substrate_name: L-Ala-L-Tyr (at pH 7.5 and 28 degrees Celsius)

column_label: Table 3; TM0006; row L-Ala-L-Tyr; column K_M (x10^-3 M); raw Km 0.71 +/- 0.08 x10^-3 M; normalized Km=0.71 mM.

raw_value_unit_evidence: Table 3 gives L-Ala-L-Tyr K_M 0.71 +/- 0.08 x10^-3 M.

row_label: L-Ala-L-Tyr


enzyme_display_name: L-Ala-D/L-Glu epimerase

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

substrate_name: L-Ala-L-His (at pH 7.5 and 28 degrees Celsius)

source_db: uniprot

verification_status: verified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

column_label: Table 3; TM0006; row L-Ala-L-His; column K_M (x10^-3 M); raw Km 5.3 +/- 2.4 x10^-3 M; normalized Km=5.3 mM.

raw_value_unit_evidence: Table 3 gives L-Ala-L-His K_M 5.3 +/- 2.4 x10^-3 M.

row_label: L-Ala-L-His

table_label: PMID 19000819, Table 3: kinetic constants for epimerization of selected dipeptide substrates of TM0006

data_origin: experimental

enzyme: L-Ala-D/L-Glu epimerase

status: verified

source: uniprot


substrate_name: L-Ala-L-Leu (at pH 7.5 and 28 degrees Celsius)

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

column_label: Table 3; TM0006; row L-Ala-L-Leu; column K_M (x10^-3 M); raw Km 2.9 +/- 0.89 x10^-3 M; normalized Km=2.9 mM.

raw_value_unit_evidence: Table 3 gives L-Ala-L-Leu K_M 2.9 +/- 0.89 x10^-3 M.

row_label: L-Ala-L-Leu


substrate_name: L-Ile-L-Phe (at pH 7.5 and 28 degrees Celsius)

column_label: Table 3; TM0006; row L-Ile-L-Phe; column K_M (x10^-3 M); raw Km 4.7 +/- 1.4 x10^-3 M; normalized Km=4.7 mM.

raw_value_unit_evidence: Table 3 gives L-Ile-L-Phe K_M 4.7 +/- 1.4 x10^-3 M.

row_label: L-Ile-L-Phe


substrate_name: L-Lys-L-Phe (at pH 7.5 and 28 degrees Celsius)

column_label: Table 3; TM0006; row L-Lys-L-Phe; column K_M (x10^-3 M); raw Km 3.9 +/- 0.68 x10^-3 M; normalized Km=3.9 mM.

raw_value_unit_evidence: Table 3 gives L-Lys-L-Phe K_M 3.9 +/- 0.68 x10^-3 M.

row_label: L-Lys-L-Phe


enzyme_display_name: aspartate racemase

organism: Crassostrea gigas

substrate_name: D-Aspartate

source_db: oed

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S150P/S151P/S152Y to reconstruct the assayed variant sequence.

enzyme: aspartate racemase

substrate: D-Aspartate

source: oed


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

column_label: Table label: Table 1 Comparison of kinetic constants of SerRs and AspRs. Species/enzyme block: Crassostrea gigas | AspR | WT (SSS). Reaction row: d-Asp to l-Asp. Km column cell = 6.21 ± 0.64; Kcat column cell = 13,100 ± 700; Kcat/Km column cell = 2120 ± 110. Km, Kcat and Kcat/Km are read from the one printed row of this species/enzyme block, so they are one measurement; no value comes from another row, another block, or another paper.

normalized_value_unit_evidence: Km 6.21 ± 0.64 mM is already in mM and normalizes to 6.21 mM. Kcat 13,100 ± 700 is printed in the column unit 10^-3 s^-1, so it normalizes to 13.1 s^-1 (multiply by 0.001). kcat/Km = 13.1 s^-1 / 6.21 mM = 2.109500805152979 s^-1 mM^-1, the quotient of the two printed cells of this same row. Table 1 also prints a separately fitted Kcat/Km cell for this row, 2120 ± 110 (10^-3 s^-1 mM^-1) = 2.12 s^-1 mM^-1. That printed cell is disclosed, not used: the exported kcat_over_km is the quotient of this row's own printed Kcat and Km cells (13.1 s^-1 / 6.21 mM = 2.109500805152979 s^-1 mM^-1), and that quotient lies inside the printed cell's own stated standard deviation (± 0.11 s^-1 mM^-1), so the two are the same quantity at the table's printing precision and no ratio correction is warranted.

raw_value_unit_evidence: Table 1 Comparison of kinetic constants of SerRs and AspRs | species/enzyme block: Crassostrea gigas | AspR | WT (SSS) | reaction row: d-Asp to l-Asp | columns: Km (mM); Kcat (10^-3 s^-1); Kcat/Km (10^-3 s^-1 mM^-1) | row as printed: (SSS)             d-Asp to l-Asp     (Uda et al. 2016)   6.21 ± 0.64       13,100 ± 700       2120 ± 110        1190 ± 180 | Km cell = 6.21 ± 0.64 mM; Kcat cell = 13,100 ± 700 (10^-3 s^-1); Kcat/Km cell = 2120 ± 110 (10^-3 s^-1 mM^-1).

row_label: Crassostrea gigas | AspR | WT (SSS) | d-Asp to l-Asp


substrate_name: L-Aspartate

substrate: L-Aspartate


column_label: Table label: Table 1 Comparison of kinetic constants of SerRs and AspRs. Species/enzyme block: Crassostrea gigas | AspR | WT (SSS). Reaction row: l-Asp to d-Asp. Km column cell = 4.75 ± 0.48; Kcat column cell = 8650 ± 850; Kcat/Km column cell = 1820 ± 60. Km, Kcat and Kcat/Km are read from the one printed row of this species/enzyme block, so they are one measurement; no value comes from another row, another block, or another paper.

normalized_value_unit_evidence: Km 4.75 ± 0.48 mM is already in mM and normalizes to 4.75 mM. Kcat 8650 ± 850 is printed in the column unit 10^-3 s^-1, so it normalizes to 8.65 s^-1 (multiply by 0.001). kcat/Km = 8.65 s^-1 / 4.75 mM = 1.8210526315789475 s^-1 mM^-1, the quotient of the two printed cells of this same row. Table 1 also prints a separately fitted Kcat/Km cell for this row, 1820 ± 60 (10^-3 s^-1 mM^-1) = 1.82 s^-1 mM^-1. That printed cell is disclosed, not used: the exported kcat_over_km is the quotient of this row's own printed Kcat and Km cells (8.65 s^-1 / 4.75 mM = 1.8210526315789475 s^-1 mM^-1), and that quotient lies inside the printed cell's own stated standard deviation (± 0.06 s^-1 mM^-1), so the two are the same quantity at the table's printing precision and no ratio correction is warranted.

raw_value_unit_evidence: Table 1 Comparison of kinetic constants of SerRs and AspRs | species/enzyme block: Crassostrea gigas | AspR | WT (SSS) | reaction row: l-Asp to d-Asp | columns: Km (mM); Kcat (10^-3 s^-1); Kcat/Km (10^-3 s^-1 mM^-1) | row as printed: gigas              WT                l-Asp to d-Asp     (Uda et al. 2016)   4.75 ± 0.48       8650 ± 850         1820 ± 60         517 ± 109 | Km cell = 4.75 ± 0.48 mM; Kcat cell = 8650 ± 850 (10^-3 s^-1); Kcat/Km cell = 1820 ± 60 (10^-3 s^-1 mM^-1).

row_label: Crassostrea gigas | AspR | WT (SSS) | l-Asp to d-Asp


enzyme_display_name: serine racemase

organism: Homo sapiens

substrate_name: L-serine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C113S with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

mutation_type: substitution

enzyme: serine racemase

substrate: L-serine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D318N to reconstruct the assayed variant sequence.


organism: Penaeus monodon

column_label: Table label: Table 1 Comparison of kinetic constants of SerRs and AspRs. Species/enzyme block: Penaeus monodon | AspR | WT (SSS). Reaction row: d-Asp to l-Asp. Km column cell = 9.86 ± 0.56; Kcat column cell = 27,600 ± 1000; Kcat/Km column cell = 2810 ± 60. Km, Kcat and Kcat/Km are read from the one printed row of this species/enzyme block, so they are one measurement; no value comes from another row, another block, or another paper.

normalized_value_unit_evidence: Km 9.86 ± 0.56 mM is already in mM and normalizes to 9.86 mM. Kcat 27,600 ± 1000 is printed in the column unit 10^-3 s^-1, so it normalizes to 27.6 s^-1 (multiply by 0.001). kcat/Km = 27.6 s^-1 / 9.86 mM = 2.799188640973631 s^-1 mM^-1, the quotient of the two printed cells of this same row. Table 1 also prints a separately fitted Kcat/Km cell for this row, 2810 ± 60 (10^-3 s^-1 mM^-1) = 2.81 s^-1 mM^-1. That printed cell is disclosed, not used: the exported kcat_over_km is the quotient of this row's own printed Kcat and Km cells (27.6 s^-1 / 9.86 mM = 2.799188640973631 s^-1 mM^-1), and that quotient lies inside the printed cell's own stated standard deviation (± 0.06 s^-1 mM^-1), so the two are the same quantity at the table's printing precision and no ratio correction is warranted.

raw_value_unit_evidence: Table 1 Comparison of kinetic constants of SerRs and AspRs | species/enzyme block: Penaeus monodon | AspR | WT (SSS) | reaction row: d-Asp to l-Asp | columns: Km (mM); Kcat (10^-3 s^-1); Kcat/Km (10^-3 s^-1 mM^-1) | row as printed: (SSS)             d-Asp to l-Asp     (Uda et al. 2016)   9.86 ± 0.56       27,600 ± 1000      2810 ± 60         1390 ± 50 | Km cell = 9.86 ± 0.56 mM; Kcat cell = 27,600 ± 1000 (10^-3 s^-1); Kcat/Km cell = 2810 ± 60 (10^-3 s^-1 mM^-1).

row_label: Penaeus monodon | AspR | WT (SSS) | d-Asp to l-Asp


column_label: Table label: Table 1 Comparison of kinetic constants of SerRs and AspRs. Species/enzyme block: Penaeus monodon | AspR | WT (SSS). Reaction row: l-Asp to d-Asp. Km column cell = 14.9 ± 1.6; Kcat column cell = 33,000 ± 2000; Kcat/Km column cell = 2230 ± 170. Km, Kcat and Kcat/Km are read from the one printed row of this species/enzyme block, so they are one measurement; no value comes from another row, another block, or another paper.

normalized_value_unit_evidence: Km 14.9 ± 1.6 mM is already in mM and normalizes to 14.9 mM. Kcat 33,000 ± 2000 is printed in the column unit 10^-3 s^-1, so it normalizes to 33.0 s^-1 (multiply by 0.001). kcat/Km = 33.0 s^-1 / 14.9 mM = 2.214765100671141 s^-1 mM^-1, the quotient of the two printed cells of this same row. Table 1 also prints a separately fitted Kcat/Km cell for this row, 2230 ± 170 (10^-3 s^-1 mM^-1) = 2.23 s^-1 mM^-1. That printed cell is disclosed, not used: the exported kcat_over_km is the quotient of this row's own printed Kcat and Km cells (33.0 s^-1 / 14.9 mM = 2.214765100671141 s^-1 mM^-1), and that quotient lies inside the printed cell's own stated standard deviation (± 0.17 s^-1 mM^-1), so the two are the same quantity at the table's printing precision and no ratio correction is warranted.

raw_value_unit_evidence: Table 1 Comparison of kinetic constants of SerRs and AspRs | species/enzyme block: Penaeus monodon | AspR | WT (SSS) | reaction row: l-Asp to d-Asp | columns: Km (mM); Kcat (10^-3 s^-1); Kcat/Km (10^-3 s^-1 mM^-1) | row as printed: don                WT                l-Asp to d-Asp     (Uda et al. 2016)   14.9 ± 1.6        33,000 ± 2000      2230 ± 170        1360 ± 100 | Km cell = 14.9 ± 1.6 mM; Kcat cell = 33,000 ± 2000 (10^-3 s^-1); Kcat/Km cell = 2230 ± 170 (10^-3 s^-1 mM^-1).

row_label: Penaeus monodon | AspR | WT (SSS) | l-Asp to d-Asp


organism: Mus musculus

substrate_name: D-serine

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9QZX7 and applied mutation signature H150S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 1 (Comparison of kinetic constants of SerRs and AspRs), column heads 'Species', 'Enzyme (150th-152nd residues)', 'Reaction', 'References', 'Km (mM)', 'Kcat (10^-3 s^-1)', 'Kcat/Km (10^-3 s^-1 mM^-1)' and 'v (umol/mg/h)'. The cited cell is the reaction row 'd-Ser to l-Ser' of the Mus musculus SerR H150S (SPN) block: Km = 37.4, Kcat = 516, Kcat/Km = 14.1, v = 9.56.

normalized_value_unit_evidence: Km: printed Table 1 cell 37.4 under the column head 'Km (mM)'; the printed unit is already mM, so no conversion is applied and the normalized value is 37.4 mM. kcat: printed Table 1 cell 516 under the column head 'Kcat (10^-3 s^-1)'; 516 x 10^-3 = 0.516 s^(-1). kcat/Km: printed Table 1 cell 14.1 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; the unit 10^-3 s^-1 mM^-1 is exactly M^-1 s^-1, so the same printed number reads 14.1 M^-1 s^-1, and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 14.1 x 0.001 = 0.0141 s^(-1)*mM^(-1). No min^-1, uM or M cell is involved in this row.

raw_value_unit_evidence: Table 1, Mus musculus SerR H150S (SPN) block, reaction row 'd-Ser to l-Ser': printed Km cell 37.4 under the column head 'Km (mM)'; printed Kcat cell 516 under the column head 'Kcat (10^-3 s^-1)'; printed Kcat/Km cell 14.1 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; printed v cell 9.56 under the column head 'v (umol/mg/h)'; References cell 'This work'.

row_label: Table 1, reaction row 'd-Ser to l-Ser' of the Mus musculus SerR H150S (SPN) block

table_label: Table 1: Comparison of kinetic constants of SerRs and AspRs (Amino Acids 2017, 49:1743-1754)

substrate: D-serine

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9QZX7 and applied mutation signature H150S/N152S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 1 (Comparison of kinetic constants of SerRs and AspRs), column heads 'Species', 'Enzyme (150th-152nd residues)', 'Reaction', 'References', 'Km (mM)', 'Kcat (10^-3 s^-1)', 'Kcat/Km (10^-3 s^-1 mM^-1)' and 'v (umol/mg/h)'. The cited cell is the reaction row 'd-Ser to l-Ser' of the Mus musculus SerR H150S/N152S (SPS) block: Km = 55.2, Kcat = 611, Kcat/Km = 11.6, v = 8.56.

normalized_value_unit_evidence: Km: printed Table 1 cell 55.2 under the column head 'Km (mM)'; the printed unit is already mM, so no conversion is applied and the normalized value is 55.2 mM. kcat: printed Table 1 cell 611 under the column head 'Kcat (10^-3 s^-1)'; 611 x 10^-3 = 0.611 s^(-1). kcat/Km: printed Table 1 cell 11.6 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; the unit 10^-3 s^-1 mM^-1 is exactly M^-1 s^-1, so the same printed number reads 11.6 M^-1 s^-1, and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 11.6 x 0.001 = 0.0116 s^(-1)*mM^(-1). No min^-1, uM or M cell is involved in this row.

raw_value_unit_evidence: Table 1, Mus musculus SerR H150S/N152S (SPS) block, reaction row 'd-Ser to l-Ser': printed Km cell 55.2 under the column head 'Km (mM)'; printed Kcat cell 611 under the column head 'Kcat (10^-3 s^-1)'; printed Kcat/Km cell 11.6 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; printed v cell 8.56 under the column head 'v (umol/mg/h)'; References cell 'This work'.

row_label: Table 1, reaction row 'd-Ser to l-Ser' of the Mus musculus SerR H150S/N152S (SPS) block


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9QZX7 and applied mutation signature H150S/P151S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 1 (Comparison of kinetic constants of SerRs and AspRs), column heads 'Species', 'Enzyme (150th-152nd residues)', 'Reaction', 'References', 'Km (mM)', 'Kcat (10^-3 s^-1)', 'Kcat/Km (10^-3 s^-1 mM^-1)' and 'v (umol/mg/h)'. The cited cell is the reaction row 'd-Ser to l-Ser' of the Mus musculus SerR H150S/P151S (SSN) block: Km = 44.1, Kcat = 376, Kcat/Km = 8.58, v = 6.27.

normalized_value_unit_evidence: Km: printed Table 1 cell 44.1 under the column head 'Km (mM)'; the printed unit is already mM, so no conversion is applied and the normalized value is 44.1 mM. kcat: printed Table 1 cell 376 under the column head 'Kcat (10^-3 s^-1)'; 376 x 10^-3 = 0.376 s^(-1). kcat/Km: printed Table 1 cell 8.58 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; the unit 10^-3 s^-1 mM^-1 is exactly M^-1 s^-1, so the same printed number reads 8.58 M^-1 s^-1, and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.58 x 0.001 = 0.00858 s^(-1)*mM^(-1). No min^-1, uM or M cell is involved in this row.

raw_value_unit_evidence: Table 1, Mus musculus SerR H150S/P151S (SSN) block, reaction row 'd-Ser to l-Ser': printed Km cell 44.1 under the column head 'Km (mM)'; printed Kcat cell 376 under the column head 'Kcat (10^-3 s^-1)'; printed Kcat/Km cell 8.58 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; printed v cell 6.27 under the column head 'v (umol/mg/h)'; References cell 'This work'.

row_label: Table 1, reaction row 'd-Ser to l-Ser' of the Mus musculus SerR H150S/P151S (SSN) block


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9QZX7 and applied mutation signature H150S/P151S/N152S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 1 (Comparison of kinetic constants of SerRs and AspRs), column heads 'Species', 'Enzyme (150th-152nd residues)', 'Reaction', 'References', 'Km (mM)', 'Kcat (10^-3 s^-1)', 'Kcat/Km (10^-3 s^-1 mM^-1)' and 'v (umol/mg/h)'. The cited cell is the reaction row 'd-Ser to l-Ser' of the Mus musculus SerR H150S/P151S/N152S (SSS) block: Km = 172, Kcat = 816, Kcat/Km = 4.77, v = 4.37.

normalized_value_unit_evidence: Km: printed Table 1 cell 172 under the column head 'Km (mM)'; the printed unit is already mM, so no conversion is applied and the normalized value is 172.0 mM. kcat: printed Table 1 cell 816 under the column head 'Kcat (10^-3 s^-1)'; 816 x 10^-3 = 0.816 s^(-1). kcat/Km: printed Table 1 cell 4.77 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; the unit 10^-3 s^-1 mM^-1 is exactly M^-1 s^-1, so the same printed number reads 4.77 M^-1 s^-1, and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.77 x 0.001 = 0.00477 s^(-1)*mM^(-1). No min^-1, uM or M cell is involved in this row.

raw_value_unit_evidence: Table 1, Mus musculus SerR H150S/P151S/N152S (SSS) block, reaction row 'd-Ser to l-Ser': printed Km cell 172 under the column head 'Km (mM)'; printed Kcat cell 816 under the column head 'Kcat (10^-3 s^-1)'; printed Kcat/Km cell 4.77 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; printed v cell 4.37 under the column head 'v (umol/mg/h)'; References cell 'This work'.

row_label: Table 1, reaction row 'd-Ser to l-Ser' of the Mus musculus SerR H150S/P151S/N152S (SSS) block


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9QZX7 and applied mutation signature N152S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 1 (Comparison of kinetic constants of SerRs and AspRs), column heads 'Species', 'Enzyme (150th-152nd residues)', 'Reaction', 'References', 'Km (mM)', 'Kcat (10^-3 s^-1)', 'Kcat/Km (10^-3 s^-1 mM^-1)' and 'v (umol/mg/h)'. The cited cell is the reaction row 'd-Ser to l-Ser' of the Mus musculus SerR N152S (HPS) block: Km = 45.1, Kcat = 2160, Kcat/Km = 47.8, v = 38.8.

normalized_value_unit_evidence: Km: printed Table 1 cell 45.1 under the column head 'Km (mM)'; the printed unit is already mM, so no conversion is applied and the normalized value is 45.1 mM. kcat: printed Table 1 cell 2160 under the column head 'Kcat (10^-3 s^-1)'; 2160 x 10^-3 = 2.16 s^(-1). kcat/Km: printed Table 1 cell 47.8 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; the unit 10^-3 s^-1 mM^-1 is exactly M^-1 s^-1, so the same printed number reads 47.8 M^-1 s^-1, and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 47.8 x 0.001 = 0.0478 s^(-1)*mM^(-1). No min^-1, uM or M cell is involved in this row.

raw_value_unit_evidence: Table 1, Mus musculus SerR N152S (HPS) block, reaction row 'd-Ser to l-Ser': printed Km cell 45.1 under the column head 'Km (mM)'; printed Kcat cell 2160 under the column head 'Kcat (10^-3 s^-1)'; printed Kcat/Km cell 47.8 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; printed v cell 38.8 under the column head 'v (umol/mg/h)'; References cell 'This work'.

row_label: Table 1, reaction row 'd-Ser to l-Ser' of the Mus musculus SerR N152S (HPS) block


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9QZX7 and applied mutation signature P151S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 1 (Comparison of kinetic constants of SerRs and AspRs), column heads 'Species', 'Enzyme (150th-152nd residues)', 'Reaction', 'References', 'Km (mM)', 'Kcat (10^-3 s^-1)', 'Kcat/Km (10^-3 s^-1 mM^-1)' and 'v (umol/mg/h)'. The cited cell is the reaction row 'd-Ser to l-Ser' of the Mus musculus SerR P151S (HSN) block: Km = 28.9, Kcat = 5680, Kcat/Km = 195, v = 124.

normalized_value_unit_evidence: Km: printed Table 1 cell 28.9 under the column head 'Km (mM)'; the printed unit is already mM, so no conversion is applied and the normalized value is 28.9 mM. kcat: printed Table 1 cell 5680 under the column head 'Kcat (10^-3 s^-1)'; 5680 x 10^-3 = 5.68 s^(-1). kcat/Km: printed Table 1 cell 195 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; the unit 10^-3 s^-1 mM^-1 is exactly M^-1 s^-1, so the same printed number reads 195 M^-1 s^-1, and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 195 x 0.001 = 0.195 s^(-1)*mM^(-1). No min^-1, uM or M cell is involved in this row.

raw_value_unit_evidence: Table 1, Mus musculus SerR P151S (HSN) block, reaction row 'd-Ser to l-Ser': printed Km cell 28.9 under the column head 'Km (mM)'; printed Kcat cell 5680 under the column head 'Kcat (10^-3 s^-1)'; printed Kcat/Km cell 195 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; printed v cell 124 under the column head 'v (umol/mg/h)'; References cell 'This work'.

row_label: Table 1, reaction row 'd-Ser to l-Ser' of the Mus musculus SerR P151S (HSN) block


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9QZX7 and applied mutation signature P151S/N152S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 1 (Comparison of kinetic constants of SerRs and AspRs), column heads 'Species', 'Enzyme (150th-152nd residues)', 'Reaction', 'References', 'Km (mM)', 'Kcat (10^-3 s^-1)', 'Kcat/Km (10^-3 s^-1 mM^-1)' and 'v (umol/mg/h)'. The cited cell is the reaction row 'd-Ser to l-Ser' of the Mus musculus SerR P151S/N152S (HSS) block: Km = 69.7, Kcat = 3740, Kcat/Km = 53.7, v = 45.2.

normalized_value_unit_evidence: Km: printed Table 1 cell 69.7 under the column head 'Km (mM)'; the printed unit is already mM, so no conversion is applied and the normalized value is 69.7 mM. kcat: printed Table 1 cell 3740 under the column head 'Kcat (10^-3 s^-1)'; 3740 x 10^-3 = 3.74 s^(-1). kcat/Km: printed Table 1 cell 53.7 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; the unit 10^-3 s^-1 mM^-1 is exactly M^-1 s^-1, so the same printed number reads 53.7 M^-1 s^-1, and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 53.7 x 0.001 = 0.0537 s^(-1)*mM^(-1). No min^-1, uM or M cell is involved in this row.

raw_value_unit_evidence: Table 1, Mus musculus SerR P151S/N152S (HSS) block, reaction row 'd-Ser to l-Ser': printed Km cell 69.7 under the column head 'Km (mM)'; printed Kcat cell 3740 under the column head 'Kcat (10^-3 s^-1)'; printed Kcat/Km cell 53.7 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; printed v cell 45.2 under the column head 'v (umol/mg/h)'; References cell 'This work'.

row_label: Table 1, reaction row 'd-Ser to l-Ser' of the Mus musculus SerR P151S/N152S (HSS) block


column_label: Table 1 row Mus musculus SerR WT (HPN); d-Ser to l-Ser; Km column raw cell 20.9 mM; Kcat column raw cell 840 x 10^-3 s^-1, normalized 0.84 s^-1; Kcat/Km column raw cell 40.2 x 10^-3 s^-1*mM^-1, normalized 0.0402 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=20.9 normalized_unit=mM; kcat normalized_value=0.84 normalized_unit=s^-1; kcat/Km normalized_value=0.0402 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=20.9 raw_unit=mM; Kcat raw_value=840 raw_unit=10^-3 s^-1; Kcat/Km raw_value=40.2 raw_unit=10^-3 s^-1*mM^-1

table_label: Table 1. Comparison of kinetic constants of SerRs and AspRs


column_label: Table 1 (Comparison of kinetic constants of SerRs and AspRs), column heads 'Species', 'Enzyme (150th-152nd residues)', 'Reaction', 'References', 'Km (mM)', 'Kcat (10^-3 s^-1)', 'Kcat/Km (10^-3 s^-1 mM^-1)' and 'v (umol/mg/h)'. The cited cell is the reaction row 'l-Ser to d-Ser' of the Mus musculus SerR H150S (SPN) block: Km = 46.4, Kcat = 605, Kcat/Km = 13.2, v = 9.78.

normalized_value_unit_evidence: Km: printed Table 1 cell 46.4 under the column head 'Km (mM)'; the printed unit is already mM, so no conversion is applied and the normalized value is 46.4 mM. kcat: printed Table 1 cell 605 under the column head 'Kcat (10^-3 s^-1)'; 605 x 10^-3 = 0.605 s^(-1). kcat/Km: printed Table 1 cell 13.2 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; the unit 10^-3 s^-1 mM^-1 is exactly M^-1 s^-1, so the same printed number reads 13.2 M^-1 s^-1, and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 13.2 x 0.001 = 0.0132 s^(-1)*mM^(-1). No min^-1, uM or M cell is involved in this row.

raw_value_unit_evidence: Table 1, Mus musculus SerR H150S (SPN) block, reaction row 'l-Ser to d-Ser': printed Km cell 46.4 under the column head 'Km (mM)'; printed Kcat cell 605 under the column head 'Kcat (10^-3 s^-1)'; printed Kcat/Km cell 13.2 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; printed v cell 9.78 under the column head 'v (umol/mg/h)'; References cell 'This work'.

row_label: Table 1, reaction row 'l-Ser to d-Ser' of the Mus musculus SerR H150S (SPN) block


column_label: Table 1 (Comparison of kinetic constants of SerRs and AspRs), column heads 'Species', 'Enzyme (150th-152nd residues)', 'Reaction', 'References', 'Km (mM)', 'Kcat (10^-3 s^-1)', 'Kcat/Km (10^-3 s^-1 mM^-1)' and 'v (umol/mg/h)'. The cited cell is the reaction row 'l-Ser to d-Ser' of the Mus musculus SerR H150S/N152S (SPS) block: Km = 69.9, Kcat = 824, Kcat/Km = 12.0, v = 10.0.

normalized_value_unit_evidence: Km: printed Table 1 cell 69.9 under the column head 'Km (mM)'; the printed unit is already mM, so no conversion is applied and the normalized value is 69.9 mM. kcat: printed Table 1 cell 824 under the column head 'Kcat (10^-3 s^-1)'; 824 x 10^-3 = 0.824 s^(-1). kcat/Km: printed Table 1 cell 12.0 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; the unit 10^-3 s^-1 mM^-1 is exactly M^-1 s^-1, so the same printed number reads 12.0 M^-1 s^-1, and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 12.0 x 0.001 = 0.012 s^(-1)*mM^(-1). No min^-1, uM or M cell is involved in this row.

raw_value_unit_evidence: Table 1, Mus musculus SerR H150S/N152S (SPS) block, reaction row 'l-Ser to d-Ser': printed Km cell 69.9 under the column head 'Km (mM)'; printed Kcat cell 824 under the column head 'Kcat (10^-3 s^-1)'; printed Kcat/Km cell 12.0 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; printed v cell 10.0 under the column head 'v (umol/mg/h)'; References cell 'This work'.

row_label: Table 1, reaction row 'l-Ser to d-Ser' of the Mus musculus SerR H150S/N152S (SPS) block


enzyme_display_name: 2-aminohexano-6-lactam racemase

organism: Achromobacter obae

substrate_name: L-2-aminobutyric acid amide

source_db: brenda

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

assay_conditions_summary: pH 7; buffer pH 7

column_label: ACS full text lists K_m values for L-ACL and D- and L-2-aminobutyric acid amide and D- and L-alanine amide as 10, 3.5, 1.1, 3.4, and 2.5 mM respectively; the third value maps to L-2-aminobutyric acid amide.

raw_value_unit_evidence: Km raw_value=1.1 raw_unit=mM

row_label: ACL racemase / L-2-aminobutyric acid amide

table_label: ACS full text PMID 15913357 ACL racemase substrate specificity prose

enzyme: 2-aminohexano-6-lactam racemase

substrate: L-2-aminobutyric acid amide

source: brenda


substrate_name: L-Ala

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

substrate: L-Ala


substrate_name: D-alpha-Amino-epsilon-caprolactam

substrate: D-alpha-Amino-epsilon-caprolactam


enzyme_display_name: nocardicin-A epimerase

organism: Nocardia uniformis

substrate_name: nocardicin A

sequence_source: multiple

proof_lines: kcat is 0.59 sec(-1) with isonocardicin A as substrate. kcat is 0.35 sec(-1) with nocardicin A as substrate.

source_databases_merged: brenda uniprot

enzyme: nocardicin-A epimerase

substrate: nocardicin A


organism: Anadara broughtonii

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

assay_conditions_summary: pH 8


enzyme_display_name: isopenicillin-N epimerase

organism: Streptomyces clavuligerus

substrate_name: pyridoxal 5'-phosphate

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

enzyme: isopenicillin-N epimerase

substrate: pyridoxal 5'-phosphate


substrate_name: isopenicillin N

column_label: Results text reports the epimerase had a Km of 0.30 mM for IPN.

raw_value_unit_evidence: Km raw_value=0.30 mM raw_unit=mM

row_label: Purified isopenicillin N epimerase / isopenicillin N substrate

table_label: Results text near Fig. 2, PMID 2804141 PDF

substrate: isopenicillin N


organism: Schizosaccharomyces pombe

proof_lines: pH and temperature not specified in the publication


organism: Aplysia californica


organism: Pyrococcus horikoshii

substrate_name: L-aspartate

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

proof_lines:
pH 8.0, 70°C
Raw SKiD Env: Temp=70°C, pH=8

source_databases_merged: brenda skid uniprot

substrate: L-aspartate


organism: Dictyostelium discoideum


enzyme_display_name: O-ureido-serine racemase

organism: Streptomyces lavendulae subsp. lavendulae

substrate_name: O-ureido-D-serine

enzyme: O-ureido-serine racemase

substrate: O-ureido-D-serine


substrate_name: O-ureido-L-serine

substrate: O-ureido-L-serine


organism: Roseobacter litoralis


organism: Oryza sativa subsp. japonica

substrate_name: L-serine (racemase activity)

substrate: L-serine (racemase activity)


organism: Arabidopsis thaliana


organism: Escherichia coli

substrate_name: L-Ala-D-Asp

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NADH

column_label: Table label: Table 2:  Kinetic Parameters for the Reactions Catalyzed by YcjG and YkfB. Row: l-Ala-d-Asp. Enzyme column group: YcjG (E. coli). Columns read: KM (M) cell (1.9 ± 0.7) × 10-4, kcat (s-1) cell 17 ± 2.7, kcat/KM (M-1 s-1) cell 8.9 × 104. KM (1.9 ± 0.7) × 10-4 M normalizes to 0.19 mM and equals the exported km; kcat 17 ± 2.7 s^-1 normalizes to 17 s^-1 and equals the exported kcat; the exported kcat_over_km 89.47368421052632 s^-1 mM^-1 is the exact quotient of those two printed cells and agrees with the printed kcat/KM cell 8.9 × 104 M-1 s-1 at its two-significant-figure precision.

normalized_value_unit_evidence: YcjG (E. coli) columns of row l-Ala-d-Asp: KM (1.9 ± 0.7) × 10-4 M = 0.19 mM; kcat 17 ± 2.7 s^-1 = 17 s^-1; kcat/KM taken as the quotient of those two printed cells, 17 s^-1 / 0.19 mM = 89.47368421052632 s^-1 mM^-1, which the table prints rounded to two significant figures as 8.9 × 104 M-1 s-1.

raw_value_unit_evidence: Table 2:  Kinetic Parameters for the Reactions Catalyzed by YcjG and YkfB | column header: substrate	KM (M)	kcat (s-1)	kcat/KM (M-1 s-1)	KI (M)	KM (M)	kcat (s-1)	kcat/KM (M-1 s-1)	KI (M) | row: l-Ala-d-Asp	(1.9 ± 0.7) × 10-4	17 ± 2.7	8.9 × 104	8.2 × 10-4	(2.8 ± 1.2) × 10-5	0.053 ± 0.009	1.9 × 103	1.1 × 10-3

row_label: YcjG (E. coli) | l-Ala-d-Asp

substrate: L-Ala-D-Asp


substrate_name: L-Ala-D-Gln

column_label: Table label: Table 2:  Kinetic Parameters for the Reactions Catalyzed by YcjG and YkfB. Row: l-Ala-d-Gln. Enzyme column group: YcjG (E. coli). Columns read: KM (M) cell (1.8 ± 0.2) × 10-3, kcat (s-1) cell 3.3 ± 0.1, kcat/KM (M-1 s-1) cell 1.8 × 103. KM (1.8 ± 0.2) × 10-3 M normalizes to 1.8 mM and equals the exported km; kcat 3.3 ± 0.1 s^-1 normalizes to 3.3 s^-1 and equals the exported kcat; the exported kcat_over_km 1.8333333333333333 s^-1 mM^-1 is the exact quotient of those two printed cells and agrees with the printed kcat/KM cell 1.8 × 103 M-1 s-1 at its two-significant-figure precision.

normalized_value_unit_evidence: YcjG (E. coli) columns of row l-Ala-d-Gln: KM (1.8 ± 0.2) × 10-3 M = 1.8 mM; kcat 3.3 ± 0.1 s^-1 = 3.3 s^-1; kcat/KM taken as the quotient of those two printed cells, 3.3 s^-1 / 1.8 mM = 1.8333333333333333 s^-1 mM^-1, which the table prints rounded to two significant figures as 1.8 × 103 M-1 s-1.

raw_value_unit_evidence: Table 2:  Kinetic Parameters for the Reactions Catalyzed by YcjG and YkfB | column header: substrate	KM (M)	kcat (s-1)	kcat/KM (M-1 s-1)	KI (M)	KM (M)	kcat (s-1)	kcat/KM (M-1 s-1)	KI (M) | row: l-Ala-d-Gln	(1.8 ± 0.2) × 10-3	3.3 ± 0.1	1.8 × 103	−	−	−	−	−

row_label: YcjG (E. coli) | l-Ala-d-Gln

substrate: L-Ala-D-Gln


substrate_name: L-Ala-D-Glu

column_label: Table label: Table 2:  Kinetic Parameters for the Reactions Catalyzed by YcjG and YkfB. Row: l-Ala-d-Glu. Enzyme column group: YcjG (E. coli). Columns read: KM (M) cell (1.3 ± 0.3) × 10-4, kcat (s-1) cell 10 ± 0.4, kcat/KM (M-1 s-1) cell 7.7 × 104. KM (1.3 ± 0.3) × 10-4 M normalizes to 0.13 mM and equals the exported km; kcat 10 ± 0.4 s^-1 normalizes to 10 s^-1 and equals the exported kcat; the exported kcat_over_km 76.92307692307692 s^-1 mM^-1 is the exact quotient of those two printed cells and agrees with the printed kcat/KM cell 7.7 × 104 M-1 s-1 at its two-significant-figure precision.

normalized_value_unit_evidence: YcjG (E. coli) columns of row l-Ala-d-Glu: KM (1.3 ± 0.3) × 10-4 M = 0.13 mM; kcat 10 ± 0.4 s^-1 = 10 s^-1; kcat/KM taken as the quotient of those two printed cells, 10 s^-1 / 0.13 mM = 76.92307692307692 s^-1 mM^-1, which the table prints rounded to two significant figures as 7.7 × 104 M-1 s-1.

raw_value_unit_evidence: Table 2:  Kinetic Parameters for the Reactions Catalyzed by YcjG and YkfB | column header: substrate	KM (M)	kcat (s-1)	kcat/KM (M-1 s-1)	KI (M)	KM (M)	kcat (s-1)	kcat/KM (M-1 s-1)	KI (M) | row: l-Ala-d-Glu	(1.3 ± 0.3) × 10-4	10 ± 0.4	7.7 × 104	−	(3.2 ± 1.1) × 10-4	15 ± 2.7	4.7 × 104	2.0 × 10-3

row_label: YcjG (E. coli) | l-Ala-d-Glu

substrate: L-Ala-D-Glu


substrate_name: L-Ala-D-Met

column_label: Table label: Table 2:  Kinetic Parameters for the Reactions Catalyzed by YcjG and YkfB. Row: l-Ala-d-Met. Enzyme column group: YcjG (E. coli). Columns read: KM (M) cell (6.9 ± 0.4) × 10-4, kcat (s-1) cell 1.9 ± 0.1, kcat/KM (M-1 s-1) cell 2.8 × 103. KM (6.9 ± 0.4) × 10-4 M normalizes to 0.69 mM and equals the exported km; kcat 1.9 ± 0.1 s^-1 normalizes to 1.9 s^-1 and equals the exported kcat; the exported kcat_over_km 2.7536231884057973 s^-1 mM^-1 is the exact quotient of those two printed cells and agrees with the printed kcat/KM cell 2.8 × 103 M-1 s-1 at its two-significant-figure precision.

normalized_value_unit_evidence: YcjG (E. coli) columns of row l-Ala-d-Met: KM (6.9 ± 0.4) × 10-4 M = 0.69 mM; kcat 1.9 ± 0.1 s^-1 = 1.9 s^-1; kcat/KM taken as the quotient of those two printed cells, 1.9 s^-1 / 0.69 mM = 2.7536231884057973 s^-1 mM^-1, which the table prints rounded to two significant figures as 2.8 × 103 M-1 s-1.

raw_value_unit_evidence: Table 2:  Kinetic Parameters for the Reactions Catalyzed by YcjG and YkfB | column header: substrate	KM (M)	kcat (s-1)	kcat/KM (M-1 s-1)	KI (M)	KM (M)	kcat (s-1)	kcat/KM (M-1 s-1)	KI (M) | row: l-Ala-d-Met	(6.9 ± 0.4) × 10-4	1.9 ± 0.1	2.8 × 103	2.1 × 10-3	(5.1 ± 1.7) × 10-4	1.1 ± 0.1	2.2 × 103	−

row_label: YcjG (E. coli) | l-Ala-d-Met

substrate: L-Ala-D-Met


enzyme_display_name: 4-hydroxyproline epimerase

organism: Labrenzia aggregata

assay_conditions_summary: pH 8; 298.15 K; buffer pH 8

column_label: Official eLife HTML Table 2 row SIAM614_28492 / A0NXQ7 / 4HypE; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.008

normalized_value_unit_evidence: kcat normalized_value=55 normalized_unit=s^-1; Km normalized_value=3.2 normalized_unit=mM; kcat/KM normalized_value=17 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=55 +/- 3 raw_unit=s^-1; Km raw_value=3.2 +/- 0.5 raw_unit=mM; kcat/KM raw_value=17000 raw_unit=M^-1 s^-1

table_label: Table 2. Kinetic constants for 3/4HypE and t3HypD activities of the screened PRS targets

enzyme: 4-hydroxyproline epimerase


organism: Homo sapiens

source_db: skid

source_databases_merged: skid uniprot

source: skid


organism: Rattus norvegicus


organism: Labrenzia alexandrii

column_label: Official eLife HTML Table 2 row SADFL11_2813 / B9R4E3 / 4HypE; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.008

normalized_value_unit_evidence: kcat normalized_value=67 normalized_unit=s^-1; Km normalized_value=4.1 normalized_unit=mM; kcat/KM normalized_value=16 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=67 +/- 5 raw_unit=s^-1; Km raw_value=4.1 +/- 0.8 raw_unit=mM; kcat/KM raw_value=16000 raw_unit=M^-1 s^-1


organism: Caenorhabditis elegans


organism: Chromohalobacter salexigens

row_label: Csal_2339 / Q1QV19 / 4HypE

table_label: Table 2


organism: Paracoccus denitrificans

column_label: Official eLife HTML Table 2 row Pden_4859 / A1BBM5 / 4HypE; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.008

normalized_value_unit_evidence: kcat normalized_value=16 normalized_unit=s^-1; Km normalized_value=25 normalized_unit=mM; kcat/KM normalized_value=0.63 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=16 +/- 2 raw_unit=s^-1; Km raw_value=25 +/- 5 raw_unit=mM; kcat/KM raw_value=630 raw_unit=M^-1 s^-1

row_label: Pden_4859 / A1BBM5 / 4HypE


organism: Rhizobium meliloti

column_label: Table 2 (PDF page 9 of 32); cluster 3; row group `SM_b20270 | Q92WR9`; Function sub-row `4HypE`; columns kcat [s-1] = `0.089`, KM [mM] = `6.3`, kcat/KM[M-1s-1] = `14`.

normalized_value_unit_evidence: kcat: printed cell 0.089 s^-1 -> 0.089 s^(-1); the export holds 0.089 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 6.3 mM -> 6.3 mM; the export holds 6.3 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 14 M^-1 s^-1 converted as 14 / 1000 = 0.014 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 0.014126984126984127 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `SM_b20270 | Q92WR9`, sub-row `4HypE`: kcat = 0.089 s^-1; KM = 6.3 mM; kcat/KM = 14 M^-1 s^-1.

row_label: SM_b20270 | Q92WR9 / 4HypE (Table 2 cluster 3)


verification_status: unverified

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

status: unverified


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

proof_lines: pH 8.0, 37°C, recombinant wild-type enzyme


organism: Bacillus subtilis


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


organism: Shewanella loihica

column_label: Official eLife HTML Table 2 row Shew_2363 / A3QFI1 / 4HypE; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.008

normalized_value_unit_evidence: kcat normalized_value=50 normalized_unit=s^-1; Km normalized_value=12 normalized_unit=mM; kcat/KM normalized_value=4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=50 +/- 6 raw_unit=s^-1; Km raw_value=12 +/- 3 raw_unit=mM; kcat/KM raw_value=4000 raw_unit=M^-1 s^-1

row_label: Shew_2363 / A3QFI1 / 4HypE


organism: Mus musculus

proof_lines: pH 8.0, 30°C, recombinant mutant H150S/P151S/N152S


proof_lines: pH 8.0, 30°C, recombinant mutant H150S/P151S


proof_lines: pH 8.0, 30°C, recombinant mutant P151S/N152S


proof_lines: pH 8.0, 30°C, recombinant mutant H150S/N152S


organism: Microcystis aeruginosa


enzyme_display_name: L-dopachrome isomerase

substrate_name: dopachrome

enzyme: L-dopachrome isomerase

substrate: dopachrome


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Magallana gigas

substrate_name: L-serine

proof_lines: pH 8.0, 30°C, recombinant wild-type enzyme

substrate: L-serine


substrate_name: D-serine

proof_lines: pH 8.0, 30°C, recombinant mutant P150S/P151S/Y152S

substrate: D-serine


enzyme_display_name: protoporphyrin ferrochelatase

enzyme: protoporphyrin ferrochelatase


substrate_name: protoporphyrin

substrate: protoporphyrin


enzyme_display_name: phosphoenolpyruvate mutase

organism: Mytilus edulis

substrate_name: Phosphonopyruvate

enzyme: phosphoenolpyruvate mutase

substrate: Phosphonopyruvate


enzyme_display_name: alanine racemase

organism: Mycobacterium tuberculosis

substrate_name: L-alanine

enzyme: alanine racemase

substrate: L-alanine


enzyme_display_name: glutamate racemase

substrate_name: D-glutamate

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

enzyme: glutamate racemase

substrate: D-glutamate


enzyme_display_name: UniProt P11444

organism: Pseudomonas putida

substrate_name: (S)-Mandelate

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=7.5

enzyme: UniProt P11444

substrate: (S)-Mandelate


substrate_name: (R)-mandelamide

substrate: (R)-mandelamide


enzyme_display_name: UDP-galactopyranose mutase

substrate_name: UDP-alpha-D-galactofuranose

enzyme: UDP-galactopyranose mutase

substrate: UDP-alpha-D-galactofuranose


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


substrate_name: L-serine O-sulfate

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: pH 8.0, 37°C, presence of 1 mM ATP, elimination reaction

substrate: L-serine O-sulfate


enzyme_display_name: lactoylglutathione lyase

organism: Neisseria meningitidis

substrate_name: methylglyoxal

smiles: CC(=O)C=O

assay_conditions_summary: pH 7

proof_lines:
presence of Co2+, pH 7.0
presence of Ni2+, pH 7.0

enzyme: lactoylglutathione lyase

substrate: methylglyoxal


substrate_name: (R)-S-lactoylglutathione

proof_lines:
pH 7.0, 0.5 mM CoCl2
pH 7.0, 0.5 mM NiCl2

substrate: (R)-S-lactoylglutathione


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

proof_lines:
mutant N122A, pH 7.5, 25°C
mutant enzyme N122A, at pH 7.5 and 25°C
mutant N122A, 25°C, pH 7.5


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K120A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

proof_lines:
mutant K120A, pH 7.5, 25°C
mutant enzyme K120A, at pH 7.5 and 25°C


enzyme_display_name: phosphomannomutase

organism: Oryctolagus cuniculus

substrate_name: D-Glucose 1-phosphate

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

enzyme: phosphomannomutase

substrate: D-Glucose 1-phosphate


substrate_name: mannose 6-phosphate

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

substrate: mannose 6-phosphate


proof_lines: wild type enzyme, at pH 8.0, temperature not specified in the publication


enzyme_display_name: lactate racemase

organism: Latilactobacillus curvatus

substrate_name: D-lactate

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

enzyme: lactate racemase

substrate: D-lactate


substrate_name: L-lactate

substrate: L-lactate


assay_conditions_summary: pH 7.4; cofactor ATP

proof_lines: wild-type, racemization, presence of ATP, pH 7.4, 37°C


proof_lines: mutant Q155D, racemization, pH 7.4, 37°C

proof_lines: mutant Q155D, racemization, presence of ATP, pH 7.4, 37°C

proof_lines: mutant Q155D, presence of ATP, pH 7.4, 37°C


enzyme_display_name: adenylate cyclase

substrate_name: ATP

assay_conditions_summary: 303.15 K; cofactor ATP

proof_lines: cortical adenylyl cyclase, in the presence of 7 mM Mg2+, at 30°C, pH not specified in the publication

proof_lines: medulla adenylyl cyclase, in the presence of 7 mM Mg2+, at 30°C, pH not specified in the publication

enzyme: adenylate cyclase

substrate: ATP


substrate_name: Unknown

proof_lines: cortical adenylyl cyclase, in the presence of 7 mM Mn2+, at 30°C, pH not specified in the publication

proof_lines: medulla adenylyl cyclase, in the presence of 7 mM Mn2+, at 30°C, pH not specified in the publication

substrate: Unknown


organism: Latilactobacillus sakei


enzyme_display_name: histidine racemase

organism: Leuconostoc mesenteroides subsp. mesenteroides

substrate_name: L-histidine

enzyme: histidine racemase

substrate: L-histidine


enzyme_display_name: 4-hydroxyproline betaine 2-epimerase

organism: Salipiger bermudensis

substrate_name: L-proline betaine

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

proof_lines: kcat is 330 sec(-1) with trans-4-hydroxy-L-proline betaine as substrate and 5.3 sec(-1) with L-proline betaine as substrate.

enzyme: 4-hydroxyproline betaine 2-epimerase

substrate: L-proline betaine


substrate_name: trans-4-hydroxy-L-proline betaine

substrate: trans-4-hydroxy-L-proline betaine


organism: Paracoccus denitrificans (strain Pd 1222)

proof_lines: kcat is 110 sec(-1) with trans-4-hydroxy-L-proline betaine as substrate (PubMed:24056934). kcat is 68 sec(-1) with L-proline betaine as substrate (PubMed:24056934). kcat is 28 sec(-1) with D-proline betaine as substrate (PubMed:24520058).


enzyme_display_name: isoleucine 2-epimerase

organism: Arabidopsis thaliana

substrate_name: L-isoleucine

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

proof_lines: recombinant His-tagged enzyme, pH 8.0, 22°C

enzyme: isoleucine 2-epimerase

substrate: L-isoleucine


organism: Lentilactobacillus buchneri

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D222N with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant D222N, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D222A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant D222A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y142F to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant Y142F, pH and temperature not specified in the publication


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

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


proof_lines:
pH 5.5, 37°C
Raw SKiD Env: Temp=37°C, pH=5.5
Raw SKiD Env: Temp=-----, pH=-----


organism: Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032)

proof_lines: kcat is 986 sec(-1) for conversion of L-lactate to D-lactate. kcat is 551 sec(-1) for conversion of D-lactate to L-lactate.


enzyme_display_name: mandelate racemase

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: mandelate racemase


enzyme_display_name: 3-hydroxybutyryl-CoA epimerase

organism: Escherichia coli (strain K12)

substrate_name: L-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA hydratase activity)

assay_conditions_summary: cofactor CoA

enzyme: 3-hydroxybutyryl-CoA epimerase


organism: Fusobacterium nucleatum subsp. nucleatum (strain ATCC 23726 / VPI 4351)

proof_lines: kcat is 42 sec(-1) with L-histidine as substrate. kcat is 64 sec(-1) with D-histidine as substrate.


proof_lines: kcat is 502 sec(-1) with L-isoleucine as substrate. kcat is 939 sec(-1) with D-allo-isoleucine as substrate.


organism: Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355)

substrate_name: L,L-lanthionine

proof_lines: kcat is 74 sec(-1) with L-histidine as substrate (PubMed:39424140). kcat is 250 sec(-1) with D-histidine as substrate (PubMed:39424140). kcat is 0.07 sec(-1) with L,L-lanthionine as substrate (PubMed:37329940).

substrate: L,L-lanthionine


organism: Leuconostoc mesenteroides subsp. sake


organism: Lactiplantibacillus plantarum

substrate_name: (R)-lactate

proof_lines: pH and temperature not specified in the publication

proof_lines: kcat is 4745 sec(-1) for conversion of L-lactate to D-lactate. kcat is 1333 sec(-1) for conversion of D-lactate to L-lactate.

substrate: (R)-lactate


organism: Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)


organism: Pseudomonas putida

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11444 and applied mutation signature V22I to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer Tris-HCl

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(R)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I': Km = 15.51 mM, kcat = 1.82 s^(-1), kcat/Km = 117.82 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 15.51 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 15.51 mM. kcat: printed Table 2 cell 1.82 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 1.82 s^(-1). kcat/Km: printed Table 2 cell 117.82 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 117.82 / 1000 = 0.11782 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (R)-2-CMA half of the printed line for enzyme form V22I: Km = 15.51 mM; kcat = 1.82 s^(-1); printed kcat/Km = 117.82 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11444 and applied mutation signature V22I/V29I to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(R)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I/V29I': Km = 15.10 mM, kcat = 2.60 s^(-1), kcat/Km = 172.25 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 15.10 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 15.1 mM. kcat: printed Table 2 cell 2.60 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 2.6 s^(-1). kcat/Km: printed Table 2 cell 172.25 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 172.25 / 1000 = 0.17225 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (R)-2-CMA half of the printed line for enzyme form V22I/V29I: Km = 15.10 mM; kcat = 2.60 s^(-1); printed kcat/Km = 172.25 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11444 and applied mutation signature V22I/V29I/Y54F to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(R)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I/V29I/Y54F': Km = 14.52 mM, kcat = 2.57 s^(-1), kcat/Km = 176.70 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 14.52 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 14.52 mM. kcat: printed Table 2 cell 2.57 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 2.57 s^(-1). kcat/Km: printed Table 2 cell 176.70 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 176.70 / 1000 = 0.1767 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (R)-2-CMA half of the printed line for enzyme form V22I/V29I/Y54F: Km = 14.52 mM; kcat = 2.57 s^(-1); printed kcat/Km = 176.70 M^-1 s^-1.


sequence_variant_note: Mutation signature V22I/Y45F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11444 and applied mutation signature V29I to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(R)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V29I': Km = 11.99 mM, kcat = 1.45 s^(-1), kcat/Km = 121.37 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 11.99 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 11.99 mM. kcat: printed Table 2 cell 1.45 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 1.45 s^(-1). kcat/Km: printed Table 2 cell 121.37 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 121.37 / 1000 = 0.12137 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (R)-2-CMA half of the printed line for enzyme form V29I: Km = 11.99 mM; kcat = 1.45 s^(-1); printed kcat/Km = 121.37 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V29I/Y45F with inferred residue-numbering offset -25 to reconstruct the assayed variant sequence.


column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(R)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'WT': Km = 14.82 mM, kcat = 0.90 s^(-1), kcat/Km = 60.74 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 14.82 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 14.82 mM. kcat: printed Table 2 cell 0.90 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 0.9 s^(-1). kcat/Km: printed Table 2 cell 60.74 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 60.74 / 1000 = 0.06074 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (R)-2-CMA half of the printed line for enzyme form WT: Km = 14.82 mM; kcat = 0.90 s^(-1); printed kcat/Km = 60.74 M^-1 s^-1.


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


column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(S)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I': Km = 19.91 mM, kcat = 2.47 s^(-1), kcat/Km = 123.97 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 19.91 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 19.91 mM. kcat: printed Table 2 cell 2.47 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 2.47 s^(-1). kcat/Km: printed Table 2 cell 123.97 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 123.97 / 1000 = 0.12397 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (S)-2-CMA half of the printed line for enzyme form V22I: Km = 19.91 mM; kcat = 2.47 s^(-1); printed kcat/Km = 123.97 M^-1 s^-1.


column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(S)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I/V29I': Km = 13.74 mM, kcat = 2.35 s^(-1), kcat/Km = 159.31 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 13.74 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 13.74 mM. kcat: printed Table 2 cell 2.35 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 2.35 s^(-1). kcat/Km: printed Table 2 cell 159.31 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 159.31 / 1000 = 0.15931 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (S)-2-CMA half of the printed line for enzyme form V22I/V29I: Km = 13.74 mM; kcat = 2.35 s^(-1); printed kcat/Km = 159.31 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V26S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V29L to reconstruct the assayed variant sequence.


column_label: Table 1: Kinetic parameters of the wild type and mutants towards R-3-chloromandelic acid, R-mandelamide and R-2-naphthylglycolate (Enzyme and Microbial Technology 55 (2014) 121-127); row 'WT' of the 'R-3-Chloromandelic acid' section; column 'Km (mM)' = 1.89; column 'kcat (s^-1)' = 4.69 x 10^2; column 'kcat/Km (M^-1 s^-1)' = 2.49 x 10^5

normalized_value_unit_evidence: Km: printed Table 1 cell 1.89 mM; the cell is already in mM, so no unit conversion applies; 1.89 mM. kcat: printed Table 1 cell 4.69 x 10^2 s^-1, which is 469.0 s^-1; the cell is already in s^-1, so no unit conversion applies (this paper prints no min^-1 kinetic cell). kcat/Km: printed Table 1 cell 2.49 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.49 x 10^5 / 1000 = 249.0 s^-1 mM^-1. The printed efficiency cell is the paper's own fitted primary value, so this pass carries 249.0 s^-1 mM^-1 for kcat/Km.

raw_value_unit_evidence: Table 1, section 'R-3-Chloromandelic acid', row 'WT': Km cell 1.89 mM; kcat cell 4.69 x 10^2 s^-1; printed kcat/Km cell 2.49 x 10^5 M^-1 s^-1.

row_label: Table 1, section 'R-3-Chloromandelic acid', printed row label 'WT'


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y54A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y54F with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y54I with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y54L with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y54V with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


substrate_name: (R)-mandelamide

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V26L to reconstruct the assayed variant sequence.

substrate: (R)-mandelamide


column_label: Table 1: Kinetic parameters of the wild type and mutants towards R-3-chloromandelic acid, R-mandelamide and R-2-naphthylglycolate (Enzyme and Microbial Technology 55 (2014) 121-127); row 'WT' of the 'R-Mandelamide' section; column 'Km (mM)' = 1.13; column 'kcat (s^-1)' = 11.03; column 'kcat/Km (M^-1 s^-1)' = 9.79 x 10^3

normalized_value_unit_evidence: Km: printed Table 1 cell 1.13 mM; the cell is already in mM, so no unit conversion applies; 1.13 mM. kcat: printed Table 1 cell 11.03 s^-1, which is 11.03 s^-1; the cell is already in s^-1, so no unit conversion applies (this paper prints no min^-1 kinetic cell). kcat/Km: printed Table 1 cell 9.79 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9.79 x 10^3 / 1000 = 9.79 s^-1 mM^-1. The printed efficiency cell is the paper's own fitted primary value, so this pass carries 9.79 s^-1 mM^-1 for kcat/Km.

raw_value_unit_evidence: Table 1, section 'R-Mandelamide', row 'WT': Km cell 1.13 mM; kcat cell 11.03 s^-1; printed kcat/Km cell 9.79 x 10^3 M^-1 s^-1.

row_label: Table 1, section 'R-Mandelamide', printed row label 'WT'


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V22I to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L319F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V22L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V26I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V26I/Y54I with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V26I/Y54V with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


substrate_name: crotonyl-CoA (for enoyl-CoA hydratase activity)


substrate_name: acetoacetyl-CoA (for 3-hydroxyacyl-CoA dehydrogenase activity)


substrate_name: NADH (for 3-hydroxyacyl-CoA dehydrogenase activity)

assay_conditions_summary: cofactor NADH


enzyme_display_name: 4-hydroxyproline epimerase

organism: Streptosporangium roseum

column_label: Table 2 (PDF page 10 of 32); cluster 11; row group `Sros_6004 | D2AV87`; Function sub-row `4HypE`; columns kcat [s-1] = `14`, KM [mM] = `7.8`, kcat/KM[M-1s-1] = `1800`.

normalized_value_unit_evidence: kcat: printed cell 14 s^-1 -> 14.0 s^(-1); the export holds 14.0 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 7.8 mM -> 7.8 mM; the export holds 7.8 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 1800 M^-1 s^-1 converted as 1800 / 1000 = 1.8 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 1.794871794871795 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `Sros_6004 | D2AV87`, sub-row `4HypE`: kcat = 14 s^-1; KM = 7.8 mM; kcat/KM = 1800 M^-1 s^-1.

row_label: Sros_6004 | D2AV87 / 4HypE (Table 2 cluster 11)

enzyme: 4-hydroxyproline epimerase


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


substrate_name: (R)-trifluorolactate

substrate: (R)-trifluorolactate


substrate_name: (S)-trifluorolactate

substrate: (S)-trifluorolactate


substrate_name: L-Isoleucine

substrate: L-Isoleucine


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


substrate_name: D-allo-isoleucine

substrate: D-allo-isoleucine


substrate_name: (R)-mandelate

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

substrate: (R)-mandelate


substrate_name: (S)-Mandelate

substrate: (S)-Mandelate


substrate_name: Unknown


enzyme_display_name: serine racemase

organism: Oryza sativa

substrate_name: D-serine

proof_lines: mutant enzyme E219A/D225A, in the absence of Mg2+, pH and temperature not specified in the publication

proof_lines: mutant enzyme E219A/D225A, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication

enzyme: serine racemase

substrate: D-serine


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

proof_lines: wild type enzyme, in the presence of 1 mM Mg2+, pH and temperature not specified in the publication

proof_lines: wild type enzyme, in the absence of Mg2+, pH and temperature not specified in the publication


enzyme_display_name: diaminopimelate epimerase

organism: Priestia megaterium

substrate_name: LL-diaminoheptanedioate

enzyme: diaminopimelate epimerase

substrate: LL-diaminoheptanedioate


substrate_name: meso-diaminoheptanedioate

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

substrate: meso-diaminoheptanedioate


enzyme_display_name: L-3-cyanoalanine synthase

organism: Pieris rapae

substrate_name: hydrogen sulfide

smiles: S

enzyme: L-3-cyanoalanine synthase

substrate: hydrogen sulfide


substrate_name: L-cysteine

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

substrate: L-cysteine


substrate_name: (R)-mandelamide


enzyme_display_name: methylmalonyl-CoA mutase

organism: Propionibacterium freudenreichii subsp. shermanii

enzyme: methylmalonyl-CoA mutase


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22F


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26L


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant A25V


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26F


proof_lines: mutant V22I/V29L, pH 7.5, 25°C, presence of 20 mM Mg2+

proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22I/V29L


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A/V29L


proof_lines:
mutant V26L, pH 7.5, 25°C
pH 7.5, 3.3 mM Mg2+, mutant V26L
pH 7.5, 25°C, mutant V26L


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant T24S


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29F


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22A


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29A


proof_lines:
mutant V29L, pH 7.5, 25°C
pH 7.5, 3.3 mM Mg2+, mutant V29L
pH 7.5, 25°C, mutant V29L


proof_lines:
mutant V22A, pH 7.5, 25°C
pH 7.5, 3.3 mM Mg2+ mutant V22A
pH 7.5, 3.3 mM Mg2+, mutant V22A


proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29L


proof_lines: mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+

proof_lines: pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22I


proof_lines: pH 7.5, mutant V22A, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V22F, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V26F, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V29A, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V26L, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V26A, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V29F, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant T24S, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, wild-type, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V29L, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V26A/V29L, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant A25V, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V22I, addition of either 10 mM (R)- or (S)-mandelate


proof_lines: pH 7.5, mutant V22I/V29L, addition of either 10 mM (R)- or (S)-mandelate


assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

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


substrate_name: adenosylcobalamin

substrate: adenosylcobalamin


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11444 and applied mutation signature V22I/V29I/Y54F to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(S)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V22I/V29I/Y54F': Km = 17.94 mM, kcat = 3.49 s^(-1), kcat/Km = 194.69 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 17.94 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 17.94 mM. kcat: printed Table 2 cell 3.49 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 3.49 s^(-1). kcat/Km: printed Table 2 cell 194.69 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 194.69 / 1000 = 0.19469 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (S)-2-CMA half of the printed line for enzyme form V22I/V29I/Y54F: Km = 17.94 mM; kcat = 3.49 s^(-1); printed kcat/Km = 194.69 M^-1 s^-1.


sequence_variant_note: Mutation signature V22I/Y45F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11444 and applied mutation signature V29I to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(S)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'V29I': Km = 14.35 mM, kcat = 1.83 s^(-1), kcat/Km = 127.66 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 14.35 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 14.35 mM. kcat: printed Table 2 cell 1.83 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 1.83 s^(-1). kcat/Km: printed Table 2 cell 127.66 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 127.66 / 1000 = 0.12766 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (S)-2-CMA half of the printed line for enzyme form V29I: Km = 14.35 mM; kcat = 1.83 s^(-1); printed kcat/Km = 127.66 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V29I/Y45F with inferred residue-numbering offset -25 to reconstruct the assayed variant sequence.


column_label: Table 2: Kinetic analysis of the WT and mutants of MR toward (S)-o-chloromandelic acid and (R)-o-chloromandelic acid; group header column '(S)-2-CMA' covering the three kinetic columns 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (s-1 M-1)'; line for enzyme form 'WT': Km = 17.74 mM, kcat = 0.99 s^(-1), kcat/Km = 56.34 M^-1 s^-1; the trailing 'Keq' column of that line is not a kinetic metric of the export schema.

normalized_value_unit_evidence: Km: printed Table 2 cell 17.74 mM; the printed unit is already the export unit, so no unit conversion applies and the normalized value is 17.74 mM. kcat: printed Table 2 cell 0.99 s^(-1); the printed unit is already the export unit, so no unit conversion applies and the normalized value is 0.99 s^(-1). kcat/Km: printed Table 2 cell 56.34 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 56.34 / 1000 = 0.05634 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, (S)-2-CMA half of the printed line for enzyme form WT: Km = 17.74 mM; kcat = 0.99 s^(-1); printed kcat/Km = 56.34 M^-1 s^-1.


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


organism: Pseudomonas aeruginosa

substrate_name: alpha-D-glucose 1-phosphate

proof_lines: mutant H329A, pH 7.5, temperature not specified in the publication

substrate: alpha-D-glucose 1-phosphate


proof_lines: wild-type enzyme, pH 7.5, temperature not specified in the publication


proof_lines:
25°C, pH 7.5, mutant enzyme N197A
mutant N197A

substrate: Unknown


substrate_name: methylglyoxal

proof_lines:
presence of Co2+, pH 7.0
presence of Ni2+, pH 7.0

substrate: methylglyoxal


substrate_name: (R)-S-lactoylglutathione

proof_lines:
pH 7.0, 0.5 mM CoCl2
pH 7.0, 0.5 mM NiCl2

substrate: (R)-S-lactoylglutathione


enzyme_display_name: protoporphyrin ferrochelatase

enzyme: protoporphyrin ferrochelatase


substrate_name: mesoporphyrin IX

substrate: mesoporphyrin IX


proof_lines: 25°C, pH 7.5, mutant enzyme C92S/C264S/166thiaK


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


proof_lines:
mutant V29I, pH 7.5, 25°C
mutant V29I/V29I, 20 mM Mg2+, pH 7.5


proof_lines: mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+


enzyme_display_name: amino-acid racemase

substrate_name: D-Lys

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

enzyme: amino-acid racemase

substrate: D-Lys


substrate_name: D-Thr

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

substrate: D-Thr


substrate_name: L-Leu

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

substrate: L-Leu


substrate_name: (R)-mandelate


proof_lines:
mutant K166R
pH 7.5, 25°C, mutant enzyme K166R


enzyme_display_name: methionine gamma-lyase

organism: Pseudomonas sp.

enzyme: methionine gamma-lyase


substrate_name: L-methionine

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

substrate: L-methionine


enzyme_display_name: UniProt Q9A1H8

organism: Streptococcus pyogenes

substrate_name: D-ribulose 5-phosphate

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

enzyme: UniProt Q9A1H8

substrate: D-ribulose 5-phosphate


enzyme_display_name: UDP-glucose 4-epimerase

organism: Galdieria sulphuraria

substrate_name: UDPgalactose

enzyme: UDP-glucose 4-epimerase

substrate: UDPgalactose


enzyme_display_name: UniProt A3MUJ4

organism: Pyrobaculum calidifontis

substrate_name: UDP-galactose

enzyme: UniProt A3MUJ4

substrate: UDP-galactose


enzyme_display_name: UniProt C8VAU8

organism: Aspergillus nidulans

substrate_name: UDP-alpha-D-glucose

enzyme: UniProt C8VAU8

substrate: UDP-alpha-D-glucose


enzyme_display_name: UniProt P09147

organism: Escherichia coli

substrate_name: D-galactose

enzyme: UniProt P09147

substrate: D-galactose


substrate_name: D-tagatose

substrate: D-tagatose


enzyme_display_name: guanylate cyclase

organism: Rattus norvegicus

substrate_name: GTP

proof_lines: pH 8.0, 30°C, wild-type enzyme, in presence of NO-donor S-nitroso-N-acetylpenicillamine

enzyme: guanylate cyclase

substrate: GTP


substrate_name: Unknown


enzyme_display_name: cysteine-S-conjugate beta-lyase

enzyme: cysteine-S-conjugate beta-lyase


substrate_name: kynurenine

substrate: kynurenine


enzyme_display_name: protein disulfide-isomerase

substrate_name: insulin-(SS)

enzyme: protein disulfide-isomerase

substrate: insulin-(SS)


substrate_name: GSH

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

substrate: GSH


enzyme_display_name: mandelate racemase

substrate_name: (S)-Mandelate

proof_lines:
mutant E317Q
E317Q mutant

enzyme: mandelate racemase

substrate: (S)-Mandelate


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


substrate: Unknown


enzyme_display_name: FAD-AMP lyase (cyclizing)

substrate_name: FAD

assay_conditions_summary: cofactor FAD

enzyme: FAD-AMP lyase (cyclizing)

substrate: FAD


enzyme_display_name: prostaglandin-D synthase

substrate_name: glutathione

proof_lines: conjugation of glutathione to 1-chloro-2,4-dinitrobenzene

enzyme: prostaglandin-D synthase

substrate: glutathione


enzyme_display_name: leukotriene-C4 synthase

substrate_name: leukotriene A4 free acid

enzyme: leukotriene-C4 synthase

substrate: leukotriene A4 free acid


substrate_name: leukotriene A4 methyl ester

substrate: leukotriene A4 methyl ester


organism: Poterioochromonas malhamensis


organism: Saccharomyces fragilis


enzyme_display_name: aldose 1-epimerase

organism: Batrachoididae gen. sp.

substrate_name: alpha-D-glucose

enzyme: aldose 1-epimerase

substrate: alpha-D-glucose


organism: Thermotoga maritima

substrate_name: UDP-alpha-D-galactose

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

substrate: UDP-alpha-D-galactose


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

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


organism: Meriones unguiculatus


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

proof_lines: mitochondria cytoplasm


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


organism: Capsicum frutescens


organism: Torulopsis candida

substrate_name: UDPgalactose

substrate: UDPgalactose


organism: Pyrococcus horikoshii


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

organism: Escherichia coli (strain K12)

proof_lines: kcat is 20.4 sec(-1) for L-ribulose 5-phosphate (LRu5P) as substrate (PubMed:9548961). kcat is 19.4 sec(-1) for L-ribulose 5-phosphate (LRu5P) as substrate (PubMed:11732896). kcat is 17.3 sec(-1) for L-ribulose 5-phosphate (LRu5P) as substr

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


substrate_name: L-ribulose 5-phosphate (LRu5P) (with zinc ion)


substrate_name: L-ribulose 5-phosphate (LRu5P)

proof_lines: kcat is 12 sec(-1) with L-ribulose 5-phosphate (LRu5P) as substrate.

substrate: L-ribulose 5-phosphate (LRu5P)


proof_lines: kcat is 25 sec(-1) with L-ribulose 5-phosphate (LRu5P) as substrate.


substrate_name: UDP-galactose

substrate: UDP-galactose


organism: Ovis aries

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

proof_lines: alpha-D-glucose, kidney, embryo and adult


organism: Perca flavescens


enzyme_display_name: tagaturonate epimerase

substrate_name: D-fructuronate

proof_lines: kcat is 6.5 sec(-1) with D-fructuronate as substrate.

enzyme: tagaturonate epimerase

substrate: D-fructuronate


enzyme_display_name: ribulose-phosphate 3-epimerase

organism: Oryza sativa subsp. japonica

substrate_name: Unknown

enzyme: ribulose-phosphate 3-epimerase


organism: Arabidopsis thaliana


organism: Homo sapiens


organism: Kluyveromyces marxianus


organism: Thermus thermophilus

assay_conditions_summary: pH 8.9; cofactor NAD+

proof_lines: recombinant enzyme, 100 mM glycine-NaOH (pH 8.9), 4 mM UDP-galactose, 1 mM beta-NAD+, 8.3 mM MgCl2, and 5.4 U of UDP-glucose dehydrogenase


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

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


substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


organism: Escherichia coli

substrate_name: alpha-D-Galactose

substrate: alpha-D-Galactose


substrate_name: alpha-D-Glucose

substrate: alpha-D-Glucose


substrate_name: alpha-D-galactose

proof_lines: kcat is 12000 sec(-1) with galactose as substrate (PubMed:12753898). kcat is 4900 sec(-1) with glucose as substrate (PubMed:12753898).

substrate: alpha-D-galactose


normalized_value_unit_evidence: Normalized values: kcat=12000 s^-1; Km=37 mM; independently printed kcat/Km=340 s^-1 mM^-1 after converting 340000 L mol^-1 s^-1.

row_label: Galactose

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H95N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08203 and applied mutation signature H97N to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Constants for Different Metal Ions for WT and Mutant L-Ru5P 4-Epimerases (Biochemistry 2000, volume 39, number 16, pages 4821-4830); four metal columns headed ZnCl2, CoCl2, MnCl2 and MgCl2, each enzyme block printing Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). The enzyme block is the printed row label and each metal column prints Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). Enzyme block 'H97N', column 'CoCl2': Km = 1.67; kcat = 2.14; kcat/Km = 1.28.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.14 in the kcat cell of this cell group, whose head prints s-1, so no unit conversion applies and the paper value is 2.14 s^(-1). Km: printed Table 1 cell 1.67 in the Km cell of this cell group, whose head prints uM; 1.67 / 1000 = 0.00167 mM. kcat/Km: printed Table 1 cell 1.28 in the kcat/Km cell of this cell group, whose head prints uM-1 s-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 1.28 x 1000 = 1280.0 s^-1 mM^-1. Closure check on the paper's own cells: 2.14 / 0.00167 = 1281.437125748503 s^-1 mM^-1, which the printed efficiency cell 1.28 reproduces at the precision Table 1 uses.

raw_value_unit_evidence: Table 1, enzyme block 'H97N', metal-ion column 'CoCl2': Km = 1.67 uM; kcat = 2.14 s^-1; printed kcat/Km = 1.28 uM^-1 s^-1.


column_label: Table 1: Kinetic Constants for Different Metal Ions for WT and Mutant L-Ru5P 4-Epimerases (Biochemistry 2000, volume 39, number 16, pages 4821-4830); four metal columns headed ZnCl2, CoCl2, MnCl2 and MgCl2, each enzyme block printing Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). The enzyme block is the printed row label and each metal column prints Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). Enzyme block 'wild-type', column 'CoCl2': Km = 0.29; kcat = 24.3; kcat/Km = 83.8.

normalized_value_unit_evidence: kcat: printed Table 1 cell 24.3 in the kcat cell of this cell group, whose head prints s-1, so no unit conversion applies and the paper value is 24.3 s^(-1). Km: printed Table 1 cell 0.29 in the Km cell of this cell group, whose head prints uM; 0.29 / 1000 = 0.00029 mM. kcat/Km: printed Table 1 cell 83.8 in the kcat/Km cell of this cell group, whose head prints uM-1 s-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 83.8 x 1000 = 83800.0 s^-1 mM^-1. Closure check on the paper's own cells: 24.3 / 0.00029 = 83793.10344827586 s^-1 mM^-1, which the printed efficiency cell 83.8 reproduces at the precision Table 1 uses.

raw_value_unit_evidence: Table 1, enzyme block 'wild-type', metal-ion column 'CoCl2': Km = 0.29 uM; kcat = 24.3 s^-1; printed kcat/Km = 83.8 uM^-1 s^-1.


substrate_name: L-Ribulose 5-phosphate

substrate: L-Ribulose 5-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H97N to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08203 and applied mutation signature Y229F to reconstruct the assayed variant sequence.

column_label: Table 3 of Biochemistry 2000, volume 39, number 16, pages 4821-4830; the L-Ru5P kinetic constants table for the Zn(II)-substituted mutant enzymes, whose column groups print Km (mM), kcat (s^-1) and kcat/Km (mM^-1 s^-1). The metric is the printed row label and each column group prints Km (mM), kcat (s^-1) and kcat/Km (mM^-1 s^-1). Column group 'Zn(II)-Y229F': Km = 0.129; kcat = 0.0118; kcat/Km = 0.0915.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.0118 in the kcat cell of this cell group, whose head prints s-1, so no unit conversion applies and the paper value is 0.0118 s^(-1). Km: printed Table 3 cell 0.129 in the Km cell of this cell group, whose head prints mM, so no unit conversion applies and the paper value is 0.129 mM. kcat/Km: printed Table 3 cell 0.0915 in the kcat/Km cell of this cell group, whose head prints mM-1 s-1, the export unit, so no unit conversion applies and the printed cell is 0.0915 s^-1 mM^-1. Closure check on the paper's own cells: 0.0118 / 0.129 = 0.09147286821705426 s^-1 mM^-1, which the printed efficiency cell 0.0915 reproduces at the precision Table 3 uses.

raw_value_unit_evidence: Table 3, L-Ru5P column group 'Zn(II)-Y229F': Km = 0.129 mM; kcat = 0.0118 s^-1; printed kcat/Km = 0.0915 mM^-1 s^-1.


column_label: Table 1: Kinetic Constants for Different Metal Ions for WT and Mutant L-Ru5P 4-Epimerases (Biochemistry 2000, volume 39, number 16, pages 4821-4830); four metal columns headed ZnCl2, CoCl2, MnCl2 and MgCl2, each enzyme block printing Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). The enzyme block is the printed row label and each metal column prints Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). Enzyme block 'wild-type', column 'MgCl2': Km = 1350; kcat = 0.855; kcat/Km = 0.000633.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.855 in the kcat cell of this cell group, whose head prints s-1, so no unit conversion applies and the paper value is 0.855 s^(-1). Km: printed Table 1 cell 1350 in the Km cell of this cell group, whose head prints uM; 1350 / 1000 = 1.35 mM. kcat/Km: printed Table 1 cell 0.000633 in the kcat/Km cell of this cell group, whose head prints uM-1 s-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.000633 x 1000 = 0.633 s^-1 mM^-1. Quotient disclosure for this cell group: 0.855 / 1.35 = 0.6333333333333333 s^-1 mM^-1, which is the value the export carries; the printed efficiency cell is that same quotient carried to the precision Table 1 uses, and it sits inside the last-place rounding interval of the quotient.

raw_value_unit_evidence: Table 1, enzyme block 'wild-type', metal-ion column 'MgCl2': Km = 1350 uM; kcat = 0.855 s^-1; printed kcat/Km = 0.000633 uM^-1 s^-1.


substrate_name: UDP-xylose

substrate: UDP-xylose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D103G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G319E with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G90E with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K257R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L183P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L313M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N34S with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R335H with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


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


organism: Hordeum vulgare

substrate_name: UDP-D-galactose

substrate: UDP-D-galactose


substrate_name: UDP-D-glucose

substrate: UDP-D-glucose


column_label: Table 1: Kinetic Constants for Different Metal Ions for WT and Mutant L-Ru5P 4-Epimerases (Biochemistry 2000, volume 39, number 16, pages 4821-4830); four metal columns headed ZnCl2, CoCl2, MnCl2 and MgCl2, each enzyme block printing Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). The enzyme block is the printed row label and each metal column prints Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). Enzyme block 'wild-type', column 'MnCl2': Km = 0.54; kcat = 37.2; kcat/Km = 68.9.

normalized_value_unit_evidence: kcat: printed Table 1 cell 37.2 in the kcat cell of this cell group, whose head prints s-1, so no unit conversion applies and the paper value is 37.2 s^(-1). Km: printed Table 1 cell 0.54 in the Km cell of this cell group, whose head prints uM; 0.54 / 1000 = 0.00054 mM. kcat/Km: printed Table 1 cell 68.9 in the kcat/Km cell of this cell group, whose head prints uM-1 s-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 68.9 x 1000 = 68900.0 s^-1 mM^-1. Closure check on the paper's own cells: 37.2 / 0.00054 = 68888.88888888889 s^-1 mM^-1, which the printed efficiency cell 68.9 reproduces at the precision Table 1 uses.

raw_value_unit_evidence: Table 1, enzyme block 'wild-type', metal-ion column 'MnCl2': Km = 0.54 uM; kcat = 37.2 s^-1; printed kcat/Km = 68.9 uM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08203 and applied mutation signature H95N to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Constants for Different Metal Ions for WT and Mutant L-Ru5P 4-Epimerases (Biochemistry 2000, volume 39, number 16, pages 4821-4830); four metal columns headed ZnCl2, CoCl2, MnCl2 and MgCl2, each enzyme block printing Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). The enzyme block is the printed row label and each metal column prints Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). Enzyme block 'H95N', column 'ZnCl2': Km = 2.02; kcat = 0.190; kcat/Km = 0.094.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.190 in the kcat cell of this cell group, whose head prints s-1, so no unit conversion applies and the paper value is 0.19 s^(-1). Km: printed Table 1 cell 2.02 in the Km cell of this cell group, whose head prints uM; 2.02 / 1000 = 0.00202 mM. kcat/Km: printed Table 1 cell 0.094 in the kcat/Km cell of this cell group, whose head prints uM-1 s-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.094 x 1000 = 94.0 s^-1 mM^-1. Closure check on the paper's own cells: 0.19 / 0.00202 = 94.05940594059406 s^-1 mM^-1, which the printed efficiency cell 0.094 reproduces at the precision Table 1 uses.

raw_value_unit_evidence: Table 1, enzyme block 'H95N', metal-ion column 'ZnCl2': Km = 2.02 uM; kcat = 0.190 s^-1; printed kcat/Km = 0.094 uM^-1 s^-1.


column_label: Table 1: Kinetic Constants for Different Metal Ions for WT and Mutant L-Ru5P 4-Epimerases (Biochemistry 2000, volume 39, number 16, pages 4821-4830); four metal columns headed ZnCl2, CoCl2, MnCl2 and MgCl2, each enzyme block printing Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). The enzyme block is the printed row label and each metal column prints Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). Enzyme block 'H97N', column 'ZnCl2': Km = 0.53; kcat = 1.77; kcat/Km = 3.34.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.77 in the kcat cell of this cell group, whose head prints s-1, so no unit conversion applies and the paper value is 1.77 s^(-1). Km: printed Table 1 cell 0.53 in the Km cell of this cell group, whose head prints uM; 0.53 / 1000 = 0.00053 mM. kcat/Km: printed Table 1 cell 3.34 in the kcat/Km cell of this cell group, whose head prints uM-1 s-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 3.34 x 1000 = 3340.0 s^-1 mM^-1. Closure check on the paper's own cells: 1.77 / 0.00053 = 3339.622641509434 s^-1 mM^-1, which the printed efficiency cell 3.34 reproduces at the precision Table 1 uses.

raw_value_unit_evidence: Table 1, enzyme block 'H97N', metal-ion column 'ZnCl2': Km = 0.53 uM; kcat = 1.77 s^-1; printed kcat/Km = 3.34 uM^-1 s^-1.


column_label: Table 1: Kinetic Constants for Different Metal Ions for WT and Mutant L-Ru5P 4-Epimerases (Biochemistry 2000, volume 39, number 16, pages 4821-4830); four metal columns headed ZnCl2, CoCl2, MnCl2 and MgCl2, each enzyme block printing Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). The enzyme block is the printed row label and each metal column prints Km (uM), kcat (s^-1) and kcat/Km (uM^-1 s^-1). Enzyme block 'wild-type', column 'ZnCl2': Km = 0.17; kcat = 16.7; kcat/Km = 98.2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 16.7 in the kcat cell of this cell group, whose head prints s-1, so no unit conversion applies and the paper value is 16.7 s^(-1). Km: printed Table 1 cell 0.17 in the Km cell of this cell group, whose head prints uM; 0.17 / 1000 = 0.00017 mM. kcat/Km: printed Table 1 cell 98.2 in the kcat/Km cell of this cell group, whose head prints uM-1 s-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 98.2 x 1000 = 98200.0 s^-1 mM^-1. Closure check on the paper's own cells: 16.7 / 0.00017 = 98235.29411764706 s^-1 mM^-1, which the printed efficiency cell 98.2 reproduces at the precision Table 1 uses.

raw_value_unit_evidence: Table 1, enzyme block 'wild-type', metal-ion column 'ZnCl2': Km = 0.17 uM; kcat = 16.7 s^-1; printed kcat/Km = 98.2 uM^-1 s^-1.


organism: Pisum sativum

substrate_name: UDP-D-xylose

assay_conditions_summary: pH 8.6; 298.15 K; cofactor NAD+

column_label: Table 5: Substrate saturation kinetics of rPsUGE1 (Biochem. J. 2009, 424(2):169-177), substrate row UDP-Xyl; column 'K m (mM)' = 0.15 ± 0.02; column 'k cat (s^-1)' = 17; column 'k cat/K m (mM^-1 s^-1)' = 115.

normalized_value_unit_evidence: Km: printed Table 5 cell 0.15 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.15 mM; the exported value is 0.15 mM. kcat: printed Table 5 cell 17 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 17.0 s^(-1); the exported value is 17.0 s^(-1). kcat/Km: printed Table 5 cell 115 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 115.0 s^(-1)*mM^(-1); the exported value is 113.33333333333334 s^(-1)*mM^(-1), the full-precision quotient of the exported kcat and Km.

raw_value_unit_evidence: Table 5, substrate row UDP-Xyl: K m = 0.15 ± 0.02 mM; k cat = 17 s^-1; printed k cat/K m = 115 mM^-1 s^-1.

row_label: Table 5, substrate row UDP-Xyl

substrate: UDP-D-xylose


column_label: Table 5: Substrate saturation kinetics of rPsUGE1 (Biochem. J. 2009, 424(2):169-177), substrate row UDP-Gal; column 'K m (mM)' = 0.29 ± 0.03; column 'k cat (s^-1)' = 64; column 'k cat/K m (mM^-1 s^-1)' = 220.

normalized_value_unit_evidence: Km: printed Table 5 cell 0.29 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.29 mM; the exported value is 0.29 mM. kcat: printed Table 5 cell 64 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 64.0 s^(-1); the exported value is 64.0 s^(-1). kcat/Km: printed Table 5 cell 220 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 220.0 s^(-1)*mM^(-1); the exported value is 220.6896551724138 s^(-1)*mM^(-1), the full-precision quotient of the exported kcat and Km.

raw_value_unit_evidence: Table 5, substrate row UDP-Gal: K m = 0.29 ± 0.03 mM; k cat = 64 s^-1; printed k cat/K m = 220 mM^-1 s^-1.

row_label: Table 5, substrate row UDP-Gal


substrate_name: UDP-glucose

column_label: Table 5: Substrate saturation kinetics of rPsUGE1 (Biochem. J. 2009, 424(2):169-177), substrate row UDP-Glc; column 'K m (mM)' = 0.31 ± 0.03; column 'k cat (s^-1)' = 9; column 'k cat/K m (mM^-1 s^-1)' = 28.

normalized_value_unit_evidence: Km: printed Table 5 cell 0.31 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.31 mM; the exported value is 0.31 mM. kcat: printed Table 5 cell 9 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 9.0 s^(-1); the exported value is 9.0 s^(-1). kcat/Km: printed Table 5 cell 28 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 28.0 s^(-1)*mM^(-1); the exported value is 29.032258064516128 s^(-1)*mM^(-1), the full-precision quotient of the exported kcat and Km.

raw_value_unit_evidence: Table 5, substrate row UDP-Glc: K m = 0.31 ± 0.03 mM; k cat = 9 s^-1; printed k cat/K m = 28 mM^-1 s^-1.

row_label: Table 5, substrate row UDP-Glc

substrate: UDP-glucose


substrate_name: UDP-L-arabinose

column_label: Table 5: Substrate saturation kinetics of rPsUGE1 (Biochem. J. 2009, 424(2):169-177), substrate row UDP-Ara; column 'K m (mM)' = 0.16 ± 0.01; column 'k cat (s^-1)' = 23; column 'k cat/K m (mM^-1 s^-1)' = 141.

normalized_value_unit_evidence: Km: printed Table 5 cell 0.16 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.16 mM; the exported value is 0.16 mM. kcat: printed Table 5 cell 23 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 23.0 s^(-1); the exported value is 23.0 s^(-1). kcat/Km: printed Table 5 cell 141 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 141.0 s^(-1)*mM^(-1); the exported value is 143.75 s^(-1)*mM^(-1), the full-precision quotient of the exported kcat and Km.

raw_value_unit_evidence: Table 5, substrate row UDP-Ara: K m = 0.16 ± 0.01 mM; k cat = 23 s^-1; printed k cat/K m = 141 mM^-1 s^-1.

row_label: Table 5, substrate row UDP-Ara

substrate: UDP-L-arabinose


organism: Spinacia oleracea

substrate_name: ribulose 5-phosphate

substrate: ribulose 5-phosphate


substrate_name: UDP-alpha-D-galactose

substrate: UDP-alpha-D-galactose


organism: Marinithermus hydrothermalis

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

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G118A/G119A with inferred residue-numbering offset -22 to reconstruct the assayed variant sequence.

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G118S/G119S with inferred residue-numbering offset -22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S279Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S116A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T117S 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: Aspergillus nidulans

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


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


substrate_name: UDPgalactose

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

proof_lines:
native and renatured enzyme
25°C, pH 8.8

substrate: UDPgalactose


assay_conditions_summary: pH 8.6; cofactor NAD+

proof_lines: recombinant enzyme UGE4, 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 enzyme UGE4, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase


proof_lines: recombinant enzyme UGE3, 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 enzyme UGE3, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase


proof_lines: recombinant Arabidopsis thaliana enzyme UGE2, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDPGlc dehydrogenase

proof_lines: recombinant Arabidopsis thaliana enzyme UGE2, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase


proof_lines: recombinant enzyme UGE5, 100 mM glycine/NaOH (pH 8.6), 0.015-1 mM UDP-Gal, 2 mM NAD+ and 40 mU of UDP-glucose dehydrogenase