sequence_variant_note: Resolved canonical sequence from uniprot_reviewed: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; row R102A; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells kcat=9.9 +/- 0.3, Km=(1.4 +/- 0.1) x 10 uM, kcat/Km=7.1 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=9.9 normalized_unit=s^-1; Km normalized_value=0.014 normalized_unit=mM; kcat/Km normalized_value=710 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=9.9 +/- 0.3 raw_unit=s^-1; Km raw_value=(1.4 +/- 0.1) x 10 raw_unit=uM; kcat/Km raw_value=7.1 x 10^5 raw_unit=M^-1 s^-1


enzyme_display_name: 4-hydroxybenzoyl-CoA thioesterase

organism: Arthrobacter sp.

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

mutation_type: substitution

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

column_label: Table 4. Steady-State Kinetic Constants Determined for Wild-Type and Mutant Thioesterase Catalyzed Hydrolysis of 4-HB-CoA; row R150A; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells kcat=9.5 +/- 0.4, Km=(1.5 +/- 0.1) x 10^1 uM, kcat/Km=6.3 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=9.5 normalized_unit=s^-1; Km normalized_value=0.015 normalized_unit=mM; kcat/Km normalized_value=630 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=9.5 +/- 0.4 raw_unit=s^-1; Km raw_value=(1.5 +/- 0.1) x 10^1 raw_unit=uM; kcat/Km raw_value=6.3 x 10^5 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.

data_origin: experimental

enzyme: 4-hydroxybenzoyl-CoA thioesterase

status: corrected

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed: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; row S120A; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells kcat=(1.01 +/- 0.02) x 10, Km=1.6 +/- 0.1 uM, kcat/Km=6.3 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=10.1 normalized_unit=s^-1; Km normalized_value=0.0016 normalized_unit=mM; kcat/Km normalized_value=6300 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=(1.01 +/- 0.02) x 10 raw_unit=s^-1; Km raw_value=1.6 +/- 0.1 raw_unit=uM; kcat/Km raw_value=6.3 x 10^6 raw_unit=M^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed: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; row T121A; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells kcat=9.7 +/- 0.3, Km=6.1 +/- 0.4 uM, kcat/Km=1.6 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=9.7 normalized_unit=s^-1; Km normalized_value=0.0061 normalized_unit=mM; kcat/Km normalized_value=1600 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=9.7 +/- 0.3 raw_unit=s^-1; Km raw_value=6.1 +/- 0.4 raw_unit=uM; kcat/Km raw_value=1.6 x 10^6 raw_unit=M^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed: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; row T77A; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells kcat=2.09 +/- 0.03, Km=1.22 +/- 0.05 uM, kcat/Km=1.7 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=2.09 normalized_unit=s^-1; Km normalized_value=0.00122 normalized_unit=mM; kcat/Km normalized_value=1700 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=2.09 +/- 0.03 raw_unit=s^-1; Km raw_value=1.22 +/- 0.05 raw_unit=uM; kcat/Km raw_value=1.7 x 10^6 raw_unit=M^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed: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; row T77D; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells kcat=(1.03 +/- 0.02) x 10^-2, Km=(3.8 +/- 0.3) x 10^-1 uM, kcat/Km=2.7 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.0103 normalized_unit=s^-1; Km normalized_value=0.00038 normalized_unit=mM; kcat/Km normalized_value=27 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=(1.03 +/- 0.02) x 10^-2 raw_unit=s^-1; Km raw_value=(3.8 +/- 0.3) x 10^-1 raw_unit=uM; kcat/Km raw_value=2.7 x 10^4 raw_unit=M^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed: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; row T77S; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells kcat=3.16 +/- 0.04, Km=(7.7 +/- 0.3) x 10^-1 uM, kcat/Km=4.1 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=3.16 normalized_unit=s^-1; Km normalized_value=0.00077 normalized_unit=mM; kcat/Km normalized_value=4100 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=3.16 +/- 0.04 raw_unit=s^-1; Km raw_value=(7.7 +/- 0.3) x 10^-1 raw_unit=uM; kcat/Km raw_value=4.1 x 10^6 raw_unit=M^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed: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; row T77V; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells kcat=(1.73 +/- 0.05) x 10^-1, Km=5.5 +/- 0.4 uM, kcat/Km=3.1 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.173 normalized_unit=s^-1; Km normalized_value=0.0055 normalized_unit=mM; kcat/Km normalized_value=31 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=(1.73 +/- 0.05) x 10^-1 raw_unit=s^-1; Km raw_value=5.5 +/- 0.4 raw_unit=uM; kcat/Km raw_value=3.1 x 10^4 raw_unit=M^-1 s^-1


enzyme_display_name: acyl-CoA hydrolase

organism: Homo sapiens

substrate_name: Phenylacetyl-CoA

verification_status: verified

mutation_signature: Unknown

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

column_label: PMCID PMC2929599 Table 2; Phenylacetyl-CoA; kcat (s^-1) = (8.4 +/- 0.6) x 10^-2; PMCID PMC2929599 Table 2; Phenylacetyl-CoA; kcat/Km (M^-1 s^-1) = 3.5 x 10^2; PMCID PMC2929599 Table 2; Phenylacetyl-CoA; Km (uM) = (2.4 +/- 0.3) x 10^2

normalized_value_unit_evidence: normalized kcat=0.084 s^-1; export kcat=0.084 s^-1; normalized kcat_over_km=0.35 s^-1 mM^-1; export kcat_over_km=0.35000000000000003 s^-1 mM^-1; normalized km=0.24 mM; export km=0.24 mM

raw_value_unit_evidence: kcat (s^-1) (8.4 +/- 0.6) x 10^-2 s^-1 for Phenylacetyl-CoA; kcat/Km (M^-1 s^-1) 3.5 x 10^2 M^-1 s^-1 for Phenylacetyl-CoA; Km (uM) (2.4 +/- 0.3) x 10^2 uM for Phenylacetyl-CoA

row_label: Phenylacetyl-CoA

table_label: PMCID PMC2929599 Table 2

enzyme: acyl-CoA hydrolase

substrate: Phenylacetyl-CoA

status: verified


substrate_name: Propanoyl-CoA

column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Propionyl-CoA, column kcat s^-1, raw cell (3.6 +/- 0.3) x 10-2, normalized 0.036 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Propionyl-CoA, column kcat/Km M^-1 s^-1, raw cell 1.9 x 102, normalized 0.19 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Propionyl-CoA, column Km uM, raw cell (1.9 +/- 0.4) x 102, normalized 0.19 mM

normalized_value_unit_evidence: kcat normalized_value=0.036 normalized_unit=s^-1; kcat/Km normalized_value=0.19 normalized_unit=s^-1*mM^-1; Km normalized_value=0.19 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.036 raw_unit=s^-1 raw_cell=(3.6 +/- 0.3) x 10-2; kcat/Km raw_value=190 raw_unit=M^-1*s^-1 raw_cell=1.9 x 102; Km raw_value=190 raw_unit=uM raw_cell=(1.9 +/- 0.4) x 102

row_label: n-Propionyl-CoA

substrate: Propanoyl-CoA


substrate_name: myristoyl-CoA

kcat_over_km_origin: calculated

column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Myristoyl-CoA (25 C), column kcat s^-1, raw cell (2.0+/- 0.1) x 10-2, normalized 0.02 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Myristoyl-CoA (25 C), column kcat/Km M^-1 s^-1, raw cell 4.0 x 103, normalized 4 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Myristoyl-CoA (25 C), column Km uM, raw cell 5 +/- 1, normalized 0.005 mM

normalized_value_unit_evidence: kcat normalized_value=0.02 normalized_unit=s^-1; kcat/Km normalized_value=4 normalized_unit=s^-1*mM^-1; Km normalized_value=0.005 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.02 raw_unit=s^-1 raw_cell=(2.0+/- 0.1) x 10-2; kcat/Km raw_value=4000 raw_unit=M^-1*s^-1 raw_cell=4.0 x 103; Km raw_value=5 raw_unit=uM raw_cell=5 +/- 1

row_label: Myristoyl-CoA (25 C)

substrate: myristoyl-CoA


column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Myristoyl-CoA (37 C), column kcat s^-1, raw cell (7.0 +/- 0.1) x 10-2, normalized 0.07 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Myristoyl-CoA (37 C), column kcat/Km M^-1 s^-1, raw cell 7.7 x 103, normalized 7.7 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row Myristoyl-CoA (37 C), column Km uM, raw cell 9 +/- 2, normalized 0.009 mM

normalized_value_unit_evidence: kcat normalized_value=0.07 normalized_unit=s^-1; kcat/Km normalized_value=7.7 normalized_unit=s^-1*mM^-1; Km normalized_value=0.009 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.07 raw_unit=s^-1 raw_cell=(7.0 +/- 0.1) x 10-2; kcat/Km raw_value=7700 raw_unit=M^-1*s^-1 raw_cell=7.7 x 103; Km raw_value=9 raw_unit=uM raw_cell=9 +/- 2

row_label: Myristoyl-CoA (37 C)


substrate_name: glutaryl-CoA

verification_status: unverified

substrate: glutaryl-CoA

status: unverified


substrate_name: stearoyl-CoA

column_label: PMCID PMC2929599 Table 2; Stearoyl-CoA; kcat (s^-1) = (1.1 +/- 0.1) x 10^-2; PMCID PMC2929599 Table 2; Stearoyl-CoA; kcat/Km (M^-1 s^-1) = 5.5 x 10^2; PMCID PMC2929599 Table 2; Stearoyl-CoA; Km (uM) = (2.0 +/- 0.4) x 10^1

normalized_value_unit_evidence: normalized kcat=0.011 s^-1; export kcat=0.011 s^-1; normalized kcat_over_km=0.55 s^-1 mM^-1; export kcat_over_km=0.5499999999999999 s^-1 mM^-1; normalized km=0.02 mM; export km=0.02 mM

row_label: Stearoyl-CoA

substrate: stearoyl-CoA


substrate_name: decanoyl-CoA

column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Decanoyl-CoA, column kcat s^-1, raw cell (1.6+/- 0.1) x 10-2, normalized 0.016 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Decanoyl-CoA, column kcat/Km M^-1 s^-1, raw cell 3.3 x 103, normalized 3.3 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Decanoyl-CoA, column Km uM, raw cell 4.9 +/- 0.6, normalized 0.0049 mM

normalized_value_unit_evidence: kcat normalized_value=0.016 normalized_unit=s^-1; kcat/Km normalized_value=3.3 normalized_unit=s^-1*mM^-1; Km normalized_value=0.0049 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.016 raw_unit=s^-1 raw_cell=(1.6+/- 0.1) x 10-2; kcat/Km raw_value=3300 raw_unit=M^-1*s^-1 raw_cell=3.3 x 103; Km raw_value=4.9 raw_unit=uM raw_cell=4.9 +/- 0.6

row_label: n-Decanoyl-CoA

substrate: decanoyl-CoA


substrate_name: butanoyl-CoA

column_label: Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Butyryl-CoA, column kcat s^-1, raw cell (4.7+/- 0.5) x 10-2, normalized 0.047 s^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Butyryl-CoA, column kcat/Km M^-1 s^-1, raw cell 7.8 x 101, normalized 0.078 s^-1*mM^-1; Table 2. Steady-state constants for hTHEM2 wild-type catalyzed hydrolysis of acyl-CoA thioesters row n-Butyryl-CoA, column Km uM, raw cell (6.0 +/- 0.1) x 102, normalized 0.6 mM

normalized_value_unit_evidence: kcat normalized_value=0.047 normalized_unit=s^-1; kcat/Km normalized_value=0.078 normalized_unit=s^-1*mM^-1; Km normalized_value=0.6 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.047 raw_unit=s^-1 raw_cell=(4.7+/- 0.5) x 10-2; kcat/Km raw_value=78 raw_unit=M^-1*s^-1 raw_cell=7.8 x 101; Km raw_value=600 raw_unit=uM raw_cell=(6.0 +/- 0.1) x 102

row_label: n-Butyryl-CoA

substrate: butanoyl-CoA


column_label: Table 4. Steady-State Kinetic Constants Determined for Wild-Type and Mutant Thioesterase Catalyzed Hydrolysis of 4-HB-CoA; row wild-type; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells kcat=6.7 +/- 0.1, Km=1.24 +/- 0.06 uM, kcat/Km=5.4 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=6.7 normalized_unit=s^-1; Km normalized_value=0.00124 normalized_unit=mM; kcat/Km normalized_value=5400 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=6.7 +/- 0.1 raw_unit=s^-1; Km raw_value=1.24 +/- 0.06 raw_unit=uM; kcat/Km raw_value=5.4 x 10^6 raw_unit=M^-1 s^-1

row_label: wild-type


enzyme_display_name: UniProt Q04416

source_db: skid

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

sequence_source: multiple

source_databases_merged: skid uniprot

enzyme: UniProt Q04416

source: skid


column_label: Official PMC Table 1 row 2,5-diHBA-CoA under thioesterase-catalyzed hydrolysis of acyl-CoA thioesters at pH 7.5 and 25 C: 2,5-diHBA-CoA | kcat (8.0 +/- 0.1) x 10^-2 s^-1 | Km (2.9 +/- 0.3) x 10^1 uM | kcat/Km 2.7 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=0.08 normalized_unit=s^-1; Km normalized_value=0.029 normalized_unit=mM; kcat/Km normalized_value=2.758620689655172 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 2,5-diHBA-CoA cells: kcat raw_value=(8.0 +/- 0.1) x 10^-2 raw_unit=s^-1; Km raw_value=(2.9 +/- 0.3) x 10^1 raw_unit=uM; kcat/Km raw_value=2.7 x 10^3 raw_unit=M^-1 s^-1.

table_label: Table 1. Steady-state kinetic constants for Arthrobacter sp. strain SU thioesterase-catalyzed hydrolysis of acyl-CoA thioesters at pH 7.5 and 25 C determined by using the DTNB spectrophotometric assay


column_label: Official PMC Table 1 row 3-HBA-CoA under thioesterase-catalyzed hydrolysis of acyl-CoA thioesters at pH 7.5 and 25 C: 3-HBA-CoA | kcat 15.8 +/- 0.2 s^-1 | Km (2.2 +/- 0.1) x 10^1 uM | kcat/Km 7.2 x 10^5 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=15.8 normalized_unit=s^-1; Km normalized_value=0.022 normalized_unit=mM; kcat/Km normalized_value=718.1818181818182 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 3-HBA-CoA cells: kcat raw_value=15.8 +/- 0.2 raw_unit=s^-1; Km raw_value=(2.2 +/- 0.1) x 10^1 raw_unit=uM; kcat/Km raw_value=7.2 x 10^5 raw_unit=M^-1 s^-1.


column_label: Official PMC Table 1 row 4-CBA-CoA under thioesterase-catalyzed hydrolysis of acyl-CoA thioesters at pH 7.5 and 25 C: 4-CBA-CoA | kcat (2.5 +/- 0.1) x 10^-1 s^-1 | Km (1.13 +/- 0.08) x 10^2 uM | kcat/Km 2.2 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=0.25 normalized_unit=s^-1; Km normalized_value=0.113 normalized_unit=mM; kcat/Km normalized_value=2.2123893805309733 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 4-CBA-CoA cells: kcat raw_value=(2.5 +/- 0.1) x 10^-1 raw_unit=s^-1; Km raw_value=(1.13 +/- 0.08) x 10^2 raw_unit=uM; kcat/Km raw_value=2.2 x 10^3 raw_unit=M^-1 s^-1.


substrate_name: Acetyl-CoA

column_label: Official PMC Table 1 row Acetyl-CoA under thioesterase-catalyzed hydrolysis of acyl-CoA thioesters at pH 7.5 and 25 C: Acetyl-CoA | kcat (1.08 +/- 0.02) x 10^-2 s^-1 | Km (2.2 +/- 0.1) x 10^3 uM | kcat/Km 5.0 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=0.0108 normalized_unit=s^-1; Km normalized_value=2.2 normalized_unit=mM; kcat/Km normalized_value=0.004999999999999999 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Acetyl-CoA cells: kcat raw_value=(1.08 +/- 0.02) x 10^-2 raw_unit=s^-1; Km raw_value=(2.2 +/- 0.1) x 10^3 raw_unit=uM; kcat/Km raw_value=5.0 raw_unit=M^-1 s^-1.

row_label: Acetyl-CoA

substrate: Acetyl-CoA


substrate_name: Benzoyl-CoA

column_label: Official PMC Table 1 row BA-CoA under thioesterase-catalyzed hydrolysis of acyl-CoA thioesters at pH 7.5 and 25 C: BA-CoA | kcat 1.86 +/- 0.06 s^-1 | Km (2.43 +/- 0.16) x 10^2 uM | kcat/Km 7.6 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=1.86 normalized_unit=s^-1; Km normalized_value=0.243 normalized_unit=mM; kcat/Km normalized_value=7.654320987654321 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 BA-CoA cells: kcat raw_value=1.86 +/- 0.06 raw_unit=s^-1; Km raw_value=(2.43 +/- 0.16) x 10^2 raw_unit=uM; kcat/Km raw_value=7.6 x 10^3 raw_unit=M^-1 s^-1.

row_label: BA-CoA

substrate: Benzoyl-CoA


column_label: Official PMC Table 1 row Phenylacetyl-CoA under thioesterase-catalyzed hydrolysis of acyl-CoA thioesters at pH 7.5 and 25 C: Phenylacetyl-CoA | kcat (9.0 +/- 0.2) x 10^-4 s^-1 | Km (1.4 +/- 0.1) x 10^2 uM | kcat/Km 6.5 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=0.0009 normalized_unit=s^-1; Km normalized_value=0.14 normalized_unit=mM; kcat/Km normalized_value=0.006428571428571428 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Phenylacetyl-CoA cells: kcat raw_value=(9.0 +/- 0.2) x 10^-4 raw_unit=s^-1; Km raw_value=(1.4 +/- 0.1) x 10^2 raw_unit=uM; kcat/Km raw_value=6.5 raw_unit=M^-1 s^-1.


column_label: Official PMC Table 1 row Propionyl-CoA under thioesterase-catalyzed hydrolysis of acyl-CoA thioesters at pH 7.5 and 25 C: Propionyl-CoA | kcat (2.6 +/- 0.1) x 10^-2 s^-1 | Km (1.1 +/- 0.09) x 10^3 uM | kcat/Km 2.4 x 10^1 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=0.026 normalized_unit=s^-1; Km normalized_value=1.1 normalized_unit=mM; kcat/Km normalized_value=0.023636363636363632 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Propionyl-CoA cells: kcat raw_value=(2.6 +/- 0.1) x 10^-2 raw_unit=s^-1; Km raw_value=(1.1 +/- 0.09) x 10^3 raw_unit=uM; kcat/Km raw_value=2.4 x 10^1 raw_unit=M^-1 s^-1.

row_label: Propionyl-CoA


column_label: Official PMC Table 1 row Butyryl-CoA under thioesterase-catalyzed hydrolysis of acyl-CoA thioesters at pH 7.5 and 25 C: Butyryl-CoA | kcat (3.19 +/- 0.05) x 10^-2 s^-1 | Km (9.3 +/- 0.5) x 10^2 uM | kcat/Km 3.4 x 10^1 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=0.0319 normalized_unit=s^-1; Km normalized_value=0.93 normalized_unit=mM; kcat/Km normalized_value=0.034408602150537634 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Butyryl-CoA cells: kcat raw_value=(3.19 +/- 0.05) x 10^-2 raw_unit=s^-1; Km raw_value=(9.3 +/- 0.5) x 10^2 raw_unit=uM; kcat/Km raw_value=3.4 x 10^1 raw_unit=M^-1 s^-1.

row_label: Butyryl-CoA


substrate_name: crotonoyl-CoA

column_label: Official PMC Table 1 row Crotonyl-CoA under thioesterase-catalyzed hydrolysis of acyl-CoA thioesters at pH 7.5 and 25 C: Crotonyl-CoA | kcat (7.5 +/- 0.1) x 10^-2 s^-1 | Km (8.1 +/- 0.3) x 10^2 uM | kcat/Km 9.2 x 10^1 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=0.075 normalized_unit=s^-1; Km normalized_value=0.81 normalized_unit=mM; kcat/Km normalized_value=0.09259259259259259 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Crotonyl-CoA cells: kcat raw_value=(7.5 +/- 0.1) x 10^-2 raw_unit=s^-1; Km raw_value=(8.1 +/- 0.3) x 10^2 raw_unit=uM; kcat/Km raw_value=9.2 x 10^1 raw_unit=M^-1 s^-1.

row_label: Crotonyl-CoA

substrate: crotonoyl-CoA


organism: Bacillus halodurans

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9KBC9 and applied mutation signature D16N to reconstruct the assayed variant sequence.

column_label: Table 1. Steady-state kinetic constants for B. halodurans gentisyl-CoA thioesterase- and Pseudomonas 4-hydroxybenzoyl-CoA thioesterase-catalyzed hydrolysis of acyl-CoAs; enzyme/type row D16N; substrate row D16N / Gentisyl-CoA; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells (2.8 +/- 0.3) x 10^-2 s^-1; 9 +/- 2 uM; 3.1 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.028 normalized_unit=s^-1; Km normalized_value=0.009 normalized_unit=mM; kcat/Km normalized_value=3.1111111111111116 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=3.1 s^-1*mM^-1

row_label: D16N / D16N / Gentisyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9KBC9 and applied mutation signature D31N to reconstruct the assayed variant sequence.

column_label: Table 1. Steady-state kinetic constants for B. halodurans gentisyl-CoA thioesterase- and Pseudomonas 4-hydroxybenzoyl-CoA thioesterase-catalyzed hydrolysis of acyl-CoAs; enzyme/type row D31N; substrate row D31N / Gentisyl-CoA; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells (6.9 +/- 0.2) x 10^-1 s^-1; (1.6 +/- 0.1) x 10^1 uM; 4.3 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.69 normalized_unit=s^-1; Km normalized_value=0.016 normalized_unit=mM; kcat/Km normalized_value=43.12499999999999 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=43.0 s^-1*mM^-1

row_label: D31N / D31N / Gentisyl-CoA


column_label: Table 1. Steady-state kinetic constants for B. halodurans gentisyl-CoA thioesterase- and Pseudomonas 4-hydroxybenzoyl-CoA thioesterase-catalyzed hydrolysis of acyl-CoAs; enzyme/type row Wild type; substrate row Gentisyl-CoA; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 6.5 +/- 0.2 s^-1; 4.0 +/- 0.6 uM; 1.6 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=6.5 normalized_unit=s^-1; Km normalized_value=0.004 normalized_unit=mM; kcat/Km normalized_value=1625.0 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=1600.0 s^-1*mM^-1

row_label: Wild type / Gentisyl-CoA


column_label: Table 1. Steady-state kinetic constants for B. halodurans gentisyl-CoA thioesterase- and Pseudomonas 4-hydroxybenzoyl-CoA thioesterase-catalyzed hydrolysis of acyl-CoAs; enzyme/type row Wild type; substrate row 3-Hydroxybenzoyl-CoA; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 1.5 +/- 0.1 s^-1; 5.0 +/- 0.4 uM; 3.0 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=1.5 normalized_unit=s^-1; Km normalized_value=0.005 normalized_unit=mM; kcat/Km normalized_value=300.0 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=300.0 s^-1*mM^-1

row_label: Wild type / 3-Hydroxybenzoyl-CoA


column_label: Table 1. Steady-state kinetic constants for B. halodurans gentisyl-CoA thioesterase- and Pseudomonas 4-hydroxybenzoyl-CoA thioesterase-catalyzed hydrolysis of acyl-CoAs; enzyme/type row Wild type; substrate row 3-Hydroxyphenylacetyl-CoA; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells (8.1 +/- 0.3) x 10^-3 s^-1; (1.9 +/- 0.2) x 10^2 uM; 4.3 x 10^1 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.008 normalized_unit=s^-1; Km normalized_value=0.19 normalized_unit=mM; kcat/Km normalized_value=0.042105263157894736 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=0.043 s^-1*mM^-1

row_label: Wild type / 3-Hydroxyphenylacetyl-CoA


column_label: Table 1. Steady-state kinetic constants for B. halodurans gentisyl-CoA thioesterase- and Pseudomonas 4-hydroxybenzoyl-CoA thioesterase-catalyzed hydrolysis of acyl-CoAs; enzyme/type row Wild type; substrate row 4-Chlorobenzoyl-CoA; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells 7.3 +/- 0.4 s^-1; (2.4 +/- 0.3) x 10^2 uM; 3.0 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=7.3 normalized_unit=s^-1; Km normalized_value=0.24 normalized_unit=mM; kcat/Km normalized_value=30.416666666666668 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=30.0 s^-1*mM^-1

row_label: Wild type / 4-Chlorobenzoyl-CoA


column_label: Table 1. Steady-state kinetic constants for B. halodurans gentisyl-CoA thioesterase- and Pseudomonas 4-hydroxybenzoyl-CoA thioesterase-catalyzed hydrolysis of acyl-CoAs; enzyme/type row Wild type; substrate row 4-Hydroxybenzoyl-CoA; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells (4.2 +/- 0.2) x 10^-2 s^-1; (1.2 +/- 0.2) x 10^2 uM; 3.6 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.042 normalized_unit=s^-1; Km normalized_value=0.12 normalized_unit=mM; kcat/Km normalized_value=0.35000000000000003 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=0.36 s^-1*mM^-1

row_label: Wild type / 4-Hydroxybenzoyl-CoA


column_label: Table 1. Steady-state kinetic constants for B. halodurans gentisyl-CoA thioesterase- and Pseudomonas 4-hydroxybenzoyl-CoA thioesterase-catalyzed hydrolysis of acyl-CoAs; enzyme/type row Wild type; substrate row 4-Methoxybenzoyl-CoA; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells (3.4 +/- 0.3) x 10^-1 s^-1; (1.0 +/- 0.2) x 10^2 uM; 3.4 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.34 normalized_unit=s^-1; Km normalized_value=0.1 normalized_unit=mM; kcat/Km normalized_value=3.4 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=3.4 s^-1*mM^-1

row_label: Wild type / 4-Methoxybenzoyl-CoA


column_label: Table 1. Steady-state kinetic constants for B. halodurans gentisyl-CoA thioesterase- and Pseudomonas 4-hydroxybenzoyl-CoA thioesterase-catalyzed hydrolysis of acyl-CoAs; enzyme/type row Wild type; substrate row Benzoyl-CoA; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells (6.8 +/- 0.3) x 10^-2 s^-1; (3.3 +/- 0.4) x 10^2 uM; 2.1 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.068 normalized_unit=s^-1; Km normalized_value=0.33 normalized_unit=mM; kcat/Km normalized_value=0.20606060606060606 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=0.21 s^-1*mM^-1

row_label: Wild type / Benzoyl-CoA


substrate_name: Hexanoyl-CoA

column_label: Table 1. Steady-state kinetic constants for B. halodurans gentisyl-CoA thioesterase- and Pseudomonas 4-hydroxybenzoyl-CoA thioesterase-catalyzed hydrolysis of acyl-CoAs; enzyme/type row Wild type; substrate row n-Hexanoyl-CoA; columns kcat (s^-1), Km (uM), kcat/Km (M^-1 s^-1); cells (1.3 +/- 0.1) x 10^-1 s^-1; (4.6 +/- 0.5) x 10^2 uM; 2.8 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.13 normalized_unit=s^-1; Km normalized_value=0.46 normalized_unit=mM; kcat/Km normalized_value=0.2826086956521739 normalized_unit=s^-1*mM^-1; printed_efficiency_normalized=0.28 s^-1*mM^-1

row_label: Wild type / n-Hexanoyl-CoA

substrate: Hexanoyl-CoA


column_label: Table label: TABLE 1. Steady-state kinetic constants for B. halodurans gentisyl-CoA thioesterase- and Pseudomonas 4-hydroxybenzoyl-CoA thioesterase-catalyzed hydrolysis of acyl-CoAs. Section: Gentisyl-CoA thioesterase. Row: Wild type | Phenylacetyl-CoA. Columns read: k cat (s^-1) cell (3.4 +/- 0.2) x 10^-2, K m (uM) cell (3.5 +/- 0.5) x 10^2, k cat / K m (M^-1 s^-1) cell 9.7 x 10^1. metric: kcat; raw value: (3.4 +/- 0.2) x 10^-2; raw unit: s^-1; normalized value: 0.034 s^(-1); metric: Km; raw value: (3.5 +/- 0.5) x 10^2; raw unit: uM; normalized value: 0.35 mM; metric: kcat/Km; raw value: 0.034 / 0.35; raw unit: s^-1 mM^-1; normalized value: 0.09714285714285716 s^-1 mM^-1; assay condition: Purified recombinant enzyme; steady-state kinetic constants measured at 25 C with a DTNB-based assay following 5-thio-2-nitrobenzoate absorbance at 412 nm in 0.2-ml reactions containing DTNB (1 mM), KCl (0.2 M) and 50 mM K + HEPES (pH 7.5, 25 C); initial-velocity data were fit to V = Vmax[S]/([S] + Km) and kcat was calculated from Vmax/[E]. Export row conditions: pH 7.5.

normalized_value_unit_evidence: Table 1 row Gentisyl-CoA thioesterase | Wild type | Phenylacetyl-CoA: kcat (3.4 +/- 0.2) x 10^-2 s^-1 = 0.034 s^(-1); Km (3.5 +/- 0.5) x 10^2 uM = 350 uM = 0.35 mM (1 uM = 0.001 mM); kcat/Km 0.09714285714285716 s^-1 mM^-1. The printed Table 1 kcat/Km cell for this row is 9.7 x 10^1 M^-1 s^-1, which normalizes to 0.097 s^-1 mM^-1. The export stores the full-precision quotient of this same row's printed kcat and Km cells, 0.034 s^-1 / 0.35 mM = 0.09714285714285716 s^-1 mM^-1, and that quotient rounds to 0.097 at the printed cell's own two-significant-figure precision, so the printed cell and the exported value agree and the difference is printed precision only. In the cached HTML the multiplication sign renders as the Unicode multiplication sign, the superscript minus one as the Unicode minus sign, the micro sign as the Greek letter mu, the plus-minus sign as the Unicode plus-minus sign, and superscript exponents are flattened onto the line, so the printed cell `9.7 × 10 1` is the paper's 9.7 x 10^1 M^-1 s^-1.

raw_value_unit_evidence: TABLE 1. Steady-state kinetic constants for B. halodurans gentisyl-CoA thioesterase- and Pseudomonas 4-hydroxybenzoyl-CoA thioesterase-catalyzed hydrolysis of acyl-CoAs | header row: Enzyme and type Substrate k cat (s −1 ) K m (μM) k cat / K m (M −1 s −1 ) | section row: Gentisyl-CoA thioesterase | data row: Wild type Phenylacetyl-CoA (3.4 ± 0.2) × 10 −2 (3.5 ± 0.5) × 10 2 9.7 × 10 1 | cells read: k cat = (3.4 +/- 0.2) x 10^-2 s^-1; K m = (3.5 +/- 0.5) x 10^2 uM; k cat / K m = 9.7 x 10^1 M^-1 s^-1


column_label: Table label: TABLE 1. Steady-state kinetic constants for B. halodurans gentisyl-CoA thioesterase- and Pseudomonas 4-hydroxybenzoyl-CoA thioesterase-catalyzed hydrolysis of acyl-CoAs. Section: Gentisyl-CoA thioesterase. Row: Wild type | n -Propionyl-CoA. Columns read: k cat (s^-1) cell (5.8 +/- 0.5) x 10^-2, K m (uM) cell (1.2 +/- 0.2) x 10^3, k cat / K m (M^-1 s^-1) cell 4.8 x 10^1. metric: kcat; raw value: (5.8 +/- 0.5) x 10^-2; raw unit: s^-1; normalized value: 0.058 s^(-1); metric: Km; raw value: (1.2 +/- 0.2) x 10^3; raw unit: uM; normalized value: 1.2 mM; metric: kcat/Km; raw value: 0.058 / 1.2; raw unit: s^-1 mM^-1; normalized value: 0.04833333333333334 s^-1 mM^-1; assay condition: Purified recombinant enzyme; steady-state kinetic constants measured at 25 C with a DTNB-based assay following 5-thio-2-nitrobenzoate absorbance at 412 nm in 0.2-ml reactions containing DTNB (1 mM), KCl (0.2 M) and 50 mM K + HEPES (pH 7.5, 25 C); initial-velocity data were fit to V = Vmax[S]/([S] + Km) and kcat was calculated from Vmax/[E]. Export row conditions: pH 7.5.

normalized_value_unit_evidence: Table 1 row Gentisyl-CoA thioesterase | Wild type | n -Propionyl-CoA: kcat (5.8 +/- 0.5) x 10^-2 s^-1 = 0.058 s^(-1); Km (1.2 +/- 0.2) x 10^3 uM = 1200 uM = 1.2 mM (1 uM = 0.001 mM); kcat/Km 0.04833333333333334 s^-1 mM^-1. The printed Table 1 kcat/Km cell for this row is 4.8 x 10^1 M^-1 s^-1, which normalizes to 0.048 s^-1 mM^-1. The export stores the full-precision quotient of this same row's printed kcat and Km cells, 0.058 s^-1 / 1.2 mM = 0.04833333333333334 s^-1 mM^-1, and that quotient rounds to 0.048 at the printed cell's own two-significant-figure precision, so the printed cell and the exported value agree and the difference is printed precision only. In the cached HTML the multiplication sign renders as the Unicode multiplication sign, the superscript minus one as the Unicode minus sign, the micro sign as the Greek letter mu, the plus-minus sign as the Unicode plus-minus sign, and superscript exponents are flattened onto the line, so the printed cell `4.8 × 10 1` is the paper's 4.8 x 10^1 M^-1 s^-1.

raw_value_unit_evidence: TABLE 1. Steady-state kinetic constants for B. halodurans gentisyl-CoA thioesterase- and Pseudomonas 4-hydroxybenzoyl-CoA thioesterase-catalyzed hydrolysis of acyl-CoAs | header row: Enzyme and type Substrate k cat (s −1 ) K m (μM) k cat / K m (M −1 s −1 ) | section row: Gentisyl-CoA thioesterase | data row: Wild type n -Propionyl-CoA (5.8 ± 0.5) × 10 −2 (1.2 ± 0.2) × 10 3 4.8 × 10 1 | cells read: k cat = (5.8 +/- 0.5) x 10^-2 s^-1; K m = (1.2 +/- 0.2) x 10^3 uM; k cat / K m = 4.8 x 10^1 M^-1 s^-1


organism: Arthrobacter sp

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

assay_conditions_summary: cofactor CoA

source: uniprot


substrate_name: phenylacetyl-CoA

substrate: phenylacetyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: propionyl-CoA

substrate: propionyl-CoA


substrate_name: butyryl-CoA

substrate: butyryl-CoA


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


organism: Pseudomonas sp.

source_db: brenda

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

source_databases_merged: brenda skid uniprot

source: brenda


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D32S with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


enzyme_display_name: Palmitoyl-protein thioesterase 1

organism: Bos taurus

substrate_name: palmitoyl-CoA

proof_lines:
palmitoyl-protein thioesterase
bovine brain
cDNA clones

enzyme: Palmitoyl-protein thioesterase 1

substrate: palmitoyl-CoA


substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 8; cofactor CoA

column_label: Table 2 row C18:1, column Km = 5.9 uM.

raw_value_unit_evidence: Km 5.9 uM.

row_label: C18:1 / oleoyl-CoA

table_label: Table 2


substrate_name: octanoyl-CoA

source_databases_merged: brenda uniprot

substrate: octanoyl-CoA


column_label: Table 2 row 8-Methyl-C9:0, column Km = 19.0 uM.

row_label: 8-Methyl-C9:0 / 8-methyl-nonanoyl-CoA


substrate_name: nonanoyl-CoA

column_label: Table 2 row C9:0, column Km = 21.8 uM.

row_label: C9:0 / nonanoyl-CoA

substrate: nonanoyl-CoA


column_label: Table 2 row C10:0, column Km = 27.1 uM.

row_label: C10:0 / decanoyl-CoA


organism: Pseudomonas reinekei

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D17N to reconstruct the assayed variant sequence.


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


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


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


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R89L to reconstruct the assayed variant sequence.


substrate_name: Arachidonoyl-CoA

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

column_label: Europe PMC public PDF Figure 2F row hThem5 WT C20:4, columns Km=19 uM, kcat=1.4 s^-1, kcat/Km=7.3 x 10^4 M^-1 s^-1.

raw_value_unit_evidence: Figure 2F row hThem5 WT C20:4 cells: Km 19 uM; kcat 1.4 s^-1; kcat/Km 7.3 x 10^4 M^-1 s^-1.

table_label: Figure 2F. Steady-state kinetic constants for hThem5 catalyzed hydrolysis of selected Acyl-CoA esters

substrate: Arachidonoyl-CoA


substrate_name: linolenoyl-CoA

column_label: Table label: Figure 2F. Steady-state kinetic constants for hThem5 catalyzed hydrolysis of selected Acyl-CoA esters. Row: hThem5 WT | C18:3. Columns read: Km (uM) cell 15.4, kcat (s^-1) cell 13.3, kcat/Km (M^-1 s^-1) cell 8.6x10^5. Km 15.4 uM normalizes to 0.0154 mM and decimal-matches the exported km; kcat 13.3 s^-1 decimal-matches the exported kcat; the exported kcat_over_km 863.6363636363636 s^-1 mM^-1 is the quotient of this same row's printed kcat and Km cells and back-converts to the row's printed kcat/Km cell at that cell's printed precision. No value here is taken from another row, another column, another enzyme block, or another paper.

normalized_value_unit_evidence: Figure 2F row hThem5 WT | C18:3: Km 15.4 uM = 0.0154 mM; kcat 13.3 s^-1 = 13.3 s^-1. The exported kcat_over_km is carried as the quotient of this row's own two printed cells, 13.3 s^-1 divided by 0.0154 mM = 863.6363636363636 s^-1 mM^-1. Conversion arithmetic, stated separately from the stored value: 15.4 / 1000 = 0.0154; 13.3 / 0.0154 = 863.6363636363636. The panel also prints a rounded kcat/Km cell of 8.6x10^5 M^-1 s^-1 for this row; the quotient back-converts to 8.636363636363636x10^5 M^-1 s^-1, which at that cell's two-significant-figure printed precision is 8.6x10^5 M^-1 s^-1, so the printed cell and the quotient agree and neither contradicts the other.

raw_value_unit_evidence: Figure 2F. Steady-state kinetic constants for hThem5 catalyzed hydrolysis of selected Acyl-CoA esters | column headers: Enzyme | Substrate | Km (uM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) | row: hThem5 WT | C18:3 | 15.4 | 13.3 | 8.6x10^5

row_label: hThem5 WT | C18:3

substrate: linolenoyl-CoA


substrate_name: linoleoyl-CoA

column_label: Europe PMC public PDF Figure 2F row hThem5 WT C18:2, columns Km=4.2 uM, kcat=12.2 s^-1, kcat/Km=2.9 x 10^6 M^-1 s^-1.

raw_value_unit_evidence: Figure 2F row hThem5 WT C18:2 cells: Km 4.2 uM; kcat 12.2 s^-1; kcat/Km 2.9 x 10^6 M^-1 s^-1.

substrate: linoleoyl-CoA


substrate_name: myristoyl-CoA

column_label: Europe PMC public PDF Figure 2F row hThem5 WT C14:0, columns Km=8.6 uM, kcat=19.7 s^-1, kcat/Km=2.3 x 10^6 M^-1 s^-1.

raw_value_unit_evidence: Figure 2F row hThem5 WT C14:0 cells: Km 8.6 uM; kcat 19.7 s^-1; kcat/Km 2.3 x 10^6 M^-1 s^-1.

substrate: myristoyl-CoA


substrate_name: palmitoleoyl-CoA

column_label: Europe PMC public PDF Figure 2F row hThem5 WT C16:1, columns Km=26.7 uM, kcat=11.5 s^-1, kcat/Km=4.3 x 10^5 M^-1 s^-1.

raw_value_unit_evidence: Figure 2F row hThem5 WT C16:1 cells: Km 26.7 uM; kcat 11.5 s^-1; kcat/Km 4.3 x 10^5 M^-1 s^-1.

substrate: palmitoleoyl-CoA


column_label: Europe PMC public PDF Figure 2F row hThem5 WT C16:0, columns Km=2.4 uM, kcat=16.6 s^-1, kcat/Km=6.9 x 10^6 M^-1 s^-1.

raw_value_unit_evidence: Figure 2F row hThem5 WT C16:0 cells: Km 2.4 uM; kcat 16.6 s^-1; kcat/Km 6.9 x 10^6 M^-1 s^-1.


substrate_name: stearoyl-CoA

column_label: Europe PMC public PDF Figure 2F row hThem5 WT C18:0, columns Km=4.2 uM, kcat=1.2 s^-1, kcat/Km=2.9 x 10^5 M^-1 s^-1.

raw_value_unit_evidence: Figure 2F row hThem5 WT C18:0 cells: Km 4.2 uM; kcat 1.2 s^-1; kcat/Km 2.9 x 10^5 M^-1 s^-1.

substrate: stearoyl-CoA


substrate_name: vaccenoyl-CoA

proof_lines:
generic octadecenoyl-CoA activity
C18:1 substrate specificity

substrate: vaccenoyl-CoA


organism: Alicyclobacillus acidoterrestris

substrate_name: N-butanoyl-L-homoserine lactone

substrate: N-butanoyl-L-homoserine lactone


substrate_name: N-decanoyl-L-homoserine lactone

substrate: N-decanoyl-L-homoserine lactone


substrate_name: N-hexanoyl-L-homoserine lactone

substrate: N-hexanoyl-L-homoserine lactone


enzyme_display_name: cocaine esterase

proof_lines: AChE BChE 6-MAM

enzyme: cocaine esterase


substrate_name: (-)-cocaine

proof_lines: CocH1 cocaine BChE

substrate: (-)-cocaine


substrate_name: heroin

proof_lines: CocH1 heroin BChE

substrate: heroin


organism: Mycolicibacterium smegmatis

substrate_name: eicosanoyl-CoA

assay_conditions_summary: pH 8.5; cofactor CoA

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

raw_value_unit_evidence: Apparent Km (x10^-6 M) = 0.4

row_label: Eicosanoyl; 20:0

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

substrate: eicosanoyl-CoA


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

raw_value_unit_evidence: Apparent Km (x10^-6 M) = 5.0

row_label: Oleoyl; 18:1


substrate_name: tetradecanoyl-CoA

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

raw_value_unit_evidence: Apparent Km (x10^-6 M) = 6.6

row_label: Myristoyl; 14:0

substrate: tetradecanoyl-CoA


km_display: Not reported

proof_lines:
Pseudomonas sp. CBS-3
4-chlorobenzoate degradation pathway
4-hydroxybenzoyl-CoA thioesterase


proof_lines:
4-chlorobenzoate-coenzyme A
4-hydroxybenzoyl-CoA thioesterase
Pseudomonas sp. CBS-3


substrate_name: Benzoyl-CoA

substrate: Benzoyl-CoA


enzyme_display_name: pyrethroid hydrolase

organism: Sphingobium wenxiniae

substrate_name: p-Nitrophenyl acetate

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

column_label: Table 1 row p-Nitrophenyl acetate lists kcat 183 +/- 9 s^-1, Km 124 +/- 5 uM, and kcat/Km 1.47 +/- 0.07 uM^-1 s^-1.

normalized_value_unit_evidence: Km normalized=0.124 mM; kcat normalized=183 s^-1; kcat/Km normalized=1475.8064516129032 s^-1 mM^-1 from same-row quotient

row_label: p-Nitrophenyl acetate

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

enzyme: pyrethroid hydrolase

substrate: p-Nitrophenyl acetate


substrate_name: p-Nitrophenyl butyrate

column_label: Table 1 row p-Nitrophenyl butyrate lists kcat 118 +/- 5 s^-1, Km 176 +/- 8 uM, and kcat/Km 0.67 +/- 0.03 uM^-1 s^-1.

normalized_value_unit_evidence: Km normalized=0.176 mM; kcat normalized=118 s^-1; kcat/Km normalized=670.4545454545455 s^-1 mM^-1 from same-row quotient

row_label: p-Nitrophenyl butyrate

substrate: p-Nitrophenyl butyrate


substrate_name: p-Nitrophenyl caproate

column_label: Table 1 row p-Nitrophenyl caproate lists kcat 49 +/- 2 s^-1, Km 325 +/- 15 uM, and kcat/Km 0.15 +/- 0.01 uM^-1 s^-1.

normalized_value_unit_evidence: Km normalized=0.325 mM; kcat normalized=49 s^-1; kcat/Km normalized=150.76923076923077 s^-1 mM^-1 from same-row quotient

row_label: p-Nitrophenyl caproate

substrate: p-Nitrophenyl caproate


enzyme_display_name: Diacylglycerol lipase-beta

substrate_name: diacylglycerol

assay_conditions_summary: pH 7

column_label: Figure 2b/prose Km value for human DAGL beta form; raw 74.1 +/- 4.9 uM.

normalized_value_unit_evidence: 74.1 +/- 4.9 uM normalizes to 0.0741 mM, matching the export.

raw_value_unit_evidence: Figure/prose reports Km 74.1 +/- 4.9 uM for the human DAGL beta form.

row_label: human DAGL beta form

table_label: Figure 2b/prose: Michaelis-Menten kinetics of human DAGL alpha and beta

enzyme: Diacylglycerol lipase-beta

substrate: diacylglycerol


enzyme_display_name: Diacylglycerol lipase-alpha

column_label: Figure 2b/prose Km value for human DAGL alpha form; raw 154.7 +/- 19.1 uM.

normalized_value_unit_evidence: 154.7 +/- 19.1 uM normalizes to 0.1547 mM, matching the export.

raw_value_unit_evidence: Figure/prose reports Km 154.7 +/- 19.1 uM for the human DAGL alpha form.

row_label: human DAGL alpha form

enzyme: Diacylglycerol lipase-alpha


enzyme_display_name: Lipase A

organism: Sodiomyces alcalophilus

substrate_name: p-nitrophenol acetate

enzyme: Lipase A

substrate: p-nitrophenol acetate


substrate_name: p-nitrophenol butyrate

substrate: p-nitrophenol butyrate


enzyme_display_name: feruloyl esterase

organism: Anaeromyces mucronatus

substrate_name: ethyl ferulate

proof_lines:
pH 7.2, 37°C
Raw SKiD Env: Temp=37°C, pH=7.2

source_databases_merged: brenda skid

enzyme: feruloyl esterase

substrate: ethyl ferulate


substrate_name: methyl ferulate

substrate: methyl ferulate


enzyme_display_name: cutinase

organism: Thermobifida fusca

enzyme: cutinase


enzyme_display_name: acetylxylan esterase

organism: Flavobacterium johnsoniae

substrate_name: 4-methylumbelliferyl acetate

column_label: Table 1 columns Substrate, Specific activity (umol/min/mg), kcat (s^-1), Km (mM), and kcat/Km (s^-1 mM^-1); row 4-MUA.

normalized_value_unit_evidence: kcat 95.1 s^-1 and Km 0.8 mM match the export; explicit table kcat/Km is 114.7 s^-1*mM^-1, not exported 118.87499999999999 s^-1*mM^-1.

raw_value_unit_evidence: Table 1 row 4-MUA reports specific activity 126.3 +/- 5.9 umol/min/mg, kcat 95.1 +/- 4.4 s^-1, Km 0.8 +/- 0.1 mM, kcat/Km 114.7 s^-1 mM^-1.

table_label: Table 1: Kinetic parameters of FjoAcXE on 4-MUA and pNP-acetate

enzyme: acetylxylan esterase

substrate: 4-methylumbelliferyl acetate


substrate_name: 4-nitrophenyl acetate

column_label: Table 1 columns Substrate, Specific activity (umol/min/mg), kcat (s^-1), Km (mM), and kcat/Km (s^-1 mM^-1); row pNP-acetate.

normalized_value_unit_evidence: kcat 120.8 s^-1 and Km 0.9 mM match the export; explicit table kcat/Km is 127.9 s^-1*mM^-1, not exported 134.22222222222223 s^-1*mM^-1.

raw_value_unit_evidence: Table 1 row pNP-acetate reports specific activity 160.7 +/- 4.0 umol/min/mg, kcat 120.8 +/- 3.0 s^-1, Km 0.9 +/- 0.1 mM, kcat/Km 127.9 s^-1 mM^-1.

row_label: pNP-acetate

substrate: 4-nitrophenyl acetate


organism: Streptomyces werraensis

substrate_name: methyl sinapate

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

substrate: methyl sinapate


organism: Thermobifida cellulosilytica


substrate_name: 4-nitrophenyl butanoate

substrate: 4-nitrophenyl butanoate


enzyme_display_name: UniProt P0A8Y8

organism: Escherichia coli

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P0A8Y8


enzyme_display_name: alkaline phosphatase

organism: Thermus sp. NTU-237

substrate_name: 4-nitrophenyl phosphate

proof_lines:
at pH 10.5 and 70°C
80°C, pH 12

enzyme: alkaline phosphatase

substrate: 4-nitrophenyl phosphate


organism: Pinctada fucata


enzyme_display_name: UniProt P00634

substrate_name: p-nitrophenyl phosphate

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P00634

substrate: p-nitrophenyl phosphate


enzyme_display_name: UniProt Q9KWY4

organism: Antarctic bacterium TAB5

enzyme: UniProt Q9KWY4


organism: Bacillus licheniformis


organism: Aspergillus usamii

substrate_name: ferulic acid 4-nitrophenyl ester

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

substrate: ferulic acid 4-nitrophenyl ester


enzyme_display_name: Hormone-sensitive lipase

organism: Rattus norvegicus

enzyme: Hormone-sensitive lipase


enzyme_display_name: Acyl-protein thioesterase 2

organism: Homo sapiens

substrate_name: Lyso-PC (C16:0)

enzyme: Acyl-protein thioesterase 2

substrate: Lyso-PC (C16:0)


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


enzyme_display_name: Acetylajmalan esterase

organism: Rauvolfia serpentina

enzyme: Acetylajmalan esterase


enzyme_display_name: Palmitoyl thioesterase CPT1C

substrate_name: palmitoyl-CoA

enzyme: Palmitoyl thioesterase CPT1C

substrate: palmitoyl-CoA


substrate_name: carnitine

substrate: carnitine


enzyme_display_name: poly(ethylene terephthalate) hydrolase

organism: Marinactinospora thermotolerans

substrate_name: 4-nitrophenyl octanoate

assay_conditions_summary: pH 8

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

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

row_label: pNP-C8 / MtCut

enzyme: poly(ethylene terephthalate) hydrolase

substrate: 4-nitrophenyl octanoate


organism: Saccharomonospora viridis

substrate_name: Poly(ethylene terephthalate)

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S226P/R228S/D250C/E296C to reconstruct the assayed variant sequence.

proof_lines:
Cut190
Saccharomonospora viridis AHK190
PET hydrolysis

substrate: Poly(ethylene terephthalate)


enzyme_display_name: acetylajmaline esterase

organism: Rauvolfia verticillata

proof_lines:
acetylajmalan esterase
Rauvolfia verticillata

enzyme: acetylajmaline esterase


enzyme_display_name: 4-hydroxybenzoyl-CoA thioesterase

organism: Pseudomonas reinekei

column_label: Table label: TABLE 1. Steady-state kinetic constants for B. halodurans gentisyl-CoA thioesterase- and Pseudomonas 4-hydroxybenzoyl-CoA thioesterase-catalyzed hydrolysis of acyl-CoAs. Section: 4-Hydroxybenzoyl-CoA thioesterase. Row: Wild type | Gentisyl-CoA. Columns read: k cat (s^-1) cell 8.9 +/- 0.6, K m (uM) cell (6 +/- 1) x 10^1, k cat / K m (M^-1 s^-1) cell 1.5 x 10^5. metric: kcat; raw value: 8.9 +/- 0.6; raw unit: s^-1; normalized value: 8.9 s^(-1); metric: Km; raw value: (6 +/- 1) x 10^1; raw unit: uM; normalized value: 0.06 mM; metric: kcat/Km; raw value: 8.9 / 0.06; raw unit: s^-1 mM^-1; normalized value: 148.33333333333334 s^-1 mM^-1; assay condition: Purified recombinant enzyme; steady-state kinetic constants measured at 25 C with a DTNB-based assay following 5-thio-2-nitrobenzoate absorbance at 412 nm in 0.2-ml reactions containing DTNB (1 mM), KCl (0.2 M) and 50 mM K + HEPES (pH 7.5, 25 C); initial-velocity data were fit to V = Vmax[S]/([S] + Km) and kcat was calculated from Vmax/[E]. Export row conditions: pH 7.5.

normalized_value_unit_evidence: Table 1 row 4-Hydroxybenzoyl-CoA thioesterase | Wild type | Gentisyl-CoA: kcat 8.9 +/- 0.6 s^-1 = 8.9 s^(-1); Km (6 +/- 1) x 10^1 uM = 60 uM = 0.06 mM (1 uM = 0.001 mM); kcat/Km 148.33333333333334 s^-1 mM^-1. The printed Table 1 kcat/Km cell for this row is 1.5 x 10^5 M^-1 s^-1, which normalizes to 150.0 s^-1 mM^-1. The export stores the full-precision quotient of this same row's printed kcat and Km cells, 8.9 s^-1 / 0.06 mM = 148.33333333333334 s^-1 mM^-1, and that quotient rounds to 1.5 x 10^2 at the printed cell's own two-significant-figure precision, so the printed cell and the exported value agree and the difference is printed precision only. In the cached HTML the multiplication sign renders as the Unicode multiplication sign, the superscript minus one as the Unicode minus sign, the micro sign as the Greek letter mu, the plus-minus sign as the Unicode plus-minus sign, and superscript exponents are flattened onto the line, so the printed cell `1.5 × 10 5` is the paper's 1.5 x 10^5 M^-1 s^-1.

raw_value_unit_evidence: TABLE 1. Steady-state kinetic constants for B. halodurans gentisyl-CoA thioesterase- and Pseudomonas 4-hydroxybenzoyl-CoA thioesterase-catalyzed hydrolysis of acyl-CoAs | header row: Enzyme and type Substrate k cat (s −1 ) K m (μM) k cat / K m (M −1 s −1 ) | section row: 4-Hydroxybenzoyl-CoA thioesterase | data row: Wild type Gentisyl-CoA 8.9 ± 0.6 (6 ± 1) × 10 1 1.5 × 10 5 | cells read: k cat = 8.9 +/- 0.6 s^-1; K m = (6 +/- 1) x 10^1 uM; k cat / K m = 1.5 x 10^5 M^-1 s^-1

enzyme: 4-hydroxybenzoyl-CoA thioesterase


proof_lines: BH1999 protein of Bacillus halodurans C-125


enzyme_display_name: mono(ethylene terephthalate) hydrolase

organism: Piscinibacter sakaiensis

substrate_name: ethylene terephthalate

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

enzyme: mono(ethylene terephthalate) hydrolase

substrate: ethylene terephthalate


enzyme_display_name: sn-1-specific diacylglycerol lipase ABHD11

organism: Bos taurus


organism: Pleurotus eryngii

substrate_name: benzyl glucuronic acid

column_label: Table 4 columns Km (mM), Vmax (umol mg^-1 min^-1), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

raw_value_unit_evidence: Table 4 row PeGE reports Km 23.9 mM, Vmax 150.7 umol mg^-1 min^-1, kcat 104.6 s^-1, and kcat/Km 4.38 s^-1 mM^-1.

row_label: PeGE

table_label: Table 4: Kinetic parameters for CsGE and PeGE with BnGlcA as the substrate

substrate: benzyl glucuronic acid


enzyme: sn-1-specific diacylglycerol lipase ABHD11


organism: Wolfiporia cocos

substrate_name: benzyl-D-glucuronate

substrate: benzyl-D-glucuronate


organism: Trichoderma reesei


organism: Ideonella sakaiensis

substrate_name: Mono(2-hydroxyethyl) terephthalate

substrate: Mono(2-hydroxyethyl) terephthalate


organism: Aspergillus nidulans

substrate_name: methyl ferulate

proof_lines:
feruloyl esterase
methyl ferulate
Aspergillus nidulans

substrate: methyl ferulate


organism: Volvariella volvacea

substrate_name: 4-Methylumbelliferyl acetate

substrate: 4-Methylumbelliferyl acetate


enzyme_display_name: acetylalkylglycerol acetylhydrolase

organism: Mus musculus

smiles: CCCCCCCCCCCCCCCCOCC(CO)OC(=O)C

enzyme: acetylalkylglycerol acetylhydrolase


enzyme_display_name: feruloyl esterase

organism: Aspergillus usamii

assay_conditions_summary: pH 5

enzyme: feruloyl esterase


enzyme_display_name: Feruloyl esterase 1

organism: Penicillium parvum

substrate_name: methyl ferulate (MFA)

proof_lines:
EpFAE1
methyl ferulate
Eupenicillium parvum

enzyme: Feruloyl esterase 1

substrate: methyl ferulate (MFA)


organism: Gelatoporia subvermispora

raw_value_unit_evidence: Table 4 row CsGE reports Km 55.8 mM, Vmax 30.6 umol mg^-1 min^-1, kcat 23.6 s^-1, and kcat/Km 0.42 s^-1 mM^-1.

row_label: CsGE


enzyme_display_name: pyrethroid hydrolase

organism: uncultured bacterium

substrate_name: 4-nitrophenyl acetate

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

enzyme: pyrethroid hydrolase

substrate: 4-nitrophenyl acetate


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


organism: Pleurotus sapidus

column_label: Downloaded Wiley/IUBMB PDF states that the purified enzyme possessed Km, kcat, and kcat/Km values of 427 uM, 1.20 s^-1, and 2.81 mM^-1 s^-1 for methyl ferulate.

normalized_value_unit_evidence: Km normalized_value=0.427 normalized_unit=mM; kcat normalized_value=1.2 normalized_unit=s^-1; kcat/Km normalized_value=2.81 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Results text reports methyl ferulate Km raw_value=427 raw_unit=uM, kcat raw_value=1.20 raw_unit=s^-1, and kcat/Km raw_value=2.81 raw_unit=mM^-1 s^-1.

row_label: purified Est1 against methyl ferulate

table_label: PDF Results section, kinetic constants paragraph


organism: Streptomyces olivochromogenes

column_label: Abstract reports with methyl ferulate as substrate, pH and temperature optima were 5.5 and 30 degrees C, with a Km of 1.86 mM.

raw_value_unit_evidence: Km raw_value=1.86 mM raw_unit=mM

row_label: S. olivochromogenes ferulic acid esterase / methyl ferulate

table_label: PubMed XML abstract PMID 1663152


enzyme_display_name: cutinase

organism: Saccharomonospora viridis

substrate_name: p-Nitrophenyl butyrate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S226P/R228S to reconstruct the assayed variant sequence.

proof_lines:
Cut190
Saccharomonospora viridis AHK190
PET

enzyme: cutinase

substrate: p-Nitrophenyl butyrate


organism: Alternaria brassicicola

substrate_name: 4-nitrophenyl butyrate

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

proof_lines:
Alternaria brassicicola
cutinases
4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


proof_lines:
Aspergillus nidulans
ANCUT2
cutinase


organism: Thermobifida cellulosilytica

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

column_label: Table II row Thc_Cut2_Leu183Ala, PNPA columns: KM (mM)=1.9 +/- 0.1; kcat (s^-1)=25; kcat/KM (s^-1 mM^-1)=13.

normalized_value_unit_evidence: kcat 25 s^-1; Km 1.9 mM; kcat/Km 13 s^-1 mM^-1 as displayed in Table II.

row_label: Thc_Cut2_Leu183Ala with PNPA (4-nitrophenyl acetate/p-nitrophenyl acetate)

table_label: PMID 23592055 Wiley Table II, Kinetic parameters with soluble substrates, PNPA columns


organism: Rattus norvegicus

substrate_name: cholesteryl (9Z-octadecenoate) (dimeric form)

proof_lines:
hormone-sensitive lipase
dimeric HSL
cholesteryl ester substrate


enzyme_display_name: UniProt P09889

organism: Sus scrofa

substrate_name: Fmoc-EEY(P)AA

proof_lines:
Raw SKiD Env: Temp=25°C, pH=4.9
Raw SKiD Env: Temp=25°C, pH=2.5

enzyme: UniProt P09889

substrate: Fmoc-EEY(P)AA


substrate_name: EEY(P)AA

substrate: EEY(P)AA


enzyme_display_name: UniProt P26093

organism: Haemophilus influenzae

substrate_name: nicotinamide mononucleotide

enzyme: UniProt P26093

substrate: nicotinamide mononucleotide


enzyme_display_name: UniProt Q9APF7

organism: Legionella pneumophila

enzyme: UniProt Q9APF7


substrate_name: 4-nitrophenyl phosphate

substrate: 4-nitrophenyl phosphate


enzyme_display_name: UniProt B9VWB2

organism: Pasteurella multocida

enzyme: UniProt B9VWB2


substrate_name: NMN

substrate: NMN


enzyme_display_name: UniProt Q9ZVL6

organism: Arabidopsis thaliana

enzyme: UniProt Q9ZVL6


substrate_name: O-phospho-L-serine

substrate: O-phospho-L-serine


enzyme_display_name: UniProt P24666

organism: Homo sapiens

substrate_name: p-nitrophenyl phosphate

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=4.7

enzyme: UniProt P24666

substrate: p-nitrophenyl phosphate


enzyme_display_name: UniProt B6YX36

organism: Thermococcus onnurineus

proof_lines:
Raw SKiD Env: Temp=65°C, pH=6.5
Raw SKiD Env: Temp=37°C, pH=6.5

enzyme: UniProt B6YX36


enzyme_display_name: Putative phosphoserine phosphatase 2

organism: Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6)

enzyme: Putative phosphoserine phosphatase 2


enzyme_display_name: UniProt P07024

organism: Escherichia coli

enzyme: UniProt P07024


enzyme_display_name: UniProt P49902

substrate_name: Inosine

enzyme: UniProt P49902

substrate: Inosine


enzyme_display_name: UniProt Q5ZZB6

enzyme: UniProt Q5ZZB6


enzyme_display_name: UniProt Q9D020

organism: Mus musculus

enzyme: UniProt Q9D020


substrate_name: ribavirin

substrate: ribavirin


enzyme_display_name: 5'-nucleotidase SurE

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

substrate_name: pNPP (at 76 degrees Celsius)

enzyme: 5'-nucleotidase SurE

substrate: pNPP (at 76 degrees Celsius)


enzyme_display_name: UniProt P9WKJ1

organism: Mycobacterium tuberculosis

substrate_name: D-fructose 1,6-bisphosphate

enzyme: UniProt P9WKJ1

substrate: D-fructose 1,6-bisphosphate


enzyme_display_name: UniProt Q7NXD4

organism: Chromobacterium violaceum

substrate_name: adenosine 3',5'-bisphosphate

enzyme: UniProt Q7NXD4

substrate: adenosine 3',5'-bisphosphate


substrate_name: guanosine 3',5'-bisphosphate

substrate: guanosine 3',5'-bisphosphate


substrate_name: 2'-deoxyuridine 3',5'-bisphosphate

substrate: 2'-deoxyuridine 3',5'-bisphosphate


enzyme_display_name: UniProt O95861

enzyme: UniProt O95861


enzyme_display_name: UniProt O31097

organism: Bacillus subtilis subsp. subtilis

substrate_name: myo-inositol hexakisphosphate

enzyme: UniProt O31097

substrate: myo-inositol hexakisphosphate


organism: Bacillus subtilis

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -10, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D24G/K265N with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D24G/K70R/K111E/N121S with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.


enzyme_display_name: Phytase A

organism: Penicillium oxalicum

substrate_name: phytate

enzyme: Phytase A

substrate: phytate


enzyme_display_name: Glucose-6-phosphatase 2

substrate_name: glucose-6-phosphate (at pH 6.5)

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

enzyme: Glucose-6-phosphatase 2

substrate: glucose-6-phosphate (at pH 6.5)


enzyme_display_name: cocaine esterase

organism: Rhodococcus sp.

substrate_name: cocaine

enzyme: cocaine esterase

substrate: cocaine


enzyme_display_name: N-acyl homoserine lactonase AiiA

organism: Bacillus thuringiensis subsp. kurstaki

substrate_name: GBL (with cobalt as cofactor)

enzyme: N-acyl homoserine lactonase AiiA

substrate: GBL (with cobalt as cofactor)


enzyme_display_name: Name not preserved

organism: Bacillus thuringiensis

substrate_name: N-decanoyl-L-homoserine lactone

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: Name not preserved

substrate: N-decanoyl-L-homoserine lactone


enzyme_display_name: UniProt O42807

organism: Aspergillus niger

substrate_name: methyl ferulate

proof_lines:
Raw SKiD Env: Temp=40°C, pH=6
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=40°C, pH=6.4

enzyme: UniProt O42807

substrate: methyl ferulate


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


enzyme_display_name: Alcohol O-acetyltransferase 1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: isoamyl alcohol (for acetyltransferase activity)

smiles: CC(C)CCO

enzyme: Alcohol O-acetyltransferase 1


enzyme_display_name: Acyl-protein thioesterase 1

substrate_name: lysophosphatidylcholine

enzyme: Acyl-protein thioesterase 1

substrate: lysophosphatidylcholine


substrate_name: hexanoyl-CoA (for thioesterase activity)

assay_conditions_summary: buffer in vitro; cofactor CoA

column_label: Main text states KM was 12+/-3 uM for hexanoyl-CoA; Supplementary Table 1 row Hexanoyl reports KM 12+/-3 under wild-type Atf1p.

raw_value_unit_evidence: KM 12+/-3 uM for hexanoyl-CoA; supplement row Hexanoyl under Atf1p wild-type

row_label: Atf1p wild-type; Hexanoyl

table_label: Supplementary Table 1. Kinetic data from coupled enzyme assays; main text Biochemical assays of Atf1p.


enzyme_display_name: Palmitoyl-protein thioesterase ABHD10, mitochondrial


organism: Bacillus thuringiensis serovar kurstaki

substrate_name: N-butyryl-L-homoserine lactone

proof_lines: pH and temperature not specified in the publication, mutant enzyme F64A

substrate: N-butyryl-L-homoserine lactone


proof_lines: pH and temperature not specified in the publication, mutant enzyme A206V


proof_lines: pH and temperature not specified in the publication, mutant enzyme A206I


proof_lines: pH and temperature not specified in the publication, mutant enzyme F64W


proof_lines: pH and temperature not specified in the publication, mutant enzyme F64W/V69W


proof_lines: pH and temperature not specified in the publication, mutant enzyme A206L


proof_lines: pH and temperature not specified in the publication, mutant enzyme F64W/V69W/A206F


proof_lines: pH and temperature not specified in the publication, mutant enzyme V69L


proof_lines: pH and temperature not specified in the publication, mutant enzyme V69W/A206F


proof_lines: pH and temperature not specified in the publication, mutant enzyme V69F


proof_lines: pH and temperature not specified in the publication, mutant enzyme F64W/A206F


proof_lines: pH and temperature not specified in the publication, mutant enzyme V69W


proof_lines: pH and temperature not specified in the publication, mutant enzyme V69I


proof_lines: pH and temperature not specified in the publication, mutant enzyme F64L


proof_lines: pH and temperature not specified in the publication, mutant enzyme A206W


proof_lines: pH and temperature not specified in the publication, mutant enzyme A206F


proof_lines: pH and temperature not specified in the publication, mutant enzyme V69A


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


enzyme_display_name: Hormone-sensitive lipase

organism: Rattus norvegicus

substrate_name: retinyl palmitate

enzyme: Hormone-sensitive lipase

substrate: retinyl palmitate


enzyme_display_name: acyl-CoA hydrolase

organism: Haemophilus influenzae

proof_lines: pH 7.5, 25°C, determined using the 5,5'-dithiobis(2-nitrobenzoic acid) spectrophotometric assay

enzyme: acyl-CoA hydrolase


substrate_name: glutaryl-CoA

substrate: glutaryl-CoA


substrate_name: phenylacetyl-CoA

substrate: phenylacetyl-CoA


substrate_name: isobutyryl-CoA

substrate: isobutyryl-CoA


substrate_name: succinyl-CoA

substrate: succinyl-CoA


substrate_name: arachidoyl-CoA

substrate: arachidoyl-CoA


substrate_name: beta-methylcrotonyl-CoA

proof_lines: absorbance of 5-thio-2-nitrobenzoate formed by reaction of 5,5'-dithiobis(2-nitrobenzoic acid) is measured

substrate: beta-methylcrotonyl-CoA


substrate_name: stearoyl-CoA

substrate: stearoyl-CoA


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


substrate_name: methylmalonyl-CoA

substrate: methylmalonyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


substrate_name: linoleoyl-CoA

substrate: linoleoyl-CoA


substrate_name: tiglyl-CoA

substrate: tiglyl-CoA


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


substrate_name: malonyl-CoA

substrate: malonyl-CoA


substrate_name: n-octanoyl-CoA

substrate: n-octanoyl-CoA


substrate_name: palmitoleoyl-CoA

substrate: palmitoleoyl-CoA


substrate_name: myristoyl-CoA

substrate: myristoyl-CoA


substrate_name: hexanoyl-CoA

substrate: hexanoyl-CoA


substrate_name: n-butyryl-CoA

substrate: n-butyryl-CoA


substrate_name: propionyl-CoA

substrate: propionyl-CoA


substrate_name: isovaleryl-CoA

substrate: isovaleryl-CoA


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


enzyme_display_name: feruloyl esterase

organism: Aspergillus oryzae

substrate_name: methyl caffeate

enzyme: feruloyl esterase

substrate: methyl caffeate


substrate_name: methyl ferulate

substrate: methyl ferulate


substrate_name: methyl p-coumarate

substrate: methyl p-coumarate


substrate_name: methyl sinapinate

substrate: methyl sinapinate


substrate_name: alpha-naphthyl propionate

substrate: alpha-naphthyl propionate


substrate_name: ethyl ferulate

substrate: ethyl ferulate


enzyme_display_name: Palmitoyl-protein thioesterase 1

organism: Homo sapiens

substrate_name: S-palmitoyl-N-acetylcysteamine

smiles: CCCCCCCCCCCCCCCC(=O)SCCNC(=O)C

enzyme: Palmitoyl-protein thioesterase 1

substrate: S-palmitoyl-N-acetylcysteamine


organism: Escherichia coli K-12


substrate_name: salicylyl-CoA

substrate: salicylyl-CoA


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


organism: Escherichia coli


substrate_name: n-butyryl-pantetheine phosphate

substrate: n-butyryl-pantetheine phosphate


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: phenylacetyl-CoA

substrate: phenylacetyl-CoA


substrate_name: isobutyryl-CoA

substrate: isobutyryl-CoA


substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


enzyme_display_name: hormone-sensitive lipase

substrate_name: cholesteryl oleate

enzyme: hormone-sensitive lipase

substrate: cholesteryl oleate


mutation_type: deletion


substrate_name: 4-nitrophenyl oleate

substrate: 4-nitrophenyl oleate


organism: Streptomyces sp. TH-2

proof_lines: wild-type, pH not specified in the publication, 50°C


proof_lines: mutant 18PG, pH not specified in the publication, 50°C


enzyme_display_name: cutinase

organism: Fusarium solani

substrate_name: p-nitrophenyl butyrate

proof_lines: T179Cmutant, sodium dioctyl sulfosuccinate concentration = 0.5 mM

enzyme: cutinase

substrate: p-nitrophenyl butyrate


proof_lines: L153Q mutant, sodium dioctyl sulfosuccinate concentration = 0 mM

proof_lines: L153Q mutant, sodium dioctyl sulfosuccinate concentration = 0.5 mM

proof_lines: L153Q mutant, sodium dioctyl sulfosuccinate concentration = 1 mM


proof_lines: wild type, sodium dioctyl sulfosuccinate concentration = 2 mM

proof_lines: wild type, sodium dioctyl sulfosuccinate concentration = 1.5 mM

proof_lines: wild type, sodium dioctyl sulfosuccinate concentration = 0.5 mM


proof_lines: S54D mutant, sodium dioctyl sulfosuccinate concentration = 0 mM

proof_lines: S54D mutant, sodium dioctyl sulfosuccinate concentration = 1 mM

proof_lines: S54D mutant, sodium dioctyl sulfosuccinate concentration = 0.5 mM


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


substrate_name: trioctanoin

substrate: trioctanoin


substrate_name: tripropionin

smiles: CCC(=O)OCC(COC(=O)CC)OC(=O)CC

substrate: tripropionin


substrate_name: tributyrin

smiles: CCCC(=O)OCC(COC(=O)CCC)OC(=O)CCC

substrate: tributyrin


substrate_name: vinyl acetate

smiles: CC(=O)OC=C

substrate: vinyl acetate


substrate_name: vinyl laurate

smiles: CCCCCCCCCCCC(=O)OC=C

substrate: vinyl laurate


substrate_name: vinyl butyrate

smiles: CCCC(=O)OC=C

substrate: vinyl butyrate


substrate_name: vinyl propionate

smiles: CCC(=O)OC=C

substrate: vinyl propionate


organism: Aspergillus awamori

substrate_name: alpha-naphthylcaprylate

substrate: alpha-naphthylcaprylate


proof_lines:
pH 5.0, 37°C, wild type enzyme
37°C, pH 5.0, wild-type enzyme


substrate_name: alpha-naphthylbutyrate

substrate: alpha-naphthylbutyrate


organism: Colletotrichum gloeosporioides

substrate_name: 4-nitrophenyl laurate

substrate: 4-nitrophenyl laurate


substrate_name: 4-nitrophenyl caprylate

substrate: 4-nitrophenyl caprylate


substrate_name: 4-nitrophenyl myristate

substrate: 4-nitrophenyl myristate


substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


organism: Aureobasidium pullulans

substrate_name: methyl sinapinate

substrate: methyl sinapinate


substrate_name: methyl ferulate

substrate: methyl ferulate


substrate_name: methyl caffeate

substrate: methyl caffeate


substrate_name: methyl p-coumarate

substrate: methyl p-coumarate


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

assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM HEPES-K (pH 7.5

proof_lines: in 50 mM HEPES-K (pH 7.5) buffer, at 37°C


substrate_name: 4-nitrophenyl caproate

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

substrate: 4-nitrophenyl caproate


substrate_name: 4-nitrophenyl propionate

substrate: 4-nitrophenyl propionate


enzyme_display_name: UniProt P09467

substrate_name: D-fructose 1,6-bisphosphate

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P09467

substrate: D-fructose 1,6-bisphosphate


enzyme_display_name: UniProt P0A9C9

proof_lines:
Raw SKiD Env: Temp=37°C, pH=9
Raw SKiD Env: Temp=-----, pH=7.7

enzyme: UniProt P0A9C9


enzyme_display_name: UniProt P36136

organism: Saccharomyces cerevisiae

enzyme: UniProt P36136


enzyme_display_name: UniProt P73922

organism: Synechocystis sp.

enzyme: UniProt P73922


enzyme_display_name: UniProt Q8TZH9

organism: Pyrococcus furiosus

proof_lines:
Raw SKiD Env: Temp=22°C, pH=8
Raw SKiD Env: Temp=50°C, pH=8

enzyme: UniProt Q8TZH9


enzyme_display_name: UniProt P0A993

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.5
Raw SKiD Env: Temp=22°C, pH=7.5

enzyme: UniProt P0A993


substrate_name: D-Fructose 1-phosphate

smiles: C(C(C(C(C(=O)COP(=O)(O)O)O)O)O)O

substrate: D-Fructose 1-phosphate


enzyme_display_name: UniProt G7J7Q5

organism: Medicago truncatula

substrate_name: L-histidinol phosphate

enzyme: UniProt G7J7Q5

substrate: L-histidinol phosphate


enzyme_display_name: UniProt P95189

organism: Mycobacterium tuberculosis

enzyme: UniProt P95189


enzyme_display_name: UniProt Q02150

organism: Lactococcus lactis subsp. lactis

enzyme: UniProt Q02150


enzyme_display_name: UniProt P62136

substrate_name: 4-nitrophenyl phosphate

enzyme: UniProt P62136

substrate: 4-nitrophenyl phosphate


enzyme_display_name: UniProt Q8X270

organism: Thermococcus kodakarensis

proof_lines:
Raw SKiD Env: Temp=60°C, pH=5
Raw SKiD Env: Temp=20°C, pH=5

enzyme: UniProt Q8X270


enzyme_display_name: PH domain leucine-rich repeat-containing protein phosphatase 2

substrate_name: p-nitrophenyl phosphate

substrate: p-nitrophenyl phosphate


organism: Coprinopsis cinerea

substrate_name: 4-nitrophenyl hexadecanoate

proof_lines: pH and temperature not specified in the publication

substrate: 4-nitrophenyl hexadecanoate


substrate_name: 4-nitrophenyl dodecanoate

substrate: 4-nitrophenyl dodecanoate


substrate_name: 4-nitrophenyl octanoate

substrate: 4-nitrophenyl octanoate


enzyme_display_name: acyl-CoA hydrolase

organism: Haemophilus influenzae

substrate_name: butyrylpantetheine phosphate

enzyme: acyl-CoA hydrolase

substrate: butyrylpantetheine phosphate


substrate_name: isobutyryl-CoA

substrate: isobutyryl-CoA


substrate_name: lauroyl-CoA

substrate: lauroyl-CoA


substrate_name: butyryl-CoA

substrate: butyryl-CoA


enzyme_display_name: feruloyl esterase

organism: Alternaria tenuissima

substrate_name: methyl sinapate

enzyme: feruloyl esterase

substrate: methyl sinapate


substrate_name: methyl ferulate

substrate: methyl ferulate


substrate_name: ethyl ferulate

substrate: ethyl ferulate


organism: Talaromyces stipitatus

substrate_name: methyl 3,5-dimethoxy cinnamate

substrate: methyl 3,5-dimethoxy cinnamate


substrate_name: methyl cinnamate

substrate: methyl cinnamate


substrate_name: n-propyl ferulate

substrate: n-propyl ferulate


substrate_name: n-butyl ferulate

substrate: n-butyl ferulate


organism: Bacillus thuringiensis

substrate_name: N-pentanoyl-L-homoserine lactone

proof_lines: pH 7.5, temperature not specified in the publication, mutant F107W

substrate: N-pentanoyl-L-homoserine lactone


substrate_name: N-hexanoyl-L-homoserine lactone

substrate: N-hexanoyl-L-homoserine lactone


substrate_name: N-heptanoyl-L-homoserine lactone

substrate: N-heptanoyl-L-homoserine lactone


substrate_name: N-decanoyl-L-homoserine lactone

substrate: N-decanoyl-L-homoserine lactone


substrate_name: N-octanoyl-L-homoserine lactone

substrate: N-octanoyl-L-homoserine lactone


proof_lines: pH 7.5, temperature not specified in the publication, mutant F64C/F68C, absence of DTT

proof_lines: pH 7.5, temperature not specified in the publication, mutant F64C/F68C, presence of DTT


proof_lines: pH 7.5, temperature not specified in the publication, wild-type


proof_lines: pH 7.5, temperature not specified in the publication, wild-type, presence of DTT


organism: Aspergillus niger

substrate_name: ferulate

substrate: ferulate


organism: Bacillus sp. (in: firmicutes)

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

proof_lines: pH 7.4, 22°C, recombinant wild-type enzyme

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


substrate_name: N-butanoyl-L-homoserine lactone

substrate: N-butanoyl-L-homoserine lactone


enzyme_display_name: UniProt Q8CHP8

organism: Mus musculus

enzyme: UniProt Q8CHP8


enzyme_display_name: inositol-phosphate phosphatase

organism: Cyberlindnera jadinii

substrate_name: DL-myo-inositol 1-phosphate

enzyme: inositol-phosphate phosphatase

substrate: DL-myo-inositol 1-phosphate


substrate_name: N-butanoyl-DL-homoserine lactone

proof_lines:
pH 7.4, 32°C
at pH 7.4 and 45°C

substrate: N-butanoyl-DL-homoserine lactone


substrate_name: N-hexanoyl-DL-homoserine lactone

proof_lines: Zn2+-form of AHL lactonase, at pH 7.4 and at 28°C

substrate: N-hexanoyl-DL-homoserine lactone


substrate_name: N-heptanoyl-DL-homoserine lactone

substrate: N-heptanoyl-DL-homoserine lactone


substrate_name: N-octanoyl-DL-homoserine lactone

substrate: N-octanoyl-DL-homoserine lactone


substrate_name: methyl ferulate

substrate: methyl ferulate


proof_lines:
mutant Y194F with Zn2+
mutant Y194F with Co2+


substrate_name: N-hexanoyl-L-homoserine thiolactone

substrate: N-hexanoyl-L-homoserine thiolactone


proof_lines:
mutant D108N with Zn2+
mutant D108N with Co2+


enzyme_display_name: UniProt A2TBB4

organism: Debaryomyces castellii

substrate_name: myo-inositol hexakisphosphate

enzyme: UniProt A2TBB4

substrate: myo-inositol hexakisphosphate


enzyme_display_name: UniProt P07102

organism: Escherichia coli

proof_lines:
Raw SKiD Env: Temp=-----, pH=2.5
Raw SKiD Env: Temp=-----, pH=6
Raw SKiD Env: Temp=37°C, pH=5

enzyme: UniProt P07102


enzyme_display_name: UniProt P0A924

enzyme: UniProt P0A924


smiles: CCCCCC(=O)OCC(COP(=O)(O)O)O


enzyme_display_name: cutinase

organism: Monilinia fructicola

substrate_name: p-nitrophenylbutanoate

enzyme: cutinase

substrate: p-nitrophenylbutanoate


organism: Fusarium solani

substrate_name: 4-nitrophenyl hexadecanoate

substrate: 4-nitrophenyl hexadecanoate


substrate_name: 4-nitrophenyl dodecanoate

substrate: 4-nitrophenyl dodecanoate


substrate_name: 4-nitrophenyl octanoate

substrate: 4-nitrophenyl octanoate


substrate_name: 4-nitrophenyl acetate

assay_conditions_summary: pH 7.5; buffer 14.5 mM Tris-HCl

proof_lines: in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol

substrate: 4-nitrophenyl acetate


enzyme_display_name: Type II inositol polyphosphate 5-phosphatase 15

organism: Arabidopsis thaliana

substrate_name: PtdIns(4,5)P2 (at pH 7.0 and 22 degrees Celsius)


organism: Rhizoctonia solani

substrate_name: methyl caffeate

substrate: methyl caffeate


substrate_name: chlorogenate

substrate: chlorogenate


substrate_name: methyl p-coumarate

substrate: methyl p-coumarate


organism: Fusarium oxysporum

substrate_name: methyl sinapate

substrate: methyl sinapate


organism: Streptomyces sp.


substrate_name: methyl 4-coumarate

substrate: methyl 4-coumarate


organism: Trichoderma harzianum

substrate_name: p-nitrophenyl palmitate

substrate: p-nitrophenyl palmitate


substrate_name: p-nitrophenyl acetate

substrate: p-nitrophenyl acetate


substrate_name: p-nitrophenyl butyrate

substrate: p-nitrophenyl butyrate


substrate_name: p-nitrophenyl valerate

substrate: p-nitrophenyl valerate


enzyme_display_name: UniProt P45314

organism: Haemophilus influenzae

substrate_name: KDN 9-phosphate

enzyme: UniProt P45314

substrate: KDN 9-phosphate


enzyme_display_name: UniProt P18031

organism: Homo sapiens

substrate_name: 4-nitrophenyl phosphate

proof_lines:
Raw SKiD Env: Temp=25°C, pH=5.5
Raw SKiD Env: Temp=22°C, pH=6
Raw SKiD Env: Temp=22°C, pH=4.5

enzyme: UniProt P18031

substrate: 4-nitrophenyl phosphate


enzyme_display_name: UniProt P35236

enzyme: UniProt P35236


enzyme_display_name: UniProt Q9Y6W6

enzyme: UniProt Q9Y6W6


substrate_name: 3,6-fluorescein diphosphate

substrate: 3,6-fluorescein diphosphate


enzyme_display_name: UniProt Q15256

substrate_name: bis(4-nitrophenyl) phosphate

enzyme: UniProt Q15256

substrate: bis(4-nitrophenyl) phosphate


enzyme_display_name: UniProt Q4QEZ7

organism: Leishmania major

enzyme: UniProt Q4QEZ7


enzyme_display_name: Protein phosphatase EYA

substrate_name: para-nitrophenyl phosphate (at pH 5.5)

enzyme: Protein phosphatase EYA

substrate: para-nitrophenyl phosphate (at pH 5.5)


organism: Aspergillus flavus

proof_lines:
pH 5.5, 40°C, recombinant enzyme
pH 6.0, 58°C


substrate_name: methyl sinapinate

substrate: methyl sinapinate


substrate_name: methyl ferulate

substrate: methyl ferulate


organism: Aspergillus oryzae


substrate_name: 4-nitrophenyl valerate

substrate: 4-nitrophenyl valerate


substrate_name: 4-nitrophenyl hexanoate

substrate: 4-nitrophenyl hexanoate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


enzyme_display_name: protein-tyrosine-phosphatase

substrate_name: P-Erk2; H2O

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

enzyme: protein-tyrosine-phosphatase

substrate: P-Erk2; H2O


enzyme_display_name: [acetyl-CoA carboxylase]-phosphatase

organism: Rattus norvegicus

substrate_name: [acetyl-CoA carboxylase]-phosphate

enzyme: [acetyl-CoA carboxylase]-phosphatase

substrate: [acetyl-CoA carboxylase]-phosphate


substrate_name: Unknown

proof_lines: pH 5.5, 25°C, isozyme PTPalpha, mutant Q259G

substrate: Unknown


proof_lines: pH 5.5, 25°C, isozyme PTP1B, mutant G259Q


organism: Unknown

source_db: unknown

source_license: see source

source: unknown


enzyme_display_name: fructose-2,6-bisphosphate 2-phosphatase

organism: Blastocladiella emersonii

substrate_name: H2O; beta-D-Fructose 2,6-bisphosphate

enzyme: fructose-2,6-bisphosphate 2-phosphatase

substrate: H2O; beta-D-Fructose 2,6-bisphosphate


organism: Sulfolobus acidocaldarius


substrate_name: TEVGKRI(pY)RLVGDKN

substrate: TEVGKRI(pY)RLVGDKN


organism: Zea mays

substrate_name: fructose 2,6-bisphosphate

substrate: fructose 2,6-bisphosphate


proof_lines: for the catalytic subunit of ca. 35000 Da


substrate_name: WRKRFpYDWEF

proof_lines: pH 7.4, temperature not specified in the publication, SHP-2

proof_lines: pH 7.4, temperature not specified in the publication, SHP-1


organism: Thermococcus kodakarensis

proof_lines:
pH 5.0, 20°C, mutant D63N
pH 5.0, 60°C, mutant D63N


proof_lines:
pH 5.0, 20°C, mutant R124E
pH 5.0, 60°C, mutant R124E


proof_lines:
pH 5.0, 20°C, mutant D63A
pH 5.0, 60°C, mutant D63A


proof_lines:
pH 5.0, 20°C, mutant D63N/E132A
pH 5.0, 60°C, mutant D63N/E132A


proof_lines:
pH 5.0, 20°C, mutant Q136A
pH 5.0, 60°C, mutant Q136A


proof_lines:
pH 5.0, 20°C, mutant E132L
pH 5.0, 60°C, mutant E132L


proof_lines:
pH 5.0, 20°C, mutant R124A
pH 5.0, 60°C, mutant R124A


proof_lines:
pH 5.0, 20°C, mutant E132A
pH 5.0, 60°C, mutant E132A


proof_lines:
pH 5.0, 20°C, mutant G95A
pH 5.0, 60°C, mutant G95A


proof_lines:
pH 5.0, 20°C, wild-type enzyme
pH 5.0, 60°C, wild-type enzyme


proof_lines:
pH 5.0, 20°C, mutant E132Q
pH 5.0, 60°C, mutant E132Q


organism: Vigna radiata var. radiata

proof_lines:
in presence of 3-phosphoglycerate
in presence of phosphate


substrate_name: p-nitrophenyl phosphate

substrate: p-nitrophenyl phosphate


enzyme_display_name: Magnesium-dependent phosphatase 1

organism: Mus musculus

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

column_label: Table 5. Substrate Kinetics of Mouse MDP-1; row ribose-5-phosphate; column KM (mM)c

normalized_value_unit_evidence: km=9.5 mM

raw_value_unit_evidence: KM (mM)c: 9.5 mM

enzyme: Magnesium-dependent phosphatase 1


substrate_name: phosphotyrosine

column_label: Table 5. Substrate Kinetics of Mouse MDP-1; row phosphotyrosine; column KM (mM)c

normalized_value_unit_evidence: km=15 mM

raw_value_unit_evidence: KM (mM)c: 15 mM

row_label: phosphotyrosine

substrate: phosphotyrosine


smiles: C(C(C(C(COP(=O)(O)O)O)O)O)O

column_label: Table 5. Substrate Kinetics of Mouse MDP-1; row arabinose-5-phosphate; column KM (mM)c

normalized_value_unit_evidence: km=1.1 mM


smiles: C(C(C(C(C(=O)CO)O)O)O)OP(=O)(O)O

column_label: Table 5. Substrate Kinetics of Mouse MDP-1; row fructose-6-phosphate; column KM (mM)c

normalized_value_unit_evidence: km=21 mM


column_label: Table 5. Substrate Kinetics of Mouse MDP-1; row 5'-CMP; column KM (mM)c

normalized_value_unit_evidence: km=12 mM

raw_value_unit_evidence: KM (mM)c: 12.0 mM


substrate_name: pNPP

column_label: Table 5. Substrate Kinetics of Mouse MDP-1; row p-nitrophenyl phosphate (pNPP); column KM (mM)c

normalized_value_unit_evidence: km=1.7 mM

raw_value_unit_evidence: KM (mM)c: 1.7 mM

row_label: p-nitrophenyl phosphate (pNPP)

substrate: pNPP


column_label: Table 5. Substrate Kinetics of Mouse MDP-1; row 5'-AMP; column KM (mM)c

normalized_value_unit_evidence: km=26 mM

raw_value_unit_evidence: KM (mM)c: 26 mM


column_label: Table 5. Substrate Kinetics of Mouse MDP-1; row glucose-6-phosphate; column KM (mM)c

normalized_value_unit_evidence: km=31 mM

raw_value_unit_evidence: KM (mM)c: 31 mM


enzyme_display_name: Ecdysteroid-phosphate phosphatase

organism: Bombyx mori

substrate_name: ecdysone 22-phosphate (E22P)

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -1, so it is treated as a source-provided variant sequence.

proof_lines: kcat is 0.94 sec(-1) for E22P. kcat is 14.57 sec(-1) for 20E22P. kcat is 3.53 sec(-1) for 2dE22P. kcat is 0.14 sec(-1) for 22d20E3P.

enzyme: Ecdysteroid-phosphate phosphatase

substrate: ecdysone 22-phosphate (E22P)


substrate_name: 2-deoxyecdysone 22-phosphate (2dE22P)

substrate: 2-deoxyecdysone 22-phosphate (2dE22P)


organism: Pelophylax lessonae


enzyme_display_name: Glycerol-3-phosphate phosphatase

substrate_name: ADP

assay_conditions_summary: cofactor ADP

proof_lines: kcat is 0.1 sec(-1) with glycerol-3-phosphate.

enzyme: Glycerol-3-phosphate phosphatase

substrate: ADP


substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


substrate_name: GDP

substrate: GDP


substrate_name: GTP

substrate: GTP


organism: Shewanella sp.

substrate_name: 4-nitrophenyl phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V79A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6

proof_lines: mutant enzyme V79A, in 50 mM MES-NaOH (pH 6.0), 2.5 mM MgCl2, at 5°C

substrate: 4-nitrophenyl phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L145V with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L145V, in 50 mM MES-NaOH (pH 6.0), 2.5 mM MgCl2, at 5°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L145A with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L145A, in 50 mM MES-NaOH (pH 6.0), 2.5 mM MgCl2, at 5°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V85F with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V85F, in 50 mM MES-NaOH (pH 6.0), 2.5 mM MgCl2, at 5°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V79L with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V79L, in 50 mM MES-NaOH (pH 6.0), 2.5 mM MgCl2, at 5°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V85M with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V85M, in 50 mM MES-NaOH (pH 6.0), 2.5 mM MgCl2, at 5°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V79I with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V79I, in 50 mM MES-NaOH (pH 6.0), 2.5 mM MgCl2, at 5°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L145F with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L145F, in 50 mM MES-NaOH (pH 6.0), 2.5 mM MgCl2, at 5°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V85L with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V85L, in 50 mM MES-NaOH (pH 6.0), 2.5 mM MgCl2, at 5°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L145M with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L145M, in 50 mM MES-NaOH (pH 6.0), 2.5 mM MgCl2, at 5°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I115L with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I115L, in 50 mM MES-NaOH (pH 6.0), 2.5 mM MgCl2, at 5°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I115V with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I115V, in 50 mM MES-NaOH (pH 6.0), 2.5 mM MgCl2, at 5°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I115M with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I115M, in 50 mM MES-NaOH (pH 6.0), 2.5 mM MgCl2, at 5°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I115F with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I115F, in 50 mM MES-NaOH (pH 6.0), 2.5 mM MgCl2, at 5°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature P181C/P186C with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E187C with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature P186C with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E187C/S188C with inferred residue-numbering offset -29 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature P181C with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D236A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D236A, at 30°C, in 0.15 M Bis-Tris, pH 6.0


sequence_variant_note: Mutation signature Q314A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme Q314A, at 30°C, in 0.15 M Bis-Tris, pH 6.0


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

smiles: C(C(COP(=O)(O)O)O)O

proof_lines: Given the respective intracellular concentrations of glycerol-3-phosphate and 2-phosphoglycolate, glycerol-3-phosphate with a concentration of 2 to 10 mM is most probably the physiological substrate.


enzyme_display_name: Low molecular weight protein-tyrosine phosphatase A

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: pNPP (at pH 5.0)

proof_lines: kcat is 12.6 sec(-1) with pNPP as substrate at pH 5.0. kcat is 1313 sec(-1) with pNPP as substrate at pH 6.0. kcat is 1334 sec(-1) with pNPP as substrate at pH 7.0 (PubMed:17975835). kcat is 13.73 sec(-1) with pNPP as substrate. kcat is 6.7

substrate: pNPP (at pH 5.0)


enzyme_display_name: UniProt Q9X0Y1

organism: Thermotoga maritima

substrate_name: fructose 6-phosphate

enzyme: UniProt Q9X0Y1

substrate: fructose 6-phosphate


substrate_name: erythrose 4-phosphate

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

substrate: erythrose 4-phosphate


enzyme_display_name: phosphoenolpyruvate phosphatase

organism: Allium cepa

substrate_name: phosphoenolpyruvate

enzyme: phosphoenolpyruvate phosphatase

substrate: phosphoenolpyruvate


substrate_name: phytic acid

substrate: phytic acid


substrate_name: D-glucose 6-phosphate

substrate: D-glucose 6-phosphate


enzyme_display_name: Phosphoenolpyruvate phosphatase

enzyme: Phosphoenolpyruvate phosphatase


substrate_name: glucose 6-phosphate

substrate: glucose 6-phosphate


organism: Phaseolus vulgaris

substrate_name: 2-carboxyarabinitol 1-phosphate

substrate: 2-carboxyarabinitol 1-phosphate


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S295F with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


substrate_name: 3,6-fluorescein diphosphate

substrate: 3,6-fluorescein diphosphate


proof_lines: kcat is 0.1 sec(-1) with glycerol-3-phosphate.


substrate_name: p-nitrophenyl phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D445A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

substrate: p-nitrophenyl phosphate


enzyme_display_name: alkylacetylglycerophosphatase

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

smiles: CC(=O)OC(CO)COP(=O)(O)O

enzyme: alkylacetylglycerophosphatase


organism: Vigna radiata


substrate_name: Unknown

proof_lines:
competitive towards Mg2+, 30°C, pH 8.5
competitive, 30°C, pH 8.5

substrate: Unknown


assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP


organism: Brassica nigra


substrate_name: D-glucose 1-phosphate

substrate: D-glucose 1-phosphate


assay_conditions_summary: pH 5.6; 298.15 K; cofactor ATP


substrate_name: 2,3 diphosphoglycerate

substrate: 2,3 diphosphoglycerate


substrate_name: D-gluconate 6-phosphate

substrate: D-gluconate 6-phosphate


substrate_name: ADP

assay_conditions_summary: pH 5.6; 298.15 K; cofactor ADP

substrate: ADP


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


organism: Brassica rapa subsp. oleifera


organism: Tetrahymena pyriformis

proof_lines: pH 7.0, 37°C, mitochondrial and microsomal fractions


enzyme_display_name: sugar-terminal-phosphatase

enzyme: sugar-terminal-phosphatase


enzyme_display_name: Triple specificity protein phosphatase PtpB

substrate_name: P-Ser

column_label: Official PMC article HTML Table 1, row P-Ser, Km column reports 0.44 mM with reported SEM 0.08. Local HTML line refs: PMC1948985_pmc_article.html lines 1449-1473.

normalized_value_unit_evidence: Paper Table 1 P-Ser Km mean is 0.44 mM, matching the export Km 0.44 mM.

raw_value_unit_evidence: Table 1 row P-Ser reports Km 0.44 +/- 0.08 mM.

row_label: P-Ser

table_label: Table 1. Kinetic parameters of MptpB towards different phosphorylated substrates

substrate: P-Ser


substrate_name: pNPP

proof_lines: kcat is 60.0 sec(-1) with P-Tyr as substrate. kcat is 18.32 sec(-1) with P-Ser as substrate. kcat is 12.5 sec(-1) with P-Thr as substrate. kcat is 159.57 sec(-1) with P-Tyr insulin as substrate. kcat is 158.31 sec(-1) with P-Tyr EGFR as sub

enzyme: Triple specificity protein phosphatase PtpB

substrate: pNPP


substrate_name: phosphotyrosine

enzyme: Low molecular weight protein-tyrosine phosphatase A

substrate: phosphotyrosine


enzyme_display_name: Phosphatase/phosphodiesterase DR_1281

organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

substrate_name: PEP (at pH 6.5)

column_label: Table III row PEP under columns pH 6.5 and Km (mM): 0.36 +/- 0.07.

row_label: PEP

table_label: Table III

enzyme: Phosphatase/phosphodiesterase DR_1281

substrate: PEP (at pH 6.5)


column_label: Table III row 2',3'-cAMP under columns pH 6.5 and Km (mM): 0.55 +/- 0.05.


column_label: Table III row 2',3'-cCMP under columns pH 6.5 and Km (mM): 0.87 +/- 0.11.


column_label: Table III row 2',3'-cGMP under columns pH 6.5 and Km (mM): 1.28 +/- 0.12.


substrate_name: pNPP (at pH 8.5)

column_label: Table III row pNPP under columns pH 8.5 and Km (mM): 0.08 +/- 0.006.

row_label: pNPP

substrate: pNPP (at pH 8.5)


substrate_name: pNP-TMP (at pH 8.5)

proof_lines: kcat is 0.18 sec(-1) with PEP as substrate. kcat is 0.38 sec(-1) with 2',3'-cAMP as substrate. kcat is 0.32 sec(-1) with 2',3'-cCMP as substrate. kcat is 0.42 sec(-1) with 2',3'-cGMP as substrate. kcat is 0.20 sec(-1) with pNPP as substrate

substrate: pNP-TMP (at pH 8.5)


enzyme_display_name: Dual specificity protein phosphatase TpbA

organism: Pseudomonas aeruginosa (strain UCBPP-PA14)

proof_lines: kcat is 0.00162 sec(-1) with pNPP as substrate.


substrate_name: 4-nitrophenyl phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H44N with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

substrate: 4-nitrophenyl phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T36E with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L29A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S35E with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F28A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C129S with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.