sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E3PY95 and applied mutation signature S162A to reconstruct the assayed variant sequence.

column_label: Table 1: Summary of steady-state kinetic parameters for OAM and its active site variants with substrate D-ornithine and inhibitor 2,4-diaminobutyrate (BBA - Proteins and Proteomics 2017, 1865:1077-1084); Enzyme row 'S162A': column 'kcat (s-1)' = 0.37; column 'Km (uM)' = 29; column 'kcat/Km x 103 (s-1 M-1)' = 13; column 'Ki (DABA) (uM)' = 270 uM. The efficiency column is printed in units of 10^3 s-1 M-1, which is the same size as 1 s-1 mM-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.37 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.37 s^(-1); the exported value is 0.37 s^(-1). Km: printed Table 1 cell 29 uM; 29 / 1000 = 0.029 mM; the exported value is 0.029 mM. kcat/Km: printed Table 1 cell 13 in units of 10^3 s-1 M-1, that is 13000 s-1 M-1; 1 s-1 M-1 is 0.001 s-1 mM-1, so the printed cell becomes 13.0 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed component cells is 0.37 / 0.029 = 12.75862068965517 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Enzyme row 'S162A': kcat = 0.37 s-1; Km = 29 uM; printed kcat/Km = 13 in the column's units of 10^3 s-1 M-1.

row_label: Table 1, Enzyme row 'S162A', the printed kcat, Km and kcat/Km cells of that row


enzyme_display_name: D-ornithine 4,5-aminomutase

organism: Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF)

substrate_name: D-ornithine

source_db: uniprot

verification_status: verified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

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

column_label: Primary paper abstract/results list apparent Km values in substrate order D-ornithine, AdoCbl, PLP and Figure 4A is the D-ornithine panel.

normalized_value_unit_evidence: 44.5 uM normalizes to 0.0445 mM.

raw_value_unit_evidence: D-ornithine apparent Km 44.5 +/- 2.8 uM.

row_label: D-ornithine

table_label: Abstract and Results: Kinetic Analysis; Figure 4A

data_origin: experimental

enzyme: D-ornithine 4,5-aminomutase

substrate: D-ornithine

status: verified

source: uniprot


substrate_name: adenosylcobalamin

column_label: Primary paper abstract/results give apparent Km values and Figure 4B is the AdoCbl panel.

normalized_value_unit_evidence: 0.43 uM normalizes to 0.00043 mM.

raw_value_unit_evidence: AdoCbl apparent Km 0.43 +/- 0.04 uM.

row_label: 5'-deoxyadenosylcobalamin (AdoCbl)

table_label: Abstract and Results: Kinetic Analysis; Figure 4B

substrate: adenosylcobalamin


substrate_name: pyridoxal phosphate

column_label: Primary paper abstract/results list apparent Km values in substrate order D-ornithine, AdoCbl, PLP and Figure 4C is the PLP panel.

normalized_value_unit_evidence: 1.5 uM normalizes to 0.0015 mM.

raw_value_unit_evidence: PLP apparent Km 1.5 +/- 0.1 uM.

row_label: pyridoxal 5'-phosphate (PLP)

table_label: Abstract and Results: Kinetic Analysis; Figure 4C

substrate: pyridoxal phosphate


enzyme_display_name: lysine 5,6-aminomutase

organism: Clostridium sticklandii

substrate_name: D-Lysine

verification_status: unverified

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

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

enzyme: lysine 5,6-aminomutase

substrate: D-Lysine

status: unverified


organism: Acetoanaerobium sticklandii

source_db: oed

kcat_over_km_origin: calculated

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

mutation_type: substitution

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E338A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E338D with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


substrate_name: DL-Ornithine

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

substrate: DL-Ornithine


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E3PY95 and applied mutation signature I424E with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 298.15 K; cofactor NADH

column_label: Table 2 (The steady-state kinetic parameters for wild-type OAM and variant forms); Table 2, classification 'Group A', enzyme row 'I424E'; column 'kcat' = 0.76; column 'Km' = 185; column 'kcat/Km' = 4.12, the table printing a single unit row x 10^3 M^-1 s^-1 above that column.

normalized_value_unit_evidence: kcat: printed cell 0.76 s^-1; no unit conversion applies, so the canonical value is 0.76 s^(-1). Km: printed cell 185 uM; 185 / 1000 = 0.185 mM. kcat/Km: printed cell 4.12 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.12 x 10^3 / 1000 = 4.12 s^-1 mM^-1. The quotient of the two printed component cells is 0.76 / 0.185 = 4.108108108108108 s^-1 mM^-1, which lies outside the rounding interval of the printed efficiency cell, so the printed efficiency cell is the paper's own fitted primary value and 4.12 s^(-1)*mM^(-1) is proposed for kcat_over_km.

raw_value_unit_evidence: Table 2, classification 'Group A', enzyme row 'I424E': printed kcat cell 0.76; printed Km cell 185; printed kcat/Km cell 4.12 carrying the table's own unit row x 10^3 M^-1 s^-1. Section 6 of the local extract resolves the kcat column as s^-1 and the Km column as uM from that printed unit row and from the arithmetic of all ten numeric rows of Tables 1 and 2.

table_label: Table 2: the steady-state kinetic parameters measured with D-ornithine (J. Biol. Chem. 2014, 289(49):34161-34174)

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E3PY95 and applied mutation signature D627A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

column_label: Table 2 (The steady-state kinetic parameters for wild-type OAM and variant forms); Table 2, classification 'Group A', enzyme row 'D627A'; column 'kcat' = 2.89; column 'Km' = 193; column 'kcat/Km' = 15.0, the table printing a single unit row x 10^3 M^-1 s^-1 above that column.

normalized_value_unit_evidence: kcat: printed cell 2.89 s^-1; no unit conversion applies, so the canonical value is 2.89 s^(-1). Km: printed cell 193 uM; 193 / 1000 = 0.193 mM. kcat/Km: printed cell 15.0 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 15.0 x 10^3 / 1000 = 15.0 s^-1 mM^-1. The exported kcat/Km 14.974093264248705 s^(-1)*mM^(-1) is the exact quotient 2.89 / 0.193 of the two printed component cells of this same table line, and the printed efficiency cell is that quotient rendered at the table's own precision, so the exported ratio is kept as printed evidence of it.

raw_value_unit_evidence: Table 2, classification 'Group A', enzyme row 'D627A': printed kcat cell 2.89; printed Km cell 193; printed kcat/Km cell 15.0 carrying the table's own unit row x 10^3 M^-1 s^-1. Section 6 of the local extract resolves the kcat column as s^-1 and the Km column as uM from that printed unit row and from the arithmetic of all ten numeric rows of Tables 1 and 2.


organism: Schizosaccharomyces pombe

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

sequence_source: multiple

proof_lines:
phosphatase activity
mutase activity


source_db: brenda

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E93D to reconstruct the assayed variant sequence.

source: brenda


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R14Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R120Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R121Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R120Q/R121Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R94Q with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: 2,3-bisphosphoglycerate (for mutase reaction)

proof_lines: kcat is 490 sec(-1) for the mutase reaction, 0.0074 sec(-1) for the synthase reaction and 0.0087 sec(-1) for the phosphatase reaction with 3-phosphoglycerate as substrate.


organism: Schistosoma mansoni

proof_lines: at pH 7.8, temperature not specified in the publication

source_databases_merged: brenda uniprot


organism: Escherichia coli (strain K12)

substrate_name: 2-PGA (at pH 7 and 30 degrees Celsius)

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

assay_conditions_summary: pH 7

column_label: ScienceDirect Table 1 row Km 2-PGA, dPGM column, reports 190 +/- 35 microM.

raw_value_unit_evidence: Table 1 dPGM Km 2-PGA=190 +/- 35 microM.

row_label: E. coli dPGM / 2-PGA

table_label: ScienceDirect Table 1

substrate: 2-PGA (at pH 7 and 30 degrees Celsius)


proof_lines: kcat is 22 sec(-1) for mutase with 3-PGA as substrate (at pH 7 and 30 degrees Celsius). kcat is 10 sec(-1) for mutase with 2-PGA as substrate (at pH 7 and 30 degrees Celsius).


organism: Saccharomyces cerevisiae

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

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

source_databases_merged: sabio_rk skid uniprot


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H225Q with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y160F 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 S162A 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 Y187F with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


organism: Lactococcus lactis subsp. lactis

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

assay_conditions_summary: pH 7.2; buffer triethanol-HCl

proof_lines: in triethanol-HCl buffer (125 mM, pH 7.2, 5 mM MgCl2, 10 mM KCl), 0.1 mM 2,3-bisphosphoglyceric acid, temperature not specified in the publication


organism: Gallus gallus

substrate_name: 2,3-Bisphospho-D-glycerate; H2O

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

substrate: 2,3-Bisphospho-D-glycerate; H2O


organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)


enzyme_display_name: lysine 2,3-aminomutase

organism: Clostridium subterminale

enzyme: lysine 2,3-aminomutase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H225A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


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


substrate_name: Glycerate 3-phosphate

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

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

substrate: Glycerate 3-phosphate


organism: Escherichia coli

assay_conditions_summary: pH 7; cofactor NADH

column_label: Primary article Section 3.3, Table 1, iPGM column; rows Km 3-PGA, kcat forward, and Forward kcat/Km.

normalized_value_unit_evidence: Km 0.21 mM; kcat 22 s^-1; explicit printed kcat/Km 100 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 iPGM column: Km 3-PGA 210 +/- 39 uM; kcat forward 22 +/- 1 s^-1; forward kcat/Km 1.0 x 10^5 M^-1 s^-1.

row_label: iPGM; forward reaction; 3-PGA substrate

table_label: Table 1. Kinetic constants for E. coli dPGM and iPGM and S. cerevisiae PGM


substrate_name: L-lysine

substrate: L-lysine


substrate_name: adenosylmethionine

substrate: adenosylmethionine


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

column_label: Abstract reports Km for 4-thialysine is 1.4 +/- 0.1 mM under the same assay conditions.

raw_value_unit_evidence: Km raw_value=1.4 +/- 0.1 mM raw_unit=mM

row_label: Clostridium subterminale lysine 2,3-aminomutase / 4-thialysine

table_label: PubMed XML abstract PMID 11370852


organism: Rattus norvegicus


organism: Thermoplasma acidophilum


organism: Saccharolobus solfataricus

proof_lines: 65°C, pH not specified in the publication

proof_lines: 70°C, pH not specified in the publication

proof_lines: 80°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y187A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

proof_lines: pH 8.5, 20°C, recombinant beta-subunit mutant Y187A


proof_lines: pH 8.5, 20°C, recombinant beta-subunit mutant Y187F

proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant Y187F


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E3PY95 and applied mutation signature S162A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 298.15 K; buffer and pH stated in its Fig

table_label: Table 1: Summary of steady-state kinetic parameters for OAM and its active site variants with substrate D-ornithine and inhibitor 2,4-diaminobutyrate (BBA - Proteins and Proteomics 2017, 1865:1077-1084)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E3PY95 and applied mutation signature Y160F to reconstruct the assayed variant sequence.

column_label: Table 1: Summary of steady-state kinetic parameters for OAM and its active site variants with substrate D-ornithine and inhibitor 2,4-diaminobutyrate (BBA - Proteins and Proteomics 2017, 1865:1077-1084); Enzyme row 'Y160F': column 'kcat (s-1)' = 0.027; column 'Km (uM)' = 140; column 'kcat/Km x 103 (s-1 M-1)' = 0.19; column 'Ki (DABA) (uM)' = 2000 uM. The efficiency column is printed in units of 10^3 s-1 M-1, which is the same size as 1 s-1 mM-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.027 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.027 s^(-1); the exported value is 0.027 s^(-1). Km: printed Table 1 cell 140 uM; 140 / 1000 = 0.14 mM; the exported value is 0.14 mM. kcat/Km: printed Table 1 cell 0.19 in units of 10^3 s-1 M-1, that is 190 s-1 M-1; 1 s-1 M-1 is 0.001 s-1 mM-1, so the printed cell becomes 0.19 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed component cells is 0.027 / 0.14 = 0.19285714285714284 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Enzyme row 'Y160F': kcat = 0.027 s-1; Km = 140 uM; printed kcat/Km = 0.19 in the column's units of 10^3 s-1 M-1.

row_label: Table 1, Enzyme row 'Y160F', the printed kcat, Km and kcat/Km cells of that row


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E3PY95 and applied mutation signature Y187F to reconstruct the assayed variant sequence.

column_label: Table 1: Summary of steady-state kinetic parameters for OAM and its active site variants with substrate D-ornithine and inhibitor 2,4-diaminobutyrate (BBA - Proteins and Proteomics 2017, 1865:1077-1084); Enzyme row 'Y187F': column 'kcat (s-1)' = 0.12; column 'Km (uM)' = 31; column 'kcat/Km x 103 (s-1 M-1)' = 3.9; column 'Ki (DABA) (uM)' = 32 uM. The efficiency column is printed in units of 10^3 s-1 M-1, which is the same size as 1 s-1 mM-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.12 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.12 s^(-1); the exported value is 0.12 s^(-1). Km: printed Table 1 cell 31 uM; 31 / 1000 = 0.031 mM; the exported value is 0.031 mM. kcat/Km: printed Table 1 cell 3.9 in units of 10^3 s-1 M-1, that is 3900 s-1 M-1; 1 s-1 M-1 is 0.001 s-1 mM-1, so the printed cell becomes 3.9 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed component cells is 0.12 / 0.031 = 3.8709677419354835 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Enzyme row 'Y187F': kcat = 0.12 s-1; Km = 31 uM; printed kcat/Km = 3.9 in the column's units of 10^3 s-1 M-1.

row_label: Table 1, Enzyme row 'Y187F', the printed kcat, Km and kcat/Km cells of that row


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S11G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Archaeoglobus fulgidus

column_label: Primary PDF results prose, text lines 310-312: 3PGA Vmax 3.3 +/- 0.2 U/mg and Km 0.8 +/- 0.1 mM.

raw_value_unit_evidence: Results prose: Vmax 3.3 +/- 0.2 U mg^-1 and Km 0.8 +/- 0.1 mM for 3PGA.

row_label: A. fulgidus AF1751; 3PGA to 2PGA direction

table_label: Rate-dependence results prose


column_label: Primary PDF results prose, text lines 310-313: 2PGA Vmax 0.8 +/- 0.01 U/mg and Km 0.2 +/- 0.01 mM.

raw_value_unit_evidence: Results prose: Vmax 0.8 +/- 0.01 U mg^-1 and Km 0.2 +/- 0.01 mM for 2PGA.

row_label: A. fulgidus AF1751; 2PGA to 3PGA direction


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E3PY95 and applied mutation signature G339W with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

column_label: Table 2 (The steady-state kinetic parameters for wild-type OAM and variant forms); Table 2, classification 'Group B', enzyme row 'G339W'; column 'kcat' = 0.20; column 'Km' = 190; column 'kcat/Km' = 1.05, the table printing a single unit row x 10^3 M^-1 s^-1 above that column.

normalized_value_unit_evidence: kcat: printed cell 0.20 s^-1; no unit conversion applies, so the canonical value is 0.2 s^(-1). Km: printed cell 190 uM; 190 / 1000 = 0.19 mM. kcat/Km: printed cell 1.05 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.05 x 10^3 / 1000 = 1.05 s^-1 mM^-1. The exported kcat/Km 1.0526315789473684 s^(-1)*mM^(-1) is the exact quotient 0.2 / 0.19 of the two printed component cells of this same table line, and the printed efficiency cell is that quotient rendered at the table's own precision, so the exported ratio is kept as printed evidence of it.

raw_value_unit_evidence: Table 2, classification 'Group B', enzyme row 'G339W': printed kcat cell 0.20; printed Km cell 190; printed kcat/Km cell 1.05 carrying the table's own unit row x 10^3 M^-1 s^-1. Section 6 of the local extract resolves the kcat column as s^-1 and the Km column as uM from that printed unit row and from the arithmetic of all ten numeric rows of Tables 1 and 2.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E3PY95 and applied mutation signature C700S with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

column_label: Table 1 (The steady-state kinetic parameters for wild-type OAM and C700S variant before and after MTSL nitroxide spin labeling); Table 1, enzyme row 'C700S unlabeled' (cysteine residues labeled with MTSL: NA); column 'kcat' = 2.88; column 'Km' = 186; column 'kcat/Km' = 15.5, the table printing a single unit row x 10^3 M^-1 s^-1 above that column.

normalized_value_unit_evidence: kcat: printed cell 2.88 s^-1; no unit conversion applies, so the canonical value is 2.88 s^(-1). Km: printed cell 186 uM; 186 / 1000 = 0.186 mM. kcat/Km: printed cell 15.5 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 15.5 x 10^3 / 1000 = 15.5 s^-1 mM^-1. The exported kcat/Km 15.483870967741934 s^(-1)*mM^(-1) is the exact quotient 2.88 / 0.186 of the two printed component cells of this same table line, and the printed efficiency cell is that quotient rendered at the table's own precision, so the exported ratio is kept as printed evidence of it.

raw_value_unit_evidence: Table 1, enzyme row 'C700S unlabeled' (cysteine residues labeled with MTSL: NA): printed kcat cell 2.88; printed Km cell 186; printed kcat/Km cell 15.5 carrying the table's own unit row x 10^3 M^-1 s^-1. Section 6 of the local extract resolves the kcat column as s^-1 and the Km column as uM from that printed unit row and from the arithmetic of all ten numeric rows of Tables 1 and 2.

table_label: Table 1: the steady-state kinetic parameters measured with D-ornithine (J. Biol. Chem. 2014, 289(49):34161-34174)


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

proof_lines:
pH 7.0, 50°C
Raw SKiD Env: Temp=50°C, pH=7

source_databases_merged: brenda skid


organism: Brugia malayi


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S11A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


column_label: Primary article Section 3.3, Table 1, iPGM column; rows Km 2-PGA, kcat reverse, and Reverse kcat/Km.

normalized_value_unit_evidence: Km 0.097 mM; kcat 10 s^-1; explicit printed kcat/Km 100 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 iPGM column: Km 2-PGA 97 +/- 14 uM; kcat reverse 10 +/- 0.5 s^-1; reverse kcat/Km 1.0 x 10^5 M^-1 s^-1.

row_label: iPGM; reverse reaction; 2-PGA substrate


assay_conditions_summary: pH 7; 303.15 K; cofactor NADH


organism: Triticum aestivum


organism: Homo sapiens

substrate_name: 2,3-Bisphosphoglycerate; H2O

substrate: 2,3-Bisphosphoglycerate; H2O


substrate_name: H2O; 2,3-Bisphospho-D-glycerate

substrate: H2O; 2,3-Bisphospho-D-glycerate


organism: Geobacillus stearothermophilus

source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)

substrate_name: 3-phosphoglycerate (at pH 7.4, 37 degrees Celsius and in the presence of Mn(2+) and Co(2+))


substrate_name: 3-phosphoglycerate (at pH 7.4 and 25 degrees Celsius)


substrate_name: 2-phosphoglycerate (at pH 7.4 and 25 degrees Celsius)


organism: Zea mays


organism: Trypanosoma brucei


organism: Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF)

substrate_name: adenosylcobalamin (for recombinant alpha and beta subunits expressed together in E.coli to overcome presence of corrinoids in native system)

column_label: Metric label Km; row adenosylcobalamin; value 6.6 microM

raw_value_unit_evidence: adenosylcobalamin 6.6 microM

row_label: Km values for adenosylcobalamin and pyridoxal 5'-phosphate

table_label: Abstract


substrate_name: adenosylcobalamin (for recombinant alpha and beta subunits expressed together in E.coli to overcome the presence of corrinoids in native system)


enzyme_display_name: UniProt Q68G84

organism: Taxus chinensis

substrate_name: L-beta-phenylalanine

enzyme: UniProt Q68G84

substrate: L-beta-phenylalanine


enzyme_display_name: phenylalanine aminomutase (D-beta-phenylalanine forming)

organism: Pantoea agglomerans


enzyme: phenylalanine aminomutase (D-beta-phenylalanine forming)


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


organism: Amycolatopsis methanolica


organism: Wolbachia sp.

proof_lines: recombinant His-tagged enzyme, pH 7.5, 30°C


organism: Wolbachia endosymbiont of Dirofilaria immitis

proof_lines: in 30 mM Tris-HCl, 5 mM MgSO4, 20 mM KCl, pH 7.5, at 30°C


organism: Acetoanaerobium sticklandii

substrate_name: D-ornithine


organism: Escherichia coli

proof_lines: kcat is 330 sec(-1) for mutase with 3-PGA as substrate (at pH 7 and 30 degrees Celsius). kcat is 220 sec(-1) for mutase with 2-PGA as substrate (at pH 7 and 30 degrees Celsius).


enzyme_display_name: phenylalanine aminomutase (L-beta-phenylalanine forming)

substrate_name: trans-cinnamic acid

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

substrate: trans-cinnamic acid


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

enzyme: phenylalanine aminomutase (L-beta-phenylalanine forming)


enzyme_display_name: tyrosine 2,3-aminomutase

organism: Oryza sativa

substrate_name: L-tyrosine

proof_lines: alpha-tyrosine, pH 8.0, 29°C, recombinant mutant N446K

enzyme: tyrosine 2,3-aminomutase

substrate: L-tyrosine


substrate_name: L-phenylalanine

proof_lines: alpha-phenylalanine, pH 8.0, 29°C, recombinant mutant Y125C

substrate: L-phenylalanine


proof_lines: alpha-phenylalanine, pH 8.0, 29°C, recombinant mutant Y125C/N446K


proof_lines: alpha-tyrosine, pH 8.0, 29°C, recombinant mutant Y125C


proof_lines: alpha-phenylalanine, pH 8.0, 29°C, recombinant mutant N446K


proof_lines: alpha-phenylalanine, pH 8.0, 29°C, recombinant wild-type enzyme


proof_lines: alpha-tyrosine, pH 8.0, 29°C, recombinant wild-type enzyme


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


normalized_value_unit_evidence: kcat: printed cell 0.20 s^-1; no unit conversion applies, so the canonical value is 0.2 s^(-1). Km: printed cell 190 uM; 190 / 1000 = 0.19 mM. kcat/Km: printed cell 1.05 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.05 x 10^3 / 1000 = 1.05 s^-1 mM^-1. All three printed primary cells of this G339W line are proposed for this row: kcat 0.2 s^(-1), Km 0.19 mM and kcat/Km 1.05 s^(-1)*mM^(-1).

row_label: Table 2, classification 'Group B', enzyme row 'G339W'

substrate: D-ornithine


normalized_value_unit_evidence: kcat: printed cell 2.88 s^-1; no unit conversion applies, so the canonical value is 2.88 s^(-1). Km: printed cell 186 uM; 186 / 1000 = 0.186 mM. kcat/Km: printed cell 15.5 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 15.5 x 10^3 / 1000 = 15.5 s^-1 mM^-1. All three printed primary cells of this C700S line are proposed for this row: kcat 2.88 s^(-1), Km 0.186 mM and kcat/Km 15.5 s^(-1)*mM^(-1).

row_label: Table 1, enzyme row 'C700S unlabeled' (cysteine residues labeled with MTSL: NA)


organism: Cupriavidus crocatus

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: isochorismate synthase

organism: Arabidopsis thaliana

substrate_name: chorismate

enzyme: isochorismate synthase

substrate: chorismate


organism: Galium mollugo

substrate_name: isochorismate

substrate: isochorismate


substrate_name: Chorismate

proof_lines: kcat is 290 min(-1) for mutase activity with chorismate. kcat is 173 min(-1) for mutase activity with chorismate (at pH 7.8 and 37 degrees Celsius). kcat is 108 min(-1) for mutase activity with isochorismate (at pH 7.8 and 37 degrees Celsiu

substrate: Chorismate


substrate_name: Isochorismate

substrate: Isochorismate


proof_lines:
pH 8.0, 31°C, recombinant enzyme
Raw SKiD Env: Temp=31°C, pH=8


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

proof_lines: 25°C, pH not specified in the publication


organism: Taxus canadensis

proof_lines: kcat is 0.053 sec(-1) for L-phenylalanine.

source_databases_merged: skid uniprot


organism: Escherichia coli (strain K12)

substrate_name: isochorismate (at pH 7.5 and 37 degrees Celsius)

proof_lines: kcat is 213 min(-1) for mutase activity with chorismate. kcat is 176 min(-1) for mutase activity with chorismate in the presence of 30 mM of beta-mercaptoethanol (BME). kcat is 144.9 min(-1) for mutase activity with chorismate (at pH 7.5 an


substrate_name: magnesium

smiles: [Mg]

substrate: magnesium


organism: Chondromyces crocatus

substrate_name: L-Tyrosine

source_databases_merged: sabio_rk brenda uniprot

substrate: L-Tyrosine


proof_lines: mutant CmdF_MIYMLV, product (R)-beta-tyrosine

proof_lines: mutant CmdF_MIYMLV, product para-hydroxycinnamic acid


proof_lines: wild-type enzme, product para-hydroxycinnamic acid

proof_lines: wild-type enzme, product (R)-beta-tyrosine


substrate_name: DL-Ornithine

substrate: DL-Ornithine


sequence_variant_note: Mutation signature Y187F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Streptomyces maritimus


substrate_name: D-beta-phenylalanine

substrate: D-beta-phenylalanine


substrate_name: D-alpha-phenylalanine

substrate: D-alpha-phenylalanine


organism: Streptomyces globisporus


substrate_name: Unknown

substrate: Unknown


organism: Gallus gallus


organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

column_label: Primary PDF results prose, text lines 199-203 and Figure 1 caption lines 280-285: apparent Km 17 +/- 0.7 uM.

normalized_value_unit_evidence: Km 17 uM = 0.017 mM (uncertainty 0.0007 mM).

raw_value_unit_evidence: Results prose/Figure 1: apparent Km 17 +/- 0.7 uM for 2,3-bisphosphoglycerate; apparent Vmax 14 +/- 0.3 U mg^-1.

row_label: T. acidophilum TA1347; 2,3-bisphosphoglycerate cofactor dependence

table_label: Figure 1 and cofactor-dependence results prose


organism: Catharanthus roseus

column_label: Abstract states: The Km values for chorismate were 558 and 319 microM for isoforms I and II, respectively.

raw_value_unit_evidence: Km raw_value=319 raw_unit=microM

row_label: Catharanthus roseus isochorismate synthase isoform II with chorismate

table_label: PubMed abstract PMID 9952467


substrate_name: Mg(2+) (in the presence of 2 mM chorismate)


organism: Pantoea agglomerans


organism: Sus scrofa

sequence: IVYELDQALKPTKPMRFLGDEETVRKAMEAVAAQGKAK


organism: Streptomyces coelicolor


organism: Zymomonas mobilis


organism: Geobacillus stearothermophilus


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L104A to reconstruct the assayed variant sequence.


column_label: Table 3; row substrate 2 3'-methyl-alpha-phenylalanine; enzyme TcPAM (wild_type); columns K_M (M)x10^3, beta-kcat (s^-1), beta-kcat/K_M (M^-1 s^-1); cells 0.397 (+/-0.03), 0.022 (+/-0.002), 55 (+/-7).

normalized_value_unit_evidence: K_M 0.397 mM; beta-kcat 0.022 s^-1; beta-kcat/K_M 55 M^-1 s^-1 = 0.055 s^-1*mM^-1; exported kcat/K_M 0.0554156 is consistent with beta-kcat/K_M after table rounding or kcat/K_M recomputation from beta-kcat and K_M.

raw_value_unit_evidence: Table 3 row substrate 2 3'-methyl-alpha-phenylalanine; enzyme TcPAM (wild_type): K_M 0.397 (+/-0.03) mM; beta-kcat 0.022 (+/-0.002) s^-1; beta-kcat/K_M 55 (+/-7) M^-1 s^-1. Sibling columns: cin-kcat 0.017 (+/-0.002) s^-1; total kcat/K_M 98 (+/-20) M^-1 s^-1.

table_label: PMID 21361343 Table 3, TcPAM/PAMeLA_104 kinetic parameters


column_label: Table 3; row substrate 3 4'-methyl-alpha-phenylalanine; enzyme TcPAM (wild_type); columns K_M (M)x10^3, beta-kcat (s^-1), beta-kcat/K_M (M^-1 s^-1); cells 0.091 (+/-0.005), 0.030 (+/-0.002), 330 (+/-20).

normalized_value_unit_evidence: K_M 0.091 mM; beta-kcat 0.030 s^-1; beta-kcat/K_M 330 M^-1 s^-1 = 0.33 s^-1*mM^-1; exported kcat/K_M 0.32967 is consistent with beta-kcat/K_M after table rounding or kcat/K_M recomputation from beta-kcat and K_M.

raw_value_unit_evidence: Table 3 row substrate 3 4'-methyl-alpha-phenylalanine; enzyme TcPAM (wild_type): K_M 0.091 (+/-0.005) mM; beta-kcat 0.030 (+/-0.002) s^-1; beta-kcat/K_M 330 (+/-20) M^-1 s^-1. Sibling columns: cin-kcat 0.005 (+/-0.002) s^-1; total kcat/K_M 380 (+/-20) M^-1 s^-1.


substrate_name: styryl-alpha-alanine

substrate: styryl-alpha-alanine


substrate_name: L-Phenylalanine


column_label: Table 3; row substrate 1 alpha-phenylalanine / L-Phenylalanine; enzyme TcPAM (wild_type); columns K_M (M)x10^3, beta-kcat (s^-1), beta-kcat/K_M (M^-1 s^-1); cells 0.057 (+/-0.004), 0.053 (+/-0.01), 930 (+/-20).

normalized_value_unit_evidence: K_M 0.057 mM; beta-kcat 0.053 s^-1; beta-kcat/K_M 930 M^-1 s^-1 = 0.93 s^-1*mM^-1; exported kcat/K_M 0.929825 is consistent with beta-kcat/K_M after table rounding or kcat/K_M recomputation from beta-kcat and K_M.

raw_value_unit_evidence: Table 3 row substrate 1 alpha-phenylalanine / L-Phenylalanine; enzyme TcPAM (wild_type): K_M 0.057 (+/-0.004) mM; beta-kcat 0.053 (+/-0.01) s^-1; beta-kcat/K_M 930 (+/-20) M^-1 s^-1. Sibling columns: cin-kcat 0.012 (+/-0.002) s^-1; total kcat/K_M 1100 (+/-100) M^-1 s^-1.


organism: Dirofilaria immitis


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

assay_conditions_summary: pH 8

proof_lines: kcat is 2.6 min(-1) for isochorismate pyruvate lyase activity (at pH 8 and 37 degrees Celsius). kcat is 2.8 min(-1) for salicylate synthase activity (at pH 8 and 37 degrees Celsius). kcat is 3.1 min(-1) for isochorismate synthase activity (


organism: Caenorhabditis elegans


enzyme_display_name: glutamate 2,3-aminomutase

organism: Clostridioides difficile (strain 630)

substrate_name: L-glutamate

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

proof_lines: kcat is 6.1 sec(-1) with L-glutamate as substrate.

enzyme: glutamate 2,3-aminomutase

substrate: L-glutamate


organism: Trypanosoma brucei


enzyme_display_name: (hydroxyamino)benzene mutase

organism: Ectopseudomonas oleovorans

substrate_name: hydroxylaminobenzene (at pH 7)

enzyme: (hydroxyamino)benzene mutase

substrate: hydroxylaminobenzene (at pH 7)


organism: Bacillus subtilis


organism: Pyrococcus furiosus

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

assay_conditions_summary: pH 8; buffer 200 mM Tris-maleate

column_label: Table 1 lists PF1959 Km 3-phosphoglycerate (mM) = 0.49 +/- 0.06.

raw_value_unit_evidence: Km raw_value=0.49 +/- 0.06 mM raw_unit=mM

row_label: Km 3-phosphoglycerate (mM), PF1959 / P. furiosus column

table_label: Oxford Academic Table 1: The iPGMs of the archaea P. furiosus and M. jannaschii


organism: Onchocerca volvulus

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


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A213K to reconstruct the assayed variant sequence.


organism: Taxus chinensis

substrate_name: L-phenylalanine


organism: Saccharomyces cerevisiae

assay_conditions_summary: cofactor NADPH

column_label: Table 2; reaction GPM; isoenzyme Gpm1p; parameter kcat value 400 s^-1; parameter Kp2g value 1.41 mM; kcat/Km computed from those explicit cells

normalized_value_unit_evidence: kcat normalized_value=400 normalized_unit=s^-1; Km normalized_value=1.41 normalized_unit=mM; kcat/Km normalized_value=283.68794326241135 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=400 raw_unit=s^-1; Km raw_value=1.41 raw_unit=mM; kcat/Km computed from explicit Table 2 cells 400/1.41 raw_unit=s^-1*mM^-1

row_label: GPM / Gpm1p / Kp2g

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


assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH


organism: Streptomyces globisporus


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


proof_lines: pH and temperature not specified in the publication, recombinant mutant L97G/C89T


substrate_name: L-beta-phenylalanine

substrate: L-beta-phenylalanine


substrate_name: L-tyrosine

substrate: L-tyrosine


proof_lines: pH and temperature not specified in the publication, recombinant mutant L97G


substrate: L-phenylalanine


substrate_name: L-beta-tyrosine

substrate: L-beta-tyrosine


organism: Mus musculus


organism: Acetoanaerobium sticklandii

substrate_name: D-ornithine

proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant E81D

substrate: D-ornithine


proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant E81A


proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant E81Q


proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant R297K


proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant N226D


substrate_name: chorismate

proof_lines: mutant enzyme F327Y/I346L, in 100 mM phosphate pH 7.0, 10 mM MgCl2

substrate: chorismate


proof_lines: mutant enzyme A303T, in 100 mM phosphate pH 7.0, 10 mM MgCl2


proof_lines: mutant enzyme F327Y, in 100 mM phosphate pH 7.0, 10 mM MgCl2


proof_lines: mutant enzyme F359Q/I346L, in 100 mM phosphate pH 7.0, 10 mM MgCl2


proof_lines: mutant enzyme F327Y/F359Q, in 100 mM phosphate pH 7.0, 10 mM MgCl2


proof_lines: mutant enzyme I346L, in 100 mM phosphate pH 7.0, 10 mM MgCl2


proof_lines: mutant enzyme F359Q, in 100 mM phosphate pH 7.0, 10 mM MgCl2


organism: Pseudomonas aeruginosa


organism: Cupriavidus metallidurans

assay_conditions_summary: pH 8.8; 303.15 K; buffer. Assay condition: Tris

column_label: Table 1 (Kinetic parameters for enzymes characterized in this study), Table 1, row CmTAL wt; column 'K_M [uM]' = 348; column 'kcat [s^-1] (L-Tyr to beta-Tyr)' = 0.9 x 10^-3; column 'kcat [s^-1] (L-Tyr to pHCA)' = 0.011 s^-1; the table has no kcat/Km column.

normalized_value_unit_evidence: Km: printed Table 1 cell 348 uM; 348 / 1000 = 0.348 mM; the exported value is 0.348 mM. kcat: printed Table 1 cell 0.9 x 10^-3 s^-1; the cell is already in s^-1, so no unit conversion applies; the exported value is 0.0009 s^(-1). kcat/Km: Table 1 prints no efficiency cell; the exported value is the full-precision same-measurement quotient 0.0009 / 0.348 = 0.002586206896551724 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row CmTAL wt, column 'kcat [s^-1] (L-Tyr to beta-Tyr)' = 0.9 x 10^-3; column 'K_M [uM]' = 348. Table 1 prints no kcat/Km column, so no efficiency cell is quoted.

row_label: Table 1, row CmTAL wt, aminomutase channel column kcat [s^-1] (L-Tyr to beta-Tyr)

table_label: Table 1: Kinetic parameters for enzymes characterized in this study and comparison to the known aminomutase SgcC4 (ChemBioChem 2009, 10, 741-750)


organism: Chondromyces crocatus


enzyme_display_name: pancreatic ribonuclease

organism: Bos taurus

substrate_name: cytidine-2',3'-cyclic monophosphate

enzyme: pancreatic ribonuclease

substrate: cytidine-2',3'-cyclic monophosphate


enzyme_display_name: methylmalonyl-CoA mutase

organism: Ovis aries

substrate_name: succinyl-CoA

enzyme: methylmalonyl-CoA mutase

substrate: succinyl-CoA


substrate_name: L-Dopa

substrate: L-Dopa


enzyme_display_name: protein disulfide-isomerase

substrate_name: ribonuclease

proof_lines: dithiothreitol, with scrambled ribonuclease as substrate

proof_lines: scrambled, with dithiothreitol as substrate

enzyme: protein disulfide-isomerase

substrate: ribonuclease


smiles: C(CS)O

proof_lines: with scrambled ribonuclease as substrate


substrate_name: cysteine

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

proof_lines: GSH, with scrambled ribonuclease as substrate

substrate: cysteine


enzyme_display_name: thromboxane-A synthase

organism: Homo sapiens

substrate_name: prostaglandin H3

enzyme: thromboxane-A synthase

substrate: prostaglandin H3


substrate_name: prostaglandin G2

substrate: prostaglandin G2


substrate_name: Prostaglandin H1

substrate: Prostaglandin H1


proof_lines: recombinant His-tagged mutant E338D, pH 7.5, 30°C

proof_lines: recombinant beta-subunit mutant E338D, pH 8.5, 25°C


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

proof_lines: pH 8.5, 20°C, recombinant wild-type enzyme


proof_lines: recombinant His-tagged mutant E338Q, pH 7.5, 30°C

proof_lines: recombinant beta-subunit mutant E338Q, pH 8.5, 25°C


sequence_source: UniProtKB E3PY95

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -2, so it is treated as a source-provided variant sequence.

proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant P343W


sequence_variant_note: Mutation signature E338A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant E338A

proof_lines: recombinant His-tagged mutant E338A, pH 7.5, 30°C

proof_lines: recombinant beta-subunit mutant E338A, pH 8.5, 25°C


sequence_variant_note: Mutation signature I424E could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant I424E


sequence_variant_note: Mutation signature D627A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.5, 25°C, recombinant beta-subunit mutant D627A


enzyme_display_name: protoporphyrin ferrochelatase

organism: Rattus norvegicus

substrate_name: mesoporphyrin IX

enzyme: protoporphyrin ferrochelatase

substrate: mesoporphyrin IX


substrate_name: protoporphyrin IX

substrate: protoporphyrin IX


organism: Propionibacterium freudenreichii subsp. shermanii

assay_conditions_summary: cofactor CoA


organism: Colletotrichum gloeosporioides

substrate_name: palmitoleate

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

proof_lines: recombinant enzyme, whole enzyme activity, pH 6.5, 40°C

substrate: palmitoleate


substrate_name: oleate

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

substrate: oleate


substrate_name: alpha-linolenate

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

substrate: alpha-linolenate


smiles: CCCCCC=CCC=CC(CCCCCCC(=O)O)OO


enzyme_display_name: methylaspartate mutase

organism: Clostridium tetanomorphum

substrate_name: adenosylcobalamin

proof_lines: kcat is 20.6 sec(-1) for mutase activity with L-glutamate.

enzyme: methylaspartate mutase

substrate: adenosylcobalamin


substrate_name: L-glutamate

substrate: L-glutamate


organism: Streptomyces ansochromogenes

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


organism: Mammalia


substrate_name: methylmalonyl-carba(dethia)-coenzyme A

substrate: methylmalonyl-carba(dethia)-coenzyme A


organism: Escherichia coli

substrate_name: Chorismate

substrate: Chorismate


sequence_variant_note: Mutation signature H610A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: 310.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H610A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H610N to reconstruct the assayed variant sequence.


substrate_name: methylmalonyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y89F to reconstruct the assayed variant sequence.

substrate: methylmalonyl-CoA


enzyme_display_name: 3-(hydroxyamino)phenol mutase

organism: Cupriavidus necator

proof_lines: The values are approximate data due to the instability of the substrate.

enzyme: 3-(hydroxyamino)phenol mutase


enzyme_display_name: geraniol isomerase

organism: Castellaniella defragrans

substrate_name: geraniol

smiles: CC(=CCCC(=CCO)C)C

assay_conditions_summary: pH 9

proof_lines: kcat is 4.37 min(-1) for linalool dehydration. kcat is 9.0 min(-1) for beta-myrcene hydration. kcat is 1.66 min(-1) for geraniol isomerization.

enzyme: geraniol isomerase

substrate: geraniol


substrate_name: Unknown

substrate: Unknown


organism: Caenorhabditis elegans

proof_lines: with apo-enzyme, pH 7.0, temperature not specified in the publication


organism: Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197)


organism: Castellaniella defragrans (strain DSM 12143 / CCUG 39792 / 65Phen)


organism: Emericella nidulans


organism: Gaeumannomyces graminis


enzyme_display_name: hydroperoxy icosatetraenoate isomerase

substrate_name: synthetic fatty acid 9E,11Z,14Z-20:3omega6 (at pH 7.5)

proof_lines: Has a 5 to 10 fold higher activity toward (12R)-HPETE (hydroperoxyeicosatetraenoic acid) compared to (12S)-HPETE and (15S)-HPETE (PubMed:12881489). From (12R)-HPETE produces a stereoisomer of hepoxilin A3 (PubMed:12881489). More active on h

enzyme: hydroperoxy icosatetraenoate isomerase


enzyme_display_name: linalool isomerase

organism: Thauera linaloolentis (strain DSM 12138 / JCM 21573 / CCUG 41526 / CIP 105981 / IAM 15112 / NBRC 102519 / 47Lol)

enzyme: linalool isomerase


assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


sequence_variant_note: Mutation signature Y89A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y89F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Clostridium cochlearium

substrate_name: L-Glutamate

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

substrate: L-Glutamate


substrate_name: Coenzyme B12

substrate: Coenzyme B12


organism: Taxus canadensis

substrate_name: styryl-alpha-alanine

substrate: styryl-alpha-alanine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


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


smiles: CC/C=C\C/C=C\C/C=C\CCCCCCCC(=O)O


smiles: CCCCCCCC/C=C\CCCCCCCC(=O)O


smiles: CCCCCC/C=C\CCCCCCCC(=O)O


substrate_name: palmitoleic acid

smiles: CCCCCCC=CCCCCCCCC(=O)O

column_label: Table 3. Kinetic parameters for different substrates; row 16:1delta9Z; column Km = 5.00 +/- 0.85 umol/liter

raw_value_unit_evidence: Table 3 row 16:1delta9Z (palmitoleic acid); Km = 5.00 +/- 0.85 umol/liter

substrate: palmitoleic acid


substrate_name: oleic acid

smiles: CCCCCCCC=CCCCCCCCCC(=O)O

column_label: Table 3. Kinetic parameters for different substrates; row 18:1delta9Z; column Km = 6.71 +/- 0.74 umol/liter

raw_value_unit_evidence: Table 3 row 18:1delta9Z (oleic acid); Km = 6.71 +/- 0.74 umol/liter

substrate: oleic acid


substrate_name: linoleic acid

smiles: CCCCCC=CCC=CCCCCCCCC(=O)O

column_label: Table 3. Kinetic parameters for different substrates; row 18:2delta9Z,12Z; column Km = 18.30 +/- 2.6 umol/liter

raw_value_unit_evidence: Table 3 row 18:2delta9Z,12Z (linoleic acid); Km = 18.30 +/- 2.6 umol/liter

substrate: linoleic acid


substrate_name: alpha-linolenic acid

smiles: CCC=CCC=CCC=CCCCCCCCC(=O)O

column_label: Table 3. Kinetic parameters for different substrates; row 18:3delta9Z,12Z,15Z; column Km = 22.6 +/- 4.3 umol/liter

raw_value_unit_evidence: Table 3 row 18:3delta9Z,12Z,15Z (alpha-linolenic acid); Km = 22.6 +/- 4.3 umol/liter

substrate: alpha-linolenic acid


substrate_name: oxygen

smiles: O=O

column_label: Abstract reports Km values were 8 microM for linoleic acid and 30 microM for oxygen.

raw_value_unit_evidence: Km raw_value=30 microM raw_unit=microM

row_label: Gaeumannomyces graminis linoleate 8-dioxygenase / oxygen

table_label: PubMed XML abstract PMID 8662736

substrate: oxygen


raw_value_unit_evidence: Km raw_value=8 microM raw_unit=microM

row_label: Gaeumannomyces graminis linoleate 8-dioxygenase / linoleic acid


organism: Homo sapiens

substrate_name: adenosylcob(III)alamin

substrate: adenosylcob(III)alamin


substrate_name: L-glutamate

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


proof_lines:
23°C, wild-type enzyme
25°C, wild-type enzyme


assay_conditions_summary: pH 8.5; 298.15 K; cofactor CoA


organism: Mus musculus


substrate_name: (R)-methylmalonyl-CoA

proof_lines: recombinant His-tagged mutant E392D, pH 8.5, 25°C

substrate: (R)-methylmalonyl-CoA


proof_lines: recombinant His-tagged mutant E392Q, pH 8.5, 25°C


proof_lines: recombinant His-tagged mutant E392A, pH 8.5, 25°C


proof_lines: recombinant His-tagged wild-type enzyme, pH 8.5, 25°C


organism: Rhizobium meliloti (strain 1021)

substrate_name: (R,S)-methylmalonyl-CoA (in the presence of 3 mM NH4(+))


organism: Propionibacterium freudenreichii subsp. shermanii

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA


substrate_name: Ethylmalonyl-CoA

substrate: Ethylmalonyl-CoA


organism: Euglena gracilis

assay_conditions_summary: pH 7.5; buffer 100 mM potassium phosphate; cofactor CoA

column_label: Results prose reports apparent Km values of 55.8 uM for (R,S)-methylmalonyl-CoA, 27.9 uM for R-methylmalonyl-CoA, and 347.4 uM for succinyl-CoA in the reverse reaction.

raw_value_unit_evidence: Km raw_value=27.9 raw_unit=uM

row_label: Euglena methylmalonyl-CoA mutase forward reaction

table_label: Springer/PDF Results prose - Some properties of Euglena MCM


substrate_name: succinyl-CoA

raw_value_unit_evidence: Km raw_value=347.4 raw_unit=uM

row_label: Euglena methylmalonyl-CoA mutase reverse reaction

substrate: succinyl-CoA


enzyme_display_name: cysteine-S-conjugate beta-lyase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: L-cystathionine

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

enzyme: cysteine-S-conjugate beta-lyase

substrate: L-cystathionine


substrate_name: L-cysteine

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

substrate: L-cysteine


substrate_name: L-cystine

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

substrate: L-cystine


enzyme_display_name: L-3-cyanoalanine synthase

organism: Spinacia oleracea

enzyme: L-3-cyanoalanine synthase


substrate_name: chloroalanine

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

proof_lines:
vs. L-cysteine
26°C, pH 9.8

substrate: chloroalanine


substrate_name: Unknown

proof_lines:
vs. O-acetyl-L-serine
vs. chloroalanine
vs. L-cysteine

substrate: Unknown


organism: Thauera linaloolentis

substrate_name: geraniol

column_label: Abstract reports a specific activity of 3.42+/-0.28 nkat mg protein(-1) and a kM value of 455+/-124 microM for the thermodynamically favored isomerization of geraniol to both linalool isomers at pH 8 and 35 C.

raw_value_unit_evidence: Km raw_value=455+/-124 microM raw_unit=microM

row_label: Thauera linaloolentis 47Lol linalool isomerase / geraniol

table_label: PubMed XML abstract PMID 26979141

substrate: geraniol


assay_conditions_summary: 298.15 K; cofactor CoA


substrate_name: beta-myrcene

smiles: CC(=CCCC(=C)C=C)C

substrate: beta-myrcene


organism: Sus scrofa

substrate_name: hemin

substrate: hemin


substrate_name: mesoporphyrin IX

substrate: mesoporphyrin IX


substrate_name: protoporphyrin

substrate: protoporphyrin


substrate_name: mesoporphyrin

substrate: mesoporphyrin


proof_lines:
cosubstrate protoporphyrin
cosubstrate mesoporphyrin


substrate: L-glutamate


enzyme_display_name: UniProt A9S498

organism: Physcomitrium patens

substrate_name: chorismate

enzyme: UniProt A9S498

substrate: chorismate


enzyme_display_name: UniProt P39912

organism: Bacillus subtilis

enzyme: UniProt P39912


enzyme_display_name: UniProt Q48485

organism: Klebsiella pneumoniae

substrate_name: UDP-D-galactopyranose

enzyme: UniProt Q48485

substrate: UDP-D-galactopyranose


enzyme_display_name: UniProt Q4W1X2

organism: Aspergillus fumigatus

substrate_name: UDP-beta-L-arabinofuranose

enzyme: UniProt Q4W1X2

substrate: UDP-beta-L-arabinofuranose


smiles: CCCCCC=CCC(C=CC=CCC=CCCCC(=O)[O-])OO


smiles: CCCCCC(C=CC=CCC=CCC=CCCCC(=O)[O-])OO


enzyme_display_name: lactoylglutathione lyase

organism: Trypanosoma cruzi

substrate_name: glutathionylspermidine

proof_lines:
with phenylglyoxal
with methylglyoxal

enzyme: lactoylglutathione lyase

substrate: glutathionylspermidine


substrate_name: trypanothione

proof_lines: pH and temperature not specified in the publication

substrate: trypanothione


substrate_name: glutathione

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

proof_lines:
with methylglyoxal
with phenylglyoxal

substrate: glutathione


enzyme_display_name: phosphoacetylglucosamine mutase

organism: Aedes aegypti

enzyme: phosphoacetylglucosamine mutase


enzyme_display_name: methionine gamma-lyase

organism: Streptomyces avermitilis

enzyme: methionine gamma-lyase

substrate: L-cysteine


substrate_name: L-homocysteine

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

substrate: L-homocysteine


substrate_name: L-methionine

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

substrate: L-methionine


organism: Aspergillus niger


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


enzyme_display_name: methylmalonyl-CoA mutase

organism: Homo sapiens

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

enzyme: methylmalonyl-CoA mutase


enzyme_display_name: chorismate mutase

organism: Kitasatospora aureofaciens

enzyme: chorismate mutase


enzyme_display_name: 2-acetolactate mutase

organism: Mycobacterium tuberculosis

enzyme: 2-acetolactate mutase


enzyme_display_name: lanosterol synthase

enzyme: lanosterol synthase


organism: Ustilago maydis

substrate_name: Chorismate

substrate: Chorismate


substrate_name: Unknown

substrate: Unknown


organism: Propionibacterium freudenreichii subsp. shermanii

substrate_name: succinyl-CoA

proof_lines: kcat is 48 sec(-1) with succinyl-CoA as substrate.

substrate: succinyl-CoA


organism: Ruta graveolens

proof_lines:
enzyme form CM2
enzyme CM1


enzyme_display_name: cycloartenol synthase

organism: Isodon japonicus

enzyme: cycloartenol synthase


organism: Poterioochromonas malhamensis


organism: Archaeoglobus fulgidus


enzyme_display_name: UDP-galactopyranose mutase

organism: Deinococcus radiodurans

substrate_name: UDP-galactopyranose

assay_conditions_summary: pH 7; buffer pH 7

proof_lines: wild type enzyme, in 50 mM sodium phosphate buffer pH 7.0

enzyme: UDP-galactopyranose mutase

substrate: UDP-galactopyranose


organism: Lathyrus oleraceus


organism: Ogataea angusta

proof_lines:
37°C, in presence of 0.1 mM tyrosine
37°C
37°C, in presence of 0.01 mM tryptophan


organism: Corynebacterium glutamicum


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88L/G89A/H90M with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88N/G89A/H90M with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V11L/D15V/K40Q/T52P/V55D/V62I/D72V/R87P/L88D/G89A/H90M with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T52P/V55D/L88D with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 30°C, mutant enzyme T52P/V55D/L88D


enzyme_display_name: geraniol isomerase

organism: Castellaniella defragrans (strain DSM 12143 / CCUG 39792 / 65Phen)

substrate_name: linalool

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

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

proof_lines: kcat is 4.37 min(-1) for linalool dehydration. kcat is 9.0 min(-1) for beta-myrcene hydration. kcat is 1.66 min(-1) for geraniol isomerization.

enzyme: geraniol isomerase

substrate: linalool


organism: Aspergillus fumigatus

substrate_name: UDP-alpha-D-galactofuranose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N207A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, recombinant mutant N207A

substrate: UDP-alpha-D-galactofuranose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y104A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, recombinant mutant Y104A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y317A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, recombinant mutant Y317A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q4W1X2 and applied mutation signature Q107A to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for UGM Variants (Biochemistry 2014, 53, 7794-7804); printed column heads mutants | kcat, s-1 | KM (uM) | kcat/KM, M-1 s-1 | relative change. Table 2, AfUGM section, mutant row Q107A; column KM (uM) = 2153; column kcat, s-1 = 4.7; column kcat/KM, M-1 s-1 = 2000; column relative change = 0.003. captured primary segment: UDP-Galf | AfUGMQ107A | Km 2153 uM | kcat 4.7 s^-1 | kcat/Km 2000 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 2153 uM; 1 uM is 1/1000 mM, so 2153 / 1000 = 2.153 mM. kcat: printed Table 2 kcat cell 4.7 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 4.7 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 2000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2000 / 1000 = 2.0 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 4.7 / 2.153 = 2.183000464468184 s^-1 mM^-1, alongside the printed catalytic-efficiency cell 2.0 s^-1 mM^-1 that Table 2 fits and reports in its own right.

raw_value_unit_evidence: Table 2, AfUGM section, mutant row Q107A: KM = 2153 uM; kcat = 4.7 s^-1; kcat/KM = 2000 M^-1 s^-1; relative change = 0.003.


assay_conditions_summary: pH 7

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

proof_lines: pH 7.0, 37°C, recombinant wild-type enzyme


organism: Enterobacter agglomerans

substrate_name: chorismate (at 32 degrees Celsius)

column_label: Table 5 reports Erwinia herbicola Km (uM) = 169; table footnote states reaction kinetics were monitored at 32 C.

raw_value_unit_evidence: Km raw_value=169 raw_unit=uM

row_label: Erwinia herbicola

table_label: Table 5 - Kinetic constants, pI and Mw of *AroQ enzymes

substrate: chorismate (at 32 degrees Celsius)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: isochorismate (for isochorismate pyruvate lyase activity at pH 8 and 37 degrees Celsius)

proof_lines: kcat is 2.6 min(-1) for isochorismate pyruvate lyase activity (at pH 8 and 37 degrees Celsius). kcat is 2.8 min(-1) for salicylate synthase activity (at pH 8 and 37 degrees Celsius). kcat is 3.1 min(-1) for isochorismate synthase activity (


substrate_name: chorismate (for chorismate mutase activity without magnesium at pH 7.5 and 37 degrees Celsius)


organism: Bacillus subtilis

substrate_name: chorismate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K111N/A112S/V113N to reconstruct the assayed variant sequence.

proof_lines: 30°C, pH 7.5, mutant DELTA118-127/K111N/A112S/V113N, with 4 mM substrate

substrate: chorismate


organism: Trypanosoma cruzi

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q5EEK1 and applied mutation signature Y100A to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for UGM Variants (Biochemistry 2014, 53, 7794-7804); printed column heads mutants | kcat, s-1 | KM (uM) | kcat/KM, M-1 s-1 | relative change. Table 2, TcUGM section, mutant row Y100A; column KM (uM) = 32; column kcat, s-1 = 0.03; column kcat/KM, M-1 s-1 = 800; column relative change = 0.008. captured primary segment: UDP-Galf | TcUGMY100A | Km 32 uM | kcat 0.03 s^-1 | kcat/Km 800 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 32 uM; 1 uM is 1/1000 mM, so 32 / 1000 = 0.032 mM. kcat: printed Table 2 kcat cell 0.03 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.03 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 800 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 800 / 1000 = 0.8 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 0.03 / 0.032 = 0.9375 s^-1 mM^-1, alongside the printed catalytic-efficiency cell 0.8 s^-1 mM^-1 that Table 2 fits and reports in its own right.

raw_value_unit_evidence: Table 2, TcUGM section, mutant row Y100A: KM = 32 uM; kcat = 0.03 s^-1; kcat/KM = 800 M^-1 s^-1; relative change = 0.008.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q103A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, recombinant mutant Q103A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y317A to reconstruct the assayed variant sequence.


column_label: Table 2: Steady-State Kinetic Parameters for UGM Variants (Biochemistry 2014, 53, 7794-7804); printed column heads mutants | kcat, s-1 | KM (uM) | kcat/KM, M-1 s-1 | relative change. Table 2, TcUGM section, row Wild-type; column KM (uM) = 140; column kcat, s-1 = 13.4; column kcat/KM, M-1 s-1 = 90000; column relative change = 1. captured primary segment: UDP-Galf | TcUGM wild-type | Km 140 uM | kcat 13.4 s^-1 | kcat/Km 90000 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 140 uM; 1 uM is 1/1000 mM, so 140 / 1000 = 0.14 mM. kcat: printed Table 2 kcat cell 13.4 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 13.4 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 90000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 90000 / 1000 = 90.0 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 13.4 / 0.14 = 95.71428571428571 s^-1 mM^-1, alongside the printed catalytic-efficiency cell 90.0 s^-1 mM^-1 that Table 2 fits and reports in its own right.

raw_value_unit_evidence: Table 2, TcUGM section, row Wild-type: KM = 140 uM; kcat = 13.4 s^-1; kcat/KM = 90000 M^-1 s^-1; relative change = 1.

row_label: Table 2, TcUGM section, row Wild-type


organism: Methanocaldococcus jannaschii

proof_lines: kcat is 5.7 sec(-1) (at 30 degrees Celsius).


organism: Escherichia coli (strain K12)

substrate_name: prephenate (at pH 7.8 and at 37 degrees Celsius)

proof_lines: kcat is 72 sec(-1) at pH 7.5. kcat is 31 sec(-1) at pH 4.9.


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: isochorismate (at pH 7.5 and 30 degrees Celsius)

proof_lines: kcat is 1.01 sec(-1) for lyase activity (at pH 7.5 and 22 degrees Celsius). kcat is 23.5 sec(-1) for chorismate mutase activity (at pH 7.5 and 22 degrees Celsius). kcat is 106 min(-1) for lyase activity (at pH 7 and 30 degrees Celsius). kca


organism: Pseudomonas aeruginosa


organism: Aspergillus nidulans

proof_lines: 30°C, pH 7.6, in presence of 0.005 mM tryptophan

proof_lines: 30°C, pH 7.6, in presence of 0.005 mM tyrosine


organism: Mycobacterium tuberculosis


organism: Salmonella typhimurium


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: chorismate (at 30 degrees Celsius)

proof_lines: kcat is 176 sec(-1) for chorismate (PubMed:2187528). kcat is 176 sec(-1) for chorismate (in the presence of 10 uM of tryptophan) (PubMed:2187528). kcat is 348 sec(-1) for chorismate (in the presence of 10 uM of tryptophan and at 30 degrees

substrate: chorismate (at 30 degrees Celsius)


organism: Yersinia pestis

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.5
kcat is 70 sec(-1).


substrate_name: UDP-D-galactofuranose

proof_lines: in 25 mM HEPES, 125 mM NaCl, 20 mM dithionite, pH 7.5, at 37°C

substrate: UDP-D-galactofuranose


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H131A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; 303.15 K; buffer a three-component

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H131A, mutase activity, chorismate column group; column KM (uM) = 53 ± 10; column kcat (s^-1) = 7.2 ± 0.4; column kcat/KM (M^-1 s^-1) = 1.4 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 7.2 s^-1; already in s^-1, no conversion; the exported value is 7.2 s^(-1). Km: printed Table 3 cell 53 uM; 53 / 1000 = 0.053 mM; the exported value is 0.053 mM. kcat/Km: printed Table 3 cell 1.4 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 140000.0 / 1000 = 140.0 s^-1 mM^-1; the exported value is 135.8490566037736 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H131A, mutase activity, chorismate column group: KM = 53 ± 10 uM; kcat = 7.2 ± 0.4 s^-1; printed kcat/KM = 1.4 x 10^5 M^-1 s^-1.

table_label: Table 3: Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C (Biochemistry 1998, 37(45):15703-15712)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H153N to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H153N, mutase activity, chorismate column group; column KM (uM) = 51 ± 10; column kcat (s^-1) = 10 ± 0.5; column kcat/KM (M^-1 s^-1) = 2.0 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 10 s^-1; already in s^-1, no conversion; the exported value is 10.0 s^(-1). Km: printed Table 3 cell 51 uM; 51 / 1000 = 0.051 mM; the exported value is 0.051 mM. kcat/Km: printed Table 3 cell 2.0 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 200000.0 / 1000 = 200.0 s^-1 mM^-1; the exported value is 196.07843137254903 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H153N, mutase activity, chorismate column group: KM = 51 ± 10 uM; kcat = 10 ± 0.5 s^-1; printed kcat/KM = 2.0 x 10^5 M^-1 s^-1.


organism: Leishmania major


enzyme_display_name: 2-methyleneglutarate mutase

organism: Eubacterium barkeri

enzyme: 2-methyleneglutarate mutase


organism: Bos taurus


organism: Aspergillus fumigatus

substrate_name: UDP-alpha-D-galactopyranose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R182A to reconstruct the assayed variant sequence.

substrate: UDP-alpha-D-galactopyranose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R327K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R182K to reconstruct the assayed variant sequence.


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


organism: Arabidopsis thaliana

assay_conditions_summary: pH 8

proof_lines: kcat is 16.1 sec(-1) with chorismate as substrate (at pH 8).


proof_lines:
dimeric chorismate mutase, at 20°C
monomeric chorismate mutase, at 20°C


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Mycosarcoma maydis


organism: Trypanosoma cruzi

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R176A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y395F with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y317F with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R327A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y429F with inferred residue-numbering offset -10 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.


organism: Thermus thermophilus


organism: Pneumocystis carinii

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


proof_lines: pH and temperature not specified in the publication, recombinant mutant F66A


proof_lines: pH 7.0, 25°C, recombinant detagged enzyme


proof_lines: pH and temperature not specified in the publication, recombinant mutant N201A


organism: Methanocaldococcus jannaschii

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q88N with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 293.15 K; buffer PBS

proof_lines: mutant enzyme Q88N, in PBS buffer (pH 7.5) at 20°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F77W with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F77W, in PBS buffer (pH 7.5) at 20°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V35A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V35A, in PBS buffer (pH 7.5) at 20°C


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -7, so it is treated as a source-provided variant sequence.

proof_lines: mutant enzyme D48G, in PBS buffer (pH 7.5) at 20°C


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.

proof_lines: mutant enzyme R51Q, in PBS buffer (pH 7.5) at 20°C


proof_lines: wild type enzyme, in PBS buffer (pH 7.5) at 20°C


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

column_label: Table 5 reports Pseudomonas aeruginosa Km (uM) = 98; table footnote states reaction kinetics were monitored at 32 C.

raw_value_unit_evidence: Km raw_value=98 raw_unit=uM

row_label: Pseudomonas aeruginosa


proof_lines: kcat is 38.7 sec(-1) with chorismate as substrate (at pH 8).


proof_lines: Does not follow Michaelis-Menten kinetics but displays a positive cooperativity with a Hill coefficient of 2.1 indicating that substrate binding at one active site of the homodimer enhances interaction at the second active site (PubMed:2516


organism: Pichia angusta

substrate_name: chorismate (in the presence of 10 uM tryptophan and at 37 degrees Celsius)

column_label: PMC101906 results prose reports that 10 uM tryptophan produced Michaelis-Menten-type kinetics with Km 1.6 mM for chorismate mutase.

raw_value_unit_evidence: Results prose reports Michaelis-Menten-type kinetics with Km raw_value=1.6 raw_unit=mM in the presence of 10 uM tryptophan.

row_label: Purified H. polymorpha HARO7 chorismate mutase with 10 uM tryptophan

table_label: PMC101906 results prose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W315A to reconstruct the assayed variant sequence.


column_label: Table 1 of Biochemistry 2018, 57(26):3713-3721; the printed metric rows are 'kcat (s-1)', 'KM (uM)' and 'kcat/KM (M-1 s-1)'; the enzyme heading read here is 'AfUGM' and the substrate column head under it is 'UDP-Galf'; that column prints kcat 100 s^-1, KM 450 uM and kcat/KM 230000 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 100 s^-1; the printed unit is already the canonical unit, so no unit conversion applies; canonical value 100.0 s^(-1). Km: printed Table 1 cell 450 uM; 450 / 1000 = 0.45; canonical value 0.45 mM. kcat/Km: printed Table 1 cell 230000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 230000 / 1000 = 230.0; canonical value 230.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme heading 'AfUGM', substrate column 'UDP-Galf': kcat = 100 s^-1; KM = 450 uM; printed kcat/KM = 230000 M^-1 s^-1.

row_label: Table 1, decoded plain-numeral transcription line for the wild-type AfUGM enzyme with substrate UDP-Galf

table_label: Table 1: Kinetic Parameters for AfUGM and W315A Using UDP-Galf or UDP-Araf as the Substrate (Biochemistry 2018, 57(26):3713-3721)


substrate_name: UDP-beta-L-arabinofuranose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q4W1X2 and applied mutation signature W315A to reconstruct the assayed variant sequence.

column_label: Table 1 of Biochemistry 2018, 57(26):3713-3721; the printed metric rows are 'kcat (s-1)', 'KM (uM)' and 'kcat/KM (M-1 s-1)'; the enzyme heading read here is 'W315A' and the substrate column head under it is 'UDP-Araf'; that column prints kcat 0.23 s^-1, KM 700 uM and kcat/KM 331 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.23 s^-1; the printed unit is already the canonical unit, so no unit conversion applies; canonical value 0.23 s^(-1). Km: printed Table 1 cell 700 uM; 700 / 1000 = 0.7; canonical value 0.7 mM. kcat/Km: printed Table 1 cell 331 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 331 / 1000 = 0.331; canonical value 0.331 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme heading 'W315A', substrate column 'UDP-Araf': kcat = 0.23 s^-1; KM = 700 uM; printed kcat/KM = 331 M^-1 s^-1.

row_label: Table 1, decoded plain-numeral transcription line for the W315A variant with substrate UDP-Araf

substrate: UDP-beta-L-arabinofuranose


column_label: Table 1 of Biochemistry 2018, 57(26):3713-3721; the printed metric rows are 'kcat (s-1)', 'KM (uM)' and 'kcat/KM (M-1 s-1)'; the enzyme heading read here is 'AfUGM' and the substrate column head under it is 'UDP-Araf'; that column prints kcat 0.14 s^-1, KM 94 uM and kcat/KM 1540 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.14 s^-1; the printed unit is already the canonical unit, so no unit conversion applies; canonical value 0.14 s^(-1). Km: printed Table 1 cell 94 uM; 94 / 1000 = 0.094; canonical value 0.094 mM. kcat/Km: printed Table 1 cell 1540 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1540 / 1000 = 1.54; canonical value 1.54 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme heading 'AfUGM', substrate column 'UDP-Araf': kcat = 0.14 s^-1; KM = 94 uM; printed kcat/KM = 1540 M^-1 s^-1.

row_label: Table 1, decoded plain-numeral transcription line for the wild-type AfUGM enzyme with substrate UDP-Araf


substrate_name: Chorismate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C216A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C216S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E159A with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N160A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q215A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T278A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T278S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T278V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W226A 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.

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


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C88K/R90S to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature C88S/R90K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R90G with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


organism: Chlamydomonas reinhardtii

column_label: Abstract names chorismate mutase EC 5.4.99.5 from Chlamydomonas reinhardi and reports the Michaelis constant for 20-fold purified enzyme was 0.46 mM.

raw_value_unit_evidence: Km raw_value=0.46 mM raw_unit=mM

row_label: Chlamydomonas reinhardtii chorismate mutase / chorismate

table_label: PubMed XML abstract PMID 1122289


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W315A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R182A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R182K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R327K to reconstruct the assayed variant sequence.


organism: Mycobacterium tuberculosis


organism: Pseudomonas aeruginosa

assay_conditions_summary: pH 7.5; 303.15 K; buffer 50 mM potassium phosphate

column_label: Table One row pKIL10A-W prints CM kcat 0.085 +/- 0.011 s^-1 and CM kcat/Km 2,200 +/- 500 M^-1 s^-1; Table One does not print CM Km.

normalized_value_unit_evidence: kcat=0.085 s^-1; Km=0.038 mM preserved from the exact current source tuple; independently printed kcat/Km=2.2 s^-1 mM^-1; current quotient-derived kcat/Km=2.236842105263158 s^-1 mM^-1.

raw_value_unit_evidence: Table One pKIL10A-W WT PchBH CM cells print kcat 0.085 +/- 0.011 s^-1 and kcat/Km 2,200 +/- 500 M^-1 s^-1; the exact current OED source tuple supplies Km 0.038 mM.

row_label: pKIL10A-W (WT PchBH), CM activity

table_label: Table One. Genetic and kinetic characteristics of representative PchB variants


assay_conditions_summary: pH 7.4; buffer pH 7

column_label: PMID 14678783 kinetic prose, true substrate (3S)-2,3-oxidosqualene, apparent KM = 11 uM; assay method states pH 7.4 and 37 deg C.

raw_value_unit_evidence: The apparent KM and kcat/KM values for the true substrate (3S)-2,3-oxidosqualene were determined to be 11 uM and 1.45 mM^-1 min^-1.

row_label: True substrate (3S)-2,3-oxidosqualene

table_label: Kinetic prose for purified bovine liver oxidosqualene-lanosterol cyclase


organism: Yersinia pestis


organism: Saccharomyces cerevisiae


organism: Ustilago maydis


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


organism: Escherichia coli (strain K12)

substrate_name: UDP-GalF

substrate: UDP-GalF


proof_lines:
Raw SKiD Env: Temp=30°C, pH=7
Raw SKiD Env: Temp=37°C, pH=7.5


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C75A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C75S with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


organism: Escherichia coli


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H131A to reconstruct the assayed variant sequence.

row_label: Table 3, protein row H131A, mutase activity, chorismate column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H153N to reconstruct the assayed variant sequence.

row_label: Table 3, protein row H153N, mutase activity, chorismate column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H197N to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H197N, mutase activity, chorismate column group; column KM (uM) = 68 ± 10; column kcat (s^-1) = 16 ± 0.5; column kcat/KM (M^-1 s^-1) = 2.3 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 16 s^-1; already in s^-1, no conversion; the exported value is 16.0 s^(-1). Km: printed Table 3 cell 68 uM; 68 / 1000 = 0.068 mM; the exported value is 0.068 mM. kcat/Km: printed Table 3 cell 2.3 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 229999.99999999997 / 1000 = 229.99999999999997 s^-1 mM^-1; the exported value is 235.2941176470588 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H197N, mutase activity, chorismate column group: KM = 68 ± 10 uM; kcat = 16 ± 0.5 s^-1; printed kcat/KM = 2.3 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H239N with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H239N, mutase activity, chorismate column group; column KM (uM) = 126 ± 12; column kcat (s^-1) = 2.3 ± 0.1; column kcat/KM (M^-1 s^-1) = 0.18 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 2.3 s^-1; already in s^-1, no conversion; the exported value is 2.3 s^(-1). Km: printed Table 3 cell 126 uM; 126 / 1000 = 0.126 mM; the exported value is 0.126 mM. kcat/Km: printed Table 3 cell 0.18 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 18000.0 / 1000 = 18.0 s^-1 mM^-1; the exported value is 18.253968253968253 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H239N, mutase activity, chorismate column group: KM = 126 ± 12 uM; kcat = 2.3 ± 0.1 s^-1; printed kcat/KM = 0.18 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H245N to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H245N, mutase activity, chorismate column group; column KM (uM) = 225 ± 1; column kcat (s^-1) = 4.8 ± 0.1; column kcat/KM (M^-1 s^-1) = 0.21 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 4.8 s^-1; already in s^-1, no conversion; the exported value is 4.8 s^(-1). Km: printed Table 3 cell 225 uM; 225 / 1000 = 0.225 mM; the exported value is 0.225 mM. kcat/Km: printed Table 3 cell 0.21 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 21000.0 / 1000 = 21.0 s^-1 mM^-1; the exported value is 21.333333333333332 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H245N, mutase activity, chorismate column group: KM = 225 ± 1 uM; kcat = 4.8 ± 0.1 s^-1; printed kcat/KM = 0.21 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H257A to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H257A, mutase activity, chorismate column group; column KM (uM) = 98 ± 2; column kcat (s^-1) = 8.0 ± 0.5; column kcat/KM (M^-1 s^-1) = 0.81 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 8.0 s^-1; already in s^-1, no conversion; the exported value is 8.0 s^(-1). Km: printed Table 3 cell 98 uM; 98 / 1000 = 0.098 mM; the exported value is 0.098 mM. kcat/Km: printed Table 3 cell 0.81 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 81000.0 / 1000 = 81.0 s^-1 mM^-1; the exported value is 81.63265306122449 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H257A, mutase activity, chorismate column group: KM = 98 ± 2 uM; kcat = 8.0 ± 0.5 s^-1; printed kcat/KM = 0.81 x 10^5 M^-1 s^-1.


sequence_variant_note: Mutation signature H265A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H347N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H347N, mutase activity, chorismate column group; column KM (uM) = 41 ± 8; column kcat (s^-1) = 6.0 ± 0.2; column kcat/KM (M^-1 s^-1) = 1.5 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 6.0 s^-1; already in s^-1, no conversion; the exported value is 6.0 s^(-1). Km: printed Table 3 cell 41 uM; 41 / 1000 = 0.041 mM; the exported value is 0.041 mM. kcat/Km: printed Table 3 cell 1.5 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 150000.0 / 1000 = 150.0 s^-1 mM^-1; the exported value is 146.34146341463415 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H347N, mutase activity, chorismate column group: KM = 41 ± 8 uM; kcat = 6.0 ± 0.2 s^-1; printed kcat/KM = 1.5 x 10^5 M^-1 s^-1.


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

assay_conditions_summary: pH 7.2; 303.15 K; buffer a three-component; cofactor NAD+

column_label: Table label: Table 3: Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 °C. Row: WT. Column group: mutase activity, chorismate. Columns read: KM (µM) cell 45, kcat (s-1) cell 27, kcat/KM (M-1 s-1) cell 6.0 x 10^5. metric: kcat; raw value: 27; raw unit: s^-1; normalized value: 27.0 s^(-1); metric: Km; raw value: 45; raw unit: uM; normalized value: 0.045 mM; metric: kcat/Km; raw value: 6.0 x 10^5; raw unit: M^-1 s^-1; normalized value: 600.0 s^-1 mM^-1; assay condition: Chorismate mutase-prephenate dehydrogenase from E. coli; Table 3 constants measured at pH 7.2 and 30 C; mutase activity was monitored by following the disappearance of chorismate at 274 nm in a three-component buffer of 0.10 M MES, 0.051 M N-ethylmorpholine, 0.051 M diethanolamine (pH 7.2), 1 mM EDTA and 1 mM DTT. Export row conditions: pH 7.2; 303.15 K.

normalized_value_unit_evidence: Mutase-activity/chorismate columns of Table 3, row WT: kcat 27 s^-1 = 27.0 s^(-1); KM 45 µM = 0.045 mM (1 µM = 0.001 mM); kcat/KM 6.0 x 10^5 M^-1 s^-1 = 600.0 s^-1 mM^-1 (1 M^-1 s^-1 = 0.001 mM^-1 s^-1). Rendering quirks of the PDF text extract: superscript exponents are flattened, so the printed cell `6.0 x 10^5` appears as `6.0 × 105` and the header `kcat (s-1)` is the paper's kcat (s^-1); the plus-or-minus sign is extracted as `(`, so `45 ( 7` is the paper's 45 +/- 7 µM; the micro sign renders as µ; and the superscript -1 of the first two column groups is lifted into the separate header line `-1                  -1 -1                    -1                   -1 -1`.

raw_value_unit_evidence: Table 3: Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C | column group header row: mutase activity, chorismate / prephenate / NAD+ (the last two under the spanning header `dehydrogenase activity`); metric header row: `KM (µM)     kcat (s )   kcat/KM (M     s )   KM (µM)     kcat (s )    kcat/KM (M     s )   KM (µM)     kcat (s-1)   kcat/KM (M-1 s-1)` | data row: `WT            45 ( 7   27 ( 0.7          6.0 × 105          44 ( 8  27 ( 1             6.2 × 105         103 ( 11   27 ( 0.7         2.6 × 105` | the three mutase-activity/chorismate cells of the WT row read: KM = 45 µM (printed `45 ( 7`, the `(` being the flattened plus-or-minus sign); kcat = 27 s^-1 (printed `27 ( 0.7`); kcat/KM = 6.0 x 10^5 M^-1 s^-1 (printed `6.0 × 105`).

row_label: WT | mutase activity, chorismate


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


substrate_name: Unknown


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


substrate_name: UDP-L-arabinofuranose

substrate: UDP-L-arabinofuranose


substrate_name: UDP-galactopyranose


mutation_type: deletion

proof_lines: 30°C, pH 7.5, mutant DELTA118-127, with 5.8 mM substrate

proof_lines: 30°C, pH 7.5, mutant DELTA118-127, with 3.4 mM substrate


proof_lines: 30°C, pH 7.5, mutant DELTA119-127/D118N, with 5.8 mM substrate


proof_lines: 30°C, pH 7.5, mutant DELTA117-127, with 3.8 mM substrate and DELTA 118-127/R116L/P117T, with 3.9 mM substrate

proof_lines: 30°C, pH 7.5, mutant DELTA118-127/R116L/P117T, with 3.9 mM substrate


organism: Klebsiella pneumoniae

proof_lines: in 50 mM MOPS, 10 mM sodium dithionite, 2 mM MgCl2 pH 7.4, at 37°C


substrate_name: UDP-D-galactopyranose

substrate: UDP-D-galactopyranose


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


enzyme_display_name: ribonuclease T2

organism: Aspergillus oryzae

substrate_name: ApG

enzyme: ribonuclease T2

substrate: ApG


substrate_name: ApU

substrate: ApU


enzyme_display_name: S-ribosylhomocysteine lyase

substrate_name: S-ribosylhomocysteine

enzyme: S-ribosylhomocysteine lyase

substrate: S-ribosylhomocysteine


enzyme_display_name: protoporphyrin ferrochelatase

organism: Bdellovibrio bacteriovorus

enzyme: protoporphyrin ferrochelatase


substrate_name: mesoporphyrin IX

substrate: mesoporphyrin IX


proof_lines:
pH 2.6, transphosphorylation
pH 6.7, transphosphorylation
pH 7.2, transphosphorylation


substrate_name: adenylyl (3'-5')uridine

proof_lines:
pH 3.1, transphosphorylation
pH 8.1, transphosphorylation
pH 7.1, transphosphorylation

substrate: adenylyl (3'-5')uridine


enzyme_display_name: prostaglandin-E synthase

organism: Bos taurus

substrate_name: Prostaglandin H1

enzyme: prostaglandin-E synthase

substrate: Prostaglandin H1


substrate_name: Prostaglandin G1

substrate: Prostaglandin G1


substrate_name: chorismate

proof_lines: 30°C, pH 7.5, mutant DELTA117-127, with 3.8 mM substrate


proof_lines: 30°C, pH 7.5, wild-type, with 4 mM substrate


proof_lines:
30°C, pH 7.5, wild-type
30°C, pH 7, wild-type

substrate: Unknown


enzyme_display_name: sirohydrochlorin ferrochelatase

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

enzyme: sirohydrochlorin ferrochelatase


substrate_name: sirohydrochlorin

proof_lines: chimeric mutant enzyme, with Co2+, pH and temperature not specified in the publication

substrate: sirohydrochlorin


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


proof_lines: wild-type enzyme, with Co2+, pH and temperature not specified in the publication


enzyme_display_name: prostaglandin-I synthase

substrate_name: prostaglandin H2

enzyme: prostaglandin-I synthase

substrate: prostaglandin H2


enzyme_display_name: alkylmercury lyase

substrate_name: methyl mercuric chloride

smiles: C[Hg]Cl

enzyme: alkylmercury lyase

substrate: methyl mercuric chloride


substrate_name: n-butyl mercurial

substrate: n-butyl mercurial


substrate_name: phenyl mercuric acetate

substrate: phenyl mercuric acetate


substrate_name: vinylmercuric bromide

substrate: vinylmercuric bromide


substrate_name: cis-2-butenylmercuric chloride

substrate: cis-2-butenylmercuric chloride


substrate_name: UDP-D-galactofuranose

proof_lines: 37°C, pH 7.5, in presence of 20 mM sodium dithionite

substrate: UDP-D-galactofuranose


substrate_name: tetravinyltin

smiles: C=C[Sn](C=C)(C=C)C=C

substrate: tetravinyltin


substrate_name: triethylvinyltin

smiles: CC[Sn](CC)(CC)C=C

substrate: triethylvinyltin


proof_lines: mutant enzyme Glu23Ala, activated by 0.01 mM Trp

substrate: chorismate


proof_lines: mutant enzyme Tyr234Glu, activated by 0.01 mM Trp


proof_lines: mutant enzyme Tyr234Ser, activated by 0.01 mM Trp


proof_lines: mutant enzyme Glu23Gln, activated by 0.01 mM Trp


proof_lines: mutant enzyme Tyr234Ala, activated by 0.01 mM Trp


proof_lines: chorismate, mutant enzyme Thr226Ile, activated by 0.01 mM Trp


proof_lines: wild-type enzyme, activated by 0.01 mM Trp


proof_lines: mutant enzyme Ile225Thr/Thr226Ile, activated by 0.01 mM Trp


proof_lines: mutant enzyme Tyr234Phe, activated by 0.01 mM Trp


proof_lines: mutant enzyme Glu23Asp, activated by 0.01 mM Trp


organism: Sporosarcina pasteurii

substrate_name: phenylmercuric acetate

substrate: phenylmercuric acetate


substrate_name: thiomersol

substrate: thiomersol


enzyme_display_name: cysteine-S-conjugate beta-lyase

organism: Brassica oleracea

substrate_name: L-cystine

enzyme: cysteine-S-conjugate beta-lyase

substrate: L-cystine


substrate_name: Unknown


enzyme_display_name: sirohydrochlorin cobaltochelatase

organism: Methanocaldococcus jannaschii

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

enzyme: sirohydrochlorin cobaltochelatase


enzyme_display_name: methionine gamma-lyase

organism: Citrobacter freundii

substrate_name: S-ethyl-L-homocysteine sulfoxide

proof_lines: pH and temperature not specified in the publication

enzyme: methionine gamma-lyase

substrate: S-ethyl-L-homocysteine sulfoxide


substrate_name: S-butyl-L-cysteine

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

substrate: S-butyl-L-cysteine


enzyme_display_name: methylaspartate mutase

organism: Clostridium cochlearium

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

enzyme: methylaspartate mutase


enzyme_display_name: Delta(3)-Delta(2)-enoyl-CoA isomerase

assay_conditions_summary: cofactor CoA

enzyme: Delta(3)-Delta(2)-enoyl-CoA isomerase


organism: Clostridium tetanomorphum

substrate_name: L-Glu

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

proof_lines: reaction of L-Glu with benzimidazolribofuranosyl-adenosylcobinamide, fusion protein in which the cobalamin-binding subunit is linked to the catalytic subunit

substrate: L-Glu


proof_lines: reaction of L-Glu with benzimidazolribofuranosyl-adenosylcobinamide, wild-type enzyme

proof_lines: reaction with benzimidazolribofuranosyl-adenosylcobinamide, wild-type enzyme and fusion protein in which the cobalamin-binding subunit is linked to the catalytic subunit


proof_lines: genetically engineered enzyme with S subunit fused to the C-terminus of the E subunit through an 11 amino acid (Gly-Gln)5-Gly linker segment

proof_lines: genetically engineered enzyme with S subunit fused to the C-terminus of the E-subunit through an 11 amino acid (Gly-Gln)5-Gly linker segment


organism: Cereibacter sphaeroides


substrate_name: deuteroporphyrin

substrate: deuteroporphyrin


organism: Entamoeba histolytica


substrate_name: Glycerate 3-phosphate

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

substrate: Glycerate 3-phosphate


organism: Cucumis sativus


substrate_name: deuteroporphyrin IX

substrate: deuteroporphyrin IX


enzyme_display_name: D-cysteine desulfhydrase

substrate_name: D-cysteine

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

enzyme: D-cysteine desulfhydrase

substrate: D-cysteine


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

proof_lines:
37°C, pH 8.0
30°C, pH 8.0, alpha,beta-elimination


enzyme_display_name: selenocysteine lyase

substrate_name: L-selenocysteine

smiles: C(C(C(=O)O)N)[SeH]

enzyme: selenocysteine lyase

substrate: L-selenocysteine


substrate_name: L-cysteine sulfinate

substrate: L-cysteine sulfinate


enzyme_display_name: protein disulfide-isomerase

substrate_name: scrambled reoxidized lysozyme

proof_lines: pH 7.0, temperature not specified in the publication

enzyme: protein disulfide-isomerase

substrate: scrambled reoxidized lysozyme


substrate_name: Insulin

substrate: Insulin


substrate_name: S-ribosylhomocysteine

substrate: S-ribosylhomocysteine


enzyme_display_name: isochorismate synthase

substrate_name: chorismate

enzyme: isochorismate synthase


proof_lines: wild type enzyme, in 100 mM phosphate pH 7.0, 10 mM MgCl2


enzyme_display_name: chorismate mutase

substrate_name: prephenate

enzyme: chorismate mutase

substrate: prephenate


proof_lines: 37°C, pH 7.8, DELTA102-285 in presence of 0.05 mM phenylalanine

proof_lines: 37°C, pH 7.8, DELTA102-285 in presence of 0.5 mM phenylalanine

proof_lines: 37°C, pH 7.8, DELTA102-285 in presence of 2 mM phenylalanine

substrate: chorismate


enzyme_display_name: guanylate cyclase

organism: Drosophila melanogaster

substrate_name: GTP

proof_lines:
with 0.273 mM oxygen
under anaerobic conditions

enzyme: guanylate cyclase

substrate: GTP


substrate: Unknown


enzyme_display_name: phosphopentomutase

substrate_name: deoxyribose 1-phosphate

proof_lines:
enzyme form I
enzyme form II
enzyme form III

enzyme: phosphopentomutase

substrate: deoxyribose 1-phosphate


substrate_name: ribose 1-phosphate

substrate: ribose 1-phosphate


enzyme_display_name: protoporphyrin ferrochelatase

organism: Gallus gallus

substrate_name: protoporphyrin

enzyme: protoporphyrin ferrochelatase

substrate: protoporphyrin


enzyme_display_name: S-ribosylhomocysteine lyase

enzyme: S-ribosylhomocysteine lyase


substrate_name: Unknown


organism: Flavobacterium sp.

substrate_name: isochorismate

proof_lines:
enzyme immobilized on alkylamine glass
enzyme immobilized on CNBr-Sepharose
soluble enzyme

substrate: isochorismate


proof_lines:
enzyme immobilized on CNBr-Sepharose
enzyme immobilized on alkylamine glass
soluble enzyme