sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_070323.1 and applied mutation signature H80A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row H80A; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); H80A: app. kcat 0.43 +/- 0.07 s^-1; app. Km(F6P) 20.3 +/- 5.3 mM; kcat/Km 0.02 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=0.43 s^-1; Km=20.3 mM; kcat/Km=0.02 s^-1*mM^-1.


enzyme_display_name: glucose-6-phosphate isomerase

organism: Archaeoglobus fulgidus

substrate_name: D-Fructose 6-phosphate

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_070323.1 and applied mutation signature H80D to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.4; 343.15 K; cofactor NADP+

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row H80D; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); H80D: app. kcat 0.42 +/- 0.06 s^-1; app. Km(F6P) 0.39 +/- 0.05 mM; kcat/Km 1.1 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=0.42 s^-1; Km=0.39 mM; kcat/Km=1.1 s^-1*mM^-1.

data_origin: experimental

enzyme: glucose-6-phosphate isomerase

substrate: D-Fructose 6-phosphate

status: corrected

source: oed


verification_status: verified

sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_070323.1 and applied mutation signature H82A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row H82A; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); H82A: app. kcat 8.0 +/- 1.0 s^-1; app. Km(F6P) 2.0 +/- 0.2 mM; kcat/Km 4.0 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=8.0 s^-1; Km=2.0 mM; kcat/Km=4.0 s^-1*mM^-1.

status: verified


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_070323.1 and applied mutation signature T63A to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row T63A; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); T63A: app. kcat 1.9 +/- 0.1 s^-1; app. Km(F6P) 0.22 +/- 0.04 mM; kcat/Km 8.6 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=1.9 s^-1; Km=0.22 mM; kcat/Km=8.6 s^-1*mM^-1.


mutation_signature: Unknown

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

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row WT; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); WT: app. kcat 32.4 +/- 1.9 s^-1; app. Km(F6P) 0.25 +/- 0.05 mM; kcat/Km 130 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=32.4 s^-1; Km=0.25 mM; kcat/Km=130 s^-1*mM^-1.

row_label: WT


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_accession:NP_070323.1 and applied mutation signature Y160F to reconstruct the assayed variant sequence.

column_label: Table 3. Kinetic constants, apparent nickel concentrations at half maximal velocity, and apparent melting temperature of wild-type and mutant cupin type phosphoglucose isomerase from Archaeoglobus fulgidus; row Y160F; columns app. kcat (s^-1), app. Km (F6P, mM), and kcat/Km (mM^-1 s^-1); Y160F: app. kcat 11.6 +/- 1.0 s^-1; app. Km(F6P) 1.4 +/- 0.4 mM; kcat/Km 8.3 mM^-1*s^-1. The printed central values already use export units, so no unit scaling is applied: kcat=11.6 s^-1; Km=1.4 mM; kcat/Km=8.3 s^-1*mM^-1.


enzyme_display_name: mannose isomerase

organism: Serratia proteamaculans

substrate_name: D-fructose

source_db: uniprot

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: mannose isomerase

substrate: D-fructose

source: uniprot


organism: Geobacillus stearothermophilus

substrate_name: D-Glucose 6-phosphate

kcat_over_km_origin: calculated

substrate: D-Glucose 6-phosphate


organism: Homo sapiens

substrate_name: D-glucose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y341F to reconstruct the assayed variant sequence.

substrate: D-glucose 6-phosphate


enzyme_display_name: mannose-6-phosphate isomerase

organism: Thermus thermophilus

substrate_name: D-Mannose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H50A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

enzyme: mannose-6-phosphate isomerase

substrate: D-Mannose 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q48A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R142A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W13A 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 E132A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E67A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H122A to reconstruct the assayed variant sequence.


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

substrate_name: fructose 6-phosphate

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

proof_lines: kcat is 17.4 sec(-1) with fructose 6-phosphate as substrate.

substrate: fructose 6-phosphate


enzyme_display_name: xylose isomerase

organism: Bacillus coagulans

substrate_name: alpha-D-Fructofuranose

enzyme: xylose isomerase

substrate: alpha-D-Fructofuranose


substrate_name: alpha-D-Glucose

substrate: alpha-D-Glucose


substrate_name: alpha-D-Xylose

substrate: alpha-D-Xylose


substrate_name: D-Fructose

substrate: D-Fructose


substrate_name: D-Glucose

substrate: D-Glucose


substrate_name: D-Xylose

substrate: D-Xylose


substrate_name: D-Xylulose

assay_conditions_summary: pH 7; 308.15 K; buffer this record. Assay condition: 0.028 M Veronal/acetate

column_label: Table 1 (PDF page 5 of 8, journal page 289), substrate row `D-Xylulose`, enzyme source `B. coagulans`, Mn2+ columns: kcat Mn2+ (s^-1) = 11; Km Mn2+ (mM) = 0.40; kcat/Km Mn2+ (s^-1 M^-1) = 27500.

normalized_value_unit_evidence: kcat: printed cell 11 s^-1 is already the export unit s^(-1); the exported value is 11.0 s^(-1). Km: printed cell 0.40 mM is already the export unit mM; the exported value is 0.4 mM. kcat/Km: the paper PRINTS the kcat/Km cell 27500 s^-1 M^-1 for this line and 1 s^-1 M^-1 equals 0.001 s^(-1)*mM^(-1), so the printed cell is 27.5 s^(-1)*mM^(-1); the exported value is 27.5 s^(-1)*mM^(-1).

row_label: Table 1, decoded plain-numeral transcription, substrate row `D-Xylulose`, enzyme source `B. coagulans`

table_label: Table 1 (PDF page 5 of 8, journal page 289) 'Kinetic parameters for D-xylose and D-xylulose'

substrate: D-Xylulose


verification_status: unverified

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D511N with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

status: unverified


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E495Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H100L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H396L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N154Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N386A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q388A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S185A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y274F to reconstruct the assayed variant sequence.


organism: Escherichia coli O157:H7

substrate_name: L-gulose

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

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.

substrate: L-gulose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E372G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E372G/F163L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E372G/V379A to reconstruct the assayed variant sequence.


organism: Lactococcus lactis subsp. lactis


enzyme_display_name: ribose-5-phosphate isomerase

organism: Acetivibrio thermocellus

substrate_name: D-Psicose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

enzyme: ribose-5-phosphate isomerase

substrate: D-Psicose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132D with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132E with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132I with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132K with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R132Q with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.5; 353.15 K; buffer 50 mM Tris-HCl

column_label: Table 2, enzyme row Wild type; column Specific activity (nmol min-1 mg-1) = 1,994; column Km (mM) = 53; column kcat (s-1) = 2,347; column kcat/Km (mM-1 s-1) = 44.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2,347 s-1; the turnover column of this paper is already per second, so no unit conversion applies and the paper value is 2347.0 s^(-1). Km: printed Table 2 cell 53 mM; the Michaelis-constant column of this paper is already in millimolar, so no unit conversion applies and the paper value is 53.0 mM. kcat/Km: printed Table 2 cell 44 mM-1 s-1; the efficiency column of this paper is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 44.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row Wild type: Specific activity = 1,994 nmol min-1 mg-1; Km = 53 mM; kcat = 2,347 s-1; printed kcat/Km = 44 mM-1 s-1.

row_label: Table 2, enzyme row Wild type

table_label: Table 2: Kinetic parameters and specific activities of the wild-type and mutant enzymes at position 132 of ribose-5-phosphate isomerases from C. thermocellum for D-psicose (Appl Microbiol Biotechnol 2011, 89:1859-1866)


organism: Lactobacillus brevis


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K144A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K294A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K356A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K425A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K425D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K425F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K425V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K425W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R207A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R207K to reconstruct the assayed variant sequence.


enzyme_display_name: L-arabinose isomerase

substrate_name: L-Arabinose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D308A with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

enzyme: L-arabinose isomerase

substrate: L-Arabinose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9S467 and applied mutation signature E351A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters determined for US100 L-AIs (wild type and mutants) (J. Bacteriol. 2007, 189(9):3556-3563), enzyme row 'E351A mutant'; column 'Km (mM)' = 30.1 ± 0.09; column 'kcat (min^-1)' = 174.3 ± 0.01; column 'kcat/Km (mM^-1 min^-1)' = 5.79; column 'Activity loss (%)' = 85.

normalized_value_unit_evidence: Km: the printed Table 2 cell is 30.1 mM and the export unit is mM, so no unit conversion applies; the exported value is 30.1 mM. kcat: the printed Table 2 cell is 174.3 min^-1; min^-1 becomes s^-1 on division by 60, so 174.3 / 60 = 2.905 s^-1, which is the exported value 2.905 s^(-1). kcat/Km: the printed Table 2 cell is 5.79 mM^-1 min^-1, which converts as 5.79 / 60 = 0.0965 s^-1 mM^-1. The exported catalytic efficiency 0.09651162790697673 s^(-1)*mM^(-1) is the full-precision quotient 2.905 / 30.1 of those same two printed cells, and the paper's printed efficiency cell is that same quotient carried to the paper's own two-decimal place: 174.3 / 30.1 = 5.790698 mM^-1 min^-1, which the paper prints as 5.79.

raw_value_unit_evidence: Table 2, enzyme row 'E351A mutant': Km = 30.1 ± 0.09 mM; kcat = 174.3 ± 0.01 min^-1; printed kcat/Km = 5.79 mM^-1 min^-1; activity loss = 85 %.

row_label: Table 2, enzyme row 'E351A mutant'


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F279Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F329A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9S467 and applied mutation signature H446A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters determined for US100 L-AIs (wild type and mutants) (J. Bacteriol. 2007, 189(9):3556-3563), enzyme row 'H446A mutant'; column 'Km (mM)' = 30.4 ± 0.28; column 'kcat (min^-1)' = 857.7 ± 0.12; column 'kcat/Km (mM^-1 min^-1)' = 28.21; column 'Activity loss (%)' = 57.

normalized_value_unit_evidence: Km: the printed Table 2 cell is 30.4 mM and the export unit is mM, so no unit conversion applies; the exported value is 30.4 mM. kcat: the printed Table 2 cell is 857.7 min^-1; min^-1 becomes s^-1 on division by 60, so 857.7 / 60 = 14.295 s^-1, which is the exported value 14.295 s^(-1). kcat/Km: the printed Table 2 cell is 28.21 mM^-1 min^-1, which converts as 28.21 / 60 = 0.4701666666666667 s^-1 mM^-1. The exported catalytic efficiency 0.47023026315789473 s^(-1)*mM^(-1) is the full-precision quotient 14.295 / 30.4 of those same two printed cells, and the paper's printed efficiency cell is that same quotient carried to the paper's own two-decimal place: 857.7 / 30.4 = 28.213816 mM^-1 min^-1, which the paper prints as 28.21.

raw_value_unit_evidence: Table 2, enzyme row 'H446A mutant': Km = 30.4 ± 0.28 mM; kcat = 857.7 ± 0.12 min^-1; printed kcat/Km = 28.21 mM^-1 min^-1; activity loss = 57 %.

row_label: Table 2, enzyme row 'H446A mutant'


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

column_label: Table 2: Kinetic parameters determined for US100 L-AIs (wild type and mutants) (J. Bacteriol. 2007, 189(9):3556-3563), enzyme row 'WT'; column 'Km (mM)' = 28.42 ± 0.12; column 'kcat (min^-1)' = 2036.4 ± 0.07; column 'kcat/Km (mM^-1 min^-1)' = 71.65; column 'Activity loss (%)' = 0.

normalized_value_unit_evidence: Km: the printed Table 2 cell is 28.42 mM and the export unit is mM, so no unit conversion applies; the exported value is 28.42 mM. kcat: the printed Table 2 cell is 2036.4 min^-1; min^-1 becomes s^-1 on division by 60, so 2036.4 / 60 = 33.94 s^-1, which is the exported value 33.94 s^(-1). kcat/Km: the printed Table 2 cell is 71.65 mM^-1 min^-1, which converts as 71.65 / 60 = 1.1941666666666668 s^-1 mM^-1. The exported catalytic efficiency 1.1942294159042925 s^(-1)*mM^(-1) is the full-precision quotient 33.94 / 28.42 of those same two printed cells, and the paper's printed efficiency cell is that same quotient carried to the paper's own two-decimal place: 2036.4 / 28.42 = 71.653765 mM^-1 min^-1, which the paper prints as 71.65.

raw_value_unit_evidence: Table 2, enzyme row 'WT': Km = 28.42 ± 0.12 mM; kcat = 2036.4 ± 0.07 min^-1; printed kcat/Km = 71.65 mM^-1 min^-1; activity loss = 0 %.

row_label: Table 2, enzyme row 'WT' (the wild-type US100 L-AI)


substrate_name: L-Fucose

substrate: L-Fucose


organism: Thermococcus litoralis

substrate_name: D-Fructose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E98V to reconstruct the assayed variant sequence.

substrate: D-Fructose 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H137A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H89A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H91A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


organism: Streptomyces violaceoruber

sequence: GVTFHDDDLIPF

wild_type_sequence: GVTFHDDDLIPF


substrate_name: L-ribulose

source_db: brenda

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

assay_conditions_summary: pH 7.5; buffer 50 mM Tris-HCl

proof_lines: in 50 mM Tris-HCl buffer (pH 7.5), at 65°C

substrate: L-ribulose

source: brenda


substrate_name: D-talose

substrate: D-talose


substrate_name: L-ribose

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

substrate: L-ribose


substrate_name: L-tagatose

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

substrate: L-tagatose


substrate_name: D-psicose

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

sequence_source: multiple

assay_conditions_summary: pH 7.5; 338.15 K; buffer 50 mM Tris-HCl

source_databases_merged: brenda skid

substrate: D-psicose


organism: Arthrobacter sp.


substrate_name: D-Lyxose

column_label: Table 3; row D-Lyxose (30 deg C); columns Km (mM), Vmax (umol/min per mg), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 3 row D-Lyxose (30 deg C): Km=86 mM; Vmax=0.086 umol/min per mg; kcat=3.7 min^-1; kcat/Km=0.04 min^-1 mM^-1.

row_label: D-Lyxose (30 deg C)

table_label: Table 3. Kinetic parameters for purified Arthrobacter B3728 D-xylose isomerase

substrate: D-Lyxose


substrate_name: D-Ribose

column_label: Table 3; row D-Ribose (30 deg C); columns Km (mM), Vmax (umol/min per mg), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 3 row D-Ribose (30 deg C): Km=190 mM; Vmax=0.71 umol/min per mg; kcat=30.9 min^-1; kcat/Km=0.16 min^-1 mM^-1.

row_label: D-Ribose (30 deg C)

substrate: D-Ribose


column_label: Table 3; row D-Xylose (30 deg C); columns Km (mM), Vmax (umol/min per mg), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 3 row D-Xylose (30 deg C): Km=3.3 mM; Vmax=12.25 umol/min per mg; kcat=533 min^-1; kcat/Km=162 min^-1 mM^-1.

row_label: D-Xylose (30 deg C)


column_label: Table 3; row L-Arabinose (30 deg C); columns Km (mM), Vmax (umol/min per mg), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 3 row L-Arabinose (30 deg C): Km=280 mM; Vmax=1.8 umol/min per mg; kcat=78.3 min^-1; kcat/Km=0.28 min^-1 mM^-1.

row_label: L-Arabinose (30 deg C)


organism: Leishmania donovani

substrate_name: D-Ribose 5-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession:G9JM00 and applied mutation signature H11N to reconstruct the assayed variant sequence.

column_label: PMID 26953696, PDF page 7 / 20, Table 1, row H11N, columns Km (mM), Vmax (U mg^-1 min^-1), kcat (s^-1), and kcat / Km (M^-1 s^-1).

normalized_value_unit_evidence: Same-row central values: Km 3.40 mM; kcat 32 s^-1; independently printed kcat/Km 9.51202 s^-1 mM^-1 after dividing the M^-1 value by 1000.

table_label: Table 1

substrate: D-Ribose 5-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession:G9JM00 and applied mutation signature H138N to reconstruct the assayed variant sequence.

column_label: PMID 26953696, PDF page 7 / 20, Table 1, row H138N, columns Km (mM), Vmax (U mg^-1 min^-1), kcat (s^-1), and kcat / Km (M^-1 s^-1).

normalized_value_unit_evidence: Same-row central values: Km 8.14 mM; kcat 11 s^-1; independently printed kcat/Km 1.35507 s^-1 mM^-1 after dividing the M^-1 value by 1000.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:G9JM00 and applied mutation signature P47A to reconstruct the assayed variant sequence.

column_label: PMID 26953696, PDF page 7 / 20, Table 1, row P47A, columns Km (mM), Vmax (U mg^-1 min^-1), kcat (s^-1), and kcat / Km (M^-1 s^-1).

normalized_value_unit_evidence: Same-row central values: Km 4.30 mM; kcat 18 s^-1; independently printed kcat/Km 4.24106 s^-1 mM^-1 after dividing the M^-1 value by 1000.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G9JM00 and applied mutation signature Y46F to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for wild type LdRpiB and its mutants), body row 'Y46F'; column 'Km (mM)' = 2.59; column 'kcat (s-1)' = 25; column 'kcat / Km (M-1 s-1)' = 9820.05. The value printed after the plus/minus sign beside each of these cells is the printed uncertainty and is not an exported metric; the 'Vmax (Umg-1min-1)' column of the same line prints 0.401.

normalized_value_unit_evidence: kcat: printed Table 1 cell 25 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 25.0 s^(-1). Km: printed Table 1 cell 2.59 in a column headed Km (mM); mM is already canonical, so no unit conversion applies and the value is 2.59 mM. kcat/Km: printed Table 1 cell 9820.05 in a column headed kcat / Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9820.05 / 1000 = 9.82005 s^-1 mM^-1. Before this pass the live export row carried kcat 25.0 s^(-1), Km 2.59 mM and kcat_over_km 9.652509652509654 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, body row 'Y46F': Km = 2.59 mM; kcat = 25 s-1; printed kcat/Km = 9820.05 in a column headed kcat / Km (M-1 s-1).

row_label: Table 1, row Y46F

table_label: Table 1: Kinetic parameters for wild type LdRpiB and its mutants (PLoS ONE 2016, volume 11, issue 3, article e0150764). Printed column heads, in printed order: the unheaded enzyme-form column; Km (mM); Vmax (Umg-1min-1); kcat (s-1); kcat / Km (M-1 s-1).


column_label: PMID 26953696, PDF page 7 / 20, Table 1, row RpiB (Wt), columns Km (mM), Vmax (U mg^-1 min^-1), kcat (s^-1), and kcat / Km (M^-1 s^-1); footnote ND, not determined.

normalized_value_unit_evidence: Same-row central values: Km 2.51 mM; kcat 29 s^-1; independently printed kcat/Km 11.17548 s^-1 mM^-1 after dividing the M^-1 value by 1000.

row_label: RpiB (Wt)


organism: Actinoplanes missouriensis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F26W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q256D with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D256R to reconstruct the assayed variant sequence.


substrate_name: D-Mannose

substrate: D-Mannose


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

substrate_name: D-mannose 6-phosphate

kcat_display: Not reported

kcat_over_km_display: Not reported

column_label: Abstract reports apparent Km for D-mannose 6-phosphate was 3.03 mM.

raw_value_unit_evidence: Km raw_value=3.03 mM raw_unit=mM

row_label: Pseudomonas aeruginosa PMI-GMP / D-mannose 6-phosphate

table_label: PubMed XML abstract PMID 1846611

substrate: D-mannose 6-phosphate


substrate_name: D-mannose 1-phosphate

substrate: D-mannose 1-phosphate


substrate_name: GTP

substrate: GTP


substrate_name: GDP-D-mannose

substrate: GDP-D-mannose


organism: Spinacia oleracea

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E91A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


organism: Thermotoga maritima

substrate_name: D-allose

substrate: D-allose


substrate_name: D-ribose

substrate: D-ribose


substrate_name: L-talose

substrate: L-talose


organism: Bacillus licheniformis

substrate_name: L-Arabinose

substrate: L-Arabinose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y333F with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y333I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y333V with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y333W with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


organism: Escherichia coli

substrate_name: D-fructose

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

assay_conditions_summary: pH 7

column_label: PubMed abstract reports the D-fructose row with Km 203.7 mM, kcat 27.7 s^-1, and catalytic efficiency 136.0 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=203.7 normalized_unit=mM; kcat normalized_value=27.7 normalized_unit=s^-1; kcat/Km normalized_value=0.136 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: D-fructose kinetic row: Km=203.7+/-6.7 mM; kcat=27.7+/-0.7 s^-1; catalytic efficiency=136.0+/-2.9 M^-1 s^-1

row_label: recombinant Escherichia coli BL21 d-mannose isomerase with d-fructose

table_label: PubMed abstract PMID 27138861

substrate: D-fructose


protein_accession_database: NCBI Protein


organism: Bacillus subtilis

column_label: Table 2 row D-Lyxose lists Km 433 +/- 3 mM, kcat 7089 +/- 78 s^-1, and kcat/Km 16.4 +/- 0.1 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized=433 mM; kcat normalized=7089 s^-1; kcat/Km normalized=16.371824480369515 s^-1 mM^-1 from same-row quotient

row_label: D-Lyxose

table_label: Table 2. Kinetic parameters of B. subtilis mannose 6-phosphate isomerase for aldoses


column_label: Table 2 row D-Ribose lists Km 110 +/- 1 mM, kcat 72 +/- 1 s^-1, and kcat/Km 0.6 +/- 0.01 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized=110 mM; kcat normalized=72 s^-1; kcat/Km normalized=0.6545454545454545 s^-1 mM^-1 from same-row quotient

row_label: D-Ribose


substrate_name: L-allose

column_label: Table 2 row L-Allose lists Km 312 +/- 14 mM, kcat 920 +/- 41 s^-1, and kcat/Km 2.9 +/- 0.2 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized=312 mM; kcat normalized=920 s^-1; kcat/Km normalized=2.948717948717949 s^-1 mM^-1 from same-row quotient

row_label: L-Allose

substrate: L-allose


column_label: Table 2 row D-Mannose lists Km 946 +/- 7 mM, kcat 3748 +/- 240 s^-1, and kcat/Km 3.5 +/- 0.2 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized=946 mM; kcat normalized=3748 s^-1; kcat/Km normalized=3.9619450317124736 s^-1 mM^-1 from same-row quotient

row_label: D-Mannose


organism: Geobacillus thermodenitrificans

substrate_name: D-galactose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C450S/N475K to reconstruct the assayed variant sequence.

substrate: D-galactose


sequence_variant_note: Mutation signature F280N/C450S/N475K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Aeropyrum pernix

substrate_name: D-fructose 6-phosphate

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

column_label: Table I row A. pernix PGI/PMI | F6P alternate 50 C value, Km block, reports 0.21 +/- 0.05 mM.

raw_value_unit_evidence: Table I A. pernix PGI/PMI | F6P alternate 50 C value, Km block, raw value 0.21 +/- 0.05 mM.

table_label: Table I. Molecular and kinetic properties of bifunctional PGI/PMI purified from A. pernix and recombinant PGI/PMI from T. acidophilum

substrate: D-fructose 6-phosphate


column_label: Table I row A. pernix PGI/PMI | M6P, Km block, reports 1.1 +/- 0.3 mM.

raw_value_unit_evidence: Table I A. pernix PGI/PMI | M6P, Km block, raw value 1.1 +/- 0.3 mM.

row_label: A. pernix PGI/PMI | M6P

source_databases_merged: brenda uniprot


substrate_name: D-glucose 6-phosphate

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

substrate: D-glucose 6-phosphate


substrate_name: D-Allose 6-phosphate

substrate: D-Allose 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H99N to reconstruct the assayed variant sequence.


organism: Thermoplasma acidophilum

column_label: Table I row T. acidophilum PGI/PMI | F6P, Km block, reports 0.20 +/- 0.03 mM.

raw_value_unit_evidence: Table I T. acidophilum PGI/PMI | F6P, Km block, raw value 0.20 +/- 0.03 mM.

row_label: T. acidophilum PGI/PMI | F6P


column_label: Table I row T. acidophilum PGI/PMI | M6P, Km block, reports 0.25 +/- 0.03 mM.

raw_value_unit_evidence: Table I T. acidophilum PGI/PMI | M6P, Km block, raw value 0.25 +/- 0.03 mM.

row_label: T. acidophilum PGI/PMI | M6P


column_label: Table I; T. acidophilum column; Km block; F6P row; raw Km value 0.20 +/- 0.03 mM; normalized Km=0.2 mM.

raw_value_unit_evidence: Table I gives T. acidophilum F6P Km 0.20 +/- 0.03 mM.

row_label: T. acidophilum F6P row

table_label: PMID 14551194, Table I: Molecular and kinetic properties of bifunctional PGI/PMI


column_label: Table I; T. acidophilum column; Km block; M6P row; raw Km value 0.25 +/- 0.03 mM; normalized Km=0.25 mM.

raw_value_unit_evidence: Table I gives T. acidophilum M6P Km 0.25 +/- 0.03 mM.

row_label: T. acidophilum M6P row


organism: Bacillus halodurans

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E268K to reconstruct the assayed variant sequence.


column_label: Table I; A. pernix column; Km block; F6P row; raw Km value 0.21 +/- 0.05 mM; normalized Km=0.21 mM.

raw_value_unit_evidence: Table I gives A. pernix F6P Km 0.44 +/- 0.10 mM at 80 C and a separate 0.21 +/- 0.05 mM value explicitly labeled 50 C.

row_label: A. pernix F6P row, alternate 50 C value


column_label: Table I; A. pernix column; Km block; M6P row; raw Km value 1.1 +/- 0.3 mM; normalized Km=1.1 mM.

raw_value_unit_evidence: Table I gives A. pernix M6P Km 1.1 +/- 0.3 mM.

row_label: A. pernix M6P row


organism: Anoxybacillus flavithermus


organism: Streptomyces rubiginosus

substrate_name: D-glyceraldehyde

substrate: D-glyceraldehyde


substrate_name: D-Xylose

substrate: D-Xylose


organism: Saccharomyces cerevisiae

substrate_name: D-Ribose 5-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R189K to reconstruct the assayed variant sequence.

substrate: D-Ribose 5-phosphate


organism: Vibrio sp.

substrate_name: D-glucose

substrate: D-glucose


organism: Pyrobaculum aerophilum


substrate_name: D-mannose 6-phosphate

substrate: D-mannose 6-phosphate


organism: Geobacillus stearothermophilus

substrate_name: L-arabinose

assay_conditions_summary: pH 7.5; buffer pH 7

column_label: Official ScienceDirect HTML Table 4 reports l-arabinose for B. stearothermophilus US100: Vmax 41.8 U/mg, Km 28.57 mM, kcat/Km 71.4 min^-1 mM^-1, reference This study; the exact cell does not equal the exported 28.42 mM.

raw_value_unit_evidence: Km raw_value=28.57 raw_unit=mM

row_label: l-arabinose / B. stearothermophilus US100

table_label: Table 4 - Kinetic properties of L-AIs from several organisms

substrate: L-arabinose


column_label: Official ScienceDirect HTML Table 4 reports d-galactose for B. stearothermophilus US100: Vmax 8.9 U/mg, Km 57 mM, kcat/Km 8.48 min^-1 mM^-1, reference This study.

raw_value_unit_evidence: Km raw_value=57 raw_unit=mM

row_label: d-galactose / B. stearothermophilus US100


organism: Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)

substrate_name: fructose 6-phosphate (at 50 degrees Celsius)


substrate_name: mannose 6-phosphate (at 80 degrees Celsius)


organism: Methanocaldococcus jannaschii


organism: Arabidopsis thaliana

column_label: The abstract reports the apparent Km for Man-6P of purified recombinant PMI2 was 372+/-13 microM.

raw_value_unit_evidence: Km raw_value=372+/-13 microM raw_unit=microM

row_label: Prose segment: PMI2 Man-6P Km

table_label: PubMed PMID 18755683 abstract


column_label: The abstract reports the apparent Km for Man-6P of purified recombinant PMI1 was 41.3+/-4.2 microM.

raw_value_unit_evidence: Km raw_value=41.3+/-4.2 microM raw_unit=microM

row_label: Prose segment: PMI1 Man-6P Km


substrate_name: glucose 6-phosphate (at 50 degrees Celsius)


substrate: fructose 6-phosphate (at 50 degrees Celsius)


organism: Mycobacterium tuberculosis


organism: Thermoanaerobacter mathranii

substrate_name: D-fucose

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

substrate: D-fucose


organism: Lactobacillus plantarum

substrate_name: D-Galactose

substrate: D-Galactose


substrate_name: L-Arabinose


organism: Lactobacillus sakei


organism: Rattus norvegicus

column_label: Abstract states apparent Km and Vmax were 0.593 +/- 0.031 mM and 2291 +/- 61 nmol/min/mg protein for glucose 6-phosphate.

raw_value_unit_evidence: Km raw_value=0.593 mM raw_unit=mM

row_label: Rat brain phosphoglucose isomerase / glucose 6-phosphate

table_label: PubMed XML abstract


column_label: Abstract states apparent Km and Vmax were 0.095 +/- 0.013 mM and 2035 +/- 98 nmol/min/mg protein for fructose 6-phosphate.

raw_value_unit_evidence: Km raw_value=0.095 mM raw_unit=mM

row_label: Rat brain phosphoglucose isomerase / fructose 6-phosphate


organism: Thermoanaerobacter ethanolicus

substrate_name: D-xylose

assay_conditions_summary: pH 7; buffer 100 mM MOPS

substrate: D-xylose


organism: Escherichia coli (strain K12)

substrate_name: D-allose 6-phosphate

substrate: D-allose 6-phosphate


organism: Pyrococcus furiosus

substrate_name: L-talose

proof_lines:
pH 7.0, 95°C
Raw SKiD Env: Temp=95°C, pH=7

substrate: L-talose


organism: [Clostridium] hylemonae

substrate_name: D-galactose


substrate_name: D-ribose 5-phosphate (at 37 degrees Celsius)


organism: Homo sapiens


organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)

substrate_name: fructose 6-phosphate

column_label: Table I; A. pernix column; Km block; F6P row; raw Km value 0.44 +/- 0.10 mM; normalized Km=0.44 mM.

raw_value_unit_evidence: Table I gives A. pernix F6P Km 0.44 +/- 0.10 mM.

row_label: A. pernix F6P row

substrate: fructose 6-phosphate


organism: Pseudoalteromonas haloplanktis

column_label: PubMed XML abstract PMID 27586234, same L-arabinose measurement: Km 111.68 mM; kcat 773.30 min^-1; kcat/Km 6.92 mM^-1 min^-1.

normalized_value_unit_evidence: Preserve catalog-rounded Km 111.7 mM and kcat 12.9 s^-1; normalize the independently printed ratio to 0.11533333333333333 s^-1 mM^-1.

raw_value_unit_evidence: PubMed abstract: Km 111.68 mM; kcat 773.30 min^-1; independently printed kcat/Km 6.92 mM^-1 min^-1.

row_label: recombinant Pseudoalteromonas haloplanktis L-arabinose isomerase / L-arabinose

table_label: PubMed XML abstract (no table)

substrate: L-Arabinose


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


organism: Pseudomonas aeruginosa

substrate_name: D-Mannose 6-phosphate

substrate: D-Mannose 6-phosphate


organism: Saccharomyces cerevisiae


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


substrate_name: D-Fructose 6-phosphate

substrate: D-Fructose 6-phosphate


organism: Chlorella variabilis


organism: Oryctolagus cuniculus


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Mycobacterium tuberculosis

substrate_name: D-fructose 6-phosphate

assay_conditions_summary: pH 7.6; buffer assay

column_label: PMID 17126561 Determination of kinetic constants/Fig. 5A, rPGI-His6 with fructose-6-phosphate, Km = 0.27 +/- 0.03 mM.

raw_value_unit_evidence: Kinetic constants prose/Fig. 5A reports Km = 0.27 +/- 0.03 mM for fructose-6-phosphate.

row_label: rPGI-His6 / fructose-6-phosphate

table_label: Determination of kinetic constants prose and Fig. 5A

substrate: D-fructose 6-phosphate


organism: Geobacillus thermodenitrificans

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


substrate: D-galactose


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


substrate_name: D-Glucose 6-phosphate

substrate: D-Glucose 6-phosphate


organism: Archaeoglobus fulgidus


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


organism: Alicyclobacillus hesperidum


substrate_name: L-arabinose


organism: Thermus thermophilus

substrate_name: D-glucose


substrate_name: D-glucose; D-mannose

proof_lines:
60°C, pH 7, wild-type
wild type enzyme, at pH 7.0 and 85°C

substrate: D-glucose; D-mannose


substrate: D-glucose


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Limosilactobacillus fermentum

proof_lines: mutant enzyme D268K/D269K/D299K, at pH 5.0 and 65°C

proof_lines: mutant enzyme D268K/D269K/D299K, at pH 4.0 and 65°C

proof_lines: mutant enzyme D268K/D269K/D299K, at pH 6.0 and 65°C


proof_lines: mutant enzyme D269K/D299K, at pH 5.0 and 65°C

proof_lines: mutant enzyme D269K/D299K, at pH 6.0 and 65°C

proof_lines: mutant enzyme D269K/D299K, at pH 4.0 and 65°C


proof_lines:
wild type enzyme, at pH 6.0 and 65°C
wild type enzyme, at pH 5.0 and 65°C


proof_lines:
mutant enzyme D299K, at pH 5.0 and 65°C
mutant enzyme D299K, at pH 6.0 and 65°C
mutant enzyme D299K, at pH 4.0 and 65°C


proof_lines:
mutant enzyme D299R, at pH 5.0 and 65°C
mutant enzyme D299R, at pH 6.0 and 65°C
mutant enzyme D299R, at pH 4.0 and 65°C


proof_lines:
mutant enzyme D268K, at pH 6.0 and 65°C
mutant enzyme D268K, at pH 5.0 and 65°C
mutant enzyme D268K, at pH 4.0 and 65°C


proof_lines:
mutant enzyme D269K, at pH 6.0 and 65°C
mutant enzyme D269K, at pH 5.0 and 65°C
mutant enzyme D269K, at pH 4.0 and 65°C


proof_lines: mutant enzyme D268K/D269K, at pH 5.0 and 65°C

proof_lines: mutant enzyme D268K/D269K, at pH 6.0 and 65°C

proof_lines: mutant enzyme D268K/D269K, at pH 4.0 and 65°C


proof_lines: mutant enzyme D268K/D299K, at pH 6.0 and 65°C

proof_lines: mutant enzyme D268K/D299K, at pH 5.0 and 65°C

proof_lines: mutant enzyme D268K/D299K, at pH 4.0 and 65°C


substrate_name: D-glucose 6-phosphate

assay_conditions_summary: pH 7.5; 294.15 K; buffer 20 mM HEPES

proof_lines: mutant enzyme D511N, at 21°C in 20 mM HEPES buffer (pH 7.5)

substrate: D-glucose 6-phosphate


proof_lines: mutant enzyme H100L, at 21°C in 20 mM HEPES buffer (pH 7.5)


proof_lines: mutant enzyme E495Q, at 21°C in 20 mM HEPES buffer (pH 7.5)


proof_lines: wild type enzyme, at 21°C in 20 mM HEPES buffer (pH 7.5)


proof_lines: mutant enzyme H396L, at 21°C in 20 mM HEPES buffer (pH 7.5)


proof_lines: mutant enzyme Y274F, at 21°C in 20 mM HEPES buffer (pH 7.5)


proof_lines: mutant enzyme Y341F, at 21°C in 20 mM HEPES buffer (pH 7.5)


proof_lines: mutant enzyme S185A, at 21°C in 20 mM HEPES buffer (pH 7.5)


proof_lines: mutant enzyme N386A, at 21°C in 20 mM HEPES buffer (pH 7.5)


proof_lines: mutant enzyme N154Q, at 21°C in 20 mM HEPES buffer (pH 7.5)


organism: Actinoplanes missouriensis


proof_lines:
mutant H220Q
D-xylose, mutant H220Q


proof_lines:
mutant H220Q
D-glucose, mutant H220Q


proof_lines:
wild-type enzyme
wild-type


substrate_name: D-fructose

substrate: D-fructose


organism: Streptomyces pseudogriseolus

proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant E221A


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D56N


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D163N/E167Q


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D65A


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D81A


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, wild-type

proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D81A and wild-type


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutants E221A and D56N


substrate_name: D-mannose 6-phosphate

substrate: D-mannose 6-phosphate


organism: Thermococcus litoralis


proof_lines: 50°C, pH 7.5, D-fructose 6-phosphate as substrate


substrate_name: D-xylose

proof_lines: mutant enzyme D57H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme D57H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme E186Q/N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme E186Q/N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme K289H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme K289H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme K289E, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme K289E, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme N247D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme N247D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme Q256D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


proof_lines: recombinant His12-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: recombinant His6-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: native wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme D57N, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme D57N, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


organism: Bacillus licheniformis

substrate: L-arabinose


proof_lines: pH 7.5, 50°C, recombinant wild-type enzyme


organism: Geobacillus stearothermophilus


substrate_name: L-fucose

substrate: L-fucose


organism: Brucella anthropi

substrate_name: D-allose

substrate: D-allose


proof_lines: recombinant mutant S9T/S98H/S134H, pH 7.5, 50°C


proof_lines: recombinant mutant S98H/S134H, pH 7.5, 50°C


substrate_name: L-ribulose

substrate: L-ribulose


organism: Bacillus subtilis

substrate_name: D-ribose

substrate: D-ribose


substrate_name: L-allose

substrate: L-allose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: L-ribose

substrate: L-ribose


proof_lines:
wild-type
wild-type enzyme


substrate: D-xylose


organism: Clostridioides difficile

substrate_name: L-talose

substrate: L-talose


proof_lines:
pH 7.5 and 40°C
pH 7.5, 40°C


substrate_name: D-ribose 5-phosphate

substrate: D-ribose 5-phosphate


organism: Streptomyces olivochromogenes

substrate_name: xylulose

substrate: xylulose


substrate_name: D-glucose

substrate: D-glucose


substrate_name: D-fructose 6-phosphate

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

substrate: D-fructose 6-phosphate


substrate: D-glucose 6-phosphate


substrate_name: Unknown

substrate: Unknown


substrate_name: L-arabinose


substrate_name: D-galactose

proof_lines:
mutant C450S/N475K, pH 8, 55°C
C450S /N475K mutant

substrate: D-galactose


substrate: L-arabinose


organism: Escherichia coli


substrate_name: D-glucose 6-phosphate


organism: Arthrobacter sp.

substrate_name: D-Lyxose

proof_lines:
30°C
D-xylose, with 30 mM Mg2+
D-xylose, 30°C

substrate: D-Lyxose


substrate_name: D-fructose

substrate: D-fructose


organism: Homo sapiens

substrate_name: fructose 6-phosphate

proof_lines:
mutant enzyme Thr224 to Met
mutant enzyme Thr5 to Ile
mutant enzyme Asp539 to Asn

substrate: fructose 6-phosphate


substrate_name: glucose 6-phosphate

substrate: glucose 6-phosphate


organism: Geobacillus thermodenitrificans

proof_lines: in the presence of 10 mM Mn2+, enzyme treated with EDTA

proof_lines: in the presence of 1 mM Mn2+, enzyme treated with EDTA


organism: Methanosarcina mazei


organism: Oryctolagus cuniculus

proof_lines: muscle enzyme, values of 0.03 mM, 0.31 mM and 0.8 mM are determined by different authors


organism: Sinorhizobium meliloti


organism: Spinacia oleracea

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


organism: Streptomyces sp.


substrate_name: D-xylose


organism: Streptomyces albus


substrate_name: L-rhamnose

substrate: L-rhamnose


organism: Thermoanaerobacterium saccharolyticum


organism: Lactococcus lactis


organism: Thermus thermophilus

substrate_name: D-mannose

substrate: D-mannose


proof_lines:
wild type enzyme, at pH 7.0 and 85°C
60°C, pH 7, wild-type


organism: Alicyclobacillus acidocaldarius

proof_lines:
pH 6.0, 65°C, recombinant enzyme
pH 7.5, 75°C, recombinant enzyme


organism: Alicyclobacillus hesperidum


organism: Salmonella enterica


proof_lines:
wild-type at pH 8 and 65°C
wild-type at pH 7 and 65°C
wild-type at pH 6 and 65°C


organism: Anoxybacillus flavithermus

assay_conditions_summary: pH 9.5; 368.15 K; buffer 50 mM glycine-NaOH

proof_lines: in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C


proof_lines: without borate, in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C

proof_lines: with 10 mM borate, in 50 mM glycine-NaOH buffer (pH 9.5), at 95°C


organism: Bacillus subtilis

substrate_name: L-aldose

proof_lines: pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme

substrate: L-aldose


substrate_name: L-ribulose

substrate: L-ribulose


organism: Bacillus sp. (in: firmicutes)


substrate: D-xylose


organism: Bifidobacterium adolescentis


organism: Bifidobacterium longum

proof_lines:
at pH 6.5 and 45°C
pH 6.0-6.5, 55°C, recombinant enzyme


organism: Candida albicans

substrate_name: mannose 6-phosphate

assay_conditions_summary: buffer selenomethionine-labelled enzyme Hepes buffer selenomethionine-labelled enzyme

proof_lines: selenomethionine-labelled enzyme, Hepes buffer

substrate: mannose 6-phosphate


organism: Brucella anthropi

substrate_name: D-allose

proof_lines: pH 7.5, 45°C, recombinant wild-type enzyme

proof_lines: pH 7.0, 45°C, recombinant wild-type enzyme

proof_lines: recombinant wild-type enzyme, pH 7.5, 50°C

substrate: D-allose


proof_lines: pH 7.5, 45°C, recombinant mutant A10T/T32S/G101N


organism: Bacteroides stercoris

assay_conditions_summary: pH 7.5; 303.15 K; buffer 100 mM Tris-HCl

proof_lines: in 100 mM Tris-HCl buffer (pH 7.5), 10 mM MgCl2, at 30°C


substrate_name: D-mannose 6-phosphate

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

substrate: D-mannose 6-phosphate


organism: Cricetulus griseus


organism: Enterococcus faecium

proof_lines:
at pH 7.0 and 50°C
pH 7.0-7.5, 45-50°C, recombinant enzyme


organism: Escherichia coli

substrate_name: D-ribose 5-phosphate

proof_lines:
ribosephosphate isomerase B
ribosephosphate isomerase A

substrate: D-ribose 5-phosphate


substrate_name: Unknown


substrate_name: beta-D-mannose 6-phosphate

assay_conditions_summary: pH 7.1; 298.15 K; buffer 50 mM HEPES

proof_lines:
in 50 mM HEPES buffer, pH 7.1, at 25°C
22°C, pH 7.4

substrate: beta-D-mannose 6-phosphate


proof_lines:
in 50 mM HEPES buffer, pH 7.1, at 25°C
pH 7.1, 25°C, recombinant enzyme

substrate: Unknown


substrate_name: D-tagatose

proof_lines:
pH 7.0, 37°C, purified enzyme
pH 7.0, 37°C, whole cells

substrate: D-tagatose


substrate_name: D-galactose

substrate: D-galactose


organism: Geobacillus stearothermophilus

proof_lines: pH 8.0, 60°C, recombinant enzyme expressed in Escherichia coli

proof_lines: pH 8.0, 60°C, recombinant enzyme expressed in Bacillus subtilis


substrate_name: L-arabinose

proof_lines: in the presence of 0.8 mM Mn2+, at pH 7.5 and 60°C

substrate: L-arabinose


proof_lines: without borate, pH 8.0, 60°C, recombinant wild-type enzyme

proof_lines: with borate, pH 8.0, 60°C, recombinant wild-type enzyme


proof_lines: pH 8.0, 60°C, recombinant wild-type enzyme


organism: Geobacillus kaustophilus


substrate_name: D-xylulose

substrate: D-xylulose


substrate_name: D-fructose

substrate: D-fructose


organism: Halalkalibacterium halodurans


organism: Heyndrickxia coagulans


substrate_name: D-glucose

substrate: D-glucose


organism: Homo sapiens

substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


substrate_name: D-glucose 6-phosphate

substrate: D-glucose 6-phosphate


organism: Klebsiella aerogenes


substrate_name: glucose 6-phosphate

substrate: glucose 6-phosphate


organism: Lactiplantibacillus plantarum

substrate: L-ribulose


proof_lines:
at 60°C, pH 7.5
pH 7.5, 60°C, recombinant enzyme


organism: Lentilactobacillus parabuchneri


organism: Latilactobacillus sakei

assay_conditions_summary: pH 5; buffer 100 mM sodium acetate

proof_lines: with 0.8 mM MgCl2 and 0.8 mM MnCl2, in 100 mM sodium acetate buffer (pH 5.0), at 35°C


proof_lines:
wild-type at pH 6 and 50°C
wild-type at pH 7 and 50°C
wild-type at pH 8 and 50°C


proof_lines:
mutant E268K at pH 6 and 50°C
mutant E268K at pH 8 and 50°C
mutant E268K at pH 7 and 50°C


organism: Limosilactobacillus fermentum

assay_conditions_summary: pH 6.5; 338.15 K; buffer 50 mM phosphate

proof_lines: in 50 mM phosphate buffer (pH 6.5), 1mM Mn2+, 2mM Co2+, at 65°C


organism: Levilactobacillus brevis

substrate_name: D-ribose

substrate: D-ribose


organism: Mus musculus

substrate_name: fructose 6-phosphate

substrate: fructose 6-phosphate


organism: Limosilactobacillus reuteri


substrate_name: D-xylose

substrate: D-xylose


organism: Piromyces sp.

proof_lines: wild type enzyme, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C


proof_lines: mutant enzyme E129D/V433I, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C


enzyme_display_name: glutamate racemase

organism: Pediococcus pentosaceus

substrate_name: L-Glu

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

enzyme: glutamate racemase

substrate: L-Glu


substrate: D-ribose 5-phosphate


organism: Lathyrus oleraceus

substrate_name: D-ribulose 5-phosphate

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

substrate: D-ribulose 5-phosphate


substrate_name: D-ribose 5-phosphate


organism: Saccharomyces cerevisiae

substrate_name: D-mannose 6-phosphate

substrate: D-mannose 6-phosphate


substrate_name: Unknown

proof_lines:
pH 7.1, 25°C
pH 7.1, 25°C, recombinant enzyme

substrate: Unknown


organism: Pseudomonas aeruginosa


assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM HEPES

proof_lines:
in 50 mM HEPES buffer, pH 7.1, at 25°C
pH 8.0


proof_lines: values of 0.27 mM, 0.3 mM, 0.7 mM, 0.8 mM and 1.5 mM are determined by different authors


organism: Streptomyces pseudogriseolus

substrate_name: D-glyceraldehyde

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

proof_lines: in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C

substrate: D-glyceraldehyde


organism: Streptomyces sp. 32


organism: Streptomyces sp. 1


organism: Shewanella sp. ANA-3

substrate: L-arabinose


substrate_name: D-galactose

substrate: D-galactose


substrate_name: L-arabinose


organism: Thermotoga petrophila


substrate_name: alpha-D-xylopyranose

substrate: alpha-D-xylopyranose


enzyme_display_name: protein disulfide-isomerase

organism: Triticum aestivum

substrate_name: ribonuclease

enzyme: protein disulfide-isomerase

substrate: ribonuclease


organism: Thermus thermophilus


organism: Arabidopsis thaliana


organism: Thermotoga neapolitana

proof_lines:
pH 7.0, 85°C
pH 7.0, 85°C, recombinant enzyme


organism: Bacillus amyloliquefaciens


organism: Bacillus cereus

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

proof_lines: in presence of 0.5 mM UDP-N-acetylglucosamine

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


organism: Vibrio sp.

substrate_name: D-glucose

assay_conditions_summary: pH 7.5; buffer 50 mM sodium phosphate

proof_lines: in 50 mM sodium phosphate buffer (pH 7.5), at 40°C

substrate: D-glucose


enzyme_display_name: phosphopentomutase

proof_lines: in 25 mM Tris-HCl, pH 8.0, and 0.1 mM MnCl2, 0.0005 mM glucose 1,6-bisphosphate,at 23°C

enzyme: phosphopentomutase


organism: Bacillus licheniformis

assay_conditions_summary: pH 7.5; 323.15 K; buffer 50 mM phosphate

proof_lines: pH and temperature not specified in the publication

proof_lines: immobilized enzyme, in 50 mM phosphate buffer (pH 7.5),1 mM MnCl2, at 50°C


enzyme_display_name: L-rhamnose isomerase

organism: Thermobacillus composti

substrate_name: L-rhamnose

enzyme: L-rhamnose isomerase

substrate: L-rhamnose


substrate_name: L-Mannose

substrate: L-Mannose


substrate_name: D-psicose

substrate: D-psicose


substrate_name: D-allose

substrate: D-allose


enzyme_display_name: UniProt Q75WH8

organism: Pseudomonas stutzeri

substrate_name: D-ribose

source_db: skid

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=35°C, pH=9
Raw SKiD Env: Temp=50°C, pH=9

enzyme: UniProt Q75WH8

substrate: D-ribose

source: skid


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=35°C, pH=9
Raw SKiD Env: Temp=50°C, pH=9


substrate_name: L-Lyxose

substrate: L-Lyxose


organism: Bacillus subtilis


substrate_name: L-Rhamnose

substrate: L-Rhamnose


enzyme_display_name: D-lyxose ketol-isomerase

organism: Paenibacillus baekrokdamisoli

substrate_name: D-allulose

enzyme: D-lyxose ketol-isomerase

substrate: D-allulose


organism: Thermosediminibacter oceani

substrate_name: D-fructose

substrate: D-fructose


substrate_name: D-Lyxose

substrate: D-Lyxose


substrate_name: D-Mannose

substrate: D-Mannose


proof_lines: pH 7, 25°C, in presence of dihexanoylphosphatidylcholine

proof_lines: pH 7, 25°C, in absence of dihexanoylphosphatidylcholine


enzyme_display_name: lysine 2,3-aminomutase

substrate_name: L-lysine

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

enzyme: lysine 2,3-aminomutase

substrate: L-lysine


enzyme_display_name: beta-phosphoglucomutase

substrate_name: beta-D-glucose 1-phosphate

proof_lines:
phosphoglucomutase activity
1-phosphate phosphodismutase activity

enzyme: beta-phosphoglucomutase

substrate: beta-D-glucose 1-phosphate


organism: Arthrobacter sp.

substrate_name: D-galactose

substrate: D-galactose


enzyme_display_name: ribulose-phosphate 3-epimerase

organism: Bacillus methanolicus

substrate_name: D-ribulose 5-phosphate

enzyme: ribulose-phosphate 3-epimerase

substrate: D-ribulose 5-phosphate


enzyme_display_name: S-ribosylhomocysteine lyase

substrate_name: S-ribosylhomocysteine

enzyme: S-ribosylhomocysteine lyase

substrate: S-ribosylhomocysteine


proof_lines:
Fe2+ containing BsLuxS
Co2+ substituted BsLuxS
native enzyme


organism: Stutzerimonas stutzeri

assay_conditions_summary: pH 9; 308.15 K; buffer 50 mM glycine-NaOH

proof_lines: mutant enzyme S329F, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C


proof_lines: mutant enzyme S329K, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C


proof_lines: mutant enzyme S329L, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C


proof_lines: mutant enzyme S329A, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C


proof_lines: wild type enzyme, in 50 mM glycine-NaOH buffer (pH 9.0), 1 mM MnCl2, at 35°C


enzyme_display_name: glucuronate isomerase

organism: Escherichia coli

substrate_name: D-Glucuronate

enzyme: glucuronate isomerase

substrate: D-Glucuronate


substrate_name: L-rhamnose

substrate: L-rhamnose


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


substrate_name: L-Xylose

substrate: L-Xylose


substrate_name: D-glucose

substrate: D-glucose


substrate_name: D-altrose

substrate: D-altrose


substrate_name: D-xylose

substrate: D-xylose


substrate_name: L-rhamnulose

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

substrate: L-rhamnulose


organism: Thermotoga maritima

assay_conditions_summary: pH 8; 358.15 K; buffer 50 mM EPPS

proof_lines: purified enzyme, at 85°C for 10 min in 50 mM EPPS buffer (pH 8.0)


substrate_name: L-Fructose

substrate: L-Fructose


substrate_name: L-xylulose

substrate: L-xylulose


substrate_name: L-Mannose

substrate: L-Mannose


substrate_name: L-Lyxose

substrate: L-Lyxose


organism: Thermoprotei archaeon

substrate_name: D-fructose

substrate: D-fructose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: D-Lyxose

substrate: D-Lyxose


substrate_name: L-ribose

substrate: L-ribose


enzyme_display_name: arabinose-5-phosphate isomerase

organism: Acidipropionibacterium acidipropionici

substrate_name: D-arabinose 5-phosphate

enzyme: arabinose-5-phosphate isomerase

substrate: D-arabinose 5-phosphate


substrate_name: D-allose

substrate: D-allose


proof_lines: mutant enzyme H101N, pH and temperature not specified in the publication


organism: Clostridium tetani

substrate_name: D-ribulose 5-phosphate

substrate: D-ribulose 5-phosphate


organism: Caldanaerobius polysaccharolyticus


organism: Thermoflavimicrobium dichotomicum


substrate_name: L-rhamnose

proof_lines: 50°C, pH 9.0, intrinsic enzyme from Pseudomonas stutzeri

substrate: L-rhamnose


organism: Thermofilum sp. ex4484_79


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

substrate_name: ProFAR

substrate: ProFAR


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9X0C7 and applied mutation signature R83N to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Enzyme Kinetic Constants for Wild-Type (WT) and Mutant tHisA and tTrpF Enzymes (Biochemistry 2002, 41(40):12032-12042); printed metric rows kcat (s-1), KmProFAR (uM) and kcat/KmProFAR (uM-1 s-1); the table is printed transposed, with the enzyme forms as its columns. Table 3, tHisA enzyme column 'R83N tHisA'; metric row kcat (s-1) = 0.23; metric row KmProFAR (uM) = 37.9; metric row kcat/KmProFAR (uM-1 s-1) = 0.006. captured primary segment: R83N tHisA | kcat 0.23 s^-1 | Km(ProFAR) 37.9 uM | kcat/Km(ProFAR) 0.006 uM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.23 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.23 s^(-1). Km: printed Table 3 cell 37.9 uM; 1 uM is 1/1000 mM, so 37.9 / 1000 = 0.0379 mM. kcat/Km: printed Table 3 cell 0.006 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.006 x 1000 = 6.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, tHisA enzyme column 'R83N tHisA': kcat = 0.23 s^-1; Km(ProFAR) = 37.9 uM; printed kcat/Km(ProFAR) = 0.006 uM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9X0C7 and applied mutation signature D127N to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Enzyme Kinetic Constants for Wild-Type (WT) and Mutant tHisA and tTrpF Enzymes (Biochemistry 2002, 41(40):12032-12042); printed metric rows kcat (s-1), KmProFAR (uM) and kcat/KmProFAR (uM-1 s-1); the table is printed transposed, with the enzyme forms as its columns. Table 3, tHisA enzyme column 'D127N tHisA'; metric row kcat (s-1) = 0.00027; metric row KmProFAR (uM) = 2.0; metric row kcat/KmProFAR (uM-1 s-1) = 0.00013. captured primary segment: D127N tHisA | kcat 0.00027 s^-1 | Km(ProFAR) 2.0 uM | kcat/Km(ProFAR) 0.00013 uM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.00027 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.00027 s^(-1). Km: printed Table 3 cell 2.0 uM; 1 uM is 1/1000 mM, so 2.0 / 1000 = 0.002 mM. kcat/Km: printed Table 3 cell 0.00013 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.00013 x 1000 = 0.13 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, tHisA enzyme column 'D127N tHisA': kcat = 0.00027 s^-1; Km(ProFAR) = 2.0 uM; printed kcat/Km(ProFAR) = 0.00013 uM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9X0C7 and applied mutation signature H48A to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Enzyme Kinetic Constants for Wild-Type (WT) and Mutant tHisA and tTrpF Enzymes (Biochemistry 2002, 41(40):12032-12042); printed metric rows kcat (s-1), KmProFAR (uM) and kcat/KmProFAR (uM-1 s-1); the table is printed transposed, with the enzyme forms as its columns. Table 3, tHisA enzyme column 'H48A tHisA'; metric row kcat (s-1) = 0.38; metric row KmProFAR (uM) = 2.9; metric row kcat/KmProFAR (uM-1 s-1) = 0.131. captured primary segment: H48A tHisA | kcat 0.38 s^-1 | Km(ProFAR) 2.9 uM | kcat/Km(ProFAR) 0.131 uM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.38 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.38 s^(-1). Km: printed Table 3 cell 2.9 uM; 1 uM is 1/1000 mM, so 2.9 / 1000 = 0.0029 mM. kcat/Km: printed Table 3 cell 0.131 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.131 x 1000 = 131.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, tHisA enzyme column 'H48A tHisA': kcat = 0.38 s^-1; Km(ProFAR) = 2.9 uM; printed kcat/Km(ProFAR) = 0.131 uM^-1 s^-1.


proof_lines:
25°C, pH 7.5, wild-type enzyme
37°C, pH 7.5, wild-type enzyme
80°C, pH 7.5, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9X0C7 and applied mutation signature T164A to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Enzyme Kinetic Constants for Wild-Type (WT) and Mutant tHisA and tTrpF Enzymes (Biochemistry 2002, 41(40):12032-12042); printed metric rows kcat (s-1), KmProFAR (uM) and kcat/KmProFAR (uM-1 s-1); the table is printed transposed, with the enzyme forms as its columns. Table 3, tHisA enzyme column 'T164A tHisA'; metric row kcat (s-1) = 0.018; metric row KmProFAR (uM) = 5.6; metric row kcat/KmProFAR (uM-1 s-1) = 0.003. captured primary segment: T164A tHisA | kcat 0.018 s^-1 | Km(ProFAR) 5.6 uM | kcat/Km(ProFAR) 0.003 uM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.018 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.018 s^(-1). Km: printed Table 3 cell 5.6 uM; 1 uM is 1/1000 mM, so 5.6 / 1000 = 0.0056 mM. kcat/Km: printed Table 3 cell 0.003 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.003 x 1000 = 3.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, tHisA enzyme column 'T164A tHisA': kcat = 0.018 s^-1; Km(ProFAR) = 5.6 uM; printed kcat/Km(ProFAR) = 0.003 uM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9X0C7 and applied mutation signature D51N to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Enzyme Kinetic Constants for Wild-Type (WT) and Mutant tHisA and tTrpF Enzymes (Biochemistry 2002, 41(40):12032-12042); printed metric rows kcat (s-1), KmProFAR (uM) and kcat/KmProFAR (uM-1 s-1); the table is printed transposed, with the enzyme forms as its columns. Table 3, tHisA enzyme column 'D51N tHisA'; metric row kcat (s-1) = 0.29; metric row KmProFAR (uM) = 6.4; metric row kcat/KmProFAR (uM-1 s-1) = 0.046. captured primary segment: D51N tHisA | kcat 0.29 s^-1 | Km(ProFAR) 6.4 uM | kcat/Km(ProFAR) 0.046 uM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.29 s^-1; already in s^-1, no unit conversion applies; the paper value is 0.29 s^(-1). Km: printed Table 3 cell 6.4 uM; 1 uM is 1/1000 mM, so 6.4 / 1000 = 0.0064 mM. kcat/Km: printed Table 3 cell 0.046 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.046 x 1000 = 46.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, tHisA enzyme column 'D51N tHisA': kcat = 0.29 s^-1; Km(ProFAR) = 6.4 uM; printed kcat/Km(ProFAR) = 0.046 uM^-1 s^-1.


organism: Bacteroides fragilis

substrate_name: Unknown

substrate: Unknown


organism: Escherichia coli (strain K12)


organism: Cohnella laeviribosi


organism: Escherichia coli O157:H7

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.


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 Aldose block, substrate row D-Lyxose (product D-Xylulose): Specific activity (umol min^-1 mg^-1) = 10.0; Km (mmol l^-1) = 13.3; kcat (s^-1) = 30 810; kcat/Km ((mmol l^-1)^-1 s^-1) = 2333.

normalized_value_unit_evidence: Km: printed Table 1 cell 13.3 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 13.3 mM. kcat: printed Table 1 cell 30 810 under the column head kcat (s^-1); the thousands space is typography and the cell reads 30810; the column is already in s^-1, so no unit conversion applies and the paper value is 30810.0 s^(-1). kcat/Km: printed Table 1 cell 2333 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 2333.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Aldose block, substrate row D-Lyxose (product D-Xylulose): Km = 13.3 mmol l^-1; kcat = 30 810 s^-1 (printed with a thousands space); printed kcat/Km = 2333 (mmol l^-1)^-1 s^-1.


proof_lines: kcat is 30810 sec(-1) with D-lyxose as substrate. kcat is 16170 sec(-1) with D-mannose as substrate. kcat is 31620 sec(-1) with D-xylulose as substrate. kcat is 4297 sec(-1) with D-fructose as substrate.


organism: Mesorhizobium loti

substrate_name: D-ribose

assay_conditions_summary: pH 9

proof_lines: in 50 mM glycine-NaOH, pH 9.0, 1 mM MnCl2, at 60°C

substrate: D-ribose


substrate_name: L-talose; L-mannose

substrate: L-talose; L-mannose


substrate_name: L-lyxose

substrate: L-lyxose


substrate_name: D-Mannose

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

normalized_value_unit_evidence: paper normalized kcat_over_km=502 s^-1*mM^-1; expected normalized value 502.1739130434782 s^-1*mM^-1 agrees by table rounding/SD

row_label: D-Mannose -> D-Fructose

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

substrate: D-Mannose


substrate_name: D-xylulose

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-Xylulose (product D-Lyxose): Specific activity (umol min^-1 mg^-1) = 26.2; Km (mmol l^-1) = 3.83; kcat (s^-1) = 31 620; kcat/Km ((mmol l^-1)^-1 s^-1) = 9560.

normalized_value_unit_evidence: Km: printed Table 1 cell 3.83 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 3.83 mM. kcat: printed Table 1 cell 31 620 under the column head kcat (s^-1); the thousands space is typography and the cell reads 31620; the column is already in s^-1, so no unit conversion applies and the paper value is 31620.0 s^(-1). kcat/Km: printed Table 1 cell 9560 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 9560.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Ketose block, substrate row D-Xylulose (product D-Lyxose): Km = 3.83 mmol l^-1; kcat = 31 620 s^-1 (printed with a thousands space); printed kcat/Km = 9560 (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)

substrate: D-xylulose


substrate_name: D-lyxose

row_label: Table 1, Aldose block, substrate row D-Lyxose

substrate: D-lyxose


substrate_name: D-Xylulose

column_label: Table 1 row D-Xylulose -> D-Lyxose, primary kcat/Km column: 9560 +/- 34 ((mmol l^-1)^-1 s^-1), not the current 8255.874673629243 s^-1 mM^-1.

normalized_value_unit_evidence: Km 3.83 mM; kcat 31620 s^-1; explicit kcat/Km 9560 s^-1 mM^-1.

row_label: D-Xylulose -> D-Lyxose

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

substrate: D-Xylulose


organism: Thermofilum sp. (strain ex4484_79)


organism: Thermosediminibacter oceani

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.


organism: Dictyoglomus turgidum

assay_conditions_summary: pH 8


substrate_name: L-Fructose

substrate: L-Fructose


substrate_name: L-xylulose

substrate: L-xylulose


substrate_name: L-Mannose

substrate: L-Mannose


substrate_name: L-Lyxose

substrate: L-Lyxose


assay_conditions_summary: pH 8; 348.15 K; buffer 50 mM EPPS

column_label: Table 1: Kinetic parameters of L-rhamnose isomerase from D. turgidum (Biotechnol Lett 2013, volume 35, pages 259-264); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). The cited cell set is Table 1, printed substrate row D-Allose: column Km (mM) = 61.5; column kcat (s-1) = 81; column kcat/Km (mM-1 s-1) = 1.3.

normalized_value_unit_evidence: Km: printed Table 1 cell 61.5 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 61.5 mM. kcat: printed Table 1 cell 81 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 81.0 s^(-1). kcat/Km: printed Table 1 cell 1.3 mM-1 s-1; that printed unit is already the canonical one, so no unit conversion applies and the printed cell is 1.3 s^(-1)*mM^(-1). Quotient disclosure for this row: 81 / 61.5 = 1.3170731707317074 s^-1 mM^-1, which is the value the catalog holds, and the printed efficiency cell 1.3 mM-1 s-1 is that quotient written to the one decimal place the efficiency column uses.

raw_value_unit_evidence: Table 1, printed substrate row D-Allose: Km = 61.5 mM; kcat = 81 s-1; printed kcat/Km = 1.3 mM-1 s-1.

row_label: Table 1, printed substrate row D-Allose


column_label: Table 1: Kinetic parameters of L-rhamnose isomerase from D. turgidum (Biotechnol Lett 2013, volume 35, pages 259-264); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). The cited cell set is Table 1, printed substrate row D-Ribose: column Km (mM) = 54.5; column kcat (s-1) = 49; column kcat/Km (mM-1 s-1) = 0.9.

normalized_value_unit_evidence: Km: printed Table 1 cell 54.5 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 54.5 mM. kcat: printed Table 1 cell 49 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 49.0 s^(-1). kcat/Km: printed Table 1 cell 0.9 mM-1 s-1; that printed unit is already the canonical one, so no unit conversion applies and the printed cell is 0.9 s^(-1)*mM^(-1). Quotient disclosure for this row: 49 / 54.5 = 0.8990825688073395 s^-1 mM^-1, which is the value the catalog holds, and the printed efficiency cell 0.9 mM-1 s-1 is that quotient written to the one decimal place the efficiency column uses.

raw_value_unit_evidence: Table 1, printed substrate row D-Ribose: Km = 54.5 mM; kcat = 49 s-1; printed kcat/Km = 0.9 mM-1 s-1.

row_label: Table 1, printed substrate row D-Ribose


column_label: Table 1: Kinetic parameters of L-rhamnose isomerase from D. turgidum (Biotechnol Lett 2013, volume 35, pages 259-264); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). The cited cell set is Table 1, printed substrate row L-Fructose: column Km (mM) = 73.2; column kcat (s-1) = 116; column kcat/Km (mM-1 s-1) = 1.6.

normalized_value_unit_evidence: Km: printed Table 1 cell 73.2 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 73.2 mM. kcat: printed Table 1 cell 116 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 116.0 s^(-1). kcat/Km: printed Table 1 cell 1.6 mM-1 s-1; that printed unit is already the canonical one, so no unit conversion applies and the printed cell is 1.6 s^(-1)*mM^(-1). Quotient disclosure for this row: 116 / 73.2 = 1.5846994535519126 s^-1 mM^-1, which is the value the catalog holds, and the printed efficiency cell 1.6 mM-1 s-1 is that quotient written to the one decimal place the efficiency column uses.

raw_value_unit_evidence: Table 1, printed substrate row L-Fructose: Km = 73.2 mM; kcat = 116 s-1; printed kcat/Km = 1.6 mM-1 s-1.


organism: Pseudomonas stutzeri

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q75WH8 and applied mutation signature S329A to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), S329A block, row 'D-allose'; column 'Km (mM)' = 25.9; column 'Vmax (U/mg)' = 9.3; column 'kcat (s^-1)' = 7.4; column 'kcat/Km (mM^-1 s^-1)' = 2.8 x 10^-1.

normalized_value_unit_evidence: Km: printed Table II cell 25.9 mM; the column head prints mM, so no unit conversion applies and the paper value is 25.9 mM. kcat: printed Table II cell 7.4 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 7.4 s^(-1). kcat/Km: printed Table II cell 2.8 x 10^-1 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.28 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.28571428571428575.

raw_value_unit_evidence: Table II, S329A block, row D-allose: Km = 25.9 mM; kcat = 7.4 s^-1; printed kcat/Km = 2.8 x 10^-1 mM^-1 s^-1; the Vmax column of the same row prints 9.3 U/mg.

row_label: Table II, S329A block, row D-allose

table_label: Table II: Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants (Protein Engineering, Design & Selection 2010, 23(12):919-927)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q75WH8 and applied mutation signature S329F to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), S329F block, row 'D-allose'; column 'Km (mM)' = 53.3; column 'Vmax (U/mg)' = 4.7; column 'kcat (s^-1)' = 3.8; column 'kcat/Km (mM^-1 s^-1)' = 7.1 x 10^-2.

normalized_value_unit_evidence: Km: printed Table II cell 53.3 mM; the column head prints mM, so no unit conversion applies and the paper value is 53.3 mM. kcat: printed Table II cell 3.8 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 3.8 s^(-1). kcat/Km: printed Table II cell 7.1 x 10^-2 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.071 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.07129455909943715.

raw_value_unit_evidence: Table II, S329F block, row D-allose: Km = 53.3 mM; kcat = 3.8 s^-1; printed kcat/Km = 7.1 x 10^-2 mM^-1 s^-1; the Vmax column of the same row prints 4.7 U/mg.

row_label: Table II, S329F block, row D-allose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q75WH8 and applied mutation signature S329K to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), S329K block, row 'D-allose'; column 'Km (mM)' = 33.9; column 'Vmax (U/mg)' = 3.4; column 'kcat (s^-1)' = 2.7; column 'kcat/Km (mM^-1 s^-1)' = 8.1 x 10^-2.

normalized_value_unit_evidence: Km: printed Table II cell 33.9 mM; the column head prints mM, so no unit conversion applies and the paper value is 33.9 mM. kcat: printed Table II cell 2.7 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 2.7 s^(-1). kcat/Km: printed Table II cell 8.1 x 10^-2 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.081 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.07964601769911506.

raw_value_unit_evidence: Table II, S329K block, row D-allose: Km = 33.9 mM; kcat = 2.7 s^-1; printed kcat/Km = 8.1 x 10^-2 mM^-1 s^-1; the Vmax column of the same row prints 3.4 U/mg.

row_label: Table II, S329K block, row D-allose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q75WH8 and applied mutation signature S329L to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), S329L block, row 'D-allose'; column 'Km (mM)' = 35.6; column 'Vmax (U/mg)' = 12.2; column 'kcat (s^-1)' = 9.8; column 'kcat/Km (mM^-1 s^-1)' = 2.7 x 10^-1.

normalized_value_unit_evidence: Km: printed Table II cell 35.6 mM; the column head prints mM, so no unit conversion applies and the paper value is 35.6 mM. kcat: printed Table II cell 9.8 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 9.8 s^(-1). kcat/Km: printed Table II cell 2.7 x 10^-1 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.27 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.2752808988764045.

raw_value_unit_evidence: Table II, S329L block, row D-allose: Km = 35.6 mM; kcat = 9.8 s^-1; printed kcat/Km = 2.7 x 10^-1 mM^-1 s^-1; the Vmax column of the same row prints 12.2 U/mg.

row_label: Table II, S329L block, row D-allose


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

column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), Wild-type block, row 'D-allose'; column 'Km (mM)' = 44.7; column 'Vmax (U/mg)' = 26.5; column 'kcat (s^-1)' = 21.2; column 'kcat/Km (mM^-1 s^-1)' = 4.7 x 10^-1.

normalized_value_unit_evidence: Km: printed Table II cell 44.7 mM; the column head prints mM, so no unit conversion applies and the paper value is 44.7 mM. kcat: printed Table II cell 21.2 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 21.2 s^(-1). kcat/Km: printed Table II cell 4.7 x 10^-1 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.47 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.4742729306487695.

raw_value_unit_evidence: Table II, Wild-type block, row D-allose: Km = 44.7 mM; kcat = 21.2 s^-1; printed kcat/Km = 4.7 x 10^-1 mM^-1 s^-1; the Vmax column of the same row prints 26.5 U/mg.

row_label: Table II, Wild-type block, row D-allose


column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), S329A block, row 'D-ribose'; column 'Km (mM)' = 44.4; column 'Vmax (U/mg)' = 11; column 'kcat (s^-1)' = 8.9; column 'kcat/Km (mM^-1 s^-1)' = 2.0 x 10^-1.

normalized_value_unit_evidence: Km: printed Table II cell 44.4 mM; the column head prints mM, so no unit conversion applies and the paper value is 44.4 mM. kcat: printed Table II cell 8.9 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 8.9 s^(-1). kcat/Km: printed Table II cell 2.0 x 10^-1 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.2 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.20045045045045046.

raw_value_unit_evidence: Table II, S329A block, row D-ribose: Km = 44.4 mM; kcat = 8.9 s^-1; printed kcat/Km = 2.0 x 10^-1 mM^-1 s^-1; the Vmax column of the same row prints 11 U/mg.

row_label: Table II, S329A block, row D-ribose


column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), S329F block, row 'D-ribose'; column 'Km (mM)' = 39.1; column 'Vmax (U/mg)' = 2.1; column 'kcat (s^-1)' = 1.7; column 'kcat/Km (mM^-1 s^-1)' = 4.3 x 10^-2.

normalized_value_unit_evidence: Km: printed Table II cell 39.1 mM; the column head prints mM, so no unit conversion applies and the paper value is 39.1 mM. kcat: printed Table II cell 1.7 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 1.7 s^(-1). kcat/Km: printed Table II cell 4.3 x 10^-2 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.043 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.043478260869565216.

raw_value_unit_evidence: Table II, S329F block, row D-ribose: Km = 39.1 mM; kcat = 1.7 s^-1; printed kcat/Km = 4.3 x 10^-2 mM^-1 s^-1; the Vmax column of the same row prints 2.1 U/mg.

row_label: Table II, S329F block, row D-ribose


column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), S329K block, row 'D-ribose'; column 'Km (mM)' = 67.3; column 'Vmax (U/mg)' = 2.3; column 'kcat (s^-1)' = 1.8; column 'kcat/Km (mM^-1 s^-1)' = 2.7 x 10^-2.

normalized_value_unit_evidence: Km: printed Table II cell 67.3 mM; the column head prints mM, so no unit conversion applies and the paper value is 67.3 mM. kcat: printed Table II cell 1.8 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 1.8 s^(-1). kcat/Km: printed Table II cell 2.7 x 10^-2 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.027 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.026745913818722142.

raw_value_unit_evidence: Table II, S329K block, row D-ribose: Km = 67.3 mM; kcat = 1.8 s^-1; printed kcat/Km = 2.7 x 10^-2 mM^-1 s^-1; the Vmax column of the same row prints 2.3 U/mg.

row_label: Table II, S329K block, row D-ribose


column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), S329L block, row 'D-ribose'; column 'Km (mM)' = 65.6; column 'Vmax (U/mg)' = 4.1; column 'kcat (s^-1)' = 3.3; column 'kcat/Km (mM^-1 s^-1)' = 5.0 x 10^-2.

normalized_value_unit_evidence: Km: printed Table II cell 65.6 mM; the column head prints mM, so no unit conversion applies and the paper value is 65.6 mM. kcat: printed Table II cell 3.3 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 3.3 s^(-1). kcat/Km: printed Table II cell 5.0 x 10^-2 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.05 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.05030487804878049.

raw_value_unit_evidence: Table II, S329L block, row D-ribose: Km = 65.6 mM; kcat = 3.3 s^-1; printed kcat/Km = 5.0 x 10^-2 mM^-1 s^-1; the Vmax column of the same row prints 4.1 U/mg.

row_label: Table II, S329L block, row D-ribose


column_label: Table II (Kinetic parameters of wild-type P. Stutzeri L-RhI and Ser329 mutants), Wild-type block, row 'D-ribose'; column 'Km (mM)' = 85.1; column 'Vmax (U/mg)' = 14; column 'kcat (s^-1)' = 11.4; column 'kcat/Km (mM^-1 s^-1)' = 1.3 x 10^-1.

normalized_value_unit_evidence: Km: printed Table II cell 85.1 mM; the column head prints mM, so no unit conversion applies and the paper value is 85.1 mM. kcat: printed Table II cell 11.4 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 11.4 s^(-1). kcat/Km: printed Table II cell 1.3 x 10^-1 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the cell is 0.13 s^(-1)*mM^(-1) with no unit conversion applied, while the exported ratio is 0.1339600470035253.

raw_value_unit_evidence: Table II, Wild-type block, row D-ribose: Km = 85.1 mM; kcat = 11.4 s^-1; printed kcat/Km = 1.3 x 10^-1 mM^-1 s^-1; the Vmax column of the same row prints 14 U/mg.

row_label: Table II, Wild-type block, row D-ribose


column_label: Table 1: Kinetic parameters of L-rhamnose isomerase from D. turgidum (Biotechnol Lett 2013, volume 35, pages 259-264); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). The cited cell set is Table 1, printed substrate row L-Lyxose: column Km (mM) = 33.4; column kcat (s-1) = 200; column kcat/Km (mM-1 s-1) = 6.0.

normalized_value_unit_evidence: Km: printed Table 1 cell 33.4 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 33.4 mM. kcat: printed Table 1 cell 200 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 200.0 s^(-1). kcat/Km: printed Table 1 cell 6.0 mM-1 s-1; that printed unit is already the canonical one, so no unit conversion applies and the printed cell is 6.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 200 / 33.4 = 5.9880239520958085 s^-1 mM^-1, which is the value the catalog holds, and the printed efficiency cell 6.0 mM-1 s-1 is that quotient written to the one decimal place the efficiency column uses.

raw_value_unit_evidence: Table 1, printed substrate row L-Lyxose: Km = 33.4 mM; kcat = 200 s-1; printed kcat/Km = 6.0 mM-1 s-1.

row_label: Table 1, printed substrate row L-Lyxose


column_label: Table 1: Kinetic parameters of L-rhamnose isomerase from D. turgidum (Biotechnol Lett 2013, volume 35, pages 259-264); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). The cited cell set is Table 1, printed substrate row L-Mannose: column Km (mM) = 36.8; column kcat (s-1) = 155; column kcat/Km (mM-1 s-1) = 4.2.

normalized_value_unit_evidence: Km: printed Table 1 cell 36.8 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 36.8 mM. kcat: printed Table 1 cell 155 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 155.0 s^(-1). kcat/Km: printed Table 1 cell 4.2 mM-1 s-1; that printed unit is already the canonical one, so no unit conversion applies and the printed cell is 4.2 s^(-1)*mM^(-1). Quotient disclosure for this row: 155 / 36.8 = 4.211956521739131 s^-1 mM^-1, which is the value the catalog holds, and the printed efficiency cell 4.2 mM-1 s-1 is that quotient written to the one decimal place the efficiency column uses.

raw_value_unit_evidence: Table 1, printed substrate row L-Mannose: Km = 36.8 mM; kcat = 155 s-1; printed kcat/Km = 4.2 mM-1 s-1.


substrate_name: L-Xylulose

column_label: Table 1: Kinetic parameters of L-rhamnose isomerase from D. turgidum (Biotechnol Lett 2013, volume 35, pages 259-264); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). The cited cell set is Table 1, printed substrate row L-Xylulose: column Km (mM) = 63.0; column kcat (s-1) = 130; column kcat/Km (mM-1 s-1) = 2.1.

normalized_value_unit_evidence: Km: printed Table 1 cell 63.0 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 63.0 mM. kcat: printed Table 1 cell 130 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 130.0 s^(-1). kcat/Km: printed Table 1 cell 2.1 mM-1 s-1; that printed unit is already the canonical one, so no unit conversion applies and the printed cell is 2.1 s^(-1)*mM^(-1). Quotient disclosure for this row: 130 / 63.0 = 2.0634920634920637 s^-1 mM^-1, which is the value the catalog holds, and the printed efficiency cell 2.1 mM-1 s-1 is that quotient written to the one decimal place the efficiency column uses.

raw_value_unit_evidence: Table 1, printed substrate row L-Xylulose: Km = 63.0 mM; kcat = 130 s-1; printed kcat/Km = 2.1 mM-1 s-1.

substrate: L-Xylulose


substrate_name: L-Rhamnose

column_label: Table 1: Kinetic parameters of L-rhamnose isomerase from D. turgidum (Biotechnol Lett 2013, volume 35, pages 259-264); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). The cited cell set is Table 1, printed substrate row L-Rhamnose: column Km (mM) = 24.6; column kcat (s-1) = 195; column kcat/Km (mM-1 s-1) = 7.9.

normalized_value_unit_evidence: Km: printed Table 1 cell 24.6 mM; the printed Km column of this paper is already in millimolar, so no unit conversion applies and the paper value is 24.6 mM. kcat: printed Table 1 cell 195 s-1; the printed turnover column is already per second, so no unit conversion applies and the paper value is 195.0 s^(-1). kcat/Km: printed Table 1 cell 7.9 mM-1 s-1; that printed unit is already the canonical one, so no unit conversion applies and the printed cell is 7.9 s^(-1)*mM^(-1). Quotient disclosure for this row: 195 / 24.6 = 7.926829268292683 s^-1 mM^-1, which is the value the catalog holds, and the printed efficiency cell 7.9 mM-1 s-1 is that quotient written to the one decimal place the efficiency column uses.

raw_value_unit_evidence: Table 1, printed substrate row L-Rhamnose: Km = 24.6 mM; kcat = 195 s-1; printed kcat/Km = 7.9 mM-1 s-1.

substrate: L-Rhamnose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S329A to reconstruct the assayed variant sequence.

column_label: Table II columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1) for S329A with L-rhamnose.

normalized_value_unit_evidence: kcat_over_km=7.7 s^-1*mM^-1; package value 7.675675675675675 is consistent with displayed rounded table values.

row_label: S329A / Hexose / L-rhamnose

table_label: Table II Kinetic parameters of wild-type P. stutzeri L-RhI and Ser329 mutants


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S329F to reconstruct the assayed variant sequence.

column_label: Table II columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1) for S329F with L-rhamnose.

normalized_value_unit_evidence: kcat_over_km=0.55 s^-1*mM^-1; package value 0.5495867768595042 is consistent with displayed rounded table values.

row_label: S329F / Hexose / L-rhamnose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S329K to reconstruct the assayed variant sequence.

column_label: Table II columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1) for S329K with L-rhamnose.

normalized_value_unit_evidence: kcat_over_km=0.41 s^-1*mM^-1; package value 0.4180327868852459 is consistent with displayed rounded table values.

row_label: S329K / Hexose / L-rhamnose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S329L to reconstruct the assayed variant sequence.

column_label: Table II columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1) for S329L with L-rhamnose.

normalized_value_unit_evidence: kcat_over_km=6.8 s^-1*mM^-1; package value 6.784810126582278 is consistent with displayed rounded table values.

row_label: S329L / Hexose / L-rhamnose


column_label: Table II columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1) for Wild-type with L-rhamnose.

normalized_value_unit_evidence: kcat_over_km=11.6 s^-1*mM^-1; package value 11.546391752577321 is consistent with displayed rounded table values.

row_label: Wild-type / Hexose / L-rhamnose


organism: Thermotoga maritima

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D127N with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D51N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H48A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R83N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T164A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


column_label: Table 1: Temperature Dependence of the Steady-State Kinetic Constants of eHisA and tHisA (Biochemistry 2002, 41(40):12032-12042); printed column heads enzyme | T (C) | kcat (s-1) | KMProFAR (uM) | kcat/KMProFAR (uM-1 s-1). Table 1, tHisA enzyme block, temperature row 37 C; column kcat (s-1) = 1.54; column KMProFAR (uM) = 0.6; column kcat/KMProFAR (uM-1 s-1) = 2.6. captured primary segment: tHisA | 37 | kcat 1.54 s^-1 | Km(ProFAR) 0.6 uM | kcat/Km(ProFAR) 2.6 uM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.54 s^-1; already in s^-1, no unit conversion applies; the exported value is 1.54 s^(-1). Km: printed Table 1 cell 0.6 uM; 1 uM is 1/1000 mM, so 0.6 / 1000 = 0.0006 mM; the exported value is 0.0006 mM. kcat/Km: printed Table 1 cell 2.6 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 2.6 x 1000 = 2600.0 s^-1 mM^-1. Quotient disclosure for this row: 1.54 / 0.0006 = 2566.666666666667 s^-1 mM^-1, which is the exported kcat_over_km, and 2566.666666666667 s^-1 mM^-1 is 2.566666666666667 uM^-1 s^-1, which the table prints to its own two figures as the cell 2.6.

raw_value_unit_evidence: Table 1, tHisA enzyme block, temperature row 37 C: kcat = 1.54 s^-1; Km(ProFAR) = 0.6 uM; printed kcat/Km(ProFAR) = 2.6 uM^-1 s^-1.


organism: Caldicellulosiruptor obsidiansis


substrate_name: D-allose

substrate: D-allose


substrate_name: L-rhamnose

substrate: L-rhamnose