enzyme_display_name: Name not preserved

organism: Thermus thermophilus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ADP

proof_lines:
pH 7.5, 25°C
pH 9.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7.5

enzyme: Name not preserved


substrate_name: FAD

source_db: brenda

verification_status: unverified

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

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

km_unit: mM

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

assay_conditions_summary: pH 9; 298.15 K; cofactor FAD

data_origin: experimental

source_databases_merged: brenda skid

substrate: FAD

status: unverified

source: brenda


assay_conditions_summary: pH 7.5; 298.15 K; cofactor FAD


source_db: skid

source: skid


enzyme_display_name: S-adenosylhomocysteine deaminase

organism: Thermotoga maritima

substrate_name: S-Adenosyl-L-homocysteine

source_db: oed

verification_status: corrected

protein_accession_database: UniProt

source_license: CC BY 4.0

column_label: Table 2 row S-adenosyl-L-homocysteine gives Km 210 +/- 40 uM, kcat 12.2 +/- 0.8 s^-1, and kcat/Km 5.8 x 10^4 M^-1 s^-1; Figure S3 confirms the same SAH kinetic plot at pH 8.0 and 30 C.

row_label: S-adenosyl-L-homocysteine

table_label: Table 2: Docking ranks and Tm0936 catalytic constants for five predicted substrates

enzyme: S-adenosylhomocysteine deaminase

substrate: S-Adenosyl-L-homocysteine

status: corrected

source: oed


enzyme_display_name: UniProt A6G7B1

organism: Plesiocystis pacifica

source_license: CC BY-NC-ND 4.0

smiles: C(CBr)Br

enzyme: UniProt A6G7B1


smiles: CCCCCCBr


smiles: CCCBr


smiles: CC(CBr)Br


smiles: CCCCCCCBr


smiles: CCCCBr


smiles: CCCCCBr


enzyme_display_name: UniProt Q6DND9

organism: Lyngbya majuscula

smiles: CCCCCl

enzyme: UniProt Q6DND9


smiles: CCCCI


smiles: C(CC#N)CBr


smiles: CCCI


enzyme_display_name: UniProt Q9A919

organism: Caulobacter vibrioides

smiles: CCCCCCCl

enzyme: UniProt Q9A919


smiles: C(CCCl)CCCl


smiles: C(CBr)CBr


enzyme_display_name: atrazine chlorohydrolase

organism: Arthrobacter sp.

substrate_name: Atrazine

kcat_display: Not reported

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

enzyme: atrazine chlorohydrolase

substrate: Atrazine


enzyme_display_name: dCTP deaminase, dUMP-forming

organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

substrate_name: dUTP (at 60 degrees Celsius)

source_db: uniprot

verification_status: verified

column_label: PMID 12538648 dUTP diphosphatase kinetic evidence, dUTP row/segment, Km = 263 +/- 64 uM at 60 deg C.

raw_value_unit_evidence: The paper reports dUTP diphosphatase Km = 263 +/- 64 uM.

row_label: dUTP diphosphatase reaction

table_label: Table III and dUTP diphosphatase kinetic prose for MjDCD-DUT

enzyme: dCTP deaminase, dUMP-forming

substrate: dUTP (at 60 degrees Celsius)

status: verified

source: uniprot


organism: Methanocaldococcus jannaschii

substrate_name: dCTP

sequence_source: multiple

source_databases_merged: brenda uniprot

substrate: dCTP


enzyme_display_name: GTP cyclohydrolase-2

organism: Escherichia coli

substrate_name: GTP

enzyme: GTP cyclohydrolase-2

substrate: GTP


organism: Haematococcus lacustris

km_display: Not reported

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


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


proof_lines: more than 0.153 mM. AtzA wild type, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216S/T217A/T219P/A220F/D250G, site-directed mutagenesis, AtzA-variant 357, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216A/T217D/T219E/A220A/D250D, site-directed mutagenesis, AtzA-variant 288, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216G/T217D/T219A/A220V/D250W, site-directed mutagenesis, AtzA-variant 305, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216Y/T217D/T219Y/A220H/D250V, site-directed mutagenesis, AtzA-variant 422, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216S/T217D/T219V/A220H/D250G, site-directed mutagenesis, AtzA-variant 297, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216H/T217A/T219E/A220S/D250S, site-directed mutagenesis, AtzA-variant 662, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216A/T217S/T219H/A220G/D250Y, site-directed mutagenesis, AtzA-variant 431, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216S/T217D/T219G/A220S/D250D, site-directed mutagenesis, AtzA-variant 841, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216G/T217D/T219G/A220H/D250G, site-directed mutagenesis, AtzA-variant 430, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216G/T217D/T219G/A220H/D250D, site-directed mutagenesis, AtzA-variant 734, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216Y/T217D/T219T/A220H/D250E, site-directed mutagenesis, AtzA best variant consensus, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: AtzA wild-type, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216S/T217A/T219P/A220F/D250G, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: T217D/T219E, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216G/T217D/T219A/A220V/D250W, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216Y/T217D/T219Y/A220H/D250V, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216S/T217D/T219V/A220H/D250G, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216H/T217A/T219E/A220S/D250S, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: T217S/T219H/A220G/D250Y, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216S/T217D/T219G/A220S, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216G/T217D/T219G/A220H/D250G, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216G/T217D/T219G/A220H/D250D, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216Y/T217D/A220H/D250E, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


enzyme_display_name: haloalkane dehalogenase

enzyme: haloalkane dehalogenase


organism: Dyella ginsengisoli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148N to reconstruct the assayed variant sequence.

mutation_type: substitution


kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148Y to reconstruct the assayed variant sequence.


organism: Paenarthrobacter aurescens

proof_lines: mutant R325S, pH and temperature not specified in the publication


proof_lines: mutant E241Q, pH and temperature not specified in the publication


substrate_name: ametryn

substrate: ametryn


assay_conditions_summary: pH 7

proof_lines: wild-type enzyme, pH 7.0, temperature not specified in the publication


proof_lines: mutant R325, pH and temperature not specified in the publicationS


organism: Alloalcanivorax dieselolei

assay_conditions_summary: pH 8.6; buffer pH 8

column_label: Table 2 row 1-Chlorobutane / HLD DadB; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1).

table_label: Table 2


column_label: Table 2 row 1,3-Dibromopropane / HLD DadB; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1).


column_label: Table 2 row 1,2-Dibromoethane / HLD DadB; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1).


smiles: C=C(CCl)Cl

column_label: Table 2 row 2,3-Dichloroprop-1-ene / HLD DadB; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1).


column_label: Table 2 row 4-bromobutanenitrile (synonym: 4-bromobutyronitrile) / HLD DadB; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1).


smiles: CC(=C)CCl

column_label: Table 2 row 3-chloro-2-methylprop-1-ene / HLD DadB; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1).


enzyme_display_name: (R)-2-haloacid dehalogenase

organism: Agrobacterium sp.

enzyme: (R)-2-haloacid dehalogenase


enzyme_display_name: S-methyl-5'-thioadenosine deaminase

column_label: Table 2 row 5-Methyl-thioadenosine gives Km 44 +/- 4 uM, kcat 7.2 +/- 0.2 s^-1, and kcat/Km 1.4 x 10^5 M^-1 s^-1; Figure S3 confirms the same MTA kinetic plot at pH 8.0 and 30 C.

enzyme: S-methyl-5'-thioadenosine deaminase


enzyme_display_name: 4-chlorobenzoate dehalogenase

enzyme: 4-chlorobenzoate dehalogenase


organism: Strongylocentrotus purpuratus

proof_lines: pH 8.6, 37°C, recombinant His-tagged enzyme


enzyme_display_name: 4-chlorobenzoyl-CoA dehalogenase

organism: Pseudomonas sp.

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5JTM5 and applied mutation signature G114A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM K+Hepes; cofactor CoA

column_label: Table 3, enzyme row 'G114A'; under the group head '4-CBA-CoA', column 'kcat (s-1)' = 0.002 and column 'Km (uM)' = 110. The remaining columns of the same row stand under the group heads '4-MeBA-CoA' and '4-HBA-CoA' and hold Ki or Kd ligand constants. Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.002 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.002 s^(-1). Km: printed Table 3 cell 110 uM; 110 / 1000 = 0.11 mM; the paper value is 0.11 mM. kcat/Km: neither Table 1 nor Table 3 carries a kcat/Km column, so the paper value 0.01818181818181818 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.002 / 0.11 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'G114A': kcat = 0.002 s-1; Km = 110 uM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row G114A

table_label: Table 3: Kinetic Constants (kcat and Km) for Wild-Type and Mutant 4-CBA-CoA Dehalogenase Catalysis and Dissociation Constants (Kd) and/or Inhibition Constants (Ki) for 4-MeBA-CoA, 4-HBA-CoA, and CoA with Wild-Type and Mutant 4-CBA-CoA Dehalogenase (Measured at pH 7.5 and 25 °C in 50 mM K+Hepes Buffer) (Biochemistry 2001, 40(51):15684-15692)

enzyme: 4-chlorobenzoyl-CoA dehalogenase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G113A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5JTM5 and applied mutation signature F64A to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme row 'F64A'; under the group head '4-CBA-CoA', column 'kcat (s-1)' = 0.03 and column 'Km (uM)' = 5.2. The remaining columns of the same row stand under the group heads '4-MeBA-CoA' and '4-HBA-CoA' and hold Ki or Kd ligand constants. Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.03 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.03 s^(-1). Km: printed Table 3 cell 5.2 uM; 5.2 / 1000 = 0.0052 mM; the paper value is 0.0052 mM. kcat/Km: neither Table 1 nor Table 3 carries a kcat/Km column, so the paper value 5.769230769230769 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.03 / 0.0052 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'F64A': kcat = 0.03 s-1; Km = 5.2 uM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row F64A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5JTM5 and applied mutation signature R257L to reconstruct the assayed variant sequence.

column_label: Table 1, enzyme row 'R257L'; under the group head '4-CBA-CoA', column 'kcat (s-1)' = 0.14 and column 'Km (uM)' = 70. The remaining columns of the same row stand under the group heads '4-MeBA-CoA' and '4-HBA-CoA' and hold Ki or Kd ligand constants. Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.14 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.14 s^(-1). Km: printed Table 1 cell 70 uM; 70 / 1000 = 0.07 mM; the paper value is 0.07 mM. kcat/Km: neither Table 1 nor Table 3 carries a kcat/Km column, so the paper value 2.0 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.14 / 0.07 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, enzyme row 'R257L': kcat = 0.14 s-1; Km = 70 uM; Table 1 prints no kcat/Km cell for this row.

row_label: Table 1, enzyme row R257L

table_label: Table 1: Kinetic Constants (kcat and Km) for Wild-Type and Mutant 4-CBA-CoA Dehalogenase Catalysis and Dissociation Constants (Kd) and/or Inhibition Constants (Ki) for 4-MeBA-CoA, 4-HBA-CoA, and CoA with Wild-Type and Mutant 4-CBA-CoA Dehalogenase (Measured at pH 7.5 and 25 °C in 50 mM K+Hepes Buffer) (Biochemistry 2001, 40(51):15684-15692)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5JTM5 and applied mutation signature R24L to reconstruct the assayed variant sequence.

column_label: Table 1, enzyme row 'R24L'; under the group head '4-CBA-CoA', column 'kcat (s-1)' = 0.33 and column 'Km (uM)' = 41. The remaining columns of the same row stand under the group heads '4-MeBA-CoA' and '4-HBA-CoA' and hold Ki or Kd ligand constants. Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.33 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.33 s^(-1). Km: printed Table 1 cell 41 uM; 41 / 1000 = 0.041 mM; the paper value is 0.041 mM. kcat/Km: neither Table 1 nor Table 3 carries a kcat/Km column, so the paper value 8.048780487804878 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.33 / 0.041 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, enzyme row 'R24L': kcat = 0.33 s-1; Km = 41 uM; Table 1 prints no kcat/Km cell for this row.

row_label: Table 1, enzyme row R24L


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5JTM5 and applied mutation signature R67K to reconstruct the assayed variant sequence.

column_label: Table 1, enzyme row 'R67K'; under the group head '4-CBA-CoA', column 'kcat (s-1)' = 0.38 and column 'Km (uM)' = 6.9. The remaining columns of the same row stand under the group heads '4-MeBA-CoA' and '4-HBA-CoA' and hold Ki or Kd ligand constants. Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.38 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.38 s^(-1). Km: printed Table 1 cell 6.9 uM; 6.9 / 1000 = 0.0069 mM; the paper value is 0.0069 mM. kcat/Km: neither Table 1 nor Table 3 carries a kcat/Km column, so the paper value 55.072463768115945 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.38 / 0.0069 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, enzyme row 'R67K': kcat = 0.38 s-1; Km = 6.9 uM; Table 1 prints no kcat/Km cell for this row.

row_label: Table 1, enzyme row R67K


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5JTM5 and applied mutation signature R257K to reconstruct the assayed variant sequence.

column_label: Table 1, enzyme row 'R257K'; under the group head '4-CBA-CoA', column 'kcat (s-1)' = 0.55 and column 'Km (uM)' = 5.8. The remaining columns of the same row stand under the group heads '4-MeBA-CoA' and '4-HBA-CoA' and hold Ki or Kd ligand constants. Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.55 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.55 s^(-1). Km: printed Table 1 cell 5.8 uM; 5.8 / 1000 = 0.0058 mM; the paper value is 0.0058 mM. kcat/Km: neither Table 1 nor Table 3 carries a kcat/Km column, so the paper value 94.82758620689657 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.55 / 0.0058 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, enzyme row 'R257K': kcat = 0.55 s-1; Km = 5.8 uM; Table 1 prints no kcat/Km cell for this row.

row_label: Table 1, enzyme row R257K


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

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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5JTM5 and applied mutation signature R24K to reconstruct the assayed variant sequence.

column_label: Table 1, enzyme row 'R24K'; under the group head '4-CBA-CoA', column 'kcat (s-1)' = 0.95 and column 'Km (uM)' = 21. The remaining columns of the same row stand under the group heads '4-MeBA-CoA' and '4-HBA-CoA' and hold Ki or Kd ligand constants. Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.95 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.95 s^(-1). Km: printed Table 1 cell 21 uM; 21 / 1000 = 0.021 mM; the paper value is 0.021 mM. kcat/Km: neither Table 1 nor Table 3 carries a kcat/Km column, so the paper value 45.238095238095234 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.95 / 0.021 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, enzyme row 'R24K': kcat = 0.95 s-1; Km = 21 uM; Table 1 prints no kcat/Km cell for this row.

row_label: Table 1, enzyme row R24K


enzyme_display_name: Haloalkane dehalogenase

organism: Sphingobium indicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S)

proof_lines: kcat is 0.98 sec(-1) with 1-chlorobutane as substrate.

enzyme: Haloalkane dehalogenase


smiles: C(CBr)Cl


smiles: CC(C)CBr


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G113S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A112V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y65D to reconstruct the assayed variant sequence.


organism: Agrobacterium tumefaciens

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

smiles: C(CCl)CCl


column_label: PMC HTML Table 1 and Europe PMC PDF text lines 110-123 report row 1-Chlorohexane columns K0.5 (mM), kcat (s^-1), and kcat/K0.5 (s^-1 mM^-1).

normalized_value_unit_evidence: kcat=0.039 s^-1; Km-like K0.5=0.07 mM; kcat_over_km table value=0.58 s^-1 mM^-1, consistent with expected 0.557142857142857 from rounded K0.5/kcat cells.

table_label: Table 1. Kinetic characteristics of DatA with six halogenated substrates


smiles: CCCCCCI

column_label: PMC HTML Table 1 and Europe PMC PDF text lines 110-123 report row 1-Iodohexane columns K0.5 (mM), kcat (s^-1), and kcat/K0.5 (s^-1 mM^-1).

normalized_value_unit_evidence: kcat=0.26 s^-1; Km-like K0.5=0.63 mM; kcat_over_km table value=0.42 s^-1 mM^-1, consistent with expected 0.41269841269841273 from rounded K0.5/kcat cells.


smiles: C(CI)CI

column_label: PMC HTML Table 1 and Europe PMC PDF text lines 110-123 report row 1,3-Diiodopropane columns K0.5 (mM), kcat (s^-1), and kcat/K0.5 (s^-1 mM^-1).


column_label: PMC HTML Table 1 and Europe PMC PDF text lines 110-123 report row 1,3-Dibromopropane columns K0.5 (mM), kcat (s^-1), and kcat/K0.5 (s^-1 mM^-1).

normalized_value_unit_evidence: kcat=1.47 s^-1; Km-like K0.5=2.15 mM; kcat_over_km table value=0.69 s^-1 mM^-1, consistent with expected 0.6837209302325582 from rounded K0.5/kcat cells.


smiles: CCCCCCBr

column_label: PMC HTML Table 1 and Europe PMC PDF text lines 110-123 report row 1-Bromohexane columns K0.5 (mM), kcat (s^-1), and kcat/K0.5 (s^-1 mM^-1).

normalized_value_unit_evidence: kcat=1.7 s^-1; Km-like K0.5=0.14 mM; kcat_over_km table value=12.20 s^-1 mM^-1, consistent with expected 12.14285714285714 from rounded K0.5/kcat cells.


organism: Ancylobacter aquaticus

smiles: C(CCl)Cl

assay_conditions_summary: pH 9

proof_lines: GJ10, calculated from rate constants for four-steps reaction mechanism


organism: Xanthobacter autotrophicus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature F172W to reconstruct the assayed variant sequence.

proof_lines: GJ10, F172W mutant, calculated from rate constants for four-steps reaction mechanism


smiles: C(CBr)Br


organism: Mycolicibacterium rhodesiae


organism: Rhodococcus rhodochrous

smiles: C(CBr)O


smiles: CCCCCl


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature W175Y to reconstruct the assayed variant sequence.

column_label: PMID 9790663 DOI 10.1021/bi9815187 Table 3; substrate block 1,2-dibromoethane; row Trp175Tyr; columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

raw_value_unit_evidence: Table 3 row 1,2-dibromoethane Trp175Tyr: Km 0.06 mM; kcat 5.0 s^-1; kcat/Km 85 mM^-1 s^-1.

row_label: 1,2-dibromoethane / Trp175Tyr

table_label: Table 3. Halide-Binding and Steady-State Activity Parameters of Purified Wild-Type and Trp175Tyr Haloalkane Dehalogenase for DBE and DCE at pH 8.2 and 30 C


column_label: PMID 9790663 DOI 10.1021/bi9815187 Table 3; substrate block 1,2-dichloroethane; row Trp175Tyr; columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

raw_value_unit_evidence: Table 3 row 1,2-dichloroethane Trp175Tyr: Km 2.85 mM; kcat 0.33 s^-1; kcat/Km 0.1 mM^-1 s^-1.

row_label: 1,2-dichloroethane / Trp175Tyr


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y109W to reconstruct the assayed variant sequence.

proof_lines: below, recombinant mutant Y109W, pH 8.6, 37°C


smiles: CCCCBr


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H90Q to reconstruct the assayed variant sequence.

proof_lines: multiple turnovers, mutant H90Q, pH 7.5, 25°C

proof_lines: single turnover, mutant H90Q, pH 7.5, 25°C


organism: Yarrowia lipolytica

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

smiles: CCCCCCCCCCBr


smiles: CCCCCCCCCCCCBr


smiles: CCCBr


substrate_name: bis(2-chloroethyl) ether

smiles: C(CCl)OCCCl

proof_lines: 37°C, pH 8.2, enzyme multi-PEGylated with the thiosuccinimido butylamine linker

proof_lines: 37°C, pH 8.2, enzyme mono-PEGylated with the thiosuccinimido butylamine linker

proof_lines: inulin-conjugated enzyme, at pH 7.4 and 37°C

substrate: bis(2-chloroethyl) ether


organism: uncultured marine bacterium

smiles: C(CBr)CBr

proof_lines: pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E232G to reconstruct the assayed variant sequence.


organism: Pseudomonas putida

substrate_name: Monochloroacetate

proof_lines: pH 7.5, D-2-haloacid dehalogenase subtype

substrate: Monochloroacetate


substrate_name: 1-Chloropropane; H2O

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

substrate: 1-Chloropropane; H2O


assay_conditions_summary: pH 8

proof_lines: enzyme in 40% (v/v) DSMO, in the absence of poly(allylamine hydrochloride), at pH 8.0 and 30°C

proof_lines: enzyme in 40% (v/v) DSMO, poly(allylamine hydrochloride):enzyme ratio of 4:1, at pH 8.0 and 30°C

proof_lines: enzyme in 40% (v/v) DSMO, poly(allylamine hydrochloride):enzyme ratio of 8:1, at pH 8.0 and 30°C


organism: Sphingobium sp.

substrate_name: beta-hexachlorocyclohexane

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature I253M to reconstruct the assayed variant sequence.

substrate: beta-hexachlorocyclohexane


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature V134I/H247A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 30°C, recombinant mutant V134I/H247A


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature H247A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature T81A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H247A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V134I/H247A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T81A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I253M to reconstruct the assayed variant sequence.


organism: Sphingomonas paucimobilis

substrate_name: H2O; 1-Chlorobutane

substrate: H2O; 1-Chlorobutane


substrate_name: Unknown

ki_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R24K with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

substrate: Unknown


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

assay_conditions_summary: pH 7.2; 298.15 K; cofactor ADP

proof_lines: kcat is 11 sec(-1) with atrazine as substrate.

source_databases_merged: brenda skid uniprot


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

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


assay_conditions_summary: cofactor CoA

proof_lines:
multiple turnovers
single turnover


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R257L with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R67K with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R24L with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G114A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines: wild-type enzyme, pH 7.5, 25°C, in presence of 1 mM 5'-ADP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G113A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R257K with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F64P with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

proof_lines:
mutant F64P, pH 7.5, 25°C
below, mutant F64P, pH 7.5, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G113N to reconstruct the assayed variant sequence.


substrate_name: H2O; 4-Chlorobenzoyl-CoA

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

source_databases_merged: sabio_rk brenda uniprot

substrate: H2O; 4-Chlorobenzoyl-CoA


assay_conditions_summary: cofactor ADP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L288A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N203A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V51F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L288I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L288V to reconstruct the assayed variant sequence.


column_label: Primary measurement evidence: evidence location type: table note; evidence location label: article page 1108 unnumbered kinetic-parameter table; measurement identity label: wild-type AtzA-AD1; atrazine; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 100 mM Tris-HCl pH 7.2; atrazine 4.6-140 uM; 25 C; 10 min; HPLC; captured primary segment: wild-type AtzA-AD1 values were Km 146 +/- 10 uM, kcat 1.6 +/- 0.1 s^-1, and kcat/Km 1.1x10^4 +/- 0.1x10^4 s^-1 M^-1.

normalized_value_unit_evidence: Km 0.146 mM; kcat 1.6 s^-1; exact quotient of the printed point values 1.6/0.146 = 10.958904109589042 s^-1 mM^-1; the table independently prints the rounded efficiency 11 +/- 1 s^-1 mM^-1.

raw_value_unit_evidence: Page 1108 table note reports wild-type AtzA-AD1 Km 146 +/- 10 uM, kcat 1.6 +/- 0.1 s^-1, and kcat/Km 1.1x10^4 +/- 0.1x10^4 s^-1 M^-1.

row_label: Wild-type AtzA-AD1 values in table note

table_label: Page 1108 unnumbered table: Mutation sites, specific activity, and kinetic parameters of the variants relative to wild type


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

column_label: Table 1; row 18; compound 2-bromoacetamide; column log Km (mM); cell 1.30

raw_value_unit_evidence: Table 1 row 18 / 2-bromoacetamide: log Km (mM)=1.30

row_label: 18 / 2-bromoacetamide


substrate_name: epichlorohydrin

column_label: Table 1; row 13; compound epichlorohydrine; column log Km (mM); cell 1.68

raw_value_unit_evidence: Table 1 row 13 / epichlorohydrine: log Km (mM)=1.68

row_label: 13 / epichlorohydrine

substrate: epichlorohydrin


substrate_name: Dichloromethane

smiles: C(Cl)Cl

column_label: Table 1; row 5; compound dichloromethane; column log Km (mM); cell 2.00

raw_value_unit_evidence: Table 1 row 5 / dichloromethane: log Km (mM)=2.00

row_label: 5 / dichloromethane

substrate: Dichloromethane


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

column_label: Table 1; row 17; compound 2-chloroacetamide; column log Km (mM); cell 2.00

raw_value_unit_evidence: Table 1 row 17 / 2-chloroacetamide: log Km (mM)=2.00

row_label: 17 / 2-chloroacetamide


smiles: C(CCl)O

column_label: Table 1; row 11; compound 2-chloroethanol; column log Km (mM); cell 2.60

raw_value_unit_evidence: Table 1 row 11 / 2-chloroethanol: log Km (mM)=2.60

row_label: 11 / 2-chloroethanol


column_label: Table 1; row 3; compound 1-bromobutane; column log Km (mM); cell -1.22

raw_value_unit_evidence: Table 1 row 3 / 1-bromobutane: log Km (mM)=-1.22

row_label: 3 / 1-bromobutane


column_label: Table 1; row 4; compound 1-bromohexane; column log Km (mM); cell -0.52

raw_value_unit_evidence: Table 1 row 4 / 1-bromohexane: log Km (mM)=-0.52

row_label: 4 / 1-bromohexane


smiles: C(C#N)Br

column_label: Table 1; row 16; compound 2-bromoacetonitrile; column log Km (mM); cell -0.31

raw_value_unit_evidence: Table 1 row 16 / 2-bromoacetonitrile: log Km (mM)=-0.31

row_label: 16 / 2-bromoacetonitrile


smiles: CC(CBr)Br

column_label: Table 1; row 10; compound 1,2-dibromopropane; column log Km (mM); cell 0.11

raw_value_unit_evidence: Table 1 row 10 / 1,2-dibromopropane: log Km (mM)=0.11

row_label: 10 / 1,2-dibromopropane


smiles: CCCCCCCl

column_label: Table 1; row 2; compound 1-chlorohexane; column log Km (mM); cell 0.15

raw_value_unit_evidence: Table 1 row 2 / 1-chlorohexane: log Km (mM)=0.15

row_label: 2 / 1-chlorohexane


substrate_name: epibromohydrine

column_label: Table 1; row 14; compound epibromohydrine; column log Km (mM); cell 0.34

raw_value_unit_evidence: Table 1 row 14 / epibromohydrine: log Km (mM)=0.34

row_label: 14 / epibromohydrine

substrate: epibromohydrine


substrate_name: Dibromomethane

smiles: C(Br)Br

column_label: Table 1; row 7; compound dibromomethane; column log Km (mM); cell 0.38

raw_value_unit_evidence: Table 1 row 7 / dibromomethane: log Km (mM)=0.38

row_label: 7 / dibromomethane

substrate: Dibromomethane


smiles: C(C#N)Cl

column_label: Table 1; row 15; compound 2-chloroacetonitrile; column log Km (mM); cell 0.80

raw_value_unit_evidence: Table 1 row 15 / 2-chloroacetonitrile: log Km (mM)=0.80

row_label: 15 / 2-chloroacetonitrile


smiles: C(CBr)O

column_label: Table 1; row 12; compound 2-bromoethanol; column log Km (mM); cell 1.04

raw_value_unit_evidence: Table 1 row 12 / 2-bromoethanol: log Km (mM)=1.04

row_label: 12 / 2-bromoethanol


smiles: CC(CCl)Cl

column_label: Table 1; row 9; compound 1,2-dichloropropane; column log Km (mM); cell 1.11

raw_value_unit_evidence: Table 1 row 9 / 1,2-dichloropropane: log Km (mM)=1.11

row_label: 9 / 1,2-dichloropropane


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L288I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L288A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L288V to reconstruct the assayed variant sequence.


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

proof_lines:
Pseudomonas sp. CBS-3
4-chlorobenzoyl-CoA dehalogenase


proof_lines:
4-iodobenzoyl-CoA
1.1 s-1
Pseudomonas sp. CBS-3


proof_lines:
4-bromobenzoyl-CoA
1.4 s-1
Pseudomonas sp. CBS-3


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

substrate_name: S-adenosyl-L-homocysteine

column_label: Table 2 row S-adenosyl-L-homocysteine, column Km (uM), gives 210 +/- 40 uM; Figure S3 repeats Km=(0.21 +/- 0.04) mM for SAH.

raw_value_unit_evidence: Km raw=210 +/- 40 uM; Table 2 also gives kcat 12.2 +/- 0.8 s^-1 and kcat/Km 5.8 x 10^4 M^-1 s^-1 for the same row.

row_label: S-adenosyl-L-homocysteine

substrate: S-adenosyl-L-homocysteine


smiles: C(C(CCl)Cl)Cl

column_label: Table 1; row 1,2,3-trichloropropane; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized Table 1 values: Km=2.2 mM; kcat=0.08 s^-1; printed kcat/Km=0.036 s^-1 mM^-1; exported kcat/Km=0.03636363636363636 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 1,2,3-trichloropropane; columns: kcat=0.08 s^-1; Km=2.2 mM; kcat/Km=36 M^-1 s^-1.

table_label: Table 1


smiles: CCCCl

column_label: Table 1 row 1-chloropropane, columns kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table row 1-chloropropane reports kcat 0.48 s^-1, Km 1.0 mM, kcat/Km 480 M^-1 s^-1.

table_label: Table 1. Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 C, PMID 12834356


smiles: C(CCl)CCl

column_label: Table 1; row 1,3-dichloropropane; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized Table 1 values: Km=0.63 mM; kcat=1.3 s^-1; printed kcat/Km=2.0 s^-1 mM^-1; exported kcat/Km=2.0634920634920637 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 1,3-dichloropropane; columns: kcat=1.3 s^-1; Km=0.63 mM; kcat/Km=2000 M^-1 s^-1.


column_label: Table 1; row 1,2-dibromopropane; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized Table 1 values: Km=1.0 mM; kcat=2.3 s^-1; printed kcat/Km=2.3 s^-1 mM^-1; exported kcat/Km=2.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 1,2-dibromopropane; columns: kcat=2.3 s^-1; Km=1.0 mM; kcat/Km=2300 M^-1 s^-1.


column_label: Table 1 row 1,3-dibromopropane, columns kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table row 1,3-dibromopropane reports kcat 2.7 s^-1, Km 0.005 mM, kcat/Km 540000 M^-1 s^-1.


smiles: CCCBr

column_label: Table 1; row 1-bromopropane; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized Table 1 values: Km=0.6 mM; kcat=2.7 s^-1; printed kcat/Km=4.5 s^-1 mM^-1; exported kcat/Km=4.500000000000001 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 1-bromopropane; columns: kcat=2.7 s^-1; Km=0.6 mM; kcat/Km=4500 M^-1 s^-1.


smiles: C(CO)CBr

column_label: Table 1; row 3-bromo-1-propanol; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized Table 1 values: Km=3.3 mM; kcat=3.0 s^-1; printed kcat/Km=0.91 s^-1 mM^-1; exported kcat/Km=0.9090909090909092 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 3-bromo-1-propanol; columns: kcat=3.0 s^-1; Km=3.3 mM; kcat/Km=910 M^-1 s^-1.


smiles: C(C(CBr)Br)Br

column_label: Table 1 row 1,2,3-tribromopropane, columns kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table row 1,2,3-tribromopropane reports kcat 3.6 s^-1, Km 0.3 mM, kcat/Km 12000 M^-1 s^-1.


smiles: C(CBr)Br

column_label: Table 1; row 1,2-dibromoethane; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized Table 1 values: Km=4.0 mM; kcat=14.3 s^-1; printed kcat/Km=3.6 s^-1 mM^-1; exported kcat/Km=3.575 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 1,2-dibromoethane; columns: kcat=14.3 s^-1; Km=4.0 mM; kcat/Km=3600 M^-1 s^-1.


enzyme_display_name: glucosamine-6-phosphate deaminase

organism: Bacillus subtilis

substrate_name: D-Glucosamine 6-phosphate

column_label: Official JBC full-text visible article, abstract and kinetic analysis prose for BsuNagB

raw_value_unit_evidence: BsuNagB kcat 28 s-1; Km(app) 0.13 mM; kinetic text kcat = 28 +/- 6 s-1 and Km(GlcN-6-P) = 0.13 +/- 0.02 mM

row_label: BsuNagB monomeric glucosamine-6-phosphate deaminase; GlcN-6-P

table_label: Official JBC full-text visible prose

enzyme: glucosamine-6-phosphate deaminase

substrate: D-Glucosamine 6-phosphate


enzyme_display_name: 2-aminomuconate deaminase

organism: Ectopseudomonas oleovorans

enzyme: 2-aminomuconate deaminase


organism: Escherichia coli

substrate_name: alpha-D-glucosamine 6-phosphate

substrate: alpha-D-glucosamine 6-phosphate


organism: Psychrobacter cryohalolentis

smiles: CCCCBr


smiles: C(CBr)CBr


organism: Shewanella oneidensis


organism: Staphylococcus aureus


enzyme_display_name: 4-chlorobenzoyl coenzyme A dehalogenase-2

organism: Arthrobacter sp

substrate_name: 4-iodobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)

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

assay_conditions_summary: pH 7.2; buffer 20 mM phosphate; cofactor CoA

proof_lines:
Arthrobacter sp. strain TM-1
4-chlorobenzoyl CoA dehalogenase
4-CBCoA


substrate_name: 4-bromobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)

enzyme: 4-chlorobenzoyl coenzyme A dehalogenase-2


substrate_name: 4-chlorobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)

assay_conditions_summary: pH 7.5; 303.15 K; buffer 20 mM phosphate; cofactor CoA


substrate_name: 4-fluorobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)


enzyme_display_name: 4-chlorobenzoyl coenzyme A dehalogenase-1

substrate: 4-iodobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)


enzyme: 4-chlorobenzoyl coenzyme A dehalogenase-1

substrate: 4-bromobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)


substrate: 4-chlorobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)


substrate: 4-fluorobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)


organism: Methylobacterium nodulans


organism: Methylobacterium radiotolerans


enzyme_display_name: Diphosphoinositol polyphosphate phosphohydrolase 1

organism: Homo sapiens


enzyme_display_name: Diphosphoinositol polyphosphate phosphohydrolase DDP1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Rattus norvegicus

column_label: The abstract reports rat hepatic DIPP cleaves PP-InsP5 with Km = 340 nM.

raw_value_unit_evidence: Km raw_value=340 nM raw_unit=nM

row_label: Prose segment: PP-InsP5 Km

table_label: PubMed PMID 9822604 abstract

enzyme: Diphosphoinositol polyphosphate phosphohydrolase 1


enzyme_display_name: exopolyphosphatase

organism: Leishmania major

substrate_name: guanosine 5'-tetraphosphate

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: does not hydrolyze pyrophosphate, ATP, or p-nitrophenylphosphate

enzyme: exopolyphosphatase

substrate: guanosine 5'-tetraphosphate


enzyme_display_name: ADP-ribose pyrophosphatase

substrate_name: ADP-ribose

enzyme: ADP-ribose pyrophosphatase

substrate: ADP-ribose


organism: Enterobacter cloacae

proof_lines:
Enterobacter cloacae
ACC deaminase activity
lineweaver Burk plot


enzyme_display_name: ADP-ribose diphosphatase

organism: Methanocaldococcus jannaschii

substrate_name: ADPribose 2'-phosphate

enzyme: ADP-ribose diphosphatase

substrate: ADPribose 2'-phosphate


organism: Autographa californica multiple nucleopolyhedrovirus

assay_conditions_summary: pH 8; cofactor ADP


substrate_name: ADPribose

substrate: ADPribose


organism: Saccharomyces cerevisiae


organism: Synechococcus sp.

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

assay_conditions_summary: pH 9.5; cofactor ADP

column_label: PMID 15158734 DOI 10.1016/j.bbapap.2004.03.004 Table 1; row NuhA; columns Kcat (s^-1), Km (mM), and Kcat/Km (M^-1 s^-1).

row_label: NuhA / ADP-ribose

table_label: Table 1. Kinetic parameters of the recombinant NuhA and NuhA-DPfam for ADP-ribose


enzyme_display_name: diadenosine hexaphosphate hydrolase (AMP-forming)

organism: Arabidopsis thaliana


enzyme_display_name: Genome polyprotein

organism: Tick-borne encephalitis virus European subtype (strain Neudoerfl)

substrate_name: ATP

assay_conditions_summary: cofactor ATP

enzyme: Genome polyprotein

substrate: ATP


enzyme: diadenosine hexaphosphate hydrolase (AMP-forming)


enzyme: Diphosphoinositol polyphosphate phosphohydrolase DDP1


enzyme_display_name: Diphosphoinositol polyphosphate phosphohydrolase 2

column_label: JBC Table II, row hDIPP2alpha, column K m (nM), for PP-InsP5 substrate reports 4.2 +/- 0.4.

raw_value_unit_evidence: Km raw_value=4.2 +/- 0.4 raw_unit=nM

table_label: Table II. Comparison of the catalytic properties of hDIPP isoforms with PP-InsP5 as substrate


column_label: Table I row Ap6A, column Km, reports 5.9 +/- 3.0 microM.

raw_value_unit_evidence: Ap6A Km=5.9 +/- 3.0 microM in Table I.

row_label: DIPP / Ap6A

table_label: JBC full text Table I


enzyme_display_name: inosine diphosphate phosphatase

substrate_name: ADP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP

enzyme: inosine diphosphate phosphatase

substrate: ADP


enzyme_display_name: Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

organism: Mus musculus

column_label: Article results prose states purified recombinant mENPP3 hydrolyzes cGAMP with KM = 76.5 +/- 18.7 uM at pH 9.0 in Figure 2C.

row_label: purified recombinant mouse ENPP3 hydrolyzing cGAMP

table_label: Results prose, Figure 2C


organism: Metapseudomonas resinovorans

assay_conditions_summary: pH 7.5; buffer 50 mM sodium phosphate

raw_value_unit_evidence: Table 1 row CarCCA10 / 6-Phenyl HODA columns: Km 2.51 uM; kcat 2.14 s^-1; kcat/Km 8.5 x 10^5 M^-1 s^-1.

row_label: CarCCA10 / 6-Phenyl HODA

table_label: Table 1. Kinetic parameters of native CarCCA10, ht-CarCCA10, and ht-CarCJ3


enzyme_display_name: diadenosine hexaphosphate hydrolase (ATP-forming)

organism: Thermus thermophilus

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

column_label: Table I. Kinetic constants for Ndx1; row Ap6A / ATP; columns kcat, Km, same-row quotient.

raw_value_unit_evidence: Table I Ap6A / ATP row: kcat 4.1 s^-1; Km 1.4 uM; printed kcat/Km 2.9 x 10^6 M^-1 s^-1.

row_label: Ap6A / ATP

table_label: Table I. Kinetic constants for Ndx1


organism: Burkholderia xenovorans LB400

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S112C to reconstruct the assayed variant sequence.


organism: Janthinobacterium sp. J3

column_label: Table 2; row ht-CarCJ3 / 6-Phenyl HODA; columns Km, kcat, same-row quotient.

raw_value_unit_evidence: Table 2 ht-CarCJ3 / 6-Phenyl HODA row: Km 2.73 uM; kcat 1.99 s^-1; printed scaled kcat/Km 7.3.

row_label: ht-CarCJ3 / 6-Phenyl HODA


organism: Paraburkholderia xenovorans

substrate_name: 4-nitrophenyl benzoate

substrate: 4-nitrophenyl benzoate


organism: Burkholderia xenovorans


organism: Paraburkholderia xenovorans (strain LB400)

substrate_name: HOPDA

substrate: HOPDA


enzyme_display_name: atrazine chlorohydrolase

organism: Pseudomonas sp.

substrate_name: hydroxyatrazine

enzyme: atrazine chlorohydrolase

substrate: hydroxyatrazine


enzyme_display_name: UniProt P9WNH5

organism: Mycobacterium tuberculosis

source_databases_merged: skid uniprot

enzyme: UniProt P9WNH5


enzyme_display_name: nucleoside-triphosphate phosphatase

organism: Southampton virus

enzyme: nucleoside-triphosphate phosphatase


substrate_name: Monochloroacetate

substrate: Monochloroacetate


substrate_name: Atrazine

column_label: Primary measurement evidence: evidence location type: table note; evidence location label: article page 1108 unnumbered kinetic-parameter table; measurement identity label: wild-type AtzA-AD1; atrazine; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 100 mM Tris-HCl pH 7.2; atrazine 4.6-140 uM; 25 C; 10 min; HPLC; captured primary segment: wild-type AtzA-AD1 values were Km 146 +/- 10 uM, kcat 1.6 +/- 0.1 s^-1, and kcat/Km 1.1x10^4 +/- 0.1x10^4 s^-1 M^-1.

raw_value_unit_evidence: Page 1108 table note reports wild-type AtzA-AD1 Km 146 +/- 10 uM, kcat 1.6 +/- 0.1 s^-1, and kcat/Km 1.1x10^4 +/- 0.1x10^4 s^-1 M^-1.

row_label: Wild-type AtzA-AD1 values in table note

substrate: Atrazine


organism: uncultured archaeon

proof_lines: coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase


enzyme_display_name: 4-chlorobenzoyl-CoA dehalogenase

assay_conditions_summary: pH 7

enzyme: 4-chlorobenzoyl-CoA dehalogenase


organism: Escherichia coli


organism: Homo sapiens

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


substrate_name: CDP-choline

substrate: CDP-choline


substrate_name: cADP-ribose

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

substrate: cADP-ribose


organism: Pseudomonas fluorescens

proof_lines:
mutant A129/V227I
mutant V227I


proof_lines:
mutant A129/I199V
mutant I199V


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


enzyme_display_name: phosphonoacetaldehyde hydrolase

organism: Achromobacter insolitus

substrate_name: phosphonoacetaldehyde

enzyme: phosphonoacetaldehyde hydrolase

substrate: phosphonoacetaldehyde


enzyme_display_name: UniProt O31156

organism: Bacillus cereus

enzyme: UniProt O31156


enzyme_display_name: Phosphonoacetaldehyde hydrolase

organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

substrate_name: phosphonoacetaldehyde (at pH 7.0, 25 degrees Celsius)

enzyme: Phosphonoacetaldehyde hydrolase


organism: Spinacia oleracea

substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: sulfite

substrate: sulfite


organism: Archaeoglobus fulgidus


enzyme_display_name: haloalkane dehalogenase

organism: Sphingobium sp.

substrate_name: beta-hexachlorocyclohexane

enzyme: haloalkane dehalogenase

substrate: beta-hexachlorocyclohexane


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


substrate_name: ADP-D-ribose

assay_conditions_summary: pH 7; 310.15 K; cofactor ADP

substrate: ADP-D-ribose


proof_lines: mutant enzyme W28A/W46A, at pH 7.0 and 37°C


substrate_name: ADP-ribose

proof_lines:
pH 7.0, 37°C, wild-type enzyme
wild type enzyme, at pH 7.0 and 37°C
wild-type, pH 7.5, 37°C

substrate: ADP-ribose


enzyme_display_name: adenosylhomocysteinase

organism: Cytophaga hutchinsonii

substrate_name: S-adenosyl-L-homocysteine

proof_lines:
pH 7.5, 22°C
at pH 7.5 and 22°C

enzyme: adenosylhomocysteinase

substrate: S-adenosyl-L-homocysteine


enzyme_display_name: UniProt P10760

organism: Rattus norvegicus

substrate_name: S-adenosyl-DL-homocysteine

enzyme: UniProt P10760

substrate: S-adenosyl-DL-homocysteine


enzyme_display_name: UniProt P23526

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.2
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=41°C, pH=6.5

enzyme: UniProt P23526


enzyme_display_name: UniProt P74008

organism: Synechocystis sp. PCC 6803

enzyme: UniProt P74008


enzyme_display_name: UniProt Q9I685

organism: Pseudomonas aeruginosa

enzyme: UniProt Q9I685


organism: Pyrococcus horikoshii

proof_lines:
at pH 8.5 and 37°C
Raw SKiD Env: Temp=37°C, pH=8.5


enzyme_display_name: ADP-ribose diphosphatase

organism: Bacillus methanolicus

substrate_name: ADPribose

assay_conditions_summary: pH 9.5; 323.15 K; cofactor ADP

enzyme: ADP-ribose diphosphatase

substrate: ADPribose


organism: Arthrobacter sp.


smiles: CCCCCCl


smiles: CCCCCl


smiles: CCCI


smiles: CC(C)CBr


smiles: CCI


organism: Bradyrhizobium japonicum


substrate_name: chlorocyclohexane

substrate: chlorocyclohexane


substrate_name: bromocyclohexane

substrate: bromocyclohexane


smiles: CC(CBr)Br


smiles: CCCCCCCl


smiles: CC(=C)CCl


organism: Classical swine fever virus

substrate_name: dUTP

mutation_signature: recombinant truncated protein ntNS3 / recombinant truncated protein ntNS3

mutation_type: truncation

proof_lines: pH 6.5, 37°C, recombinant truncated protein ntNS3, in absence of poly(U)

proof_lines: pH 6.5, 37°C, recombinant truncated protein ntNS3, in presence of poly(U)

substrate: dUTP


substrate_name: UTP

substrate: UTP


substrate_name: dCTP

substrate: dCTP


substrate_name: dGTP

substrate: dGTP


substrate_name: ATP

assay_conditions_summary: pH 6.5; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: dATP

substrate: dATP


substrate_name: CTP

substrate: CTP


substrate_name: GTP

substrate: GTP


enzyme_display_name: exopolyphosphatase

organism: Escherichia coli

substrate_name: (Polyphosphate)n

smiles: N#N

enzyme: exopolyphosphatase

substrate: (Polyphosphate)n


substrate_name: p-nitrophenyl phosphate

substrate: p-nitrophenyl phosphate


substrate_name: Unknown

substrate: Unknown


organism: Homo sapiens

substrate_name: XDP

substrate: XDP


substrate_name: ITP

substrate: ITP


substrate_name: ADP

substrate: ADP


proof_lines: with ADP as substrate, at pH 7.5 and 37°C

proof_lines: with ITP as substrate, at pH 7.5 and 37°C

proof_lines: with IDP as substrate, at pH 7.5 and 37°C


proof_lines: pH 8.0, 25°C, mutant enzyme D235A, approximate value from activity of the cell extract


proof_lines:
pH 8.0, 25°C, wild-type enzyme
pH 8.0, 25?, wild-type enzyme


enzyme_display_name: nucleotide diphosphatase

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

enzyme: nucleotide diphosphatase


substrate_name: cAMP

substrate: cAMP


assay_conditions_summary: pH 7.4; 297.15 K; cofactor ATP

proof_lines: versus 4-nitrophenyl 5'-thymidine monophosphate, pH 9.0, 37°C, NPP1


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines: E-NPP1, in 10 mM HEPES, 1 mM MgCl2, and 2 mM CaCl2, pH 7.4, at 37°C

proof_lines: E-NPP3, in 10 mM HEPES, 1 mM MgCl2, and 2 mM CaCl2, pH 7.4, at 37°C


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


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


organism: Hepacivirus hominis

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: pH 7.5, 25°C, NTP hydrolysis-dependent helicase activity

proof_lines: pH 7.5, 25°C, inhibition of ATPase activity


substrate_name: 2',3'-didehydro-thymidine triphosphate

substrate: 2',3'-didehydro-thymidine triphosphate


substrate_name: ddTTP

substrate: ddTTP


substrate_name: dTTP

substrate: dTTP


substrate_name: ddCTP

substrate: ddCTP


substrate_name: dCTP

substrate: dCTP


organism: Staphylococcus aureus

proof_lines: mutant E126A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication


substrate_name: ATP

assay_conditions_summary: pH 7.5; cofactor ATP

substrate: ATP


proof_lines: mutant Y88A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication


proof_lines: N45A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication


proof_lines: wild-type, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication


organism: Agrobacterium tumefaciens

smiles: C(CCl)CCl

proof_lines: below, recombinant wild-type enzyme, pH 8.6, 37°C

proof_lines: above, recombinant wild-type enzyme and mutant Y109W, pH 8.6, 37°C


proof_lines: recombinant wild-type enzyme, pH 8.6, 37°C


smiles: C(CI)CI


smiles: CCCCCCBr


enzyme_display_name: GTP cyclohydrolase II

organism: Bacillus subtilis

enzyme: GTP cyclohydrolase II


proof_lines: mutant enzyme Y210C/A290T/Q293R/A296T/K322R/M361I, at pH 8.5 and 30°C


proof_lines: mutant enzyme Y210C/A290T/Q293R/A296T/K322R/F339Y/M361I, at pH 8.5 and 30°C


organism: Bos taurus


substrate_name: UTP

substrate: UTP


substrate_name: CTP

substrate: CTP


substrate_name: CDP

substrate: CDP


substrate_name: FAD

assay_conditions_summary: cofactor FAD

substrate: FAD


substrate_name: 3-Aminopyridine adenine dinucleotide

substrate: 3-Aminopyridine adenine dinucleotide


substrate_name: adenosine diphosphoribose

substrate: adenosine diphosphoribose


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: 8-oxo-dGDP phosphatase

assay_conditions_summary: pH 8; 303.15 K; buffer Tris-HCl; cofactor ADP

proof_lines:
pH 8.0, 30°C
in Tris-HCl buffer (pH 8.0), at 37°C

enzyme: 8-oxo-dGDP phosphatase


assay_conditions_summary: pH 8; 303.15 K; cofactor ADP


substrate_name: dADP

substrate: dADP


substrate_name: dGDP

substrate: dGDP


organism: Caulobacter vibrioides

proof_lines:
pH 8.2, 25°C
at pH 8.2 and 25°C


smiles: C(CCCl)CCCl


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


substrate_name: thymidine 5'-monophosphate p-nitrophenyl ester


substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: CDP-choline

substrate: CDP-choline


enzyme_display_name: glucosamine-6-phosphate deaminase

substrate_name: D-glucosamine 6-phosphate

proof_lines: pH 8.0, 30°C, in presence of N-acetylglucosamine 6-phosphate

enzyme: glucosamine-6-phosphate deaminase

substrate: D-glucosamine 6-phosphate


substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


organism: Campylobacter jejuni


organism: Mus musculus

proof_lines: pH and temperature not specified in the publication


assay_conditions_summary: cofactor ATP


substrate_name: GTP

substrate: GTP


organism: Pseudomonas fluorescens


assay_conditions_summary: cofactor CoA


substrate_name: dITP

substrate: dITP


substrate_name: ITP

substrate: ITP


substrate_name: xanthosine 5'-triphosphate

substrate: xanthosine 5'-triphosphate


enzyme_display_name: 8-oxoguanine deaminase

organism: Pseudomonas aeruginosa

substrate_name: guanine

enzyme: 8-oxoguanine deaminase

substrate: guanine


substrate_name: isocytosine

substrate: isocytosine


organism: Pseudomonas sp.


substrate_name: beta-Chloro-D-alanine

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

substrate: beta-Chloro-D-alanine


substrate_name: O-acetyl-D-serine

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

substrate: O-acetyl-D-serine


organism: Rattus sp.

substrate: thymidine 5'-monophosphate p-nitrophenyl ester


substrate_name: NAD+

substrate: NAD+


substrate_name: UTP

substrate: UTP


substrate_name: D-vinylglycine

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

substrate: D-vinylglycine


substrate_name: GDP-mannose

substrate: GDP-mannose


substrate_name: p-nitrophenyl 5'-TMP

proof_lines: potent inhibition at nearly stoichiometric concentrations

substrate: p-nitrophenyl 5'-TMP


substrate_name: FAD

substrate: FAD


substrate_name: NADH

substrate: NADH


substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: ADP-ribose

assay_conditions_summary: cofactor ADP

substrate: ADP-ribose


organism: Aspergillus niger

substrate_name: fructose 6-phosphate

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

substrate: fructose 6-phosphate


substrate_name: glucosamine 6-phosphate

substrate: glucosamine 6-phosphate


substrate_name: dTTP

substrate: dTTP


enzyme_display_name: aminopyrimidine aminohydrolase

organism: Helicobacter pylori

proof_lines: mutant enzyme F47Y, in 30 mM Tris, 50 mM NaCl (pH 8.0), at 20°C

enzyme: aminopyrimidine aminohydrolase


proof_lines: wild type enzyme, in 30 mM Tris, 50 mM NaCl (pH 8.0), at 20°C


substrate_name: D-fructose 6-phosphate

proof_lines: pH 8.5, 37°C, in presence of N-acetylglucosamine 6-phosphate and Mn2+

substrate: D-fructose 6-phosphate


enzyme_display_name: single-stranded DNA cytosine deaminase

substrate_name: CCCA

enzyme: single-stranded DNA cytosine deaminase

substrate: CCCA


substrate_name: TTCA

substrate: TTCA


organism: Mycobacterium tuberculosis


organism: Mycobacterium tuberculosis variant bovis


smiles: C(CBr)CBr


mutation_signature: truncated enzyme


organism: Pseudomonas putida

substrate_name: D-Cystine

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

proof_lines: mutant enzyme E295S/L322T, pH and temperature not specified in the publication

substrate: D-Cystine


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


substrate_name: thiamine

substrate: thiamine


proof_lines: mutant enzyme D111A/K115A, at pH 7.5 and 37°C


enzyme_display_name: nucleoside-triphosphate phosphatase

organism: West Nile virus

substrate_name: ATP

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

enzyme: nucleoside-triphosphate phosphatase

substrate: ATP


substrate_name: DNA duplex

substrate: DNA duplex


organism: Arabidopsis sp.


organism: Arabidopsis thaliana

assay_conditions_summary: pH 8; 310.15 K; cofactor ADP

proof_lines:
37°C, pH 8.0, AtNUDT10
37°C, pH 8.0, AtNUDT6
37°C, pH 8.0, AtNUDT2


organism: Archaeoglobus fulgidus


organism: Bacillus sp. (in: firmicutes)

proof_lines:
at 60°C
at 25°C


organism: Bacillus subtilis


substrate_name: D-glucosamine 6-phosphate

proof_lines:
22°C, pH 8.0
recombinant enzyme, pH 7.4, 37°C

substrate: D-glucosamine 6-phosphate


organism: Bos taurus

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

proof_lines: in the presence of B4 lectin from Vicia villosa

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


organism: Campylobacter jejuni


organism: Candida albicans


organism: Canis lupus familiaris

proof_lines: per subunit, hyperbolic kinetic conditions, in presence of 1 mM N-acetylglucosamine 6-phosphate, pH 8.8

proof_lines: hexameric enzyme, hyperbolic kinetic conditions, in presence of 1 mM N-acetylglucosamine 6-phosphate, pH 8.8


organism: Dengue virus

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

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


organism: Enterovirus C


organism: Escherichia coli


organism: Haemophilus influenzae

substrate_name: alpha-D-glucosamine 6-phosphate

substrate: alpha-D-glucosamine 6-phosphate


organism: Homo sapiens

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP

proof_lines:
pH 7.5, 37°C
at pH 8.0 and 37°C
pH 7.0, 37°C


substrate_name: ADPribose

substrate: ADPribose


substrate_name: ADP-mannose

assay_conditions_summary: pH 7; 310.15 K; cofactor ADP

substrate: ADP-mannose


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


enzyme_display_name: double-stranded RNA adenine deaminase

substrate_name: adenine in double-stranded RNA

enzyme: double-stranded RNA adenine deaminase

substrate: adenine in double-stranded RNA


substrate_name: GDP

substrate: GDP


assay_conditions_summary: pH 10; 310.15 K; cofactor ADP

proof_lines:
at pH 10.0 and 37°C
at pH 8.0 and 37°C


substrate_name: 7-methylguanosine 5'-diphosphate

substrate: 7-methylguanosine 5'-diphosphate


proof_lines: N-terminally tagged protein, pH 7.2, 20°C

proof_lines: C-terminally tagged protein, pH 7.2, 20°C


enzyme_display_name: endothelin-converting enzyme 1

substrate_name: Big endothelin-1

enzyme: endothelin-converting enzyme 1

substrate: Big endothelin-1


organism: Methylorubrum extorquens


substrate_name: formyl-tetrahydromethanopterin

substrate: formyl-tetrahydromethanopterin


organism: Methanosarcina barkeri


enzyme_display_name: ADAMTS-4 endopeptidase

organism: Mus musculus

substrate_name: Unknown

enzyme: ADAMTS-4 endopeptidase

substrate: Unknown


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


substrate_name: UDP-alpha-D-galactose

substrate: UDP-alpha-D-galactose


organism: Mycobacterium tuberculosis


organism: Oryctolagus cuniculus


enzyme_display_name: GPR endopeptidase

organism: Priestia megaterium

substrate_name: spore protein A

proof_lines:
spore protein A, Km lower than 0.014 mM
Km lower than 0.008 mM
pH 7.4, 37°C

enzyme: GPR endopeptidase

substrate: spore protein A


organism: Pseudomonas putida


substrate_name: D-cysteine

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

proof_lines: double mutant Pseudomonas putida E295S+L322T

substrate: D-cysteine


organism: Rattus norvegicus

substrate_name: H2O; p-Nitrophenylthymidine phosphate

assay_conditions_summary: pH 8.9; 310.15 K; cofactor ATP

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

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

substrate: H2O; p-Nitrophenylthymidine phosphate


proof_lines:
ADPRibase I
ADPRibase-Mn
ADPRibase II


organism: Rattus sp.

substrate_name: ATP

substrate: ATP


enzyme_display_name: tRNA(adenine(34)) deaminase

organism: Saccharomyces cerevisiae

substrate_name: adenine34 in tRNASer(AGA)

proof_lines: pH and temperature not specified in the publication

enzyme: tRNA(adenine(34)) deaminase

substrate: adenine34 in tRNASer(AGA)


enzyme_display_name: endopolyphosphatase

enzyme: endopolyphosphatase


organism: Staphylococcus aureus

substrate_name: thiamine

proof_lines: apparent value, in 100 mM Tris-HCl, pH 7.5, at 37°C

substrate: thiamine


enzyme_display_name: lysostaphin

organism: Staphylococcus simulans

proof_lines: value from Grafit and Hanes plot analyses

enzyme: lysostaphin


substrate_name: pentaglycine

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

proof_lines: 37°C, pH 7.5, pentaglycine incorporated into the cell wall

substrate: pentaglycine


organism: Sus scrofa

substrate_name: D-glucosamine 6-phosphate

proof_lines: pH 7.9, 37°C, activated by N-acetylglucosamine 6-phosphate

substrate: D-glucosamine 6-phosphate


enzyme_display_name: 4-chlorobenzoyl-CoA dehalogenase

organism: Arthrobacter sp.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

enzyme: 4-chlorobenzoyl-CoA dehalogenase


substrate_name: ADP

assay_conditions_summary: pH 7; 295.15 K; cofactor ADP

proof_lines: pH 7.0, 22°C, recombinant wild-type enzyme

substrate: ADP


substrate_name: UTP

substrate: UTP


substrate_name: CTP

substrate: CTP


substrate_name: TTP

substrate: TTP


substrate_name: GTP

substrate: GTP


assay_conditions_summary: pH 7; 295.15 K; cofactor ATP


enzyme_display_name: ADP-ribose diphosphatase

organism: Bacillus subtilis

substrate_name: ADPribose

enzyme: ADP-ribose diphosphatase

substrate: ADPribose


organism: Escherichia coli


organism: Haemophilus influenzae


enzyme_display_name: alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase

proof_lines: pH 8.5, temperature not specified in the publication


enzyme_display_name: GTP cyclohydrolase II

proof_lines: full-length bifunctional enzyme ribA2, at pH 8.0 and 37°C

proof_lines: GCHII-domain of enzyme ribA2, at pH 8.0 and 37°C


organism: Homo sapiens

substrate_name: ADPribose; H2O

substrate: ADPribose; H2O


enzyme_display_name: GTP cyclohydrolase IIa

organism: Methanocaldococcus jannaschii

substrate_name: diphosphate

enzyme: GTP cyclohydrolase IIa

substrate: diphosphate


organism: Pseudomonas sp.

substrate_name: (R)-2-chloropropionic acid; 2-chloropropionic acid; (S)-2-chloropropionic acid

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


enzyme_display_name: peroxisome-assembly ATPase

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines: recombinant Pex1p/Pex6p complex, pH 7.4, 37°C

proof_lines: recombinant Pex1-FLAG/His-Pex6 complex, pH and temperature not specified in the publication

enzyme: peroxisome-assembly ATPase


enzyme_display_name: non-chaperonin molecular chaperone ATPase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: ATP (at 2.5 mM potassium acetate)

proof_lines: kcat is 0.95 min(-1) with ATP as substrate (at 2.5 mM potassium acetate) and 0.81 min(-1) with ATP as substrate (at 100 mM potassium acetate).

substrate: ATP (at 2.5 mM potassium acetate)


enzyme_display_name: vesicle-fusing ATPase

proof_lines: higher order oligomer of the enzyme, pH and temperature not specified in the publication

enzyme: vesicle-fusing ATPase


substrate_name: ATP; H2O

enzyme: non-chaperonin molecular chaperone ATPase

substrate: ATP; H2O


substrate_name: H2O; ATP

substrate: H2O; ATP


organism: Pseudomonas aeruginosa


organism: Arabidopsis thaliana


substrate_name: Unknown

substrate: Unknown


substrate_name: ATP

proof_lines:
human Hsp90alpha and Hsp90beta
ATP hydrolysis
Hsp90 ATPase cycle

substrate: ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R826M with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y819W with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N728A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T317A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


organism: Agrobacterium tumefaciens


substrate_name: ATP (at pH 7.8 and 30 degrees Celsius)

assay_conditions_summary: pH 7.8; cofactor ATP

substrate: ATP (at pH 7.8 and 30 degrees Celsius)


column_label: Full text reports wild type Drg1p exhibited ATPase activity with a Km(app) for ATP of 35 uM.

raw_value_unit_evidence: Km raw_value=35 uM raw_unit=microM

row_label: Wild type Drg1p ATPase activity

table_label: JBC full text Figure 4 / ATPase kinetics prose


organism: Caenorhabditis elegans

substrate_name: ATP (at 30 degrees Celsius)

substrate: ATP (at 30 degrees Celsius)


organism: Rattus norvegicus


enzyme_display_name: UniProt P06672

organism: Zymomonas mobilis

substrate_name: 2-ketohexanoic acid

smiles: CCCCC(=O)C(=O)O

enzyme: UniProt P06672

substrate: 2-ketohexanoic acid


substrate_name: 2-ketopentanoic acid

smiles: CCCC(=O)C(=O)O

substrate: 2-ketopentanoic acid


substrate_name: benzoylformate

substrate: benzoylformate


enzyme_display_name: UniProt A9H275

organism: Ipomoea batatas

substrate_name: pyruvate

enzyme: UniProt A9H275

substrate: pyruvate


enzyme_display_name: UniProt P20906

organism: Pseudomonas putida

substrate_name: 2-oxohexanoic acid

enzyme: UniProt P20906

substrate: 2-oxohexanoic acid


substrate_name: 2-oxo-4-methylhexanoic acid

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

substrate: 2-oxo-4-methylhexanoic acid


substrate_name: 2-oxopentanoic acid

substrate: 2-oxopentanoic acid


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


proof_lines:
Raw SKiD Env: Temp=30°C, pH=6.5
Raw SKiD Env: Temp=-----, pH=7
Raw SKiD Env: Temp=30°C, pH=6


substrate_name: phenylpyruvate

substrate: phenylpyruvate


substrate_name: methyl benzoylphosphonate

substrate: methyl benzoylphosphonate


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


enzyme_display_name: benzoylformate decarboxylase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T377L/A460Y to reconstruct the assayed variant sequence.

enzyme: benzoylformate decarboxylase


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


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


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


enzyme_display_name: pyruvate decarboxylase

organism: Saccharomyces cerevisiae

enzyme: pyruvate decarboxylase


proof_lines:
per subunit, pH 6.0, 30°C, mutant E91D
pH 6, 25°C, E91D mutant PDC


organism: Mycolicibacterium smegmatis


organism: Lactococcus lactis subsp. lactis

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


proof_lines: per subunit, pH 6.0, 30°C, wild-type enzyme


substrate_name: 2 pyruvate

proof_lines:
wild type enzyme, at pH 6.0 and 30°C
pH 6, wild-type YPDC

substrate: 2 pyruvate


proof_lines: mutant enzyme A143T/T156A/Q367H/N396I/K478R, at pH 6.0 and 30°C


organism: [Bacillus] caldolyticus


organism: Lactococcus lactis

substrate_name: Pyruvic acid

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

proof_lines:
pH 6.0, 30C, recombinant mutant V461I
pH 6.0, 30°C, recombinant mutant V461I

substrate: Pyruvic acid


proof_lines:
pH 6.0, 30C, recombinant mutant M538W
pH 6.0, 30°C, recombinant mutant M538W


proof_lines:
pH 6.0, 30C, recombinant mutant S286Y
pH 6.0, 30°C, recombinant mutant S286Y


proof_lines:
pH 6.0, 30C, recombinant mutant F381W
pH 6.0, 30°C, recombinant mutant F381W


proof_lines: pH 6, 25°C, C221E/C222A double mutant YPDC

proof_lines: per subunit, pH 6.0, 30°C, mutant C221E/C222A


proof_lines: pH 6, 25°C, C221D/C222A double mutant YPDC


assay_conditions_summary: pH 6


proof_lines:
pH 6, D28A mutant YPDC
D28A mutant YPDC


proof_lines: histidine buffer, enzyme from healthy tissue

proof_lines: histidine buffer, enzyme from diseased tissue

proof_lines: phosphate buffer, enzyme from healthy tissue


organism: Komagataella pastoris


organism: Pyrococcus furiosus

proof_lines: pH and temperature not specified in the publication


organism: Rhizopus arrhizus

proof_lines:
pH 6.5, 35C, isozyme 1
pH 6.5, 35°C, isozyme 2


organism: Rhodopseudomonas palustris


proof_lines: pH 6, 4°C, C221A/C222A double mutant PDC

proof_lines: pH 6, 30°C, C221A/C222A double mutant PDC

proof_lines: mutant enzyme C221A/C222A, at pH 6.5 and 10°C


substrate_name: Pyruvate

proof_lines:
isoform PDC6, at pH 7.0 and 25°C
isoform PDC1, at pH 7.0 and 25°C
isoform PDC5, at pH 7.0 and 25°C

substrate: Pyruvate


organism: Thermococcus kodakarensis


organism: Tritrichomonas suis

proof_lines:
pH 6.2, 25°C
pH 6.2, 25°C, presence of 0.1 M NaCl


organism: uncultured bacterium


enzyme_display_name: oxalate decarboxylase

organism: Cavia porcellus

substrate_name: oxalate

enzyme: oxalate decarboxylase

substrate: oxalate


organism: Zygosaccharomyces rouxii


organism: Lactiplantibacillus plantarum


enzyme_display_name: acetoacetate decarboxylase

organism: Rattus norvegicus

substrate_name: Acetoacetate

enzyme: acetoacetate decarboxylase

substrate: Acetoacetate


organism: Pseudothermotoga hypogea


organism: Stutzerimonas stutzeri


proof_lines: recombinant, his-tagged enzyme at pH 6.0 and 35°C


organism: Thermococcus guaymasensis


organism: Thermotoga maritima


enzyme_display_name: oxalyl-CoA decarboxylase

organism: Oxalobacter formigenes

substrate_name: Oxalyl-CoA

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

assay_conditions_summary: pH 6.7; 303.15 K; cofactor CoA

proof_lines:
pH 6.7, 30°C
at 37°C
Raw SKiD Env: Temp=30°C, pH=6.7

source_databases_merged: sabio_rk brenda skid uniprot

enzyme: oxalyl-CoA decarboxylase

substrate: Oxalyl-CoA


substrate_name: oxalyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E121A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; buffer 25 mM sodium phosphate; cofactor CoA

proof_lines: mutant enzyme E121A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl

substrate: oxalyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y120A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y120A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y483A with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y483A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y483F with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y483F, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E121Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E121Q, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y120F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y120F, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature S553A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S553A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature R555A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R555A, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl


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

proof_lines: wild type enzyme, in 25 mM sodium phosphate buffer, pH 6.5, containing 300 mM NaCl


enzyme_display_name: cis-aconitate decarboxylase

organism: Homo sapiens

substrate_name: cis-aconitate

enzyme: cis-aconitate decarboxylase

substrate: cis-aconitate


organism: Kluyveromyces lactis

proof_lines:
pH 6, 30°C, enzyme monomer
pH 6, 30°C


organism: Nakaseomyces glabratus

proof_lines: pH and temperature not specified in the publication


assay_conditions_summary: pH 6.5; buffer pH 6

proof_lines: wild-type, pH 6.5, 37°C, 167 mM phosphate buffer

proof_lines: pH 6.5, 37°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R273H to reconstruct the assayed variant sequence.

proof_lines: mutant R273H, pH 6.5, 37°C, 167 mM phosphate buffer


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N152S to reconstruct the assayed variant sequence.

proof_lines: mutant N152S, pH 6.5, 37°C, 167 mM phosphate buffer


organism: Zygosaccharomyces bisporus

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

proof_lines: pH 6, 25°C, sigmoidal dependence of the reaction rate from substrate concentration, Hill coefficient 2.10


organism: Zea mays

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E50D with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


organism: Sarcina ventriculi

sequence: MKITIAEYLLKRLKEVNVEHMFGVPGDYNLGFLDYV

wild_type_sequence: MKITIAEYLLKRLKEVNVEHMFGVPGDYNLGFLDYV

proof_lines: pH 6.5, potassium MES buffer, two affinities for pyruvate, sigmoidal kinetics

proof_lines: pH 6.5, sodium hydrogen maleate buffer, two affinities for pyruvate, sigmoidal kinetics


organism: Flammulina velutipes

proof_lines: recombinant OXDC, expressed in Nicotiana tabaccum


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E161A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 4


organism: Zymomonas mobilis

source_databases_merged: sabio_rk brenda skid


organism: Chromobacterium violaceum

substrate_name: acetoacetate

proof_lines: kcat is 350 sec(-1) at pH 6. kcat is 440 sec(-1) at pH 5.4. kcat is 420 sec(-1) at pH 4.8.

substrate: acetoacetate


organism: Aspergillus terreus (strain NIH 2624 / FGSC A1156)


organism: Clostridium acetobutylicum


organism: Escherichia coli

assay_conditions_summary: pH 6.5; 303.15 K; cofactor CoA

proof_lines: kcat is 69.7 sec(-1) for decarboxylase activity with oxalyl-CoA as substrate (with 300 uM ADP at pH 6.5 and 30 degrees Celsius). kcat is 60.7 sec(-1) for decarboxylase activity with oxalyl-CoA as substrate (at pH 6.5 and 30 degrees Celsius)


organism: Mus musculus


substrate_name: Oxalate

substrate: Oxalate


organism: Bacillus subtilis (strain 168)

substrate_name: Unknown

substrate: Unknown


organism: Pseudomonas putida

substrate_name: alpha-Oxo-benzeneacetic acid

substrate: alpha-Oxo-benzeneacetic acid


organism: Oxalobacter formigenes


substrate_name: 2-Keto-4-methylhexanoic acid

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

substrate: 2-Keto-4-methylhexanoic acid


proof_lines:
Raw SKiD Env: Temp=25°C, pH=-----
Raw SKiD Env: Temp=30°C, pH=6


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

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


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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P06672 and applied mutation signature I472A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADH

column_label: Table III, compound row 2-Keto-4-methylhexanoic acid (10), column PDCI472A; column 'Km (mM)' = 1.7; column 'kcat (s^-1)' = 7.7; column 'kcat/Km (mM^-1 s^-1)' = 4.5.

normalized_value_unit_evidence: Km: printed Table III cell 1.7 mM; the column is already millimolar, so no conversion is applied and the value is 1.7 mM. kcat: printed Table III cell 7.7 s^-1; the column is already per second, so no conversion is applied and the value is 7.7 s^(-1). kcat/Km: printed Table III cell 4.5 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1 with the two factors written in the other order, so no conversion is applied and the value is 4.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, compound row 2-Keto-4-methylhexanoic acid (10), column PDCI472A: Km = 1.7 mM; kcat = 7.7 s^-1; printed kcat/Km = 4.5 mM^-1 s^-1.

table_label: Table III: Michaelis-Menten constants for decarboxylation of branched chain 2-keto acids (Protein Engineering, Design & Selection 2005, 18(7):345-357)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P06672 and applied mutation signature I472A/I476F to reconstruct the assayed variant sequence.

column_label: Table III, compound row 2-Keto-4-methylhexanoic acid (10), column PDCI472A/I476F; column 'Km (mM)' = 3.7; column 'kcat (s^-1)' = 8.1; column 'kcat/Km (mM^-1 s^-1)' = 2.2.

normalized_value_unit_evidence: Km: printed Table III cell 3.7 mM; the column is already millimolar, so no conversion is applied and the value is 3.7 mM. kcat: printed Table III cell 8.1 s^-1; the column is already per second, so no conversion is applied and the value is 8.1 s^(-1). kcat/Km: printed Table III cell 2.2 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1 with the two factors written in the other order, so no conversion is applied and the value is 2.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, compound row 2-Keto-4-methylhexanoic acid (10), column PDCI472A/I476F: Km = 3.7 mM; kcat = 8.1 s^-1; printed kcat/Km = 2.2 mM^-1 s^-1.


column_label: Table II, compound row 2-Ketobutanoic acid (2), column I472A; column 'Km (mM)' = 6.7; column 'kcat (s^-1)' = 250; column 'kcat/Km (mM^-1 s^-1)' = 37; the same cell prints the relative value (54) in parentheses, which Table II defines as a percentage of the wild-type value.

normalized_value_unit_evidence: Km: printed Table II cell 6.7 mM; the column is already millimolar, so no conversion is applied and the value is 6.7 mM. kcat: printed Table II cell 250 s^-1; the column is already per second, so no conversion is applied and the value is 250.0 s^(-1). kcat/Km: printed Table II cell 37 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1 with the two factors written in the other order, so no conversion is applied and the value is 37.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, compound row 2-Ketobutanoic acid (2), column I472A: Km = 6.7 mM; kcat = 250 s^-1; printed kcat/Km = 37 mM^-1 s^-1.

table_label: Table II: Michaelis-Menten constants for decarboxylase activity of PDC variants (Protein Engineering, Design & Selection 2005, 18(7):345-357)


column_label: Table II, compound row 2-Ketobutanoic acid (2), column I472A/I476F; column 'Km (mM)' = 50; column 'kcat (s^-1)' = 9.0; column 'kcat/Km (mM^-1 s^-1)' = 0.2; the same cell prints the relative value (0.3) in parentheses, which Table II defines as a percentage of the wild-type value.

normalized_value_unit_evidence: Km: printed Table II cell 50 mM; the column is already millimolar, so no conversion is applied and the value is 50.0 mM. kcat: printed Table II cell 9.0 s^-1; the column is already per second, so no conversion is applied and the value is 9.0 s^(-1). kcat/Km: printed Table II cell 0.2 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1 with the two factors written in the other order, so no conversion is applied and the value is 0.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, compound row 2-Ketobutanoic acid (2), column I472A/I476F: Km = 50 mM; kcat = 9.0 s^-1; printed kcat/Km = 0.2 mM^-1 s^-1.


column_label: Table II, compound row 2-Ketobutanoic acid (2), column WT; column 'Km (mM)' = 4.7; column 'kcat (s^-1)' = 320; column 'kcat/Km (mM^-1 s^-1)' = 68; the same cell prints the relative value (100) in parentheses, which Table II defines as a percentage of the wild-type value.

normalized_value_unit_evidence: Km: printed Table II cell 4.7 mM; the column is already millimolar, so no conversion is applied and the value is 4.7 mM. kcat: printed Table II cell 320 s^-1; the column is already per second, so no conversion is applied and the value is 320.0 s^(-1). kcat/Km: printed Table II cell 68 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1 with the two factors written in the other order, so no conversion is applied and the value is 68.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, compound row 2-Ketobutanoic acid (2), column WT: Km = 4.7 mM; kcat = 320 s^-1; printed kcat/Km = 68 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I472A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from accession_anchored:P20906/AY143338/AAC15502.1/1MCZ and applied mutation signature A460Y to reconstruct the assayed variant sequence.

raw_value_unit_evidence: Table 3 row A460Y; column 2KB; kcat=6.0 ± 0.4 s^-1; Km=1.3 ± 0.2 mM; kcat/Km=4.6 mM^-1 s^-1 (parenthetical 9-fold over wt).

table_label: Table 3


sequence_variant_note: Resolved canonical sequence from accession_anchored:P20906/AY143338/AAC15502.1/1MCZ and applied mutation signature T377L to reconstruct the assayed variant sequence.

raw_value_unit_evidence: Table 3 row T377L; column 2KB; kcat=7.5 ± 0.3 s^-1; Km=4.3 ± 0.4 mM; kcat/Km=1.7 mM^-1 s^-1 (parenthetical 3-fold over wt).


sequence_variant_note: Resolved canonical sequence from accession_anchored:P20906/AY143338/AAC15502.1/1MCZ and applied mutation signature T377L/A460Y to reconstruct the assayed variant sequence.

raw_value_unit_evidence: Table 3 row T377L-A460Y; column 2KB; kcat=5.8 ± 0.2 s^-1; Km=0.42 ± 0.02 mM; kcat/Km=14 mM^-1 s^-1 (parenthetical 28-fold over wt).


column_label: Table 3 | row wt | column 2KB | kcat (s^-1)=4 ± 1 | Km (mM)=7.5 ± 0.6 | kcat/Km (mM^-1 s^-1)=0.5

raw_value_unit_evidence: Table 3 row wt; column 2KB; kcat=4 ± 1 s^-1; Km=7.5 ± 0.6 mM; kcat/Km=0.5 mM^-1 s^-1 (parenthetical 1-fold over wt).

row_label: wt


raw_value_unit_evidence: Table 3 row A460Y; column 2KH; kcat=4.4 ± 0.2 s^-1; Km=0.28 ± 0.05 mM; kcat/Km=16 mM^-1 s^-1 (parenthetical 12-fold over wt).


raw_value_unit_evidence: Table 3 row T377L; column 2KH; kcat=1.1 ± 0.1 s^-1; Km=1.3 ± 0.3 mM; kcat/Km=0.86 mM^-1 s^-1 (parenthetical 0.6-fold over wt).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T377L/A460Y to reconstruct the assayed variant sequence.


raw_value_unit_evidence: Table 3 row A460Y; column 2KP; kcat=6.2 ± 0.2 s^-1; Km=0.28 ± 0.03 mM; kcat/Km=22 mM^-1 s^-1 (parenthetical 12-fold over wt).


raw_value_unit_evidence: Table 3 row T377L; column 2KP; kcat=3.3 ± 0.1 s^-1; Km=1.1 ± 0.1 mM; kcat/Km=3 mM^-1 s^-1 (parenthetical 1.6-fold over wt).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I472A/I476F with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


column_label: PMID 15930043, Table II. Michaelis-Menten constants for decarboxylase activity of PDC variants; row Compound 2-Ketohexanoic acid (4); PDC variant WT; columns kcat (s^-1)=4.0, Km (mM)=12.7, kcat/Km (mM^-1 s^-1)=0.3.

normalized_value_unit_evidence: kcat normalized_value=4.0 normalized_unit=s^-1; Km normalized_value=12.7 normalized_unit=mM; kcat/Km normalized_value=0.3 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=4.0 raw_unit=s^-1; Km raw_value=12.7 raw_unit=mM; kcat/Km raw_value=0.3 raw_unit=s^-1*mM^-1; source_context=PDC from Zymomonas mobilis; wild-type variant column in Table II. 2-Oxohexanoate maps to 2-ketohexanoic acid.


column_label: Table II, compound row 2-Ketopentanoic acid (3), column I472A; column 'Km (mM)' = 2.5; column 'kcat (s^-1)' = 220; column 'kcat/Km (mM^-1 s^-1)' = 87; the same cell prints the relative value (1260) in parentheses, which Table II defines as a percentage of the wild-type value.

normalized_value_unit_evidence: Km: printed Table II cell 2.5 mM; the column is already millimolar, so no conversion is applied and the value is 2.5 mM. kcat: printed Table II cell 220 s^-1; the column is already per second, so no conversion is applied and the value is 220.0 s^(-1). kcat/Km: printed Table II cell 87 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1 with the two factors written in the other order, so no conversion is applied and the value is 87.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, compound row 2-Ketopentanoic acid (3), column I472A: Km = 2.5 mM; kcat = 220 s^-1; printed kcat/Km = 87 mM^-1 s^-1.


column_label: Table II, compound row 2-Ketopentanoic acid (3), column I472A/I476F; column 'Km (mM)' = 11; column 'kcat (s^-1)' = 30; column 'kcat/Km (mM^-1 s^-1)' = 2.7; the same cell prints the relative value (39) in parentheses, which Table II defines as a percentage of the wild-type value.

normalized_value_unit_evidence: Km: printed Table II cell 11 mM; the column is already millimolar, so no conversion is applied and the value is 11.0 mM. kcat: printed Table II cell 30 s^-1; the column is already per second, so no conversion is applied and the value is 30.0 s^(-1). kcat/Km: printed Table II cell 2.7 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1 with the two factors written in the other order, so no conversion is applied and the value is 2.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, compound row 2-Ketopentanoic acid (3), column I472A/I476F: Km = 11 mM; kcat = 30 s^-1; printed kcat/Km = 2.7 mM^-1 s^-1.


column_label: PMID 15930043, Table II. Michaelis-Menten constants for decarboxylase activity of PDC variants; row Compound 2-Ketopentanoic acid (3); PDC variant WT; columns kcat (s^-1)=53, Km (mM)=7.6, kcat/Km (mM^-1 s^-1)=7.0.

normalized_value_unit_evidence: kcat normalized_value=53.0 normalized_unit=s^-1; Km normalized_value=7.6 normalized_unit=mM; kcat/Km normalized_value=7.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=53 raw_unit=s^-1; Km raw_value=7.6 raw_unit=mM; kcat/Km raw_value=7.0 raw_unit=s^-1*mM^-1; source_context=PDC from Zymomonas mobilis; wild-type variant column in Table II. 2-Oxopentanoate maps to 2-ketopentanoic acid.


column_label: Table II, compound row Benzoylformate (12), column I472A; column 'Km (mM)' = 1.8; column 'kcat (s^-1)' = 6.9; column 'kcat/Km (mM^-1 s^-1)' = 3.8.

normalized_value_unit_evidence: Km: printed Table II cell 1.8 mM; the column is already millimolar, so no conversion is applied and the value is 1.8 mM. kcat: printed Table II cell 6.9 s^-1; the column is already per second, so no conversion is applied and the value is 6.9 s^(-1). kcat/Km: printed Table II cell 3.8 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1 with the two factors written in the other order, so no conversion is applied and the value is 3.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, compound row Benzoylformate (12), column I472A: Km = 1.8 mM; kcat = 6.9 s^-1; printed kcat/Km = 3.8 mM^-1 s^-1.


column_label: Table II, compound row Benzoylformate (12), column I472A/I476F; column 'Km (mM)' = 4.4; column 'kcat (s^-1)' = 1.2; column 'kcat/Km (mM^-1 s^-1)' = 0.3.

normalized_value_unit_evidence: Km: printed Table II cell 4.4 mM; the column is already millimolar, so no conversion is applied and the value is 4.4 mM. kcat: printed Table II cell 1.2 s^-1; the column is already per second, so no conversion is applied and the value is 1.2 s^(-1). kcat/Km: printed Table II cell 0.3 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1 with the two factors written in the other order, so no conversion is applied and the value is 0.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, compound row Benzoylformate (12), column I472A/I476F: Km = 4.4 mM; kcat = 1.2 s^-1; printed kcat/Km = 0.3 mM^-1 s^-1.


substrate_name: pyruvate

column_label: Table II, compound row Pyruvate (1), column I472A; column 'Km (mM)' = 7.8; column 'kcat (s^-1)' = 200; column 'kcat/Km (mM^-1 s^-1)' = 26; the same cell prints the relative value (6) in parentheses, which Table II defines as a percentage of the wild-type value.

normalized_value_unit_evidence: Km: printed Table II cell 7.8 mM; the column is already millimolar, so no conversion is applied and the value is 7.8 mM. kcat: printed Table II cell 200 s^-1; the column is already per second, so no conversion is applied and the value is 200.0 s^(-1). kcat/Km: printed Table II cell 26 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1 with the two factors written in the other order, so no conversion is applied and the value is 26.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, compound row Pyruvate (1), column I472A: Km = 7.8 mM; kcat = 200 s^-1; printed kcat/Km = 26 mM^-1 s^-1.

substrate: pyruvate


column_label: Table II, compound row Pyruvate (1), column I472A/I476F; column 'Km (mM)' = 50; column 'kcat (s^-1)' = 8.0; column 'kcat/Km (mM^-1 s^-1)' = 0.2; the same cell prints the relative value (2) in parentheses, which Table II defines as a percentage of the wild-type value.

normalized_value_unit_evidence: Km: printed Table II cell 50 mM; the column is already millimolar, so no conversion is applied and the value is 50.0 mM. kcat: printed Table II cell 8.0 s^-1; the column is already per second, so no conversion is applied and the value is 8.0 s^(-1). kcat/Km: printed Table II cell 0.2 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1 with the two factors written in the other order, so no conversion is applied and the value is 0.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, compound row Pyruvate (1), column I472A/I476F: Km = 50 mM; kcat = 8.0 s^-1; printed kcat/Km = 0.2 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P06672 and applied mutation signature I476F to reconstruct the assayed variant sequence.

column_label: Table II, compound row Pyruvate (1), column I476F; column 'Km (mM)' = 2.6; column 'kcat (s^-1)' = 77; column 'kcat/Km (mM^-1 s^-1)' = 30; the same cell prints the relative value (7) in parentheses, which Table II defines as a percentage of the wild-type value.

normalized_value_unit_evidence: Km: printed Table II cell 2.6 mM; the column is already millimolar, so no conversion is applied and the value is 2.6 mM. kcat: printed Table II cell 77 s^-1; the column is already per second, so no conversion is applied and the value is 77.0 s^(-1). kcat/Km: printed Table II cell 30 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1 with the two factors written in the other order, so no conversion is applied and the value is 30.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, compound row Pyruvate (1), column I476F: Km = 2.6 mM; kcat = 77 s^-1; printed kcat/Km = 30 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P20906 and applied mutation signature A460I to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 303.15 K; buffer 50 mM potassium phosphate; cofactor NADH

column_label: Table IV, compound row 2-Ketopentanoic acid (3), column A460I; column 'Km (mM)' = 1.2; column 'kcat (s^-1)' = 40.6; column 'kcat/Km (mM^-1 s^-1)' = 33.8; the same cell prints the relative value (457) in parentheses, which Table IV defines as a percentage of the wild-type value; the Km cell carries the table footnote marker for substrate inhibition (Displays substrate inhibition with Ki = 20 mM.).

normalized_value_unit_evidence: Km: printed Table IV cell 1.2 mM; the column is already millimolar, so no conversion is applied and the value is 1.2 mM. kcat: printed Table IV cell 40.6 s^-1; the column is already per second, so no conversion is applied and the value is 40.6 s^(-1). kcat/Km: printed Table IV cell 33.8 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^-1 mM^-1 with the two factors written in the other order, so no conversion is applied and the value is 33.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table IV, compound row 2-Ketopentanoic acid (3), column A460I: Km = 1.2 mM; kcat = 40.6 s^-1; printed kcat/Km = 33.8 mM^-1 s^-1.

table_label: Table IV: Michaelis-Menten constants for decarboxylase activity of BFD variants (Protein Engineering, Design & Selection 2005, 18(7):345-357)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A460I to reconstruct the assayed variant sequence.