sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P20906 and applied mutation signature A460I/F464I to reconstruct the assayed variant sequence.

column_label: Table IV, compound row Benzoylformate (12), column A460I/F464I; column 'Km (mM)' = 1.1; column 'kcat (s^-1)' = 21; column 'kcat/Km (mM^-1 s^-1)' = 19; the same cell prints the relative value (1) in parentheses, which Table IV defines as a percentage of the wild-type value.

normalized_value_unit_evidence: Km: printed Table IV cell 1.1 mM; the column is already millimolar, so no conversion is applied and the value is 1.1 mM. kcat: printed Table IV cell 21 s^-1; the column is already per second, so no conversion is applied and the value is 21.0 s^(-1). kcat/Km: printed Table IV cell 19 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 19.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table IV, compound row Benzoylformate (12), column A460I/F464I: Km = 1.1 mM; kcat = 21 s^-1; printed kcat/Km = 19 mM^-1 s^-1.


enzyme_display_name: benzoylformate decarboxylase

organism: Pseudomonas putida

substrate_name: alpha-Oxo-benzeneacetic acid

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P20906 and applied mutation signature F464I to reconstruct the assayed variant sequence.

mutation_type: substitution

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

column_label: Table IV, compound row Benzoylformate (12), column F464I; column 'Km (mM)' = 2.3; column 'kcat (s^-1)' = 123; column 'kcat/Km (mM^-1 s^-1)' = 53; the same cell prints the relative value (3) in parentheses, which Table IV defines as a percentage of the wild-type value.

normalized_value_unit_evidence: Km: printed Table IV cell 2.3 mM; the column is already millimolar, so no conversion is applied and the value is 2.3 mM. kcat: printed Table IV cell 123 s^-1; the column is already per second, so no conversion is applied and the value is 123.0 s^(-1). kcat/Km: printed Table IV cell 53 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 53.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table IV, compound row Benzoylformate (12), column F464I: Km = 2.3 mM; kcat = 123 s^-1; printed kcat/Km = 53 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)

data_origin: experimental

enzyme: benzoylformate decarboxylase

substrate: alpha-Oxo-benzeneacetic acid

status: corrected

source: oed


verification_status: unverified

kcat_over_km_origin: calculated

sequence_variant_note: Mutation signature F464I matches the mutant residue at offset +0 and the reference residue at offset -14; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

status: unverified


mutation_signature: Unknown

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

ki_unit: mM

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

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


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

proof_lines:
Pseudomonas putida
benzoylformate decarboxylase
substrate specificity exchange


substrate_name: Pyruvate

proof_lines:
pyruvate
BFDA460I
benzoylformate decarboxylase

substrate: Pyruvate


substrate_name: 2-Keto-4-methylpentanoic acid

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

proof_lines:
substrate-spectrum shift
branch-chain substrate context
benzoylformate decarboxylase

substrate: 2-Keto-4-methylpentanoic acid


substrate_name: 2-Keto-4-methylhexanoic acid

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

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

column_label: Table III, compound row 2-Keto-4-methylhexanoic acid (10), column BFDA460I; column 'Km (mM)' = 1.1; column 'kcat (s^-1)' = 9.8; column 'kcat/Km (mM^-1 s^-1)' = 8.9; the Km cell carries the table footnote marker for substrate inhibition (Displays substrate inhibition with Ki = 48 mM.).

normalized_value_unit_evidence: Km: printed Table III cell 1.1 mM; the column is already millimolar, so no conversion is applied and the value is 1.1 mM. kcat: printed Table III cell 9.8 s^-1; the column is already per second, so no conversion is applied and the value is 9.8 s^(-1). kcat/Km: printed Table III cell 8.9 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 8.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, compound row 2-Keto-4-methylhexanoic acid (10), column BFDA460I: Km = 1.1 mM; kcat = 9.8 s^-1; printed kcat/Km = 8.9 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)

substrate: 2-Keto-4-methylhexanoic acid


column_label: Table III, compound row 2-Keto-4-methylpentanoic acid (8), column BFDA460I; column 'Km (mM)' = 3.4; column 'kcat (s^-1)' = 38; column 'kcat/Km (mM^-1 s^-1)' = 11; the same cell prints the relative value (975) in parentheses, which Table III 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 = 60 mM.).

normalized_value_unit_evidence: Km: printed Table III cell 3.4 mM; the column is already millimolar, so no conversion is applied and the value is 3.4 mM. kcat: printed Table III cell 38 s^-1; the column is already per second, so no conversion is applied and the value is 38.0 s^(-1). kcat/Km: printed Table III cell 11 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 11.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, compound row 2-Keto-4-methylpentanoic acid (8), column BFDA460I: Km = 3.4 mM; kcat = 38 s^-1; printed kcat/Km = 11 mM^-1 s^-1.


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

column_label: Table III, compound row 2-Keto-4-methylpentanoic acid (8), column BFD WT; column 'Km (mM)' = 9.6; column 'kcat (s^-1)' = 11; column 'kcat/Km (mM^-1 s^-1)' = 1.1; the same cell prints the relative value (100) in parentheses, which Table III defines as a percentage of the wild-type value.

normalized_value_unit_evidence: Km: printed Table III cell 9.6 mM; the column is already millimolar, so no conversion is applied and the value is 9.6 mM. kcat: printed Table III cell 11 s^-1; the column is already per second, so no conversion is applied and the value is 11.0 s^(-1). kcat/Km: printed Table III cell 1.1 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 1.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, compound row 2-Keto-4-methylpentanoic acid (8), column BFD WT: Km = 9.6 mM; kcat = 11 s^-1; printed kcat/Km = 1.1 mM^-1 s^-1.


column_label: Table IV, compound row 2-Ketobutanoic acid (2), column A460I; column 'Km (mM)' = 18.3; column 'kcat (s^-1)' = 18.8; column 'kcat/Km (mM^-1 s^-1)' = 1.0.

normalized_value_unit_evidence: Km: printed Table IV cell 18.3 mM; the column is already millimolar, so no conversion is applied and the value is 18.3 mM. kcat: printed Table IV cell 18.8 s^-1; the column is already per second, so no conversion is applied and the value is 18.8 s^(-1). kcat/Km: printed Table IV cell 1.0 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 1.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table IV, compound row 2-Ketobutanoic acid (2), column A460I: Km = 18.3 mM; kcat = 18.8 s^-1; printed kcat/Km = 1.0 mM^-1 s^-1.


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

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


enzyme_display_name: oxalyl-CoA decarboxylase

organism: Oxalobacter formigenes

substrate_name: Oxalyl-CoA

verification_status: verified

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

assay_conditions_summary: pH 6.5; 303.15 K; cofactor CoA

column_label: PMID 17637344 Table 2. Summary of Kinetic Data for OXC Mutants; row E121A; columns KM (uM)=41 +/- 8, kcat (s^-1)=0.1 +/- 0.01, and printed kcat/KM=2.4 x 10^3 s^-1 M^-1; strict kcat/Km value is locked from the same-row kcat and KM central values for oxalyl-CoA.

normalized_value_unit_evidence: kcat normalized_value=0.1 normalized_unit=s^-1; km normalized_value=0.041 normalized_unit=mM; kcat_over_km normalized_value=2.4390243902439024 normalized_unit=s^-1*mM^-1.

enzyme: oxalyl-CoA decarboxylase

substrate: Oxalyl-CoA

status: verified


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

column_label: PMID 17637344 Table 2. Summary of Kinetic Data for OXC Mutants; row E121Q; columns KM (uM)=18 +/- 4, kcat (s^-1)=3.3 +/- 0.3, and printed kcat/KM=1.8 x 10^5 s^-1 M^-1; strict kcat/Km value is locked from the same-row kcat and KM central values for oxalyl-CoA.

normalized_value_unit_evidence: kcat normalized_value=3.3 normalized_unit=s^-1; km normalized_value=0.018 normalized_unit=mM; kcat_over_km normalized_value=183.33333333333334 normalized_unit=s^-1*mM^-1.


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

column_label: PMID 17637344 Table 2. Summary of Kinetic Data for OXC Mutants; row R555A; columns KM (uM)=66 +/- 8, kcat (s^-1)=85 +/- 4, and printed kcat/KM=1.3 x 10^6 s^-1 M^-1; strict kcat/Km value is locked from the same-row kcat and KM central values for oxalyl-CoA.

normalized_value_unit_evidence: kcat normalized_value=85.0 normalized_unit=s^-1; km normalized_value=0.066 normalized_unit=mM; kcat_over_km normalized_value=1287.8787878787878 normalized_unit=s^-1*mM^-1.


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

column_label: PMID 17637344 Table 2. Summary of Kinetic Data for OXC Mutants; row S553A; columns KM (uM)=21 +/- 5, kcat (s^-1)=13 +/- 1.5, and printed kcat/KM=6.2 x 10^5 s^-1 M^-1; strict kcat/Km value is locked from the same-row kcat and KM central values for oxalyl-CoA.

normalized_value_unit_evidence: kcat normalized_value=13.0 normalized_unit=s^-1; km normalized_value=0.021 normalized_unit=mM; kcat_over_km normalized_value=619.047619047619 normalized_unit=s^-1*mM^-1.


column_label: PMID 17637344 Table 2. Summary of Kinetic Data for OXC Mutants; row OXC; columns KM (uM)=23 +/- 3.5, kcat (s^-1)=88 +/- 4, and printed kcat/KM=3.8 x 10^6 s^-1 M^-1; strict kcat/Km value is locked from the same-row kcat and KM central values for oxalyl-CoA.

normalized_value_unit_evidence: kcat normalized_value=88.0 normalized_unit=s^-1; km normalized_value=0.023 normalized_unit=mM; kcat_over_km normalized_value=3826.086956521739 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 row OXC: KM 23 +/- 3.5 uM; kcat 88 +/- 4 s^-1; printed kcat/KM 3.8 x 10^6 s^-1 M^-1.

row_label: OXC


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

column_label: PMID 17637344 Table 2. Summary of Kinetic Data for OXC Mutants; row Y120A; columns KM (uM)=60 +/- 14, kcat (s^-1)=0.26 +/- 0.03, and printed kcat/KM=4.1 x 10^3 s^-1 M^-1; strict kcat/Km value is locked from the same-row kcat and KM central values for oxalyl-CoA.

normalized_value_unit_evidence: kcat normalized_value=0.26 normalized_unit=s^-1; km normalized_value=0.06 normalized_unit=mM; kcat_over_km normalized_value=4.333333333333334 normalized_unit=s^-1*mM^-1.


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

column_label: PMID 17637344 Table 2. Summary of Kinetic Data for OXC Mutants; row Y120F; columns KM (uM)=43 +/- 9, kcat (s^-1)=7.2 +/- 0.6, and printed kcat/KM=1.7 x 10^5 s^-1 M^-1; strict kcat/Km value is locked from the same-row kcat and KM central values for oxalyl-CoA.

normalized_value_unit_evidence: kcat normalized_value=7.2 normalized_unit=s^-1; km normalized_value=0.043 normalized_unit=mM; kcat_over_km normalized_value=167.4418604651163 normalized_unit=s^-1*mM^-1.


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

column_label: PMID 17637344 Table 2. Summary of Kinetic Data for OXC Mutants; row Y483A; columns KM (uM)=24 +/- 7, kcat (s^-1)=1.4 +/- 0.1, and printed kcat/KM=5.6 x 10^4 s^-1 M^-1; strict kcat/Km value is locked from the same-row kcat and KM central values for oxalyl-CoA.

normalized_value_unit_evidence: kcat normalized_value=1.4 normalized_unit=s^-1; km normalized_value=0.024 normalized_unit=mM; kcat_over_km normalized_value=58.33333333333333 normalized_unit=s^-1*mM^-1.


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

column_label: PMID 17637344 Table 2. Summary of Kinetic Data for OXC Mutants; row Y483F; columns KM (uM)=40 +/- 11, kcat (s^-1)=1.7 +/- 0.2, and printed kcat/KM=4.1 x 10^4 s^-1 M^-1; strict kcat/Km value is locked from the same-row kcat and KM central values for oxalyl-CoA.

normalized_value_unit_evidence: kcat normalized_value=1.7 normalized_unit=s^-1; km normalized_value=0.04 normalized_unit=mM; kcat_over_km normalized_value=42.5 normalized_unit=s^-1*mM^-1.


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


substrate_name: benzylformate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P20906 and applied mutation signature A460Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 303.15 K; cofactor NADH

column_label: Table 3 (Steady-State Kinetic Characterization of BFDC Variants Showing Improved PDC Activity); the five substrate column heads are 'BF', '2KH', '2KP', '2KB' and 'Pyr' and the three parameter rows of each BFDC variant block are 'kcat (s-1)', 'Km (mM)' and 'kcat/Km (mM-1 s-1)'. For BFDC variant 'A460Y' in column 'BF': kcat = 1.7; Km = 0.04; kcat/Km = 43. The second number printed in parentheses inside each kcat/Km cell is the -fold increase over wt stated in footnote a, not a kinetic value.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.7 s-1; the paper already prints this metric in s^(-1), so no unit conversion applies and the normalized value is 1.7 s^(-1). Km: printed Table 3 cell 0.04 mM; the paper already prints this metric in mM, so no unit conversion applies and the normalized value is 0.04 mM. kcat/Km: printed Table 3 cell 43 mM-1 s-1; mM^-1 s^-1 is the canonical efficiency unit, so no unit conversion applies and the normalized value is 43.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, BFDC variant row 'A460Y', substrate column 'BF': kcat = 1.7 s-1; Km = 0.04 mM; printed kcat/Km = 43 mM-1 s-1.

table_label: Table 3: Steady-State Kinetic Characterization of BFDC Variants Showing Improved PDC Activity (Biochemistry 2009, 48, 8387-8395)

substrate: benzylformate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P20906 and applied mutation signature T377L to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetic Characterization of BFDC Variants Showing Improved PDC Activity); the five substrate column heads are 'BF', '2KH', '2KP', '2KB' and 'Pyr' and the three parameter rows of each BFDC variant block are 'kcat (s-1)', 'Km (mM)' and 'kcat/Km (mM-1 s-1)'. For BFDC variant 'T377L' in column 'BF': kcat = 110; Km = 0.45; kcat/Km = 244. The second number printed in parentheses inside each kcat/Km cell is the -fold increase over wt stated in footnote a, not a kinetic value.

normalized_value_unit_evidence: kcat: printed Table 3 cell 110 s-1; the paper already prints this metric in s^(-1), so no unit conversion applies and the normalized value is 110.0 s^(-1). Km: printed Table 3 cell 0.45 mM; the paper already prints this metric in mM, so no unit conversion applies and the normalized value is 0.45 mM. kcat/Km: printed Table 3 cell 244 mM-1 s-1; mM^-1 s^-1 is the canonical efficiency unit, so no unit conversion applies and the normalized value is 244.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, BFDC variant row 'T377L', substrate column 'BF': kcat = 110 s-1; Km = 0.45 mM; printed kcat/Km = 244 mM-1 s-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P20906 and applied mutation signature T377L/A460Y to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetic Characterization of BFDC Variants Showing Improved PDC Activity); the five substrate column heads are 'BF', '2KH', '2KP', '2KB' and 'Pyr' and the three parameter rows of each BFDC variant block are 'kcat (s-1)', 'Km (mM)' and 'kcat/Km (mM-1 s-1)'. For BFDC variant 'T377L-A460Y' in column 'BF': kcat = 25; Km = 1.5; kcat/Km = 16. The second number printed in parentheses inside each kcat/Km cell is the -fold increase over wt stated in footnote a, not a kinetic value.

normalized_value_unit_evidence: kcat: printed Table 3 cell 25 s-1; the paper already prints this metric in s^(-1), so no unit conversion applies and the normalized value is 25.0 s^(-1). Km: printed Table 3 cell 1.5 mM; the paper already prints this metric in mM, so no unit conversion applies and the normalized value is 1.5 mM. kcat/Km: printed Table 3 cell 16 mM-1 s-1; mM^-1 s^-1 is the canonical efficiency unit, so no unit conversion applies and the normalized value is 16.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, BFDC variant row 'T377L-A460Y', substrate column 'BF': kcat = 25 s-1; Km = 1.5 mM; printed kcat/Km = 16 mM-1 s-1.


column_label: Table 3 (Steady-State Kinetic Characterization of BFDC Variants Showing Improved PDC Activity); the five substrate column heads are 'BF', '2KH', '2KP', '2KB' and 'Pyr' and the three parameter rows of each BFDC variant block are 'kcat (s-1)', 'Km (mM)' and 'kcat/Km (mM-1 s-1)'. For BFDC variant 'wt' in column 'BF': kcat = 320; Km = 0.27; kcat/Km = 1180. The second number printed in parentheses inside each kcat/Km cell is the -fold increase over wt stated in footnote a, not a kinetic value.

normalized_value_unit_evidence: kcat: printed Table 3 cell 320 s-1; the paper already prints this metric in s^(-1), so no unit conversion applies and the normalized value is 320.0 s^(-1). Km: printed Table 3 cell 0.27 mM; the paper already prints this metric in mM, so no unit conversion applies and the normalized value is 0.27 mM. kcat/Km: printed Table 3 cell 1180 mM-1 s-1; mM^-1 s^-1 is the canonical efficiency unit, so no unit conversion applies and the normalized value is 1180.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, BFDC variant row 'wt', substrate column 'BF': kcat = 320 s-1; Km = 0.27 mM; printed kcat/Km = 1180 mM-1 s-1.


substrate_name: pyruvate

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

column_label: Table 3 (Steady-State Kinetic Characterization of BFDC Variants Showing Improved PDC Activity); the five substrate column heads are 'BF', '2KH', '2KP', '2KB' and 'Pyr' and the three parameter rows of each BFDC variant block are 'kcat (s-1)', 'Km (mM)' and 'kcat/Km (mM-1 s-1)'. For BFDC variant 'A460Y' in column 'Pyr': kcat = 1.4; Km = 21; kcat/Km = 0.065. The second number printed in parentheses inside each kcat/Km cell is the -fold increase over wt stated in footnote a, not a kinetic value.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.4 s-1; the paper already prints this metric in s^(-1), so no unit conversion applies and the normalized value is 1.4 s^(-1). Km: printed Table 3 cell 21 mM; the paper already prints this metric in mM, so no unit conversion applies and the normalized value is 21.0 mM. kcat/Km: printed Table 3 cell 0.065 mM-1 s-1; mM^-1 s^-1 is the canonical efficiency unit, so no unit conversion applies and the normalized value is 0.065 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, BFDC variant row 'A460Y', substrate column 'Pyr': kcat = 1.4 s-1; Km = 21 mM; printed kcat/Km = 0.065 mM-1 s-1.

substrate: pyruvate


column_label: Table 3 (Steady-State Kinetic Characterization of BFDC Variants Showing Improved PDC Activity); the five substrate column heads are 'BF', '2KH', '2KP', '2KB' and 'Pyr' and the three parameter rows of each BFDC variant block are 'kcat (s-1)', 'Km (mM)' and 'kcat/Km (mM-1 s-1)'. For BFDC variant 'T377L' in column 'Pyr': kcat = 2.0; Km = 4.8; kcat/Km = 0.42. The second number printed in parentheses inside each kcat/Km cell is the -fold increase over wt stated in footnote a, not a kinetic value.

normalized_value_unit_evidence: kcat: printed Table 3 cell 2.0 s-1; the paper already prints this metric in s^(-1), so no unit conversion applies and the normalized value is 2.0 s^(-1). Km: printed Table 3 cell 4.8 mM; the paper already prints this metric in mM, so no unit conversion applies and the normalized value is 4.8 mM. kcat/Km: printed Table 3 cell 0.42 mM-1 s-1; mM^-1 s^-1 is the canonical efficiency unit, so no unit conversion applies and the normalized value is 0.42 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, BFDC variant row 'T377L', substrate column 'Pyr': kcat = 2.0 s-1; Km = 4.8 mM; printed kcat/Km = 0.42 mM-1 s-1.


enzyme_display_name: oxalate decarboxylase

organism: Bacillus subtilis

substrate_name: oxalate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E280Q to reconstruct the assayed variant sequence.

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

column_label: Table 1 row E280Q columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1); Mn column preserved as condition/modifier evidence

table_label: Table 1. Mn Incorporation and Steady-State Kinetic Parameters for Metal-Binding OxDC Mutants

enzyme: oxalate decarboxylase

substrate: oxalate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E280A to reconstruct the assayed variant sequence.

column_label: Table 1 row E280A columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1); Mn column preserved as condition/modifier evidence


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E280D to reconstruct the assayed variant sequence.

column_label: Table 1 row E280D columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1); Mn column preserved as condition/modifier evidence


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E101A to reconstruct the assayed variant sequence.

column_label: Table 1 row E101A columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1); Mn column preserved as condition/modifier evidence


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E101D to reconstruct the assayed variant sequence.

column_label: Table 1 row E101D columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1); Mn column preserved as condition/modifier evidence


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E101Q to reconstruct the assayed variant sequence.

column_label: Table 1 row E101Q columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1); Mn column preserved as condition/modifier evidence


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E101Q/E280Q to reconstruct the assayed variant sequence.

column_label: Table 1 row E101Q/E280Q columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1); footnote c confirms both substitutions; Mn column preserved

raw_value_unit_evidence: Km 2.9 +/- 0.3 mM; kcat 0.012 +/- 0.0003 s^-1; kcat/Km 4 M^-1 s^-1; Mn 0.07 per monomer; footnote c identifies both glutamine substitutions


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

column_label: Table 1 row WT OxDC columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1); Mn column preserved as condition/modifier evidence

row_label: WT OxDC


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H281A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H70A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S26A to reconstruct the assayed variant sequence.


substrate_name: Oxalate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E162D to reconstruct the assayed variant sequence.

substrate: Oxalate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E162Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R92K with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


enzyme_display_name: pyruvate decarboxylase

organism: Saccharomyces cerevisiae

proof_lines:
yeast glycolysis
isoenzymes
pyruvate decarboxylase

enzyme: pyruvate decarboxylase


assay_conditions_summary: pH 6.5; 303.15 K; buffer a standardised reaction; cofactor NADPH

column_label: Table label: Table 2, "Enzyme kinetics parameters determined in this project and contrasted with those of Ref. [23]". Reaction: PDC. Isoenzyme: Pdc6p. Rows read: PDC | Pdc6p | kcat -> Value cell 9.21, Unit cell s−1; PDC | Pdc6p | Kpyr -> Value cell 2.92, Unit cell mM. kcat/Km: no printed cell (Table 2 has no kcat/Km column).

normalized_value_unit_evidence: kcat 9.21 s−1 = 9.21 s^(-1) (printed unit s−1 is the export unit s^(-1), no conversion); decimal-equal to the catalog kcat 9.21; Km (Kpyr) 2.92 mM = 2.92 mM (already the export unit, no conversion); decimal-equal to the catalog km 2.92. In the on-disk transcription the printed superscript minus renders as the flattened `s−1` (U+2212) and empty SEM/Ref cells render as empty ` | ` fields.

raw_value_unit_evidence: Table 2, "Enzyme kinetics parameters determined in this project and contrasted with those of Ref. [23]" | header row: Reaction | Isoenzyme | Parameter | Value | SEM (%) | Ref. [23] | Unit | kcat evidence: PDC | Pdc6p | kcat | 9.21 |  |  | s−1 | Km evidence: PDC | Pdc6p | Kpyr | 2.92 |  | 4.33 | mM | cells read: kcat = 9.21 s−1 (Value column); Kpyr = 2.92 mM

row_label: PDC | Pdc6p


organism: Acetobacter pasteurianus

kcat_display: Not reported

kcat_over_km_display: Not reported

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

proof_lines:
Zymobacter palmae
pyruvate decarboxylase
three other bacteria


organism: Clostridium acetobutylicum

source_db: brenda

km_display: Not reported

proof_lines:
pyruvate
n-butanol
neutral pH

source: brenda


organism: Hanseniaspora uvarum

column_label: Abstract states the Km for pyruvate was 0.75 mM.

raw_value_unit_evidence: Km raw_value=0.75 raw_unit=mM

row_label: Hanseniaspora uvarum pyruvate decarboxylase with pyruvate

table_label: PubMed abstract PMID 7725793


organism: Sarcina ventriculi


organism: Zymobacter palmae


organism: Zymomonas mobilis

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADH

column_label: PMID 15930043, Table II. Michaelis-Menten constants for decarboxylase activity of PDC variants; row Compound Pyruvate (1); PDC variant WT; columns kcat (s^-1)=486, Km (mM)=1.1, kcat/Km (mM^-1 s^-1)=442.

normalized_value_unit_evidence: kcat normalized_value=486.0 normalized_unit=s^-1; Km normalized_value=1.1 normalized_unit=mM; kcat/Km normalized_value=442.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=486 raw_unit=s^-1; Km raw_value=1.1 raw_unit=mM; kcat/Km raw_value=442 raw_unit=s^-1*mM^-1; source_context=PDC from Zymomonas mobilis; wild-type variant column in Table II.

row_label: Compound Pyruvate (1); PDC variant WT


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W132F to reconstruct the assayed variant sequence.


organism: Escherichia coli

substrate_name: oxalyl-CoA

proof_lines:
oxalyl-CoA decarboxylase
oxalyl coenzyme A
Escherichia coli

substrate: oxalyl-CoA


organism: Candida albicans

proof_lines:
Candida albicans
pyruvate decarboxylase
pyruvate


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

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

assay_conditions_summary: pH 6; 303.15 K; buffer 100 mM potassium phosphate

proof_lines: mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C


proof_lines: mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C


proof_lines: mutant enzyme T377L/A460Y, at pH 6.0 and 30°C


proof_lines: mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C


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

proof_lines: wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C


proof_lines: pH 6.0, 30°C, wild-type enzyme and mutant enzyme A460I


assay_conditions_summary: cofactor NADPH

column_label: Table 2; reaction PDC; isoenzyme Pdc6p; parameter kcat value 9.21 s^-1; parameter Kpyr value 2.92 mM; kcat/Km computed from those explicit cells

normalized_value_unit_evidence: kcat normalized_value=9.21 normalized_unit=s^-1; Km normalized_value=2.92 normalized_unit=mM; kcat/Km normalized_value=3.1541095890410964 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=9.21 raw_unit=s^-1; Km raw_value=2.92 raw_unit=mM; kcat/Km computed from explicit Table 2 cells 9.21/2.92 raw_unit=s^-1*mM^-1

row_label: PDC / Pdc6p / Kpyr

table_label: Table 2. Enzyme kinetics parameters determined in this project and contrasted with those of [23].


substrate_name: 2-keto-4-methylhexanoic acid

proof_lines:
wild type, pH 6.5, 30°C
and above, wild type, pH 6.5, 30°C

substrate: 2-keto-4-methylhexanoic acid


substrate_name: 2-ketohexanoic acid

substrate: 2-ketohexanoic acid


substrate_name: benzoylformate

substrate: benzoylformate


substrate_name: 2-ketobutanoic acid

substrate: 2-ketobutanoic acid


substrate_name: 2-ketopentanoic acid

substrate: 2-ketopentanoic acid


proof_lines: mutant enzyme H281T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C


proof_lines: mutant enzyme H70F, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

proof_lines: pH and temperature not specified in the publication, mutant H70F


proof_lines: mutant enzyme H70S, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C


proof_lines: mutant enzyme H281Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

proof_lines: pH and temperature not specified in the publication, mutant H281Y


proof_lines: mutant enzyme H281Q, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C


proof_lines: mutant enzyme H70L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

proof_lines: pH and temperature not specified in the publication, mutant H70L


proof_lines: mutant enzyme H281W, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C


proof_lines: mutant enzyme H281N in 100 mM potassium phosphate buffer (pH 6.0), at 30°C


proof_lines: mutant enzyme S26M, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

proof_lines: pH and temperature not specified in the publication, mutant S26M


proof_lines: mutant enzyme H70T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C


proof_lines: mutant enzyme H281F, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

proof_lines: pH and temperature not specified in the publication, mutant H281F


proof_lines: mutant enzyme S26T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C


proof_lines: mutant enzyme S26L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

proof_lines: pH and temperature not specified in the publication, mutant S26L


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

proof_lines: mutant enzyme L476G, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C


proof_lines: mutant enzyme S181T/L476P, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C


proof_lines: mutant enzyme L476H, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C


proof_lines: mutant enzyme L476T, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C


proof_lines: mutant enzyme L476P, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C


proof_lines: mutant enzyme L476Q/S525G, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C


proof_lines: mutant enzyme L476M, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C


proof_lines: mutant enzyme L476S, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C


proof_lines: mutant enzyme L476A, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C


proof_lines: mutant enzyme S181T, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C


proof_lines: mutant enzyme L476C, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C


proof_lines: mutant enzyme L476K, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C


proof_lines: mutant enzyme T377L/A460Y, at pH 6.0 and 30°C


substrate_name: phenylpyruvate

substrate: phenylpyruvate


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


substrate_name: 2-oxo-4-methylhexanoic acid

substrate: 2-oxo-4-methylhexanoic acid


substrate_name: 2-oxo-4-methylpentanoic acid

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

substrate: 2-oxo-4-methylpentanoic acid


substrate_name: 2-oxobutanoic acid

substrate: 2-oxobutanoic acid


proof_lines:
pH 6.0, 30°C, mutant enzyme A460I/F464I
mutant enzyme A460I/F464I


substrate_name: 2-oxohexanoic acid

substrate: 2-oxohexanoic acid


substrate_name: 2-oxopentanoic acid

substrate: 2-oxopentanoic acid


proof_lines:
pH 6.0, 30°C, mutant enzyme A460I
mutant enzyme A460I


proof_lines:
pH 6.0, 30°C, mutant enzyme F464I
mutant enzyme F464I


mutation_type: deletion

proof_lines: pH 4.0, 26°C, recombinant deletion mutant DELTA163-163


proof_lines: mutant enzyme E101Q/E280Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C


proof_lines: mutant enzyme E280A , in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C


proof_lines: mutant enzyme E101A , in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C


proof_lines: mutant enzyme E280D, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C


proof_lines: mutant enzyme E101D, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C


proof_lines: mutant enzyme E101Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C


proof_lines: mutant enzyme E280Q, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C


assay_conditions_summary: pH 7; 303.15 K; buffer 100 mM potassium phosphate

proof_lines: mutant enzyme H70A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

proof_lines: pH and temperature not specified in the publication, mutant H70A


proof_lines: mutant enzyme H281A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

proof_lines: pH and temperature not specified in the publication, mutant H281A


proof_lines: mutant enzyme S26A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

proof_lines: pH and temperature not specified in the publication, mutant S26A


assay_conditions_summary: pH 7; 303.15 K; buffer pH 7

proof_lines: wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C

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


substrate_name: Unknown

substrate: Unknown


proof_lines: below, recombinant mutant W96F/W274F, pH and temperature not specified in the publication


proof_lines: recombinant mutant W96Y/W274Y, pH and temperature not specified in the publication


proof_lines: recombinant mutant W96F, pH and temperature not specified in the publication


proof_lines: recombinant mutant W274F, pH and temperature not specified in the publication


proof_lines: recombinant mutant W96Y, pH and temperature not specified in the publication


proof_lines: recombinant mutant W274Y, pH and temperature not specified in the publication


proof_lines: mutant enzyme D440E and mutant enzyme N467D


assay_conditions_summary: pH 6.5; buffer potassium phosphate

proof_lines: mutant enzyme L461V, in potassium phosphate buffer (pH 6.5, 50 mM)


proof_lines: mutant enzyme L461A, in potassium phosphate buffer (pH 6.5, 50 mM)


proof_lines: mutant enzyme P24A, in potassium phosphate buffer (pH 6.5, 50 mM)


proof_lines: mutant enzyme L461G, in potassium phosphate buffer (pH 6.5, 50 mM)


proof_lines: mutant enzyme A460G, in potassium phosphate buffer (pH 6.5, 50 mM)


organism: Methylorubrum extorquens

assay_conditions_summary: cofactor CoA

proof_lines: recombinant mutant Y497A/S568A, pH and temperature not specified in the publication, oxalyl-CoA decarboxylation


proof_lines: recombinant mutant Y497A, pH and temperature not specified in the publication, oxalyl-CoA decarboxylation


proof_lines: recombinant mutant S568A, pH and temperature not specified in the publication, oxalyl-CoA decarboxylation


proof_lines: recombinant wild-type enzyme, pH and temperature not specified in the publication, oxalyl-CoA decarboxylation

proof_lines: recombinant wild-type enzyme, pH and temperature not specified in the publication oxalyl-CoA decarboxylation


proof_lines:
pH 4, 26°C, E333A mutant OxdC
pH 4.0, 26°C, recombinant mutant E333A


proof_lines:
pH 4, 26°C, R270A mutant OxdC
pH 4.0, 26°C, recombinant mutant R270A


proof_lines:
pH 4.2, 23C, mutant E162Q
pH 4.0, 26°C, recombinant mutant E162Q
pH 4, 26°C, E162Q mutant OxdC


proof_lines:
pH 4.2, 23C, mutant R92K
pH 4.0, 26°C, recombinant mutant R92K
pH 4, 26°C, R92K mutant OxdC


proof_lines:
pH 4.2, 23C, mutant E162D
pH 4.0, 26°C, recombinant mutant E162D


assay_conditions_summary: pH 4

proof_lines: pH 4.0, recombinant mutant E162A/N163S/S164N


proof_lines: pH 4.0, recombinant mutant S161D/N163S/S164N


assay_conditions_summary: pH 6; 303.15 K; buffer 50 mM MES

proof_lines: wild type enzyme, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate


substrate_name: benzaldehyde

assay_conditions_summary: pH 7

substrate: benzaldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: p-nitro-benzoylformate

proof_lines: prolonged incubation of BFD with benzoylphosphonate results in permanent inactivation of the enzyme

substrate: p-nitro-benzoylformate


assay_conditions_summary: pH 6.5; 303.15 K; buffer 50 mM potassium phosphate

proof_lines: at 30°C, in 50 mM potassium phosphate buffer, pH 6.5

proof_lines: in 50 mM potassium phosphate buffer, pH 6.5, at 30°C


assay_conditions_summary: pH 7.5; 293.15 K; buffer 50 mM phosphate

proof_lines: free mutant enzyme A460I/F464I, in 50 mM phosphate buffer at pH 7.5 and 20°C

proof_lines: immobilized mutant enzyme A460I/F464I, in 50 mM phosphate buffer at pH 7.5 and 20°C


substrate_name: pyruvate

proof_lines: mutant enzyme E473D, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate

substrate: pyruvate


proof_lines: mutant enzyme E473Q, at 30°C in 50 mM MES buffer (pH 6.0) containing 1 mM MgSO4 and 0.1 mM thiamine diphosphate


assay_conditions_summary: pH 6.5; buffer 50 mM potassium phosphate

proof_lines: pH and temperature not specified in the publication

proof_lines: in 50 mM potassium phosphate buffer pH 6.5, 2.5 mM MgSO4, 0.1 mM thiamine diphosphate


substrate_name: oxalic acid

proof_lines:
non-His-tagged recombinant enzyme
His-tagged recombinant enzyme

substrate: oxalic acid


proof_lines: apparent value, pH and temperature not specified in the publication


substrate_name: oxalate

proof_lines: soluble enzyme, citrate buffer (0.05 M, pH 4.0), at 37°C

substrate: oxalate


enzyme_display_name: acetolactate decarboxylase

enzyme: acetolactate decarboxylase


proof_lines: pH 7.2, 25°C, recombinant wild-type enzyme, decarboxylase activity

proof_lines: pH 4.2, 25°C, recombinant wild-type enzyme, decarboxylase activity

proof_lines: wild type enzyme, in 50 mM NaOAc (pH 4.2), 0.2% (v/v) Triton X-100, 0.5 mM o-phenylenediamine, at 22°C


organism: Enterobacter cloacae


organism: Gluconobacter oxydans

proof_lines:
pH 5.0, 55°C, recombinant enzyme
pH 6.5, 55°C, recombinant enzyme
pH 7.0, 55°C, recombinant enzyme


organism: Klebsiella aerogenes


organism: Lactococcus lactis

proof_lines:
in presence of Leu
in absence of Leu


organism: Pseudomonas putida

substrate_name: methyl benzoylphosphonate

substrate: methyl benzoylphosphonate


substrate_name: benzoylformate

proof_lines: mutant enzyme L476Q, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C

substrate: benzoylformate


substrate_name: (p-methoxybenzoyl)formate

substrate: (p-methoxybenzoyl)formate


organism: Staphylococcus aureus


organism: Triticum aestivum

substrate_name: Pyruvate

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

substrate: Pyruvate


organism: Zea mays


assay_conditions_summary: pH 6


organism: Oryza sativa


enzyme_display_name: (S)-2-haloacid dehalogenase

organism: Pseudoalteromonas sp.

substrate_name: monobromoacetic acid

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

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

enzyme: (S)-2-haloacid dehalogenase

substrate: monobromoacetic acid


enzyme_display_name: UniProt Q51645

organism: Burkholderia cepacia

substrate_name: monobromoacetate

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q51645

substrate: monobromoacetate

source: skid


enzyme_display_name: haloacetate dehalogenase

organism: Delftia acidovorans

substrate_name: difluoroacetate

proof_lines:
at pH 6.0 and 37°C
at pH 7.0 and 37°C

enzyme: haloacetate dehalogenase

substrate: difluoroacetate


substrate_name: fluoroacetate

proof_lines:
at pH 7.0 and 37°C
at pH 6.0 and 37°C

substrate: fluoroacetate


organism: Cupriavidus necator

substrate_name: 2-hydroxymuconic semialdehyde

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

proof_lines:
isoform HODHI, at pH 7.6 and 23°C
isoform HODHII, at pH 7.6 and 23°C

substrate: 2-hydroxymuconic semialdehyde


organism: Dechloromonas aromatica (nom. nud.)


organism: Rattus norvegicus


organism: Ancylobacter aquaticus

substrate_name: Monochloroacetate

substrate: Monochloroacetate


organism: Azotobacter sp.


organism: Mus musculus

substrate_name: monofluoroacetate

smiles: C(C(=O)O)F

substrate: monofluoroacetate


organism: Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)

source_db: uniprot

proof_lines: kcat is 6.7 min(-1) with fluoroacetate as substrate. kcat is 1.38 min(-1) with chloroacetate as substrate.

source: uniprot


substrate_name: chloroacetate

substrate: chloroacetate


enzyme_display_name: 2,4-diacetylphloroglucinol hydrolase

organism: Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)

substrate_name: DAPG

enzyme: 2,4-diacetylphloroglucinol hydrolase

substrate: DAPG


organism: Rhodococcus jostii RHA1

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y61F to reconstruct the assayed variant sequence.


organism: Pseudomonas protegens (strain DSM 19095 / LMG 27888 / CFBP 6595 / CHA0)


organism: Pseudomonas sp.

sequence_source: multiple

proof_lines:
recombinant enzyme, pH 7.0, 25°C
kcat is 5.8 sec(-1).

source_databases_merged: brenda uniprot


organism: Sphingomonas sp. SKA58

substrate_name: Acetylpyruvate

proof_lines: kcat is 14.2 min(-1) with acetylpyruvate as substrate. kcat is 34.8 min(-1) with trimethylacetopyruvate as substrate.

substrate: Acetylpyruvate


organism: Rhodobacteraceae bacterium UDC319

substrate_name: 2-bromoacetic acid

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

substrate: 2-bromoacetic acid


organism: Sulfurisphaera tokodaii

substrate_name: (S)-2-chloropropionic acid

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

assay_conditions_summary: pH 9

proof_lines:
pH 9.0, 50°C, soluble enzyme
pH 9.0, 22°C, immobilized enzyme
pH 9.0, 37°C, immobilized enzyme

substrate: (S)-2-chloropropionic acid


organism: Pseudomonas sp. (strain YL)

substrate_name: (2S)-2-chloropropanoic acid

proof_lines: kcat is 47 sec(-1) for (2S)-2-chloropropanoic acid as substrate.

substrate: (2S)-2-chloropropanoic acid


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


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

proof_lines:
pH 9.5, 70°C
Raw SKiD Env: Temp=70°C, pH=9.5

source_databases_merged: brenda skid


organism: Pseudomonas fluorescens


substrate_name: Unknown

substrate: Unknown


substrate_name: trimethylacetopyruvate

substrate: trimethylacetopyruvate


organism: Burkholderia sp


organism: Polaromonas sp. JS666


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H214Q with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N132A to reconstruct the assayed variant sequence.


column_label: Table 2 'Table 2: Kinetic parameters of PhlG wild type and active-site mutants'; row Wild type; Km, kcat, and kcat/Km cells.

normalized_value_unit_evidence: Table 2 row Wild type, normalized where unambiguous: kcat 4.7 s^-1; Km 0.272 mM; kcat/Km 17 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Wild type: Km 272 ± 42 uM; kcat 4.7 ± 0.1 s^-1; kcat/Km 17000.

row_label: Wild type


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y121A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y229A with inferred residue-numbering offset -5 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:
Burkholderia sp
fluoroacetate
fluoroacetate dehalogenase


organism: Rhodopseudomonas palustris

substrate_name: 2-fluoropropionic acid

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

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

substrate: 2-fluoropropionic acid


column_label: Table 2 reports ST2570 defluorination kcat 7.0 +/- 0.4 min^-1, KM 2.4 +/- 0.7 mM, Kcat/KM 49 +/- 15 s^-1 M^-1; paper-unit values convert to slightly different normalized values than current export

normalized_value_unit_evidence: KM normalized_value=2.4 normalized_unit=mM; kcat normalized_value=0.1166666667 normalized_unit=s^-1; kcat_over_km normalized_value=0.049 normalized_unit=s^-1*mM^-1; current_export_kcat=0.12 s^-1; current_export_kcat_over_km=0.05 s^-1*mM^-1

raw_value_unit_evidence: KM raw_value=2.4 +/- 0.7 raw_unit=mM; kcat raw_value=7.0 +/- 0.4 raw_unit=min^-1; kcat_over_km raw_value=49 +/- 15 raw_unit=s^-1*M^-1 for ST2570 defluorination

row_label: Table 2 steady-state defluorination ST2570 row; kcat, KM, and Kcat/KM columns

table_label: PMID 34643018 PMC HTML Table 2


column_label: Table 2 reports ST2570 dechlorination kcat 15.4 +/- 0.2 min^-1, KM 3.53 x 10^-3 +/- 3 x 10^-5 mM, Kcat/KM 7.3 x 10^4 +/- 1.1 x 10^3 s^-1 M^-1; paper-unit values convert to slightly different normalized values than current export

normalized_value_unit_evidence: KM normalized_value=0.00353 normalized_unit=mM; kcat normalized_value=0.2566666667 normalized_unit=s^-1; kcat_over_km normalized_value=73 normalized_unit=s^-1*mM^-1; current_export_kcat=0.26 s^-1; current_export_km=0.0035 mM; current_export_kcat_over_km=74.28571428571429 s^-1*mM^-1

raw_value_unit_evidence: KM raw_value=3.53 x 10^-3 +/- 3 x 10^-5 raw_unit=mM; kcat raw_value=15.4 +/- 0.2 raw_unit=min^-1; kcat_over_km raw_value=7.3 x 10^4 +/- 1.1 x 10^3 raw_unit=s^-1*M^-1 for ST2570 dechlorination

row_label: Table 2 steady-state dechlorination ST2570 row; kcat, KM, and Kcat/KM columns


substrate_name: monoiodoacetate

smiles: C(C(=O)O)I

substrate: monoiodoacetate


organism: Agrobacterium sp.


organism: Burkholderia cepacia


substrate_name: Dichloroacetate

substrate: Dichloroacetate


substrate_name: Chloroacetate

substrate: Chloroacetate


organism: Ralstonia solanacearum


enzyme_display_name: D-amino-acid oxidase

organism: Rhodotorula toruloides

substrate_name: D-alanine

sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature S335G to reconstruct the assayed variant sequence.

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

proof_lines: mutant enzyme S335G, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

enzyme: D-amino-acid oxidase

substrate: D-alanine


substrate_name: cephalosporin C

substrate: cephalosporin C


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature Y223F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y223F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


proof_lines: wild type enzyme, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature S335H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S335H, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


substrate_name: D-Aspartate

substrate: D-Aspartate


substrate_name: D-arginine

sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature Q339E to reconstruct the assayed variant sequence.

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

proof_lines: kcat less than 0.2/s, mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

substrate: D-arginine


sequence_variant_note: Mutation signature Y228F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme Y228F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


proof_lines: mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature Y223S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y223S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature Y238S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y238S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature S335R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S335R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature Q339N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q339N, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y238R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y238R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M213E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M213E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S335R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M213R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M213R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q339E to reconstruct the assayed variant sequence.


enzyme_display_name: deacetoxycephalosporin-C synthase

organism: Streptomyces clavuligerus

substrate_name: ampicillin

sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature C281Y/N304K to reconstruct the assayed variant sequence.

enzyme: deacetoxycephalosporin-C synthase

substrate: ampicillin


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature C281Y/R307L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature C281Y/N304M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature V275I/N304M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature V275I/R307L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature R306L to reconstruct the assayed variant sequence.

proof_lines:
mutant R306L, pH 7.4, 30°C
mutant R306L, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature R307L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature N304R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature C281Y/N304A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature N304M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature I305M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature V275I/I305M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature C281Y/I305M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature N304M/R306L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature N304L/R306L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature N304R/R306L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature V275L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature N304K/R306L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature N304A/R306L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:P18548 and applied mutation signature V275I/R306L to reconstruct the assayed variant sequence.


enzyme_display_name: methylamine dehydrogenase (amicyanin)

organism: Paracoccus denitrificans

substrate_name: methylamine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_candidate and applied mutation signature I107V with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

smiles: CN

enzyme: methylamine dehydrogenase (amicyanin)

substrate: methylamine


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

smiles: CCCCCN


substrate_name: Butylamine

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

smiles: CCCCN

substrate: Butylamine


substrate_name: ethylamine

smiles: CCN

substrate: ethylamine


substrate_name: Propylamine

smiles: CCCN

substrate: Propylamine


smiles: C(CCCN)CCCN


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_candidate and applied mutation signature I107N with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


enzyme_display_name: galactokinase

organism: Rattus norvegicus

substrate_name: alpha-D-galactose / D-talose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R37A to reconstruct the assayed variant sequence.

enzyme: galactokinase

substrate: alpha-D-galactose / D-talose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y109F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y109H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y236F to reconstruct the assayed variant sequence.


assay_conditions_summary: cofactor ATP


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


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


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


enzyme_display_name: hydroxymethylglutaryl-CoA synthase

organism: Brassica juncea

substrate_name: acetoacetyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R157A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor CoA

enzyme: hydroxymethylglutaryl-CoA synthase

substrate: acetoacetyl-CoA


substrate_name: acetyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9M6U3 and applied mutation signature R157A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

column_label: Table 3: Kinetic properties of wild-type and mutant His6-BjHMGS1 (Biochem. J. 2004, 383:517-527), enzyme row 'R157A'; column 'V max (umol . min^-1 . mg^-1)' = 0.032; column 'K m-acetyl-CoA (uM)' = 52; column 'K i-AcAc-CoA (uM)' = 242 uM; column 'K cat (min^-1) (V max /[E])' = 1.7; column 'acetyl-CoA hydrolysis (t 1/2)' = 24.1 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 52 uM; 52 / 1000 = 0.052 mM. kcat: printed Table 3 cell 1.7 min^-1 under the column head 'K cat (min^-1)'; 1.7 / 60 = 0.028333333333333332 s^-1. kcat/Km: this paper prints no catalytic-efficiency cell in any table, so the ratio here is the full-precision quotient of the two printed cells of this same Table 3 row, 0.028333333333333332 / 0.052 = 0.5448717948717948 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'R157A': V max = 0.032 umol min^-1 mg^-1; K m-acetyl-CoA = 52 uM; K i-AcAc-CoA = 242 uM; K cat = 1.7 min^-1; acetyl-CoA hydrolysis t1/2 = 24.1 min.

row_label: Table 3, enzyme row 'R157A'

substrate: acetyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9M6U3 and applied mutation signature H188N to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic properties of wild-type and mutant His6-BjHMGS1 (Biochem. J. 2004, 383:517-527), enzyme row 'H188N'; column 'V max (umol . min^-1 . mg^-1)' = 0.056; column 'K m-acetyl-CoA (uM)' = 55; column 'K i-AcAc-CoA (uM)' = n.i. (no inhibition); column 'K cat (min^-1) (V max /[E])' = 2.9; column 'acetyl-CoA hydrolysis (t 1/2)' = 61.7 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 55 uM; 55 / 1000 = 0.055 mM. kcat: printed Table 3 cell 2.9 min^-1 under the column head 'K cat (min^-1)'; 2.9 / 60 = 0.04833333333333333 s^-1. kcat/Km: this paper prints no catalytic-efficiency cell in any table, so the ratio here is the full-precision quotient of the two printed cells of this same Table 3 row, 0.04833333333333333 / 0.055 = 0.8787878787878788 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'H188N': V max = 0.056 umol min^-1 mg^-1; K m-acetyl-CoA = 55 uM; K i-AcAc-CoA = n.i. (no inhibition); K cat = 2.9 min^-1; acetyl-CoA hydrolysis t1/2 = 61.7 min.

row_label: Table 3, enzyme row 'H188N'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9M6U3 and applied mutation signature C212S to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic properties of wild-type and mutant His6-BjHMGS1 (Biochem. J. 2004, 383:517-527), enzyme row 'C212S'; column 'V max (umol . min^-1 . mg^-1)' = 0.078; column 'K m-acetyl-CoA (uM)' = 29; column 'K i-AcAc-CoA (uM)' = 39 uM; column 'K cat (min^-1) (V max /[E])' = 4.1; column 'acetyl-CoA hydrolysis (t 1/2)' = 14.7 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 29 uM; 29 / 1000 = 0.029 mM. kcat: printed Table 3 cell 4.1 min^-1 under the column head 'K cat (min^-1)'; 4.1 / 60 = 0.06833333333333333 s^-1. kcat/Km: this paper prints no catalytic-efficiency cell in any table, so the ratio here is the full-precision quotient of the two printed cells of this same Table 3 row, 0.06833333333333333 / 0.029 = 2.3563218390804597 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'C212S': V max = 0.078 umol min^-1 mg^-1; K m-acetyl-CoA = 29 uM; K i-AcAc-CoA = 39 uM; K cat = 4.1 min^-1; acetyl-CoA hydrolysis t1/2 = 14.7 min.

row_label: Table 3, enzyme row 'C212S'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9M6U3 and applied mutation signature S89A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic properties of wild-type and mutant His6-BjHMGS1 (Biochem. J. 2004, 383:517-527), enzyme row 'S89A'; column 'V max (umol . min^-1 . mg^-1)' = 0.14; column 'K m-acetyl-CoA (uM)' = 18; column 'K i-AcAc-CoA (uM)' = 46 uM; column 'K cat (min^-1) (V max /[E])' = 7.6; column 'acetyl-CoA hydrolysis (t 1/2)' = 18.8 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 18 uM; 18 / 1000 = 0.018 mM. kcat: printed Table 3 cell 7.6 min^-1 under the column head 'K cat (min^-1)'; 7.6 / 60 = 0.12666666666666665 s^-1. kcat/Km: this paper prints no catalytic-efficiency cell in any table, so the ratio here is the full-precision quotient of the two printed cells of this same Table 3 row, 0.12666666666666665 / 0.018 = 7.037037037037036 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'S89A': V max = 0.14 umol min^-1 mg^-1; K m-acetyl-CoA = 18 uM; K i-AcAc-CoA = 46 uM; K cat = 7.6 min^-1; acetyl-CoA hydrolysis t1/2 = 18.8 min.

row_label: Table 3, enzyme row 'S89A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9M6U3 and applied mutation signature S356A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic properties of wild-type and mutant His6-BjHMGS1 (Biochem. J. 2004, 383:517-527), enzyme row 'S356A'; column 'V max (umol . min^-1 . mg^-1)' = 0.30; column 'K m-acetyl-CoA (uM)' = 26; column 'K i-AcAc-CoA (uM)' = 199 uM; column 'K cat (min^-1) (V max /[E])' = 16.1; column 'acetyl-CoA hydrolysis (t 1/2)' = 25 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 26 uM; 26 / 1000 = 0.026 mM. kcat: printed Table 3 cell 16.1 min^-1 under the column head 'K cat (min^-1)'; 16.1 / 60 = 0.26833333333333337 s^-1. kcat/Km: this paper prints no catalytic-efficiency cell in any table, so the ratio here is the full-precision quotient of the two printed cells of this same Table 3 row, 0.26833333333333337 / 0.026 = 10.320512820512823 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'S356A': V max = 0.30 umol min^-1 mg^-1; K m-acetyl-CoA = 26 uM; K i-AcAc-CoA = 199 uM; K cat = 16.1 min^-1; acetyl-CoA hydrolysis t1/2 = 25 min.

row_label: Table 3, enzyme row 'S356A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9M6U3 and applied mutation signature N115A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic properties of wild-type and mutant His6-BjHMGS1 (Biochem. J. 2004, 383:517-527), enzyme row 'N115A'; column 'V max (umol . min^-1 . mg^-1)' = 0.44; column 'K m-acetyl-CoA (uM)' = 27; column 'K i-AcAc-CoA (uM)' = 91 uM; column 'K cat (min^-1) (V max /[E])' = 23.4; column 'acetyl-CoA hydrolysis (t 1/2)' = 8.8 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 27 uM; 27 / 1000 = 0.027 mM. kcat: printed Table 3 cell 23.4 min^-1 under the column head 'K cat (min^-1)'; 23.4 / 60 = 0.38999999999999996 s^-1. kcat/Km: this paper prints no catalytic-efficiency cell in any table, so the ratio here is the full-precision quotient of the two printed cells of this same Table 3 row, 0.38999999999999996 / 0.027 = 14.444444444444443 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'N115A': V max = 0.44 umol min^-1 mg^-1; K m-acetyl-CoA = 27 uM; K i-AcAc-CoA = 91 uM; K cat = 23.4 min^-1; acetyl-CoA hydrolysis t1/2 = 8.8 min.

row_label: Table 3, enzyme row 'N115A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9M6U3 and applied mutation signature S359A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic properties of wild-type and mutant His6-BjHMGS1 (Biochem. J. 2004, 383:517-527), enzyme row 'S359A'; column 'V max (umol . min^-1 . mg^-1)' = 4.04; column 'K m-acetyl-CoA (uM)' = 24; column 'K i-AcAc-CoA (uM)' = 28 uM; column 'K cat (min^-1) (V max /[E])' = 214.1; column 'acetyl-CoA hydrolysis (t 1/2)' = 4.7 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 24 uM; 24 / 1000 = 0.024 mM. kcat: printed Table 3 cell 214.1 min^-1 under the column head 'K cat (min^-1)'; 214.1 / 60 = 3.5683333333333334 s^-1. kcat/Km: this paper prints no catalytic-efficiency cell in any table, so the ratio here is the full-precision quotient of the two printed cells of this same Table 3 row, 3.5683333333333334 / 0.024 = 148.68055555555554 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'S359A': V max = 4.04 umol min^-1 mg^-1; K m-acetyl-CoA = 24 uM; K i-AcAc-CoA = 28 uM; K cat = 214.1 min^-1; acetyl-CoA hydrolysis t1/2 = 4.7 min.

row_label: Table 3, enzyme row 'S359A'


column_label: Table 3: Kinetic properties of wild-type and mutant His6-BjHMGS1 (Biochem. J. 2004, 383:517-527), enzyme row 'Wild-Type'; column 'V max (umol . min^-1 . mg^-1)' = 0.47; column 'K m-acetyl-CoA (uM)' = 43; column 'K i-AcAc-CoA (uM)' = 38 uM; column 'K cat (min^-1) (V max /[E])' = 24.9; column 'acetyl-CoA hydrolysis (t 1/2)' = 11.1 min.

normalized_value_unit_evidence: Km: printed Table 3 cell 43 uM; 43 / 1000 = 0.043 mM. kcat: printed Table 3 cell 24.9 min^-1 under the column head 'K cat (min^-1)'; 24.9 / 60 = 0.415 s^-1. kcat/Km: this paper prints no catalytic-efficiency cell in any table, so the ratio here is the full-precision quotient of the two printed cells of this same Table 3 row, 0.415 / 0.043 = 9.651162790697676 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'Wild-Type': V max = 0.47 umol min^-1 mg^-1; K m-acetyl-CoA = 43 uM; K i-AcAc-CoA = 38 uM; K cat = 24.9 min^-1; acetyl-CoA hydrolysis t1/2 = 11.1 min.

row_label: Table 3, enzyme row 'Wild-Type'


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H188N/S359A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H188N to reconstruct the assayed variant sequence.


substrate_name: Unknown

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S359A 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.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C212S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S89A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N115A to reconstruct the assayed variant sequence.


enzyme_display_name: leucine dehydrogenase

organism: Geobacillus stearothermophilus

substrate_name: L-Leu

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

enzyme: leucine dehydrogenase

substrate: L-Leu


substrate_name: alpha-keto-isocaproate

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

substrate: alpha-keto-isocaproate


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


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


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A113A/V291L to reconstruct the assayed variant sequence.


substrate_name: alpha-keto-beta-methylvalerate

substrate: alpha-keto-beta-methylvalerate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A113A to reconstruct the assayed variant sequence.


substrate_name: L-norvaline

substrate: L-norvaline


substrate_name: L-norleucine

substrate: L-norleucine


substrate_name: L-Phe

substrate: L-Phe


substrate_name: L-Ile

substrate: L-Ile


substrate_name: methylamine

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +12, so it is treated as a source-provided variant sequence.

substrate: methylamine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I107V with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I107N with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


substrate_name: Butylamine

substrate: Butylamine


substrate_name: ethylamine

substrate: ethylamine


substrate_name: Propylamine

substrate: Propylamine


enzyme_display_name: aryldialkylphosphatase

organism: Homo sapiens

proof_lines: wild type enzyme, in 50 mM CHES (pH 9.0), at 30°C

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

enzyme: aryldialkylphosphatase


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -8, so it is treated as a source-provided variant sequence.

proof_lines: mutant enzyme S308G, in 50 mM CHES (pH 9.0), at 30°C


sequence_variant_note: Mutation signature H254G/H257W/L303T could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme H254G/H257W/L303T, in 50 mM CHES (pH 9.0), at 30°C


sequence_variant_note: Mutation signature H275Y/L303T could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme H275Y/L303T, in 50 mM CHES (pH 9.0), at 30°C


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +3, so it is treated as a source-provided variant sequence.

proof_lines: mutant enzyme G60A, in 50 mM CHES (pH 9.0), at 30°C


substrate_name: soman

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

substrate: soman


proof_lines: wild type enzyme, in 20 mM Tris-HCl with 1 mM CaCl2 (pH 7.4), at 25°C


substrate_name: sarin

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

substrate: sarin


enzyme_display_name: alpha-tubulin N-acetyltransferase

substrate_name: alpha-tubulin L-lysine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L164A to reconstruct the assayed variant sequence.

enzyme: alpha-tubulin N-acetyltransferase

substrate: alpha-tubulin L-lysine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F186A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P159A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L173A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P178A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R69A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K103A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q131A to reconstruct the assayed variant sequence.


mutation_signature: truncation variant 1-193

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

mutation_type: truncation


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K169A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S160A to reconstruct the assayed variant sequence.


mutation_signature: truncation variant 1-236


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N182A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R158A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N73A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V184A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F190A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K162A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S66A to reconstruct the assayed variant sequence.


enzyme_display_name: L-amino-acid oxidase

organism: Rhodococcus opacus

substrate_name: L-lysine

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

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

enzyme: L-amino-acid oxidase

substrate: L-lysine


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


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


substrate_name: L-citrulline

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

substrate: L-citrulline


substrate_name: L-leucine

substrate: L-leucine


substrate_name: L-asparagine

substrate: L-asparagine


substrate_name: L-ornithine

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

substrate: L-ornithine


substrate_name: L-methionine

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

substrate: L-methionine


substrate_name: L-arginine

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

substrate: L-arginine


substrate_name: L-glutamine

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

substrate: L-glutamine


substrate_name: L-Glutamic acid

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

substrate: L-Glutamic acid


substrate_name: L-serine

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

substrate: L-serine


substrate_name: L-valine

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

substrate: L-valine


substrate_name: L-isoleucine

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

substrate: L-isoleucine


substrate_name: L-Orn

substrate: L-Orn


enzyme_display_name: hydrogen dehydrogenase

substrate_name: methyl viologen

sequence: MKHSEKNEIASHELPTTPLDPVLAAGRES

proof_lines:
at pH 9.4
at pH 8.0

enzyme: hydrogen dehydrogenase

substrate: methyl viologen


substrate_name: FAD

assay_conditions_summary: cofactor FAD

substrate: FAD


substrate_name: methylene blue

substrate: methylene blue


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: cephalosporin C

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q339E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q339E, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

substrate: cephalosporin C


substrate_name: D-Aspartate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y238R to reconstruct the assayed variant sequence.

substrate: D-Aspartate


substrate_name: D-alanine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M213E to reconstruct the assayed variant sequence.

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

substrate: D-alanine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S335R to reconstruct the assayed variant sequence.


substrate_name: D-arginine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y223F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y223F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value

substrate: D-arginine


sequence_variant_note: Mutation signature Y228F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme Y228F, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S335G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S335G, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


proof_lines: mutant enzyme S335R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M213R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M213R, apparent value, at 25°C and pH 8.5


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y238S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y238S, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


proof_lines: mutant enzyme Y238R, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


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 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S335H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S335H, in 50 mM sodium diphosphate, pH 8.5, at air (21%) oxygen saturation, at 25°C, apparent value


enzyme_display_name: alcohol dehydrogenase (azurin)

organism: Comamonas testosteroni

smiles: CCCCCC(C)O

proof_lines: soluble enzyme, pH 7.7, presence of CaCl2

proof_lines: enzyme electrode, pH 7.7, presence of CaCl2

enzyme: alcohol dehydrogenase (azurin)


smiles: CCCCCCC(C)O


smiles: CCCCC(C)O


smiles: CC(C)CCC(C)O


smiles: CCCCCCC(CCC)O


smiles: CCCC(C)O


smiles: CCCC(CCC)O


smiles: CC(C)CC(C)O


smiles: CCCCCCC(CC)O


substrate_name: Cyclohexanol

substrate: Cyclohexanol


smiles: CCCCCC(CC)O


smiles: CCC(C)C(C)O


smiles: CCCCC(CC)O


substrate_name: (S)-glycidol

substrate: (S)-glycidol


smiles: CCC(C)O


smiles: CCCC(CC)O


smiles: CC(C)O


smiles: CCC(CC)O


enzyme_display_name: acetoacetate decarboxylase

organism: Streptomyces bingchenggensis

proof_lines: pH 6.5, 25°C, aldolase-dehydratase reaction, with pyruvate

enzyme: acetoacetate decarboxylase


substrate_name: trans-cinnamaldehyde

sequence_variant_note: Mutation signature Q118N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 6.5, 25°C, mutant Q118N, aldolase-dehydratase reaction, with pyruvate

substrate: trans-cinnamaldehyde


proof_lines: pH 6.5, 25°C, mutant Q118N, hydratase-retroaldolase reaction


sequence_variant_note: Mutation signature Y82F/Y252F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 6.5, 25°C, mutant Y82F/Y252F, hydratase-retroaldolase reaction


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

proof_lines: pH 6.5, 25°C, mutant E84Q, hydratase-retroaldolase reaction


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_candidate and applied mutation signature Y252F with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

proof_lines: pH 6.5, 25°C, mutant Y252F, hydratase-retroaldolase reaction


proof_lines: pH 6.5, 25°C, wild-type enzyme, hydratase-retroaldolase reaction

proof_lines: pH 6.5, 4°C, wild-type enzyme, aldolase-dehydratase reaction, with pyruvate

proof_lines: pH 6.5, 25°C, wild-type enzyme, dehydration


proof_lines: pH 6.5, 25°C, mutant Y82F/Y252F, aldolase-dehydratase reaction, with pyruvate


proof_lines: pH 6.5, 25°C, mutant Y252F, aldolase-dehydratase reaction, with pyruvate


sequence_variant_note: Mutation signature Y82F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 6.5, 4°C, mutant Y82F, aldolase-dehydratase reaction, with pyruvate

proof_lines: pH 6.5, 25°C, mutant Y82F, hydratase-retroaldolase reaction


proof_lines: pH 6.5, 25°C, mutant E84Q, aldolase-dehydratase reaction, with pyruvate


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


substrate_name: pyruvate

substrate: pyruvate


proof_lines: pH 6.5, 25°C, wild-type enzyme, aldolase-dehydratase reaction, with pyruvate


enzyme_display_name: thiopurine S-methyltransferase

enzyme: thiopurine S-methyltransferase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R226H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R226E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R152H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R226A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R152A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R152E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R152A/R226A to reconstruct the assayed variant sequence.


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y238S to reconstruct the assayed variant sequence.

smiles: O=O


substrate_name: D-Ala

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y238F to reconstruct the assayed variant sequence.

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

substrate: D-Ala


substrate_name: D-Phe

substrate: D-Phe


substrate_name: D-Trp

substrate: D-Trp


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


assay_conditions_summary: pH 8.5; 298.15 K; buffer 75 mM sodium diphosphate

proof_lines: wild type enzyme, in 75 mM sodium diphosphate buffer, pH 8.5 at 25°C


substrate_name: D-Ser

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

substrate: D-Ser


substrate_name: D-Val

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

substrate: D-Val


substrate_name: D-Pro

substrate: D-Pro


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_mutation_ranked_match and applied mutation signature K119T with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

proof_lines: mutant K119T, cytosolic fraction of yeast cells is incubated with 0-350 microM of 6-TG and 1mM of SAM


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G144R with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A80P with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K122T with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R163H with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G36S with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C132Y with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


enzyme_display_name: NADPH--hemoprotein reductase

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines:
wild type, cosubstrate FAD, Km below
wild type, cosubstrate cytochrome c

enzyme: NADPH--hemoprotein reductase

substrate: NADPH


proof_lines:
T491V mutant, cosubstrate FAD
T491V mutant, cosubstrate cytochrome c


substrate_name: cytochrome c

proof_lines:
T491V mutant, cosubstrate FAD
T491V mutant, cosubstrate NADPH

substrate: cytochrome c


proof_lines:
G488L mutant, cosubstrate FAD
G488L mutant, cosubstrate cytochrome c


proof_lines:
G488L mutant, cosubstrate FAD
G488L mutant, cosubstrate NADPH


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

proof_lines:
W677X mutant, cosubstrate NADPH
S678X mutant, cosubstrate NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R454E with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

proof_lines:
R454E mutant, cosubstrate NADPH
R454E mutant, cosubstrate FAD


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y456S with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines:
Y456S mutant, cosubstrate NADPH
Y456S mutant, cosubstrate FAD


proof_lines:
Y456S mutant, cosubstrate FAD
Y456S mutant, cosubstrate cytochrome c


proof_lines:
W677X mutant, cosubstrate cytochrome c
S678X mutant, cosubstrate cytochrome c


proof_lines:
R454E mutant, cosubstrate cytochrome c
R454E mutant, cosubstrate FAD


enzyme_display_name: tryptophan dehydrogenase

organism: Nostoc punctiforme

substrate_name: L-tryptophan

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L288M to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L288M, at pH 11.0 and 25°C

enzyme: tryptophan dehydrogenase

substrate: L-tryptophan


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M65A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature A69M to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 11; 298.15 K; cofactor NAD+

column_label: Table 2 | A69M NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.82 +/- 0.071 mM | kcat 1.2 +/- 0.058 s^-1 | kcat/Km 1.5 mM^-1 s^-1

normalized_value_unit_evidence: kcat=1.2 s^(-1); km=0.82 mM; kcat_over_km=1.5 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row A69M, non-parenthetical L-tryptophan cells

table_label: Table 2: kinetic constants of NpTrpDH mutants


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature A69L to reconstruct the assayed variant sequence.

column_label: Table 2 | A69L NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 1.1 +/- 0.047 mM | kcat 1.2 +/- 0.090 s^-1 | kcat/Km 1.1 mM^-1 s^-1

normalized_value_unit_evidence: kcat=1.2 s^(-1); km=1.1 mM; kcat_over_km=1.1 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row A69L, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature V133A to reconstruct the assayed variant sequence.

column_label: Table 2 | V133A NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.019 +/- 0.0019 mM | kcat 2.6 +/- 0.18 s^-1 | kcat/Km 140 mM^-1 s^-1

normalized_value_unit_evidence: kcat=2.6 s^(-1); km=0.019 mM; kcat_over_km=140 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row V133A, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature V291A to reconstruct the assayed variant sequence.

column_label: Table 2 | V291A NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.047 +/- 0.0030 mM | kcat 2.9 +/- 0.12 s^-1 | kcat/Km 62 mM^-1 s^-1

normalized_value_unit_evidence: kcat=2.9 s^(-1); km=0.047 mM; kcat_over_km=62 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row V291A, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature Y292H to reconstruct the assayed variant sequence.

column_label: Table 2 | Y292H NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.021 +/- 0.0030 mM | kcat 3.5 +/- 0.41 s^-1 | kcat/Km 170 mM^-1 s^-1

normalized_value_unit_evidence: kcat=3.5 s^(-1); km=0.021 mM; kcat_over_km=170 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row Y292H, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature V132A to reconstruct the assayed variant sequence.

column_label: Table 2 | V132A NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.017 +/- 0.0010 mM | kcat 4.6 +/- 0.20 s^-1 | kcat/Km 270 mM^-1 s^-1

normalized_value_unit_evidence: kcat=4.6 s^(-1); km=0.017 mM; kcat_over_km=270 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row V132A, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature M295A to reconstruct the assayed variant sequence.

column_label: Table 2 | M295A NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.047 +/- 0.0025 mM | kcat 8.0 +/- 0.58 s^-1 | kcat/Km 170 mM^-1 s^-1

normalized_value_unit_evidence: kcat=8 s^(-1); km=0.047 mM; kcat_over_km=170 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row M295A, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature Y292W to reconstruct the assayed variant sequence.

column_label: Table 2 | Y292W NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.030 +/- 0.0050 mM | kcat 8.5 +/- 0.58 s^-1 | kcat/Km 280 mM^-1 s^-1

normalized_value_unit_evidence: kcat=8.5 s^(-1); km=0.03 mM; kcat_over_km=280 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row Y292W, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature I296A to reconstruct the assayed variant sequence.

column_label: Table 2 | I296A NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.059 +/- 0.0070 mM | kcat 10 +/- 1.0 s^-1 | kcat/Km 170 mM^-1 s^-1

normalized_value_unit_evidence: kcat=10 s^(-1); km=0.059 mM; kcat_over_km=170 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row I296A, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature M40L to reconstruct the assayed variant sequence.

column_label: Table 2 | M40L NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.047 +/- 0.0036 mM | kcat 12 +/- 0.63 s^-1 | kcat/Km 260 mM^-1 s^-1

normalized_value_unit_evidence: kcat=12 s^(-1); km=0.047 mM; kcat_over_km=260 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row M40L, non-parenthetical L-tryptophan cells