrees Celsius)

proof_lines: kcat is 242 sec(-1) with p-nitrophenyl acetate as substrate (at pH 9 and 37 degrees Celsius).

enzyme: Cutinase 2


substrate_name: p-nitrophenyl propionate (at pH 8.0 and 37 degrees Celsius)


enzyme_display_name: Peptidoglycan deacetylase

organism: Helicobacter pylori (strain ATCC 700392 / 26695)

substrate_name: pNP-acetate

proof_lines: kcat is 775 min(-1), 968 min(-1), 2549 min(-1) and 1029 min(-1) with chitin, chitosan, acetylated xylan, and pNP-acetate as substrate, respectively.

enzyme: Peptidoglycan deacetylase

substrate: pNP-acetate


enzyme_display_name: Cutinase

organism: Amycolatopsis mediterranei (strain S699)

substrate_name: p-nitrophenyl palmitate (p-NPP)

proof_lines: kcat is 1468 sec(-1) with p-nitrophenyl palmitate (p-NPP) as substrate (at pH 8.0 and 60 degrees Celsius).

enzyme: Cutinase

substrate: p-nitrophenyl palmitate (p-NPP)


enzyme_display_name: UniProt P00590

organism: Fusarium solani

substrate_name: p-nitrophenyl butyrate

proof_lines: kcat is 1800 sec(-1) with p-nitrophenyl butyrate as substrate (at pH 9 and 30 degrees Celsius).

enzyme: UniProt P00590

substrate: p-nitrophenyl butyrate


enzyme_display_name: cocaine esterase

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

substrate_name: cocaine

proof_lines: mutant enzyme T172R/G173Q/G4C/S10C, at 37°C, pH not specified in the publication

enzyme: cocaine esterase

substrate: cocaine


proof_lines: mutant enzyme T172R/G173Q/L196C/I301C, at 37°C, pH not specified in the publication


organism: Salinicola salarius

substrate_name: N-(3-oxooctanoyl)-L-homoserine lactone

proof_lines: enzyme-based hybrid nanoflower, pH 8.0, 30°C

substrate: N-(3-oxooctanoyl)-L-homoserine lactone


enzyme_display_name: Cutinase cut2

organism: Thermobifida fusca

substrate_name: pNP-acetate (at 25 degrees Celsius and pH 7)

proof_lines: kcat is 39.5 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (Ref.5). kcat is 253 sec(-1) with pNP-butanoate as substrate (at 50 degrees Celsius and pH 8) (PubMed:23604968). kcat is 30.9 sec(-1) with pNP-butanoate as

enzyme: Cutinase cut2


organism: Homo sapiens

substrate_name: (-)-cocaine

proof_lines: mutant enzyme A199S/S287G/A328W/Y332G, at 25°C, in 0.1 M potassium phosphate, pH 7.5

proof_lines: mutant enzyme A199S/S287G/A328W/Y332G, pH not specified in the publication, at 25°C

proof_lines: mutant enzyme A199S/S287G/A328W/Y332G, at pH 7.4 and 25°C

substrate: (-)-cocaine


proof_lines:
pH 7.5, 30°C
Raw SKiD Env: Temp=-----, pH=7.4
Raw SKiD Env: Temp=37°C, pH=7.4


enzyme_display_name: Cocaine esterase

substrate_name: 4-methylumbelliferyl acetate

proof_lines: kcat is 43 min(-1), 49 min(-1), 150 min(-1) with 2-arachidonoylglycerol, prostaglandin F2alpha 1-glyceryl ester and prostaglandin E2 1-glyceryl ester as substrates, respectively.

enzyme: Cocaine esterase

substrate: 4-methylumbelliferyl acetate


enzyme_display_name: UniProt Q9L9D7

organism: Rhodococcus sp.

substrate_name: cocaethylene

enzyme: UniProt Q9L9D7

substrate: cocaethylene


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L169K/G173Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L169K/G173Q, after 24 h preincubation at 37°C, at pH 7.4 and 37°C

proof_lines: mutant enzyme L169K/G173Q, without preincubation, at pH 7.4 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T172R/G173Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T172R/G173Q -YGRKKRRQRRR, at pH 7.4 and 37°C

proof_lines: mutant enzyme YGRKKRRQRRR-T172R/G173Q, at pH 7.4 and 37°C

proof_lines: mutant enzyme LMWP-T172R/G173Q, at pH 7.4 and 37°C


enzyme_display_name: cutinase

organism: Sirococcus conigenus

substrate_name: 4-nitrophenyl butyrate

enzyme: cutinase

substrate: 4-nitrophenyl butyrate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G4C/S10C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme G4C/S10C, pH not specified in the publication, 37°C


enzyme_display_name: feruloyl esterase

organism: Aspergillus awamori

substrate_name: H2O; 1-Naphthylbutanoic acid

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

enzyme: feruloyl esterase

substrate: H2O; 1-Naphthylbutanoic acid


enzyme_display_name: UniProt O42807

organism: Aspergillus niger

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=40°C, pH=6

enzyme: UniProt O42807


substrate_name: n-decyl ferulate

substrate: n-decyl ferulate


enzyme_display_name: Feruloyl esterase B

organism: Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799)

enzyme: Feruloyl esterase B


organism: Fusarium vanettenii

substrate_name: H2O; p-Nitrophenyl butyrate

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

substrate: H2O; p-Nitrophenyl butyrate


organism: Saccharomonospora viridis


enzyme_display_name: poly(3-hydroxybutyrate) depolymerase

organism: Burkholderia pickettii

substrate_name: H2O; Poly[(R)-3-hydroxybutanoate]n

enzyme: poly(3-hydroxybutyrate) depolymerase

substrate: H2O; Poly[(R)-3-hydroxybutanoate]n


organism: Halobacterium volcanii

substrate_name: H2O; D-Xylonolactone

substrate: H2O; D-Xylonolactone


enzyme_display_name: Acetylxylan esterase

organism: Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)

substrate_name: 4-nitrophanyl acetate

enzyme: Acetylxylan esterase

substrate: 4-nitrophanyl acetate


enzyme_display_name: acetylxylan esterase

organism: Neocallimastix patriciarum

substrate_name: birchwood xylan

enzyme: acetylxylan esterase

substrate: birchwood xylan


enzyme_display_name: Lipase A

organism: Sodiomyces alcalophilus

substrate_name: p-nitrophenol caprylate

enzyme: Lipase A

substrate: p-nitrophenol caprylate


enzyme_display_name: Cephalosporin-C deacetylase

organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

substrate_name: p-nitrophenyl-acetate

enzyme: Cephalosporin-C deacetylase

substrate: p-nitrophenyl-acetate


organism: Volvariella volvacea

substrate_name: 4-yethylumbelliferyl acetate

substrate: 4-yethylumbelliferyl acetate


organism: Bacillus sp.


organism: Bacillus thuringiensis

substrate_name: N-Hexanoyl-L-homoserine lactone; H2O

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

source_databases_merged: sabio_rk skid uniprot

substrate: N-Hexanoyl-L-homoserine lactone; H2O


enzyme_display_name: UniProt I7HB71

organism: Chryseobacterium sp. StRB126

substrate_name: N-3-oxooctanoyl-L-homoserine lactone

enzyme: UniProt I7HB71

substrate: N-3-oxooctanoyl-L-homoserine lactone


enzyme_display_name: Pheophorbidase

organism: Raphanus sativus

substrate_name: bacterio-pheophorbide a (for the native enzyme)

enzyme: Pheophorbidase


organism: Homo sapiens

substrate_name: Cocaine; H2O

substrate: Cocaine; H2O


enzyme_display_name: pyrethroid hydrolase

organism: Rhodopseudomonas palustris

substrate_name: H2O; Fenpropathrin

enzyme: pyrethroid hydrolase

substrate: H2O; Fenpropathrin


enzyme_display_name: Carboxylesterase 1D

organism: Rattus norvegicus

substrate_name: Unknown

proof_lines: kcat is 0.22 min(-1) with retinyl palmitate as substrate.

enzyme: Carboxylesterase 1D

substrate: Unknown


enzyme_display_name: Cellulase/esterase CelE

organism: Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)

substrate_name: acetylated birchwood xylan

proof_lines: kcat is 7032 min(-1) for the deacetylation of 4-nitrophenyl acetate. kcat is 12 min(-1) for the deacetylation of birchwood xylan. kcat is 1.1 min(-1) for the deacetylation of glucomannan.

enzyme: Cellulase/esterase CelE

substrate: acetylated birchwood xylan


organism: Aspergillus awamori

proof_lines: substrate: alpha-naphthylacetate, mutant enzyme S146A


proof_lines: substrate: alpha-naphthylacetate, mutant enzyme D168A


enzyme_display_name: Acetylxylan esterase / glucomannan deacetylase

organism: Cellvibrio japonicus (strain Ueda107)

proof_lines: kcat is 49820 min(-1) for the deacetylation of 4-nitrophenyl acetate. kcat is 66 min(-1) for the deacetylation of birchwood xylan. kcat is 1348 min(-1) for the deacetylation of glucomannan.


proof_lines: kcat is 7717 min(-1) for the deacetylation of 4-nitrophenyl acetate. kcat is 69 min(-1) for the deacetylation of birchwood xylan. kcat is 163 min(-1) for the deacetylation of glucomannan.

enzyme: Acetylxylan esterase / glucomannan deacetylase


organism: Fibrobacter succinogenes subsp. succinogenes S85

substrate_name: tetraacetyl-xylopyranoside

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D270N with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 310.15 K; buffer 100 mM Tris-HCl

proof_lines: mutant D270N, at 37°C, in 100 mM Tris-HCl buffer, pH 7.4, and 3 mM MgCl2

substrate: tetraacetyl-xylopyranoside


organism: Geobacillus stearothermophilus

substrate_name: 2-naphtyl acetate (at pH 6.0 and 30 degrees Celsius)

proof_lines: kcat is 77 sec(-1) with phenyl acetate as substrate. kcat is 190 sec(-1) with 2-naphtyl acetate as substrate. kcat is 123 sec(-1) with 4-methylumbelliferyl acetate as substrate. kcat is 31 sec(-1) with 4-nitrophenyl acetate as substrate (at


organism: Helicobacter pylori

substrate_name: acetylated Xylan; H2O

proof_lines: kcat is 775 min(-1), 968 min(-1), 2549 min(-1) and 1029 min(-1) with chitin, chitosan, acetylated xylan, and pNP-acetate as substrate, respectively.

substrate: acetylated Xylan; H2O


substrate_name: alpha-naphthylcaprylate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D71I with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

substrate: alpha-naphthylcaprylate


organism: Aspergillus usamii

substrate_name: ferulic acid 4-nitrophenyl ester

substrate: ferulic acid 4-nitrophenyl ester


sequence_variant_note: Mutation signature A126C/N152C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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

proof_lines: mutant E194N, at 37°C, in 100 mM Tris-HCl buffer, pH 7.4, and 3 mM MgCl2


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

proof_lines: mutants E194A, D270N and D270A, at 37°C, in 100 mM Tris-HCl buffer, pH 7.4, and 3 mM MgCl2


proof_lines: wild-type and mutant TM1, at 37°C, in 100 mM Tris-HCl buffer, pH 7.4, and 3 mM MgCl2

proof_lines: wild-type, at 37°C, in 100 mM Tris-HCl buffer, pH 7.4, and 3 mM MgCl2

proof_lines: wild-type and mutant TM2, at 37°C, in 100 mM Tris-HCl buffer, pH 7.4, and 3 mM MgCl2


proof_lines: mutant TM2, at 37°C, in 100 mM Tris-HCl buffer, pH 7.4, and 3 mM MgCl2

proof_lines: mutant TM1, at 37°C, in 100 mM Tris-HCl buffer, pH 7.4, and 3 mM MgCl2


sequence_variant_note: Mutation signature E194A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant E194A, at 37°C, in 100 mM Tris-HCl buffer, pH 7.4, and 3 mM MgCl2


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D270A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant D270A, at 37°C, in 100 mM Tris-HCl buffer, pH 7.4, and 3 mM MgCl2


organism: Sphingobium wenxiniae

substrate_name: trans-Permethrin; H2O

assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM sodium phosphate

column_label: TABLE 1: Kinetic constants determined for the purified recombinant PytH (Appl. Environ. Microbiol. 2009, 75(17):5496-5500). Column heads, in printed order: 'Substrate'; 'Sp act (umol/min/mg)'; 'kcat (s^-1)'; 'Km (uM)'; 'kcat/Km (uM^-1 . s^-1)', all under the banner head 'Mean +/- SD'. The line read here is the one whose substrate label is 'trans-Permethrin': its Sp act cell, its kcat cell 3.03, its Km cell 0.062 and its kcat/Km cell 48.90 sit at the four fixed character columns of the rendering, so each number belongs to the head above it.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.03 s^-1; the printed unit is already the canonical one, so no unit conversion applies; normalized 3.03 s^(-1). Km: printed Table 1 cell 0.062 uM; 0.062 / 1000 = 0.000062 mM. kcat/Km: printed Table 1 cell 48.90 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 48.90 x 1000 = 48900.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, line 'trans-Permethrin': kcat column (s^-1) = 3.03; Km column (uM) = 0.062; printed kcat/Km column (uM^-1 s^-1) = 48.90.

row_label: Table 1 line 'trans-Permethrin'

substrate: trans-Permethrin; H2O


enzyme_display_name: Feruloyl esterase 1

organism: Penicillium parvum

enzyme: Feruloyl esterase 1


enzyme_display_name: Cutinase

organism: Amycolatopsis mediterranei (strain S699)

proof_lines: kcat is 1468 sec(-1) with p-nitrophenyl palmitate (p-NPP) as substrate (at pH 8.0 and 60 degrees Celsius).

enzyme: Cutinase


enzyme_display_name: cutinase

organism: Fusarium solani

substrate_name: p-nitrophenyl butyrate

proof_lines: T179C mutant, sodium dioctyl sulfosuccinate concentration = 0 mM

proof_lines: T179C mutant, sodium dioctyl sulfosuccinate concentration = 1.5 mM

proof_lines: T179C mutant, sodium dioctyl sulfosuccinate concentration = 1 mM

enzyme: cutinase

substrate: p-nitrophenyl butyrate


ki_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T179C with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


organism: Thermobifida alba

substrate_name: p-Nitrophenyl acetate; H2O

proof_lines: kcat is 2.06 sec(-1) with pNP-acetate as substrate (at 37 degrees Celsius and pH 7) (PubMed:22183084). kcat is 4.48 sec(-1) with pNP-butyrate as substrate (at 37 degrees Celsius and pH 7) (PubMed:22183084). kcat is 3.28 sec(-1) with pNP-hex

substrate: p-Nitrophenyl acetate; H2O


organism: Thermobifida cellulosilytica

substrate_name: H2O; p-Nitrophenyl acetate

proof_lines: kcat is 2.4 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (Ref.1). kcat is 17 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (PubMed:23592055). kcat is 5.3 sec(-1) with pNP-butanoate as subst

substrate: H2O; p-Nitrophenyl acetate


proof_lines: kcat is 211.9 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (Ref.1). kcat is 436 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (PubMed:23592055). kcat is 195.1 sec(-1) with pNP-butanoate as


organism: Thermobifida fusca

substrate_name: H2O; p-Nitrophenyl butyrate

proof_lines: kcat is 220 sec(-1) with pNP-butanoate as substrate (PubMed:20729325). kcat is 304 sec(-1) with pNP-butanoate as substrate (at 20 degrees Celsius and pH 8) (PubMed:23603671).

proof_lines: kcat is 39.5 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (Ref.5). kcat is 253 sec(-1) with pNP-butanoate as substrate (at 50 degrees Celsius and pH 8) (PubMed:23604968). kcat is 30.9 sec(-1) with pNP-butanoate as

substrate: H2O; p-Nitrophenyl butyrate


substrate_name: p-Nitrophenyl butyrate; H2O

proof_lines: kcat is 178 sec(-1) for the hydrolysis of pNP-butanoate (at 50 degrees Celsius and pH 8).

substrate: p-Nitrophenyl butyrate; H2O


enzyme_display_name: Leaf-branch compost cutinase

organism: Unknown prokaryotic organism

substrate_name: pNP-butanoate (at 30 degrees Celsius and pH 8.0)

proof_lines: kcat is 232 sec(-1) with pNP-butanoate as substrate (at 30 degrees Celsius and pH 8.0). kcat is 343 sec(-1) with pNP-butanoate as substrate (at 50 degrees Celsius and pH 8.0). kcat is 318 sec(-1) with pNP-butanoate as substrate (at 70 degre

enzyme: Leaf-branch compost cutinase


enzyme_display_name: hormone-sensitive lipase

organism: Halalkalibacterium halodurans

substrate_name: 4-nitrophenyl palmitate

source_db: oed

enzyme: hormone-sensitive lipase

substrate: 4-nitrophenyl palmitate

source: oed


enzyme_display_name: Monoacylglycerol lipase ABHD2

organism: Homo sapiens

enzyme: Monoacylglycerol lipase ABHD2


enzyme_display_name: Hormone-sensitive lipase

organism: Rattus norvegicus

enzyme: Hormone-sensitive lipase


organism: Alicyclobacillus acidoterrestris

substrate_name: 3-oxo-dodecanoyl-L-homoserine lactone

sequence: MTVERVYLLPAGNCLVDQSV

proof_lines: in 2.5 mM Bicine pH 8.3, 150 mM NaCl, 0.2 mM cresol purple, 0.5% (v/v) DMSO and 0.2 mM CoCl2, at 25°C

substrate: 3-oxo-dodecanoyl-L-homoserine lactone


organism: Chryseobacterium sp. StRB126

substrate_name: N-3-oxooctanoyl-L-homoserine lactone

sequence: MYNKKYQTKRTQITRIFILN

proof_lines: pH 7.5, temperature not specified in the publication

substrate: N-3-oxooctanoyl-L-homoserine lactone


enzyme_display_name: cocaine esterase

substrate_name: (-)-cocaine

sequence: MRLHRLRARLSAVACGLLLL

wild_type_sequence: MRLHRLRARLSAVACGLLLL

sequence_variant_note: Mutation signature F227A/S287G/A328W/Y332M references residue 227, which is outside the resolved sequence length.

proof_lines: mutant enzyme F227A/S287G/A328W/Y332M, pH not specified in the publication, at 25°C

enzyme: cocaine esterase

substrate: (-)-cocaine


sequence_variant_note: Mutation signature A328W/Y332G references residue 328, which is outside the resolved sequence length.

proof_lines: mutant enzyme A328W/Y332G, pH not specified in the publication, at 25°C


sequence_variant_note: Mutation signature A199S/F227V/S287G/A328W/Y332G references residue 199, which is outside the resolved sequence length.

proof_lines: mutant enzyme A199S/F227V/S287G/A328W/Y332G, pH not specified in the publication, at 25°C


enzyme_display_name: Pyrethroid hydrolase Ces2a

substrate_name: Unknown

proof_lines: kcat is 0.05 min(-1) with retinyl palmitate as substrate.

enzyme: Pyrethroid hydrolase Ces2a


sequence_variant_note: Mutation signature A199S/F227L/S287G/A328W/Y332G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme A199S/F227L/S287G/A328W/Y332G, pH not specified in the publication, at 25°C


sequence_variant_note: Mutation signature A199S/F227I/S287G/A328W/Y332G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme A199S/F227I/S287G/A328W/Y332G, pH not specified in the publication, at 25°C


sequence_variant_note: Mutation signature A328W/Y332A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme A328W/Y332A, pH not specified in the publication, at 25°C


enzyme_display_name: Pimeloyl-[acyl-carrier protein] methyl ester esterase

organism: Escherichia coli (strain K12)

substrate_name: pNP-caproate

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

proof_lines: The highest catalytic efficiency was observed with pNP-acetate, then with pNP-propionate, pNP-butyrate and pNP-caproate.

substrate: pNP-caproate


enzyme_display_name: Pyrethroid hydrolase Ces2e

organism: Mus musculus

proof_lines: kcat is 94 sec(-1) with p-Nitrophenyl acetate as substrate. kcat is 0.12 sec(-1) with cypermethrin as substrate. kcat is 0.11 sec(-1) with (R/S)-alpha-cyano(6-methoxy-2-naphthyl)-methyl-(R/S)-trans/cis-3-(2,2-dichlorovinyl)-2,2-dimethylcycl

enzyme: Pyrethroid hydrolase Ces2e


proof_lines: kcat is 0.27 min(-1) with retinyl palmitate as substrate.

substrate: Unknown


organism: Bacillus sp.

assay_conditions_summary: pH 7.4; 295.15 K; buffer 0.1 M phosphate

column_label: Table II row 3-HO-C4-HSL; columns kcat, Km, and kcat/Km as required by this row.

raw_value_unit_evidence: Table II row 3-HO-C4-HSL: kcat 29.30 s^-1; Km 7.51 mM; kcat/Km 3.90 mM^-1*s^-1.

table_label: Table II, Kinetic parameters of AHL-lactonase against AHLs


substrate_name: N-(3-Oxobutanoyl)-L-homoserine lactone

column_label: Table II row 3-Oxo-C4-HSL; columns kcat, Km, and kcat/Km as required by this row.

raw_value_unit_evidence: Table II row 3-Oxo-C4-HSL: kcat 28.63 s^-1; Km 4.07 mM; kcat/Km 7.03 mM^-1*s^-1.

substrate: N-(3-Oxobutanoyl)-L-homoserine lactone


substrate_name: N-(3-Oxodecanoyl)-L-homoserine lactone

column_label: Table II row 3-Oxo-C10-HSL; columns kcat, Km, and kcat/Km as required by this row.

raw_value_unit_evidence: Table II row 3-Oxo-C10-HSL: kcat 20.22 s^-1; Km 1.43 mM; kcat/Km 14.1 mM^-1*s^-1.

substrate: N-(3-Oxodecanoyl)-L-homoserine lactone


substrate_name: N-(3-Oxohexanoyl)-L-homoserine lactone

column_label: Table II row 3-Oxo-C6-HSL; columns kcat, Km, and kcat/Km as required by this row.

raw_value_unit_evidence: Table II row 3-Oxo-C6-HSL: kcat 22.68 s^-1; Km 2.95 mM; kcat/Km 7.69 mM^-1*s^-1.

substrate: N-(3-Oxohexanoyl)-L-homoserine lactone


substrate_name: N-(3-Oxooctanoyl)homoserine lactone

column_label: Table II row 3-Oxo-C8-HSL; columns kcat, Km, and kcat/Km as required by this row.

raw_value_unit_evidence: Table II row 3-Oxo-C8-HSL: kcat 22.17 s^-1; Km 2.28 mM; kcat/Km 9.72 mM^-1*s^-1.

substrate: N-(3-Oxooctanoyl)homoserine lactone


substrate_name: N-Butyryl-L-homoserine lactone

column_label: Table II row C4-HSL; columns kcat, Km, and kcat/Km as required by this row.

raw_value_unit_evidence: Table II row C4-HSL: kcat 37.63 s^-1; Km 5.11 mM; kcat/Km 7.36 mM^-1*s^-1.

substrate: N-Butyryl-L-homoserine lactone


substrate_name: N-Hexanoyl-L-homoserine lactone

column_label: Table II row C6-HSL; columns kcat, Km, and kcat/Km as required by this row.

raw_value_unit_evidence: Table II row C6-HSL: kcat 35.67 s^-1; Km 3.83 mM; kcat/Km 9.31 mM^-1*s^-1.

substrate: N-Hexanoyl-L-homoserine lactone


substrate_name: N-Octanoyl-L-homoserine lactone

column_label: Table II row C8-HSL; columns kcat, Km, and kcat/Km as required by this row.

raw_value_unit_evidence: Table II row C8-HSL: kcat 27.53 s^-1; Km 2.61 mM; kcat/Km 10.5 mM^-1*s^-1.

substrate: N-Octanoyl-L-homoserine lactone


enzyme_display_name: N-acyl homoserine lactonase

organism: Bacillus sp

assay_conditions_summary: pH 7.4; buffer 0.1 M phosphate

raw_value_unit_evidence: Table II row 3-Oxo-C6-HSL: Km 2.95 mM.

enzyme: N-acyl homoserine lactonase


raw_value_unit_evidence: Table II row 3-Oxo-C8-HSL: Km 2.28 mM.


enzyme_display_name: poly(3-hydroxybutyrate) depolymerase

organism: Cupriavidus necator

substrate_name: Poly[(R)-3-hydroxybutanoate]n-x; H2O

enzyme: poly(3-hydroxybutyrate) depolymerase

substrate: Poly[(R)-3-hydroxybutanoate]n-x; H2O


substrate_name: H2O; Poly[(R)-3-hydroxybutanoate]n

substrate: H2O; Poly[(R)-3-hydroxybutanoate]n


organism: Streptomyces sp.

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


enzyme_display_name: acyloxyacyl hydrolase

substrate_name: lipopolysaccharide

enzyme: acyloxyacyl hydrolase

substrate: lipopolysaccharide


enzyme_display_name: polyneuridine-aldehyde esterase

organism: Rauvolfia serpentina Benth. ex Kurz

substrate_name: polyneuridine aldehyde

enzyme: polyneuridine-aldehyde esterase

substrate: polyneuridine aldehyde


enzyme_display_name: N-acyl homoserine lactonase AiiB

organism: Agrobacterium fabrum (strain C58 / ATCC 33970)

substrate_name: N-butyryl-(RS)-homoserine lactone (with zinc as cofactor)

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

enzyme: N-acyl homoserine lactonase AiiB


organism: Vulcanisaeta moutnovskia

substrate_name: (S)-gamma-caprolactone

assay_conditions_summary: pH 8; 298.15 K; buffer activity/lactonase

column_label: Table 2. Enzymatic characterisation of VmoLac enzyme; row γ caprolactone (S)

normalized_value_unit_evidence: Per-metric normalized values and units are preserved in paper_metric_evidence.

raw_value_unit_evidence: Per-metric raw values and units are preserved in paper_metric_evidence; captured_primary_segment preserves the exact source transcription.

row_label: γ caprolactone (S)

substrate: (S)-gamma-caprolactone


substrate_name: undecanoic-delta-lactone

column_label: Table 2; row δ undecalactone (XXIII); columns kcat (s^-1), KM (uM), kcat/KM (M^-1 s^-1)

row_label: δ undecalactone (XXIII)

table_label: Table 2. Enzymatic characterisation of VmoLac enzyme

substrate: undecanoic-delta-lactone


substrate_name: undecanoic-gamma-lactone

column_label: Table 2; row γ undecalactone (XX); columns kcat (s^-1), KM (uM), kcat/KM (M^-1 s^-1)

row_label: γ undecalactone (XX)

substrate: undecanoic-gamma-lactone


enzyme_display_name: pyrethroid hydrolase

organism: Sphingobium sp.

proof_lines:
pyrethroid-hydrolyzing carboxylesterase
Sphingobium sp. strain JZ-1
pyrethroid pesticides

enzyme: pyrethroid hydrolase


substrate_name: (alphaR)-fenpropathrin

substrate: (alphaR)-fenpropathrin


substrate_name: (alphaS)-fenpropathrin

substrate: (alphaS)-fenpropathrin


substrate_name: bifenthrin

column_label: table label: TABLE 1. Kinetic constants determined for the purified recombinant PytH; row label: Bifenthrin; column label: the kcat (s-1) and Km (uM) cells of this one TABLE 1 row only; no cell is taken from any other row of TABLE 1 and no cell is taken from the Sp act column; raw value: kcat 0.44 ± 0.02 s-1, Km 1.586 ± 0.072 uM; raw unit: s-1 for kcat, uM for Km; normalized value: kcat 0.44 s^-1, Km 0.00159 mM, kcat/Km 276.7295597484277 s^-1 mM^-1; normalized unit: s^-1, mM, s^-1 mM^-1; condition label: All assays were performed in 50 mM sodium phosphate buffer (pH 7.5) at 37°C. Kinetic values were obtained from Lineweaver-Burk plots against various substrate concentrations. Purified recombinant PytH expressed from Sphingobium sp. strain JZ-1. Exported assay conditions: pH 7.5.

normalized_value_unit_evidence: kcat 0.44 s-1 is already s^-1, giving 0.44 s^-1 at the export's stored precision; exported kcat 0.44 s^-1. Km 1.586 uM divided by 1000 gives 0.00159 mM at the export's stored precision; exported Km 0.00159 mM. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.44 s^-1 divided by 0.00159 mM giving 276.7295597484277 s^-1 mM^-1, and of nothing else; exported kcat/Km 276.7295597484277 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 1. Kinetic constants determined for the purified recombinant PytH, row Bifenthrin: kcat 0.44 ± 0.02 s-1; Km 1.586 ± 0.072 uM; printed kcat/Km 0.27 ± 0.01 uM-1 s-1.

row_label: Bifenthrin

substrate: bifenthrin


substrate_name: cis-cypermethrin

column_label: TABLE 1, substrate row `cis-Cypermethrin`; column `Sp act (μmol/min/mg)` = 4.95 ± 0.23; column `kcat (s−1)` = 2.57 ± 0.12; column `Km (μM)` = 0.108 ± 0.004; column `kcat/Km (μM−1·s−1)` = 23.87 ± 1.11.

normalized_value_unit_evidence: kcat: printed cell 2.57 ± 0.12 s−1 -> 2.57 s^(-1); the paper already prints per-second values, so no min^-1/60 conversion is involved anywhere in this paper; the exported value is 2.57 s^(-1). Km: printed cell 0.108 ± 0.004 μM -> 0.000108 mM by the exact μM/1000 conversion; the exported value is 0.0001 mM. kcat/Km: the paper PRINTS the efficiency cell 23.87 ± 1.11 μM−1·s−1 for this substrate row -> 23870.0 s^(-1)*mM^(-1) by the documented conversion 1 μM^-1 s^-1 = 1000 s^-1 mM^-1; the exported value is 25699.999999999996 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 1 of PMID 19581484, substrate row `cis-Cypermethrin`: Sp act (μmol/min/mg) = 4.95 ± 0.23; kcat (s−1) = 2.57 ± 0.12; Km (μM) = 0.108 ± 0.004; kcat/Km (μM−1·s−1) = 23.87 ± 1.11.

table_label: TABLE 1. Kinetic constants determined for the purified recombinant PytH

substrate: cis-cypermethrin


substrate_name: cis-permethrin

column_label: TABLE 1, substrate row `cis-Permethrin`; column `Sp act (μmol/min/mg)` = 5.76 ± 0.24; column `kcat (s−1)` = 3.00 ± 0.13; column `Km (μM)` = 0.065 ± 0.003; column `kcat/Km (μM−1·s−1)` = 46.15 ± 1.92.

normalized_value_unit_evidence: kcat: printed cell 3.00 ± 0.13 s−1 -> 3.0 s^(-1); the paper already prints per-second values, so no min^-1/60 conversion is involved anywhere in this paper; the exported value is 3.0 s^(-1). Km: printed cell 0.065 ± 0.003 μM -> 0.000065 mM by the exact μM/1000 conversion; the exported value is 0.00006 mM. kcat/Km: the paper PRINTS the efficiency cell 46.15 ± 1.92 μM−1·s−1 for this substrate row -> 46150.0 s^(-1)*mM^(-1) by the documented conversion 1 μM^-1 s^-1 = 1000 s^-1 mM^-1; the exported value is 50000.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 1 of PMID 19581484, substrate row `cis-Permethrin`: Sp act (μmol/min/mg) = 5.76 ± 0.24; kcat (s−1) = 3.00 ± 0.13; Km (μM) = 0.065 ± 0.003; kcat/Km (μM−1·s−1) = 46.15 ± 1.92.

row_label: TABLE 1, substrate row `cis-Permethrin`

substrate: cis-permethrin


substrate_name: cyhalothrin

substrate: cyhalothrin


substrate_name: deltamethrin

column_label: table label: TABLE 1. Kinetic constants determined for the purified recombinant PytH; row label: Deltamethrin; column label: the kcat (s-1) and Km (uM) cells of this one TABLE 1 row only; no cell is taken from any other row of TABLE 1 and no cell is taken from the Sp act column; raw value: kcat 0.79 ± 0.03 s-1, Km 0.788 ± 0.038 uM; raw unit: s-1 for kcat, uM for Km; normalized value: kcat 0.79 s^-1, Km 0.000788 mM, kcat/Km 1002.5380710659899 s^-1 mM^-1; normalized unit: s^-1, mM, s^-1 mM^-1; condition label: All assays were performed in 50 mM sodium phosphate buffer (pH 7.5) at 37°C. Kinetic values were obtained from Lineweaver-Burk plots against various substrate concentrations. Purified recombinant PytH expressed from Sphingobium sp. strain JZ-1. Exported assay conditions: pH 7.5.

normalized_value_unit_evidence: kcat 0.79 s-1 is already s^-1, giving 0.79 s^-1 at the export's stored precision; exported kcat 0.79 s^-1. Km 0.788 uM divided by 1000 gives 0.000788 mM at the export's stored precision; exported Km 0.000788 mM. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.79 s^-1 divided by 0.000788 mM giving 1002.5380710659899 s^-1 mM^-1, and of nothing else; exported kcat/Km 1002.5380710659899 s^-1 mM^-1.

raw_value_unit_evidence: TABLE 1. Kinetic constants determined for the purified recombinant PytH, row Deltamethrin: kcat 0.79 ± 0.03 s-1; Km 0.788 ± 0.038 uM; printed kcat/Km 1.00 ± 0.04 uM-1 s-1.

row_label: Deltamethrin

substrate: deltamethrin


substrate_name: trans-cypermethrin

column_label: TABLE 1, substrate row `trans-Cypermethrin`; column `Sp act (μmol/min/mg)` = 4.86 ± 0.22; column `kcat (s−1)` = 2.53 ± 0.11; column `Km (μM)` = 0.110 ± 0.005; column `kcat/Km (μM−1·s−1)` = 23.01 ± 1.04.

normalized_value_unit_evidence: kcat: printed cell 2.53 ± 0.11 s−1 -> 2.53 s^(-1); the paper already prints per-second values, so no min^-1/60 conversion is involved anywhere in this paper; the exported value is 2.53 s^(-1). Km: printed cell 0.110 ± 0.005 μM -> 0.00011 mM by the exact μM/1000 conversion; the exported value is 0.0001 mM. kcat/Km: the paper PRINTS the efficiency cell 23.01 ± 1.04 μM−1·s−1 for this substrate row -> 23010.0 s^(-1)*mM^(-1) by the documented conversion 1 μM^-1 s^-1 = 1000 s^-1 mM^-1; the exported value is 25299.999999999996 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 1 of PMID 19581484, substrate row `trans-Cypermethrin`: Sp act (μmol/min/mg) = 4.86 ± 0.22; kcat (s−1) = 2.53 ± 0.11; Km (μM) = 0.110 ± 0.005; kcat/Km (μM−1·s−1) = 23.01 ± 1.04.

substrate: trans-cypermethrin


substrate_name: trans-permethrin

normalized_value_unit_evidence: Km normalized=0.000062 mM; kcat normalized=3.03 s^-1; kcat/Km normalized=50499.99999999999 s^-1 mM^-1 from exported rounded Km quotient

row_label: trans-Permethrin

table_label: Table 1. Kinetic constants determined for the purified recombinant PytH

substrate: trans-permethrin


raw_value_unit_evidence: Table II row C4-HSL: Km 5.11 mM.


raw_value_unit_evidence: Table II row C6-HSL: Km 3.83 mM.


raw_value_unit_evidence: Table II row C8-HSL: Km 2.61 mM.


substrate_name: dodecanoic-delta-lactone

column_label: Table 2; row δ dodecalactone* (XXIV); columns kcat (s^-1), KM (uM), kcat/KM (M^-1 s^-1)

row_label: δ dodecalactone* (XXIV)

substrate: dodecanoic-delta-lactone


substrate_name: dodecanoic-gamma-lactone

column_label: Table 2; row γ dodecalactone* (XXI); columns kcat (s^-1), KM (uM), kcat/KM (M^-1 s^-1)

row_label: γ dodecalactone* (XXI)

substrate: dodecanoic-gamma-lactone


substrate_name: heptanoic-gamma-lactone

column_label: Table 2; row γ heptalactone (XVIII); columns kcat (s^-1), KM (uM), kcat/KM (M^-1 s^-1)

row_label: γ heptalactone (XVIII)

substrate: heptanoic-gamma-lactone


substrate_name: N-3-oxo-decanoyl-DL-homoserine lactone

column_label: Table 2; row 3-oxo C10 AHL (XVI); columns kcat (s^-1), KM (uM), kcat/KM (M^-1 s^-1)

row_label: 3-oxo C10 AHL (XVI)

substrate: N-3-oxo-decanoyl-DL-homoserine lactone


substrate_name: N-3-oxo-octanoyl-DL-homoserine lactone

column_label: Table 2; row 3-oxo C8 AHL (XV); columns kcat (s^-1), KM (uM), kcat/KM (M^-1 s^-1)

row_label: 3-oxo C8 AHL (XV)

substrate: N-3-oxo-octanoyl-DL-homoserine lactone


substrate_name: N-octanoyl-DL-homoserine lactone

column_label: Table 2; row C8 AHL (XIV); columns kcat (s^-1), KM (uM), kcat/KM (M^-1 s^-1)

row_label: C8 AHL (XIV)

substrate: N-octanoyl-DL-homoserine lactone


substrate_name: nonanoic-delta-lactone

column_label: Table 2; row δ nonalactone (XXII); columns kcat (s^-1), KM (uM), kcat/KM (M^-1 s^-1)

row_label: δ nonalactone (XXII)

substrate: nonanoic-delta-lactone


substrate_name: nonanoic-gamma-lactone

column_label: Table 2; row γ nonalactone (XIX); columns kcat (s^-1), KM (uM), kcat/KM (M^-1 s^-1)

row_label: γ nonalactone (XIX)

substrate: nonanoic-gamma-lactone


substrate_name: rac-gamma-caprolactone

column_label: Table 2; row γ caprolactone (r); columns kcat (s^-1), KM (uM), kcat/KM (M^-1 s^-1)

row_label: γ caprolactone (r)

substrate: rac-gamma-caprolactone


substrate_name: (R)-gamma-caprolactone

column_label: Table 2. Enzymatic characterisation of VmoLac enzyme; row γ caprolactone (R)

row_label: γ caprolactone (R)

substrate: (R)-gamma-caprolactone


enzyme_display_name: UniProt Q4A724

organism: Mycoplasmopsis synoviae

substrate_name: D-xylono-1,4-lactone 5-phosphate

enzyme: UniProt Q4A724

substrate: D-xylono-1,4-lactone 5-phosphate


substrate_name: N-3-oxododecanoyl-L-homoserine lactone

table_label: Table 2: Enzymatic characterization of the AaL enzyme

substrate: N-3-oxododecanoyl-L-homoserine lactone


substrate_name: 3-oxo-dodecanoyl-L-homoserine lactone

substrate: 3-oxo-dodecanoyl-L-homoserine lactone


substrate_name: delta-decalactone

column_label: Table 2 row delta-decalactone; kcat, KM, and kcat/KM cells: 8.4 +/- 0.6 s^-1, 18.5 +/- 0.4 uM, and (4.5 +/- 1.0) x 10^5 M^-1 s^-1.

row_label: delta-decalactone

substrate: delta-decalactone


substrate_name: delta-valerolactone

column_label: Table 2 row delta-valerolactone; kcat, KM, and kcat/KM cells: 8.4 +/- 0.4 s^-1, 18.7 +/- 0.4 uM, and (4.5 +/- 0.9) x 10^5 M^-1 s^-1.

row_label: delta-valerolactone

substrate: delta-valerolactone


substrate_name: gamma-butyrolactone

row_label: gamma-butyrolactone

substrate: gamma-butyrolactone


substrate_name: gamma-heptanolide

substrate: gamma-heptanolide


enzyme_display_name: feruloyl esterase

organism: Aspergillus niger

substrate_name: ethyl ferulate

assay_conditions_summary: pH 6; 313.15 K; buffer 5% DMSO with MES

column_label: Table 1 enzyme block AnFaeA, row ethyl ferulate; raw cells Km 611 uM, kcat 29.4 s^-1, kcat/Km 48 mM^-1 s^-1; normalized cells 0.611 mM, 29.4 s^-1, 48 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.611 normalized_unit=mM; kcat normalized_value=29.4 normalized_unit=s^-1; kcat/Km normalized_value=48 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=611 raw_unit=uM; kcat raw_value=29.4 raw_unit=s^-1; kcat/Km raw_value=48 raw_unit=mM^-1*s^-1

row_label: AnFaeA / ethyl ferulate

table_label: Table 1. Kinetic constants of feruloyl esterases and lipase for different n-alkyl ferulates

enzyme: feruloyl esterase

substrate: ethyl ferulate


substrate_name: methyl ferulate

column_label: Table 1 enzyme block AnFaeA, row methyl ferulate; raw cells Km 1123 uM, kcat 32.9 s^-1, kcat/Km 29 mM^-1 s^-1; normalized cells 1.123 mM, 32.9 s^-1, 29 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=1.123 normalized_unit=mM; kcat normalized_value=32.9 normalized_unit=s^-1; kcat/Km normalized_value=29 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=1123 raw_unit=uM; kcat raw_value=32.9 raw_unit=s^-1; kcat/Km raw_value=29 raw_unit=mM^-1*s^-1

row_label: AnFaeA / methyl ferulate

substrate: methyl ferulate


substrate_name: n-decyl ferulate

column_label: Table 1 enzyme block AnFaeA, row decyl ferulate; raw cells Km 8 uM, kcat 4.6 s^-1, kcat/Km 547 mM^-1 s^-1; normalized cells 0.008 mM, 4.6 s^-1, 547 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.008 normalized_unit=mM; kcat normalized_value=4.6 normalized_unit=s^-1; kcat/Km normalized_value=547 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=8 raw_unit=uM; kcat raw_value=4.6 raw_unit=s^-1; kcat/Km raw_value=547 raw_unit=mM^-1*s^-1

row_label: AnFaeA / decyl ferulate

substrate: n-decyl ferulate


substrate_name: n-hexyl ferulate

column_label: Table 1 enzyme block AnFaeA, row hexyl ferulate; raw cells Km 40 uM, kcat 9.8 s^-1, kcat/Km 243 mM^-1 s^-1; normalized cells 0.04 mM, 9.8 s^-1, 243 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.04 normalized_unit=mM; kcat normalized_value=9.8 normalized_unit=s^-1; kcat/Km normalized_value=243 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=40 raw_unit=uM; kcat raw_value=9.8 raw_unit=s^-1; kcat/Km raw_value=243 raw_unit=mM^-1*s^-1

row_label: AnFaeA / hexyl ferulate

substrate: n-hexyl ferulate


substrate_name: n-propyl ferulate

column_label: Table 1 enzyme block AnFaeA, row propyl ferulate; raw cells Km 245 uM, kcat 44.6 s^-1, kcat/Km 182 mM^-1 s^-1; normalized cells 0.245 mM, 44.6 s^-1, 182 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.245 normalized_unit=mM; kcat normalized_value=44.6 normalized_unit=s^-1; kcat/Km normalized_value=182 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=245 raw_unit=uM; kcat raw_value=44.6 raw_unit=s^-1; kcat/Km raw_value=182 raw_unit=mM^-1*s^-1

row_label: AnFaeA / propyl ferulate

substrate: n-propyl ferulate


organism: Muricauda olearia


substrate_name: N-3-oxohexanoyl-L-homoserine lactone

column_label: Official PMC HTML Table 2, row 3-Oxo-C6-HSL, columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1). Footnote: reactions at pH 7.1 and 25 C.

normalized_value_unit_evidence: kcat 293 s^-1; Km 0.95 mM; paper kcat/Km 3.1 x 10^5 s^-1 M^-1 = 310 s^-1 mM^-1; export kcat/Km 308.42105263157896 s^-1 mM^-1 is ratio-derived and not the exact printed metric cell.

table_label: Table 2

substrate: N-3-oxohexanoyl-L-homoserine lactone


substrate_name: N-3-oxooctanoyl-L-homoserine lactone

column_label: Official PMC HTML Table 2, row 3-Oxo-C8-HSL, columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1). Footnote: reactions at pH 7.1 and 25 C.

normalized_value_unit_evidence: kcat 218 s^-1; Km 0.49 mM; paper kcat/Km 4.5 x 10^5 s^-1 M^-1 = 450 s^-1 mM^-1; export kcat/Km 444.8979591836735 s^-1 mM^-1 is ratio-derived and not the exact printed metric cell.

substrate: N-3-oxooctanoyl-L-homoserine lactone


substrate_name: N-butyryl-L-homoserine lactone

column_label: Official PMC HTML Table 2, row C4-HSL, columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1). Footnote: reactions at pH 7.1 and 25 C.

normalized_value_unit_evidence: kcat 135 s^-1; Km 0.85 mM; paper kcat/Km 1.6 x 10^5 s^-1 M^-1 = 160 s^-1 mM^-1; export kcat/Km 158.8235294117647 s^-1 mM^-1 is ratio-derived and not the exact printed metric cell.

substrate: N-butyryl-L-homoserine lactone


substrate_name: N-hexanoyl-L-homoserine lactone

column_label: Official PMC HTML Table 2, row C6-HSL, columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1). Footnote: reactions at pH 7.1 and 25 C.

normalized_value_unit_evidence: kcat 226 s^-1; Km 0.79 mM; paper kcat/Km 2.9 x 10^5 s^-1 M^-1 = 290 s^-1 mM^-1; export kcat/Km 286.0759493670886 s^-1 mM^-1 is ratio-derived and not the exact printed metric cell.

substrate: N-hexanoyl-L-homoserine lactone


substrate_name: N-octanoyl-L-homoserine lactone

column_label: Official PMC HTML Table 2, row C8-HSL, columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1). Footnote: reactions at pH 7.1 and 25 C.

normalized_value_unit_evidence: kcat 158 s^-1; Km 0.44 mM; paper kcat/Km 3.6 x 10^5 s^-1 M^-1 = 360 s^-1 mM^-1; export kcat/Km 359.09090909090907 s^-1 mM^-1 is ratio-derived and not the exact printed metric cell.

substrate: N-octanoyl-L-homoserine lactone


organism: Aspergillus awamori

substrate_name: 1-Naphthylbutanoic acid

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D71I with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.

column_label: PDF page 7 / article page 207; Table 4; row alpha-NA butyrate / D71I; columns Km (x10^-3 M), kcat (s^-1), and kcat/Km (x10^3 M^-1 s^-1).

normalized_value_unit_evidence: paper km normalized_value=0.29 normalized_unit=mM; paper kcat normalized_value=2.70 normalized_unit=s^-1; paper kcat_over_km normalized_value=9.22 normalized_unit=s^-1*mM^-1; current_export_kcat_over_km=9.310344827586208 s^-1*mM^-1.

row_label: alpha-NA butyrate / D71I

table_label: PMID 15716038 Table 4 kinetic parameters toward alpha-NA esters

substrate: 1-Naphthylbutanoic acid


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9P979 and applied mutation signature D77I with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.

column_label: PDF page 7 / article page 207; Table 4; row alpha-NA butyrate / D77I; columns Km (x10^-3 M), kcat (s^-1), and kcat/Km (x10^3 M^-1 s^-1).

normalized_value_unit_evidence: paper km normalized_value=0.15 normalized_unit=mM; paper kcat normalized_value=3.72 normalized_unit=s^-1; paper kcat_over_km normalized_value=25.7 normalized_unit=s^-1*mM^-1; current_export_kcat_over_km=24.8 s^-1*mM^-1.

row_label: alpha-NA butyrate / D77I


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9P979 and applied mutation signature D77N with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.

column_label: PDF page 7 / article page 207; Table 4; row alpha-NA butyrate / D77N; columns Km (x10^-3 M), kcat (s^-1), and kcat/Km (x10^3 M^-1 s^-1).

normalized_value_unit_evidence: paper km normalized_value=0.18 normalized_unit=mM; paper kcat normalized_value=32.1 normalized_unit=s^-1; paper kcat_over_km normalized_value=183.4 normalized_unit=s^-1*mM^-1; current_export_kcat_over_km=178.33333333333334 s^-1*mM^-1.

row_label: alpha-NA butyrate / D77N


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T72R with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.

column_label: PDF page 7 / article page 207; Table 4; row alpha-NA butyrate / T72R; columns Km (x10^-3 M), kcat (s^-1), and kcat/Km (x10^3 M^-1 s^-1).

normalized_value_unit_evidence: paper km normalized_value=0.63 normalized_unit=mM; paper kcat normalized_value=3.77 normalized_unit=s^-1; paper kcat_over_km normalized_value=5.95 normalized_unit=s^-1*mM^-1; current_export_kcat_over_km=5.984126984126984 s^-1*mM^-1.

row_label: alpha-NA butyrate / T72R


column_label: PDF page 7 / article page 207; Table 4; row alpha-NA butyrate / wild-type; columns Km (x10^-3 M), kcat (s^-1), and kcat/Km (x10^3 M^-1 s^-1).

normalized_value_unit_evidence: paper km normalized_value=0.33 normalized_unit=mM; paper kcat normalized_value=2.33 normalized_unit=s^-1; paper kcat_over_km normalized_value=7.05 normalized_unit=s^-1*mM^-1; current_export_kcat_over_km=7.0606060606060606 s^-1*mM^-1.

row_label: alpha-NA butyrate / wild-type


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


substrate_name: alpha-Naphthyl caprylate

column_label: PDF page 7 / article page 207; Table 4; row alpha-NA caprylate / D71I; columns Km (x10^-3 M), kcat (s^-1), and kcat/Km (x10^3 M^-1 s^-1).

normalized_value_unit_evidence: paper km normalized_value=0.050 normalized_unit=mM; paper kcat normalized_value=0.64 normalized_unit=s^-1; paper kcat_over_km normalized_value=13.1 normalized_unit=s^-1*mM^-1; current_export_kcat_over_km=12.799999999999999 s^-1*mM^-1.

row_label: alpha-NA caprylate / D71I

substrate: alpha-Naphthyl caprylate


column_label: PDF page 7 / article page 207; Table 4; row alpha-NA caprylate / T72R; columns Km (x10^-3 M), kcat (s^-1), and kcat/Km (x10^3 M^-1 s^-1).

normalized_value_unit_evidence: paper km normalized_value=0.017 normalized_unit=mM; paper kcat normalized_value=0.32 normalized_unit=s^-1; paper kcat_over_km normalized_value=18.8 normalized_unit=s^-1*mM^-1; current_export_kcat_over_km=18.823529411764707 s^-1*mM^-1.

row_label: alpha-NA caprylate / T72R


column_label: PDF page 7 / article page 207; Table 4; row alpha-NA caprylate / wild-type; columns Km (x10^-3 M), kcat (s^-1), and kcat/Km (x10^3 M^-1 s^-1).

normalized_value_unit_evidence: paper km normalized_value=0.079 normalized_unit=mM; paper kcat normalized_value=0.85 normalized_unit=s^-1; paper kcat_over_km normalized_value=10.8 normalized_unit=s^-1*mM^-1; current_export_kcat_over_km=10.759493670886076 s^-1*mM^-1.

row_label: alpha-NA caprylate / wild-type


enzyme_display_name: poly(ethylene terephthalate) hydrolase

organism: Fusarium solani

substrate_name: n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n Poly(ethylene terephthalate); n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n H2O

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

enzyme: poly(ethylene terephthalate) hydrolase


enzyme_display_name: Feruloyl esterase B

organism: Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799)

substrate_name: methyl ferulate (MFA)

raw_value_unit_evidence: Table 2. Kinetic constants of MtFae1a from M. thermophila for model substrates; row MFA; column K m (mM); raw value 0.27 (0.02) mM

row_label: MFA

enzyme: Feruloyl esterase B

substrate: methyl ferulate (MFA)


substrate_name: methyl p-coumarate (MpCA)

raw_value_unit_evidence: Table 2. Kinetic constants of MtFae1a from M. thermophila for model substrates; row MpCA; column K m (mM); raw value 0.26 (0.04) mM

row_label: MpCA

substrate: methyl p-coumarate (MpCA)


substrate_name: methyl caffeate (MCA)

raw_value_unit_evidence: Table 2. Kinetic constants of MtFae1a from M. thermophila for model substrates; row MCA; column K m (mM); raw value 0.18 (0.01) mM

row_label: MCA

substrate: methyl caffeate (MCA)


substrate_name: methyl sinapate (MSA)

raw_value_unit_evidence: Table 2. Kinetic constants of MtFae1a from M. thermophila for model substrates; row MSA; column K m (mM); raw value 0.21 (0.04) mM

row_label: MSA

substrate: methyl sinapate (MSA)


substrate_name: ethyl ferulate

raw_value_unit_evidence: Table 2. Kinetic constants of MtFae1a from M. thermophila for model substrates; row Ethyl ferulate; column K m (mM); raw value 2.33 (0.27) mM

row_label: Ethyl ferulate


raw_value_unit_evidence: Table 2. Kinetic constants of MtFae1a from M. thermophila for model substrates; row n-Propyl ferulate; column K m (mM); raw value 1.14 (0.15) mM

row_label: n-Propyl ferulate


substrate_name: n-butyl ferulate

raw_value_unit_evidence: Table 2. Kinetic constants of MtFae1a from M. thermophila for model substrates; row n-Butyl ferulate; column K m (mM); raw value 0.74 (0.08) mM

row_label: n-Butyl ferulate

substrate: n-butyl ferulate


organism: uncultured bacterium

substrate_name: Unknown

substrate: Unknown


organism: Thermobifida fusca

substrate: n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n Poly(ethylene terephthalate); n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n H2O


enzyme_display_name: mono(ethylene terephthalate) hydrolase

substrate_name: Mono(2-hydroxyethyl) terephthalate

enzyme: mono(ethylene terephthalate) hydrolase

substrate: Mono(2-hydroxyethyl) terephthalate


substrate_name: H2O; Mono(2-hydroxyethyl) terephthalate

substrate: H2O; Mono(2-hydroxyethyl) terephthalate


substrate_name: ethylene terephthalate

substrate: ethylene terephthalate


substrate_name: bis(2-hydroxyethyl) terephthalic acid

substrate: bis(2-hydroxyethyl) terephthalic acid


organism: Piscinibacter sakaiensis

substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


organism: Comamonas thiooxydans

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: Cutinase 2

organism: Thermobifida cellulosilytica

substrate_name: pNP-acetate (at 25 degrees Celsius and pH 7)

proof_lines: kcat is 2.4 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (Ref.1). kcat is 17 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (PubMed:23592055). kcat is 5.3 sec(-1) with pNP-butanoate as subst

enzyme: Cutinase 2


enzyme_display_name: Cutinase 1

proof_lines: kcat is 211.9 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (Ref.1). kcat is 436 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (PubMed:23592055). kcat is 195.1 sec(-1) with pNP-butanoate as

enzyme: Cutinase 1

substrate: pNP-acetate (at 25 degrees Celsius and pH 7)


organism: Hydrogenophaga sp. PML113


enzyme_display_name: Cutinase cut2

proof_lines: kcat is 39.5 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (Ref.5). kcat is 253 sec(-1) with pNP-butanoate as substrate (at 50 degrees Celsius and pH 8) (PubMed:23604968). kcat is 30.9 sec(-1) with pNP-butanoate as

enzyme: Cutinase cut2


proof_lines: kcat is 31 sec(-1) for the hydrolysis of mono(2-hydroxyethyl) terephthalate (at pH 7 and 30 degrees Celsius).


proof_lines: kcat is 1590 sec(-1) for the hydrolysis of pNP-acetate. kcat is 1353 sec(-1) for the hydrolysis of pNP-butanoate. kcat is 1345 sec(-1) for the hydrolysis of pNP-hexanoate. kcat is 519 sec(-1) for the hydrolysis of pNP-octanoate. kcat is 153


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F495I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F495I, pH and temperature not specified in the publication


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

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S131G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S131G, pH and temperature not specified in the publication


substrate_name: L-arabino-1,4-lactone 5-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K29A with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines: mutant K29A, pH 8.3, temperature not specified in the publication

substrate: L-arabino-1,4-lactone 5-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E34Q to reconstruct the assayed variant sequence.

proof_lines: mutant E34Q, pH 8.3, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H100N to reconstruct the assayed variant sequence.

proof_lines: mutant H100N, pH 8.3, temperature not specified in the publication


proof_lines: wild-type, pH 8.3, temperature not specified in the publication


enzyme_display_name: Phospho-furanose lactonase

organism: Mycoplasmopsis synoviae (strain 53)

proof_lines: kcat is 23.4 sec(-1) with D-xylono-1,4-lactone-5-phosphate as substrate. kcat is 6.7 sec(-1) with L-arabino-1,4-lactone-5-phosphate as substrate.

enzyme: Phospho-furanose lactonase


organism: Mycoplasmopsis agalactiae (strain NCTC 10123 / CIP 59.7 / PG2)

proof_lines: kcat is 51 sec(-1) with D-xylono-1,4-lactone-5-phosphate as substrate. kcat is 8.7 sec(-1) with L-arabino-1,4-lactone-5-phosphate as substrate.


substrate_name: bis(2-hydroxyethyl) terephthalate

sequence_variant_note: Mutation signature R411K/S416A/F421I could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: 30°C, pH 9.0, mutant enzyme R411K/S416A/F421I

substrate: bis(2-hydroxyethyl) terephthalate


enzyme_display_name: ethyl acetate hydrolase

organism: Pseudomonas putida

enzyme: ethyl acetate hydrolase


substrate_name: Alpha-naphthyl acetate

substrate: Alpha-naphthyl acetate


enzyme_display_name: UniProt C5BN23

organism: Teredinibacter turnerae

substrate_name: allyl-D-glucuronate

smiles: C=CCOC(=O)C(C(C(C(C=O)O)O)O)O

enzyme: UniProt C5BN23

substrate: allyl-D-glucuronate


substrate_name: benzyl-D-glucuronate

substrate: benzyl-D-glucuronate


organism: Saccharomonospora viridis

substrate_name: n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n Poly(ethylene terephthalate); n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n H2O


organism: Ideonella sakaiensis

substrate_name: Mono(2-hydroxyethyl) terephthalate; H2O

substrate: Mono(2-hydroxyethyl) terephthalate; H2O


organism: Mycoplasmopsis agalactiae


organism: Fusarium vanettenii

substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n H2O; n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n Poly(ethylene terephthalate)


organism: Humicola insolens

substrate: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n H2O; n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n n-1 n Poly(ethylene terephthalate)


substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n H2O; p-Nitrophenyl acetate

source_databases_merged: sabio_rk brenda uniprot


organism: Marinactinospora thermotolerans

substrate_name: mono-(2-hydroxyethyl)terephthalic acid

proof_lines: pH 8.0, 40°C, recombinant wild-type enzyme

substrate: mono-(2-hydroxyethyl)terephthalic acid


organism: Pseudomonas mendocina


enzyme_display_name: Cutinase est2

organism: Thermobifida alba

substrate_name: pNP-hexanoate (at 37 degrees Celsius and pH 7)

proof_lines: kcat is 2.06 sec(-1) with pNP-acetate as substrate (at 37 degrees Celsius and pH 7) (PubMed:22183084). kcat is 4.48 sec(-1) with pNP-butyrate as substrate (at 37 degrees Celsius and pH 7) (PubMed:22183084). kcat is 3.28 sec(-1) with pNP-hex

enzyme: Cutinase est2


substrate_name: pNP-butanoate (at 25 degrees Celsius and pH 7)

proof_lines: kcat is 2.4 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (Ref.1). kcat is 17 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (PubMed:23592055). kcat is 5.3 sec(-1) with pNP-butanoate as subst


proof_lines: kcat is 211.9 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (Ref.1). kcat is 436 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (PubMed:23592055). kcat is 195.1 sec(-1) with pNP-butanoate as

substrate: pNP-butanoate (at 25 degrees Celsius and pH 7)


enzyme_display_name: Cutinase cut1

organism: Thermobifida fusca

proof_lines: kcat is 178 sec(-1) for the hydrolysis of pNP-butanoate (at 50 degrees Celsius and pH 8).

enzyme: Cutinase cut1


proof_lines: kcat is 220 sec(-1) with pNP-butanoate as substrate (PubMed:20729325). kcat is 304 sec(-1) with pNP-butanoate as substrate (at 20 degrees Celsius and pH 8) (PubMed:23603671).

proof_lines: kcat is 39.5 sec(-1) with pNP-acetate as substrate (at 25 degrees Celsius and pH 7) (Ref.5). kcat is 253 sec(-1) with pNP-butanoate as substrate (at 50 degrees Celsius and pH 8) (PubMed:23604968). kcat is 30.9 sec(-1) with pNP-butanoate as


organism: Thermomonospora curvata


organism: unknown prokaryotic organism

substrate_name: n H2O; Poly(ethylene terephthalate)

proof_lines: kcat is 232 sec(-1) with pNP-butanoate as substrate (at 30 degrees Celsius and pH 8.0). kcat is 343 sec(-1) with pNP-butanoate as substrate (at 50 degrees Celsius and pH 8.0). kcat is 318 sec(-1) with pNP-butanoate as substrate (at 70 degre

substrate: n H2O; Poly(ethylene terephthalate)


substrate_name: mono(2-hydroxyethyl) terephthalic acid

column_label: Table 2. Kinetic hydrolysis parameters of MHET and BHET by MtCut, ICCG, and IsPETase row MtCut / MHET, column MtCut; Km mM, raw cell 0.75 +/- 0.11, normalized 0.75 mM; Table 2. Kinetic hydrolysis parameters of MHET and BHET by MtCut, ICCG, and IsPETase row MtCut / MHET, column MtCut; kcat s^-1, raw cell 0.13 +/- 0.01, normalized 0.13 s^-1; Table 2. Kinetic hydrolysis parameters of MHET and BHET by MtCut, ICCG, and IsPETase row MtCut / MHET, column MtCut; kcat/Km M^-1 s^-1, raw cell (1.76 +/- 0.14) x 10^2, normalized 0.176 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.75 normalized_unit=mM; kcat normalized_value=0.13 normalized_unit=s^-1; kcat/Km normalized_value=0.176 normalized_unit=s^-1*mM^-1

row_label: MtCut / MHET

substrate: mono(2-hydroxyethyl) terephthalic acid


substrate_name: bis(2-hydroxyethyl) terephthalic acid

column_label: Table 2. Kinetic hydrolysis parameters of MHET and BHET by MtCut, ICCG, and IsPETase row MtCut / BHET, column MtCut; Km mM, raw cell 3.07 +/- 0.93, normalized 3.07 mM; Table 2. Kinetic hydrolysis parameters of MHET and BHET by MtCut, ICCG, and IsPETase row MtCut / BHET, column MtCut; kcat s^-1, raw cell 4.27 +/- 1.15, normalized 4.27 s^-1; Table 2. Kinetic hydrolysis parameters of MHET and BHET by MtCut, ICCG, and IsPETase row MtCut / BHET, column MtCut; kcat/Km M^-1 s^-1, raw cell (1.41 +/- 0.07) x 10^3, normalized 1.41 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=3.07 normalized_unit=mM; kcat normalized_value=4.27 normalized_unit=s^-1; kcat/Km normalized_value=1.41 normalized_unit=s^-1*mM^-1

row_label: MtCut / BHET


substrate_name: 4-nitrophenyl acetate

column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C2 / MtCut, column MtCut; Km mM, raw cell 0.55 +/- 0.04, normalized 0.55 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C2 / MtCut, column MtCut; kcat s^-1, raw cell 4.47 +/- 0.28, normalized 4.47 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C2 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (8.19 +/- 0.34) x 10^3, normalized 8.19 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.55 normalized_unit=mM; kcat normalized_value=4.47 normalized_unit=s^-1; kcat/Km normalized_value=8.19 normalized_unit=s^-1*mM^-1

row_label: pNP-C2 / MtCut


substrate_name: 4-nitrophenyl hexadecanoate

column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C16 / MtCut, column MtCut; Km mM, raw cell 0.15 +/- 0.01, normalized 0.15 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C16 / MtCut, column MtCut; kcat s^-1, raw cell 4.79 +/- 0.12, normalized 4.79 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C16 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (3.25 +/- 0.10) x 10^4, normalized 32.5 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.15 normalized_unit=mM; kcat normalized_value=4.79 normalized_unit=s^-1; kcat/Km normalized_value=32.5 normalized_unit=s^-1*mM^-1

row_label: pNP-C16 / MtCut

substrate: 4-nitrophenyl hexadecanoate


substrate_name: 4-nitrophenyl tetradecanoate

column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C14 / MtCut, column MtCut; Km mM, raw cell 0.19 +/- 0.04, normalized 0.19 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C14 / MtCut, column MtCut; kcat s^-1, raw cell 9.87 +/- 1.52, normalized 9.87 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C14 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (5.14 +/- 0.29) x 10^4, normalized 51.4 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=0.19 normalized_unit=mM; kcat normalized_value=9.87 normalized_unit=s^-1; kcat/Km normalized_value=51.4 normalized_unit=s^-1*mM^-1

row_label: pNP-C14 / MtCut

substrate: 4-nitrophenyl tetradecanoate


substrate_name: 4-nitrophenyl butanoate

column_label: Table 1. MtCut kinetic parameters toward pNP esters row pNP-C4 / MtCut, column MtCut; Km mM, raw cell 1.33 +/- 0.15, normalized 1.33 mM; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C4 / MtCut, column MtCut; kcat s^-1, raw cell 14.10 +/- 1.51, normalized 14.1 s^-1; Table 1. MtCut kinetic parameters toward pNP esters row pNP-C4 / MtCut, column MtCut; kcat/Km M^-1 s^-1, raw cell (1.06 +/- 0.01) x 10^4, normalized 10.6 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=1.33 normalized_unit=mM; kcat normalized_value=14.1 normalized_unit=s^-1; kcat/Km normalized_value=10.6 normalized_unit=s^-1*mM^-1

row_label: pNP-C4 / MtCut

substrate: 4-nitrophenyl butanoate