substrate_name: 4-nitrophenyl octadecanoate

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


enzyme_display_name: poly(ethylene terephthalate) hydrolase

organism: Marinactinospora thermotolerans

substrate_name: 4-nitrophenyl dodecanoate

source_db: brenda

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 8

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

data_origin: experimental

enzyme: poly(ethylene terephthalate) hydrolase

substrate: 4-nitrophenyl dodecanoate

status: corrected

source: brenda


substrate_name: 4-nitrophenyl hexanoate

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: 4-nitrophenyl hexanoate


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


organism: Opitutus terrae

substrate_name: methyl-D-galacturonate

verification_status: unverified

kcat_display: Not reported

km_display: Not reported

kcat_over_km_display: Not reported

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

proof_lines: isozyme OtCE15D, pH and temperature not specified in the publication

proof_lines: isozyme OtCE15B, pH and temperature not specified in the publication

proof_lines: isozyme OtCE15C, pH and temperature not specified in the publication

substrate: methyl-D-galacturonate

status: unverified


proof_lines: isozyme OtCE15A, pH and temperature not specified in the publication


substrate_name: allyl-D-glucuronate

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

substrate: allyl-D-glucuronate


substrate_name: benzyl-D-glucuronate

substrate: benzyl-D-glucuronate


organism: Spirosoma linguale

proof_lines: isozyme SlCE15B, pH and temperature not specified in the publication

proof_lines: isozyme SlCE15C, pH and temperature not specified in the publication

proof_lines: isozyme SlCE15A, pH and temperature not specified in the publication


organism: Teredinibacter turnerae

proof_lines: pH 8.5, temperature not specified in the publication, recombinant His-tagged enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S281A to reconstruct the assayed variant sequence.

mutation_type: substitution

row_label: BnzGlcA S281A

table_label: Table 1. Kinetic parameters of TtCE15A WT and variants on model substrates


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S304E to reconstruct the assayed variant sequence.

row_label: BnzGlcA S304E


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S304E/E374A to reconstruct the assayed variant sequence.

row_label: BnzGlcA S304E/E374A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E374A to reconstruct the assayed variant sequence.

row_label: BnzGlcA E374A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W376D to reconstruct the assayed variant sequence.

row_label: BnzGlcA W376D


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W376A to reconstruct the assayed variant sequence.

row_label: BnzGlcA W376A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F174D to reconstruct the assayed variant sequence.

row_label: BnzGlcA F174D


verification_status: verified

kcat_over_km_origin: calculated

column_label: table label: Table 1 (Kinetic parameters of TtCE15A WT and variants on model substratesEsterase activity was assayed with benzyl, allyl, and methyl esters of GlcA and GalA and pNP-Ac (acetyl esterase activity).); row label: BnzGlcA / WT; column label: kcat (s^-1); Km (mM); derived kcat/Km from normalized kcat and Km cells; printed kcat/Km (s^-1 M^-1) retained as context; raw value/unit and normalized value/unit preserved per metric; assay condition: Glucuronoyl esterase activity assayed with BnzGlcA, AllylGlcA, MeGlcA, and MeGalA using the K-URONIC kit; standard assays kept at pH 7.5 because ester substrates were unstable at higher pH; substrates dissolved in 100% DMSO and reactions contained less than 10% DMSO; kinetic parameters calculated with OriginPro 2017.; captured paper segment: Table 1 BnzGlcA / WT; kcat 132.0 s^-1, kcat_over_km 38.040345821325644 s^-1 mM^-1, km 3.47 mM.

normalized_value_unit_evidence: kcat normalized value: 132.0; normalized unit: s^-1; kcat_over_km normalized value: 38.040345821325644; normalized unit: s^-1 mM^-1; km normalized value: 3.47; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 132 +/- 3.6; raw unit: s^-1; km raw value: 3.47 +/- 0.28; raw unit: mM; printed kcat_over_km raw value: (3.83 +/- 0.16) x 10^4; raw unit: s^-1 M^-1

row_label: BnzGlcA / WT

status: verified


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F174A to reconstruct the assayed variant sequence.

row_label: BnzGlcA F174A


column_label: table label: Table 1 (Kinetic parameters of TtCE15A WT and variants on model substratesEsterase activity was assayed with benzyl, allyl, and methyl esters of GlcA and GalA and pNP-Ac (acetyl esterase activity).); row label: AllylGlcA / WT; column label: kcat (s^-1); Km (mM); derived kcat/Km from normalized kcat and Km cells; printed kcat/Km (s^-1 M^-1) retained as context; raw value/unit and normalized value/unit preserved per metric; assay condition: Glucuronoyl esterase activity assayed with BnzGlcA, AllylGlcA, MeGlcA, and MeGalA using the K-URONIC kit; standard assays kept at pH 7.5 because ester substrates were unstable at higher pH; substrates dissolved in 100% DMSO and reactions contained less than 10% DMSO; kinetic parameters calculated with OriginPro 2017.; captured paper segment: Table 1 AllylGlcA / WT; kcat 200.0 s^-1, kcat_over_km 4.081632653061225 s^-1 mM^-1, km 49.0 mM.

normalized_value_unit_evidence: kcat normalized value: 200.0; normalized unit: s^-1; kcat_over_km normalized value: 4.081632653061225; normalized unit: s^-1 mM^-1; km normalized value: 49.0; normalized unit: mM

raw_value_unit_evidence: kcat raw value: 200 +/- 4.3; raw unit: s^-1; km raw value: 49.0 +/- 1.7; raw unit: mM; printed kcat_over_km raw value: (4.08 +/- 0.17) x 10^3; raw unit: s^-1 M^-1

row_label: AllylGlcA / WT


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

proof_lines: mutant S267A, pH and temperature not specified in the publication


proof_lines: mutant H408A, pH and temperature not specified in the publication


proof_lines: mutant E290A/D356A, pH and temperature not specified in the publication


proof_lines: mutant L269Y, pH and temperature not specified in the publication


proof_lines: mutant D356A, pH and temperature not specified in the publication


proof_lines: mutant E290A, pH and temperature not specified in the publication


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

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


substrate_name: methyl-D-glucuronate

substrate: methyl-D-glucuronate


enzyme_display_name: Cutinase est2

organism: Thermobifida alba

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

source_db: uniprot

assay_conditions_summary: 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

source: uniprot


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


enzyme_display_name: ethyl acetate hydrolase

organism: Pseudomonas putida

substrate_name: Alpha-naphthyl acetate

sequence_source: multiple

proof_lines: kcat is 29 sec(-1) with alpha-naphthyl acetate as substrate. kcat is 64 sec(-1) with 4-nitrophenyl acetate as substrate.

source_databases_merged: brenda uniprot

enzyme: ethyl acetate hydrolase

substrate: Alpha-naphthyl acetate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: benzyl D-glucuronate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R268A to reconstruct the assayed variant sequence.

proof_lines: mutant R268A, pH not specified in the publication, temperature not specified in the publication

substrate: benzyl D-glucuronate


organism: Candidatus Solibacter usitatus

proof_lines: isozyme SuCE15B, pH and temperature not specified in the publication

proof_lines: isozyme SuCE15C, pH and temperature not specified in the publication

proof_lines: isozyme SuCE15A, pH and temperature not specified in the publication


organism: Burkholderia ambifaria (strain ATCC BAA-244 / DSM 16087 / CCUG 44356 / LMG 19182 / AMMD)

substrate_name: L-fucono-1,4-lactone (at pH 8.3 and pH 7.1)

proof_lines: kcat is 89 sec(-1) with L-fucono-1,4-lactone as substrate (at pH 8.3). kcat is 4.1 sec(-1) with L-fucono-1,4-lactone as substrate (at pH 7.1). kcat is 55 sec(-1) with L-galactono-1,4-lactone as substrate (at pH 8.3). kcat is 6.2 sec(-1) wit


substrate_name: L-galactono-1,4-lactone (at pH 8.3)

substrate: L-galactono-1,4-lactone (at pH 8.3)


substrate_name: D-arabinono-1,4-lactone (at pH 8.3)

substrate: D-arabinono-1,4-lactone (at pH 8.3)


substrate_name: 4-deoxy-L-fucono-1,5-lactone (at pH 7.1)


organism: Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)

substrate_name: L-fucono-1,4-lactone (at pH 8.3)

proof_lines: kcat is 139 sec(-1) with L-fucono-1,4-lactone as substrate (at pH 8.3). kcat is 3.0 sec(-1) with L-fucono-1,4-lactone as substrate (at pH 7.1). kcat is 119 sec(-1) with L-galactono-1,4-lactone as substrate (at pH 8.3). kcat is 5.7 sec(-1) w

substrate: L-fucono-1,4-lactone (at pH 8.3)


substrate: 4-deoxy-L-fucono-1,5-lactone (at pH 7.1)


organism: Caldicellulosiruptor acetigenus


enzyme_display_name: UniProt C5BN23

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt C5BN23

source: skid


organism: Trichoderma reesei

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

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

proof_lines:
pH 5.5, 30°C
Raw SKiD Env: Temp=30°C, pH=5.5

source_databases_merged: brenda skid uniprot


organism: Wolfiporia cocos

substrate_name: Benzyl D-glucuronate; H2O

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

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

source_databases_merged: sabio_rk brenda uniprot

substrate: Benzyl D-glucuronate; H2O


enzyme_display_name: Ethyl acetate hydrolase

substrate_name: Unknown

enzyme: Ethyl acetate hydrolase

substrate: Unknown


enzyme_display_name: Diacylglycerol lipase-beta

organism: Homo sapiens

enzyme: Diacylglycerol lipase-beta


enzyme_display_name: sn-1-specific diacylglycerol lipase ABHD11


organism: Armillaria fuscipes

substrate_name: lignin-rich pellet

substrate: lignin-rich pellet


organism: Cerrena unicolor

proof_lines:
recombinant enzyme, pH 6.0, 50°C
pH 6.0, 30°C


enzyme_display_name: 4-O-methyl-glucuronoyl methylesterase

organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)

proof_lines: kcat is 16.8 sec(-1) with 3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate.

enzyme: 4-O-methyl-glucuronoyl methylesterase


organism: Burkholderia multivorans

column_label: Table 1 row pH 8.3 block, BmulJ_04915, D-arabinono-1,4-lactone (6); columns BmulJ_04915 kcat (s^-1), BmulJ_04915 Km (mM), BmulJ_04915 kcat/Km (M^-1 s^-1).

table_label: Table 1


column_label: Table 1 row pH 8.3 block, BmulJ_04915, L-fucono-1,4-lactone (1); columns BmulJ_04915 kcat (s^-1), BmulJ_04915 Km (mM), BmulJ_04915 kcat/Km (M^-1 s^-1).


column_label: Table 1 row pH 7.1 block, BmulJ_04915, L-fucono-1,4-lactone (1); columns BmulJ_04915 kcat (s^-1), BmulJ_04915 Km (mM), BmulJ_04915 kcat/Km (M^-1 s^-1).


substrate_name: L-fucono-1,4-lactone (at pH 7.1)

column_label: Table 1 row pH 7.1 block, BmulJ_04915, L-fucono-1,4-lactone (1); columns BmulJ_04915 Km (mM).

normalized_value_unit_evidence: Km=0.6 mM

substrate: L-fucono-1,4-lactone (at pH 7.1)


column_label: Table 1 row pH 8.3 block, BmulJ_04915, L-galactono-1,4-lactone (2); columns BmulJ_04915 kcat (s^-1), BmulJ_04915 Km (mM), BmulJ_04915 kcat/Km (M^-1 s^-1).


column_label: Table 1 row pH 7.1 block, BmulJ_04915, 4-deoxy-L-fucono-1,5-lactone (24); columns BmulJ_04915 kcat (s^-1), BmulJ_04915 Km (mM), BmulJ_04915 kcat/Km (M^-1 s^-1).


organism: Podospora anserina

proof_lines: kcat is 16.2 min(-1) with 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside, 315.3 min(-1) with trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate, 46.5 min(-1) with 3-phenyl-1-propyl D-glucopyranos


organism: Thermothelomyces thermophilus

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

proof_lines: kcat is 115.9 min(-1) with trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate and 166.4 with 3-phenyl-1-propyl D-glucopyranosyluronate as substrate.

source_databases_merged: sabio_rk skid uniprot


organism: Phanerodontia chrysosporium

assay_conditions_summary: pH 6


substrate_name: benzyl glucuronic acid

substrate: benzyl glucuronic acid


organism: bacterium HR29

proof_lines:
BhrPETase
amorphous PET
101 C


substrate_name: 4-nitrophenyl tetradecanoate

substrate: 4-nitrophenyl tetradecanoate


substrate_name: 4-nitrophenyl dodecanoate

substrate: 4-nitrophenyl dodecanoate


substrate_name: 4-nitrophenyl octanoate

substrate: 4-nitrophenyl octanoate


substrate_name: 4-nitrophenyl hexanoate

substrate: 4-nitrophenyl hexanoate


substrate_name: 4-nitrophenyl butanoate

substrate: 4-nitrophenyl butanoate


substrate_name: 4-nitrophenyl acetate

proof_lines:
BhrPETase
amorphous PET
PETase


source_db: oed

assay_conditions_summary: pH 7; 323.15 K; buffer pH 6

column_label: Table 2 (Kinetic parameters of StGE2 and PaGE1 on the three D-glucuronate esters), substrate-column row label 'VI'; each metric head carries two enzyme sub-heads, 'StGE2' then 'PaGE1'. Column 'Km (mM)', PaGE1 sub-column = 1.34; column 'kcat (min-1)', PaGE1 sub-column = 11.4; column 'kcat/Km (mM-1 min-1)', PaGE1 sub-column = 8.5. The StGE2 sub-column of row VI reads nd in all three blocks.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.34 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 1.34 mM. kcat: printed Table 2 cell 11.4 min^-1; 11.4 / 60 = 0.19 s^-1; the exported value is 0.19 s^(-1). kcat/Km: the exported 0.1417910447761194 s^(-1)*mM^(-1) is the full-precision quotient of the two printed component cells, 0.19 / 1.34 = 0.1417910447761194; the paper's own printed efficiency cell 8.5 mM^-1 min^-1 converts as 8.5 / 60 = 0.14166666666666666 s^-1 mM^-1 and corroborates that quotient, because 11.4 / 1.34 = 8.5074626865671643 mM^-1 min^-1 rounds to the printed 8.5 at the one-decimal precision the table prints.

raw_value_unit_evidence: Table 2, substrate row VI, PaGE1 sub-column: Km column head 'Km (mM)' prints 1.34; kcat column head 'kcat (min-1)' prints 11.4; kcat/Km column head 'kcat/Km (mM-1 min-1)' prints 8.5. The StGE2 sub-column of the same row prints nd in all three blocks.

row_label: Table 2, substrate row VI (3-(4-hydroxyphenyl)-1-propyl D-glucopyranosyluronate), PaGE1 sub-column of each metric block

table_label: Table 2: Kinetic parameters of StGE2 and PaGE1 on the three D-glucuronate esters (Applied Microbiology and Biotechnology 2014, 98:5507-5516, page 5513)

source: oed


proof_lines:
PaGE1
Podospora anserina
glucuronoyl esterase


substrate_name: cinnamyl 4-O-methyl-D-glucopyranuronate

substrate: cinnamyl 4-O-methyl-D-glucopyranuronate


organism: Aspergillus fumigatus

substrate_name: 3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate


substrate_name: benzyl D-glucuronate


organism: Sodiomyces alcalophilus

substrate_name: benzyl-D-glucuronate

substrate: benzyl-D-glucuronate


organism: Piscinibacter sakaiensis


enzyme_display_name: feruloyl esterase

organism: Aspergillus niger

substrate_name: methyl ferulate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C235S with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

proof_lines:
feruloyl esterase A
thermostability
80% residual activity

enzyme: feruloyl esterase

substrate: methyl ferulate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D93G/S187F with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature L14F/T35I/K37I/T57I/T63I/A140T/Q121H/S163T/Q177H/V178A/Q185R could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
mutant
heat treatment
half-life


sequence_variant_note: Mutation signature L14F/T35I/K37I/T57I/T63I/A140T/Q121H/S163T/Q177H/V178A/Q185R/C235S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
C235S
thermostability
residual activity


substrate_name: ferulate

sequence_variant_note: Mutation signature D93G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: ferulate


sequence_variant_note: Mutation signature S187F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


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

organism: Escherichia coli

column_label: Official PMC Table III lists the pNP-acetate (C2) row with Km 0.29 +/- 0.04 mM, kcat 18.5 +/- 1.7 s^-1, and kcat/Km 63.8 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.29 normalized_unit=mM; kcat normalized_value=18.5 normalized_unit=s^-1; table specificity 63.8 x 10^3 M^-1 s^-1 is 63.8 s^-1 mM^-1, and the central-value ratio 18.5/0.29 is 63.793103448275865 s^-1 mM^-1.

row_label: pNP-acetate (C2)

table_label: PMC Table III, steady state kinetic parameters for E. coli BioH carboxylesterase activity with various substrates

substrate: 4-nitrophenyl acetate


substrate_name: 4-nitrophenyl butyrate

column_label: Table III | row pNP-butyrate (C4) | columns Km, kcat, kcat/Km | required metrics kcat,kcat_over_km.

normalized_value_unit_evidence: Km 0.33 mM; kcat 6.1 s^-1; kcat/Km 18.5 s^-1 mM^-1. Required metrics: kcat,kcat_over_km.

raw_value_unit_evidence: Row pNP-butyrate (C4): Km 0.33 mM; kcat 6.1 s^-1; kcat/Km 18.5 x 10^3 M^-1 s^-1.

row_label: pNP-butyrate (C4)

table_label: Table III, Steady state kinetic parameters for E. coli BioH carboxylesterase activity with various substrates

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

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl caproate

column_label: Table III | row pNP-caproate (C6) | columns Km, kcat, kcat/Km | required metrics kcat,kcat_over_km.

normalized_value_unit_evidence: Km 0.25 mM; kcat 4.0 s^-1; kcat/Km 16.0 s^-1 mM^-1. Required metrics: kcat,kcat_over_km.

raw_value_unit_evidence: Row pNP-caproate (C6): Km 0.25 mM; kcat 4.0 s^-1; kcat/Km 16.0 x 10^3 M^-1 s^-1.

row_label: pNP-caproate (C6)

substrate: 4-nitrophenyl caproate


substrate_name: 4-nitrophenyl laurate

column_label: Table III | row pNP-laurate (C12) | columns Km, kcat, kcat/Km | required metrics kcat,kcat_over_km.

normalized_value_unit_evidence: Km 0.60 mM; kcat 1.5 s^-1; kcat/Km 2.5 s^-1 mM^-1. Required metrics: kcat,kcat_over_km.

row_label: pNP-laurate (C12)

substrate: 4-nitrophenyl laurate


substrate_name: 4-nitrophenyl propionate

column_label: Table III | row pNP-propionate (C3) | columns Km, kcat, kcat/Km | required metrics kcat,kcat_over_km,km.

normalized_value_unit_evidence: Km 0.35 mM; kcat 13.1 s^-1; kcat/Km 37.4 s^-1 mM^-1. Required metrics: kcat,kcat_over_km,km.

raw_value_unit_evidence: Row pNP-propionate (C3): Km 0.35 mM; kcat 13.1 s^-1; kcat/Km 37.4 x 10^3 M^-1 s^-1.

row_label: pNP-propionate (C3)

substrate: 4-nitrophenyl propionate


organism: Fusarium oxysporum

substrate_name: methyl caffeate

column_label: Table 5; MCA section; row Wild type; columns Km (mM) raw 0.649 (0.183) mM, kcat (min^-1) raw 2628 (251) min^-1, kcat/Km raw 4051 (1206) min^-1 mM^-1.

raw_value_unit_evidence: Table 5, MCA section, Wild type row: Km 0.649 (0.183) mM; kcat 2628 (251) min^-1; kcat/Km 4051 (1206) min^-1 mM^-1.

row_label: Wild type MCA

table_label: Table 5. Kinetic constants of FoFaeC mutant clones and wild type.

substrate: methyl caffeate


column_label: Table 5; MFA section; row Wild type; columns Km (mM) raw 0.331 (0.102) mM, kcat (min^-1) raw 1392 (122) min^-1, kcat/Km raw 4466 (1431) min^-1 mM^-1.

raw_value_unit_evidence: Table 5, MFA section, Wild type row: Km 0.331 (0.102) mM; kcat 1392 (122) min^-1; kcat/Km 4466 (1431) min^-1 mM^-1.

row_label: Wild type MFA


substrate_name: methyl p-coumarate

column_label: PLOS PDF Table 5, WT MpCA row: Km 0.799 (0.312) mM; vmax 96.4 (14.1) umol L^-1 min^-1; kcat 3273 (478) min^-1; independently printed kcat/Km 4094 (1707) min^-1 mM^-1.

raw_value_unit_evidence: Table 5 WT MpCA row: Km 0.799 (0.312) mM; kcat 3273 (478) min^-1; independently printed kcat/Km 4094 (1707) min^-1 mM^-1.

row_label: WT, MpCA

table_label: Table 5. Kinetic constants of FoFaeC mutant clones and wild type

substrate: methyl p-coumarate


substrate_name: methyl sinapate

column_label: Table 5; MSA section; row Wild type; columns Km (mM) raw 0.424 (0.063) mM, kcat (min^-1) raw 102 (3.4) min^-1, kcat/Km raw 241 (36.7) min^-1 mM^-1.

raw_value_unit_evidence: Table 5, MSA section, Wild type row: Km 0.424 (0.063) mM; kcat 102 (3.4) min^-1; kcat/Km 241 (36.7) min^-1 mM^-1.

row_label: Wild type MSA

substrate: methyl sinapate


substrate_name: ethyl ferulate

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

column_label: Table 1 enzyme block MtFaeB, row ethyl ferulate; raw cells Km 48 uM, kcat 11.2 s^-1, kcat/Km 236 mM^-1 s^-1; normalized cells 0.048 mM, 11.2 s^-1, 236 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.048 normalized_unit=mM; kcat normalized_value=11.2 normalized_unit=s^-1; kcat/Km normalized_value=236 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=48 raw_unit=uM; kcat raw_value=11.2 raw_unit=s^-1; kcat/Km raw_value=236 raw_unit=mM^-1*s^-1

row_label: MtFaeB / ethyl ferulate

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

substrate: ethyl ferulate


column_label: Table 1 enzyme block MtFaeB, row methyl ferulate; raw cells Km 51 uM, kcat 8.8 s^-1, kcat/Km 173 mM^-1 s^-1; normalized cells 0.051 mM, 8.8 s^-1, 173 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.051 normalized_unit=mM; kcat normalized_value=8.8 normalized_unit=s^-1; kcat/Km normalized_value=173 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=51 raw_unit=uM; kcat raw_value=8.8 raw_unit=s^-1; kcat/Km raw_value=173 raw_unit=mM^-1*s^-1

row_label: MtFaeB / methyl ferulate


substrate_name: n-hexyl ferulate

column_label: Table 1 enzyme block MtFaeB, row hexyl ferulate; raw cells Km 10 uM, kcat 8.9 s^-1, kcat/Km 906 mM^-1 s^-1; normalized cells 0.01 mM, 8.9 s^-1, 906 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.01 normalized_unit=mM; kcat normalized_value=8.9 normalized_unit=s^-1; kcat/Km normalized_value=906 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=10 raw_unit=uM; kcat raw_value=8.9 raw_unit=s^-1; kcat/Km raw_value=906 raw_unit=mM^-1*s^-1

row_label: MtFaeB / hexyl ferulate

substrate: n-hexyl ferulate


substrate_name: n-propyl ferulate

column_label: Table 1 enzyme block MtFaeB, row propyl ferulate; raw cells Km 27 uM, kcat 12.1 s^-1, kcat/Km 452 mM^-1 s^-1; normalized cells 0.027 mM, 12.1 s^-1, 452 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.027 normalized_unit=mM; kcat normalized_value=12.1 normalized_unit=s^-1; kcat/Km normalized_value=452 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=27 raw_unit=uM; kcat raw_value=12.1 raw_unit=s^-1; kcat/Km raw_value=452 raw_unit=mM^-1*s^-1

row_label: MtFaeB / propyl ferulate

substrate: n-propyl ferulate


enzyme_display_name: UniProt Q8ZRM2

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: S-D-lactoylglutathione

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

enzyme: UniProt Q8ZRM2

substrate: S-D-lactoylglutathione


enzyme_display_name: UniProt Q9SID3

organism: Arabidopsis thaliana

substrate_name: S-Lactoylglutathione

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.2

enzyme: UniProt Q9SID3

substrate: S-Lactoylglutathione


enzyme_display_name: hydroxyacylglutathione hydrolase

organism: Saccharomyces cerevisiae

substrate_name: (R)-S-Mandeloylglutathione

enzyme: hydroxyacylglutathione hydrolase

substrate: (R)-S-Mandeloylglutathione


enzyme_display_name: Cutinase cut1

organism: Trichoderma harzianum

substrate_name: p-nitrophenyl acetate (at pH 8 and 25 degrees Celsius)

proof_lines:
PMID 18987860
Trichoderma harzianum
cutinase cut1

enzyme: Cutinase cut1


substrate_name: p-nitrophenyl butyrate (at pH 8 and 25 degrees Celsius)


substrate_name: p-nitrophenyl valerate (at pH 8 and 25 degrees Celsius)


substrate_name: p-nitrophenyl palmitate (at pH 8 and 37 degrees Celsius)


enzyme_display_name: cutinase

organism: Thermobifida alba

substrate_name: p-Nitrophenyl acetate

column_label: Table 1; row PNP-C2; columns kcat (s^-1), Km (mM), and same-row kcat/Km quotient; raw kcat 2.06+/-0.12; raw Km 3.22+/-0.15.

row_label: PNP-C2 (p-nitrophenyl acetate)

table_label: Table 1: Kinetic parameters of Est119 with different chain lengths of p-nitrophenyl esters

enzyme: cutinase

substrate: p-Nitrophenyl acetate


substrate_name: p-Nitrophenyl butyrate

column_label: Table 1; row PNP-C4; columns kcat (s^-1), Km (mM), and same-row kcat/Km quotient; raw kcat 4.48+/-0.21; raw Km 3.41+/-0.16.

row_label: PNP-C4 (p-nitrophenyl butyrate)

substrate: p-Nitrophenyl butyrate


substrate_name: p-Nitrophenyl caproate

column_label: Table 1; row PNP-C6; columns kcat (s^-1), Km (mM), and same-row kcat/Km quotient; raw kcat 3.28+/-0.15; raw Km 2.37+/-0.12.

row_label: PNP-C6 (p-nitrophenyl caproate)

substrate: p-Nitrophenyl caproate


substrate_name: p-Nitrophenyl octanoate

column_label: Table 1; row PNP-C8; columns kcat (s^-1), Km (mM), and same-row kcat/Km quotient; raw kcat 2.45+/-0.12; raw Km 1.87+/-0.09.

row_label: PNP-C8 (p-nitrophenyl octanoate)

substrate: p-Nitrophenyl octanoate


organism: Bos taurus

enzyme: sn-1-specific diacylglycerol lipase ABHD11


enzyme_display_name: Diacylglycerol lipase-alpha

organism: Homo sapiens

enzyme: Diacylglycerol lipase-alpha


organism: Phanerochaete chrysosporium

substrate_name: Benzyl D-glucuronate; H2O

substrate: Benzyl D-glucuronate; H2O


enzyme_display_name: 4-O-methyl-glucuronoyl methylesterase 2

organism: Phanerochaete chrysosporium (strain RP-78 / ATCC MYA-4764 / FGSC 9002)

enzyme: 4-O-methyl-glucuronoyl methylesterase 2


organism: Schizophyllum commune (strain H4-8 / FGSC 9210)

substrate_name: 4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside (purified enzyme)


organism: Parageobacillus caldoxylosilyticus

substrate_name: N-butyryl-L-homoserine lactone

substrate: N-butyryl-L-homoserine lactone


substrate_name: N-hexanoyl-L-homoserine lactone

substrate: N-hexanoyl-L-homoserine lactone


substrate_name: N-decanoyl-L-homoserine lactone

normalized_value_unit_evidence: Km 1.45 uM = 0.00145 mM; kcat 5.48 s^-1; printed kcat/Km 3.77 x 10^6 M^-1 s^-1 = 3770 s^-1 mM^-1; expected computed ratio 3779.310344827587 s^-1 mM^-1 is within table precision/rounding.

table_label: Table 1, Kinetic parameters of GcL at 25 C

substrate: N-decanoyl-L-homoserine lactone


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

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


enzyme_display_name: UniProt P40363

substrate_name: 4-nitrophenyl butyrate

enzyme: UniProt P40363

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: S-Lactoylglutathione


enzyme_display_name: Cephalosporin-C deacetylase

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

substrate_name: cephalosporin-C

assay_conditions_summary: pH 6.5; buffer 50 mM phosphate

column_label: Table 2, row Cephalosporin C, column KM (mM), cell 4.18 +/- 0.97.

raw_value_unit_evidence: Table 2 row Cephalosporin C: KM = 4.18 +/- 0.97 mM.

row_label: Cephalosporin C

table_label: Table 2: Kinetic parameters of the hydrolysis of pNP-acetate, glucose penta-acetate and cephalosporin C by recombinant AxeA in 50 mM phosphate buffer pH 6.5

enzyme: Cephalosporin-C deacetylase

substrate: cephalosporin-C


substrate_name: p-nitrophenyl acetate

substrate: p-nitrophenyl acetate


substrate_name: p-nitrophenyl-propionate

proof_lines:
AxeA
p-nitrophenyl-acetate
glucose penta-acetate

substrate: p-nitrophenyl-propionate


enzyme_display_name: cocaine esterase

organism: Rhodococcus sp.

substrate_name: cocaine

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

enzyme: cocaine esterase

substrate: cocaine


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


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


sequence_variant_note: Mutation signature T172R/G173Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Cellulosilyticum ruminicola

substrate_name: methyl caffeate

assay_conditions_summary: pH 9

substrate: methyl caffeate


substrate_name: methyl 4-coumarate

substrate: methyl 4-coumarate


substrate_name: methyl ferulate

substrate: methyl ferulate


organism: Aspergillus terreus

substrate_name: ferulic acid methyl ester

column_label: Table 1, MFA row: Km 0.61 mM; kcat 155.5 min^-1; kcat/Km 254.9 mM^-1 min^-1.

normalized_value_unit_evidence: Km normalized_value=0.61 normalized_unit=mM; kcat normalized_value=2.591666666666667 normalized_unit=s^-1; kcat/Km normalized_value=4.248333333333333 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: MFA row: Km raw_value=0.61 raw_unit=mM; kcat raw_value=155.5 raw_unit=min^-1; kcat/Km raw_value=254.9 raw_unit=mM^-1*min^-1.

row_label: MFA

table_label: Table 1, PDF page 17

substrate: ferulic acid methyl ester


substrate_name: p-coumaric acid methyl ester

column_label: Table 1, MpCA row: Km 0.38 mM; kcat 18.4 min^-1; kcat/Km 48.42 mM^-1 min^-1.

normalized_value_unit_evidence: Km normalized_value=0.38 normalized_unit=mM; kcat normalized_value=0.30666666666666664 normalized_unit=s^-1; kcat/Km normalized_value=0.807 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: MpCA row: Km raw_value=0.38 raw_unit=mM; kcat raw_value=18.4 raw_unit=min^-1; kcat/Km raw_value=48.42 raw_unit=mM^-1*min^-1.

row_label: MpCA

substrate: p-coumaric acid methyl ester


substrate_name: sinapic acid methyl ester

column_label: Table 1, MSA row: Km 0.29 mM; kcat 56.2 min^-1; kcat/Km 193.8 mM^-1 min^-1.

normalized_value_unit_evidence: Km normalized_value=0.29 normalized_unit=mM; kcat normalized_value=0.9366666666666666 normalized_unit=s^-1; kcat/Km normalized_value=3.23 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: MSA row: Km raw_value=0.29 raw_unit=mM; kcat raw_value=56.2 raw_unit=min^-1; kcat/Km raw_value=193.8 raw_unit=mM^-1*min^-1.

row_label: MSA

substrate: sinapic acid methyl ester


organism: Rhizoctonia solani

substrate_name: chlorogenate

column_label: Table 3 columns Km [uM], kcat [s^-1], kcat/Km [mM^-1 s^-1]; row Chlorogenic acid cells 18.3, 29.3, 1598.4; Results prose repeats chlorogenic acid catalytic efficiency 1598.4 mM^-1 s^-1.

normalized_value_unit_evidence: Km 18.3 uM = 0.0183 mM; kcat 29.3 s^-1; printed kcat/Km 1598.4 s^-1 mM^-1; expected computed ratio 1601.0928961748634 s^-1 mM^-1 is within table precision/rounding.

raw_value_unit_evidence: Table 3 row Chlorogenic acid: Km 18.3 uM; kcat 29.3 s^-1; kcat/Km 1598.4 mM^-1 s^-1.

row_label: Chlorogenic acid (chlorogenate synonym)

table_label: ScienceDirect article Table 3, Kinetic parameters of Rs pCAE

substrate: chlorogenate


column_label: Table 3 columns Km [uM], kcat [s^-1], kcat/Km [mM^-1 s^-1]; row Methyl caffeate cells 28.5, 20.0, 701.8; Results prose repeats MCA catalytic efficiency 701.8 mM^-1 s^-1.

normalized_value_unit_evidence: Km 28.5 uM = 0.0285 mM; kcat 20.0 s^-1; printed kcat/Km 701.8 s^-1 mM^-1; expected computed ratio 701.7543859649122 s^-1 mM^-1 is within table precision/rounding.

raw_value_unit_evidence: Table 3 row Methyl caffeate: Km 28.5 uM; kcat 20.0 s^-1; kcat/Km 701.8 mM^-1 s^-1.

row_label: Methyl caffeate (MCA)


substrate_name: methyl p-coumarate

column_label: Table 3 columns Km [uM], kcat [s^-1], kcat/Km [mM^-1 s^-1]; row Methyl p-coumarate cells 35.8, 33.1, 925.3; Results prose repeats MpCA catalytic efficiency 925.3 mM^-1 s^-1.

normalized_value_unit_evidence: Km 35.8 uM = 0.0358 mM; kcat 33.1 s^-1; printed kcat/Km 925.3 s^-1 mM^-1; expected computed ratio 924.5810055865923 s^-1 mM^-1 is within table precision/rounding.

raw_value_unit_evidence: Table 3 row Methyl p-coumarate: Km 35.8 uM; kcat 33.1 s^-1; kcat/Km 925.3 mM^-1 s^-1.

row_label: Methyl p-coumarate (MpCA)

substrate: methyl p-coumarate


enzyme_display_name: acyl-CoA hydrolase

organism: Mycolicibacterium smegmatis

substrate_name: CoA

enzyme: acyl-CoA hydrolase

substrate: CoA


enzyme_display_name: UniProt P44886

organism: Haemophilus influenzae

substrate_name: malonyl-CoA

enzyme: UniProt P44886

substrate: malonyl-CoA


substrate_name: methylmalonyl-CoA

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.5

substrate: methylmalonyl-CoA


substrate_name: hexanoyl-CoA

substrate: hexanoyl-CoA


substrate_name: palmitoleoyl-CoA

substrate: palmitoleoyl-CoA


substrate_name: tiglyl-CoA

substrate: tiglyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: linoleoyl-CoA

substrate: linoleoyl-CoA


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


substrate_name: n-butyryl-CoA

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

substrate: n-butyryl-CoA


substrate_name: isobutyryl-CoA

substrate: isobutyryl-CoA


substrate_name: propionyl-CoA

substrate: propionyl-CoA


substrate_name: stearoyl-CoA

substrate: stearoyl-CoA


substrate_name: isovaleryl-CoA

substrate: isovaleryl-CoA


substrate_name: phenylacetyl-CoA

substrate: phenylacetyl-CoA


substrate_name: succinyl-CoA

substrate: succinyl-CoA


substrate_name: glutaryl-CoA

substrate: glutaryl-CoA


substrate_name: n-octanoyl-CoA

substrate: n-octanoyl-CoA


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


substrate_name: myristoyl-CoA

substrate: myristoyl-CoA


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


substrate_name: arachidoyl-CoA

substrate: arachidoyl-CoA


enzyme_display_name: UniProt Q9NPJ3

enzyme: UniProt Q9NPJ3


substrate_name: palmitoleoyl-CoA

substrate: palmitoleoyl-CoA


substrate_name: n-propionyl-CoA

substrate: n-propionyl-CoA


proof_lines:
Raw SKiD Env: Temp=37°C, pH=-----
Raw SKiD Env: Temp=25°C, pH=-----


substrate_name: tiglyl-CoA

substrate: tiglyl-CoA


substrate_name: methylmalonyl-CoA

substrate: methylmalonyl-CoA


substrate_name: beta-hydroxybutyryl-CoA

substrate: beta-hydroxybutyryl-CoA


substrate_name: Arachidonoyl-CoA

substrate: Arachidonoyl-CoA


substrate_name: n-hexanoyl-CoA

substrate: n-hexanoyl-CoA


substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


substrate_name: stearoyl-CoA

substrate: stearoyl-CoA


substrate_name: phenylacetyl-CoA

substrate: phenylacetyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: malonyl-CoA

substrate: malonyl-CoA


substrate_name: n-octanoyl-CoA

substrate: n-octanoyl-CoA


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


enzyme_display_name: UniProt O75608

substrate_name: 1-palmitoyl lysophosphatidylcholine

enzyme: UniProt O75608

substrate: 1-palmitoyl lysophosphatidylcholine


enzyme_display_name: formyl-CoA hydrolase

organism: Unknown

substrate_name: Unknown

source_db: unknown

source_license: see source

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

assay_conditions_summary: cofactor CoA

enzyme: formyl-CoA hydrolase

substrate: Unknown

source: unknown


smiles: CC(C)(CO)C(C(=O)N(CCC(=O)NCCS)C=O)O


enzyme_display_name: hormone-sensitive lipase

organism: Halalkalibacterium halodurans

substrate_name: tricaproyl glycerol

smiles: CCCCCC(=O)OCC(COC(=O)CCCCC)OC(=O)CCCCC

enzyme: hormone-sensitive lipase

substrate: tricaproyl glycerol


substrate_name: trioleoyl glycerol

substrate: trioleoyl glycerol


substrate_name: tripalmitoyl glycerol

substrate: tripalmitoyl glycerol


enzyme_display_name: Monoacylglycerol lipase ABHD2

substrate_name: p-nitrophenyl acetate

column_label: PMID 27247428 Figure 2C/Results prose: pNPA row reports Km 12.40 +/- 1.02 mM with Vmax 2.69 +/- 0.15 umol/s*mg and kcat/Km 11.23 +/- 1.22 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=12.40 mM; expected value 12.4 mM.

raw_value_unit_evidence: Figure 2C prose reports pNPA Km 12.40 +/- 1.02 mM.

row_label: ABHD2 / pNPA (p-nitrophenyl acetate)

table_label: Figure 2C / Results prose: Ester hydrolase activity of ABHD2

enzyme: Monoacylglycerol lipase ABHD2

substrate: p-nitrophenyl acetate


substrate_name: p-nitrophenyl butyrate

column_label: PMID 27247428 Figure 2C/Results prose: pNPB row reports Km 11.76 +/- 1.15 mM with Vmax 3.71 +/- 0.36 umol/s*mg and kcat/Km 16.33 +/- 1.98 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=11.76 mM.

raw_value_unit_evidence: Figure 2C prose reports pNPB Km 11.76 +/- 1.15 mM.

row_label: ABHD2 / pNPB (p-nitrophenyl butyrate)

substrate: p-nitrophenyl butyrate


substrate_name: p-nitrophenyl palmitate

column_label: PMID 27247428 Figure 2C/Results prose: pNPP row reports Km 17.66 +/- 2.54 mM with Vmax 1.27 +/- 0.12 umol/s*mg and kcat/Km 3.72 +/- 0.95 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=17.66 mM.

raw_value_unit_evidence: Figure 2C prose reports pNPP Km 17.66 +/- 2.54 mM.

row_label: ABHD2 / pNPP (p-nitrophenyl palmitate)

substrate: p-nitrophenyl palmitate


enzyme_display_name: feruloyl esterase

organism: Talaromyces pinophilus

substrate_name: 4-nitrophenyl acetate

proof_lines:
Talaromyces cellulolyticus
feruloyl esterase B
p-nitrophenyl acetate

enzyme: feruloyl esterase

substrate: 4-nitrophenyl acetate


substrate_name: 4-nitrophenyl ferulate

substrate: 4-nitrophenyl ferulate


substrate_name: methyl ferulate

substrate: methyl ferulate


assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA


proof_lines:
wild-type protein, pH7.5, 25°C
pH 7.5, 37°C, wild-type


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


substrate_name: stearoyl-CoA

substrate: stearoyl-CoA


substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


substrate_name: n-decanoyl-CoA

substrate: n-decanoyl-CoA


substrate_name: palmitoleoyl-CoA

substrate: palmitoleoyl-CoA


substrate_name: linoleoyl-CoA

substrate: linoleoyl-CoA


substrate_name: tiglyl-CoA

substrate: tiglyl-CoA


organism: Saccharolobus solfataricus

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

column_label: Table 1 row 3-oxo-C10-L-HSL has the exact kcat and Km cells matching this tuple; package kcat/Km equals 1.5 / 0.050 = 30.0 s^-1 mM^-1.

normalized_value_unit_evidence: Km 0.050 mM; kcat 1.5 s^-1; kcat/Km 30.0 s^-1 mM^-1 from table mean kcat/Km; explicit table kcat/Km column reports 290 s^-1 mM^-1 and is internally inconsistent with the kcat and Km cells

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


column_label: Table 1 row 3-oxo-C12-L-HSL has matching Km and kcat cells; package kcat/Km equals 0.95 / 0.17 = 5.588235294117647 s^-1 mM^-1.

normalized_value_unit_evidence: Km 0.17 mM; kcat 0.95 s^-1; kcat/Km 5.5 s^-1 mM^-1 table-rounded; expected ratio 5.588235294117647 s^-1 mM^-1 from table means


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

column_label: Table 1 row 3-oxo-C6-L-HSL has matching Km and kcat cells; package kcat/Km equals 0.52 / 5.6 = 0.09285714285714286 s^-1 mM^-1.

normalized_value_unit_evidence: Km 5.6 mM; kcat 0.52 s^-1; kcat/Km 0.092 s^-1 mM^-1 table-rounded; expected ratio 0.09285714285714286 s^-1 mM^-1 from table means

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


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

column_label: Table 1 row 3-oxo-C8-L-HSL has matching Km and kcat cells; package kcat/Km equals 1.0 / 0.16 = 6.25 s^-1 mM^-1.

normalized_value_unit_evidence: Km 0.16 mM; kcat 1.0 s^-1; kcat/Km 6.6 s^-1 mM^-1 table-rounded; expected ratio 6.25 s^-1 mM^-1 from table means

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


substrate_name: myristoyl-CoA

proof_lines:
wild-type protein, pH7.5, 25°C
wild-type protein, pH7.5, 37°C
pH 7.5, 37°C, wild-type

substrate: myristoyl-CoA


substrate_name: n-hexanoyl-CoA

substrate: n-hexanoyl-CoA


substrate_name: Arachidonoyl-CoA

substrate: Arachidonoyl-CoA


substrate_name: n-propionyl-CoA

substrate: n-propionyl-CoA


substrate_name: n-butyryl-CoA

substrate: n-butyryl-CoA


substrate_name: glutaryl-CoA

substrate: glutaryl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: malonyl-CoA

substrate: malonyl-CoA


substrate_name: methylmalonyl-CoA

substrate: methylmalonyl-CoA


substrate_name: phenylacetyl-CoA

substrate: phenylacetyl-CoA


enzyme_display_name: Hormone-sensitive lipase

organism: Mus musculus

smiles: CCCCCCCCC=CCCCCCCCC(=O)OCC(CO)O

proof_lines:
MGL
hormone-sensitive lipase
monoacylglycerol

enzyme: Hormone-sensitive lipase


smiles: CCCCCCCCC=CCCCCCCCC(=O)OC(CO)CO


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

proof_lines:
MGL
2-arachidonoyl glycerol
cannabinoid receptors


substrate_name: palmitoyl-CoA

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

proof_lines: in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 1.0

proof_lines: in the presence of StarD2 protein in a molar ratio StarD2/Them2 of 0.5

substrate: palmitoyl-CoA


substrate_name: hexanoyl-CoA

substrate: hexanoyl-CoA


proof_lines: at 37°C, in the presence of small unilamellar vesicles composed of phosphatidylcholine at 4 mM total phospholipid concentration


substrate_name: lauroyl-CoA

substrate: lauroyl-CoA


substrate_name: decanoyl-CoA

substrate: decanoyl-CoA


substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


organism: Euglena gracilis

substrate_name: dodecanoyl-CoA

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA

substrate: dodecanoyl-CoA


substrate_name: hexadecanoyl-CoA

substrate: hexadecanoyl-CoA


substrate_name: tetradecanoyl-CoA

substrate: tetradecanoyl-CoA


substrate_name: octadecanoyl-CoA

substrate: octadecanoyl-CoA


substrate_name: octanoyl-CoA

substrate: octanoyl-CoA


organism: Alcaligenes faecalis

substrate_name: myristoyl-CoA

assay_conditions_summary: pH 7.6; 310.15 K; cofactor CoA

substrate: myristoyl-CoA


substrate_name: cis-vaccenoyl-CoA

substrate: cis-vaccenoyl-CoA


substrate_name: myristoleoyl-CoA

substrate: myristoleoyl-CoA


substrate_name: stearoyl-CoA

substrate: stearoyl-CoA


assay_conditions_summary: pH 7.6; 293.15 K; cofactor CoA


substrate_name: palmitoleoyl-CoA

substrate: palmitoleoyl-CoA


organism: Buckleyzyma aurantiaca

assay_conditions_summary: pH 7.4; 298.15 K; cofactor CoA


substrate_name: Arachidonoyl-CoA

substrate: Arachidonoyl-CoA


substrate_name: linoleoyl-CoA

substrate: linoleoyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


organism: Sus scrofa

substrate_name: n-butyryl-CoA

substrate: n-butyryl-CoA


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


substrate_name: succinyl-CoA

substrate: succinyl-CoA


substrate_name: n-decanoyl-CoA

assay_conditions_summary: pH 8; 301.15 K; cofactor CoA

proof_lines: pH 8.0, 28°C, with palmitoyl-CoA as substrate

substrate: n-decanoyl-CoA


organism: Homo sapiens


substrate_name: beta-hydroxybutyryl-CoA

substrate: beta-hydroxybutyryl-CoA


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


substrate_name: vaccenoyl-CoA

substrate: vaccenoyl-CoA


organism: Bos taurus


substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


organism: Cavia porcellus

substrate_name: hexadecanoyl-CoA

substrate: hexadecanoyl-CoA


enzyme_display_name: phenylacetyl-CoA hydrolase

organism: Streptococcus pneumoniae

substrate_name: phenylacetyl-CoA

assay_conditions_summary: pH 7.6; 294.15 K; cofactor CoA

enzyme: phenylacetyl-CoA hydrolase

substrate: phenylacetyl-CoA


substrate_name: decanoyl-CoA

substrate: decanoyl-CoA


organism: Diutina rugosa

substrate_name: dodecanoyl-CoA

substrate: dodecanoyl-CoA


assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA


proof_lines:
pH 7.4, 30°C
0 mM NaCl
100 mM NaCl


substrate_name: octanoyl-CoA

substrate: octanoyl-CoA


organism: Mesocricetus auratus

substrate_name: ADP

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ADP

substrate: ADP


substrate_name: Arachidonoyl-CoA

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines:
isozyme MTE-I, pH 7.4, 37°C
isozyme CTE-I, pH 7.4, 37°C
pH 7.4, 30°C

substrate: Arachidonoyl-CoA


substrate_name: nafamostat

ki_unit: mM

substrate: nafamostat


organism: Cricetulus griseus


organism: Rattus norvegicus

proof_lines:
pH 7.5, 37°C
recombinant enzyme
the induced E. coli enzyme


substrate_name: fatty-acyl-CoA thioester

substrate: fatty-acyl-CoA thioester


organism: Mougeotia scalaris


enzyme_display_name: 4-hydroxybenzoyl-CoA thioesterase

organism: Aromatoleum evansii

substrate_name: benzoyl-CoA

enzyme: 4-hydroxybenzoyl-CoA thioesterase

substrate: benzoyl-CoA


organism: Penicillium chrysogenum


organism: Arthrobacter sp.

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E73A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature E73Q to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row E73Q; column 'kcat (s-1)' = 1.7 x 10^-3; column 'Km (uM)' = 1.42 x 10^1; column 'kcat/ Km (M-1s-1)' = 1.2 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 4 cell 1.7 x 10^-3 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.0017 s^(-1). km: printed Table 4 cell 1.42 x 10^1 uM; 1.42 x 10^1 / 1000 = 0.0142 mM. kcat/Km: printed Table 4 cell 1.2 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 x 10^2 / 1000 = 0.12 s^-1 mM^-1.

row_label: Table 4, enzyme row E73Q, substrate 4-HB-CoA

table_label: Table 4: Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA plus the 4-HP-CoA dissociation and/or competitive inhibition constants (Biochemistry 2012, 51(35):7000-7016)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature T77D to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row T77D; column 'kcat (s-1)' = 1.03 x 10^-2; column 'Km (uM)' = 3.8 x 10^-1; column 'kcat/ Km (M-1s-1)' = 2.7 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 4 cell 1.03 x 10^-2 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.0103 s^(-1). km: printed Table 4 cell 3.8 x 10^-1 uM; 3.8 x 10^-1 / 1000 = 0.00038 mM. kcat/Km: printed Table 4 cell 2.7 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.7 x 10^4 / 1000 = 27.0 s^-1 mM^-1.

row_label: Table 4, enzyme row T77D, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature D31A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row D31A; column 'kcat (s-1)' = 4.17 x 10^-2; column 'Km (uM)' = 4.0; column 'kcat/ Km (M-1s-1)' = 1.0 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 4 cell 4.17 x 10^-2 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.0417 s^(-1). km: printed Table 4 cell 4.0 uM; 4.0 / 1000 = 0.004 mM. kcat/Km: printed Table 4 cell 1.0 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.0 x 10^4 / 1000 = 10.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row D31A: kcat = 4.17 x 10^-2 s^-1; Km = 4.0 uM; printed kcat/Km = 1.0 x 10^4 M^-1 s^-1.

row_label: Table 4, enzyme row D31A, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature E73D to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row E73D; column 'kcat (s-1)' = 1.23 x 10^-1; column 'Km (uM)' = 1.8 x 10^1; column 'kcat/ Km (M-1s-1)' = 6.8 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 4 cell 1.23 x 10^-1 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.123 s^(-1). km: printed Table 4 cell 1.8 x 10^1 uM; 1.8 x 10^1 / 1000 = 0.018 mM. kcat/Km: printed Table 4 cell 6.8 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.8 x 10^3 / 1000 = 6.8 s^-1 mM^-1.

row_label: Table 4, enzyme row E73D, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature Q58A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row Q58A; column 'kcat (s-1)' = 1.27 x 10^-1; column 'Km (uM)' = 1.6; column 'kcat/ Km (M-1s-1)' = 7.9 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 4 cell 1.27 x 10^-1 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.127 s^(-1). km: printed Table 4 cell 1.6 uM; 1.6 / 1000 = 0.0016 mM. kcat/Km: printed Table 4 cell 7.9 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.9 x 10^4 / 1000 = 79.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row Q58A: kcat = 1.27 x 10^-1 s^-1; Km = 1.6 uM; printed kcat/Km = 7.9 x 10^4 M^-1 s^-1.

row_label: Table 4, enzyme row Q58A, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature E73D/T77S to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row E73D/T77S; column 'kcat (s-1)' = 1.29 x 10^-1; column 'Km (uM)' = 1.3 x 10; column 'kcat/ Km (M-1s-1)' = 1.0 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 4 cell 1.29 x 10^-1 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.129 s^(-1). km: printed Table 4 cell 1.3 x 10 uM; 1.3 x 10 / 1000 = 0.013 mM. kcat/Km: printed Table 4 cell 1.0 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.0 x 10^4 / 1000 = 10.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row E73D/T77S: kcat = 1.29 x 10^-1 s^-1; Km = 1.3 x 10 uM; printed kcat/Km = 1.0 x 10^4 M^-1 s^-1.

row_label: Table 4, enzyme row E73D/T77S, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature Q58D to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row Q58D; column 'kcat (s-1)' = 1.3 x 10^-1; column 'Km (uM)' = 1.8 x 10^2; column 'kcat/ Km (M-1s-1)' = 7.2 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 4 cell 1.3 x 10^-1 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.13 s^(-1). km: printed Table 4 cell 1.8 x 10^2 uM; 1.8 x 10^2 / 1000 = 0.18 mM. kcat/Km: printed Table 4 cell 7.2 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.2 x 10^2 / 1000 = 0.72 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row Q58D: kcat = 1.3 x 10^-1 s^-1; Km = 1.8 x 10^2 uM; printed kcat/Km = 7.2 x 10^2 M^-1 s^-1.

row_label: Table 4, enzyme row Q58D, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature H64A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row H64A; column 'kcat (s-1)' = 1.5 x 10^-1; column 'Km (uM)' = 5.1 x 10^2; column 'kcat/ Km (M-1s-1)' = 2.9 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 4 cell 1.5 x 10^-1 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.15 s^(-1). km: printed Table 4 cell 5.1 x 10^2 uM; 5.1 x 10^2 / 1000 = 0.51 mM. kcat/Km: printed Table 4 cell 2.9 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.9 x 10^2 / 1000 = 0.29 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row H64A: kcat = 1.5 x 10^-1 s^-1; Km = 5.1 x 10^2 uM; printed kcat/Km = 2.9 x 10^2 M^-1 s^-1.

row_label: Table 4, enzyme row H64A, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature T77V to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row T77V; column 'kcat (s-1)' = 1.73 x 10^-1; column 'Km (uM)' = 5.5; column 'kcat/ Km (M-1s-1)' = 3.1 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 4 cell 1.73 x 10^-1 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.173 s^(-1). km: printed Table 4 cell 5.5 uM; 5.5 / 1000 = 0.0055 mM. kcat/Km: printed Table 4 cell 3.1 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.1 x 10^4 / 1000 = 31.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row T77V: kcat = 1.73 x 10^-1 s^-1; Km = 5.5 uM; printed kcat/Km = 3.1 x 10^4 M^-1 s^-1.

row_label: Table 4, enzyme row T77V, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature H64Q to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row H64Q; column 'kcat (s-1)' = 2.82 x 10^-1; column 'Km (uM)' = 2.37 x 10^2; column 'kcat/ Km (M-1s-1)' = 1.2 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 4 cell 2.82 x 10^-1 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.282 s^(-1). km: printed Table 4 cell 2.37 x 10^2 uM; 2.37 x 10^2 / 1000 = 0.237 mM. kcat/Km: printed Table 4 cell 1.2 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 x 10^3 / 1000 = 1.2 s^-1 mM^-1.

row_label: Table 4, enzyme row H64Q, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q58E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature E78A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row E78A; column 'kcat (s-1)' = 1.08; column 'Km (uM)' = 9.6 x 10^1; column 'kcat/ Km (M-1s-1)' = 1.1 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 4 cell 1.08 s^-1; already in s^-1, no unit conversion applies; the paper value is 1.08 s^(-1). km: printed Table 4 cell 9.6 x 10^1 uM; 9.6 x 10^1 / 1000 = 0.096 mM. kcat/Km: printed Table 4 cell 1.1 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^4 / 1000 = 11.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row E78A: kcat = 1.08 s^-1; Km = 9.6 x 10^1 uM; printed kcat/Km = 1.1 x 10^4 M^-1 s^-1.

row_label: Table 4, enzyme row E78A, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature D31N to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row D31N; column 'kcat (s-1)' = 1.15; column 'Km (uM)' = 1.28 x 10^1; column 'kcat/ Km (M-1s-1)' = 9.0 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 4 cell 1.15 s^-1; already in s^-1, no unit conversion applies; the paper value is 1.15 s^(-1). km: printed Table 4 cell 1.28 x 10^1 uM; 1.28 x 10^1 / 1000 = 0.0128 mM. kcat/Km: printed Table 4 cell 9.0 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9.0 x 10^4 / 1000 = 90.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row D31N: kcat = 1.15 s^-1; Km = 1.28 x 10^1 uM; printed kcat/Km = 9.0 x 10^4 M^-1 s^-1.

row_label: Table 4, enzyme row D31N, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature E73D/T77A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row E73D/T77A; column 'kcat (s-1)' = 1.54; column 'Km (uM)' = 4.6; column 'kcat/ Km (M-1s-1)' = 3.4 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 4 cell 1.54 s^-1; already in s^-1, no unit conversion applies; the paper value is 1.54 s^(-1). km: printed Table 4 cell 4.6 uM; 4.6 / 1000 = 0.0046 mM. kcat/Km: printed Table 4 cell 3.4 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.4 x 10^5 / 1000 = 340.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row E73D/T77A: kcat = 1.54 s^-1; Km = 4.6 uM; printed kcat/Km = 3.4 x 10^5 M^-1 s^-1.

row_label: Table 4, enzyme row E73D/T77A, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature T77A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row T77A; column 'kcat (s-1)' = 2.09; column 'Km (uM)' = 1.22; column 'kcat/ Km (M-1s-1)' = 1.7 x 10^6.

normalized_value_unit_evidence: kcat: printed Table 4 cell 2.09 s^-1; already in s^-1, no unit conversion applies; the paper value is 2.09 s^(-1). km: printed Table 4 cell 1.22 uM; 1.22 / 1000 = 0.00122 mM. kcat/Km: printed Table 4 cell 1.7 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.7 x 10^6 / 1000 = 1700.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row T77A: kcat = 2.09 s^-1; Km = 1.22 uM; printed kcat/Km = 1.7 x 10^6 M^-1 s^-1.

row_label: Table 4, enzyme row T77A, substrate 4-HB-CoA


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

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row Wild-Type; column 'kcat (s-1)' = 6.7; column 'Km (uM)' = 1.24; column 'kcat/ Km (M-1s-1)' = 5.4 x 10^6.

normalized_value_unit_evidence: kcat: printed Table 4 cell 6.7 s^-1; already in s^-1, no unit conversion applies; the paper value is 6.7 s^(-1). km: printed Table 4 cell 1.24 uM; 1.24 / 1000 = 0.00124 mM. kcat/Km: printed Table 4 cell 5.4 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.4 x 10^6 / 1000 = 5400.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row Wild-Type: kcat = 6.7 s^-1; Km = 1.24 uM; printed kcat/Km = 5.4 x 10^6 M^-1 s^-1.

row_label: Table 4, enzyme row Wild-Type, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature T77S to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row T77S; column 'kcat (s-1)' = 3.16; column 'Km (uM)' = 7.7 x 10^-1; column 'kcat/ Km (M-1s-1)' = 4.1 x 10^6.

normalized_value_unit_evidence: kcat: printed Table 4 cell 3.16 s^-1; already in s^-1, no unit conversion applies; the paper value is 3.16 s^(-1). km: printed Table 4 cell 7.7 x 10^-1 uM; 7.7 x 10^-1 / 1000 = 0.00077 mM. kcat/Km: printed Table 4 cell 4.1 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.1 x 10^6 / 1000 = 4100.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row T77S: kcat = 3.16 s^-1; Km = 7.7 x 10^-1 uM; printed kcat/Km = 4.1 x 10^6 M^-1 s^-1.

row_label: Table 4, enzyme row T77S, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature R150A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row R150A; column 'kcat (s-1)' = 9.5; column 'Km (uM)' = 1.5 x 10^1; column 'kcat/ Km (M-1s-1)' = 6.3 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 4 cell 9.5 s^-1; already in s^-1, no unit conversion applies; the paper value is 9.5 s^(-1). km: printed Table 4 cell 1.5 x 10^1 uM; 1.5 x 10^1 / 1000 = 0.015 mM. kcat/Km: printed Table 4 cell 6.3 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.3 x 10^5 / 1000 = 630.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row R150A: kcat = 9.5 s^-1; Km = 1.5 x 10^1 uM; printed kcat/Km = 6.3 x 10^5 M^-1 s^-1.

row_label: Table 4, enzyme row R150A, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature T121A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row T121A; column 'kcat (s-1)' = 9.7; column 'Km (uM)' = 6.1; column 'kcat/ Km (M-1s-1)' = 1.6 x 10^6.

normalized_value_unit_evidence: kcat: printed Table 4 cell 9.7 s^-1; already in s^-1, no unit conversion applies; the paper value is 9.7 s^(-1). km: printed Table 4 cell 6.1 uM; 6.1 / 1000 = 0.0061 mM. kcat/Km: printed Table 4 cell 1.6 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.6 x 10^6 / 1000 = 1600.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row T121A: kcat = 9.7 s^-1; Km = 6.1 uM; printed kcat/Km = 1.6 x 10^6 M^-1 s^-1.

row_label: Table 4, enzyme row T121A, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature S120A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row S120A; column 'kcat (s-1)' = 1.01 x 10; column 'Km (uM)' = 1.6; column 'kcat/ Km (M-1s-1)' = 6.3 x 10^6.

normalized_value_unit_evidence: kcat: printed Table 4 cell 1.01 x 10 s^-1; already in s^-1, no unit conversion applies; the paper value is 10.1 s^(-1). km: printed Table 4 cell 1.6 uM; 1.6 / 1000 = 0.0016 mM. kcat/Km: printed Table 4 cell 6.3 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.3 x 10^6 / 1000 = 6300.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row S120A: kcat = 1.01 x 10 s^-1; Km = 1.6 uM; printed kcat/Km = 6.3 x 10^6 M^-1 s^-1.

row_label: Table 4, enzyme row S120A, substrate 4-HB-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04416 and applied mutation signature R102A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic constants determined for wild-type and mutant thioesterase catalyzed hydrolysis of 4-HB-CoA), enzyme row R102A; column 'kcat (s-1)' = 9.9; column 'Km (uM)' = 1.4 x 10^1; column 'kcat/ Km (M-1s-1)' = 7.1 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 4 cell 9.9 s^-1; already in s^-1, no unit conversion applies; the paper value is 9.9 s^(-1). km: printed Table 4 cell 1.4 x 10^1 uM; 1.4 x 10^1 / 1000 = 0.014 mM. kcat/Km: printed Table 4 cell 7.1 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.1 x 10^5 / 1000 = 710.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, enzyme row R102A: kcat = 9.9 s^-1; Km = 1.4 x 10^1 uM; printed kcat/Km = 7.1 x 10^5 M^-1 s^-1.

row_label: Table 4, enzyme row R102A, substrate 4-HB-CoA


organism: Pseudomonas sp.

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K90A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


proof_lines: wild-type enzyme and mutant R89L, pH 7.5, 25°C


enzyme_display_name: Medium/long-chain acyl-CoA thioesterase YigI

organism: Escherichia coli (strain K12)

proof_lines: kcat is 1.461 sec(-1) with decanoyl-CoA as substrate. kcat is 3.204 sec(-1) with hexadecanoyl-CoA as substrate.


enzyme: Medium/long-chain acyl-CoA thioesterase YigI


enzyme_display_name: Acyl-CoA thioesterase 2

proof_lines: kcat is 83 sec(-1) with decanoyl-CoA as substrate.

enzyme: Acyl-CoA thioesterase 2


organism: Mus musculus

substrate_name: arachidoyl-CoA

substrate: arachidoyl-CoA


organism: Mycolicibacterium smegmatis

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

assay_conditions_summary: pH 8.5; cofactor CoA

column_label: Table IV row Palmitoyl, column Apparent Km (x10^-6 M)

raw_value_unit_evidence: Apparent Km (x10^-6 M) = 6.2

row_label: Palmitoyl; 16:0

table_label: Table IV: Dependence of thioesterase activity on chain length of acyl-CoAs


enzyme_display_name: Palmitoyl-protein thioesterase 1

substrate_name: S-palmitoyl H-Ras

enzyme: Palmitoyl-protein thioesterase 1

substrate: S-palmitoyl H-Ras


enzyme_display_name: Acyl-protein thioesterase 1

substrate_name: thioesterase activity

enzyme: Acyl-protein thioesterase 1

substrate: thioesterase activity


enzyme_display_name: Acyl-protein thioesterase 2

substrate_name: prostaglandin D2-glycerol ester (PGD2-G)

enzyme: Acyl-protein thioesterase 2


substrate_name: lysophosphatidylglycerol 18:1 (at pH 5)

assay_conditions_summary: pH 5

substrate: lysophosphatidylglycerol 18:1 (at pH 5)


substrate_name: 4-Hydroxybenzoyl-CoA; H2O

substrate: 4-Hydroxybenzoyl-CoA; H2O


organism: Bacillus halodurans

substrate_name: 4-Chlorobenzoyl-CoA; H2O

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

substrate: 4-Chlorobenzoyl-CoA; H2O


substrate_name: 2,5-Dihydroxybenzoyl-CoA; H2O

substrate: 2,5-Dihydroxybenzoyl-CoA; H2O


organism: Pseudomonas reinekei

substrate_name: H2O; 3-Hydroxybenzoyl-CoA

proof_lines:
pH 7.5, 25°C
Raw SKiD Env: Temp=25°C, pH=7.5

source_databases_merged: sabio_rk brenda skid uniprot

substrate: H2O; 3-Hydroxybenzoyl-CoA


organism: Escherichia coli K-12

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H54A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


organism: Homo sapiens

substrate_name: 3-Hydroxyphenylacetyl-CoA; H2O

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

assay_conditions_summary: 298.15 K; cofactor CoA

substrate: 3-Hydroxyphenylacetyl-CoA; H2O


organism: Umbellularia californica

substrate_name: tetradecanoyl-[acyl-carrier protein]

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M197R/R199H/T231K to reconstruct the assayed variant sequence.

substrate: tetradecanoyl-[acyl-carrier protein]


enzyme_display_name: Palmitoyl-protein thioesterase ABHD10, mitochondrial

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: Palmitoyl thioesterase CPT1C

enzyme: Palmitoyl thioesterase CPT1C


substrate_name: tetradecanoyl-CoA

substrate: tetradecanoyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D17E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R126L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R128A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R88A to reconstruct the assayed variant sequence.


enzyme_display_name: Acyl-CoA hydrolase 2

organism: Arabidopsis thaliana

enzyme: Acyl-CoA hydrolase 2


enzyme_display_name: UniProt P44886

organism: Haemophilus influenzae

substrate_name: n-butyrylpantethiene phosphate

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P44886

substrate: n-butyrylpantethiene phosphate


enzyme_display_name: acyl-CoA hydrolase

enzyme: acyl-CoA hydrolase


organism: Saccharomyces cerevisiae

substrate_name: dodecanoyl-CoA

assay_conditions_summary: pH 8; cofactor CoA

column_label: Table 2 row C12:0, column Km = 10.4 uM.

row_label: C12:0 / lauroyl-CoA / dodecanoyl-CoA

table_label: Table 2

substrate: dodecanoyl-CoA


substrate_name: H2O; Dodecanoyl-[acyl-carrier protein]

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

substrate: H2O; Dodecanoyl-[acyl-carrier protein]


enzyme_display_name: palmitoyl[protein] hydrolase

organism: Bos taurus

substrate_name: Myristoyl-CoA; H2O

assay_conditions_summary: cofactor CoA

enzyme: palmitoyl[protein] hydrolase

substrate: Myristoyl-CoA; H2O


substrate_name: butanoyl-CoA

column_label: Table 1 row Butyryl-CoA under TesB Kmb lists 75 uM.

raw_value_unit_evidence: Km raw_value=75 raw_unit=uM

row_label: Butyryl-CoA / TesB

table_label: Table 1. A summary of kinetic parameters and the coefficient of determination in TesB and PTE1.

substrate: butanoyl-CoA


column_label: Table 1 row trans-Delta2-butenoyl-CoA under TesB Kmb lists 60 uM.

raw_value_unit_evidence: Km raw_value=60 raw_unit=uM

row_label: trans-Delta2-butenoyl-CoA / TesB


column_label: Table 1 row DL-3-hydroxybutyryl-CoA under TesB Kmb lists 81 uM.

raw_value_unit_evidence: Km raw_value=81 raw_unit=uM

row_label: DL-3-hydroxybutyryl-CoA / TesB


column_label: Table 1 row 3-Ketobutyryl-CoA under TesB Kmb lists 46 uM.

raw_value_unit_evidence: Km raw_value=46 raw_unit=uM

row_label: 3-Ketobutyryl-CoA / TesB


column_label: Table 1 row trans-Delta2-dodecenoyl-CoA under TesB Kmb lists 12 uM.

raw_value_unit_evidence: Km raw_value=12 raw_unit=uM

row_label: trans-Delta2-dodecenoyl-CoA / TesB


substrate_name: Arachidonyl-CoA

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

column_label: Table 2, row 'Arachidonoyl-CoA', columns kcat, Km, kcat/Km. Table 2 caption: wild-type hTHEM2 acyl-CoA thioester hydrolysis in 50 mM K+ HEPES, pH 7.5, 25 C, 1 mM DTNB; kcat in s^-1, Km in uM, kcat/Km in M^-1 s^-1.

row_label: Arachidonoyl-CoA

substrate: Arachidonyl-CoA


substrate_name: crotonoyl-CoA

column_label: Table 2, row '2-Butenoyl-CoA', columns kcat, Km, kcat/Km. Table 2 caption: wild-type hTHEM2 acyl-CoA thioester hydrolysis in 50 mM K+ HEPES, pH 7.5, 25 C, 1 mM DTNB; kcat in s^-1, Km in uM, kcat/Km in M^-1 s^-1.

substrate: crotonoyl-CoA


substrate_name: Hexanoyl-CoA

column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Hexanoyl-CoA, column kcat s^-1, raw cell (2.2 +/- 0.1) x 10-2, normalized 0.022 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Hexanoyl-CoA, column kcat/Km M^-1 s^-1, raw cell 3.1 x 102, normalized 0.31 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Hexanoyl-CoA, column Km uM, raw cell (7.0 +/- 0.6) x 101, normalized 0.07 mM

normalized_value_unit_evidence: kcat normalized_value=0.022 normalized_unit=s^-1; kcat/Km normalized_value=0.31 normalized_unit=s^-1*mM^-1; Km normalized_value=0.07 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.022 raw_unit=s^-1 raw_cell=(2.2 +/- 0.1) x 10-2; kcat/Km raw_value=310 raw_unit=M^-1*s^-1 raw_cell=3.1 x 102; Km raw_value=70 raw_unit=uM raw_cell=(7.0 +/- 0.6) x 101

row_label: n-Hexanoyl-CoA

substrate: Hexanoyl-CoA


substrate_name: Lauroyl-CoA

column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Lauroyl-CoA, column kcat s^-1, raw cell (1.9 +/- 0.1) x 10-2, normalized 0.019 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Lauroyl-CoA, column kcat/Km M^-1 s^-1, raw cell 1.9 x 103, normalized 1.9 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Lauroyl-CoA, column Km uM, raw cell 9.9 +/- 0.8, normalized 0.0099 mM

normalized_value_unit_evidence: kcat normalized_value=0.019 normalized_unit=s^-1; kcat/Km normalized_value=1.9 normalized_unit=s^-1*mM^-1; Km normalized_value=0.0099 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.019 raw_unit=s^-1 raw_cell=(1.9 +/- 0.1) x 10-2; kcat/Km raw_value=1900 raw_unit=M^-1*s^-1 raw_cell=1.9 x 103; Km raw_value=9.9 raw_unit=uM raw_cell=9.9 +/- 0.8

row_label: Lauroyl-CoA

substrate: Lauroyl-CoA


substrate_name: Linoleoyl-CoA

column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Linoleoyl-CoA, column kcat s^-1, raw cell (1.7+/- 0.1) x 10-2, normalized 0.017 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Linoleoyl-CoA, column kcat/Km M^-1 s^-1, raw cell 5.4 x 101, normalized 0.054 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Linoleoyl-CoA, column Km uM, raw cell (3.1 +/- 0.4) x 102, normalized 0.31 mM

normalized_value_unit_evidence: kcat normalized_value=0.017 normalized_unit=s^-1; kcat/Km normalized_value=0.054 normalized_unit=s^-1*mM^-1; Km normalized_value=0.31 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.017 raw_unit=s^-1 raw_cell=(1.7+/- 0.1) x 10-2; kcat/Km raw_value=54 raw_unit=M^-1*s^-1 raw_cell=5.4 x 101; Km raw_value=310 raw_unit=uM raw_cell=(3.1 +/- 0.4) x 102

row_label: Linoleoyl-CoA

substrate: Linoleoyl-CoA


substrate_name: Malonyl-CoA

column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Malonyl-CoA, column kcat s^-1, raw cell (6.6 +/- 0.6) x 10-2, normalized 0.066 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Malonyl-CoA, column kcat/Km M^-1 s^-1, raw cell 2.4x 102, normalized 0.24 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Malonyl-CoA, column Km uM, raw cell (2.8 +/- 0.8) x 102, normalized 0.28 mM

normalized_value_unit_evidence: kcat normalized_value=0.066 normalized_unit=s^-1; kcat/Km normalized_value=0.24 normalized_unit=s^-1*mM^-1; Km normalized_value=0.28 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.066 raw_unit=s^-1 raw_cell=(6.6 +/- 0.6) x 10-2; kcat/Km raw_value=240 raw_unit=M^-1*s^-1 raw_cell=2.4x 102; Km raw_value=280 raw_unit=uM raw_cell=(2.8 +/- 0.8) x 102

row_label: Malonyl-CoA

substrate: Malonyl-CoA


substrate_name: Octanoyl-CoA

column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Octanoyl-CoA, column kcat s^-1, raw cell (4.7 +/- 0.1) x 10-3, normalized 0.0047 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Octanoyl-CoA, column kcat/Km M^-1 s^-1, raw cell 1.8x 102, normalized 0.18 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Octanoyl-CoA, column Km uM, raw cell (2.6 +/- 0.3) x 101, normalized 0.026 mM

normalized_value_unit_evidence: kcat normalized_value=0.0047 normalized_unit=s^-1; kcat/Km normalized_value=0.18 normalized_unit=s^-1*mM^-1; Km normalized_value=0.026 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.0047 raw_unit=s^-1 raw_cell=(4.7 +/- 0.1) x 10-3; kcat/Km raw_value=180 raw_unit=M^-1*s^-1 raw_cell=1.8x 102; Km raw_value=26 raw_unit=uM raw_cell=(2.6 +/- 0.3) x 101

row_label: n-Octanoyl-CoA

substrate: Octanoyl-CoA


substrate_name: Oleoyl-CoA

column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Oleoyl-CoA, column kcat s^-1, raw cell (1.1 +/- 0.1) x 10-2, normalized 0.011 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Oleoyl-CoA, column kcat/Km M^-1 s^-1, raw cell 1.3 x 103, normalized 1.3 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Oleoyl-CoA, column Km uM, raw cell 9 +/- 1, normalized 0.009 mM

normalized_value_unit_evidence: kcat normalized_value=0.011 normalized_unit=s^-1; kcat/Km normalized_value=1.3 normalized_unit=s^-1*mM^-1; Km normalized_value=0.009 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.011 raw_unit=s^-1 raw_cell=(1.1 +/- 0.1) x 10-2; kcat/Km raw_value=1300 raw_unit=M^-1*s^-1 raw_cell=1.3 x 103; Km raw_value=9 raw_unit=uM raw_cell=9 +/- 1

row_label: Oleoyl-CoA

substrate: Oleoyl-CoA


substrate_name: Palmitoleoyl-CoA

column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Palmitoleoyl-CoA, column kcat s^-1, raw cell (1.7+/- 0.1) x 10-2, normalized 0.017 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Palmitoleoyl-CoA, column kcat/Km M^-1 s^-1, raw cell 1.9 x 103, normalized 1.9 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Palmitoleoyl-CoA, column Km uM, raw cell 9 +/- 2, normalized 0.009 mM

normalized_value_unit_evidence: kcat normalized_value=0.017 normalized_unit=s^-1; kcat/Km normalized_value=1.9 normalized_unit=s^-1*mM^-1; Km normalized_value=0.009 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.017 raw_unit=s^-1 raw_cell=(1.7+/- 0.1) x 10-2; kcat/Km raw_value=1900 raw_unit=M^-1*s^-1 raw_cell=1.9 x 103; Km raw_value=9 raw_unit=uM raw_cell=9 +/- 2

row_label: Palmitoleoyl-CoA

substrate: Palmitoleoyl-CoA


substrate_name: Palmitoyl-CoA

column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Palmitoyl-CoA, column kcat s^-1, raw cell (4.4 +/- 0.1) x 10-3, normalized 0.0044 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Palmitoyl-CoA, column kcat/Km M^-1 s^-1, raw cell 2.8 x 102, normalized 0.28 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Palmitoyl-CoA, column Km uM, raw cell (1.6 +/- 0.1) x 101, normalized 0.016 mM

normalized_value_unit_evidence: kcat normalized_value=0.0044 normalized_unit=s^-1; kcat/Km normalized_value=0.28 normalized_unit=s^-1*mM^-1; Km normalized_value=0.016 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.0044 raw_unit=s^-1 raw_cell=(4.4 +/- 0.1) x 10-3; kcat/Km raw_value=280 raw_unit=M^-1*s^-1 raw_cell=2.8 x 102; Km raw_value=16 raw_unit=uM raw_cell=(1.6 +/- 0.1) x 101

row_label: n-Palmitoyl-CoA

substrate: Palmitoyl-CoA


column_label: Table 2, row 'β-Hydroxybutyryl-CoA', columns kcat, Km, kcat/Km. Table 2 caption: wild-type hTHEM2 acyl-CoA thioester hydrolysis in 50 mM K+ HEPES, pH 7.5, 25 C, 1 mM DTNB; kcat in s^-1, Km in uM, kcat/Km in M^-1 s^-1.

row_label: β-Hydroxybutyryl-CoA


column_label: Table 2, row 'β-Methylcrotonyl-CoA', columns kcat, Km, kcat/Km. Table 2 caption: wild-type hTHEM2 acyl-CoA thioester hydrolysis in 50 mM K+ HEPES, pH 7.5, 25 C, 1 mM DTNB; kcat in s^-1, Km in uM, kcat/Km in M^-1 s^-1.

row_label: β-Methylcrotonyl-CoA


column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Methylmalonyl-CoA, column kcat s^-1, raw cell (8.3+/- 0.1) x 10-2, normalized 0.083 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Methylmalonyl-CoA, column kcat/Km M^-1 s^-1, raw cell 3.9 x 102, normalized 0.39 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Methylmalonyl-CoA, column Km uM, raw cell (2.1 +/- 0.1) x 102, normalized 0.21 mM

normalized_value_unit_evidence: kcat normalized_value=0.083 normalized_unit=s^-1; kcat/Km normalized_value=0.39 normalized_unit=s^-1*mM^-1; Km normalized_value=0.21 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.083 raw_unit=s^-1 raw_cell=(8.3+/- 0.1) x 10-2; kcat/Km raw_value=390 raw_unit=M^-1*s^-1 raw_cell=3.9 x 102; Km raw_value=210 raw_unit=uM raw_cell=(2.1 +/- 0.1) x 102

row_label: Methylmalonyl-CoA


column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row 3,4-Dihydroxyphenylacetyl-CoA, column kcat s^-1, raw cell (1.9 +/- 0.1) x 10-1, normalized 0.19 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row 3,4-Dihydroxyphenylacetyl-CoA, column kcat/Km M^-1 s^-1, raw cell 1.8 x 104, normalized 18 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row 3,4-Dihydroxyphenylacetyl-CoA, column Km uM, raw cell (1.0 +/- 0.1) x 101, normalized 0.01 mM

normalized_value_unit_evidence: kcat normalized_value=0.19 normalized_unit=s^-1; kcat/Km normalized_value=18 normalized_unit=s^-1*mM^-1; Km normalized_value=0.01 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.19 raw_unit=s^-1 raw_cell=(1.9 +/- 0.1) x 10-1; kcat/Km raw_value=18000 raw_unit=M^-1*s^-1 raw_cell=1.8 x 104; Km raw_value=10 raw_unit=uM raw_cell=(1.0 +/- 0.1) x 101


column_label: Table 2, row '3,5-Dihydroxyphenylacetyl-CoA', columns kcat, Km, kcat/Km. Table 2 caption: wild-type hTHEM2 acyl-CoA thioester hydrolysis in 50 mM K+ HEPES, pH 7.5, 25 C, 1 mM DTNB; kcat in s^-1, Km in uM, kcat/Km in M^-1 s^-1.


column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row 3-Hydroxy-3-methylglutaryl-CoA, column kcat s^-1, raw cell (7.9 +/- 0.2) x 10-2, normalized 0.079 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row 3-Hydroxy-3-methylglutaryl-CoA, column kcat/Km M^-1 s^-1, raw cell 2.7 x 101, normalized 0.027 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row 3-Hydroxy-3-methylglutaryl-CoA, column Km uM, raw cell (2.9 +/- 0.2) x 103, normalized 2.9 mM

normalized_value_unit_evidence: kcat normalized_value=0.079 normalized_unit=s^-1; kcat/Km normalized_value=0.027 normalized_unit=s^-1*mM^-1; Km normalized_value=2.9 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.079 raw_unit=s^-1 raw_cell=(7.9 +/- 0.2) x 10-2; kcat/Km raw_value=27 raw_unit=M^-1*s^-1 raw_cell=2.7 x 101; Km raw_value=2900 raw_unit=uM raw_cell=(2.9 +/- 0.2) x 103


column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row 3-Hydroxybenzoyl-CoA, column kcat s^-1, raw cell (1.1 +/- 0.1) x 10-2, normalized 0.011 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row 3-Hydroxybenzoyl-CoA, column kcat/Km M^-1 s^-1, raw cell 3.5 x 102, normalized 0.35 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row 3-Hydroxybenzoyl-CoA, column Km uM, raw cell (3.2 +/- 0.2) x 101, normalized 0.032 mM

normalized_value_unit_evidence: kcat normalized_value=0.011 normalized_unit=s^-1; kcat/Km normalized_value=0.35 normalized_unit=s^-1*mM^-1; Km normalized_value=0.032 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.011 raw_unit=s^-1 raw_cell=(1.1 +/- 0.1) x 10-2; kcat/Km raw_value=350 raw_unit=M^-1*s^-1 raw_cell=3.5 x 102; Km raw_value=32 raw_unit=uM raw_cell=(3.2 +/- 0.2) x 101


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9NPJ3 and applied mutation signature D65E to reconstruct the assayed variant sequence.

column_label: Table 3, row 'D65E', columns kcat, Km, kcat/Km. Table 3 caption: hTHEM2 wild-type/mutant hydrolysis of 3-hydroxyphenylacetyl-CoA in 50 mM K+ HEPES, pH 7.5, 25 C, 1 mM DTNB; kcat in s^-1, Km in uM, kcat/Km in M^-1 s^-1.

table_label: Table 3


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9NPJ3 and applied mutation signature D65N to reconstruct the assayed variant sequence.

column_label: Table 3, row 'D65N', columns kcat, Km, kcat/Km. Table 3 caption: hTHEM2 wild-type/mutant hydrolysis of 3-hydroxyphenylacetyl-CoA in 50 mM K+ HEPES, pH 7.5, 25 C, 1 mM DTNB; kcat in s^-1, Km in uM, kcat/Km in M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H134A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9NPJ3 and applied mutation signature H137A to reconstruct the assayed variant sequence.

column_label: Table 3, row 'H137A', columns kcat, Km, kcat/Km. Table 3 caption: hTHEM2 wild-type/mutant hydrolysis of 3-hydroxyphenylacetyl-CoA in 50 mM K+ HEPES, pH 7.5, 25 C, 1 mM DTNB; kcat in s^-1, Km in uM, kcat/Km in M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9NPJ3 and applied mutation signature H56A to reconstruct the assayed variant sequence.

column_label: Table 3, row 'H56A', columns kcat, Km, kcat/Km. Table 3 caption: hTHEM2 wild-type/mutant hydrolysis of 3-hydroxyphenylacetyl-CoA in 50 mM K+ HEPES, pH 7.5, 25 C, 1 mM DTNB; kcat in s^-1, Km in uM, kcat/Km in M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9NPJ3 and applied mutation signature K136A to reconstruct the assayed variant sequence.

column_label: Table 3, row 'K136A', columns kcat, Km, kcat/Km. Table 3 caption: hTHEM2 wild-type/mutant hydrolysis of 3-hydroxyphenylacetyl-CoA in 50 mM K+ HEPES, pH 7.5, 25 C, 1 mM DTNB; kcat in s^-1, Km in uM, kcat/Km in M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9NPJ3 and applied mutation signature N50A to reconstruct the assayed variant sequence.

column_label: Table 3, row 'N50A', columns kcat, Km, kcat/Km. Table 3 caption: hTHEM2 wild-type/mutant hydrolysis of 3-hydroxyphenylacetyl-CoA in 50 mM K+ HEPES, pH 7.5, 25 C, 1 mM DTNB; kcat in s^-1, Km in uM, kcat/Km in M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9NPJ3 and applied mutation signature S83A to reconstruct the assayed variant sequence.

column_label: Table 3, row 'S83A', columns kcat, Km, kcat/Km. Table 3 caption: hTHEM2 wild-type/mutant hydrolysis of 3-hydroxyphenylacetyl-CoA in 50 mM K+ HEPES, pH 7.5, 25 C, 1 mM DTNB; kcat in s^-1, Km in uM, kcat/Km in M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9NPJ3 and applied mutation signature T69A to reconstruct the assayed variant sequence.

column_label: Table 3, row 'T69A', columns kcat, Km, kcat/Km. Table 3 caption: hTHEM2 wild-type/mutant hydrolysis of 3-hydroxyphenylacetyl-CoA in 50 mM K+ HEPES, pH 7.5, 25 C, 1 mM DTNB; kcat in s^-1, Km in uM, kcat/Km in M^-1 s^-1.


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

column_label: Table 3, row 'WT', columns kcat, Km, kcat/Km. Table 3 caption: hTHEM2 wild-type/mutant hydrolysis of 3-hydroxyphenylacetyl-CoA in 50 mM K+ HEPES, pH 7.5, 25 C, 1 mM DTNB; kcat in s^-1, Km in uM, kcat/Km in M^-1 s^-1.

row_label: WT


column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row 4-Chlorobenzoyl-CoA, column kcat s^-1, raw cell (3.2 +/- 0.2) x 10-3, normalized 0.0032 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row 4-Chlorobenzoyl-CoA, column kcat/Km M^-1 s^-1, raw cell 2.5 x 101, normalized 0.025 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row 4-Chlorobenzoyl-CoA, column Km uM, raw cell (1.3 +/- 0.2) x 102, normalized 0.13 mM

normalized_value_unit_evidence: kcat normalized_value=0.0032 normalized_unit=s^-1; kcat/Km normalized_value=0.025 normalized_unit=s^-1*mM^-1; Km normalized_value=0.13 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.0032 raw_unit=s^-1 raw_cell=(3.2 +/- 0.2) x 10-3; kcat/Km raw_value=25 raw_unit=M^-1*s^-1 raw_cell=2.5 x 101; Km raw_value=130 raw_unit=uM raw_cell=(1.3 +/- 0.2) x 102


column_label: Table 2, row '4-Hydroxyphenylacetyl-CoA', columns kcat, Km, kcat/Km. Table 2 caption: wild-type hTHEM2 acyl-CoA thioester hydrolysis in 50 mM K+ HEPES, pH 7.5, 25 C, 1 mM DTNB; kcat in s^-1, Km in uM, kcat/Km in M^-1 s^-1.


substrate_name: Acetyl-CoA

column_label: Table 2, row 'Acetyl-CoA', columns kcat, Km, kcat/Km. Table 2 caption: wild-type hTHEM2 acyl-CoA thioester hydrolysis in 50 mM K+ HEPES, pH 7.5, 25 C, 1 mM DTNB; kcat in s^-1, Km in uM, kcat/Km in M^-1 s^-1.

row_label: Acetyl-CoA

substrate: Acetyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed:Q04416 and applied mutation signature D31A to reconstruct the assayed variant sequence.

column_label: Table 4. Steady-State Kinetic Constants Determined for Wild-Type and Mutant Thioesterase Catalyzed Hydrolysis of 4-HB-CoA; row D31A; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells kcat=(4.17 +/- 0.05) x 10^-2, Km=4.0 +/- 0.1 uM, kcat/Km=1.0 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.0417 normalized_unit=s^-1; Km normalized_value=0.004 normalized_unit=mM; kcat/Km normalized_value=10 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=(4.17 +/- 0.05) x 10^-2 raw_unit=s^-1; Km raw_value=4.0 +/- 0.1 raw_unit=uM; kcat/Km raw_value=1.0 x 10^4 raw_unit=M^-1 s^-1

table_label: Table 4. Steady-State Kinetic Constants Determined for Wild-Type and Mutant Thioesterase Catalyzed Hydrolysis of 4-HB-CoA.


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed:Q04416 and applied mutation signature D31N to reconstruct the assayed variant sequence.

column_label: Table 4. Steady-State Kinetic Constants Determined for Wild-Type and Mutant Thioesterase Catalyzed Hydrolysis of 4-HB-CoA; row D31N; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells kcat=1.15 +/- 0.03, Km=(1.28 +/- 0.08) x 10^1 uM, kcat/Km=9.0 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=1.15 normalized_unit=s^-1; Km normalized_value=0.0128 normalized_unit=mM; kcat/Km normalized_value=90 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.15 +/- 0.03 raw_unit=s^-1; Km raw_value=(1.28 +/- 0.08) x 10^1 raw_unit=uM; kcat/Km raw_value=9.0 x 10^4 raw_unit=M^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed:Q04416 and applied mutation signature E73D to reconstruct the assayed variant sequence.

column_label: Table 4. Steady-State Kinetic Constants Determined for Wild-Type and Mutant Thioesterase Catalyzed Hydrolysis of 4-HB-CoA; row E73D; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells kcat=(1.23 +/- 0.03) x 10^-1, Km=(1.8 +/- 0.1) x 10^1 uM, kcat/Km=6.8 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.123 normalized_unit=s^-1; Km normalized_value=0.018 normalized_unit=mM; kcat/Km normalized_value=6.8 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=(1.23 +/- 0.03) x 10^-1 raw_unit=s^-1; Km raw_value=(1.8 +/- 0.1) x 10^1 raw_unit=uM; kcat/Km raw_value=6.8 x 10^3 raw_unit=M^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed:Q04416 and applied mutation signature E73D/T77A to reconstruct the assayed variant sequence.

column_label: Table 4. Steady-State Kinetic Constants Determined for Wild-Type and Mutant Thioesterase Catalyzed Hydrolysis of 4-HB-CoA; row E73D/T77A; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells kcat=1.54 +/- 0.02, Km=4.6 +/- 0.1 uM, kcat/Km=3.4 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=1.54 normalized_unit=s^-1; Km normalized_value=0.0046 normalized_unit=mM; kcat/Km normalized_value=340 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.54 +/- 0.02 raw_unit=s^-1; Km raw_value=4.6 +/- 0.1 raw_unit=uM; kcat/Km raw_value=3.4 x 10^5 raw_unit=M^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed:Q04416 and applied mutation signature E73D/T77S to reconstruct the assayed variant sequence.

column_label: Table 4. Steady-State Kinetic Constants Determined for Wild-Type and Mutant Thioesterase Catalyzed Hydrolysis of 4-HB-CoA; row E73D/T77S; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells kcat=(1.29 +/- 0.09) x 10^-1, Km=(1.3 +/- 0.2) x 10 uM, kcat/Km=1.0 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.129 normalized_unit=s^-1; Km normalized_value=0.013 normalized_unit=mM; kcat/Km normalized_value=10 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=(1.29 +/- 0.09) x 10^-1 raw_unit=s^-1; Km raw_value=(1.3 +/- 0.2) x 10 raw_unit=uM; kcat/Km raw_value=1.0 x 10^4 raw_unit=M^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed:Q04416 and applied mutation signature E73Q to reconstruct the assayed variant sequence.

column_label: Table 4. Steady-State Kinetic Constants Determined for Wild-Type and Mutant Thioesterase Catalyzed Hydrolysis of 4-HB-CoA; row E73Q; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells kcat=(1.7 +/- 0.2) x 10^-3, Km=(1.42 +/- 0.06) x 10^1 uM, kcat/Km=1.2 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.0017 normalized_unit=s^-1; Km normalized_value=0.0142 normalized_unit=mM; kcat/Km normalized_value=0.12 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=(1.7 +/- 0.2) x 10^-3 raw_unit=s^-1; Km raw_value=(1.42 +/- 0.06) x 10^1 raw_unit=uM; kcat/Km raw_value=1.2 x 10^2 raw_unit=M^-1 s^-1