proof_lines: recombinant Arabidopsis thaliana enzyme UGE1, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-Glc dehydrogenase

proof_lines: recombinant Arabidopsis thaliana enzyme UGE1, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase


enzyme_display_name: UDP-glucose 4-epimerase

organism: Arabidopsis thaliana

substrate_name: UDP-xylose

source_db: uniprot

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

column_label: Table 6: Kinetics of rAtUGEs (Biochem. J. 2009, 424(2):169-177), UDP-Xyl block, enzyme row rAtUGE3; column 'K m (mM)' = 0.32 ± 0.05; column 'k cat (s^-1)' = 13; column 'k cat/K m (mM^-1 s^-1)' = 40.

normalized_value_unit_evidence: Km: printed Table 6 cell 0.32 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.32 mM; the exported value is 0.32 mM. kcat: printed Table 6 cell 13 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 13.0 s^(-1); the exported value is 13.0 s^(-1). kcat/Km: printed Table 6 cell 40 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 40.0 s^(-1)*mM^(-1); the exported value is 40.625 s^(-1)*mM^(-1), the full-precision quotient of the exported kcat and Km.

raw_value_unit_evidence: Table 6, UDP-Xyl block, enzyme row rAtUGE3: K m = 0.32 ± 0.05 mM; k cat = 13 s^-1; printed k cat/K m = 40 mM^-1 s^-1.

data_origin: experimental

enzyme: UDP-glucose 4-epimerase

substrate: UDP-xylose

status: corrected

source: uniprot


organism: Aspergillus nidulans

substrate_name: UDP-alpha-D-glucose

source_db: brenda

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L320Y to reconstruct the assayed variant sequence.

mutation_type: substitution

substrate: UDP-alpha-D-glucose

source: brenda


substrate_name: UDPgalactose

source_db: oed

verification_status: verified

kcat_over_km_display: Not reported

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

column_label: Table label: TABLE 4 Conversion of UDP-Gal by UGE isoforms. Row: boldface UGE1 fit. Columns read: kcatUDP-Gal (s^-1) cell 24 ⴞ 0.82, KmUDP-Gal (mM) cell 0.19 ⴞ 0.02, kUDP-Gal (mM^-1 s^-1) cell 126. metric: kcat; raw value: 24; raw unit: s^-1; normalized value: 24 s^(-1); metric: Km; raw value: 0.19; raw unit: mM; normalized value: 0.19 mM; metric: kcat/Km; raw unit: mM^-1 s^-1; normalized value: 126.3157894736842 s^-1 mM^-1; assay condition: UDP-Gal 4-epimerase assay: standard epimerase reaction in 50 mM Tris/HCl, pH 7.4, containing 0.1 mM NAD+ and 125 ug/ml acetylated BSA at 25 C; maximal reaction rate and Km values were determined by varying UDP-Gal concentration between 0.05 and 2.5 mM using best fit to single site saturation kinetics in Sigmaplot 8.0. Export row conditions: pH 7.4; 298.15 K.

normalized_value_unit_evidence: Boldface UGE1 row of Table 4: kcat 24 s^-1 = 24 s^(-1) (no conversion); Km 0.19 mM stays 0.19 mM (table prints Km directly in mM); kcat/Km = 24 s^-1 / 0.19 mM = 126.3157894736842 s^-1 mM^-1, and the row's printed catalytic efficiency cell k = 126 mM^-1 s^-1 is this same quotient at the printed cell's own integer precision. In the text extract the bold plus-minus sign renders as ⴞ, the superscript minus one as −1, and column superscripts are flattened.

raw_value_unit_evidence: TABLE 4 Conversion of UDP-Gal by UGE isoforms | metric header row of Table 4: UGE kcatUDP-Gal KmUDP-Gal kUDP-Gal [E] r2, with unit row: s −1, mM, mM −1 s (flattened from mM^-1 s^-1), nM | boldface UGE1 row cells (quoted from extract line 347): 24 ⴞ 0.82          0.19 ⴞ 0.02         126         1.1        0.87 | cells read: kcat = 24 ⴞ 0.82 s^-1; Km = 0.19 ⴞ 0.02 mM; k = kcat Km^-1 = 126 mM^-1 s^-1; [E] and r2 columns follow.

row_label: UGE1 | boldface highest-kcat fit (24 ⴞ 0.82)

substrate: UDPgalactose

status: verified

source: oed


column_label: Table label: TABLE 4 Conversion of UDP-Gal by UGE isoforms. Row: boldface UGE3 fit. Columns read: kcatUDP-Gal (s^-1) cell 66 ⴞ 1.7, KmUDP-Gal (mM) cell 0.22 ⴞ 0.021, kUDP-Gal (mM^-1 s^-1) cell 300. metric: kcat; raw value: 66; raw unit: s^-1; normalized value: 66 s^(-1); metric: Km; raw value: 0.22; raw unit: mM; normalized value: 0.22 mM; metric: kcat/Km; raw unit: mM^-1 s^-1; normalized value: 300.0 s^-1 mM^-1; assay condition: UDP-Gal 4-epimerase assay: standard epimerase reaction in 50 mM Tris/HCl, pH 7.4, containing 0.1 mM NAD+ and 125 ug/ml acetylated BSA at 25 C; maximal reaction rate and Km values were determined by varying UDP-Gal concentration between 0.05 and 2.5 mM using best fit to single site saturation kinetics in Sigmaplot 8.0. Export row conditions: pH 7.4; 298.15 K.

normalized_value_unit_evidence: Boldface UGE3 row of Table 4: kcat 66 s^-1 = 66 s^(-1) (no conversion); Km 0.22 mM stays 0.22 mM (table prints Km directly in mM); printed catalytic efficiency k = 300 mM^-1 s^-1 = 300.0 s^-1 mM^-1 (mM^-1 s^-1 and s^-1 mM^-1 are the same unit), which equals the quotient 66/0.22 exactly. In the text extract the bold plus-minus sign renders as ⴞ, the superscript minus one as −1, and column superscripts are flattened.

raw_value_unit_evidence: TABLE 4 Conversion of UDP-Gal by UGE isoforms | metric header row of Table 4: UGE kcatUDP-Gal KmUDP-Gal kUDP-Gal [E] r2, with unit row: s −1, mM, mM −1 s (flattened from mM^-1 s^-1), nM | boldface UGE3 row cells (quoted from extract line 353): 66 ⴞ 1.7           0.22 ⴞ 0.021        300         0.64       0.94 | cells read: kcat = 66 ⴞ 1.7 s^-1; Km = 0.22 ⴞ 0.021 mM; k = kcat Km^-1 = 300 mM^-1 s^-1; [E] and r2 columns follow.

row_label: UGE3 | boldface highest-kcat fit (66 ⴞ 1.7)


column_label: Table label: TABLE 4 Conversion of UDP-Gal by UGE isoforms. Row: boldface UGE4 fit. Columns read: kcatUDP-Gal (s^-1) cell 34 ⴞ 0.69, KmUDP-Gal (mM) cell 0.23 ⴞ 0.019, kUDP-Gal (mM^-1 s^-1) cell 148. metric: kcat; raw value: 34; raw unit: s^-1; normalized value: 34 s^(-1); metric: Km; raw value: 0.23; raw unit: mM; normalized value: 0.23 mM; metric: kcat/Km; raw unit: mM^-1 s^-1; normalized value: 147.82608695652172 s^-1 mM^-1; assay condition: UDP-Gal 4-epimerase assay: standard epimerase reaction in 50 mM Tris/HCl, pH 7.4, containing 0.1 mM NAD+ and 125 ug/ml acetylated BSA at 25 C; maximal reaction rate and Km values were determined by varying UDP-Gal concentration between 0.05 and 2.5 mM using best fit to single site saturation kinetics in Sigmaplot 8.0. Export row conditions: pH 7.4; 298.15 K.

normalized_value_unit_evidence: Boldface UGE4 row of Table 4: kcat 34 s^-1 = 34 s^(-1) (no conversion); Km 0.23 mM stays 0.23 mM (table prints Km directly in mM); kcat/Km = 34 s^-1 / 0.23 mM = 147.82608695652172 s^-1 mM^-1, and the row's printed catalytic efficiency cell k = 148 mM^-1 s^-1 is this same quotient at the printed cell's own integer precision. In the text extract the bold plus-minus sign renders as ⴞ, the superscript minus one as −1, and column superscripts are flattened.

raw_value_unit_evidence: TABLE 4 Conversion of UDP-Gal by UGE isoforms | metric header row of Table 4: UGE kcatUDP-Gal KmUDP-Gal kUDP-Gal [E] r2, with unit row: s −1, mM, mM −1 s (flattened from mM^-1 s^-1), nM | boldface UGE4 row cells (quoted from extract line 356): 34 ⴞ 0.69          0.23 ⴞ 0.019        148         3.4        0.98 | cells read: kcat = 34 ⴞ 0.69 s^-1; Km = 0.23 ⴞ 0.019 mM; k = kcat Km^-1 = 148 mM^-1 s^-1; [E] and r2 columns follow.

row_label: UGE4 | boldface highest-kcat fit (34 ⴞ 0.69)


column_label: Table label: TABLE 4 Conversion of UDP-Gal by UGE isoforms. Row: boldface UGE5 fit. Columns read: kcatUDP-Gal (s^-1) cell 128 ⴞ 3.86, KmUDP-Gal (mM) cell 0.17 ⴞ 0.026, kUDP-Gal (mM^-1 s^-1) cell 753. metric: kcat; raw value: 128; raw unit: s^-1; normalized value: 128 s^(-1); metric: Km; raw value: 0.17; raw unit: mM; normalized value: 0.17 mM; metric: kcat/Km; raw unit: mM^-1 s^-1; normalized value: 752.9411764705882 s^-1 mM^-1; assay condition: UDP-Gal 4-epimerase assay: standard epimerase reaction in 50 mM Tris/HCl, pH 7.4, containing 0.1 mM NAD+ and 125 ug/ml acetylated BSA at 25 C; maximal reaction rate and Km values were determined by varying UDP-Gal concentration between 0.05 and 2.5 mM using best fit to single site saturation kinetics in Sigmaplot 8.0. Export row conditions: pH 7.4; 298.15 K.

normalized_value_unit_evidence: Boldface UGE5 row of Table 4: kcat 128 s^-1 = 128 s^(-1) (no conversion); Km 0.17 mM stays 0.17 mM (table prints Km directly in mM); kcat/Km = 128 s^-1 / 0.17 mM = 752.9411764705882 s^-1 mM^-1, and the row's printed catalytic efficiency cell k = 753 mM^-1 s^-1 is this same quotient at the printed cell's own integer precision. In the text extract the bold plus-minus sign renders as ⴞ, the superscript minus one as −1, and column superscripts are flattened.

raw_value_unit_evidence: TABLE 4 Conversion of UDP-Gal by UGE isoforms | metric header row of Table 4: UGE kcatUDP-Gal KmUDP-Gal kUDP-Gal [E] r2, with unit row: s −1, mM, mM −1 s (flattened from mM^-1 s^-1), nM | boldface UGE5 row cells (quoted from extract line 357): 5        128 ⴞ 3.86          0.17 ⴞ 0.026        753         0.14       0.92 | cells read: kcat = 128 ⴞ 3.86 s^-1; Km = 0.17 ⴞ 0.026 mM; k = kcat Km^-1 = 753 mM^-1 s^-1; [E] and r2 columns follow.

row_label: UGE5 | boldface highest-kcat fit (128 ⴞ 3.86)


column_label: Table label: TABLE 4 Conversion of UDP-Gal by UGE isoforms. Row: boldface UGE2 fit. Columns read: kcatUDP-Gal (s^-1) cell 101 ⴞ 1.5, KmUDP-Gal (mM) cell 0.13 ⴞ 0.007, kUDP-Gal (mM^-1 s^-1) cell 777. metric: kcat; raw value: 101; raw unit: s^-1; normalized value: 101 s^(-1); metric: Km; raw value: 0.13; raw unit: mM; normalized value: 0.13 mM; metric: kcat/Km; raw unit: mM^-1 s^-1; normalized value: 776.9230769230769 s^-1 mM^-1; assay condition: UDP-Gal 4-epimerase assay: standard epimerase reaction in 50 mM Tris/HCl, pH 7.4, containing 0.1 mM NAD+ and 125 ug/ml acetylated BSA at 25 C; maximal reaction rate and Km values were determined by varying UDP-Gal concentration between 0.05 and 2.5 mM using best fit to single site saturation kinetics in Sigmaplot 8.0. Export row conditions: pH 7.4; 298.15 K.

normalized_value_unit_evidence: Boldface UGE2 row of Table 4: kcat 101 s^-1 = 101 s^(-1) (no conversion); Km 0.13 mM stays 0.13 mM (table prints Km directly in mM); kcat/Km = 101 s^-1 / 0.13 mM = 776.9230769230769 s^-1 mM^-1, and the row's printed catalytic efficiency cell k = 777 mM^-1 s^-1 is this same quotient at the printed cell's own integer precision. In the text extract the bold plus-minus sign renders as ⴞ, the superscript minus one as −1, and column superscripts are flattened.

raw_value_unit_evidence: TABLE 4 Conversion of UDP-Gal by UGE isoforms | metric header row of Table 4: UGE kcatUDP-Gal KmUDP-Gal kUDP-Gal [E] r2, with unit row: s −1, mM, mM −1 s (flattened from mM^-1 s^-1), nM | boldface UGE2 row cells (quoted from extract line 350): 101 ⴞ 1.5           0.13 ⴞ 0.007        777         0.48       0.97 | cells read: kcat = 101 ⴞ 1.5 s^-1; Km = 0.13 ⴞ 0.007 mM; k = kcat Km^-1 = 777 mM^-1 s^-1; [E] and r2 columns follow.

row_label: UGE2 | boldface highest-kcat fit (101 ⴞ 1.5)


substrate_name: UDPglucose

column_label: Table 5 (Conversion of UDP-Glc by UGE isoforms), UGE row '1'; column 'kcat UDP-Glc' with unit 's-1' = 32; column 'Km UDP-Glc' with unit 'mM' = 0.76. Table 5 carries no catalytic-efficiency column and no standard-deviation column.

normalized_value_unit_evidence: kcat: printed Table 5 cell 32 s-1; already in s^-1, no unit conversion applies; the paper value is 32.0 s^(-1). Km: printed Table 5 cell 0.76 mM; already in mM, no unit conversion applies; the paper value is 0.76 mM. kcat/Km: Table 5 has no kcat/Km column, so the value 42.10526315789474 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 32 / 0.76 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 5, UGE row '1': kcat UDP-Glc = 32 s-1; Km UDP-Glc = 0.76 mM. Table 5 has no kcat/Km cell for this row.

row_label: Table 5, UGE row 1

table_label: Table 5: Conversion of UDP-Glc by UGE isoforms (J. Biol. Chem. 2006, 281(25):17276-17285)

substrate: UDPglucose


column_label: Table 5 (Conversion of UDP-Glc by UGE isoforms), UGE row '3'; column 'kcat UDP-Glc' with unit 's-1' = 19; column 'Km UDP-Glc' with unit 'mM' = 0.19. Table 5 carries no catalytic-efficiency column and no standard-deviation column.

normalized_value_unit_evidence: kcat: printed Table 5 cell 19 s-1; already in s^-1, no unit conversion applies; the paper value is 19.0 s^(-1). Km: printed Table 5 cell 0.19 mM; already in mM, no unit conversion applies; the paper value is 0.19 mM. kcat/Km: Table 5 has no kcat/Km column, so the value 100.0 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 19 / 0.19 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 5, UGE row '3': kcat UDP-Glc = 19 s-1; Km UDP-Glc = 0.19 mM. Table 5 has no kcat/Km cell for this row.

row_label: Table 5, UGE row 3


column_label: Table 5 (Conversion of UDP-Glc by UGE isoforms), UGE row '4'; column 'kcat UDP-Glc' with unit 's-1' = 28; column 'Km UDP-Glc' with unit 'mM' = 0.56. Table 5 carries no catalytic-efficiency column and no standard-deviation column.

normalized_value_unit_evidence: kcat: printed Table 5 cell 28 s-1; already in s^-1, no unit conversion applies; the paper value is 28.0 s^(-1). Km: printed Table 5 cell 0.56 mM; already in mM, no unit conversion applies; the paper value is 0.56 mM. kcat/Km: Table 5 has no kcat/Km column, so the value 49.99999999999999 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 28 / 0.56 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 5, UGE row '4': kcat UDP-Glc = 28 s-1; Km UDP-Glc = 0.56 mM. Table 5 has no kcat/Km cell for this row.

row_label: Table 5, UGE row 4


column_label: Table 5 (Conversion of UDP-Glc by UGE isoforms), UGE row '5'; column 'kcat UDP-Glc' with unit 's-1' = 33; column 'Km UDP-Glc' with unit 'mM' = 0.13. Table 5 carries no catalytic-efficiency column and no standard-deviation column.

normalized_value_unit_evidence: kcat: printed Table 5 cell 33 s-1; already in s^-1, no unit conversion applies; the paper value is 33.0 s^(-1). Km: printed Table 5 cell 0.13 mM; already in mM, no unit conversion applies; the paper value is 0.13 mM. kcat/Km: Table 5 has no kcat/Km column, so the value 253.84615384615384 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 33 / 0.13 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 5, UGE row '5': kcat UDP-Glc = 33 s-1; Km UDP-Glc = 0.13 mM. Table 5 has no kcat/Km cell for this row.

row_label: Table 5, UGE row 5


column_label: Table 5 (Conversion of UDP-Glc by UGE isoforms), UGE row '2'; column 'kcat UDP-Glc' with unit 's-1' = 24; column 'Km UDP-Glc' with unit 'mM' = 0.09. Table 5 carries no catalytic-efficiency column and no standard-deviation column.

normalized_value_unit_evidence: kcat: printed Table 5 cell 24 s-1; already in s^-1, no unit conversion applies; the paper value is 24.0 s^(-1). Km: printed Table 5 cell 0.09 mM; already in mM, no unit conversion applies; the paper value is 0.09 mM. kcat/Km: Table 5 has no kcat/Km column, so the value 266.6666666666667 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 24 / 0.09 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 5, UGE row '2': kcat UDP-Glc = 24 s-1; Km UDP-Glc = 0.09 mM. Table 5 has no kcat/Km cell for this row.

row_label: Table 5, UGE row 2


enzyme_display_name: ribulose-phosphate 3-epimerase

organism: Saccharomyces cerevisiae

substrate_name: D-ribulose 5-phosphate

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

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

enzyme: ribulose-phosphate 3-epimerase

substrate: D-ribulose 5-phosphate


organism: Escherichia coli

substrate_name: UDP-galactose

source_db: skid

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

proof_lines: kcat is 760 sec(-1) for UDP-Glc (at pH 8.5 and 27 degrees Celsius) and 24 sec(-1) for UDP-Gal (at pH 8.5).

source_databases_merged: skid uniprot

substrate: UDP-galactose

source: skid


organism: Spinacia oleracea

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D186A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -11, so it is treated as a source-provided variant sequence.


enzyme_display_name: L-ribulose-5-phosphate 4-epimerase

substrate_name: L-ribulose 5-phosphate

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

proof_lines: 37°C, pH 7.6, Zn2+-form after dialysis, mutant enzyme H95N

proof_lines: 37°C, pH 7.6, Zn2+-form after dialysis + 0.1 mM Zn2+, mutant enzyme H95N

proof_lines: 22°C, pH 7.5, mutant enzyme H95N, activated by 0.1 mM ZnCl2

enzyme: L-ribulose-5-phosphate 4-epimerase

substrate: L-ribulose 5-phosphate


proof_lines: 37°C, pH 7.6, Zn2+-form after dialysis, mutant enzyme H97N

proof_lines: 22°C, pH 7.5, mutant enzyme H97N, activated by 0.1 mM ZnCl2

proof_lines: 37°C, pH 7.6, Zn2+-form after dialysis + 0.1 mM Zn2+, mutant enzyme H97N


proof_lines: 37°C, pH 7.6, Zn2+-form after dialysis, mutant enzyme D76N

proof_lines: 37°C, pH 7.6, Zn2+-form after dialysis + 0.1 mM Zn2+, mutant enzyme D76N


kcat_display: Not reported

proof_lines: 37°C, pH 7.6, Zn2+-form after dialysis + 0.1 mM Zn2+, mutant enzyme H97N or D76N


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines: 37°C, pH 7.6, mutant enzyme H97N, with L-ribulose 5-phosphate as substrate

substrate: Unknown


enzyme_display_name: aldose 1-epimerase

organism: Lactococcus lactis

substrate_name: alpha-D-xylose

verification_status: unverified

enzyme: aldose 1-epimerase

substrate: alpha-D-xylose

status: unverified


substrate_name: alpha-D-glucose

substrate: alpha-D-glucose


substrate_name: alpha-L-arabinose

substrate: alpha-L-arabinose


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


organism: Homo sapiens

substrate_name: alpha-D-Glucose

column_label: Table 1, row/column Glucose, metric rows Km/mM, kcat/s^-1, and (kcat/Km)/l mol^-1 s^-1; PDF page 2 / article page 22

normalized_value_unit_evidence: Km normalized_value=54 normalized_unit=mM; kcat normalized_value=4900 normalized_unit=s^-1; kcat_over_km normalized_value=90 normalized_unit=s^-1*mM^-1

row_label: Glucose

table_label: Table 1. Kinetic parameters of human aldose 1-epimerase

substrate: alpha-D-Glucose


proof_lines: pH 6.2, temperature not specified in the publication, recombinant mutant Y149F


proof_lines: pH 6.2, temperature not specified in the publication, recombinant mutant S124A


proof_lines: pH 6.2, temperature not specified in the publication, recombinant S124T


proof_lines: pH 6.2, temperature not specified in the publication, recombinant wild-type enzyme


organism: Aeromonas hydrophila

assay_conditions_summary: pH 8; 298.15 K; buffer 20 mM sodium phosphate

proof_lines: mutant enzyme K153N, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C


proof_lines: mutant enzyme Y149G, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C


proof_lines: wild type recombinant enzyme, in 20 mM sodium phosphate buffer, pH 8.0, at 25°C


enzyme_display_name: tagaturonate epimerase

organism: Thermotoga maritima

substrate_name: D-fructuronate

enzyme: tagaturonate epimerase

substrate: D-fructuronate


organism: Rattus norvegicus

substrate_name: alpha-D-Fucose

proof_lines: alpha-D-xylose, enzyme form II from kidney and liver

substrate: alpha-D-Fucose


proof_lines: alpha-D-xylose, enzyme form I and II from small intestine

proof_lines: enzyme form III from kidney, enzyme form I and II from small intestine


proof_lines:
enzyme form IV from liver
enzyme form IV from kidney


substrate_name: D-fucose

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

proof_lines: alpha-D-galactose, enzyme form IV from liver

proof_lines: beta-L-arabinose, enzyme form III from kidney

substrate: D-fucose


substrate_name: beta-D-arabinose

substrate: beta-D-arabinose


substrate_name: D-xylose

substrate: D-xylose


substrate_name: lactose

substrate: lactose


proof_lines: wild type enzyme, in 20 mM HEPES-KOH, pH 7.5, 1 mM dithiohreitol, and 0.3 mg/ml bovine serum albumin, at 37°C

proof_lines: wild type enzyme, in 20 mM HEPES-KOH, pH 7.5, 1 mM dithiohreitol, and 0.3 mg/ml bovine serum albumin, at 24°C


organism: Bos taurus


substrate_name: alpha-D-quinovose

substrate: alpha-D-quinovose


organism: Hordeum vulgare

substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


substrate_name: UDP-glucose

substrate: UDP-glucose


organism: Campylobacter jejuni


proof_lines: 22°C, pH 7.5, mutant enzyme Y229F, activated by 0.1 mM ZnCl2


proof_lines: 22°C, pH 7.5, wild-type enzyme, activated by 0.1 mM MgCl2

proof_lines: 22°C, pH 7.5, wild-type enzyme, activated by 0.1 mM ZnCl2


organism: Streptococcus pyogenes

substrate_name: D-ribulose 5-phosphate

proof_lines: RPE metal-free, stoichiometry of Zn2+: 0.1 ion per polypeptide, substrate 10 mM D-ribulose 5-phosphate

proof_lines: RPE as isolated, stoichiometry of Zn2+: 0.3 ion per polypeptide, substrate 10 mM D-ribulose 5-phosphate

proof_lines: RPE as isolated + 0.5 mM ZnCl2 present in assay, stoichiometry of Zn2+: 0.9 ion per polypeptide, substrate 10 mM D-ribulose 5-phosphate

substrate: D-ribulose 5-phosphate


organism: Lathyrus oleraceus

assay_conditions_summary: pH 8.6; 298.15 K; cofactor NAD+

proof_lines: 50 mM Tris-HCl buffer (pH 8.6), 0.1 mM NAD+, 1 mM UDP-sugar and enzyme


substrate_name: UDP-xylose

substrate: UDP-xylose


enzyme_display_name: cysteine-S-conjugate beta-lyase

substrate_name: L-cystathionine

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

assay_conditions_summary: pH 8.5; 310.15 K; buffer 50 mM phosphate

proof_lines: in 50 mM phosphate buffer, pH 8.5, 0.02 mM pyridoxal 5'-phosphate, 1 mM EDTA, at 37°C

enzyme: cysteine-S-conjugate beta-lyase

substrate: L-cystathionine


substrate_name: L-djenkolate

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

substrate: L-djenkolate


enzyme_display_name: cellobiose epimerase

organism: Thermoanaerobacterium saccharolyticum

substrate_name: cellobiose

enzyme: cellobiose epimerase

substrate: cellobiose


organism: Caldicellulosiruptor saccharolyticus

substrate_name: epilactose

substrate: epilactose


organism: Dictyoglomus turgidum


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E161D/N365P with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E161D/S180P/S351G to reconstruct the assayed variant sequence.


substrate_name: lactulose

substrate: lactulose


substrate_name: D-galactose

substrate: D-galactose


substrate_name: D-tagatose

substrate: D-tagatose


substrate_name: UDP-galactose

substrate: UDP-galactose


substrate_name: L-ribulose 5-phosphate

substrate: L-ribulose 5-phosphate


enzyme_display_name: protoporphyrin ferrochelatase

substrate_name: myoglobin

enzyme: protoporphyrin ferrochelatase

substrate: myoglobin


organism: Ricinus communis

proof_lines:
2-phosphoglycerate, cytosolic enzyme
plastidic enzyme


proof_lines:
cytosolic enzyme
plastidic enzyme


organism: Cellvibrio vulgaris

substrate_name: D-mannose

substrate: D-mannose


substrate_name: lactose

proof_lines:
pH 8.0, 40°C, recombinant enzyme
pH 7.5, 30°C, recombinant enzyme

substrate: lactose


enzyme_display_name: UDP-arabinose 4-epimerase

organism: Sinorhizobium meliloti

substrate_name: UDP-D-xylopyranose

proof_lines: apparent value, at 37°C, in 50 mM sodium phosphate, pH 7.6

enzyme: UDP-arabinose 4-epimerase

substrate: UDP-D-xylopyranose


substrate_name: UDP-alpha-D-xylopyranose

substrate: UDP-alpha-D-xylopyranose


enzyme_display_name: UDP-N-acetylglucosamine 4-epimerase

substrate_name: UDP-D-glucose

enzyme: UDP-N-acetylglucosamine 4-epimerase

substrate: UDP-D-glucose


substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


organism: Geotrichum fermentans

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: lactoylglutathione lyase

organism: Saccharomyces cerevisiae

substrate_name: methylglyoxal

smiles: CC(=O)C=O

proof_lines: the apparent kinetic parameters are determined by varying the hemithioacetal concentration between 0.3 and 1.5 mM, which is obtained by the nonenzymatic reaction between glutathione and methylglyoxal

enzyme: lactoylglutathione lyase

substrate: methylglyoxal


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


enzyme_display_name: D-tagatose 3-epimerase

organism: Sinorhizobium sp.

substrate_name: D-sorbose

protein_accession_database: NCBI Protein

sequence_source: NCBI RefSeq protein WP_069063284.1

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

assay_conditions_summary: pH 8

column_label: Table-wrap tab1 captioned kinetic parameters of sDTE wild-type on four substrates lists the D-Sorbose row with Km 83 +/- 4.3 mM, kcat 34.0 +/- 0.92 s^-1, and kcat/Km 0.41 s^-1 mM^-1.

normalized_value_unit_evidence: Km normalized_value=83.0 normalized_unit=mM; kcat normalized_value=34.0 normalized_unit=s^-1; kcat/Km paper_cell=0.41 normalized_unit=s^-1 mM^-1; CatLog stores computed 34.0/83.0=0.40963855421686746

raw_value_unit_evidence: Km raw_value=83 +/- 4.3 raw_unit=mM; kcat raw_value=34.0 +/- 0.92 raw_unit=s^-1; kcat/Km raw_value=0.41 raw_unit=s^-1 mM^-1

row_label: D-Sorbose row

table_label: PMC9059984 full-text table-wrap tab1

enzyme: D-tagatose 3-epimerase

substrate: D-sorbose


substrate_name: D-fructose

substrate: D-fructose


enzyme_display_name: methylmalonyl-CoA mutase

substrate_name: adenosylcobalamin

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

proof_lines:
37°C, pH 7, in presence of 3 mM NH4+
37°C, pH 7, without NH4+

enzyme: methylmalonyl-CoA mutase

substrate: adenosylcobalamin


substrate_name: (R,S)-methylmalonyl-CoA

substrate: (R,S)-methylmalonyl-CoA


organism: Triticum aestivum

substrate_name: UDP-L-arabinose

substrate: UDP-L-arabinose


organism: Thermothelomyces thermophilus

substrate_name: cellobiose

substrate: cellobiose


organism: Helianthus tuberosus

substrate_name: UDP-D-xylose

substrate: UDP-D-xylose


organism: Marinithermus hydrothermalis

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

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


enzyme_display_name: UDP-glucuronate 4-epimerase

organism: Dolichospermum flos-aquae

substrate_name: UDPglucuronate

enzyme: UDP-glucuronate 4-epimerase

substrate: UDPglucuronate


organism: Bacillus cereus

substrate_name: UDP-glucuronate

substrate: UDP-glucuronate


organism: Giardia duodenalis

substrate_name: UDP-N-acetylglucosamine

proof_lines:
Vmax 1.02 mM/min
Vmax 0.59 mM/min

substrate: UDP-N-acetylglucosamine


enzyme_display_name: N-acylglucosamine 2-epimerase

organism: Synechocystis sp.

substrate_name: N-acetyl-D-mannosamine

enzyme: N-acylglucosamine 2-epimerase

substrate: N-acetyl-D-mannosamine


organism: Thermotoga maritima

substrate_name: UDP-alpha-D-galactose

substrate: UDP-alpha-D-galactose


proof_lines:
pH 7.0, 80°C
recombinant enzyme, pH 7.0, 80°C


organism: Badhamia polycephala


organism: Caldicellulosiruptor saccharolyticus

substrate_name: lactose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q371A to reconstruct the assayed variant sequence.

substrate: lactose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q371C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q371E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W355Q with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q371G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W355A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q371F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E174D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N175K/G176D with inferred residue-numbering offset -21 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G176D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E174H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E174A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I178D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V177D with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G176K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R170A/F171A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N175K to reconstruct the assayed variant sequence.


organism: Methanococcus maripaludis

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

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

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


organism: Anabaena sp. CH1

substrate_name: N-acetyl-D-glucosamine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E242Q with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ATP

proof_lines: E242Q, reverse conversion in the presence of 1 mM ATP

substrate: N-acetyl-D-glucosamine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R375K to reconstruct the assayed variant sequence.

proof_lines: R375K, reverse conversion in the presence of 1 mM ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E218D to reconstruct the assayed variant sequence.

proof_lines: E218D, reverse conversion in the presence of 1 mM ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R375A to reconstruct the assayed variant sequence.

proof_lines: R375A, reverse conversion in the presence of 1 mM ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E218A to reconstruct the assayed variant sequence.

proof_lines: E218A, reverse conversion in the presence of 1 mM ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C370A to reconstruct the assayed variant sequence.

proof_lines: C370A, reverse conversion in the presence of 1 mM ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N179A to reconstruct the assayed variant sequence.

proof_lines: N179A, reverse conversion in the presence of 1 mM ATP


organism: Arabidopsis thaliana

sequence_source: multiple

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

proof_lines: recominant Arabidopsis thaliana enzyme UGE3, UDP-Xyl 4-epimerase activity is monitored by an end-point assay containing 0.1-5.0 mM UDP-xylose, 100 mM glycine/NaOH (pH 8.6)

proof_lines: kcat is 19 sec(-1) with UDP-glucose as substrate (PubMed:16644739). kcat is 42 sec(-1) with UDP-galactose as substrate (PubMed:16644739). kcat is 57 sec(-1) with UDP-galactose as substrate (PubMed:16644739). kcat is 66 sec(-1) with UDP-gala

source_databases_merged: brenda uniprot


proof_lines: recombinant Arabidopsis thaliana enzyme UGE1, UDP-Xyl 4-epimerase activity is monitored by an end-point assay containing 0.1-5.0 mM UDP-xylose, 100 mM glycine/NaOH (pH 8.6)


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

proof_lines: pH 7.5, 70°C, mutant enzyme RaC (CsCE_loop168-178 is replaced by RaCE_loop164-174)

proof_lines: pH 7.5, 70°C, mutant enzyme RmC (CsCE_loop168-178 is replaced by RmCE_loop180-190)

proof_lines: pH 7.5, 70°C, mutant enzyme Bt (CsCE_loop168-178 is replaced by BtCE_loop168-178)


organism: Caldicellulosiruptor obsidiansis

proof_lines: pH and temperature not specified in the publication

proof_lines: recombinant His6-tagged enzyme, pH 7.5, 70°C


organism: Dictyoglomus turgidum (strain DSM 6724 / Z-1310)

proof_lines: kcat is 169 min(-1) with cellobiose as substrate. kcat is 89.4 min(-1) with lactose as substrate.


substrate_name: lactulose

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

substrate: lactulose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E161D/S180P/S351G to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant E161D/S180P/S351G, pH 7.5, 80°C

proof_lines: pH 7.5, 80°C, mutant enzyme E161D/S180P/S351G


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E161D/N365P to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant E161D/N365P, pH 7.5, 80°C


substrate_name: epilactose

substrate: epilactose


proof_lines:
pH 7.5, 50°C, recombinant enzyme
pH 7.5, 50°C
pH 7.5, 80°C


organism: Pedobacter heparinus

column_label: Table 1 (Biochemical properties of CEs from various bacterial origins) carries one Bacterial strain column, a pH span with Optimum and Stability columns, a Temperature span with Optimum (°C) and Stability (°C) columns, then three substrate spans headed Cellobiose, Lactose and β-(1→4)-Mannobiose, each printing the column heads k_cat (s^-1) | K_m (mM) | k_cat/K_m (s^-1 mM^-1), and a Reference column. The cited cell set is Table 1, row Pedobacter heparinus, Lactose column group: k_cat (s^-1) = 5.43; K_m (mM) = 24.5; k_cat/K_m (s^-1 mM^-1) = 0.222; each of the three cells carries the footnote letter f (30°C).

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.43 under the column head k_cat (s^-1) in the Lactose column group of row Pedobacter heparinus; the column is already per second, so no conversion applies and the paper value is 5.43 s^(-1). Km: printed Table 1 cell 24.5 under the column head K_m (mM) of the same column group; the column is already in mM, so no conversion applies and the paper value is 24.5 mM. kcat/Km: printed Table 1 cell 0.222 under the column head k_cat/K_m (s^-1 mM^-1) of the same column group; the column is already in the canonical unit, so 0.222 x 1 = 0.222 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row Pedobacter heparinus, Lactose column group: kcat = 5.43 s^-1; Km = 24.5 mM; printed kcat/Km = 0.222 s^-1 mM^-1; footnote f states that the kinetic parameters were determined at 30°C.

table_label: Table 1: Biochemical properties of CEs from various bacterial origins (Bioscience, Biotechnology, and Biochemistry 2016, 80(7):1294-1305)


organism: Solanum lycopersicum

substrate_name: S-adenosyl-L-methionine

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

substrate: S-adenosyl-L-methionine


assay_conditions_summary: pH 8.5; buffer containing EPPS pH 8

column_label: PMID 15983009 DOI 10.1093/jxb/eri220 Table 1; row Wild-type; columns Km (uM), Kcat (s^-1), and Kcat/Km (M^-1 s^-1).

row_label: Wild-type LeACS2 / S-adenosyl-L-methionine

table_label: Table 1. Kinetic parameters of wild-type and mutant LeACS2 activity


proof_lines: No activity with UDP-Galactose, UDP- Glucose or UDP-Xylose.


organism: Thermoanaerobacterium saccharolyticum


organism: Trichormus variabilis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K157L to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 30°C, recombinant His6-tagged mutant K157L


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K155A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 30°C, recombinant His6-tagged mutant K155A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K151V to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 30°C, recombinant His6-tagged mutant K151V


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K160P to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 30°C, recombinant His6-tagged mutant K160P


assay_conditions_summary: pH 7; cofactor ATP

proof_lines: pH 7.5, 30°C, recombinant His6-tagged wild-type enzyme

proof_lines: wild type, at pH 7, in the presence of 1 mM ATP

proof_lines: wild type, at pH 8, in the presence of 1 mM ATP


organism: Homo sapiens

substrate_name: N-acyl-D-glucosamine

substrate: N-acyl-D-glucosamine


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

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A12S to reconstruct the assayed variant sequence.

proof_lines:
pH 7.5, 80°C, recombinant mutant A12S
pH 7.5, 80°C, mutant enzyme A12S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A12S/K328I to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 80°C, recombinant mutant A12S/K328I


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R5M/A12S/F231L/K328I to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 80°C, recombinant mutant R5M/A12S/F231L/K328I

proof_lines: pH 7.5, 80°C, mutant enzyme R5M/A12S/F231L/K328I


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R5M/A12S/I52V/F231L/K328I to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 80°C, recombinant mutant R5M/A12S/I52V/F231L/K328I

proof_lines: pH 7.5, 80°C, mutant enzyme R5M/A12S/I52V/F231L/K328I


organism: Cellulosilyticum lentocellum

proof_lines: pH and temperature not specified in the publication


organism: Nostoc sp.

substrate_name: Unknown

substrate: Unknown


organism: Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / LMG 10263 / NCTC 9343 / Onslow / VPI 2553 / EN-2)

proof_lines: kcat is 67.6 sec(-1) with cellobiose as substrate (PubMed:19202279). kcat is 79.5 sec(-1) with lactose as substrate (PubMed:19202279). kcat is 104 sec(-1) with mannobiose as substrate (PubMed:21539815).


proof_lines: pH 7.5, 30°C, recombinant His6-tagged mutant K157L


proof_lines: pH 7.5, 30°C, recombinant His6-tagged mutant K155A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R5M/I52V/A12S/K328I/F231L/E327D to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 70°C, mutant enzyme R5M/I52V/A12S/K328I/F231L/E327D

proof_lines: pH 7.0, 70°C, epimerization, mutant enzyme R5M/I52V/A12S/K328I/F231L/E327D


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

proof_lines: pH 7.0, 70°C, mutant enzyme R5M/I52V/A12S/K328I/F231L

proof_lines: pH 7.0, 70°C, epimerization, mutant enzyme R5M/I52V/A12S/K328I/F231L


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A12S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A12S/K328I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R5M/A12S/F231L/K328I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R5M/A12S/I52V/F231L/K328I to reconstruct the assayed variant sequence.


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


organism: Spirochaeta thermophila


organism: Teredinibacter turnerae


organism: uncultured bacterium


substrate_name: mannobiose

substrate: mannobiose


organism: Hordeum vulgare

substrate_name: UDP-beta-L-arabinopyranose

substrate: UDP-beta-L-arabinopyranose


substrate_name: UDP-alpha-D-xylopyranose

substrate: UDP-alpha-D-xylopyranose


organism: Eubacterium cellulosolvens

proof_lines: kcat is 28.5 sec(-1) for cellobiose. kcat is 32.5 sec(-1) for lactose.


organism: Ruminococcus albus

proof_lines: kcat is 63.8 sec(-1) with cellobiose as substrate. kcat is 52.1 sec(-1) with lactose as substrate.


organism: Arabidopsis thaliana


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


organism: Pseudomonas aeruginosa

substrate_name: UDP-N-acetyl-D-glucosamine

proof_lines: kcat is 271 min(-1) with UDP-N-acetylgalactosamine as substrate. kcat is 120 min(-1) with UDP-N-acetylglucosamine as substrate. kcat is 0.188 min(-1) with UDP-galactose as substrate. kcat is 0.124 min(-1) with UDP-glucose as substrate.

substrate: UDP-N-acetyl-D-glucosamine


organism: Thermotoga maritima

substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


organism: Herpetosiphon aurantiacus

column_label: Table 1 (Biochemical properties of CEs from various bacterial origins) carries one Bacterial strain column, a pH span with Optimum and Stability columns, a Temperature span with Optimum (°C) and Stability (°C) columns, then three substrate spans headed Cellobiose, Lactose and β-(1→4)-Mannobiose, each printing the column heads k_cat (s^-1) | K_m (mM) | k_cat/K_m (s^-1 mM^-1), and a Reference column. The cited cell set is Table 1, row Herpetosiphon aurantiacus, Lactose column group: k_cat (s^-1) = 14.0; K_m (mM) = 51.9; k_cat/K_m (s^-1 mM^-1) = 0.270; each of the three cells carries the footnote letter f (30°C).

normalized_value_unit_evidence: kcat: printed Table 1 cell 14.0 under the column head k_cat (s^-1) in the Lactose column group of row Herpetosiphon aurantiacus; the column is already per second, so no conversion applies and the paper value is 14.0 s^(-1). Km: printed Table 1 cell 51.9 under the column head K_m (mM) of the same column group; the column is already in mM, so no conversion applies and the paper value is 51.9 mM. kcat/Km: printed Table 1 cell 0.270 under the column head k_cat/K_m (s^-1 mM^-1) of the same column group; the column is already in the canonical unit, so 0.270 x 1 = 0.27 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row Herpetosiphon aurantiacus, Lactose column group: kcat = 14.0 s^-1; Km = 51.9 mM; printed kcat/Km = 0.270 s^-1 mM^-1; footnote f states that the kinetic parameters were determined at 30°C.


substrate_name: cellobiose

substrate: cellobiose


organism: Spirosoma linguale

column_label: Table 1 (Biochemical properties of CEs from various bacterial origins) carries one Bacterial strain column, a pH span with Optimum and Stability columns, a Temperature span with Optimum (°C) and Stability (°C) columns, then three substrate spans headed Cellobiose, Lactose and β-(1→4)-Mannobiose, each printing the column heads k_cat (s^-1) | K_m (mM) | k_cat/K_m (s^-1 mM^-1), and a Reference column. The cited cell set is Table 1, row Spirosoma linguale, Lactose column group: k_cat (s^-1) = 92.1; K_m (mM) = 206; k_cat/K_m (s^-1 mM^-1) = 0.447; each of the three cells carries the footnote letter f (30°C).

normalized_value_unit_evidence: kcat: printed Table 1 cell 92.1 under the column head k_cat (s^-1) in the Lactose column group of row Spirosoma linguale; the column is already per second, so no conversion applies and the paper value is 92.1 s^(-1). Km: printed Table 1 cell 206 under the column head K_m (mM) of the same column group; the column is already in mM, so no conversion applies and the paper value is 206.0 mM. kcat/Km: printed Table 1 cell 0.447 under the column head k_cat/K_m (s^-1 mM^-1) of the same column group; the column is already in the canonical unit, so 0.447 x 1 = 0.447 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row Spirosoma linguale, Lactose column group: kcat = 92.1 s^-1; Km = 206 mM; printed kcat/Km = 0.447 s^-1 mM^-1; footnote f states that the kinetic parameters were determined at 30°C.


substrate_name: UDP-glucuronate

proof_lines: Equilibrium between UDP-glucuronate and UDP-D-galacturonate established at 1:1.9. No activity with UDP-Galactose, UDP-Glucose, UDP-arabinose, UDP-Xylose, CDP-glucose or GDP-mannose.

substrate: UDP-glucuronate


organism: Bacillus subtilis

substrate_name: UDP-N-acetylglucosamine

substrate: UDP-N-acetylglucosamine


organism: Plesiomonas shigelloides

substrate_name: UDP-GalNAc

proof_lines: kcat is 461 sec(-1) with UDP-GlcNAc. kcat is 1038 sec(-1) with UDP-GalNAc.

substrate: UDP-GalNAc


substrate_name: UDP-D-glucose

substrate: UDP-D-glucose


substrate_name: UDP-glucose

proof_lines: kcat is 19 sec(-1) with UDP-glucose as substrate (PubMed:16644739). kcat is 42 sec(-1) with UDP-galactose as substrate (PubMed:16644739). kcat is 57 sec(-1) with UDP-galactose as substrate (PubMed:16644739). kcat is 66 sec(-1) with UDP-gala

substrate: UDP-glucose


organism: Lathyrus oleraceus

substrate_name: UDP-D-xylose

assay_conditions_summary: pH 8.6; cofactor NAD+

proof_lines: 50 mM Tris-HCl buffer (pH 8.6), 0.1 mM NAD+, 1 mM UDP-sugar and enzyme

substrate: UDP-D-xylose


organism: Trichormus variabilis

substrate_name: N-acetyl-D-glucosamine

assay_conditions_summary: pH 9; cofactor ATP

substrate: N-acetyl-D-glucosamine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K151V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K155A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K157L to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature K160P could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Rhodothermus marinus

proof_lines: kcat is 80.8 sec(-1) with cellobiose as substrate. kcat is 111 sec(-1) with lactose as substrate.


proof_lines: Equilibrium between UDP-glucuronate and UDP-D-galacturonate established at 1:1.3.


organism: Dyadobacter fermentans

column_label: Table 1 row Dyadobacter fermentans; Cellobiose kcat = 240f, Km = 179f, kcat/Km = 1.34f.

raw_value_unit_evidence: Cellobiose columns report kcat 240 s^-1, Km 179 mM, kcat/Km 1.34 s^-1*mM^-1.

row_label: Dyadobacter fermentans; Cellobiose columns

table_label: Table 1. Biochemical properties of CEs from various bacterial origins.


substrate_name: lactose

column_label: Table 1 row Dyadobacter fermentans; Lactose kcat = 44.9f, Km = 95.7f, kcat/Km = 0.469f.

raw_value_unit_evidence: Lactose columns report kcat 44.9 s^-1, Km 95.7 mM, kcat/Km 0.469 s^-1*mM^-1.

row_label: Dyadobacter fermentans; Lactose columns

substrate: lactose


organism: [Eubacterium] cellulosolvens

column_label: Table 1; row Eubacterium cellulosolvens; column group Cellobiose; cell kcat (s-1) = 28.5; cell Km (mM) = 11.3; cell kcat/Km (s-1mM-1) = 2.52.

normalized_value_unit_evidence: kcat 28.5 s^-1 = 28.5 s^-1 (already the canonical kcat unit, no conversion). Km 11.3 mM = 11.3 mM (already the canonical Km unit, no conversion). The Cellobiose kcat/Km cell is printed rounded as 2.52 s^-1 mM^-1; the normalized kcat/Km recorded here is this same row's own kcat divided by its own Km, 28.5 / 11.3 = 2.5221238938053094 s^-1 mM^-1, which reproduces the printed cell 2.52 at the precision the table prints.

raw_value_unit_evidence: Table 1. Biochemical properties of CEs from various bacterial origins. Row Eubacterium cellulosolvens, Cellobiose column group: kcat 28.5 s^-1; Km 11.3 mM; kcat/Km 2.52 s^-1 mM^-1.

row_label: Eubacterium cellulosolvens; Cellobiose columns


column_label: Table 1; row Eubacterium cellulosolvens; column group Lactose; cell kcat (s-1) = 32.5; cell Km (mM) = 72.0; cell kcat/Km (s-1mM-1) = 0.451.

normalized_value_unit_evidence: kcat 32.5 s^-1 = 32.5 s^-1 (already the canonical kcat unit, no conversion). Km 72.0 mM = 72.0 mM (already the canonical Km unit, no conversion). The Lactose kcat/Km cell is printed rounded as 0.451 s^-1 mM^-1; the normalized kcat/Km recorded here is this same row's own kcat divided by its own Km, 32.5 / 72.0 = 0.4513888888888889 s^-1 mM^-1, which reproduces the printed cell 0.451 at the precision the table prints.

raw_value_unit_evidence: Table 1. Biochemical properties of CEs from various bacterial origins. Row Eubacterium cellulosolvens, Lactose column group: kcat 32.5 s^-1; Km 72.0 mM; kcat/Km 0.451 s^-1 mM^-1.

row_label: Eubacterium cellulosolvens; Lactose columns


organism: Flavobacterium johnsoniae

column_label: The literal Flavobacterium johnsoniae Cellobiose columns bind both current primary components and footnote f binds the assay to 30 C. The current stored efficiency is their deterministic quotient; the independently printed rounded efficiency is retained separately.

normalized_value_unit_evidence: kcat=39.9 s^-1; Km=53.2 mM; current same-row quotient=0.7499999999999999 s^-1 mM^-1; printed rounded efficiency=0.750 s^-1 mM^-1 and is preserved separately

raw_value_unit_evidence: Flavobacterium johnsoniae Cellobiose cells: kcat 39.9f s^-1; Km 53.2f mM; printed kcat/Km 0.750f s^-1 mM^-1

row_label: Flavobacterium johnsoniae / Cellobiose

table_label: Table 1. Biochemical properties of CEs from various bacterial origins


column_label: The literal Flavobacterium johnsoniae Lactose columns bind both current primary components and footnote f binds the assay to 30 C. The current stored efficiency is their deterministic quotient; the independently printed rounded efficiency is retained separately.

normalized_value_unit_evidence: kcat=17.5 s^-1; Km=34.9 mM; current same-row quotient=0.501432664756447 s^-1 mM^-1; printed rounded efficiency=0.501 s^-1 mM^-1 and is preserved separately

raw_value_unit_evidence: Flavobacterium johnsoniae Lactose cells: kcat 17.5f s^-1; Km 34.9f mM; printed kcat/Km 0.501f s^-1 mM^-1

row_label: Flavobacterium johnsoniae / Lactose


organism: Dictyoglomus turgidum

column_label: PMID 27031293 / DOI 10.1080/09168451.2016.1166934, Table 1, row Dictyoglomus turgidum / cellobiose, kcat, Km, and kcat/Km columns for the expected substrate group.

raw_value_unit_evidence: Table 1 Dictyoglomus turgidum / cellobiose: kcat 169 s^-1; Km 75.8 mM; kcat/Km 2.23 s^-1 mM^-1.

row_label: Dictyoglomus turgidum / cellobiose

table_label: Table 1: Biochemical properties of CEs from various bacterial origins


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0DKY4 and applied mutation signature R377A to reconstruct the assayed variant sequence.

column_label: Table 1 Kinetic values for cellobiose of RaCE and its mutant proteins; row R377A; columns Spec act (U mg-1), kcat (s-1), Km (mM), kcat/Km (s-1 mM-1): R377A 12.1 (43) 26.6 36.8 0.72

normalized_value_unit_evidence: kcat normalized_value=26.6 normalized_unit=s^(-1); Km normalized_value=37.0 normalized_unit=mM; kcat/Km normalized_value=0.7189189189189189 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: kcat raw_value=26.6 raw_unit=s^(-1); Km raw_value=36.8 raw_unit=mM; kcat/Km raw_value=0.72 raw_unit=s^(-1)*mM^(-1)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W303F to reconstruct the assayed variant sequence.

column_label: Table 1 Kinetic values for cellobiose of RaCE and its mutant proteins; row W303F; columns Spec act (U mg-1), kcat (s-1), Km (mM), kcat/Km (s-1 mM-1): W303F 5.99 (11) 46.4 108 0.43

normalized_value_unit_evidence: kcat normalized_value=46.4 normalized_unit=s^(-1); Km normalized_value=108.0 normalized_unit=mM; kcat/Km normalized_value=0.42962962962962964 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: kcat raw_value=46.4 raw_unit=s^(-1); Km raw_value=108.0 raw_unit=mM; kcat/Km raw_value=0.43 raw_unit=s^(-1)*mM^(-1)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W55F to reconstruct the assayed variant sequence.

column_label: Table 1 Kinetic values for cellobiose of RaCE and its mutant proteins; row W55F; columns Spec act (U mg-1), kcat (s-1), Km (mM), kcat/Km (s-1 mM-1): W55F 42.0 (84) 215 127 1.69

normalized_value_unit_evidence: kcat normalized_value=215.0 normalized_unit=s^(-1); Km normalized_value=127.0 normalized_unit=mM; kcat/Km normalized_value=1.6929133858267718 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: kcat raw_value=215.0 raw_unit=s^(-1); Km raw_value=127.0 raw_unit=mM; kcat/Km raw_value=1.69 raw_unit=s^(-1)*mM^(-1)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F114A to reconstruct the assayed variant sequence.

column_label: Table 2 Kinetic values for lactose of RaCE and its mutant proteins; row F114A; columns Spec act (U mg-1), kcat (s-1), Km (mM), kcat/Km (s-1 mM-1): F114A 0.44 (1.6) 1.79 95.2 0.019

normalized_value_unit_evidence: kcat normalized_value=1.79 normalized_unit=s^(-1); kcat/Km normalized_value=0.018842105263157896 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: kcat raw_value=1.79 raw_unit=s^(-1); Km raw_value=95.2 raw_unit=mM; kcat/Km raw_value=0.019 raw_unit=s^(-1)*mM^(-1)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0DKY4 and applied mutation signature R377A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

column_label: Table 2 Kinetic values for lactose of RaCE and its mutant proteins; row R377A; columns Spec act (U mg-1), kcat (s-1), Km (mM), kcat/Km (s-1 mM-1): R377A 6.60 (23) 20.9 73.3 0.285

normalized_value_unit_evidence: kcat normalized_value=20.9 normalized_unit=s^(-1); kcat/Km normalized_value=0.2863013698630137 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: kcat raw_value=20.9 raw_unit=s^(-1); Km raw_value=73.3 raw_unit=mM; kcat/Km raw_value=0.285 raw_unit=s^(-1)*mM^(-1)


column_label: Table 2 Kinetic values for lactose of RaCE and its mutant proteins; row W303F; columns Spec act (U mg-1), kcat (s-1), Km (mM), kcat/Km (s-1 mM-1): W303F 0.53 (1.9) 4.04 145 0.028

normalized_value_unit_evidence: kcat normalized_value=4.04 normalized_unit=s^(-1); Km normalized_value=145.0 normalized_unit=mM; kcat/Km normalized_value=0.027862068965517243 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: kcat raw_value=4.04 raw_unit=s^(-1); Km raw_value=145.0 raw_unit=mM; kcat/Km raw_value=0.028 raw_unit=s^(-1)*mM^(-1)


column_label: Table 2 Kinetic values for lactose of RaCE and its mutant proteins; row W55F; columns Spec act (U mg-1), kcat (s-1), Km (mM), kcat/Km (s-1 mM-1): W55F 22.7 (80) 78.3 72.3 1.08

normalized_value_unit_evidence: kcat normalized_value=78.3 normalized_unit=s^(-1); kcat/Km normalized_value=1.0875 normalized_unit=s^(-1)*mM^(-1)

raw_value_unit_evidence: kcat raw_value=78.3 raw_unit=s^(-1); Km raw_value=72.3 raw_unit=mM; kcat/Km raw_value=1.08 raw_unit=s^(-1)*mM^(-1)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0DKY4 and applied mutation signature F114A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic values for cellobiose of RaCE and its mutant proteins (Biotechnology Letters 2009, 31(7): 1065-1071), printed column heads Mutation | Spec act (U mg-1) | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Manuscript page 16 (PDF page 17). Table 1, mutation row F114A; columns kcat (s-1), Km (mM) and kcat/Km (s-1 mM-1); kcat cell = 4.64; Km cell = 55.6; kcat/Km cell = 0.08. captured primary segment: cellobiose | F114A RaCE, the site-directed F114A single-substitution mutant of recombinant Ruminococcus albus cellobiose 2-epimerase expressed in Escherichia coli BL21 (DE3) | Table 1 kcat 4.64 s-1 | Table 1 Km 55.6 mM | Table 1 kcat/Km printed cell 0.08 under the column head kcat/Km (s-1 mM-1)

normalized_value_unit_evidence: kcat: printed Table 1 kcat cell 4.64 under the column head kcat (s-1); the printed turnover column is already per second, so no unit conversion applies and the value is 4.64 s^(-1); the export stores 4.64 s^(-1). Km: printed Table 1 Km cell 55.6 under the column head Km (mM); the printed Michaelis column is already in millimolar, so no unit conversion applies and the value is 55.6 mM; the export stores 56.0 mM. kcat/Km: printed Table 1 kcat/Km cell 0.08 under the column head kcat/Km (s-1 mM-1); the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 0.08 s^(-1)*mM^(-1); the export stores 0.08285714285714285 s^(-1)*mM^(-1).

raw_value_unit_evidence: Manuscript page 16 (PDF page 17), Table 1, mutation row F114A: kcat = 4.64 s-1; Km = 55.6 mM; kcat/Km = 0.08 under the printed column head kcat/Km (s-1 mM-1).

row_label: Table 1, mutation row F114A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0DKY4 and applied mutation signature M106T to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic values for cellobiose of RaCE and its mutant proteins (Biotechnology Letters 2009, 31(7): 1065-1071), printed column heads Mutation | Spec act (U mg-1) | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Manuscript page 16 (PDF page 17). Table 1, mutation row M106T; columns kcat (s-1), Km (mM) and kcat/Km (s-1 mM-1); kcat cell = 29.7; Km cell = 128; kcat/Km cell = 0.23. captured primary segment: cellobiose | M106T RaCE, the site-directed M106T single-substitution mutant of recombinant Ruminococcus albus cellobiose 2-epimerase expressed in Escherichia coli BL21 (DE3) | Table 1 kcat 29.7 s-1 | Table 1 Km 128 mM | Table 1 kcat/Km printed cell 0.23 under the column head kcat/Km (s-1 mM-1)

normalized_value_unit_evidence: kcat: printed Table 1 kcat cell 29.7 under the column head kcat (s-1); the printed turnover column is already per second, so no unit conversion applies and the value is 29.7 s^(-1); the export stores 29.7 s^(-1). Km: printed Table 1 Km cell 128 under the column head Km (mM); the printed Michaelis column is already in millimolar, so no unit conversion applies and the value is 128.0 mM; the export stores 128.0 mM. kcat/Km: printed Table 1 kcat/Km cell 0.23 under the column head kcat/Km (s-1 mM-1); the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 0.23 s^(-1)*mM^(-1); the export stores 0.23203125 s^(-1)*mM^(-1).

raw_value_unit_evidence: Manuscript page 16 (PDF page 17), Table 1, mutation row M106T: kcat = 29.7 s-1; Km = 128 mM; kcat/Km = 0.23 under the printed column head kcat/Km (s-1 mM-1).

row_label: Table 1, mutation row M106T


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0DKY4 and applied mutation signature M179T to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic values for cellobiose of RaCE and its mutant proteins (Biotechnology Letters 2009, 31(7): 1065-1071), printed column heads Mutation | Spec act (U mg-1) | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Manuscript page 16 (PDF page 17). Table 1, mutation row M179T; columns kcat (s-1), Km (mM) and kcat/Km (s-1 mM-1); kcat cell = 36.9; Km cell = 146; kcat/Km cell = 0.25. captured primary segment: cellobiose | M179T RaCE, the site-directed M179T single-substitution mutant of recombinant Ruminococcus albus cellobiose 2-epimerase expressed in Escherichia coli BL21 (DE3) | Table 1 kcat 36.9 s-1 | Table 1 Km 146 mM | Table 1 kcat/Km printed cell 0.25 under the column head kcat/Km (s-1 mM-1)

normalized_value_unit_evidence: kcat: printed Table 1 kcat cell 36.9 under the column head kcat (s-1); the printed turnover column is already per second, so no unit conversion applies and the value is 36.9 s^(-1); the export stores 36.9 s^(-1). Km: printed Table 1 Km cell 146 under the column head Km (mM); the printed Michaelis column is already in millimolar, so no unit conversion applies and the value is 146.0 mM; the export stores 146.0 mM. kcat/Km: printed Table 1 kcat/Km cell 0.25 under the column head kcat/Km (s-1 mM-1); the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 0.25 s^(-1)*mM^(-1); the export stores 0.25273972602739725 s^(-1)*mM^(-1).

raw_value_unit_evidence: Manuscript page 16 (PDF page 17), Table 1, mutation row M179T: kcat = 36.9 s-1; Km = 146 mM; kcat/Km = 0.25 under the printed column head kcat/Km (s-1 mM-1).

row_label: Table 1, mutation row M179T


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0DKY4 and applied mutation signature M212T to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic values for cellobiose of RaCE and its mutant proteins (Biotechnology Letters 2009, 31(7): 1065-1071), printed column heads Mutation | Spec act (U mg-1) | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Manuscript page 16 (PDF page 17). Table 1, mutation row M212T; columns kcat (s-1), Km (mM) and kcat/Km (s-1 mM-1); kcat cell = 31.5; Km cell = 20.1; kcat/Km cell = 1.57. captured primary segment: cellobiose | M212T RaCE, the site-directed M212T single-substitution mutant of recombinant Ruminococcus albus cellobiose 2-epimerase expressed in Escherichia coli BL21 (DE3) | Table 1 kcat 31.5 s-1 | Table 1 Km 20.1 mM | Table 1 kcat/Km printed cell 1.57 under the column head kcat/Km (s-1 mM-1)

normalized_value_unit_evidence: kcat: printed Table 1 kcat cell 31.5 under the column head kcat (s-1); the printed turnover column is already per second, so no unit conversion applies and the value is 31.5 s^(-1); the export stores 31.5 s^(-1). Km: printed Table 1 Km cell 20.1 under the column head Km (mM); the printed Michaelis column is already in millimolar, so no unit conversion applies and the value is 20.1 mM; the export stores 20.0 mM. kcat/Km: printed Table 1 kcat/Km cell 1.57 under the column head kcat/Km (s-1 mM-1); the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 1.57 s^(-1)*mM^(-1); the export stores 1.575 s^(-1)*mM^(-1).

raw_value_unit_evidence: Manuscript page 16 (PDF page 17), Table 1, mutation row M212T: kcat = 31.5 s-1; Km = 20.1 mM; kcat/Km = 1.57 under the printed column head kcat/Km (s-1 mM-1).

row_label: Table 1, mutation row M212T


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M270T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0DKY4 and applied mutation signature M378T to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic values for cellobiose of RaCE and its mutant proteins (Biotechnology Letters 2009, 31(7): 1065-1071), printed column heads Mutation | Spec act (U mg-1) | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Manuscript page 16 (PDF page 17). Table 1, mutation row M378T; columns kcat (s-1), Km (mM) and kcat/Km (s-1 mM-1); kcat cell = 5.16; Km cell = 83.7; kcat/Km cell = 0.06. captured primary segment: cellobiose | M378T RaCE, the site-directed M378T single-substitution mutant of recombinant Ruminococcus albus cellobiose 2-epimerase expressed in Escherichia coli BL21 (DE3) | Table 1 kcat 5.16 s-1 | Table 1 Km 83.7 mM | Table 1 kcat/Km printed cell 0.06 under the column head kcat/Km (s-1 mM-1)

normalized_value_unit_evidence: kcat: printed Table 1 kcat cell 5.16 under the column head kcat (s-1); the printed turnover column is already per second, so no unit conversion applies and the value is 5.16 s^(-1); the export stores 5.16 s^(-1). Km: printed Table 1 Km cell 83.7 under the column head Km (mM); the printed Michaelis column is already in millimolar, so no unit conversion applies and the value is 83.7 mM; the export stores 84.0 mM. kcat/Km: printed Table 1 kcat/Km cell 0.06 under the column head kcat/Km (s-1 mM-1); the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 0.06 s^(-1)*mM^(-1); the export stores 0.06142857142857143 s^(-1)*mM^(-1).

raw_value_unit_evidence: Manuscript page 16 (PDF page 17), Table 1, mutation row M378T: kcat = 5.16 s-1; Km = 83.7 mM; kcat/Km = 0.06 under the printed column head kcat/Km (s-1 mM-1).

row_label: Table 1, mutation row M378T


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0DKY4 and applied mutation signature M380T to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic values for cellobiose of RaCE and its mutant proteins (Biotechnology Letters 2009, 31(7): 1065-1071), printed column heads Mutation | Spec act (U mg-1) | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Manuscript page 16 (PDF page 17). Table 1, mutation row M380T; columns kcat (s-1), Km (mM) and kcat/Km (s-1 mM-1); kcat cell = 40.0; Km cell = 34.3; kcat/Km cell = 1.17. captured primary segment: cellobiose | M380T RaCE, the site-directed M380T single-substitution mutant of recombinant Ruminococcus albus cellobiose 2-epimerase expressed in Escherichia coli BL21 (DE3) | Table 1 kcat 40.0 s-1 | Table 1 Km 34.3 mM | Table 1 kcat/Km printed cell 1.17 under the column head kcat/Km (s-1 mM-1)

normalized_value_unit_evidence: kcat: printed Table 1 kcat cell 40.0 under the column head kcat (s-1); the printed turnover column is already per second, so no unit conversion applies and the value is 40.0 s^(-1); the export stores 40.0 s^(-1). Km: printed Table 1 Km cell 34.3 under the column head Km (mM); the printed Michaelis column is already in millimolar, so no unit conversion applies and the value is 34.3 mM; the export stores 34.0 mM. kcat/Km: printed Table 1 kcat/Km cell 1.17 under the column head kcat/Km (s-1 mM-1); the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 1.17 s^(-1)*mM^(-1); the export stores 1.1764705882352942 s^(-1)*mM^(-1).

raw_value_unit_evidence: Manuscript page 16 (PDF page 17), Table 1, mutation row M380T: kcat = 40.0 s-1; Km = 34.3 mM; kcat/Km = 1.17 under the printed column head kcat/Km (s-1 mM-1).

row_label: Table 1, mutation row M380T


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0DKY4 and applied mutation signature M62T to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic values for cellobiose of RaCE and its mutant proteins (Biotechnology Letters 2009, 31(7): 1065-1071), printed column heads Mutation | Spec act (U mg-1) | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Manuscript page 16 (PDF page 17). Table 1, mutation row M62T; columns kcat (s-1), Km (mM) and kcat/Km (s-1 mM-1); kcat cell = 30.3; Km cell = 53.8; kcat/Km cell = 0.58. captured primary segment: cellobiose | M62T RaCE, the site-directed M62T single-substitution mutant of recombinant Ruminococcus albus cellobiose 2-epimerase expressed in Escherichia coli BL21 (DE3) | Table 1 kcat 30.3 s-1 | Table 1 Km 53.8 mM | Table 1 kcat/Km printed cell 0.58 under the column head kcat/Km (s-1 mM-1)

normalized_value_unit_evidence: kcat: printed Table 1 kcat cell 30.3 under the column head kcat (s-1); the printed turnover column is already per second, so no unit conversion applies and the value is 30.3 s^(-1); the export stores 30.3 s^(-1). Km: printed Table 1 Km cell 53.8 under the column head Km (mM); the printed Michaelis column is already in millimolar, so no unit conversion applies and the value is 53.8 mM; the export stores 54.0 mM. kcat/Km: printed Table 1 kcat/Km cell 0.58 under the column head kcat/Km (s-1 mM-1); the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 0.58 s^(-1)*mM^(-1); the export stores 0.5611111111111111 s^(-1)*mM^(-1).

raw_value_unit_evidence: Manuscript page 16 (PDF page 17), Table 1, mutation row M62T: kcat = 30.3 s-1; Km = 53.8 mM; kcat/Km = 0.58 under the printed column head kcat/Km (s-1 mM-1).

row_label: Table 1, mutation row M62T


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0DKY4 and applied mutation signature M95T to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic values for cellobiose of RaCE and its mutant proteins (Biotechnology Letters 2009, 31(7): 1065-1071), printed column heads Mutation | Spec act (U mg-1) | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Manuscript page 16 (PDF page 17). Table 1, mutation row M95T; columns kcat (s-1), Km (mM) and kcat/Km (s-1 mM-1); kcat cell = 33.4; Km cell = 56.2; kcat/Km cell = 0.61. captured primary segment: cellobiose | M95T RaCE, the site-directed M95T single-substitution mutant of recombinant Ruminococcus albus cellobiose 2-epimerase expressed in Escherichia coli BL21 (DE3) | Table 1 kcat 33.4 s-1 | Table 1 Km 56.2 mM | Table 1 kcat/Km printed cell 0.61 under the column head kcat/Km (s-1 mM-1)

normalized_value_unit_evidence: kcat: printed Table 1 kcat cell 33.4 under the column head kcat (s-1); the printed turnover column is already per second, so no unit conversion applies and the value is 33.4 s^(-1); the export stores 33.3 s^(-1). Km: printed Table 1 Km cell 56.2 under the column head Km (mM); the printed Michaelis column is already in millimolar, so no unit conversion applies and the value is 56.2 mM; the export stores 56.0 mM. kcat/Km: printed Table 1 kcat/Km cell 0.61 under the column head kcat/Km (s-1 mM-1); the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 0.61 s^(-1)*mM^(-1); the export stores 0.5946428571428571 s^(-1)*mM^(-1).

raw_value_unit_evidence: Manuscript page 16 (PDF page 17), Table 1, mutation row M95T: kcat = 33.4 s-1; Km = 56.2 mM; kcat/Km = 0.61 under the printed column head kcat/Km (s-1 mM-1).

row_label: Table 1, mutation row M95T


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M96T to reconstruct the assayed variant sequence.

column_label: Table 1 Kinetic values for cellobiose of RaCE and its mutant proteins; row M96T; columns Spec act (U mg-1), kcat (s-1), Km (mM), kcat/Km (s-1 mM-1): M96T 8.73 (17) 43.8 121 0.37

raw_value_unit_evidence: kcat raw_value=43.8 raw_unit=s^(-1); Km raw_value=121.0 raw_unit=mM; kcat/Km raw_value=0.37 raw_unit=s^(-1)*mM^(-1)


organism: Salmonella typhi

substrate_name: UDP-GlcNAcA

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

assay_conditions_summary: pH 8; buffer 40 uL of 50 mM potassium phosphate

column_label: Table 2 (Kinetic Parameters for Reactions Catalyzed by TviC Determined by the HPLC Assay and Capillary Electrophoresis Assay), substrate row 'UDP-GlcNAcA (4)b'; column 'Km (mM)' = 0.020; column 'Vmax (mM/min)' = 0.0015; column 'TviC mM' = 2.7 x 10^-5; column 'kcat (min-1)' = 56.8; column 'kcat/Km (mM-1min-1)' = 2871.6.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.020 mM; the printed column head is Km (mM), so no unit conversion applies and 0.02 mM is the canonical paper value. kcat: printed Table 2 cell 56.8 min^-1; the printed column head is kcat (min-1), and 1 min^-1 is 1/60 s^-1, so 56.8 / 60 = 0.9466666666666667 s^-1 is the canonical paper value. kcat/Km: printed Table 2 cell 2871.6 mM^-1 min^-1; the printed column head is kcat/Km (mM-1min-1), and 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 2871.6 / 60 = 47.86 s^-1 mM^-1 is the canonical paper value.

raw_value_unit_evidence: Table 2 (Kinetic Parameters for Reactions Catalyzed by TviC), substrate row 'UDP-GlcNAcA (4)b': Km = 0.020 mM; Vmax = 0.0015 mM/min; TviC = 2.7 x 10^-5 mM; kcat = 56.8 min^-1; printed kcat/Km = 2871.6 mM^-1 min^-1.

row_label: Table 2, substrate row 'UDP-GlcNAcA (4)b'

table_label: Table 2: Kinetic Parameters for Reactions Catalyzed by TviC Determined by the HPLC Assay and Capillary Electrophoresis Assay (Biochemistry 2006, 45(26): 8163-8173)

substrate: UDP-GlcNAcA


substrate_name: UDP-GalNAcA

column_label: Table 2 (Kinetic Parameters for Reactions Catalyzed by TviC Determined by the HPLC Assay and Capillary Electrophoresis Assay), substrate row 'UDP-GalNAcA (5)b'; column 'Km (mM)' = 0.042; column 'Vmax (mM/min)' = 0.0021; column 'TviC mM' = 5.3 x 10^-5; column 'kcat (min-1)' = 39.1; column 'kcat/Km (mM-1min-1)' = 931.3.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.042 mM; the printed column head is Km (mM), so no unit conversion applies and 0.042 mM is the canonical paper value. kcat: printed Table 2 cell 39.1 min^-1; the printed column head is kcat (min-1), and 1 min^-1 is 1/60 s^-1, so 39.1 / 60 = 0.6516666666666667 s^-1 is the canonical paper value. kcat/Km: printed Table 2 cell 931.3 mM^-1 min^-1; the printed column head is kcat/Km (mM-1min-1), and 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 931.3 / 60 = 15.521666666666667 s^-1 mM^-1 is the canonical paper value.

raw_value_unit_evidence: Table 2 (Kinetic Parameters for Reactions Catalyzed by TviC), substrate row 'UDP-GalNAcA (5)b': Km = 0.042 mM; Vmax = 0.0021 mM/min; TviC = 5.3 x 10^-5 mM; kcat = 39.1 min^-1; printed kcat/Km = 931.3 mM^-1 min^-1.

row_label: Table 2, substrate row 'UDP-GalNAcA (5)b'

substrate: UDP-GalNAcA


substrate_name: UDP-GlcNAc

proof_lines: kcat is 56.8 min(-1) with UDP-GlcNAcA as substrate. kcat is 39.1 min(-1) with UDP-GalNAcA as substrate. kcat is 14.2 min(-1) with UDP-GlcNAc as substrate. kcat is 52.6 min(-1) with UDP-GalNAc as substrate.

substrate: UDP-GlcNAc


organism: Bacteroides fragilis

column_label: Table 3 rBfCE Cellobiose column: specific activity 61.8 U/mg; Km 3.75 mM; kcat 67.6 s^-1; kcat/Km 18.0 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized values: kcat=67.6 s^-1; Km=3.75 mM; independently printed kcat/Km=18.0 s^-1 mM^-1; current values are kcat=67.6 s^-1, Km=4.35 mM, and quotient-derived kcat/Km=15.540229885057471 s^-1 mM^-1.

row_label: rBfCE

table_label: Table 3. Kinetic Parameters of rBfCE and rRaCE toward Cellobiose and Lactose


column_label: J-STAGE PDF Table 3 rBfCE lactose column gives Km=6.56 mM, kcat=79.5 s^-1, and kcat/Km=12.1 s^-1*mM^-1; exported kcat/Km is 12.11890243902439.

normalized_value_unit_evidence: Km normalized_value=6.56 mM; kcat normalized_value=79.5 s^-1; kcat/Km normalized_value=12.1 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=6.56 raw_unit=mM; kcat raw_value=79.5 raw_unit=s^-1; kcat/Km raw_value=12.1 raw_unit=s^-1*mM^-1

row_label: rBfCE lactose column; Km, kcat, and kcat/Km rows

table_label: Table 3 Kinetic Parameters of rBfCE and rRaCE toward Cellobiose and Lactose


organism: Pedobacter heparinus

column_label: PMID 27031293 / DOI 10.1080/09168451.2016.1166934, Table 1, row Pedobacter heparinus / cellobiose, kcat, Km, and kcat/Km columns for the expected substrate group.

raw_value_unit_evidence: Table 1 Pedobacter heparinus / cellobiose: kcat 7.02 s^-1; Km 29.6 mM; kcat/Km 0.237 s^-1 mM^-1.

row_label: Pedobacter heparinus / cellobiose


column_label: PMID 27031293 / DOI 10.1080/09168451.2016.1166934, Table 1, row Pedobacter heparinus / lactose, kcat, Km, and kcat/Km columns for the expected substrate group.

raw_value_unit_evidence: Table 1 Pedobacter heparinus / lactose: kcat 5.43 s^-1; Km 24.5 mM; kcat/Km 0.222 s^-1 mM^-1.

row_label: Pedobacter heparinus / lactose


organism: Saccharophagus degradans

column_label: Table 1; row Saccharophagus degradans; column group Cellobiose; cell kcat (s-1) = 26.1f; cell Km (mM) = 22.6f; cell kcat/Km (s-1mM-1) = 1.15f.

normalized_value_unit_evidence: kcat 26.1f s^-1 = 26.1 s^-1 (already the canonical kcat unit, no conversion). Km 22.6f mM = 22.6 mM (already the canonical Km unit, no conversion). The Cellobiose kcat/Km cell is printed rounded as 1.15f s^-1 mM^-1; the normalized kcat/Km recorded here is this same row's own kcat divided by its own Km, 26.1 / 22.6 = 1.154867256637168 s^-1 mM^-1, which reproduces the printed cell 1.15 at the precision the table prints.

raw_value_unit_evidence: Table 1. Biochemical properties of CEs from various bacterial origins. Row Saccharophagus degradans, Cellobiose column group: kcat 26.1f s^-1; Km 22.6f mM; kcat/Km 1.15f s^-1 mM^-1.

row_label: Saccharophagus degradans; Cellobiose columns


column_label: Table 1; row Saccharophagus degradans; column group Lactose; cell kcat (s-1) = 7.82f; cell Km (mM) = 29.2f; cell kcat/Km (s-1mM-1) = 0.268f.

normalized_value_unit_evidence: kcat 7.82f s^-1 = 7.82 s^-1 (already the canonical kcat unit, no conversion). Km 29.2f mM = 29.2 mM (already the canonical Km unit, no conversion). The Lactose kcat/Km cell is printed rounded as 0.268f s^-1 mM^-1; the normalized kcat/Km recorded here is this same row's own kcat divided by its own Km, 7.82 / 29.2 = 0.26780821917808223 s^-1 mM^-1, which reproduces the printed cell 0.268 at the precision the table prints.

raw_value_unit_evidence: Table 1. Biochemical properties of CEs from various bacterial origins. Row Saccharophagus degradans, Lactose column group: kcat 7.82f s^-1; Km 29.2f mM; kcat/Km 0.268f s^-1 mM^-1.

row_label: Saccharophagus degradans; Lactose columns


column_label: PMID 27031293 / DOI 10.1080/09168451.2016.1166934, Table 1, row Spirosoma linguale / cellobiose, kcat, Km, and kcat/Km columns for the expected substrate group.

raw_value_unit_evidence: Table 1 Spirosoma linguale / cellobiose: kcat 222 s^-1; Km 104 mM; kcat/Km 2.13 s^-1 mM^-1.

row_label: Spirosoma linguale / cellobiose


column_label: The literal Spirosoma linguale Lactose columns bind both current primary components and the preceding superscript-only line binds their assay to footnote f/30 C. The current stored efficiency is their deterministic quotient; the independently printed rounded efficiency is retained separately.

normalized_value_unit_evidence: kcat=92.1 s^-1; Km=206 mM; current same-row quotient=0.4470873786407767 s^-1 mM^-1; printed rounded efficiency=0.447 s^-1 mM^-1 and is preserved separately

raw_value_unit_evidence: Spirosoma linguale Lactose cells: kcat 92.1 with footnote f in s^-1; Km 206 with footnote f in mM; printed kcat/Km 0.447 with footnote f in s^-1 mM^-1

row_label: Spirosoma linguale / Lactose


organism: Caldicellulosiruptor obsidiansis


organism: Caldicellulosiruptor morganii

assay_conditions_summary: pH 7


enzyme_display_name: CDP-paratose 2-epimerase

organism: Salmonella enterica subsp. enterica serovar Enteritidis

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

enzyme: CDP-paratose 2-epimerase


organism: Spirochaeta thermophila


substrate_name: mannobiose

substrate: mannobiose


organism: Caldicellulosiruptor saccharolyticus

substrate_name: D-glucose

assay_conditions_summary: pH 7.5; buffer 50 mM PIPES

substrate: D-glucose


organism: Ruminococcus albus

column_label: J-STAGE PDF Table 3 rRaCE cellobiose column gives Km=13.8 mM, kcat=63.8 s^-1, and kcat/Km=4.62 s^-1*mM^-1; exported kcat/Km is 4.623188405797101.

normalized_value_unit_evidence: Km normalized_value=13.8 mM; kcat normalized_value=63.8 s^-1; kcat/Km normalized_value=4.62 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=13.8 raw_unit=mM; kcat raw_value=63.8 raw_unit=s^-1; kcat/Km raw_value=4.62 raw_unit=s^-1*mM^-1

row_label: rRaCE cellobiose column; Km, kcat, and kcat/Km rows


column_label: J-STAGE PDF Table 3 rRaCE lactose column gives Km=33.0 mM, kcat=52.1 s^-1, and kcat/Km=1.58 s^-1*mM^-1; exported kcat/Km is 1.5787878787878789.

normalized_value_unit_evidence: Km normalized_value=33.0 mM; kcat normalized_value=52.1 s^-1; kcat/Km normalized_value=1.58 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=33.0 raw_unit=mM; kcat raw_value=52.1 raw_unit=s^-1; kcat/Km raw_value=1.58 raw_unit=s^-1*mM^-1

row_label: rRaCE lactose column; Km, kcat, and kcat/Km rows


column_label: Table 1 R. marinus cellobiose row reports kcat 80.8, Km 27.2, and kcat/Km 2.97.

normalized_value_unit_evidence: kcat normalized_value=80.8 normalized_unit=s^-1; Km normalized_value=27.2 normalized_unit=mM; kcat/Km normalized_value=2.97 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=80.8 raw_unit=s^-1; Km raw_value=27.2 raw_unit=mM; kcat/Km raw_value=2.97 raw_unit=s^-1 mM^-1

row_label: R. marinus / Cellobiose

table_label: J-STAGE PDF Table 1. Kinetic Parameters of CE for Cellobiose and Lactose


assay_conditions_summary: pH 6.3; 333.15 K; buffer 1 mL reactions containing 30 mM sodium phosphate

column_label: Table 1 R. marinus Lactose column: kcat 111 s^-1; Km 28.8 mM; kcat/Km 3.85 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized values: kcat=111 s^-1; Km=28.8 mM; independently printed kcat/Km=3.85 s^-1 mM^-1.

row_label: R. marinus

table_label: Table 1. Kinetic Parameters of CE for Cellobiose and Lactose


organism: Herpetosiphon aurantiacus

column_label: Table 1 row Herpetosiphon aurantiacus; Cellobiose kcat = 18.7, Km = 28.2, kcat/Km = 0.663.

raw_value_unit_evidence: Cellobiose columns report kcat 18.7 s^-1, Km 28.2 mM, kcat/Km 0.663 s^-1*mM^-1.

row_label: Herpetosiphon aurantiacus; Cellobiose columns


column_label: Table 1 row Bacteroides fragilis; beta-(1->4)-Mannobiose kcat = 104f, Km = 5.51f, kcat/Km = 18.9f.

raw_value_unit_evidence: beta-(1->4)-Mannobiose columns report kcat 104 s^-1, Km 5.51 mM, kcat/Km 18.9 s^-1*mM^-1.

row_label: Bacteroides fragilis; beta-(1->4)-Mannobiose columns


organism: Arabidopsis thaliana


organism: Homo sapiens

substrate_name: UDP-galactose (at 37 degrees Celsius and pH 8.8)

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature V94M to reconstruct the assayed variant sequence.


organism: Thermotoga maritima

substrate_name: UDP-alpha-D-galactose

substrate: UDP-alpha-D-galactose


organism: Streptococcus pneumoniae

substrate_name: UDP-D-glucuronate

column_label: Figure 4D and Results prose; UDP-GlcA concentration dependence; metric apparent Km

normalized_value_unit_evidence: normalized: Km=0.24 mM

raw_value_unit_evidence: paper text: K m of 0.24 mM from Lineweaver-Burk plot of UDPGLE activity on UDP-GlcA

row_label: Cap1J UDPGLE / UDP-GlcA

table_label: Figure 4D plus Results prose

substrate: UDP-D-glucuronate


organism: Pisum sativum

substrate_name: UDP-galactose

column_label: Abstract reports apparent Km values of 0.31, 0.29, 0.16 and 0.15 mM for UDP-Glc, UDP-Gal, UDP-Ara and UDP-Xyl respectively.

raw_value_unit_evidence: Km raw_value=0.29 mM raw_unit=mM

row_label: recombinant Pisum sativum PsUGE1 / UDP-Gal

table_label: PubMed XML abstract PMID 19754426

substrate: UDP-galactose


organism: Nostoc punctiforme


enzyme_display_name: UDP-glucosamine 4-epimerase

organism: Bos taurus

substrate_name: UDPgalactose

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

enzyme: UDP-glucosamine 4-epimerase

substrate: UDPgalactose


organism: Rattus norvegicus

substrate_name: Unknown

substrate: Unknown


organism: Escherichia coli

substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


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


organism: Rhodothermus marinus


enzyme_display_name: chondroitin-glucuronate 5-epimerase

substrate_name: D-glucuronate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N648S to reconstruct the assayed variant sequence.

enzyme: chondroitin-glucuronate 5-epimerase

substrate: D-glucuronate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N336S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N183S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N642S to reconstruct the assayed variant sequence.


proof_lines: ph 5.5, 37°C, recombinant wild-type enzyme


enzyme_display_name: GDP-mannose 3,5-epimerase

organism: Auxenochlorella pyrenoidosa

substrate_name: GDP-alpha-D-mannose

proof_lines: pH and temperature not specified in the publication

enzyme: GDP-mannose 3,5-epimerase

substrate: GDP-alpha-D-mannose


column_label: PMID 27031293 / DOI 10.1080/09168451.2016.1166934, Table 1, row Ruminococcus albus / beta-(1->4)-mannobiose, kcat, Km, and kcat/Km columns for the expected substrate group.

raw_value_unit_evidence: Table 1 Ruminococcus albus / beta-(1->4)-mannobiose: kcat 201 s^-1; Km 8.74 mM; kcat/Km 23.0 s^-1 mM^-1.


proof_lines: UDP-N-acetyl-D-glucosamine, liver enzyme of tumor-bearing animals


organism: Sinorhizobium meliloti

substrate_name: UDP-D-xylopyranose

substrate: UDP-D-xylopyranose


organism: Neisseria meningitidis serogroup A / serotype 4A

substrate_name: UDP-ManNGc

proof_lines: kcat is 31 sec(-1) with UDP-GlcNAc as substrate. kcat is 52 sec(-1) with UDP-ManNAc as substrate. kcat is 4.2 sec(-1) with UDP-ManNGc as substrate. kcat is 7.8 sec(-1) with UDP-ManNPr as substrate. kcat is 6.7 sec(-1) with rUDP-ManNAc as su

substrate: UDP-ManNGc


substrate_name: D-glucuronosyl residues

substrate: D-glucuronosyl residues


enzyme_display_name: ADP-glyceromanno-heptose 6-epimerase

organism: Escherichia coli (strain K12)

substrate_name: ADP-heptose

assay_conditions_summary: cofactor ADP

enzyme: ADP-glyceromanno-heptose 6-epimerase

substrate: ADP-heptose


enzyme_display_name: dTDP-4-dehydrorhamnose 3,5-epimerase

organism: Streptococcus suis

enzyme: dTDP-4-dehydrorhamnose 3,5-epimerase


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

column_label: Table 1 reports NmSacA-His6 UDP-GlcNAc kcat 31 +/- 2 s^-1, KM 3.6 +/- 0.5 mM, and kcat/KM 8.6 s^-1 mM^-1; kcat and KM match, but kcat/KM differs from the current export

normalized_value_unit_evidence: kcat normalized_value=31 normalized_unit=s^-1; KM normalized_value=3.6 normalized_unit=mM; kcat_over_km normalized_value=8.6 normalized_unit=s^-1*mM^-1; current_export_kcat_over_km=8.61111111111111 s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=31 raw_unit=s^-1; KM raw_value=3.6 raw_unit=mM; kcat_over_km raw_value=8.6 raw_unit=s^-1*mM^-1 for UDP-GlcNAc

row_label: NmSacA-His6 UDP-GlcNAc row; kcat, KM, and kcat/KM columns

table_label: PMID 26598987 PMC HTML Table 1

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


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

column_label: Table 1 reports NmSacA-His6 UDP-ManNAc kcat 52 +/- 5 s^-1, KM 5.2 +/- 1.1 mM, and kcat/KM 10 s^-1 mM^-1; the full current metric tuple matches these explicit paper values

normalized_value_unit_evidence: kcat normalized_value=52 normalized_unit=s^-1; KM normalized_value=5.2 normalized_unit=mM; kcat_over_km normalized_value=10 normalized_unit=s^-1*mM^-1; current export matches all three values

raw_value_unit_evidence: kcat raw_value=52 raw_unit=s^-1; KM raw_value=5.2 raw_unit=mM; kcat_over_km raw_value=10 raw_unit=s^-1*mM^-1 for UDP-ManNAc

row_label: NmSacA-His6 UDP-ManNAc row; kcat, KM, and kcat/KM columns

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


substrate_name: GDP-D-mannose

substrate: GDP-D-mannose


organism: Sus scrofa

substrate_name: N-acetyl-D-glucosamine

substrate: N-acetyl-D-glucosamine


organism: Aneurinibacillus thermoaerophilus

column_label: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes; block 'DSM 10155 RmlC'; substrate row 'dTDP-6-deoxy-d-xylo-4- hexulose'; column 'Km (mM)' = 0.062 +/- 0.0063; column 'kcat (s-1)' = 2.0 +/- 0.67; the table has no kcat/Km column.

normalized_value_unit_evidence: Km: paper cell 0.062 mM; the column is already mM, so normalized Km = 0.062 mM. kcat: paper cell 2.0 s-1; the column is already s^(-1), so normalized kcat = 2.0 s^(-1). kcat/Km: not printed anywhere in the paper; the full-precision quotient of the row's own cells is 2.0 / 0.062 = 32.25806451612903 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes, block 'DSM 10155 RmlC', substrate row 'dTDP-6-deoxy-d-xylo-4- hexulose': Km = 0.062 +/- 0.0063 mM; kcat = 2.0 +/- 0.67 s-1; no kcat/Km cell is printed.

row_label: Table 4, block 'DSM 10155 RmlC', substrate row 'dTDP-6-deoxy-d-xylo-4- hexulose'


organism: Arabidopsis thaliana

assay_conditions_summary: cofactor NADPH


substrate_name: NADPH

substrate: NADPH


organism: Ruminococcus albus

substrate_name: lactose

proof_lines: F114A mutant, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C

proof_lines: F114A mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C

substrate: lactose


proof_lines: W303F mutant, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C

proof_lines: W303F mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C


substrate_name: cellobiose

proof_lines: M378T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C

substrate: cellobiose


proof_lines: M270T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C


proof_lines: R377A mutant, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C

proof_lines: R377A mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C


proof_lines: M106T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C


proof_lines: M62T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C


proof_lines: M212T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C


proof_lines: M95T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C


proof_lines: M179T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C


proof_lines: M380T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C


proof_lines: M96T mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C


proof_lines: wild type, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C

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


proof_lines: W55F mutant, 100 mM sodium phosphate, pH 7.5, 20 mM lactose, 30°C

proof_lines: W55F mutant, 100 mM sodium phosphate, pH 7.5, 20 mM cellobiose, 30°C


organism: Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)

substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


organism: Salmonella typhimurium


organism: Dictyoglomus turgidum

substrate_name: lactulose

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

substrate: lactulose


substrate_name: epilactose

substrate: epilactose


enzyme_display_name: UDP-glucose 4-epimerase

substrate_name: UDP-alpha-D-glucose

assay_conditions_summary: pH 7; 310.15 K; buffer McIlvaine

proof_lines:
pH 7.0, 37°C
24°C, pH 7.0
in McIlvaine buffer (pH 7.5), at 35°C

enzyme: UDP-glucose 4-epimerase

substrate: UDP-alpha-D-glucose


substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: UDP-glucuronate

proof_lines: recombinant AtUGlcAE2, lacking the amino acid position 1-68, in 0.1 M sodium phosphate, pH 7.6

proof_lines: recombinant AtUGlcAE3, lacking the amino acid position 1-53, in 0.1 M sodium phosphate, pH 7.6

substrate: UDP-glucuronate


substrate_name: Unknown

proof_lines: recombinant AtUGlcAE3, position 1-53 is lacking

proof_lines: recombinant AtUGlcAE2, position 1-68 is lacking

proof_lines: recombinant AtUGlcAE1, position 1-64 is lacking

substrate: Unknown


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

proof_lines: kcat is 39 sec(-1) with dTDP-6-deoxy-D-xylo-4-hexulose as substrate.


proof_lines: recombinant enzyme with N-terminal His-tag

proof_lines: recombinant enzyme with N-terminal glutathione-S-transferase tag


organism: Oryza sativa


substrate_name: D-mannose

proof_lines:
pH 7.5, 70°C, wild-type enzyme
pH 6.3, 70°C, wild-type enzyme

substrate: D-mannose


substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


proof_lines: kcat is 31 sec(-1) with UDP-GlcNAc as substrate. kcat is 52 sec(-1) with UDP-ManNAc as substrate. kcat is 4.2 sec(-1) with UDP-ManNGc as substrate. kcat is 7.8 sec(-1) with UDP-ManNPr as substrate. kcat is 6.7 sec(-1) with rUDP-ManNAc as su

source_databases_merged: brenda skid uniprot


substrate_name: D-galactose

assay_conditions_summary: pH 7.5; 308.15 K; buffer McIlvaine

substrate: D-galactose


substrate_name: D-tagatose

substrate: D-tagatose


organism: Bacillus anthracis


substrate_name: GDP-alpha-D-mannose

proof_lines: pH and temperature not specified in the publication

substrate: GDP-alpha-D-mannose


proof_lines: recombinant OsUGlcAE3, lacking the amino acid position 1-53, in 0.1 M sodium phosphate, pH 7.6


proof_lines: recombinant OsUGlcAE3, position 1-53 is lacking


organism: Oryza sativa subsp. japonica

substrate_name: GDP-mannose

proof_lines: The catalytic efficiency increases by 2-fold in the presence of NAD(+).

substrate: GDP-mannose


organism: Campylobacter jejuni


enzyme_display_name: allantoin racemase

organism: Pseudomonas fluorescens

substrate_name: (R)-allantoin

proof_lines: mutant E78D, pH 7.6, temperature not specified in the publication

enzyme: allantoin racemase

substrate: (R)-allantoin


proof_lines: wild-type, pH 7.6, temperature not specified in the publication


organism: Salmonella enterica


enzyme_display_name: D-cysteine desulfhydrase

organism: Solanum lycopersicum

substrate_name: D-cysteine

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

enzyme: D-cysteine desulfhydrase

substrate: D-cysteine


substrate_name: UDPglucuronate

substrate: UDPglucuronate


enzyme_display_name: 16-hydroxysteroid epimerase

organism: Homo sapiens

enzyme: 16-hydroxysteroid epimerase


organism: Salmonella enterica subsp. enterica serovar Typhi


enzyme_display_name: methylmalonyl-CoA epimerase

organism: Rattus norvegicus

substrate_name: DL-methylmalonyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: methylmalonyl-CoA epimerase

substrate: DL-methylmalonyl-CoA


enzyme_display_name: NAD(P)H-hydrate epimerase

organism: Escherichia coli (strain K12)

substrate_name: (S)-NADHX

enzyme: NAD(P)H-hydrate epimerase

substrate: (S)-NADHX


organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

substrate_name: (S)-methylmalonyl-CoA

proof_lines: kcat is 240 sec(-1) for (S)-methylmalonyl-CoA epimerization.

substrate: (S)-methylmalonyl-CoA


organism: Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.)


enzyme_display_name: alpha-methylacyl-CoA racemase

enzyme: alpha-methylacyl-CoA racemase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 3.7 sec(-1) with (25R)-3-oxo-cholest-4-en-26-oyl-CoA as substrate (PubMed:26348625). kcat is 450 sec(-1) with (2S)-ibuprofenoyl-CoA as substrate (PubMed:19854148). kcat is 291 sec(-1) with (2R)-ibuprofenoyl-CoA as substrate (PubMed:


enzyme_display_name: hydantoin racemase

organism: Pseudomonas sp. (strain NS671)

enzyme: hydantoin racemase


organism: Rhizobium meliloti

substrate_name: L-5-ethylhydantoin (L-EH)

proof_lines: kcat is 6.42 sec(-1) with L-5-ethylhydantoin (L-EH) as substrate. kcat is 3.24 sec(-1) with D-5-isobutylhydantoin (D-IBH) as substrate. kcat is 2.29 sec(-1) with D-5-benzylhydantoin (D-BH) as substrate. kcat is 2.12 sec(-1) with L-5-isobuty

substrate: L-5-ethylhydantoin (L-EH)


organism: Mus musculus

substrate_name: (R)-NADH-hydrate

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: in the presence of 5 mM KCl, at 30°C in 25 mM Tris-HCl, pH 8.0, 2 mM MgCl2, 0.2 mM ATP

substrate: (R)-NADH-hydrate


enzyme_display_name: cellobiose epimerase

organism: Treponema brennaborense

substrate_name: cellobiose

enzyme: cellobiose epimerase

substrate: cellobiose


substrate_name: (R)-pristanoyl-CoA

substrate: (R)-pristanoyl-CoA


organism: Klebsiella pneumoniae subsp. pneumoniae

substrate_name: (S)-allantoin

proof_lines: in 10 mM NaCl and 10 mM HEPES, pH 7.5, at 25°C

substrate: (S)-allantoin


substrate_name: pristanoyl-CoA

substrate: pristanoyl-CoA


substrate_name: trihydroxycoprostanoyl-CoA

substrate: trihydroxycoprostanoyl-CoA


substrate_name: 7,8-dihydroneopterin triphosphate

substrate: 7,8-dihydroneopterin triphosphate


organism: Agrobacterium tumefaciens

substrate_name: L-benzylhydantoin

substrate: L-benzylhydantoin


organism: Cereibacter sphaeroides