organism: Caldicellulosiruptor saccharolyticus

assay_conditions_summary: pH 7; buffer 50 mM potassium phosphate

column_label: Table 4. Comparison of Kinetic Parameters of the Recombinant L-RhIs from P. stutzeri, B. pallidus, T. maritima, B. halodurans, T. saccharolyticum, and C. saccharolyticus for Isomerization of L-Rhamnose, L-Lyxose, L-Mannose, D-Allose, and D-Ribose, Respectively; row group C. saccharolyticus, footnote a (this study); column D-allose; metric rows kcat (s^-1), KM (mM), and kcat/KM (mM^-1 s^-1); D-allose: kcat 68.1 +/- 0.5 s^-1; KM 14.3 +/- 0.3 mM; kcat/KM 4.77 +/- 0.08 mM^-1 s^-1. Normalized without derivation to kcat=68.1 s^-1; Km=14.3 mM; kcat/Km=4.77 s^-1*mM^-1.

row_label: C. saccharolyticus (footnote a, this study) / D-allose


enzyme_display_name: L-rhamnose isomerase

substrate_name: L-Mannose

source_db: brenda

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

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

normalized_value_unit_evidence: kcat normalized_value=78.7 normalized_unit=s^-1; Km normalized_value=3.64 normalized_unit=mM; computed kcat/Km normalized_value=21.62087912087912 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=78.7 (+/- 0.3) raw_unit=s^-1; Km raw_value=3.64 (+/- 0.08) raw_unit=mM; kcat/Km printed raw_value=21.6 (+/- 0.4) raw_unit=mM^-1 s^-1

row_label: C. saccharolyticus / l-mannose column

table_label: Table 4

data_origin: experimental

enzyme: L-rhamnose isomerase

substrate: L-Mannose

source: brenda


substrate_name: L-rhamnose

verification_status: corrected

column_label: Table 4. Comparison of Kinetic Parameters of the Recombinant L-RhIs from P. stutzeri, B. pallidus, T. maritima, B. halodurans, T. saccharolyticum, and C. saccharolyticus for Isomerization of L-Rhamnose, L-Lyxose, L-Mannose, D-Allose, and D-Ribose, Respectively; row group C. saccharolyticus, footnote a (this study); column L-rhamnose; metric rows kcat (s^-1), KM (mM), and kcat/KM (mM^-1 s^-1); L-rhamnose: kcat 99.9 +/- 2.4 s^-1; KM 1.03 +/- 0.20 mM; kcat/KM 97.1 +/- 17.3 mM^-1 s^-1. Normalized without derivation to kcat=99.9 s^-1; Km=1.03 mM; kcat/Km=97.1 s^-1*mM^-1.

row_label: C. saccharolyticus (footnote a, this study) / L-rhamnose

substrate: L-rhamnose

status: corrected


substrate_name: D-ribose

column_label: Table 4. Comparison of Kinetic Parameters of the Recombinant L-RhIs from P. stutzeri, B. pallidus, T. maritima, B. halodurans, T. saccharolyticum, and C. saccharolyticus for Isomerization of L-Rhamnose, L-Lyxose, L-Mannose, D-Allose, and D-Ribose, Respectively; row group C. saccharolyticus, footnote a (this study); column D-ribose; metric rows kcat (s^-1), KM (mM), and kcat/KM (mM^-1 s^-1); D-ribose: kcat 118 +/- 2 s^-1; KM 33.5 +/- 1.3 mM; kcat/KM 3.54 +/- 0.09 mM^-1 s^-1. Normalized without derivation to kcat=118 s^-1; Km=33.5 mM; kcat/Km=3.54 s^-1*mM^-1.

row_label: C. saccharolyticus (footnote a, this study) / D-ribose

substrate: D-ribose


substrate_name: L-Lyxose

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

column_label: Table 4. Comparison of Kinetic Parameters of the Recombinant L-RhIs from P. stutzeri, B. pallidus, T. maritima, B. halodurans, T. saccharolyticum, and C. saccharolyticus for Isomerization of L-Rhamnose, L-Lyxose, L-Mannose, D-Allose, and D-Ribose, Respectively; row group C. saccharolyticus, footnote a (this study); column L-lyxose; metric rows kcat (s^-1), KM (mM), and kcat/KM (mM^-1 s^-1); L-lyxose: kcat 186 +/- 3 s^-1; KM 3.65 +/- 0.25 mM; kcat/KM 50.8 +/- 2.7 mM^-1 s^-1. Normalized without derivation to kcat=186 s^-1; Km=3.65 mM; kcat/Km=50.8 s^-1*mM^-1.

row_label: C. saccharolyticus (footnote a, this study) / L-lyxose

substrate: L-Lyxose


substrate_name: D-allose

source_db: oed

assay_conditions_summary: pH 7; 338.15 K; buffer 50 mM potassium phosphate

table_label: Table 4. Comparison of Kinetic Parameters of the Recombinant L-RhIs from P. stutzeri, B. pallidus, T. maritima, B. halodurans, T. saccharolyticum, and C. saccharolyticus for Isomerization of L-Rhamnose, L-Lyxose, L-Mannose, D-Allose, and D-Ribose, Respectively

substrate: D-allose

source: oed


kcat_over_km_origin: calculated


verification_status: verified

column_label: Table 4; row group C. saccharolyticus (footnote a, this study); column l-mannose; sub-rows kcat (s^-1) = 78.7 +/- 0.3, KM (mM) = 3.64 +/- 0.08, kcat/KM (mM^-1 s^-1) = 21.6 +/- 0.4.

normalized_value_unit_evidence: kcat 78.7 s^-1 = 78.7 s^-1 (no conversion). Km 3.64 mM = 3.64 mM (no conversion). kcat/Km: the paper prints 21.6 mM^-1 s^-1 = 21.6 s^-1 mM^-1 (unit order only); the catalog holds the exact quotient of the paper's own cells, 78.7 / 3.64 = 21.62087912087912 s^-1 mM^-1, which rounds to the printed 21.6, so the only difference is printed precision.

raw_value_unit_evidence: Table 4, C. saccharolyticus row group, l-mannose column: kcat = 78.7 (+/- 0.3) s^-1; KM = 3.64 (+/- 0.08) mM; printed kcat/KM = 21.6 (+/- 0.4) mM^-1 s^-1.

row_label: C. saccharolyticus (this study), l-mannose column

table_label: Table 4. Comparison of Kinetic Parameters of the Recombinant l-RhIs ... for Isomerization of l-Rhamnose, l-Lyxose, l-Mannose, d-Allose, and d-Ribose

status: verified


substrate_name: L-Rhamnose

substrate: L-Rhamnose


enzyme_display_name: D-lyxose ketol-isomerase

organism: Escherichia coli O157:H7

substrate_name: D-lyxose

source_db: uniprot

proof_lines: kcat is 13.7 sec(-1) with D-lyxose as substrate. kcat is 12.7 sec(-1) with D-mannose as substrate. kcat is 8.78 sec(-1) with L-gulose as substrate.

enzyme: D-lyxose ketol-isomerase

substrate: D-lyxose

source: uniprot


substrate_name: D-mannose

substrate: D-mannose


substrate_name: L-gulose

substrate: L-gulose


organism: Thermoanaerobacterium saccharolyticum


organism: Cohnella laeviribosi

kcat_display: Not reported

kcat_over_km_display: Not reported

sequence_source: multiple

column_label: Primary PMC HTML Table 2 row d-Mannose, column K_m (mM) = 34.0 +/- 1.1.

normalized_value_unit_evidence: Normalized paper Km: 34.0 mM, matching export Km 34.0 mM.

row_label: d-Mannose

table_label: Table 2. Kinetic parameters of recombinant CLLI

source_databases_merged: brenda uniprot


substrate_name: L-ribose

column_label: Primary PMC HTML Table 2 row l-Ribose, column K_m (mM) = 121.7 +/- 10.8.

normalized_value_unit_evidence: Normalized paper Km: 121.7 mM, matching export Km 121.7 mM.

row_label: l-Ribose

substrate: L-ribose


substrate_name: D-Lyxose

column_label: Table 2 row D-Lyxose lists Km 22.4 mM, kcat 1902 s^-1, and kcat/Km 84.9 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=22.4 normalized_unit=mM; kcat normalized_value=1902 normalized_unit=s^-1; kcat/Km normalized_value=84.9 normalized_unit=mM^-1 s^-1

raw_value_unit_evidence: Km raw_value=22.4 raw_unit=mM; kcat raw_value=1902 raw_unit=s^-1; kcat/Km raw_value=84.9 raw_unit=mM^-1 s^-1

row_label: D-Lyxose

table_label: Table 2. Kinetic parameters of recombinant CLLI.

substrate: D-Lyxose


substrate_name: D-Mannose

column_label: Table 2 row D-Mannose lists Km 34.0 mM, kcat 46.1 s^-1, and kcat/Km 1.4 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=34.0 normalized_unit=mM; kcat normalized_value=46.1 normalized_unit=s^-1; kcat/Km normalized_value=1.4 normalized_unit=mM^-1 s^-1

raw_value_unit_evidence: Km raw_value=34.0 raw_unit=mM; kcat raw_value=46.1 raw_unit=s^-1; kcat/Km raw_value=1.4 raw_unit=mM^-1 s^-1

row_label: D-Mannose

substrate: D-Mannose


substrate_name: L-Ribose

column_label: Table 2 row L-Ribose lists Km 121.7 mM, kcat 26.4 s^-1, and kcat/Km 0.2 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=121.7 normalized_unit=mM; kcat normalized_value=26.4 normalized_unit=s^-1; kcat/Km normalized_value=0.2 normalized_unit=mM^-1 s^-1

raw_value_unit_evidence: Km raw_value=121.7 raw_unit=mM; kcat raw_value=26.4 raw_unit=s^-1; kcat/Km raw_value=0.2 raw_unit=mM^-1 s^-1

row_label: L-Ribose

substrate: L-Ribose


organism: Thermosediminibacter oceani

substrate_name: D-fructose

proof_lines: kcat is 3108 min(-1) with D-lyxose as substrate. kcat is 5686 min(-1) with D-mannose as substrate. kcat is 1030 min(-1) with D-fructose as substrate.

substrate: D-fructose


organism: Thermoclostridium stercorarium

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

assay_conditions_summary: pH 7


substrate_name: D-allulose

substrate: D-allulose


organism: Medicago truncatula

substrate_name: PrFAR

verification_status: unverified

proof_lines: kcat is 9.7 sec(-1) with PrFAR as substrate.

substrate: PrFAR

status: unverified


enzyme_display_name: arabinose-5-phosphate isomerase

organism: Bacteroides fragilis

substrate_name: D-ribulose 5-phosphate

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

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

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

source_databases_merged: brenda skid

enzyme: arabinose-5-phosphate isomerase

substrate: D-ribulose 5-phosphate


substrate_name: D-arabinose 5-phosphate

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

substrate: D-arabinose 5-phosphate


substrate_name: D-Arabinose 5-phosphate

substrate: D-Arabinose 5-phosphate


organism: Serratia proteamaculans

column_label: Table 1 (Specific activities and kinetic parameters of Serratia proteamaculans D-lyxose isomerase with respect to different substrates) carries the columns Substrate | Product | Specific activity (umol min^-1 mg^-1) | Km (mmol l^-1) | kcat (s^-1) | kcat/Km ((mmol l^-1)^-1 s^-1), with the substrate rows grouped under the block labels Aldose, Ketose and Aldose phosphate. The cited cell set is the Ketose block, substrate row D-Fructose (product D-Mannose): Specific activity (umol min^-1 mg^-1) = 1.41; Km (mmol l^-1) = 19.4; kcat (s^-1) = 4297; kcat/Km ((mmol l^-1)^-1 s^-1) = 222.

normalized_value_unit_evidence: Km: printed Table 1 cell 19.4 under the column head Km (mmol l^-1); 1 mmol l^-1 is 1 mM, so no unit conversion applies and the paper value is 19.4 mM. kcat: printed Table 1 cell 4297 under the column head kcat (s^-1); the column is already in s^-1, so no unit conversion applies and the paper value is 4297.0 s^(-1). kcat/Km: printed Table 1 cell 222 under the column head kcat/Km ((mmol l^-1)^-1 s^-1); 1 (mmol l^-1)^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the paper value is 222.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Ketose block, substrate row D-Fructose (product D-Mannose): Km = 19.4 mmol l^-1; kcat = 4297 s^-1; printed kcat/Km = 222 (mmol l^-1)^-1 s^-1.

table_label: Table 1: Specific activities and kinetic parameters of Serratia proteamaculans D-lyxose isomerase with respect to different substrates (Letters in Applied Microbiology 51 (2010) 343-350)


enzyme_display_name: glucuronate isomerase

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

substrate_name: D-galacturonate

proof_lines: kcat is 3.8 sec(-1) with D-galacturonate as substrate. kcat is 0.35 sec(-1) with D-glucuronate as substrate.

enzyme: glucuronate isomerase

substrate: D-galacturonate


organism: Dictyoglomus turgidum

substrate_name: L-Ribulose

substrate: L-Ribulose


substrate_name: D-Xylulose

substrate: D-Xylulose


organism: Bacillus licheniformis

proof_lines: in 50 mM Tris-HCl, 1 mM Mn2+, pH 8.0, at 40°C


organism: Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)

substrate_name: Ru5P (at pH 7.8 and at 37 degrees Celsius)

column_label: Official PMC full text reports KpsF Km 0.30 +/- 0.03 mM for Ru5P and lists the same Ru5P Km in Table 2.

raw_value_unit_evidence: Km raw_value=0.30 +/- 0.03 raw_unit=mM for Ru5P.

row_label: recombinant KpsF / Ru5P

table_label: PMC1422761 full text kinetic parameters prose and Table 2


substrate_name: A5P (at pH 7.8 and at 37 degrees Celsius)


organism: Escherichia coli (strain K12)

substrate_name: Ru5P (at pH 8.25 and at 37 degrees Celsius)


substrate_name: A5P (at pH 8.25 and at 37 degrees Celsius)


organism: Clostridium tetani


substrate_name: Ru5P (at pH 8.5 and at 37 degrees Celsius)

column_label: Official JBC Results/Kinetic Parameters prose reports apparent Km for Ru5P as 0.35 +/- 0.08 mM.

raw_value_unit_evidence: Km raw_value=0.35 +/- 0.08 raw_unit=mM

table_label: Official JBC fulltext Results prose: Kinetic Parameters


substrate_name: A5P (at pH 8.5 and at 37 degrees Celsius)


substrate_name: L-rhamnose

substrate: L-rhamnose


substrate_name: L-rhamnulose

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

substrate: L-rhamnulose


organism: Arabidopsis thaliana

assay_conditions_summary: pH 8

column_label: Abstract reports when D-arabinose-5-phosphate was used as substrate, Km and Vmax of AtKdsD values were 0.16 mmol/L and 0.18 mmol/L min.

raw_value_unit_evidence: Km raw_value=0.16 mmol/L raw_unit=mmol/L

row_label: Arabidopsis thaliana AtKdsD / D-arabinose-5-phosphate

table_label: PubMed XML abstract PMID 29022307


organism: Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)

substrate: A5P (at pH 8.5 and at 37 degrees Celsius)


organism: Francisella tularensis


substrate_name: D-Lyxose


substrate_name: L-lyxose

substrate: L-lyxose


organism: Escherichia coli


substrate_name: D-fructose

assay_conditions_summary: pH 7.5; 313.15 K; buffer 50 mmol/L EPPS

normalized_value_unit_evidence: paper normalized kcat_over_km=222 s^-1*mM^-1; expected normalized value 221.49484536082477 s^-1*mM^-1 agrees by table rounding/SD

row_label: D-Fructose -> D-Mannose

table_label: Table 1: Specific activities and kinetic parameters of Serratia proteamaculans D-lyxose isomerase with respect to different substrates


column_label: PMC HTML Table 2 labeled Kinetic properties of YdaE_BL has D-Lyxose row with columns Km (mM)=30.4, kcat (s^-1)=98, and kcat/Km (mM^-1 s^-1)=3.2; exported central kcat/Km equals 98/30.4=3.223684210526316.

normalized_value_unit_evidence: Km normalized_value=30.4 normalized_unit=mM; kcat normalized_value=98 normalized_unit=s^-1; kcat_over_km normalized_value=3.223684210526316 normalized_unit=s^-1 mM^-1 from 98/30.4 central values.

raw_value_unit_evidence: PMC HTML Table 2 / prose: D-Lyxose row gives Km 30.4 mM, kcat 98 s^-1, and kcat/Km 3.2 mM^-1 s^-1.

row_label: D-Lyxose row for YdaE_BL

table_label: Table 2 / kinetic-parameters prose


substrate_name: D-Mannose

column_label: Official PMC Table 2, D-Mannose row: Km 26 +/- 0.8; kcat 43 +/- 0.1; kcat/Km 1.6.

normalized_value_unit_evidence: Km 26 mM; kcat 43 s^-1; independently printed kcat/Km 1.6 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 D-Mannose row: Km 26 +/- 0.8 mM; kcat 43 +/- 0.1 s^-1; independently printed kcat/Km 1.6 mM^-1 s^-1.

table_label: Table 2. Kinetic properties of YdaE BL


organism: Streptomyces coelicolor


substrate_name: D-glucuronate

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

mutation_type: substitution

substrate: D-glucuronate


organism: Thermofilum sp. (strain ex4484_79)

column_label: Biochemical characterization text states that TsLI is strictly dependent on divalent cations, showing highest activity with Mn2+ ions with a Km of 0.4 mM.

raw_value_unit_evidence: Km raw_value=0.4 mM raw_unit=mM

row_label: Thermofilum sp. D-lyxose isomerase / Mn2+ ion dependency

table_label: PMC full-text PMID 34422783 / Figure 3B divalent-cation kinetics text


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


organism: Thermoanaerobacterium saccharolyticum

substrate_name: D-ribose

assay_conditions_summary: pH 7; 338.15 K; buffer and 1 mM Co2+ at pH 7

proof_lines: at 65°C in 50 mM potassium phosphate buffer and 1 mM Co2+ at pH 7.0

substrate: D-ribose


substrate_name: L-Mannose

substrate: L-Mannose


substrate_name: D-allose

substrate: D-allose


substrate_name: L-Lyxose

substrate: L-Lyxose


organism: Aeribacillus pallidus


proof_lines: at pH 7.5 and 40°C, in the presence of 1 mM Mn2+

substrate: D-fructose


substrate_name: D-mannose

substrate: D-mannose


substrate: D-Lyxose


substrate_name: D-xylulose

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

substrate: D-xylulose


organism: Providencia stuartii

assay_conditions_summary: pH 7.5; 318.15 K; buffer 50 mM HEPES


proof_lines:
in 50 mM HEPES buffer, at pH 7.5, 45°C
pH 6.5, 45°C


enzyme_display_name: L-arabinose isomerase

organism: Bacillus subtilis

substrate_name: L-arabinose

km_display: Not reported

enzyme: L-arabinose isomerase

substrate: L-arabinose


organism: Halalkalibacterium halodurans

assay_conditions_summary: pH 7; 343.15 K; buffer 50 mM malate

proof_lines: in 50 mM malate buffer, at pH 7.0 and 70°C


substrate_name: L-ribulose

proof_lines:
at pH 7.5 and 75°C
pH 7.5, 75°C

substrate: L-ribulose


organism: Lactiplantibacillus plantarum

substrate_name: D-galactose

proof_lines:
pH 7.5, 60°C, recombinant enzyme
pH 7.0, 50°C, recombinant enzyme

substrate: D-galactose


organism: Bacillus velezensis

substrate_name: L-ribose

substrate: L-ribose


substrate_name: D-arabinose 5-phosphate

proof_lines: at 37°C, pH not specified in the publication

substrate: D-arabinose 5-phosphate


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


substrate_name: D-galacturonate

substrate: D-galacturonate


enzyme_display_name: UniProt O31662

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt O31662

source: skid


substrate_name: L-rhamnose

substrate: L-rhamnose


enzyme_display_name: protoporphyrin ferrochelatase

substrate_name: deuteroporphyrin IX

proof_lines: mutant E272S, in the presence of 4 mM Mg2+, pH 7.4, room temperature

enzyme: protoporphyrin ferrochelatase

substrate: deuteroporphyrin IX


enzyme_display_name: D-tagatose 3-epimerase

organism: Pseudomonas sp.

substrate_name: D-tagatose

enzyme: D-tagatose 3-epimerase

substrate: D-tagatose


enzyme_display_name: S-ribosylhomocysteine lyase

proof_lines:
Co2+ substituted enzyme
Fe2+ substituted enzyme
pH 7.0, 22°C

enzyme: S-ribosylhomocysteine lyase


enzyme_display_name: ribose isomerase

organism: Mycolicibacterium smegmatis

enzyme: ribose isomerase

substrate: D-ribose


organism: Klebsiella aerogenes

substrate_name: D-Lyxose


substrate_name: mannose

substrate: mannose


enzyme_display_name: cysteine-S-conjugate beta-lyase

substrate_name: cystathionine

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

enzyme: cysteine-S-conjugate beta-lyase

substrate: cystathionine


enzyme_display_name: phosphoribosylanthranilate isomerase

organism: Ogataea henricii

enzyme: phosphoribosylanthranilate isomerase


enzyme_display_name: corticosteroid side-chain-isomerase

organism: Mesocricetus auratus

enzyme: corticosteroid side-chain-isomerase


enzyme_display_name: L-fucose isomerase

organism: Caldanaerobius polysaccharolyticus

substrate_name: L-fucose

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

enzyme: L-fucose isomerase

substrate: L-fucose


enzyme_display_name: hydroxypyruvate isomerase

organism: Metabacillus fastidiosus

substrate_name: Hydroxypyruvate

enzyme: hydroxypyruvate isomerase

substrate: Hydroxypyruvate


organism: Thermotoga maritima

sequence_variant_note: Mutation signature D173V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme D173V, in 50 mM HEPES, pH 7.5, at 25°C


sequence_variant_note: Mutation signature D130V/D176V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme D130V/D176V, in 50 mM HEPES, pH 7.5, at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D169V with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D169V, in 50 mM HEPES, pH 7.5, at 25°C


sequence_variant_note: Mutation signature D127V/D173V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme D127V/D173V, in 50 mM HEPES, pH 7.5, at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D127V/D169V with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D127V/D169V, in 50 mM HEPES, pH 7.5, at 25°C


proof_lines: wild type enzyme, in 50 mM HEPES, pH 7.5, at 25°C


organism: Escherichia coli O45:K1 (strain S88 / ExPEC)

proof_lines: kcat is 0.49 sec(-1) with 5-methylthioribose-1-phosphate as substrate. kcat is 2.02 sec(-1) with 5-deoxyribose 1-phosphate as substrate. kcat is 0.67 sec(-1) with ribose-1-phosphate as substrate.


substrate_name: 5-deoxyribose 1-phosphate

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

substrate: 5-deoxyribose 1-phosphate


organism: Bacillus thuringiensis serovar kurstaki (strain ATCC 35866 / NRRL B-4488 / HD73)

substrate_name: 5-deoxy-alpha-D-ribose 1-phosphate

proof_lines: kcat is 3.5 sec(-1) with 5-deoxy-alpha-D-ribose 1-phosphate as substrate.

substrate: 5-deoxy-alpha-D-ribose 1-phosphate


organism: Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)

proof_lines: kcat is 0.1 sec(-1) with methylthioribose-1-phosphate as substrate. kcat is 0.18 sec(-1) with deoxyribose-1-phosphate as substrate (PubMed:23042035). kcat is 0.03 sec(-1) with ribose-1-phosphate as substrate (PubMed:31950558).


organism: Methanocaldococcus jannaschii

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


proof_lines: pH 7.0, 60°C, coupled assay, recombinant enzyme


organism: Caldicellulosiruptor saccharolyticus


organism: Bacillus subtilis (strain 168)

substrate_name: methylthioribose-1-phosphate (at pH 8.5 and 35 degrees Celsius)


organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)

substrate_name: ProFAR

substrate: ProFAR


organism: Thermanaeromonas toyohensis


organism: Escherichia coli (strain K12)

substrate_name: hydroxypyruvate (at 37 degrees Celsius and pH 7.0)


substrate_name: 5-deoxy-D-ribose 1-phosphate

substrate: 5-deoxy-D-ribose 1-phosphate


sequence_variant_note: Mutation signature D130T could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.5, 25°C, D130T, mutant form of imidazole glycerol phosphate synthase


proof_lines: kcat is 0.125 sec(-1) with L-xylulose as substrate.


organism: Dictyoglomus turgidum

substrate_name: L-Fucose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V131A to reconstruct the assayed variant sequence.

substrate: L-Fucose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W102A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W510A to reconstruct the assayed variant sequence.


organism: Klebsiella pneumoniae

proof_lines:
constitutive mutant 531
constitutive mutant 502


substrate_name: D-arabinose

substrate: D-arabinose


organism: Streptomyces coelicolor


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D373A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F452A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H539A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I199A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M197A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N404A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N538A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q314A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R30A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S405A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y451A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


enzyme_display_name: glutamate racemase

organism: Bacillus subtilis

substrate_name: D-glutamate

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

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

assay_conditions_summary: pH 8; buffer potassium phosphate

proof_lines: His-tagged recombinant BsGR mutant V149A, in potassium phosphate buffer (10 mM, pH 8.0)

enzyme: glutamate racemase

substrate: D-glutamate


organism: Escherichia coli

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

proof_lines:
E. coli B/r
E. coli K-12


sequence_variant_note: Mutation signature D130V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.5, 25°C, D130V, mutant form of imidazole glycerol phosphate synthase

proof_lines: mutant enzyme D130V, in 50 mM HEPES, pH 7.5, at 25°C


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

proof_lines: pH 7.5, 25°C, D130P, mutant form of imidazole glycerol phosphate synthase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D127G with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, D127G, mutant form of EC 5.3.1.6


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D127K with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, D127K, mutant form of EC 5.3.1.6


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D127F with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, D127F, mutant form of EC 5.3.1.6


sequence_variant_note: Mutation signature D127T matches the mutant residue at offset +0 and the reference residue at offset +22; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: pH 7.5, 25°C, D127T, mutant form of EC 5.3.1.6


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D127V with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, D127V, mutant form of EC 5.3.1.6

proof_lines: mutant enzyme D127V, in 50 mM HEPES, pH 7.5, at 25°C


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +28, so it is treated as a source-provided variant sequence.

proof_lines: pH 7.5, 25°C, D127V/T164H, mutant form of EC 5.3.1.6


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R19A to reconstruct the assayed variant sequence.

proof_lines: PriA mutant R19A, PRA isomerase activity


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

proof_lines:
PriA, PRA isomerase activity
Raw SKiD Env: Temp=-----, pH=-----


organism: Raoultella sp.

substrate_name: L-Fuculose

substrate: L-Fuculose


substrate_name: D-ribulose

substrate: D-ribulose


enzyme_display_name: UniProt P63224

substrate_name: D-sedoheptulose 7-phosphate

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

enzyme: UniProt P63224

substrate: D-sedoheptulose 7-phosphate


enzyme_display_name: UniProt Q93UJ2

organism: Burkholderia pseudomallei

enzyme: UniProt Q93UJ2


enzyme_display_name: coproporphyrin ferrochelatase

substrate_name: coproporphyrin III

enzyme: coproporphyrin ferrochelatase

substrate: coproporphyrin III


substrate_name: L-xylulose

substrate: L-xylulose


organism: uncultured bacterium

substrate_name: D-arabino-hex-3-ulose 6-phosphate

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

substrate: D-arabino-hex-3-ulose 6-phosphate


substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


enzyme_display_name: chorismate mutase

substrate_name: chorismate

proof_lines:
pH 7.5, 37°C, recombinant BsCM_2
pH 7.5, 37°C, recombinant AroH
strain WB672

enzyme: chorismate mutase

substrate: chorismate


enzyme_display_name: sulfoquinovose isomerase

substrate_name: D-mannose

proof_lines: kcat is 79 sec(-1) for the formation of SF from SQ (PubMed:33791429). kcat is 25.3 sec(-1) for D-mannose. kcat is 22.2 sec(-1) for D-fructose. kcat is 13.5 sec(-1) for D-lyxose. kcat is 10.3 sec(-1) for D-xylulose (PubMed:18328504).

enzyme: sulfoquinovose isomerase

substrate: D-mannose


substrate_name: D-fructose

substrate: D-fructose


substrate_name: D-lyxose

substrate: D-lyxose


substrate_name: D-xylulose

substrate: D-xylulose


enzyme_display_name: D-sedoheptulose-7-phosphate isomerase

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature H61Q with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

enzyme: D-sedoheptulose-7-phosphate isomerase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature R69Q to reconstruct the assayed variant sequence.


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

proof_lines: kcat is 23.3 sec(-1) for D-mannose. kcat is 12.3 sec(-1) for D-fructose.


organism: Geobacillus thermopakistaniensis


organism: Thermotoga maritima

proof_lines:
pH 7.5, 25°C, dimer
in 50 mM HEPES, pH 7.5 at 25°C
pH 7.5, 45°C, dimer


enzyme_display_name: amino-acid racemase

substrate_name: L-lysine

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

enzyme: amino-acid racemase

substrate: L-lysine


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

column_label: Table 2 MtbGmhA wild-type row lists Km 0.31+/-0.06 mM in the Km (mM) column.

raw_value_unit_evidence: MtbGmhA wild-type row reports Km raw_value=0.31+/-0.06 raw_unit=mM.

row_label: MtbGmhA wild-type row

table_label: PMC7705670 Table 2


enzyme_display_name: galactose-6-phosphate isomerase

organism: Staphylococcus aureus

substrate_name: D-tagatose 6-phosphate

enzyme: galactose-6-phosphate isomerase

substrate: D-tagatose 6-phosphate


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D61A with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


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


enzyme_display_name: UniProt Q6T1W8

organism: Aneurinibacillus thermoaerophilus

enzyme: UniProt Q6T1W8


organism: Methylococcus capsulatus

substrate_name: D-arabino-3-hexulose 6-phosphate

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

substrate: D-arabino-3-hexulose 6-phosphate


column_label: Abstract states the apparent Michaelis constants for phospho-3-hexuloisomerase are D-arabino-3-hexulose 6-phosphate 1.0x10(-4) M and D-fructose 6-phosphate 1.1x10(-3) M.

raw_value_unit_evidence: Km raw_value=1.1x10(-3) raw_unit=M

row_label: Methylococcus capsulatus phospho-3-hexuloisomerase reverse reaction with D-fructose 6-phosphate

table_label: PubMed/PMC abstract PMID 4219834


enzyme_display_name: ribose-1,5-bisphosphate isomerase

organism: Thermococcus kodakarensis

substrate_name: alpha-D-ribose 1,5-bisphosphate

enzyme: ribose-1,5-bisphosphate isomerase

substrate: alpha-D-ribose 1,5-bisphosphate


enzyme_display_name: peptidylprolyl isomerase

substrate_name: RNase T1

enzyme: peptidylprolyl isomerase

substrate: RNase T1


organism: Mycobacterium tuberculosis

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


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

proof_lines: pH 8.0, 22°C, recombinant wild-type enzyme


substrate_name: D-Homocysteinesulfinate

proof_lines: pH and temperature not specified in the publication

substrate: D-Homocysteinesulfinate


proof_lines: mutant enzyme D61A, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C


proof_lines: mutant enzyme H64Q, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C


proof_lines: wild type enzyme, in 20 mM HEPES, pH 8.0, 10 mM MgCl2, 10 mM KCl, at 37°C


enzyme_display_name: phenylpyruvate tautomerase

organism: Mycolicibacterium smegmatis

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

assay_conditions_summary: pH 8; 295.15 K; buffer in 50 mM Tris-SO4

proof_lines: wild type enzyme CCH2, in in 50 mM Tris-SO4 buffer (pH 8.0), at 22°C

enzyme: phenylpyruvate tautomerase


assay_conditions_summary: pH 7.3; 295.15 K; buffer 10 mM Na2HPO4

proof_lines: wild type enzyme CCH2-P1A, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C

proof_lines: wild type enzyme cis-CAAD, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C

proof_lines: wild type enzyme CCH2, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C


substrate_name: phenylenolpyruvate

proof_lines: mutant enzyme CCH2-P1A, in 10 mM Na2HPO4 buffer, pH 7.3, at 22°C

substrate: phenylenolpyruvate


organism: Streptomyces fradiae


organism: Pseudomonas pavonaceae

substrate_name: enol-phenylpyruvate

assay_conditions_summary: pH 9

substrate: enol-phenylpyruvate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R15Y/H95R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R15Y/H95R, at pH 7.5 and 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R15Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H95R with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y35F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

column_label: Table 1: Kinetic Parameters and Sugar Product Analyses (Biochemistry 2015, 54(29):4495-4506), enzyme row 'FdtA wild-type'; column 'Km (mM)' = 0.50; column 'kcat (s-1)' = 10.5; column 'kcat/Km (M-1 s-1)' = 2.1 x 10^4; column '% original sugar epimer' = 100.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.50 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.5 mM; the exported value is 0.5 mM. kcat: printed Table 1 cell 10.5 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 10.5 s^(-1); the exported value is 10.5 s^(-1). kcat/Km: printed Table 1 cell 2.1 x 10^4 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 21000 / 1000 = 21.0 s^-1 mM^-1; the exported value is 21.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row 'FdtA wild-type': Km = 0.50 mM; kcat = 10.5 s-1; printed kcat/Km = 2.1 x 10^4 M-1 s-1.

row_label: Table 1, enzyme row 'FdtA wild-type'


organism: Mus musculus

sequence_variant_note: Mutation signature E16A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: oxaloacetate tautomerase

organism: Arabidopsis thaliana

substrate_name: enol-oxaloacetate

assay_conditions_summary: pH 7.5; cofactor NADH

column_label: Table 1 row At FAHD2 lists OAA tautomerase (enol->keto) K_M 66.0 ± 4.9 uM, kcat 0.7 ± 0.1 s^-1, and kcat/K_M 1.10 × 10^4 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.066 normalized_unit=mM; kcat normalized_value=0.7 normalized_unit=s^-1; kcat/Km normalized_value=11.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_M raw_value=66.0 ± 4.9 raw_unit=uM; kcat raw_value=0.7 ± 0.1 raw_unit=s^-1; kcat/K_M raw_value=1.10 × 10^4 raw_unit=M^-1 s^-1

row_label: At FAHD2

table_label: Table 1. Kinetic properties of FAHD enzymes

enzyme: oxaloacetate tautomerase

substrate: enol-oxaloacetate


column_label: Table 1 row At FAHD1 lists OAA tautomerase (enol->keto) K_M 48.8 ± 1.8 uM, kcat 3.7 ± 0.5 s^-1, and kcat/K_M 7.48 × 10^4 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.0488 normalized_unit=mM; kcat normalized_value=3.7 normalized_unit=s^-1; kcat/Km normalized_value=74.8 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_M raw_value=48.8 ± 1.8 raw_unit=uM; kcat raw_value=3.7 ± 0.5 raw_unit=s^-1; kcat/K_M raw_value=7.48 × 10^4 raw_unit=M^-1 s^-1

row_label: At FAHD1


organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

substrate_name: D-sedoheptulose 7-phosphate (at 30 degrees Celsius)

proof_lines: kcat is 0.14 sec(-1) for D-sedoheptulose 7-phosphate.


organism: Homo sapiens

column_label: Table 1 row Hs FAHD1 lists OAA tautomerase (enol->keto) K_M 15.8 ± 5.9 uM, kcat 31.1 ± 4.5 s^-1, and kcat/K_M 1.99 × 10^6 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.0158 normalized_unit=mM; kcat normalized_value=31.1 normalized_unit=s^-1; kcat/Km normalized_value=1990 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_M raw_value=15.8 ± 5.9 raw_unit=uM; kcat raw_value=31.1 ± 4.5 raw_unit=s^-1; kcat/K_M raw_value=1.99 × 10^6 raw_unit=M^-1 s^-1

row_label: Hs FAHD1


column_label: Table 1 row Hs FAHD2B lists OAA tautomerase (enol->keto) K_M 296 ± 12 uM, kcat 68.7 ± 3.3 s^-1, and kcat/K_M 2.32 × 10^5 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.296 normalized_unit=mM; kcat normalized_value=68.7 normalized_unit=s^-1; kcat/Km normalized_value=232 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_M raw_value=296 ± 12 raw_unit=uM; kcat raw_value=68.7 ± 3.3 raw_unit=s^-1; kcat/K_M raw_value=2.32 × 10^5 raw_unit=M^-1 s^-1

row_label: Hs FAHD2B


column_label: Table 1 row Hs FAHD2A lists OAA tautomerase (enol->keto) K_M 22.2 ± 3.6 uM, kcat 13.6 ± 2.8 s^-1, and kcat/K_M 6.28 × 10^5 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.0222 normalized_unit=mM; kcat normalized_value=13.6 normalized_unit=s^-1; kcat/Km normalized_value=628 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_M raw_value=22.2 ± 3.6 raw_unit=uM; kcat raw_value=13.6 ± 2.8 raw_unit=s^-1; kcat/K_M raw_value=6.28 × 10^5 raw_unit=M^-1 s^-1

row_label: Hs FAHD2A


organism: Escherichia coli (strain K12)

substrate_name: fumarate

proof_lines: kcat is 3000 sec(-1) for the hydration of fumarate and 300 sec(-1) for the isomerization of enol-oxaloacetate.

substrate: fumarate


proof_lines: kcat is 29.2 sec(-1) (in the presence of AMP, at 85 degrees Celsius).

source_databases_merged: brenda skid uniprot


substrate_name: sulfoquinovose

column_label: Primary article text states EcYihS exhibited Michaelis-Menten parameters for formation of SF from SQ with KM = 1.89 +/- 0.28 mM, referenced to Figure S2.

raw_value_unit_evidence: Km raw_value=1.89 +/- 0.28 raw_unit=mM

row_label: EcYihS-catalyzed formation of SF from SQ

table_label: Results text and Figure S2, SQ isomerase YihS kinetics

substrate: sulfoquinovose


organism: Bos taurus

column_label: Table 1 row Bt FAHD2A lists OAA tautomerase (enol->keto) K_M 20.2 ± 1.4 uM, kcat 32.7 ± 3.0 s^-1, and kcat/K_M 1.63 × 10^6 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.0202 normalized_unit=mM; kcat normalized_value=32.7 normalized_unit=s^-1; kcat/Km normalized_value=1630 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_M raw_value=20.2 ± 1.4 raw_unit=uM; kcat raw_value=32.7 ± 3.0 raw_unit=s^-1; kcat/K_M raw_value=1.63 × 10^6 raw_unit=M^-1 s^-1

row_label: Bt FAHD2A


organism: Bacillus subtilis


substrate_name: keto-(p-hydroxyphenyl)pyruvate

proof_lines:
23°C, pH 6.5
Raw SKiD Env: Temp=23°C, pH=6.5
Raw SKiD Env: Temp=23°C, pH=-----

substrate: keto-(p-hydroxyphenyl)pyruvate


substrate_name: enol-(p-hydroxyphenyl)pyruvate

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

substrate: enol-(p-hydroxyphenyl)pyruvate


sequence_variant_note: Mutation signature P1G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
23°C, mutant enzyme P1G
23°C, pH 6.5, mutant enzyme P1G


sequence_variant_note: Mutation signature N97A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Trichinella spiralis

substrate_name: Unknown

substrate: Unknown


proof_lines: kcat is 3.7 sec(-1) with enol-oxaloacetate as substrate.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K32A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K32R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature Y95F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y97A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


proof_lines: kcat is 31.1 sec(-1) with enol-oxaloacetate as substrate.


proof_lines: kcat is 13.6 sec(-1) with enol-oxaloacetate as substrate.


proof_lines: kcat is 210 nmol/min/mg for the decarboxylation of oxaloacetate. kcat is 140 nmol/min/mg for the hydrolysis of acetylpyruvate.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 369 sec(-1) with enol-oxaloacetate as substrate.


proof_lines: kcat is 0.7 sec(-1) with enol-oxaloacetate as substrate.


organism: Bacillus subtilis (strain 168)

proof_lines: kcat is 237 sec(-1) with enol-oxaloacetate as substrate (PubMed:38287013). kcat is 0.52 sec(-1) with oxaloacetate as substrate for koxaloacetate decarboxylase activity (PubMed:38287013).


proof_lines: kcat is 32.7 sec(-1) with enol-oxaloacetate as substrate.


proof_lines: kcat is 161 sec(-1) with enol-oxaloacetate as substrate.


proof_lines: kcat is 68.7 sec(-1) with enol-oxaloacetate as substrate.


organism: Aneurinibacillus thermoaerophilus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H95R 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 R15Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R15Y/H95R to reconstruct the assayed variant sequence.


table_label: Table 1: Kinetic Parameters and Sugar Product Analyses (Biochemistry 2015, 54(29):4495-4506)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y35F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


proof_lines:
23°C, pH 6.5, wild-type enzyme
23°C, wild-type enzyme


column_label: Table 1 row Sc FMP41 lists OAA tautomerase (enol->keto) K_M 219 ± 23 uM, kcat 369 ± 41 s^-1, and kcat/K_M 1.75 × 10^6 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.219 normalized_unit=mM; kcat normalized_value=369 normalized_unit=s^-1; kcat/Km normalized_value=1750 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_M raw_value=219 ± 23 raw_unit=uM; kcat raw_value=369 ± 41 raw_unit=s^-1; kcat/K_M raw_value=1.75 × 10^6 raw_unit=M^-1 s^-1

row_label: Sc FMP41


substrate_name: oxaloacetate

substrate: oxaloacetate


substrate_name: acetylpyruvate

substrate: acetylpyruvate


substrate_name: oxaloacetate (with oxaloacetate decarboxylase activity)


substrate_name: phenylpyruvate

substrate: phenylpyruvate


substrate_name: p-hydroxyphenylpyruvate

substrate: p-hydroxyphenylpyruvate


substrate_name: D-tartrate

substrate: D-tartrate


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


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


column_label: Table 1 row Bs YisK lists OAA tautomerase (enol->keto) K_M 43.8 ± 8.1 uM, kcat 237 ± 8 s^-1, and kcat/K_M 5.81 × 10^6 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.0438 normalized_unit=mM; kcat normalized_value=237 normalized_unit=s^-1; kcat/Km normalized_value=5810 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_M raw_value=43.8 ± 8.1 raw_unit=uM; kcat raw_value=237 ± 8 raw_unit=s^-1; kcat/K_M raw_value=5.81 × 10^6 raw_unit=M^-1 s^-1

row_label: Bs YisK


substrate_name: keto-oxaloacetate

proof_lines:
enzyme form OAT-1, 25°C, pH 9.0
enzyme form OAT-1

substrate: keto-oxaloacetate


proof_lines:
enzyme form OAT-2, 25°C, pH 9.0
enzyme form OAT-1, 25°C, pH 9.0
enzyme form OAT-1


substrate_name: keto-phenylpyruvate

column_label: Table 3; substrate row 1; columns Km, kcat, and kcat/Km

normalized_value_unit_evidence: normalized: Km=4.9 mM; kcat=285 s^-1; kcat/Km=58 s^-1 mM^-1

raw_value_unit_evidence: paper Table 3 cells for substrate 1: Km=4900 (1000) uM; kcat=285 (40) s^-1; kcat/Km=5.8 x 10^4 M^-1 s^-1

row_label: substrate 1 / keto phenylpyruvate

table_label: Table 3

substrate: keto-phenylpyruvate


substrate_name: (S)-malate

proof_lines: kcat is 3000 sec(-1) for the hydration of fumarate and 300 sec(-1) for the isomerization of enol-oxaloacetate.

substrate: (S)-malate


organism: Sus scrofa

proof_lines:
enol-form, kidney
keto-form, kidney
thyroid gland


proof_lines:
keto-form, kidney
thyroid gland


enzyme_display_name: L-arabinose isomerase

organism: Bacillus velezensis

substrate_name: L-arabinose

enzyme: L-arabinose isomerase

substrate: L-arabinose


enzyme_display_name: cellobiose epimerase

organism: Bacteroides fragilis

substrate_name: cellobiose

proof_lines: recombinant enzyme, 100 mM sodium phosphate, 20 mM cellobiose, pH 7.5, 30°C

proof_lines: pH and temperature not specified in the publication

enzyme: cellobiose epimerase

substrate: cellobiose


enzyme_display_name: UDP-glucose 4-epimerase

organism: Bifidobacterium bifidum

substrate_name: UDPgalactose

enzyme: UDP-glucose 4-epimerase

substrate: UDPgalactose


enzyme_display_name: adenylate cyclase

organism: Bombyx mori

enzyme: adenylate cyclase


organism: Bordetella pertussis

proof_lines:
in the presence of Mn2+
in 75 mM HEPES/NaOH, pH 7.4, at 25°C
in the presence of Mg2+


substrate_name: ATP

assay_conditions_summary: cofactor ATP

proof_lines: pH and temperature not specified in the publication, in absence of calmodulin

proof_lines: pH and temperature not specified in the publication, in presence of calmodulin

substrate: ATP


enzyme_display_name: aspartate racemase

substrate_name: D-Asp

enzyme: aspartate racemase

substrate: D-Asp


substrate_name: enol-oxaloacetate

substrate: enol-oxaloacetate


enzyme_display_name: lactoylglutathione lyase

enzyme: lactoylglutathione lyase


enzyme_display_name: guanylate cyclase

substrate_name: UTP

enzyme: guanylate cyclase

substrate: UTP


substrate_name: GTP

proof_lines: purified recombinant sGC in presence of 3-ethyl-3-(ethylaminoethyl)-1-hydroxy-2-oxo-1-triazene

substrate: GTP


enzyme_display_name: 2-hydroxymuconate tautomerase

organism: Leptothrix cholodnii

substrate_name: (2E)-2-Hydroxypenta-2,4-dienoic acid

enzyme: 2-hydroxymuconate tautomerase

substrate: (2E)-2-Hydroxypenta-2,4-dienoic acid


organism: Pseudomonas putida


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


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


substrate_name: Unknown

proof_lines:
at 10°C
at 27°C
37°C, pH 7.4, competitive vs. Mg2+

substrate: Unknown


enzyme_display_name: ribose-5-phosphate isomerase

substrate_name: D-ribose 5-phosphate

proof_lines:
calf spleen
ox muscle
calf liver

enzyme: ribose-5-phosphate isomerase

substrate: D-ribose 5-phosphate


enzyme_display_name: lanosterol synthase

enzyme: lanosterol synthase


enzyme_display_name: aldose 1-epimerase

substrate_name: alpha-D-glucose

proof_lines:
embryo
alpha-D-glucose, newborn calf
adult

enzyme: aldose 1-epimerase

substrate: alpha-D-glucose


enzyme_display_name: thromboxane-A synthase

substrate_name: prostaglandin H2

proof_lines:
immobilized enzyme
soluble enzyme

enzyme: thromboxane-A synthase

substrate: prostaglandin H2


enzyme_display_name: isopentenyl-diphosphate Delta-isomerase

organism: Choristoneura fumiferana

substrate_name: isopentenyl diphosphate

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

proof_lines: wild type enzyme, in 25 mM Tris-HCl, pH 7.0, at 37°C

enzyme: isopentenyl-diphosphate Delta-isomerase

substrate: isopentenyl diphosphate


proof_lines: mutant enzyme Y105F, in 25 mM Tris-HCl, pH 7.0, at 37°C


proof_lines: mutant enzyme E169Q, in 25 mM Tris-HCl, pH 7.0, at 37°C


proof_lines: mutant enzyme W216F, in 25 mM Tris-HCl, pH 7.0, at 37°C


proof_lines: mutant enzyme Y159F, in 25 mM Tris-HCl, pH 7.0, at 37°C


organism: Burkholderia lata


organism: Archaeoglobus fulgidus

proof_lines: pH 7.3, 23°C, conversion to (3E)-2-oxohex-3-enedioate


substrate_name: phenylenolpyruvate

substrate: phenylenolpyruvate


organism: Helicobacter pylori


organism: Gammaproteobacteria bacterium


substrate_name: propiolate

substrate: propiolate


organism: Methylibium petroleiphilum

assay_conditions_summary: pH 7.3; 297.15 K; buffer 10 mM potassium phosphate

proof_lines: isoform 4-oxalocrotonate tautomerase II, in 10 mM potassium phosphate buffer, pH 7.3, at 24°C

proof_lines: isoform 4-oxalocrotonate tautomerase I, in 10 mM potassium phosphate buffer, pH 7.3, at 24°C


organism: Chloroflexus aurantiacus

proof_lines: pH 7.3, 24°C, recombinant hh4-OT mutant betaP1A

proof_lines: pH 7.3, 24°C, recombinant hh4-OT mutant alphaR12A

proof_lines: pH 7.3, 24°C, recombinant hh4-OT mutant betaR39A


proof_lines: pH 7.3, 24°C, recombinant wild-type hh4-OT


organism: Cinchona robusta

proof_lines:
isomerase II
isomerase I


substrate_name: dimethylallyl diphosphate

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

substrate: dimethylallyl diphosphate


organism: Narcissus pseudonarcissus


enzyme_display_name: vinylacetyl-CoA Delta-isomerase

organism: Bos taurus

substrate_name: vinylacetyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: vinylacetyl-CoA Delta-isomerase

substrate: vinylacetyl-CoA


enzyme_display_name: steroid Delta-isomerase

organism: Nocardia erythropolis

enzyme: steroid Delta-isomerase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R39A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; buffer 10 mM potassium phosphate

proof_lines: mutant enzyme R39A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R11A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R11A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C


organism: Saccharolobus shibatae

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q160N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6

proof_lines: mutant enzyme Q160N, in 50 mM MOPS-NaOH, pH 6.0, at 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q160L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q160L, in 50 mM MOPS-NaOH, pH 6.0, at 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q160H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q160H, in 50 mM MOPS-NaOH, pH 6.0, at 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q160E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q160E, in 50 mM MOPS-NaOH, pH 6.0, at 60°C


assay_conditions_summary: pH 6; 333.15 K; cofactor NADH

proof_lines:
pH 6.0, 60°C
pH 6.0
Raw SKiD Env: Temp=60°C, pH=6


substrate_name: NADH

assay_conditions_summary: cofactor NADH

proof_lines: dehydrogenase reaction without isopentenyl diphosphate

substrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E118A/N120A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R72A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y14F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y14F, at pH 7.0, temperature not specified in the publication


organism: Aedes aegypti

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

proof_lines: in 0.4 M Tris, 1 mM dithiothreitol, 10 mM MgCl2, pH 8.0, at 50°C


organism: Methanocaldococcus jannaschii

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

proof_lines: kcat is 191 sec(-1) for isomerase activity with IPP.


organism: Homo sapiens

substrate_name: dehydroepiandrosterone

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q240R with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

substrate: dehydroepiandrosterone


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R240Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q105M to reconstruct the assayed variant sequence.

proof_lines:
mutant Q105M, isoform 1, 27°C, pH 7.4
mutant Q105M, isoform 2, 27°C, pH 7.4


organism: Rattus norvegicus

substrate_name: dihydrotestosterone (in the presence of NADPH)

assay_conditions_summary: cofactor NADPH

proof_lines: Vmax for dihydrotestosterone reduction is 15-fold higher in the presence of NADH than in the presence of NADPH.


organism: Streptomyces sp. (strain SA-COO)

substrate_name: cholesterol

proof_lines: kcat is 44 sec(-1) for the oxidation of cholesterol. kcat is 64 sec(-1) for the isomerization of cholest-5-en-3-one.

substrate: cholesterol


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D265N to reconstruct the assayed variant sequence.


organism: Pseudomonas putida

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y30F/Y55F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W92A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W92A/L125A/V127A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L125F/V127F with inferred residue-numbering offset -26 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L125A/V127A with inferred residue-numbering offset -26 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y115F with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y115F, at pH 7.0, temperature not specified in the publication


organism: Bacillus subtilis (strain 168)

substrate_name: (p-hydroxyphenyl)-enolpyruvate

proof_lines: kcat is 3 sec(-1) for 2-hydroxy-2,4-heptadiene-1,7-dioate, 4.1 sec(-1) for (p-hydroxyphenyl)-enolpyruvate, 10 sec(-1) for 2-hydroxymuconate, 26 sec(-1) for 2-hydroxymuconate, 112 sec(-1) for 2-hydroxy-2,4-pentadienoate, 125 sec(-1) for phen

substrate: (p-hydroxyphenyl)-enolpyruvate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R11A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R39A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R39Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Comamonas testosteroni


proof_lines:
Raw SKiD Env: Temp=25°C, pH=7
Raw SKiD Env: Temp=°C, pH=7


proof_lines: mutant enzyme Y30F/Y55F, at pH 7.0, temperature not specified in the publication


organism: Escherichia coli (strain K12)


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q105M with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines:
mutant Q105M, isoform 2, 27°C, pH 7.4
mutant Q105M, isoform 1, 27°C, pH 7.4


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M187T with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


proof_lines: wild type enzyme, in 50 mM MOPS-NaOH, pH 6.0, at 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q160K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q160K, in 50 mM MOPS-NaOH, pH 6.0, at 60°C


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y14F/Y30F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature Y14F/Y55F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y14F/Y30F/Y55F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: 25°C, pH 7.0, mutant enzyme Y14F/Y30F/Y55F


substrate_name: 2-hydroxymuconate (with 2-oxo-4-hexenedioate as product)

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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A9W9U6 and applied mutation signature R12A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 297.15 K; buffer this pass. Assay condition: 10 mM potassium phosphate

column_label: Table 3: Kinetic Parameters for 4-Oxalocrotonate Tautomerases using Phenylenolpyruvate (3) (Biochemistry 2010, 49(24):5016-5027), enzyme row 'αR12A'; column 'kcat (s−1)' = 0.6; column 'Km (μM)' = 143; column 'kcat/Km (M−1 s−1)' = 4.2 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.6 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 0.6 s^(-1). Km: printed Table 3 cell 143 uM; 143 / 1000 = 0.143 mM; the exported value is 0.143 mM. kcat/Km: printed Table 3 cell 4.2 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.2 x 10^3 / 1000 = 4.2 s^-1 mM^-1, which is the paper's two-significant-figure printing of the exact quotient 0.6 / 0.143 = 4.195804195804196 s^-1 mM^-1 that the catalog carries.

raw_value_unit_evidence: Table 3, enzyme row αR12A: column kcat (s−1) = 0.6; column Km (μM) = 143; column kcat/Km (M−1 s−1) = 4.2 x 10^3.

row_label: Table 3, enzyme row αR12A


column_label: Table 3: Kinetic Parameters for 4-Oxalocrotonate Tautomerases using Phenylenolpyruvate (3) (Biochemistry 2010, 49(24):5016-5027), enzyme row 'hh4-OT (wild type)'; column 'kcat (s−1)' = 13; column 'Km (μM)' = 121; column 'kcat/Km (M−1 s−1)' = 1.1 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 13 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 13.0 s^(-1). Km: printed Table 3 cell 121 uM; 121 / 1000 = 0.121 mM; the exported value is 0.121 mM. kcat/Km: printed Table 3 cell 1.1 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^5 / 1000 = 110.0 s^-1 mM^-1, which is the paper's two-significant-figure printing of the exact quotient 13.0 / 0.121 = 107.43801652892563 s^-1 mM^-1 that the catalog carries.

raw_value_unit_evidence: Table 3, enzyme row hh4-OT (wild type): column kcat (s−1) = 13; column Km (μM) = 121; column kcat/Km (M−1 s−1) = 1.1 x 10^5.

row_label: Table 3, enzyme row hh4-OT (wild type)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61615 and applied mutation signature Q160E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 333.15 K; buffer 50 mM MOPS-NaOH

column_label: Table 2 (Kinetic parameters for Q160 mutants of S. shibatae IDI-2), Enzymes column row 'Q160E'; column 'kcat (x10^3 s^-1)' = 3.28 ± 0.31; column 'Km, uM' = 8.26 ± 1.41; column 'kcat/Km, M^-1 s^-1' = 397.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 3.28 under the column head kcat (x10^3 s^-1), so kcat is 3.28 / 10^3 = 0.00328 s^(-1). Km: the printed cell is 8.26 uM; 8.26 / 1000 = 0.00826 mM. kcat/Km: the printed cell is 397 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 397 / 1000 = 0.397 s^-1 mM^-1. Closure of the paper's own three printed cells: 0.00328 / 0.00826 = 0.397094 s^-1 mM^-1, which rounds to the printed efficiency cell 397 M^-1 s^-1 at the precision the paper prints.

raw_value_unit_evidence: Table 2 (Kinetic parameters for Q160 mutants of S. shibatae IDI-2), Enzymes row 'Q160E': the kcat column, whose printed head is kcat (x10^3 s^-1), prints 3.28 ± 0.31; the Km column, printed head Km, uM, prints 8.26 ± 1.41; the catalytic-efficiency column, printed head kcat/Km, M^-1 s^-1, prints 397.

row_label: Table 2, Enzymes row 'Q160E' (Gln160 replaced, S. shibatae IDI-2)

table_label: Table 2: Kinetic parameters for Q160 mutants of S. shibatae IDI-2 (PNAS 2011, 108(51):20461-20466, page 20464)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61615 and applied mutation signature Q160H to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for Q160 mutants of S. shibatae IDI-2), Enzymes column row 'Q160H'; column 'kcat (x10^3 s^-1)' = 1.21 ± 0.11; column 'Km, uM' = 7.13 ± 1.22; column 'kcat/Km, M^-1 s^-1' = 170.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 1.21 under the column head kcat (x10^3 s^-1), so kcat is 1.21 / 10^3 = 0.00121 s^(-1). Km: the printed cell is 7.13 uM; 7.13 / 1000 = 0.00713 mM. kcat/Km: the printed cell is 170 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 170 / 1000 = 0.17 s^-1 mM^-1. Closure of the paper's own three printed cells: 0.00121 / 0.00713 = 0.169705 s^-1 mM^-1, which rounds to the printed efficiency cell 170 M^-1 s^-1 at the precision the paper prints.

raw_value_unit_evidence: Table 2 (Kinetic parameters for Q160 mutants of S. shibatae IDI-2), Enzymes row 'Q160H': the kcat column, whose printed head is kcat (x10^3 s^-1), prints 1.21 ± 0.11; the Km column, printed head Km, uM, prints 7.13 ± 1.22; the catalytic-efficiency column, printed head kcat/Km, M^-1 s^-1, prints 170.

row_label: Table 2, Enzymes row 'Q160H' (Gln160 replaced, S. shibatae IDI-2)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61615 and applied mutation signature Q160L to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for Q160 mutants of S. shibatae IDI-2), Enzymes column row 'Q160L'; column 'kcat (x10^3 s^-1)' = 0.221 ± 0.014; column 'Km, uM' = 1.52 ± 0.3; column 'kcat/Km, M^-1 s^-1' = 145.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 0.221 under the column head kcat (x10^3 s^-1), so kcat is 0.221 / 10^3 = 0.000221 s^(-1). Km: the printed cell is 1.52 uM; 1.52 / 1000 = 0.00152 mM. kcat/Km: the printed cell is 145 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 145 / 1000 = 0.145 s^-1 mM^-1. Closure of the paper's own three printed cells: 0.000221 / 0.00152 = 0.145395 s^-1 mM^-1, which rounds to the printed efficiency cell 145 M^-1 s^-1 at the precision the paper prints.

raw_value_unit_evidence: Table 2 (Kinetic parameters for Q160 mutants of S. shibatae IDI-2), Enzymes row 'Q160L': the kcat column, whose printed head is kcat (x10^3 s^-1), prints 0.221 ± 0.014; the Km column, printed head Km, uM, prints 1.52 ± 0.3; the catalytic-efficiency column, printed head kcat/Km, M^-1 s^-1, prints 145.

row_label: Table 2, Enzymes row 'Q160L' (Gln160 replaced, S. shibatae IDI-2)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P61615 and applied mutation signature Q160N to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for Q160 mutants of S. shibatae IDI-2), Enzymes column row 'Q160N'; column 'kcat (x10^3 s^-1)' = 0.197 ± 0.019; column 'Km, uM' = 3.23 ± 0.75; column 'kcat/Km, M^-1 s^-1' = 61.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 0.197 under the column head kcat (x10^3 s^-1), so kcat is 0.197 / 10^3 = 0.000197 s^(-1). Km: the printed cell is 3.23 uM; 3.23 / 1000 = 0.00323 mM. kcat/Km: the printed cell is 61 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 61 / 1000 = 0.061 s^-1 mM^-1. Closure of the paper's own three printed cells: 0.000197 / 0.00323 = 0.060991 s^-1 mM^-1, which rounds to the printed efficiency cell 61 M^-1 s^-1 at the precision the paper prints.

raw_value_unit_evidence: Table 2 (Kinetic parameters for Q160 mutants of S. shibatae IDI-2), Enzymes row 'Q160N': the kcat column, whose printed head is kcat (x10^3 s^-1), prints 0.197 ± 0.019; the Km column, printed head Km, uM, prints 3.23 ± 0.75; the catalytic-efficiency column, printed head kcat/Km, M^-1 s^-1, prints 61.

row_label: Table 2, Enzymes row 'Q160N' (Gln160 replaced, S. shibatae IDI-2)


substrate_name: isopentenyl

assay_conditions_summary: pH 8

column_label: Abstract reports K(IPP)(m) value of 22.8 microm IPP.

raw_value_unit_evidence: Km raw_value=22.8 microM raw_unit=microM

row_label: human IDI2 / IPP

table_label: PubMed XML abstract PMID 17202134

substrate: isopentenyl


organism: Saccharomyces cerevisiae


sequence_variant_note: Mutation signature L141H/Y195F/W256C could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme L141H/Y195F/W256C, at pH 7.5 and 30°C


organism: Chloroflexus aurantiacus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R39A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A9W9U6 and applied mutation signature R40A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters for 4-Oxalocrotonate Tautomerases using Phenylenolpyruvate (3) (Biochemistry 2010, 49(24):5016-5027), enzyme row 'αR40A'; column 'kcat (s−1)' = 44; column 'Km (μM)' = 152; column 'kcat/Km (M−1 s−1)' = 2.9 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 44 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 44.0 s^(-1). Km: printed Table 3 cell 152 uM; 152 / 1000 = 0.152 mM; the exported value is 0.152 mM. kcat/Km: printed Table 3 cell 2.9 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.9 x 10^5 / 1000 = 290.0 s^-1 mM^-1, which is the paper's two-significant-figure printing of the exact quotient 44.0 / 0.152 = 289.4736842105263 s^-1 mM^-1 that the catalog carries.

raw_value_unit_evidence: Table 3, enzyme row αR40A: column kcat (s−1) = 44; column Km (μM) = 152; column kcat/Km (M−1 s−1) = 2.9 x 10^5.

row_label: Table 3, enzyme row αR40A


sequence_variant_note: Mutation signature P1A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature R11A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


column_label: Table 2: Kinetic Parameters for 4-Oxalocrotonate Tautomerases using 2-Hydroxymuconate (1) (Biochemistry 2010, 49(24):5016-5027), enzyme row 'αR12A'; column 'kcat (s−1)' = 43; column 'Km (μM)' = 1033; column 'kcat/Km (M−1 s−1)' = 4.2 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 43 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 43.0 s^(-1). Km: printed Table 2 cell 1033 uM; 1033 / 1000 = 1.033 mM; the exported value is 1.033 mM. kcat/Km: printed Table 2 cell 4.2 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.2 x 10^4 / 1000 = 42.0 s^-1 mM^-1, which is the paper's two-significant-figure printing of the exact quotient 43.0 / 1.033 = 41.626331074540175 s^-1 mM^-1 that the catalog carries.

raw_value_unit_evidence: Table 2, enzyme row αR12A: column kcat (s−1) = 43; column Km (μM) = 1033; column kcat/Km (M−1 s−1) = 4.2 x 10^4.

row_label: Table 2, enzyme row αR12A


column_label: Table 2: Kinetic Parameters for 4-Oxalocrotonate Tautomerases using 2-Hydroxymuconate (1) (Biochemistry 2010, 49(24):5016-5027), enzyme row 'αR40A'; column 'kcat (s−1)' = 65; column 'Km (μM)' = 345; column 'kcat/Km (M−1 s−1)' = 1.9 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 65 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 65.0 s^(-1). Km: printed Table 2 cell 345 uM; 345 / 1000 = 0.345 mM; the exported value is 0.345 mM. kcat/Km: printed Table 2 cell 1.9 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.9 x 10^5 / 1000 = 190.0 s^-1 mM^-1, which is the paper's two-significant-figure printing of the exact quotient 65.0 / 0.345 = 188.40579710144928 s^-1 mM^-1 that the catalog carries.

raw_value_unit_evidence: Table 2, enzyme row αR40A: column kcat (s−1) = 65; column Km (μM) = 345; column kcat/Km (M−1 s−1) = 1.9 x 10^5.

row_label: Table 2, enzyme row αR40A


column_label: Table 2: Kinetic Parameters for 4-Oxalocrotonate Tautomerases using 2-Hydroxymuconate (1) (Biochemistry 2010, 49(24):5016-5027), enzyme row 'hh4-OT (wild type)'; column 'kcat (s−1)' = 3000; column 'Km (μM)' = 70; column 'kcat/Km (M−1 s−1)' = 4.3 x 10^7.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3000 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 3000.0 s^(-1). Km: printed Table 2 cell 70 uM; 70 / 1000 = 0.07 mM; the exported value is 0.07 mM. kcat/Km: printed Table 2 cell 4.3 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.3 x 10^7 / 1000 = 43000.0 s^-1 mM^-1, which is the paper's two-significant-figure printing of the exact quotient 3000.0 / 0.07 = 42857.142857142855 s^-1 mM^-1 that the catalog carries.

raw_value_unit_evidence: Table 2, enzyme row hh4-OT (wild type): column kcat (s−1) = 3000; column Km (μM) = 70; column kcat/Km (M−1 s−1) = 4.3 x 10^7.

row_label: Table 2, enzyme row hh4-OT (wild type)


organism: Archaeoglobus fulgidus

assay_conditions_summary: pH 7.3; 296.15 K; buffer 20 mM NaH2PO4

column_label: Table 4 AfDmpI reaction 1 -> 5 reports kcat 0.2, Km 170 uM, and kcat/Km 1.2 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized 0.2 s^-1; Km normalized 0.17 mM; kcat/Km normalized 1.2 s^-1 mM^-1.

row_label: AfDmpI reaction 1 -> 5

table_label: PMC2963697 Table 4, kinetic parameters for AfDmpI using 1, 3, and 7


normalized_value_unit_evidence: kcat 2.4 s^-1; Km 0.09 mM; independently printed kcat/Km 27 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 row 7 -> 8: kcat 2.4 +/- 0.3 s^-1; Km 90 +/- 20 uM; independently printed kcat/Km 2.7 x 10^4 M^-1 s^-1.

table_label: Table 4. Kinetic parameters for AfDmpI using 1, 3, and 7


column_label: Table 4 AfDmpI reaction 3 -> 6 reports kcat 0.1, Km 90 uM, and kcat/Km 1.1 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized 0.1 s^-1; Km normalized 0.09 mM; kcat/Km normalized 1.1 s^-1 mM^-1.

row_label: AfDmpI reaction 3 -> 6


organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

substrate_name: IPP (at pH 7.6 and 37 degrees Celsius)

proof_lines: kcat is 17.9 sec(-1) for isomerase activity with IPP (at pH 7.6 and 37 degrees Celsius).

substrate: IPP (at pH 7.6 and 37 degrees Celsius)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E13R/R235E 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 M187T with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Escherichia coli

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=37°C, pH=7.4

source_databases_merged: skid uniprot


organism: Microcystis aeruginosa

substrate_name: 2,3-diketo-5-methylthiopentyl-1-phosphate (at pH 8 and 37 degrees Celsius)

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

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


organism: Methylibium petroleiphilum


organism: Streptomyces sp.

substrate_name: Isopentenyl diphosphate

assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH

substrate: Isopentenyl diphosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P39A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P39G with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


organism: Staphylococcus aureus

assay_conditions_summary: pH 7; 310.15 K; cofactor FMN


column_label: Results paragraph tied to Figure 3 reports DMAPP Km=14.3 +/- 0.8 microM.

raw_value_unit_evidence: Kms for DMAPP and IPP were 14.3 +/- 0.8 and 9.5 +/- 0.5 microM, respectively.

row_label: Recombinant E. coli IPP isomerase / DMAPP

table_label: Official PMC result text / Figure 3 product inhibition kinetics


organism: Clostridium aminobutyricum


assay_conditions_summary: pH 7.5; 303.15 K; buffer 50 mM MOPS

column_label: Table 1 row IDI lists Km 41.5 +/- 0.39 uM, Kcat 8.27 +/- 0.06 s^-1, and Kcat/Km 0.20 s^-1 uM^-1. The results prose states the Km decreased from 41.5 +/- 0.39 to 37.6 +/- 0.17 uM, kcat increased from 8.27 +/- 0.06 to 10.57 +/- 0.13 s^-1, and catalytic efficiency from 0.20 to 0.28 s^-1 uM^-1.

normalized_value_unit_evidence: Km normalized_value=0.0415 normalized_unit=mM; kcat normalized_value=8.27 normalized_unit=s^-1; kcat/Km CatLog computed normalized_value=199.27710843373492 normalized_unit=s^-1 mM^-1 from 8.27/0.0415; paper printed rounded normalized ratio=200 s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=41.5 +/- 0.39 raw_unit=uM; kcat raw_value=8.27 +/- 0.06 raw_unit=s^-1; kcat/Km printed raw_value=0.20 raw_unit=s^-1 uM^-1

row_label: IDI

table_label: Table 1, kinetic parameters of IDI and IDI (L141H/Y195F/W256C)


organism: Thermococcus kodakarensis


organism: Homo sapiens

substrate_name: dehydroepiandrosterone (in the presence of NAD(+))


substrate_name: pregnenolone (in the presence of NAD(+))


substrate_name: dihydrotestosterone (in the presence of NADH)


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P1A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


column_label: PMC Table 1 row for compound 5 reports kcat 112 +/- 14 s^-1, Km 243 +/- 42 uM, kcat/Km 4.6 +/- 0.8 x 10^5 M^-1 s^-1; Table 2 identifies YwhB wt conversion of 5 to 4 with the same values.

normalized_value_unit_evidence: kcat/Km normalized_value=460.0 s^-1*mM^-1; same row kcat=112 s^-1 and Km=0.243 mM gives 460.905 s^-1*mM^-1

raw_value_unit_evidence: kcat/Km raw_value=4.6 x 10^5 raw_unit=M^-1 s^-1

row_label: compound 5 / YwhB wt conversion of 5 to 4

table_label: Table 1; Table 2


assay_conditions_summary: pH 7.3; 296.15 K; buffer Assay condition: 20 mM NaH2PO4

column_label: Table 1 compound 11 row reports kcat = 3.0 +/- 0.4 s^-1, Km = 335 +/- 55 uM, and kcat/Km = 9.0 +/- 1.5 x 10^3 M^-1 s^-1; article text identifies compound 11 as 2-hydroxy-2,4-heptadiene-1,7-dioate.

normalized_value_unit_evidence: kcat 3.0 s^-1 from explicit paper cell; kcat_over_km 9.0 s^-1 mM^-1 from explicit paper cell; km 0.335 mM from explicit paper cell

raw_value_unit_evidence: kcat raw_value=3.0 raw_unit=s^-1; Km raw_value=335 raw_unit=uM; kcat/Km raw_value=9.0e3 raw_unit=M^-1 s^-1

row_label: compound 11 / 2-hydroxy-2,4-heptadiene-1,7-dioate

table_label: Table 1 - Kinetic Parameters for YwhB Using Enol and Dienol Substrates


column_label: PMC Table 1 row for compound 8 reports kcat 4.1 +/- 0.4 s^-1, Km 160 +/- 22 uM, kcat/Km 2.6 +/- 0.4 x 10^4 M^-1 s^-1.

normalized_value_unit_evidence: kcat/Km normalized_value=26.0 s^-1*mM^-1; same row kcat=4.1 s^-1 and Km=0.160 mM gives 25.625 s^-1*mM^-1

raw_value_unit_evidence: kcat/Km raw_value=2.6 x 10^4 raw_unit=M^-1 s^-1

row_label: compound 8 / p-hydroxyphenyl(enol)pyruvate

table_label: Table 1


substrate_name: Enol-Phenylpyruvate

substrate: Enol-Phenylpyruvate


column_label: PMC Table 1 row for compound 7 reports kcat 125 +/- 18 s^-1, Km 300 +/- 60 uM, kcat/Km 4.2 +/- 0.8 x 10^5 M^-1 s^-1; Table 3 identifies YwhB wt conversion of 7 to 9 with the same values.

normalized_value_unit_evidence: kcat/Km normalized_value=420.0 s^-1*mM^-1; same row kcat=125 s^-1 and Km=0.300 mM gives 416.667 s^-1*mM^-1

raw_value_unit_evidence: kcat/Km raw_value=4.2 x 10^5 raw_unit=M^-1 s^-1

row_label: compound 7 / YwhB wt conversion of 7 to 9

table_label: Table 1; Table 3


organism: Pseudomonas putida

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


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


substrate_name: isopentenyl diphosphate


proof_lines:
wild-type enzyme
wild-type, pH 7.4, 37°C


substrate_name: pregnenolone

substrate: pregnenolone


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D241N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D265N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D36A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.4; 300.15 K; cofactor NADH


substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D36A/K37R to reconstruct the assayed variant sequence.

substrate: NADPH


proof_lines:
below, pH 7.3, 23°C, mutant R11A/R39A
pH 7.3, 23°C, mutant R11A/R39A


assay_conditions_summary: pH 7.3; 295.15 K; buffer 10 mM potassium phosphate

proof_lines: mutant enzyme P1A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C


proof_lines: wild type enzyme, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C


proof_lines: mutant enzyme R61A, in 10 mM potassium phosphate buffer, pH 7.3, at 22°C


organism: Streptococcus pneumoniae

proof_lines: wild type enzyme, at anaerobic conditions, at pH 7.0 and 37°C

proof_lines: wild type enzyme, at aerobic conditions, at pH 7.0 and 37°C


proof_lines: mutant enzyme N37A, at aerobic conditions, at pH 7.0 and 37°C


substrate_name: Unknown

substrate: Unknown


organism: Comamonas testosteroni


proof_lines: mutant enzyme K122R, in 50 mM Tris-HCl (pH 8.2), 1 mM MgCl2, at 25°C


proof_lines: wild type enzyme, in 50 mM Tris-HCl (pH 8.2), 1 mM MgCl2, at 25°C


enzyme_display_name: muconolactone Delta-isomerase

organism: Cupriavidus necator

enzyme: muconolactone Delta-isomerase


proof_lines: pH and temperature not specified in the publication


proof_lines: in 50 mM HEPES (pH 7.2) containing 10 mM MgCl2, 200 mM KCl, 1 mg/ml bovine serum albumin, 0.5 mM dithiothreitol, at 37°C


proof_lines: 25°C, pH 7.0, mutant enzyme Y14F/Y30F/Y55F/D99L


proof_lines: 25°C, pH 7.0, mutant enzyme Y14F/Y30F/Y55F/D99N


sequence_source: UniProtKB/Swiss-Prot P07445

sequence_variant_note: Resolved canonical sequence from UniProtKB/Swiss-Prot P07445 and applied mutation signature Y55F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y55F, at pH 7.0, temperature not specified in the publication


sequence_variant_note: Mutation signature Y30F/Y55F/Y115F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme Y30F/Y55F/Y115F, at pH 7.0, temperature not specified in the publication


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 Y30F, at pH 7.0, temperature not specified in the publication


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


enzyme_display_name: pancreatic ribonuclease

organism: Bos taurus

substrate_name: RNA

proof_lines:
pH 7.0, 37°C
pH 5.5, 25°C, comercial enzyme
pH 5.5, 25°C, type I enzyme

enzyme: pancreatic ribonuclease

substrate: RNA


organism: Bombyx mori

substrate: isopentenyl diphosphate


substrate_name: 2',3'-cyclic UMP

substrate: 2',3'-cyclic UMP


substrate_name: uronic acid residues

substrate: uronic acid residues


enzyme_display_name: ribulose-phosphate 3-epimerase

substrate_name: D-ribulose 5-phosphate

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

enzyme: ribulose-phosphate 3-epimerase

substrate: D-ribulose 5-phosphate


substrate_name: UDPgalactose

proof_lines:
mammary enzyme
liver enzyme

substrate: UDPgalactose


enzyme_display_name: mandelate racemase

substrate_name: 2-hydroxy-3-butenoic acid

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

enzyme: mandelate racemase

substrate: 2-hydroxy-3-butenoic acid


substrate_name: muconolactone

substrate: muconolactone


enzyme_display_name: protein disulfide-isomerase

substrate_name: scrambled ribonuclease

proof_lines: scrambled, with dithiothreitol as substrate

enzyme: protein disulfide-isomerase

substrate: scrambled ribonuclease


enzyme_display_name: methionine gamma-lyase

organism: Brevibacterium linens

substrate_name: L-methionine

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

enzyme: methionine gamma-lyase

substrate: L-methionine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N120A with inferred residue-numbering offset +4 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.


enzyme_display_name: 4-hydroxyproline epimerase

organism: Brucella abortus

enzyme: 4-hydroxyproline epimerase


organism: Brucella suis


organism: Brucella anthropi

substrate_name: L-rhamnose

substrate: L-rhamnose


organism: Brucella melitensis


organism: Brugia malayi


substrate_name: D-allose

substrate: D-allose


enzyme_display_name: mannose-6-phosphate isomerase

organism: Burkholderia cepacia

substrate_name: D-mannose 6-phosphate

proof_lines: pH 7.6, 5 mM Mg2+, temperature not specified in the publication

enzyme: mannose-6-phosphate isomerase

substrate: D-mannose 6-phosphate


enzyme_display_name: phosphoenolpyruvate mutase

organism: Burkholderia gladioli

substrate_name: Phosphonopyruvate

enzyme: phosphoenolpyruvate mutase

substrate: Phosphonopyruvate


enzyme_display_name: glutamate racemase

organism: Burkholderia cenocepacia

substrate_name: D-glutamate

assay_conditions_summary: pH 8; 310.15 K; buffer HEPES

enzyme: glutamate racemase

substrate: D-glutamate


enzyme_display_name: UniProt Q2PS28

organism: Paraburkholderia acidicola

substrate_name: D-glucose

enzyme: UniProt Q2PS28

substrate: D-glucose


substrate_name: isomaltulose

substrate: isomaltulose


substrate_name: Trehalulose

substrate: Trehalulose


enzyme_display_name: UniProt D9MPF2

organism: Erwinia rhapontici

substrate_name: sucrose

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

enzyme: UniProt D9MPF2

substrate: sucrose


enzyme_display_name: UniProt Q8KR84

organism: Klebsiella sp. LX3

enzyme: UniProt Q8KR84


organism: Saccharolobus solfataricus

substrate_name: maltoheptaose

substrate: maltoheptaose


substrate_name: maltohexaose

substrate: maltohexaose


substrate_name: maltopentaose

substrate: maltopentaose


substrate_name: maltotetraose

substrate: maltotetraose


substrate_name: maltotriose

substrate: maltotriose


enzyme_display_name: maltose alpha-D-glucosyltransferase

organism: Deinococcus geothermalis

substrate_name: maltose

enzyme: maltose alpha-D-glucosyltransferase

substrate: maltose


enzyme_display_name: alanine racemase

organism: Caldanaerobacter subterraneus subsp. tengcongensis

substrate_name: D-alanine

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

enzyme: alanine racemase

substrate: D-alanine


proof_lines: pH 10.0, 65°C, recombinant wild-type enzyme


enzyme_display_name: UDP-glucose 4-epimerase

organism: Campylobacter jejuni subsp. jejuni

substrate_name: UDP-alpha-D-glucose

enzyme: UDP-glucose 4-epimerase

substrate: UDP-alpha-D-glucose


organism: Burkholderia pseudomallei


organism: Brevibacillus brevis

substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


enzyme_display_name: isomaltulose synthase

enzyme: isomaltulose synthase


organism: Erwinia sp. Ejp617


organism: Enterobacter hormaechei

assay_conditions_summary: pH 6; 310.15 K; buffer 50 mM phosphate

proof_lines: in 50 mM phosphate buffer (pH 6) at 37°C


substrate_name: alpha,alpha-trehalose

substrate: alpha,alpha-trehalose


organism: Rhodococcus rhodochrous


proof_lines: recombinant enzyme, pH not specified in the publication, 30°C

proof_lines: pH not specified in the publication, 30°C, native enzyme

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


enzyme_display_name: serine racemase

organism: Caenorhabditis elegans

substrate_name: L-serine

sequence_source: UniProtKB Q93968

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

enzyme: serine racemase

substrate: L-serine


organism: Erwinia sp. D12

proof_lines: pH not specified in the publication, 40°C, native enzyme


proof_lines: pH 6.0, temperature not specified in the publication, enzyme immobilized on graphene oxide with addition of surfactant NP40

proof_lines: pH 6.0, temperature not specified in the publication, soluble enzyme


organism: Picrophilus oshimae

proof_lines:
45°C, pH 6.0
45°C, pH 6.0, presence of 10 mM glucose


substrate_name: trehalose

substrate: trehalose


enzyme_display_name: isobutyryl-CoA mutase

organism: Xanthobacter autotrophicus

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

enzyme: isobutyryl-CoA mutase


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

assay_conditions_summary: cofactor CoA


organism: Pantoea dispersa

proof_lines: recombinant enzyme, pH not specified in the publication, 35°C

proof_lines: pH and temperature not specified in the publication


organism: Paraburkholderia acidicola

substrate_name: Unknown

substrate: Unknown


organism: Raoultella terrigena


proof_lines: pH not specified in the publication, 20°C, native enzyme

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


organism: Nostoc flagelliforme

assay_conditions_summary: pH 7; 323.15 K; buffer 50 mM phosphate-citric acid

proof_lines: recombinant enzyme, in 50 mM phosphate-citric acid buffer (0.2 M Na3PO4, 0.1 M citric acid, pH 7.0) at 50°C


organism: Saccharolobus solfataricus

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P95869 and applied mutation signature Y290F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 5; 333.15 K; buffer 50 mM citrate phosphate

column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2006, volume 54, number 10, pages 3585-3590); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 3, MTSase form block Y290F, transglycosylation column G6; printed row label kcat (s-1) = 26.5; printed row label KM (mM) = 6.00; printed row label kcat/KM (s-1 mM-1) = 4.45. captured primary segment: Y290F MTSase | maltohexaose G6 | kcat 26.5 s^-1 | KM 6.00 mM | kcat/KM 4.45 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 6.00 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 6.0 mM. kcat: printed Table 3 kcat cell 26.5 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 26.5 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 4.45 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 4.45 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 26.5 / 6.00 = 4.416666666666667 s^-1 mM^-1, against the printed catalytic-efficiency cell 4.45 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, MTSase form block Y290F, transglycosylation column G6: kcat = 26.5 s^-1; KM = 6.00 mM; printed kcat/KM = 4.45 s^-1 mM^-1.

row_label: Table 3, MTSase form block Y290F, transglycosylation column G6 (maltohexaose)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P95869 and applied mutation signature Y409F to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2006, volume 54, number 10, pages 3585-3590); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 3, MTSase form block Y409F, transglycosylation column G4; printed row label kcat (s-1) = 114; printed row label KM (mM) = 16.1; printed row label kcat/KM (s-1 mM-1) = 7.07. captured primary segment: Y409F MTSase | maltotetraose G4 | kcat 114 s^-1 | KM 16.1 mM | kcat/KM 7.07 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 16.1 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 16.1 mM. kcat: printed Table 3 kcat cell 114 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 114.0 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 7.07 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 7.07 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 114 / 16.1 = 7.080745341614906 s^-1 mM^-1, against the printed catalytic-efficiency cell 7.07 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, MTSase form block Y409F, transglycosylation column G4: kcat = 114 s^-1; KM = 16.1 mM; printed kcat/KM = 7.07 s^-1 mM^-1.

row_label: Table 3, MTSase form block Y409F, transglycosylation column G4 (maltotetraose)


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

column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2006, volume 54, number 10, pages 3585-3590); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 3, MTSase form block wild-type, transglycosylation column G4; printed row label kcat (s-1) = 138; printed row label KM (mM) = 13.2; printed row label kcat/KM (s-1 mM-1) = 10.4. captured primary segment: wild-type MTSase | maltotetraose G4 | kcat 138 s^-1 | KM 13.2 mM | kcat/KM 10.4 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 13.2 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 13.2 mM. kcat: printed Table 3 kcat cell 138 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 138.0 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 10.4 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 10.4 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 138 / 13.2 = 10.454545454545455 s^-1 mM^-1, against the printed catalytic-efficiency cell 10.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, MTSase form block wild-type, transglycosylation column G4: kcat = 138 s^-1; KM = 13.2 mM; printed kcat/KM = 10.4 s^-1 mM^-1.

row_label: Table 3, MTSase form block wild-type, transglycosylation column G4 (maltotetraose)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P95869 and applied mutation signature Y367F to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant MTSases for Hydrolysis of G3 and Transglycosylation of G4-G7 at 60 C in 50 mM Citrate Phosphate Buffer, pH 5 (J. Agric. Food Chem. 2006, volume 54, number 10, pages 3585-3590); printed column heads MTSase form | hydrolysis G3 | transglycosylation G4 | G5 | G6 | G7. Table 3, MTSase form block Y367F, transglycosylation column G6; printed row label kcat (s-1) = 139; printed row label KM (mM) = 3.78; printed row label kcat/KM (s-1 mM-1) = 36.9. captured primary segment: Y367F MTSase | maltohexaose G6 | kcat 139 s^-1 | KM 3.78 mM | kcat/KM 36.9 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 3 KM cell 3.78 mM; the printed unit is already mM, so no unit conversion applies and the canonical value is 3.78 mM. kcat: printed Table 3 kcat cell 139 s^-1; the printed unit is already s^-1, so no unit conversion applies and the canonical value is 139.0 s^(-1). kcat/Km: printed Table 3 kcat/KM cell 36.9 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no unit conversion applies and the canonical value is 36.9 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 139 / 3.78 = 36.77248677248677 s^-1 mM^-1, against the printed catalytic-efficiency cell 36.9 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, MTSase form block Y367F, transglycosylation column G6: kcat = 139 s^-1; KM = 3.78 mM; printed kcat/KM = 36.9 s^-1 mM^-1.

row_label: Table 3, MTSase form block Y367F, transglycosylation column G6 (maltohexaose)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F405Y to reconstruct the assayed variant sequence.