column_label: Table 4 row Wild-type Lyr; L-Arg columns kcat = 650 min^-1, Km = 14.9 mM, kcat/Km (B) = 43.6 min^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=10.833333333333334 normalized_unit=s^-1; km normalized_value=14.9 normalized_unit=mM; kcat_over_km normalized_value=0.7266666666666667 normalized_unit=s^-1*mM^-1; conversions=650/60 and 43.6/60

raw_value_unit_evidence: kcat raw_value=650 raw_unit=min^-1; Km raw_value=14.9 raw_unit=mM; kcat/Km raw_value=43.6 raw_unit=min^-1*mM^-1


enzyme_display_name: diaminopimelate epimerase

organism: Mycobacterium tuberculosis

substrate_name: meso-diaminoheptanedioate

source_db: brenda

ki_display: Not reported

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C87S to reconstruct the assayed variant sequence.

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

mutation_type: substitution

data_origin: experimental

enzyme: diaminopimelate epimerase

substrate: meso-diaminoheptanedioate

source: brenda


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C226S to reconstruct the assayed variant sequence.


mutation_signature: Unknown

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


source_db: skid

protein_accession_database: UniProt

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

sequence_source: multiple

proof_lines: kcat is 0.1465 sec(-1) for epimerase activity.

source_databases_merged: skid uniprot

source: skid


enzyme_display_name: amino-acid racemase

organism: Bacillus subtilis

substrate_name: D-Lysine

source_db: oed

kcat_over_km_origin: calculated

enzyme: amino-acid racemase

substrate: D-Lysine

source: oed


substrate_name: L-lysine

substrate: L-lysine


enzyme_display_name: 4-hydroxyproline epimerase

organism: Thermococcus litoralis

verification_status: corrected

column_label: Table 1. Kinetic parameters for L-proline, T4LHyp, and T3LHyp; row TlProR WT / T4LHyp; columns Km, kcat, kcat/Km report normalized values kcat=12.1333 s^-1, Km=6.08 mM, kcat/Km=2.03333 s^-1*mM^-1.

raw_value_unit_evidence: TlProR WT / T4LHyp; kcat raw_value=728 +/- 146 min^-1; Km raw_value=6.08 +/- 1.76 mM; kcat/Km raw_value=122 +/- 13 min^-1*mM^-1.

row_label: TlProR WT / T4LHyp

enzyme: 4-hydroxyproline epimerase

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_accession:H3ZMH5 and applied mutation signature F62S to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters for D-proline and C4DHyp; row TlProR F62S / C4DHyp; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1*mM^-1); TlProR F62S / C4DHyp: kcat 0.859 +/- 0.012 min^-1; Km 3.14 +/- 0.15 mM; kcat/Km 0.274 +/- 0.010 min^-1*mM^-1. Direct /60 conversion of kcat and kcat/Km gives kcat=0.014316666666666667 s^-1; Km=3.14 mM; kcat/Km=0.004566666666666667 s^-1*mM^-1.

row_label: TlProR F62S / C4DHyp


sequence_variant_note: Resolved canonical sequence from uniprot_accession:H3ZMH5 and applied mutation signature L221H to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters for D-proline and C4DHyp; row TlProR L221H / C4DHyp; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1*mM^-1); TlProR L221H / C4DHyp: kcat 6.66 +/- 1.31 min^-1; Km 4.18 +/- 0.81 mM; kcat/Km 1.59 +/- 0.00 min^-1*mM^-1. Direct /60 conversion of kcat and kcat/Km gives kcat=0.111 s^-1; Km=4.18 mM; kcat/Km=0.026500000000000003 s^-1*mM^-1.

row_label: TlProR L221H / C4DHyp


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:H3ZMH5 and applied mutation signature W241F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 323.15 K; buffer 50 mM Tris-HCl

column_label: Table 2: Kinetic parameters for D-proline and C4DHyp. (PLOS ONE 2015, PMID 25786142). Column heads: Enzymes | Substrates | Specific activity a (units/mg protein) | K m (mM) | k cat (min-1) | k cat/K m (min-1 mM-1) | ProRHypE. The cited row is the one whose enzyme cell reads 'TlProRW241F' and whose substrate cell reads 'C4DHyp'; in that row the column 'K m (mM)' prints 6.70, the column 'k cat (min-1)' prints 41.8, the column 'k cat/K m (min-1 mM-1)' prints 6.25, and the column 'Specific activity a (units/mg protein)' prints the activity restated in the decoded line.

normalized_value_unit_evidence: K m: printed Table 2 cell 6.70 mM; the column head is K m (mM), so no conversion is needed and the paper value is 6.7 mM (the exported value is 6.7 mM). k cat: printed Table 2 cell 41.8 min-1; 1 min^-1 is 1/60 s^-1, so 41.8 / 60 = 0.6966666666666667 s^-1 (the exported value is 0.69 s^-1). k cat/K m: printed Table 2 cell 6.25 min-1 mM-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 6.25 / 60 = 0.10416666666666667 s^-1 mM^-1 (the exported value is 0.10298507462686567 s^-1 mM^-1).

raw_value_unit_evidence: Table 2 (Table 2: Kinetic parameters for D-proline and C4DHyp. (PLOS ONE 2015, PMID 25786142)), enzyme row 'TlProRW241F', substrate cell 'C4DHyp': column 'K m (mM)' = 6.70; column 'k cat (min-1)' = 41.8; column 'k cat/K m (min-1 mM-1)' = 6.25.

row_label: Table 2, row with enzyme 'TlProRW241F' and substrate 'C4DHyp'


column_label: Table 2: Kinetic parameters for D-proline and C4DHyp. (PLOS ONE 2015, PMID 25786142). Column heads: Enzymes | Substrates | Specific activity a (units/mg protein) | K m (mM) | k cat (min-1) | k cat/K m (min-1 mM-1) | ProRHypE. The cited row is the one whose enzyme cell reads 'TlProRWT' and whose substrate cell reads 'C4DHyp'; in that row the column 'K m (mM)' prints 6.65, the column 'k cat (min-1)' prints 230, the column 'k cat/K m (min-1 mM-1)' prints 34.8, and the column 'Specific activity a (units/mg protein)' prints the activity restated in the decoded line.

normalized_value_unit_evidence: K m: printed Table 2 cell 6.65 mM; the column head is K m (mM), so no conversion is needed and the paper value is 6.65 mM (the exported value is 6.65 mM). k cat: printed Table 2 cell 230 min-1; 1 min^-1 is 1/60 s^-1, so 230 / 60 = 3.8333333333333335 s^-1 (the exported value is 3.83 s^-1). k cat/K m: printed Table 2 cell 34.8 min-1 mM-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 34.8 / 60 = 0.58 s^-1 mM^-1 (the exported value is 0.5759398496240601 s^-1 mM^-1).

raw_value_unit_evidence: Table 2 (Table 2: Kinetic parameters for D-proline and C4DHyp. (PLOS ONE 2015, PMID 25786142)), enzyme row 'TlProRWT', substrate cell 'C4DHyp': column 'K m (mM)' = 6.65; column 'k cat (min-1)' = 230; column 'k cat/K m (min-1 mM-1)' = 34.8.

row_label: Table 2, row with enzyme 'TlProRWT' and substrate 'C4DHyp'


column_label: Table 1: Kinetic parameters for L-proline, T4LHyp, and T3LHyp. (PLOS ONE 2015, PMID 25786142). Column heads: Enzymes | Substrates | Specific activity a (units/mg protein) | K m (mM) | k cat (min-1) | k cat/K m (min-1 mM-1) | ProRHypE. The cited row is the one whose enzyme cell reads 'TlProRW241F' and whose substrate cell reads 'T3LHyp'; in that row the column 'K m (mM)' prints 16.4, the column 'k cat (min-1)' prints 17.5, the column 'k cat/K m (min-1 mM-1)' prints 1.07, and the column 'Specific activity a (units/mg protein)' prints the activity restated in the decoded line.

normalized_value_unit_evidence: K m: printed Table 1 cell 16.4 mM; the column head is K m (mM), so no conversion is needed and the paper value is 16.4 mM (the exported value is 16.4 mM). k cat: printed Table 1 cell 17.5 min-1; 1 min^-1 is 1/60 s^-1, so 17.5 / 60 = 0.2916666666666667 s^-1 (the exported value is 0.29 s^-1). k cat/K m: printed Table 1 cell 1.07 min-1 mM-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 1.07 / 60 = 0.017833333333333333 s^-1 mM^-1 (the exported value is 0.017682926829268295 s^-1 mM^-1).

raw_value_unit_evidence: Table 1 (Table 1: Kinetic parameters for L-proline, T4LHyp, and T3LHyp. (PLOS ONE 2015, PMID 25786142)), enzyme row 'TlProRW241F', substrate cell 'T3LHyp': column 'K m (mM)' = 16.4; column 'k cat (min-1)' = 17.5; column 'k cat/K m (min-1 mM-1)' = 1.07.

row_label: Table 1, row with enzyme 'TlProRW241F' and substrate 'T3LHyp'


column_label: Table 1. Kinetic parameters for L-proline, T4LHyp, and T3LHyp; row TlProR WT / T3LHyp; columns Km, kcat, kcat/Km report normalized values kcat=3.6 s^-1, Km=0.502 mM, kcat/Km=7.16667 s^-1*mM^-1.

raw_value_unit_evidence: TlProR WT / T3LHyp; kcat raw_value=216 +/- 4 min^-1; Km raw_value=0.502 +/- 0.021 mM; kcat/Km raw_value=430 +/- 10 min^-1*mM^-1.

row_label: TlProR WT / T3LHyp


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:H3ZMH5 and applied mutation signature F62S to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters for L-proline, T4LHyp, and T3LHyp. (PLOS ONE 2015, PMID 25786142). Column heads: Enzymes | Substrates | Specific activity a (units/mg protein) | K m (mM) | k cat (min-1) | k cat/K m (min-1 mM-1) | ProRHypE. The cited row is the one whose enzyme cell reads 'TlProRF62S' and whose substrate cell reads 'T4LHyp'; in that row the column 'K m (mM)' prints 6.22, the column 'k cat (min-1)' prints 2.35, the column 'k cat/K m (min-1 mM-1)' prints 0.379, and the column 'Specific activity a (units/mg protein)' prints the activity restated in the decoded line.

normalized_value_unit_evidence: K m: printed Table 1 cell 6.22 mM; the column head is K m (mM), so no conversion is needed and the paper value is 6.22 mM (the exported value is 6.22 mM). k cat: printed Table 1 cell 2.35 min-1; 1 min^-1 is 1/60 s^-1, so 2.35 / 60 = 0.03916666666666667 s^-1 (the exported value is 0.039 s^-1). k cat/K m: printed Table 1 cell 0.379 min-1 mM-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.379 / 60 = 0.006316666666666667 s^-1 mM^-1 (the exported value is 0.0062700964630225085 s^-1 mM^-1).

raw_value_unit_evidence: Table 1 (Table 1: Kinetic parameters for L-proline, T4LHyp, and T3LHyp. (PLOS ONE 2015, PMID 25786142)), enzyme row 'TlProRF62S', substrate cell 'T4LHyp': column 'K m (mM)' = 6.22; column 'k cat (min-1)' = 2.35; column 'k cat/K m (min-1 mM-1)' = 0.379.

row_label: Table 1, row with enzyme 'TlProRF62S' and substrate 'T4LHyp'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:H3ZMH5 and applied mutation signature F62V to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters for L-proline, T4LHyp, and T3LHyp. (PLOS ONE 2015, PMID 25786142). Column heads: Enzymes | Substrates | Specific activity a (units/mg protein) | K m (mM) | k cat (min-1) | k cat/K m (min-1 mM-1) | ProRHypE. The cited row is the one whose enzyme cell reads 'TlProRF62V' and whose substrate cell reads 'T4LHyp'; in that row the column 'K m (mM)' prints 0.905, the column 'k cat (min-1)' prints 7.84, the column 'k cat/K m (min-1 mM-1)' prints 8.67, and the column 'Specific activity a (units/mg protein)' prints the activity restated in the decoded line.

normalized_value_unit_evidence: K m: printed Table 1 cell 0.905 mM; the column head is K m (mM), so no conversion is needed and the paper value is 0.905 mM (the exported value is 0.905 mM). k cat: printed Table 1 cell 7.84 min-1; 1 min^-1 is 1/60 s^-1, so 7.84 / 60 = 0.13066666666666665 s^-1 (the exported value is 0.13 s^-1). k cat/K m: printed Table 1 cell 8.67 min-1 mM-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 8.67 / 60 = 0.1445 s^-1 mM^-1 (the exported value is 0.143646408839779 s^-1 mM^-1).

raw_value_unit_evidence: Table 1 (Table 1: Kinetic parameters for L-proline, T4LHyp, and T3LHyp. (PLOS ONE 2015, PMID 25786142)), enzyme row 'TlProRF62V', substrate cell 'T4LHyp': column 'K m (mM)' = 0.905; column 'k cat (min-1)' = 7.84; column 'k cat/K m (min-1 mM-1)' = 8.67.

row_label: Table 1, row with enzyme 'TlProRF62V' and substrate 'T4LHyp'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:H3ZMH5 and applied mutation signature L221H to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters for L-proline, T4LHyp, and T3LHyp. (PLOS ONE 2015, PMID 25786142). Column heads: Enzymes | Substrates | Specific activity a (units/mg protein) | K m (mM) | k cat (min-1) | k cat/K m (min-1 mM-1) | ProRHypE. The cited row is the one whose enzyme cell reads 'TlProRL221H' and whose substrate cell reads 'T4LHyp'; in that row the column 'K m (mM)' prints 6.50, the column 'k cat (min-1)' prints 39.0, the column 'k cat/K m (min-1 mM-1)' prints 6.01, and the column 'Specific activity a (units/mg protein)' prints the activity restated in the decoded line.

normalized_value_unit_evidence: K m: printed Table 1 cell 6.50 mM; the column head is K m (mM), so no conversion is needed and the paper value is 6.5 mM (the exported value is 6.5 mM). k cat: printed Table 1 cell 39.0 min-1; 1 min^-1 is 1/60 s^-1, so 39.0 / 60 = 0.65 s^-1 (the exported value is 0.65 s^-1). k cat/K m: printed Table 1 cell 6.01 min-1 mM-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 6.01 / 60 = 0.10016666666666667 s^-1 mM^-1 (the exported value is 0.1 s^-1 mM^-1).

raw_value_unit_evidence: Table 1 (Table 1: Kinetic parameters for L-proline, T4LHyp, and T3LHyp. (PLOS ONE 2015, PMID 25786142)), enzyme row 'TlProRL221H', substrate cell 'T4LHyp': column 'K m (mM)' = 6.50; column 'k cat (min-1)' = 39.0; column 'k cat/K m (min-1 mM-1)' = 6.01.

row_label: Table 1, row with enzyme 'TlProRL221H' and substrate 'T4LHyp'


column_label: Table 1: Kinetic parameters for L-proline, T4LHyp, and T3LHyp. (PLOS ONE 2015, PMID 25786142). Column heads: Enzymes | Substrates | Specific activity a (units/mg protein) | K m (mM) | k cat (min-1) | k cat/K m (min-1 mM-1) | ProRHypE. The cited row is the one whose enzyme cell reads 'TlProRW241F' and whose substrate cell reads 'T4LHyp'; in that row the column 'K m (mM)' prints 4.28, the column 'k cat (min-1)' prints 92.0, the column 'k cat/K m (min-1 mM-1)' prints 21.7, and the column 'Specific activity a (units/mg protein)' prints the activity restated in the decoded line.

normalized_value_unit_evidence: K m: printed Table 1 cell 4.28 mM; the column head is K m (mM), so no conversion is needed and the paper value is 4.28 mM (the exported value is 4.28 mM). k cat: printed Table 1 cell 92.0 min-1; 1 min^-1 is 1/60 s^-1, so 92.0 / 60 = 1.5333333333333332 s^-1 (the exported value is 1.53 s^-1). k cat/K m: printed Table 1 cell 21.7 min-1 mM-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 21.7 / 60 = 0.36166666666666664 s^-1 mM^-1 (the exported value is 0.3574766355140187 s^-1 mM^-1).

raw_value_unit_evidence: Table 1 (Table 1: Kinetic parameters for L-proline, T4LHyp, and T3LHyp. (PLOS ONE 2015, PMID 25786142)), enzyme row 'TlProRW241F', substrate cell 'T4LHyp': column 'K m (mM)' = 4.28; column 'k cat (min-1)' = 92.0; column 'k cat/K m (min-1 mM-1)' = 21.7.

row_label: Table 1, row with enzyme 'TlProRW241F' and substrate 'T4LHyp'


organism: Ferroplasma acidarmanus

verification_status: unverified

sequence_variant_note: Mutation signature F420W references residue 420, which is outside the resolved sequence length.

status: unverified


column_label: PMC Table 1 row FaProR WT / T4LHyp gives Km 6.12 +/- 0.30 mM, kcat 2.37 +/- 0.10 min^-1, and kcat/Km 0.387 +/- 0.002 min^-1 mM^-1.

normalized_value_unit_evidence: kcat normalized_value=0.0395 normalized_unit=s^-1; Km normalized_value=6.12 normalized_unit=mM; kcat/Km normalized_value=0.00645 normalized_unit=s^-1 mM^-1

row_label: FaProR WT / T4LHyp

table_label: PMC Table 1 Kinetic parameters for L-proline, T4LHyp, and T3LHyp


enzyme_display_name: lysine racemase

organism: Oenococcus oeni

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04HB7 and applied mutation signature T224I to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; buffer KPB

column_label: Table I (Kinetic parameters of racemases), Lysine racemase block, enzyme form T224I, substrate Lys, direction D to L; column kcat (min^-1) = 17; column Km (mM) = 12; column kcat/Km (min^-1 mM^-1) = 1.4.

normalized_value_unit_evidence: kcat: printed Table I cell 17 min^-1; 1 min^-1 is 1/60 s^-1, so 17.0 / 60 = 0.2833333333333333 s^-1. Km: printed Table I cell 12 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 12.0 mM. kcat/Km: printed Table I cell 1.4 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 1.4 / 60 = 0.02333333333333333 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Lysine racemase block, enzyme form T224I, substrate Lys, direction D to L: kcat = 17 min^-1; Km = 12 mM; printed kcat/Km = 1.4 min^-1 mM^-1.

row_label: Table I, Lysine racemase block, enzyme form T224I row, substrate Lys, direction D to L

table_label: Table I: Kinetic parameters of racemases (J. Biochem. 2012, 152(6):505-508)

enzyme: lysine racemase


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04HB7 and applied mutation signature T224I/W355Y to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic parameters of racemases), Lysine racemase block, enzyme form T224I/W355Y, substrate Lys, direction D to L; column kcat (min^-1) = 8.9; column Km (mM) = 31; column kcat/Km (min^-1 mM^-1) = 0.29.

normalized_value_unit_evidence: kcat: printed Table I cell 8.9 min^-1; 1 min^-1 is 1/60 s^-1, so 8.9 / 60 = 0.14833333333333334 s^-1. Km: printed Table I cell 31 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 31.0 mM. kcat/Km: printed Table I cell 0.29 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.29 / 60 = 0.004833333333333333 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Lysine racemase block, enzyme form T224I/W355Y, substrate Lys, direction D to L: kcat = 8.9 min^-1; Km = 31 mM; printed kcat/Km = 0.29 min^-1 mM^-1.

row_label: Table I, Lysine racemase block, enzyme form T224I/W355Y row, substrate Lys, direction D to L


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q04HB7 and applied mutation signature W355Y to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic parameters of racemases), Lysine racemase block, enzyme form W355Y, substrate Lys, direction D to L; column kcat (min^-1) = 53; column Km (mM) = 21; column kcat/Km (min^-1 mM^-1) = 2.5.

normalized_value_unit_evidence: kcat: printed Table I cell 53 min^-1; 1 min^-1 is 1/60 s^-1, so 53.0 / 60 = 0.8833333333333333 s^-1. Km: printed Table I cell 21 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 21.0 mM. kcat/Km: printed Table I cell 2.5 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 2.5 / 60 = 0.041666666666666664 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Lysine racemase block, enzyme form W355Y, substrate Lys, direction D to L: kcat = 53 min^-1; Km = 21 mM; printed kcat/Km = 2.5 min^-1 mM^-1.

row_label: Table I, Lysine racemase block, enzyme form W355Y row, substrate Lys, direction D to L


column_label: Table I (Kinetic parameters of racemases), Lysine racemase block, enzyme form Wild-type, substrate Lys, direction D to L; column kcat (min^-1) = 1.7 x 10^2; column Km (mM) = 9.8; column kcat/Km (min^-1 mM^-1) = 17.

normalized_value_unit_evidence: kcat: printed Table I cell 1.7 x 10^2 min^-1; 1 min^-1 is 1/60 s^-1, so 170.0 / 60 = 2.8333333333333335 s^-1. Km: printed Table I cell 9.8 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 9.8 mM. kcat/Km: printed Table I cell 17 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 17.0 / 60 = 0.2833333333333333 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Lysine racemase block, enzyme form Wild-type, substrate Lys, direction D to L: kcat = 1.7 x 10^2 min^-1; Km = 9.8 mM; printed kcat/Km = 17 min^-1 mM^-1.

row_label: Table I, Lysine racemase block, enzyme form Wild-type row, substrate Lys, direction D to L


substrate_name: D-ornithine

column_label: Table I (Kinetic parameters of racemases), Lysine racemase block, enzyme form Wild-type, substrate Orn, direction D to L; column kcat (min^-1) = 1.1 x 10^2; column Km (mM) = 22; column kcat/Km (min^-1 mM^-1) = 5.0.

normalized_value_unit_evidence: kcat: printed Table I cell 1.1 x 10^2 min^-1; 1 min^-1 is 1/60 s^-1, so 110.00000000000001 / 60 = 1.8333333333333335 s^-1. Km: printed Table I cell 22 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 22.0 mM. kcat/Km: printed Table I cell 5.0 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 5.0 / 60 = 0.08333333333333333 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Lysine racemase block, enzyme form Wild-type, substrate Orn, direction D to L: kcat = 1.1 x 10^2 min^-1; Km = 22 mM; printed kcat/Km = 5.0 min^-1 mM^-1.

row_label: Table I, Lysine racemase block, enzyme form Wild-type row, substrate Orn, direction D to L

substrate: D-ornithine


column_label: Table I (Kinetic parameters of racemases), Lysine racemase block, enzyme form T224I, substrate Lys, direction L to D; column kcat (min^-1) = 19; column Km (mM) = 15; column kcat/Km (min^-1 mM^-1) = 1.5.

normalized_value_unit_evidence: kcat: printed Table I cell 19 min^-1; 1 min^-1 is 1/60 s^-1, so 19.0 / 60 = 0.31666666666666665 s^-1. Km: printed Table I cell 15 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 15.0 mM. kcat/Km: printed Table I cell 1.5 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 1.5 / 60 = 0.025 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Lysine racemase block, enzyme form T224I, substrate Lys, direction L to D: kcat = 19 min^-1; Km = 15 mM; printed kcat/Km = 1.5 min^-1 mM^-1.

row_label: Table I, Lysine racemase block, enzyme form T224I row, substrate Lys, direction L to D


column_label: Table I (Kinetic parameters of racemases), Lysine racemase block, enzyme form T224I/W355Y, substrate Lys, direction L to D; column kcat (min^-1) = 9.7; column Km (mM) = 27; column kcat/Km (min^-1 mM^-1) = 0.36.

normalized_value_unit_evidence: kcat: printed Table I cell 9.7 min^-1; 1 min^-1 is 1/60 s^-1, so 9.7 / 60 = 0.16166666666666665 s^-1. Km: printed Table I cell 27 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 27.0 mM. kcat/Km: printed Table I cell 0.36 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.36 / 60 = 0.006 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Lysine racemase block, enzyme form T224I/W355Y, substrate Lys, direction L to D: kcat = 9.7 min^-1; Km = 27 mM; printed kcat/Km = 0.36 min^-1 mM^-1.

row_label: Table I, Lysine racemase block, enzyme form T224I/W355Y row, substrate Lys, direction L to D


column_label: Table I (Kinetic parameters of racemases), Lysine racemase block, enzyme form W355Y, substrate Lys, direction L to D; column kcat (min^-1) = 62; column Km (mM) = 23; column kcat/Km (min^-1 mM^-1) = 2.7.

normalized_value_unit_evidence: kcat: printed Table I cell 62 min^-1; 1 min^-1 is 1/60 s^-1, so 62.0 / 60 = 1.0333333333333332 s^-1. Km: printed Table I cell 23 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 23.0 mM. kcat/Km: printed Table I cell 2.7 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 2.7 / 60 = 0.045000000000000005 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Lysine racemase block, enzyme form W355Y, substrate Lys, direction L to D: kcat = 62 min^-1; Km = 23 mM; printed kcat/Km = 2.7 min^-1 mM^-1.

row_label: Table I, Lysine racemase block, enzyme form W355Y row, substrate Lys, direction L to D


column_label: Table I (Kinetic parameters of racemases), Lysine racemase block, enzyme form Wild-type, substrate Lys, direction L to D; column kcat (min^-1) = 2.1 x 10^2; column Km (mM) = 11; column kcat/Km (min^-1 mM^-1) = 19.

normalized_value_unit_evidence: kcat: printed Table I cell 2.1 x 10^2 min^-1; 1 min^-1 is 1/60 s^-1, so 210.0 / 60 = 3.5 s^-1. Km: printed Table I cell 11 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 11.0 mM. kcat/Km: printed Table I cell 19 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 19.0 / 60 = 0.31666666666666665 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Lysine racemase block, enzyme form Wild-type, substrate Lys, direction L to D: kcat = 2.1 x 10^2 min^-1; Km = 11 mM; printed kcat/Km = 19 min^-1 mM^-1.

row_label: Table I, Lysine racemase block, enzyme form Wild-type row, substrate Lys, direction L to D


substrate_name: L-Ornithine

column_label: Table I (Kinetic parameters of racemases), Lysine racemase block, enzyme form Wild-type, substrate Orn, direction L to D; column kcat (min^-1) = 1.1 x 10^2; column Km (mM) = 27; column kcat/Km (min^-1 mM^-1) = 4.1.

normalized_value_unit_evidence: kcat: printed Table I cell 1.1 x 10^2 min^-1; 1 min^-1 is 1/60 s^-1, so 110.00000000000001 / 60 = 1.8333333333333335 s^-1. Km: printed Table I cell 27 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 27.0 mM. kcat/Km: printed Table I cell 4.1 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 4.1 / 60 = 0.06833333333333333 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Lysine racemase block, enzyme form Wild-type, substrate Orn, direction L to D: kcat = 1.1 x 10^2 min^-1; Km = 27 mM; printed kcat/Km = 4.1 min^-1 mM^-1.

row_label: Table I, Lysine racemase block, enzyme form Wild-type row, substrate Orn, direction L to D

substrate: L-Ornithine


organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

proof_lines: kcat is 69.63 sec(-1) for c4DHyp epimerization. kcat is 7.74 sec(-1) for t4LHyp epimerization.

source: uniprot


organism: Chromohalobacter israelensis (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11)

proof_lines: kcat is 0.070 sec(-1) for t4LHyp epimerization.


organism: Brucella abortus biovar 1 (strain 9-941)


organism: Brucella suis biovar 1 (strain 1330)


organism: Aeromonas caviae

substrate_name: L-Orn

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

proof_lines: D-Lys L-Orn

substrate: L-Orn


substrate_name: D-Ser

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

proof_lines: L-Lys L-Arg

substrate: D-Ser


organism: Escherichia coli (strain K12)

substrate_name: D,L-DAP (at pH 7.8 and at 25 degrees Celsius)


substrate_name: D-Lys

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

substrate: D-Lys


substrate_name: L-Met

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

substrate: L-Met


organism: Brevibacillus brevis


substrate_name: L-Tyr

substrate: L-Tyr


organism: Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / CCUG 213 / NBRC 12614 / NCIMB 9131 / NCTC 9757 / MK)

proof_lines: kcat is 70 sec(-1) for t4LHyp epimerization. kcat is 30 sec(-1) for t3LHyp epimerization.


organism: Pseudomonas putida

substrate_name: D-Gln

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

substrate: D-Gln


substrate_name: D-Asn

proof_lines: pure lyophilisates, 20°C, pH 7, Vmax: 770 micromol/min/g

proof_lines: pure lyophilisates, 20°C, pH 7, Vmax: 1626 micromol/min/g

proof_lines: pure lyophilisates, 25°C, pH 7, Vmax: 2427 micromol/min/g

substrate: D-Asn


substrate_name: D-Phe

substrate: D-Phe


substrate_name: L-ethionine

substrate: L-ethionine


enzyme_display_name: adenylate cyclase

organism: Mus musculus

substrate_name: ATP

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines: Sf9, Mn2+, pH 7.4, 37°C, 100 microM forskolin, 10 mM NaF, 10 microM AlCl3

proof_lines: S49 cyc-, pH 7.4, 37°C, Mn2+, 100 microM forskolin

enzyme: adenylate cyclase

substrate: ATP


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines: Sf9, Mn2+, 100 microM forskolin, 10 mM NaF, 10 microM AlCl3

substrate: Unknown


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


organism: Escherichia coli

substrate_name: meso-diaminoheptanedioate


substrate_name: LL-diaminoheptanedioate

substrate: LL-diaminoheptanedioate


enzyme_display_name: selenocysteine lyase

substrate_name: L-cysteine sulfinate

enzyme: selenocysteine lyase

substrate: L-cysteine sulfinate


substrate_name: L-selenocysteine

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

substrate: L-selenocysteine


organism: Brucella melitensis biotype 1 (strain ATCC 23456 / CCUG 17765 / NCTC 10094 / 16M)


substrate_name: L-Proline

verification_status: verified

column_label: Table 2 (PDF page 9 of 32); cluster 2; locus tag `Pput_1285`; UniProt `A5VZY6`; Function sub-row `ProR`; columns kcat [s-1] = `2.8 +/- 0.1`, KM [mM] = `200 +/- 20`, kcat/KM[M-1s-1] = `14`.

normalized_value_unit_evidence: kcat 2.8 s^-1 = 2.8 s^-1 (no conversion; the paper's kcat column is already s^-1). Km 200 mM = 200 mM (no conversion; the paper's KM column is already mM). kcat/Km: the paper prints 14 M^-1 s^-1, converted as 14 / 1000 = 0.014 s^-1 mM^-1; the catalog holds 0.013999999999999999 s^-1 mM^-1, which is the exact quotient of the paper's own printed cells (2.8 / 200 = 0.013999999999999999), so the two agree to the two-significant-figure precision the paper prints its ratio column in.

row_label: Pput_1285 / A5VZY6 / ProR (Table 2 cluster 2)

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

substrate: L-Proline

status: verified


column_label: Table 2 (PDF page 9 of 32); cluster 2; row group `Pput_1285 | A5VZY6`; Function sub-row `4HypE`; columns kcat [s-1] = `26`, KM [mM] = `0.54`, kcat/KM[M-1s-1] = `48000`.

normalized_value_unit_evidence: kcat: printed cell 26 s^-1 -> 26.0 s^(-1); the export holds 26.0 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 0.54 mM -> 0.54 mM; the export holds 0.54 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 48000 M^-1 s^-1 converted as 48000 / 1000 = 48.0 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 48.148148148148145 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `Pput_1285 | A5VZY6`, sub-row `4HypE`: kcat = 26 s^-1; KM = 0.54 mM; kcat/KM = 48000 M^-1 s^-1.

row_label: Pput_1285 | A5VZY6 / 4HypE (Table 2 cluster 2)


column_label: Table 2 (PDF page 9 of 32); cluster 2; row group `Pput_1285 | A5VZY6`; Function sub-row `3HypE`; columns kcat [s-1] = `4.8`, KM [mM] = `19`, kcat/KM[M-1s-1] = `250`.

normalized_value_unit_evidence: kcat: printed cell 4.8 s^-1 -> 4.8 s^(-1); the export holds 4.8 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 19 mM -> 19.0 mM; the export holds 19.0 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 250 M^-1 s^-1 converted as 250 / 1000 = 0.25 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 0.25263157894736843 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `Pput_1285 | A5VZY6`, sub-row `3HypE`: kcat = 4.8 s^-1; KM = 19 mM; kcat/KM = 250 M^-1 s^-1.

row_label: Pput_1285 | A5VZY6 / 3HypE (Table 2 cluster 2)


organism: Chromobacterium violaceum

column_label: Table 2 (PDF page 9 of 32); cluster 2; row group `CV_2826 | Q7NU77`; Function sub-row `4HypE`; columns kcat [s-1] = `70`, KM [mM] = `6.8`, kcat/KM[M-1s-1] = `10000`.

normalized_value_unit_evidence: kcat: printed cell 70 s^-1 -> 70.0 s^(-1); the export holds 70.0 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 6.8 mM -> 6.8 mM; the export holds 6.8 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 10000 M^-1 s^-1 converted as 10000 / 1000 = 10.0 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 10.294117647058824 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `CV_2826 | Q7NU77`, sub-row `4HypE`: kcat = 70 s^-1; KM = 6.8 mM; kcat/KM = 10000 M^-1 s^-1.

row_label: CV_2826 | Q7NU77 / 4HypE (Table 2 cluster 2)


column_label: Table 2 (PDF page 9 of 32); cluster 2; row group `CV_2826 | Q7NU77`; Function sub-row `3HypE`; columns kcat [s-1] = `30`, KM [mM] = `57`, kcat/KM[M-1s-1] = `520`.

normalized_value_unit_evidence: kcat: printed cell 30 s^-1 -> 30.0 s^(-1); the export holds 30.0 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 57 mM -> 57.0 mM; the export holds 57.0 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 520 M^-1 s^-1 converted as 520 / 1000 = 0.52 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 0.5263157894736842 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `CV_2826 | Q7NU77`, sub-row `3HypE`: kcat = 30 s^-1; KM = 57 mM; kcat/KM = 520 M^-1 s^-1.

row_label: CV_2826 | Q7NU77 / 3HypE (Table 2 cluster 2)


substrate_name: L-Phe

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

substrate: L-Phe


organism: Agrobacterium tumefaciens

column_label: Table 2 (PDF page 9 of 32); cluster 3; locus tag `Atu4684`; UniProt `A9CH01`; Function sub-row `4HypE`; columns kcat [s-1] = `0.40 +/- 0.02`, KM [mM] = `2.0 +/- 0.3`, kcat/KM[M-1s-1] = `200`.

normalized_value_unit_evidence: kcat 0.40 s^-1 = 0.40 s^-1 (no conversion; the paper's kcat column is already s^-1). Km 2.0 mM = 2.0 mM (no conversion; the paper's KM column is already mM). kcat/Km: the paper prints 200 M^-1 s^-1, converted as 200 / 1000 = 0.2 s^-1 mM^-1; the catalog holds 0.2 s^-1 mM^-1, which is the exact quotient of the paper's own printed cells (0.40 / 2.0 = 0.2), so the two agree to the two-significant-figure precision the paper prints its ratio column in.

row_label: Atu4684 / A9CH01 / 4HypE (Table 2 cluster 3)


column_label: Table 2 (PDF page 10 of 32); cluster 9; row group `Atu0398 | A9CKB4`; Function sub-row `4HypE`; columns kcat [s-1] = `0.86`, KM [mM] = `4.6`, kcat/KM[M-1s-1] = `190`.

normalized_value_unit_evidence: kcat: printed cell 0.86 s^-1 -> 0.86 s^(-1); the export holds 0.86 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 4.6 mM -> 4.6 mM; the export holds 4.6 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 190 M^-1 s^-1 converted as 190 / 1000 = 0.19 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 0.18695652173913044 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `Atu0398 | A9CKB4`, sub-row `4HypE`: kcat = 0.86 s^-1; KM = 4.6 mM; kcat/KM = 190 M^-1 s^-1.

row_label: Atu0398 | A9CKB4 / 4HypE (Table 2 cluster 9)


column_label: Table 2 (PDF page 9 of 32); cluster 9; locus tag `Atu0398`; UniProt `A9CKB4`; Function sub-row `3HypE`; columns kcat [s-1] = `4.0 +/- 0.6`, KM [mM] = `25 +/- 7`, kcat/KM[M-1s-1] = `160`.

normalized_value_unit_evidence: kcat 4.0 s^-1 = 4.0 s^-1 (no conversion; the paper's kcat column is already s^-1). Km 25 mM = 25 mM (no conversion; the paper's KM column is already mM). kcat/Km: the paper prints 160 M^-1 s^-1, converted as 160 / 1000 = 0.16 s^-1 mM^-1; the catalog holds 0.16 s^-1 mM^-1, which is the exact quotient of the paper's own printed cells (4.0 / 25 = 0.16), so the two agree to the two-significant-figure precision the paper prints its ratio column in.

row_label: Atu0398 / A9CKB4 / 3HypE (Table 2 cluster 9)


enzyme_display_name: UniProt Q6L2R8

organism: Picrophilus torridus

substrate_name: D-Aspartate

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q6L2R8

substrate: D-Aspartate


enzyme_display_name: isopenicillin-N epimerase

organism: Amycolatopsis lactamdurans

substrate_name: isopenicillin N

enzyme: isopenicillin-N epimerase

substrate: isopenicillin N


organism: Rhizobium etli

column_label: Table 2 (PDF page 10 of 32); cluster 9; row group `RHE_CH00452 | Q2KD13`; Function sub-row `4HypE`; columns kcat [s-1] = `1.9`, KM [mM] = `2.1`, kcat/KM[M-1s-1] = `880`.

normalized_value_unit_evidence: kcat: printed cell 1.9 s^-1 -> 1.9 s^(-1); the export holds 1.9 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 2.1 mM -> 2.1 mM; the export holds 2.1 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 880 M^-1 s^-1 converted as 880 / 1000 = 0.88 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 0.9047619047619047 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `RHE_CH00452 | Q2KD13`, sub-row `4HypE`: kcat = 1.9 s^-1; KM = 2.1 mM; kcat/KM = 880 M^-1 s^-1.

row_label: RHE_CH00452 | Q2KD13 / 4HypE (Table 2 cluster 9)


column_label: Table 2 (PDF page 10 of 32); cluster 9; row group `RHE_CH00452 | Q2KD13`; Function sub-row `3HypE`; columns kcat [s-1] = `0.94`, KM [mM] = `2.1`, kcat/KM[M-1s-1] = `450`.

normalized_value_unit_evidence: kcat: printed cell 0.94 s^-1 -> 0.94 s^(-1); the export holds 0.94 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 2.1 mM -> 2.1 mM; the export holds 2.1 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 450 M^-1 s^-1 converted as 450 / 1000 = 0.45 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 0.4476190476190476 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `RHE_CH00452 | Q2KD13`, sub-row `3HypE`: kcat = 0.94 s^-1; KM = 2.1 mM; kcat/KM = 450 M^-1 s^-1.

row_label: RHE_CH00452 | Q2KD13 / 3HypE (Table 2 cluster 9)


organism: Bacillus cereus

column_label: Table 2 (PDF page 10 of 32); cluster 5; row group `BCE_0994 | Q73CS0`; Function sub-row `4HypE`; columns kcat [s-1] = `1.2`, KM [mM] = `3.2`, kcat/KM[M-1s-1] = `370`.

normalized_value_unit_evidence: kcat: printed cell 1.2 s^-1 -> 1.2 s^(-1); the export holds 1.2 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 3.2 mM -> 3.2 mM; the export holds 3.2 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 370 M^-1 s^-1 converted as 370 / 1000 = 0.37 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 0.37499999999999994 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `BCE_0994 | Q73CS0`, sub-row `4HypE`: kcat = 1.2 s^-1; KM = 3.2 mM; kcat/KM = 370 M^-1 s^-1.

row_label: BCE_0994 | Q73CS0 / 4HypE (Table 2 cluster 5)


organism: Agrobacterium vitis

assay_conditions_summary: pH 8; 298.15 K; buffer pH 8

column_label: Official eLife HTML Table 2 row Avi_0518 / B9JQV3 / 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=1.3 normalized_unit=s^-1; Km normalized_value=5.6 normalized_unit=mM; kcat/KM normalized_value=0.23 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.3 +/- 0.07 raw_unit=s^-1; Km raw_value=5.6 +/- 0.5 raw_unit=mM; kcat/KM raw_value=230 raw_unit=M^-1 s^-1

row_label: Avi_0518 / B9JQV3 / 4HypE


column_label: Official eLife HTML Table 2 row Avi_0518 / B9JQV3 / 3HypE; 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=0.75 normalized_unit=s^-1; Km normalized_value=4.8 normalized_unit=mM; kcat/KM normalized_value=0.16 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.75 +/- 0.04 raw_unit=s^-1; Km raw_value=4.8 +/- 0.9 raw_unit=mM; kcat/KM raw_value=160 raw_unit=M^-1 s^-1

row_label: Avi_0518 / B9JQV3 / 3HypE


organism: Burkholderia thailandensis

column_label: Table 2 (PDF page 9 of 32); cluster 2; row group `BTH_II2067 | Q2T3J4`; Function sub-row `4HypE`; columns kcat [s-1] = `40`, KM [mM] = `1.4`, kcat/KM[M-1s-1] = `28000`.

normalized_value_unit_evidence: kcat: printed cell 40 s^-1 -> 40.0 s^(-1); the export holds 40.0 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 1.4 mM -> 1.4 mM; the export holds 1.4 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 28000 M^-1 s^-1 converted as 28000 / 1000 = 28.0 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 28.571428571428573 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `BTH_II2067 | Q2T3J4`, sub-row `4HypE`: kcat = 40 s^-1; KM = 1.4 mM; kcat/KM = 28000 M^-1 s^-1.

row_label: BTH_II2067 | Q2T3J4 / 4HypE (Table 2 cluster 2)


enzyme_display_name: 2-aminohexano-6-lactam racemase

organism: Ensifer sp. 23-3

substrate_name: L-2-aminobutyric acid amide

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

enzyme: 2-aminohexano-6-lactam racemase

substrate: L-2-aminobutyric acid amide


substrate_name: L-alanine amide

substrate: L-alanine amide


substrate_name: D-alanine amide

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

substrate: D-alanine amide


organism: Xanthomonas campestris

column_label: Official eLife HTML Table 2 row XCC2415 / Q8P833 / 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=28 normalized_unit=s^-1; Km normalized_value=0.67 normalized_unit=mM; kcat/KM normalized_value=42 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=28 +/- 0.4 raw_unit=s^-1; Km raw_value=0.67 +/- 0.05 raw_unit=mM; kcat/KM raw_value=42000 raw_unit=M^-1 s^-1


column_label: Table 2 (PDF page 9 of 32); cluster 2; row group `XCC2415 | Q8P833`; Function sub-row `3HypE`; columns kcat [s-1] = `1.3`, KM [mM] = `15`, kcat/KM[M-1s-1] = `86`.

normalized_value_unit_evidence: kcat: printed cell 1.3 s^-1 -> 1.3 s^(-1); the export holds 1.3 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 15 mM -> 15.0 mM; the export holds 15.0 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 86 M^-1 s^-1 converted as 86 / 1000 = 0.086 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 0.08666666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `XCC2415 | Q8P833`, sub-row `3HypE`: kcat = 1.3 s^-1; KM = 15 mM; kcat/KM = 86 M^-1 s^-1.

row_label: XCC2415 | Q8P833 / 3HypE (Table 2 cluster 2)


organism: Burkholderia pseudomallei (strain K96243)


organism: Ochrobactrum anthropi

column_label: Official eLife HTML Table 2 row Oant_0439 / A6WW16 / 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=0.064 normalized_unit=s^-1; Km normalized_value=1.3 normalized_unit=mM; kcat/KM normalized_value=0.049 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.064 +/- 0.002 raw_unit=s^-1; Km raw_value=1.3 +/- 0.2 raw_unit=mM; kcat/KM raw_value=49 raw_unit=M^-1 s^-1

row_label: Oant_0439 / A6WW16 / 4HypE


column_label: Table 2 (PDF page 9 of 32); cluster 1; row group `Oant_1111 | A6WXX7`; Function sub-row `4HypE`; columns kcat [s-1] = `89`, KM [mM] = `7.1`, kcat/KM[M-1s-1] = `13000`.

normalized_value_unit_evidence: kcat: printed cell 89 s^-1 -> 89.0 s^(-1); the export holds 89.0 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 7.1 mM -> 7.1 mM; the export holds 7.1 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 13000 M^-1 s^-1 converted as 13000 / 1000 = 13.0 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 12.535211267605634 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `Oant_1111 | A6WXX7`, sub-row `4HypE`: kcat = 89 s^-1; KM = 7.1 mM; kcat/KM = 13000 M^-1 s^-1.

row_label: Oant_1111 | A6WXX7 / 4HypE (Table 2 cluster 1)


column_label: Table 2 (PDF page 9 of 32); cluster 1; row group `Oant_1111 | A6WXX7`; Function sub-row `3HypE`; columns kcat [s-1] = `2.4`, KM [mM] = `31`, kcat/KM[M-1s-1] = `77`.

normalized_value_unit_evidence: kcat: printed cell 2.4 s^-1 -> 2.4 s^(-1); the export holds 2.4 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 31 mM -> 31.0 mM; the export holds 31.0 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 77 M^-1 s^-1 converted as 77 / 1000 = 0.077 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 0.07741935483870968 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `Oant_1111 | A6WXX7`, sub-row `3HypE`: kcat = 2.4 s^-1; KM = 31 mM; kcat/KM = 77 M^-1 s^-1.

row_label: Oant_1111 | A6WXX7 / 3HypE (Table 2 cluster 1)


enzyme_display_name: aspartate racemase

organism: Acropora millepora

substrate_name: L-aspartate

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

proof_lines: recombinant His-tagged mutant P150S, pH 8.0, 30°C

enzyme: aspartate racemase

substrate: L-aspartate


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


organism: Saccoglossus kowalevskii

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication, wild-type enzyme, Asp/GluR enzyme

proof_lines: wild-type enzyme, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme

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


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme A156S, Asp/GluR enzyme

proof_lines: mutant enzyme A156S, pH 8.0, temperature not specified in the publication, Asp/GluR enzyme


substrate_name: L-glutamate

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

substrate: L-glutamate


substrate_name: D-glutamate

substrate: D-glutamate


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme S156A, AspR enzyme


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme AS56A, AspR enzyme


organism: Manihot esculenta

substrate_name: L-serine

proof_lines: pH 8.0, temperature not specified in the publication

substrate: L-serine


substrate_name: L-Glutamic acid

substrate: L-Glutamic acid


organism: Solanum lycopersicum


organism: Sphagnum girgensohnii


organism: Magallana gigas

proof_lines: recombinant His-tagged mutant S150P/S151P/S152Y, pH 8.0, 30°C


organism: Spirogyra pratensis


organism: Brucella melitensis biotype 1

column_label: Official eLife HTML Table 2 row BMEI1586 / D0B556 / 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=0.082 normalized_unit=s^-1; Km normalized_value=4.5 normalized_unit=mM; kcat/KM normalized_value=0.018 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.082 +/- 0.005 raw_unit=s^-1; Km raw_value=4.5 +/- 1 raw_unit=mM; kcat/KM raw_value=18 raw_unit=M^-1 s^-1


column_label: Table 2 (PDF page 9 of 32); cluster 3; row group `BMEI1586 | D0B556`; Function sub-row `3HypE`; columns kcat [s-1] = `0.085`, KM [mM] = `2.6`, kcat/KM[M-1s-1] = `33`.

normalized_value_unit_evidence: kcat: printed cell 0.085 s^-1 -> 0.085 s^(-1); the export holds 0.085 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 2.6 mM -> 2.6 mM; the export holds 2.6 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 33 M^-1 s^-1 converted as 33 / 1000 = 0.033 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 0.032692307692307694 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `BMEI1586 | D0B556`, sub-row `3HypE`: kcat = 0.085 s^-1; KM = 2.6 mM; kcat/KM = 33 M^-1 s^-1.

row_label: BMEI1586 | D0B556 / 3HypE (Table 2 cluster 3)


enzyme_display_name: serine racemase

organism: Clostridioides difficile

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

enzyme: serine racemase


organism: Streptomyces garyphalus


substrate_name: L-alanine

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

substrate: L-alanine


proof_lines: pH 8.0, 30°C, recombinant mutant P150S/P151S/F152S


substrate_name: D-serine

proof_lines: pH 8.0, 30°C, recombinant mutant P151S/F152S

substrate: D-serine


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


organism: Mus musculus


organism: Penaeus monodon


organism: Aplysia californica


organism: Enterococcus faecalis

substrate_name: L-Asp

substrate: L-Asp


organism: Macrostomum lignano


organism: Anneissia japonica


organism: Streptococcus thermophilus

proof_lines: recombinant enzyme, pH 8.3, 37°C, coupling method assay


organism: Actinomyces sp.


organism: Amphimedon queenslandica


organism: Citreicella sp. SE45


organism: Bombyx mori


organism: Pyrococcus horikoshii

proof_lines: pH and temperature not specified in the publication


organism: Thermococcus litoralis


organism: Pyrobaculum islandicum

substrate_name: D-serine / L-serine

substrate: D-serine / L-serine


organism: Burkholderia multivorans

column_label: Table 2 (PDF page 10 of 32); cluster 12; row group `Bmul_4260 | A9AKG8`; Function sub-row `4HypE`; columns kcat [s-1] = `1.3`, KM [mM] = `2.7`, kcat/KM[M-1s-1] = `470`.

normalized_value_unit_evidence: kcat: printed cell 1.3 s^-1 -> 1.3 s^(-1); the export holds 1.3 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 2.7 mM -> 2.7 mM; the export holds 2.7 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 470 M^-1 s^-1 converted as 470 / 1000 = 0.47 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 0.48148148148148145 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `Bmul_4260 | A9AKG8`, sub-row `4HypE`: kcat = 1.3 s^-1; KM = 2.7 mM; kcat/KM = 470 M^-1 s^-1.

row_label: Bmul_4260 | A9AKG8 / 4HypE (Table 2 cluster 12)


column_label: Table 2 (PDF page 9 of 32); cluster 1; row group `Bmul_5265 | A9AQW9`; Function sub-row `4HypE`; columns kcat [s-1] = `5.6`, KM [mM] = `11`, kcat/KM[M-1s-1] = `530`.

normalized_value_unit_evidence: kcat: printed cell 5.6 s^-1 -> 5.6 s^(-1); the export holds 5.6 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 11 mM -> 11.0 mM; the export holds 11.0 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 530 M^-1 s^-1 converted as 530 / 1000 = 0.53 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 0.509090909090909 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `Bmul_5265 | A9AQW9`, sub-row `4HypE`: kcat = 5.6 s^-1; KM = 11 mM; kcat/KM = 530 M^-1 s^-1.

row_label: Bmul_5265 | A9AQW9 / 4HypE (Table 2 cluster 1)


column_label: Table 2 (PDF page 10 of 32); cluster 12; row group `Bmul_4260 | A9AKG8`; Function sub-row `3HypE`; columns kcat [s-1] = `30`, KM [mM] = `18`, kcat/KM[M-1s-1] = `1700`.

normalized_value_unit_evidence: kcat: printed cell 30 s^-1 -> 30.0 s^(-1); the export holds 30.0 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 18 mM -> 18.0 mM; the export holds 18.0 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 1700 M^-1 s^-1 converted as 1700 / 1000 = 1.7 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 1.6666666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row group `Bmul_4260 | A9AKG8`, sub-row `3HypE`: kcat = 30 s^-1; KM = 18 mM; kcat/KM = 1700 M^-1 s^-1.

row_label: Bmul_4260 | A9AKG8 / 3HypE (Table 2 cluster 12)


organism: Acropora millepora

substrate_name: L-Aspartate

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

substrate: L-Aspartate


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

column_label: Table 1 row Acropora millepora AspR WT (PSS); d-Asp to l-Asp; Km column raw cell 1.37 mM; Kcat column raw cell 25300 x 10^-3 s^-1, normalized 25.3 s^-1; Kcat/Km column raw cell 18400 x 10^-3 s^-1*mM^-1, normalized 18.4 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=1.37 normalized_unit=mM; kcat normalized_value=25.3 normalized_unit=s^-1; kcat/Km normalized_value=18.4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=1.37 raw_unit=mM; Kcat raw_value=25300 raw_unit=10^-3 s^-1; Kcat/Km raw_value=18400 raw_unit=10^-3 s^-1*mM^-1

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


column_label: Table 1 row Acropora millepora AspR WT (PSS); l-Asp to d-Asp; Km column raw cell 3.11 mM; Kcat column raw cell 57700 x 10^-3 s^-1, normalized 57.7 s^-1; Kcat/Km column raw cell 18700 x 10^-3 s^-1*mM^-1, normalized 18.7 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=3.11 normalized_unit=mM; kcat normalized_value=57.7 normalized_unit=s^-1; kcat/Km normalized_value=18.7 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=3.11 raw_unit=mM; Kcat raw_value=57700 raw_unit=10^-3 s^-1; Kcat/Km raw_value=18700 raw_unit=10^-3 s^-1*mM^-1


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

organism: Bacillus subtilis

substrate_name: L-Ala-D-Met

proof_lines: The catalytic efficiency is 25-fold higher with L-Ala-D-Glu than with L-Ala-D-Asp or L-Ala-D-Met as substrate.

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

substrate: L-Ala-D-Met


substrate_name: L-Ala-D-Glu

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

substrate: L-Ala-D-Glu


substrate_name: L-Ala-D-Asp

substrate: L-Ala-D-Asp


organism: Picrophilus oshimae


organism: Anadara broughtonii

sequence: PVAPEYLFKKEEDKGANKEEEEVAPELGIRA

wild_type_sequence: PVAPEYLFKKEEDKGANKEEEEVAPELGIRA

assay_conditions_summary: pH 5.53; cofactor ATP

proof_lines:
pH 5.53, 2 mM ATP
pH 5.53, 1 mM ATP
pH 5.53


organism: Roseobacter litoralis

proof_lines: pH 8.0, 30°C, recombinant His-tagged enzyme


organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)

substrate_name: L-Ala-L-Glu

column_label: Table 1, B. thetaiotaomicron enzyme row group, substrate L-Ala-L-Glu, K_M [mM] cell 2.0 +/- 1.

raw_value_unit_evidence: Table 1 row B. thetaiotaomicron, substrate L-Ala-L-Glu: K_M raw_value=2.0 +/- 1 raw_unit=mM.

row_label: B. thetaiotaomicron dipeptide epimerase row: L-Ala-L-Glu

table_label: PMC3306705 Table 1

substrate: L-Ala-L-Glu


substrate_name: L-Val-L-Glu

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

column_label: Table 1, B. thetaiotaomicron enzyme row group, substrate L-Val-L-Glu, K_M [mM] cell 1.7 +/- 0.2.

raw_value_unit_evidence: Table 1 row B. thetaiotaomicron, substrate L-Val-L-Glu: K_M raw_value=1.7 +/- 0.2 raw_unit=mM.

row_label: B. thetaiotaomicron dipeptide epimerase row: L-Val-L-Glu

substrate: L-Val-L-Glu


organism: Achromobacter obae


substrate_name: L-Val-D-Glu

proof_lines: kcat is 147 sec(-1) for epimerization of L-Ala-L-Glu. kcat is 59 sec(-1) for epimerization of L-Ala-D-Glu. kcat is 96 sec(-1) for epimerization of L-Val-L-Glu. kcat is 43 sec(-1) for epimerization of L-Val-D-Glu. kcat is 30 sec(-1) for epim

substrate: L-Val-D-Glu


organism: Penaeus monodon

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0U4MRI4 and applied mutation signature H150S/P151S/F152S with inferred residue-numbering offset -1 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 'l-Ser to d-Ser' of the Penaeus monodon SerR H150S/P151S/F152S (SSS) block: Km = 125, Kcat = 33.5, Kcat/Km = 0.268, v = 0.258.

normalized_value_unit_evidence: Km: printed Table 1 cell 125 under the column head 'Km (mM)'; the printed unit is already mM, so no conversion is applied and the normalized value is 125.0 mM. kcat: printed Table 1 cell 33.5 under the column head 'Kcat (10^-3 s^-1)'; 33.5 x 10^-3 = 0.0335 s^(-1). kcat/Km: printed Table 1 cell 0.268 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 0.268 M^-1 s^-1, and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.268 x 0.001 = 0.000268 s^(-1)*mM^(-1). No min^-1, uM or M cell is involved in this row.

raw_value_unit_evidence: Table 1, Penaeus monodon SerR H150S/P151S/F152S (SSS) block, reaction row 'l-Ser to d-Ser': printed Km cell 125 under the column head 'Km (mM)'; printed Kcat cell 33.5 under the column head 'Kcat (10^-3 s^-1)'; printed Kcat/Km cell 0.268 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; printed v cell 0.258 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 Penaeus monodon SerR H150S/P151S/F152S (SSS) block

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


enzyme_display_name: O-ureido-serine racemase

organism: Streptomyces lavendulae subsp. lavendulae

substrate_name: O-ureido-D-serine

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

proof_lines: kcat is 158 sec(-1) and 29 sec(-1) for O-ureido-L-serine and O-ureido-D-serine, respectively (at 30 degrees Celsius).

source_databases_merged: brenda uniprot

enzyme: O-ureido-serine racemase

substrate: O-ureido-D-serine


substrate_name: Unknown

proof_lines:
pH 5.53, conversion of D-aspartate
pH 5.53, conversion of L-aspartate

substrate: Unknown


substrate_name: D-Aspartate

substrate: D-Aspartate


organism: Arabidopsis thaliana


organism: Schizosaccharomyces pombe


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T127A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58403 and applied mutation signature T84A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 343.15 K; buffer pH set

column_label: Table I (Kinetic Parameters of Mutant PhAspRs), journal page 505 (PDF page 4), D to L Direction group, row T84A; column Km (mM) = 2.6 x 10^-1; column kcat (min^-1) = 1.6 x 10^3; column kcat/Km = 6.0 x 10^3, the kcat/Km head printing no unit and the cell being in min^-1 mM^-1 by construction from the two neighbouring columns; the other three cells of the same printed row belong to the L to D Direction group, which is the L-Aspartate export row.

normalized_value_unit_evidence: Km: printed Table I cell 2.6 x 10^-1 mM = 0.26 mM, already in mM, no conversion applies; the export stores 0.26 mM. kcat: printed cell 1.6 x 10^3 min^-1 = 1600 min^-1; the printed turnover column is per MINUTE, so 1600 / 60 = 26.666666666666668 s^(-1); the export stores 26.667 s^(-1). kcat/Km: printed cell 6.0 x 10^3 = 6000 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 6000 / 60 = 100.0 s^(-1)*mM^(-1); the export stores 102.56538461538462 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I (journal page 505, PDF page 4), D to L Direction, row T84A: Km = 2.6 x 10^-1 mM; kcat = 1.6 x 10^3 min^-1; kcat/Km = 6.0 x 10^3 under the unit-less column head kcat/Km, in min^-1 mM^-1 by construction from the Km (mM) and kcat (min^-1) columns.

row_label: Table I, D to L Direction, row T84A

table_label: Table I: Kinetic Parameters of Mutant PhAspRs (Proteins 2006, 64(2):502-512), printed column heads WT | Km (mM) | kcat (min^-1) | kcat/Km | Km (mM) | kcat (min^-1) | kcat/Km under the two group heads L to D Direction and D to L Direction; the kcat/Km heads print no unit and their cells are in min^-1 mM^-1 by construction from the Km (mM) and kcat (min^-1) columns


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:O58403 and applied mutation signature C194A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters of Mutant PhAspRs), journal page 505 (PDF page 4), L to D Direction group, row C194A; column Km (mM) = 1.3; column kcat (min^-1) = 9.3 x 10^-1; column kcat/Km = 7.3 x 10^-1, the kcat/Km head printing no unit and the cell being in min^-1 mM^-1 by construction from the two neighbouring columns; the other three cells of the same printed row belong to the D to L Direction group, which is the D-Aspartate export row.

normalized_value_unit_evidence: Km: printed Table I cell 1.3 mM = 1.3 mM, already in mM, no conversion applies; the export stores 1.3 mM. kcat: printed cell 9.3 x 10^-1 min^-1 = 0.93 min^-1; the printed turnover column is per MINUTE, so 0.93 / 60 = 0.0155 s^(-1); the export stores 0.015 s^(-1). kcat/Km: printed cell 7.3 x 10^-1 = 0.73 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.73 / 60 = 0.012166666666666666 s^(-1)*mM^(-1); the export stores 0.011538461538461537 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I (journal page 505, PDF page 4), L to D Direction, row C194A: Km = 1.3 mM; kcat = 9.3 x 10^-1 min^-1; kcat/Km = 7.3 x 10^-1 under the unit-less column head kcat/Km, in min^-1 mM^-1 by construction from the Km (mM) and kcat (min^-1) columns.

row_label: Table I, L to D Direction, row C194A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58403 and applied mutation signature C82A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters of Mutant PhAspRs), journal page 505 (PDF page 4), L to D Direction group, row C82A; column Km (mM) = 1.8; column kcat (min^-1) = 4.0 x 10^-1; column kcat/Km = 2.2 x 10^-1, the kcat/Km head printing no unit and the cell being in min^-1 mM^-1 by construction from the two neighbouring columns; the other three cells of the same printed row belong to the D to L Direction group, which is the D-Aspartate export row.

normalized_value_unit_evidence: Km: printed Table I cell 1.8 mM = 1.8 mM, already in mM, no conversion applies; the export stores 1.8 mM. kcat: printed cell 4.0 x 10^-1 min^-1 = 0.4 min^-1; the printed turnover column is per MINUTE, so 0.4 / 60 = 0.006666666666666667 s^(-1); the export stores 0.007 s^(-1). kcat/Km: printed cell 2.2 x 10^-1 = 0.22 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.22 / 60 = 0.0036666666666666666 s^(-1)*mM^(-1); the export stores 0.0038888888888888888 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I (journal page 505, PDF page 4), L to D Direction, row C82A: Km = 1.8 mM; kcat = 4.0 x 10^-1 min^-1; kcat/Km = 2.2 x 10^-1 under the unit-less column head kcat/Km, in min^-1 mM^-1 by construction from the Km (mM) and kcat (min^-1) columns.

row_label: Table I, L to D Direction, row C82A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58403 and applied mutation signature K164A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters of Mutant PhAspRs), journal page 505 (PDF page 4), L to D Direction group, row K164A; column Km (mM) = 2.3 x 10^2; column kcat (min^-1) = 1.0 x 10^1; column kcat/Km = 4.6 x 10^-2, the kcat/Km head printing no unit and the cell being in min^-1 mM^-1 by construction from the two neighbouring columns; the other three cells of the same printed row belong to the D to L Direction group, which is the D-Aspartate export row. Cells printed with a bare ten are written with their implicit exponent made explicit (printed 1.0 x 10, written 1.0 x 10^1); the value is unchanged.

normalized_value_unit_evidence: Km: printed Table I cell 2.3 x 10^2 mM = 230 mM, already in mM, no conversion applies; the export stores 230.0 mM. kcat: printed cell 1.0 x 10^1 min^-1 = 10 min^-1; the printed turnover column is per MINUTE, so 10 / 60 = 0.16666666666666666 s^(-1); the export stores 0.167 s^(-1). kcat/Km: printed cell 4.6 x 10^-2 = 0.046 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.046 / 60 = 0.0007666666666666667 s^(-1)*mM^(-1); the export stores 0.0007260869565217391 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I (journal page 505, PDF page 4), L to D Direction, row K164A: Km = 2.3 x 10^2 mM; kcat = 1.0 x 10^1 min^-1; kcat/Km = 4.6 x 10^-2 under the unit-less column head kcat/Km, in min^-1 mM^-1 by construction from the Km (mM) and kcat (min^-1) columns. Cells printed with a bare ten are written with their implicit exponent made explicit (printed 1.0 x 10, written 1.0 x 10^1); the value is unchanged.

row_label: Table I, L to D Direction, row K164A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58403 and applied mutation signature K164L to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters of Mutant PhAspRs), journal page 505 (PDF page 4), L to D Direction group, row K164L; column Km (mM) = 4.3; column kcat (min^-1) = 2.8 x 10^1; column kcat/Km = 6.6, the kcat/Km head printing no unit and the cell being in min^-1 mM^-1 by construction from the two neighbouring columns; the other three cells of the same printed row belong to the D to L Direction group, which is the D-Aspartate export row. Cells printed with a bare ten are written with their implicit exponent made explicit (printed 2.8 x 10, written 2.8 x 10^1); the value is unchanged.

normalized_value_unit_evidence: Km: printed Table I cell 4.3 mM = 4.3 mM, already in mM, no conversion applies; the export stores 4.3 mM. kcat: printed cell 2.8 x 10^1 min^-1 = 28 min^-1; the printed turnover column is per MINUTE, so 28 / 60 = 0.4666666666666667 s^(-1); the export stores 0.467 s^(-1). kcat/Km: printed cell 6.6 = 6.6 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 6.6 / 60 = 0.10999999999999999 s^(-1)*mM^(-1); the export stores 0.10860465116279071 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I (journal page 505, PDF page 4), L to D Direction, row K164L: Km = 4.3 mM; kcat = 2.8 x 10^1 min^-1; kcat/Km = 6.6 under the unit-less column head kcat/Km, in min^-1 mM^-1 by construction from the Km (mM) and kcat (min^-1) columns. Cells printed with a bare ten are written with their implicit exponent made explicit (printed 2.8 x 10, written 2.8 x 10^1); the value is unchanged.

row_label: Table I, L to D Direction, row K164L


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K164R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58403 and applied mutation signature N83G to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters of Mutant PhAspRs), journal page 505 (PDF page 4), L to D Direction group, row N83G; column Km (mM) = 3.9; column kcat (min^-1) = 2.4 x 10^4; column kcat/Km = 6.1 x 10^3, the kcat/Km head printing no unit and the cell being in min^-1 mM^-1 by construction from the two neighbouring columns; the other three cells of the same printed row belong to the D to L Direction group, which is the D-Aspartate export row.

normalized_value_unit_evidence: Km: printed Table I cell 3.9 mM = 3.9 mM, already in mM, no conversion applies; the export stores 3.9 mM. kcat: printed cell 2.4 x 10^4 min^-1 = 24000 min^-1; the printed turnover column is per MINUTE, so 24000 / 60 = 400.0 s^(-1); the export stores 400.0 s^(-1). kcat/Km: printed cell 6.1 x 10^3 = 6100 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 6100 / 60 = 101.66666666666667 s^(-1)*mM^(-1); the export stores 102.56410256410257 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I (journal page 505, PDF page 4), L to D Direction, row N83G: Km = 3.9 mM; kcat = 2.4 x 10^4 min^-1; kcat/Km = 6.1 x 10^3 under the unit-less column head kcat/Km, in min^-1 mM^-1 by construction from the Km (mM) and kcat (min^-1) columns.

row_label: Table I, L to D Direction, row N83G


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58403 and applied mutation signature R48I to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters of Mutant PhAspRs), journal page 505 (PDF page 4), L to D Direction group, row R48I; column Km (mM) = 3.0 x 10^2; column kcat (min^-1) = 1.0 x 10^2; column kcat/Km = 3.5 x 10^-1, the kcat/Km head printing no unit and the cell being in min^-1 mM^-1 by construction from the two neighbouring columns; the other three cells of the same printed row belong to the D to L Direction group, which is the D-Aspartate export row.

normalized_value_unit_evidence: Km: printed Table I cell 3.0 x 10^2 mM = 300 mM, already in mM, no conversion applies; the export stores 300.0 mM. kcat: printed cell 1.0 x 10^2 min^-1 = 100 min^-1; the printed turnover column is per MINUTE, so 100 / 60 = 1.6666666666666667 s^(-1); the export stores 1.667 s^(-1). kcat/Km: printed cell 3.5 x 10^-1 = 0.35 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.35 / 60 = 0.005833333333333333 s^(-1)*mM^(-1); the export stores 0.005556666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I (journal page 505, PDF page 4), L to D Direction, row R48I: Km = 3.0 x 10^2 mM; kcat = 1.0 x 10^2 min^-1; kcat/Km = 3.5 x 10^-1 under the unit-less column head kcat/Km, in min^-1 mM^-1 by construction from the Km (mM) and kcat (min^-1) columns.

row_label: Table I, L to D Direction, row R48I


column_label: Table I (Kinetic Parameters of Mutant PhAspRs), journal page 505 (PDF page 4), D to L Direction group, row C194A; column Km (mM) = 4.5 x 10^-1; column kcat (min^-1) = 1.4 x 10^-1; column kcat/Km = 3.0 x 10^-1, the kcat/Km head printing no unit and the cell being in min^-1 mM^-1 by construction from the two neighbouring columns; the other three cells of the same printed row belong to the L to D Direction group, which is the L-Aspartate export row.

normalized_value_unit_evidence: Km: printed Table I cell 4.5 x 10^-1 mM = 0.45 mM, already in mM, no conversion applies; the export stores 0.45 mM. kcat: printed cell 1.4 x 10^-1 min^-1 = 0.14 min^-1; the printed turnover column is per MINUTE, so 0.14 / 60 = 0.0023333333333333335 s^(-1); the export stores 0.002 s^(-1). kcat/Km: printed cell 3.0 x 10^-1 = 0.3 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.3 / 60 = 0.005 s^(-1)*mM^(-1); the export stores 0.0044444444444444444 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I (journal page 505, PDF page 4), D to L Direction, row C194A: Km = 4.5 x 10^-1 mM; kcat = 1.4 x 10^-1 min^-1; kcat/Km = 3.0 x 10^-1 under the unit-less column head kcat/Km, in min^-1 mM^-1 by construction from the Km (mM) and kcat (min^-1) columns.

row_label: Table I, D to L Direction, row C194A


column_label: Table I (Kinetic Parameters of Mutant PhAspRs), journal page 505 (PDF page 4), D to L Direction group, row C82A; column Km (mM) = 3.6; column kcat (min^-1) = 1.6 x 10^-1; column kcat/Km = 4.5 x 10^-2, the kcat/Km head printing no unit and the cell being in min^-1 mM^-1 by construction from the two neighbouring columns; the other three cells of the same printed row belong to the L to D Direction group, which is the L-Aspartate export row.

normalized_value_unit_evidence: Km: printed Table I cell 3.6 mM = 3.6 mM, already in mM, no conversion applies; the export stores 3.6 mM. kcat: printed cell 1.6 x 10^-1 min^-1 = 0.16 min^-1; the printed turnover column is per MINUTE, so 0.16 / 60 = 0.0026666666666666666 s^(-1); the export stores 0.003 s^(-1). kcat/Km: printed cell 4.5 x 10^-2 = 0.045 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.045 / 60 = 0.00075 s^(-1)*mM^(-1); the export stores 0.0008333333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I (journal page 505, PDF page 4), D to L Direction, row C82A: Km = 3.6 mM; kcat = 1.6 x 10^-1 min^-1; kcat/Km = 4.5 x 10^-2 under the unit-less column head kcat/Km, in min^-1 mM^-1 by construction from the Km (mM) and kcat (min^-1) columns.

row_label: Table I, D to L Direction, row C82A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K164A to reconstruct the assayed variant sequence.


column_label: Table I (Kinetic Parameters of Mutant PhAspRs), journal page 505 (PDF page 4), D to L Direction group, row K164L; column Km (mM) = 5.4; column kcat (min^-1) = 2.6 x 10^1; column kcat/Km = 4.9, the kcat/Km head printing no unit and the cell being in min^-1 mM^-1 by construction from the two neighbouring columns; the other three cells of the same printed row belong to the L to D Direction group, which is the L-Aspartate export row. Cells printed with a bare ten are written with their implicit exponent made explicit (printed 2.6 x 10, written 2.6 x 10^1); the value is unchanged.

normalized_value_unit_evidence: Km: printed Table I cell 5.4 mM = 5.4 mM, already in mM, no conversion applies; the export stores 5.4 mM. kcat: printed cell 2.6 x 10^1 min^-1 = 26 min^-1; the printed turnover column is per MINUTE, so 26 / 60 = 0.43333333333333335 s^(-1); the export stores 0.433 s^(-1). kcat/Km: printed cell 4.9 = 4.9 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 4.9 / 60 = 0.08166666666666667 s^(-1)*mM^(-1); the export stores 0.08018518518518518 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I (journal page 505, PDF page 4), D to L Direction, row K164L: Km = 5.4 mM; kcat = 2.6 x 10^1 min^-1; kcat/Km = 4.9 under the unit-less column head kcat/Km, in min^-1 mM^-1 by construction from the Km (mM) and kcat (min^-1) columns. Cells printed with a bare ten are written with their implicit exponent made explicit (printed 2.6 x 10, written 2.6 x 10^1); the value is unchanged.

row_label: Table I, D to L Direction, row K164L


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58403 and applied mutation signature K164R to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters of Mutant PhAspRs), journal page 505 (PDF page 4), D to L Direction group, row K164R; column Km (mM) = 3.1 x 10^1; column kcat (min^-1) = 1.1 x 10^1; column kcat/Km = 3.4 x 10^-1, the kcat/Km head printing no unit and the cell being in min^-1 mM^-1 by construction from the two neighbouring columns; the other three cells of the same printed row belong to the L to D Direction group, which is the L-Aspartate export row. Cells printed with a bare ten are written with their implicit exponent made explicit (printed 3.1 x 10, written 3.1 x 10^1; printed 1.1 x 10, written 1.1 x 10^1); the value is unchanged.

normalized_value_unit_evidence: Km: printed Table I cell 3.1 x 10^1 mM = 31 mM, already in mM, no conversion applies; the export stores 31.0 mM. kcat: printed cell 1.1 x 10^1 min^-1 = 11 min^-1; the printed turnover column is per MINUTE, so 11 / 60 = 0.18333333333333332 s^(-1); the export stores 0.183 s^(-1). kcat/Km: printed cell 3.4 x 10^-1 = 0.34 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.34 / 60 = 0.005666666666666667 s^(-1)*mM^(-1); the export stores 0.005903225806451613 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I (journal page 505, PDF page 4), D to L Direction, row K164R: Km = 3.1 x 10^1 mM; kcat = 1.1 x 10^1 min^-1; kcat/Km = 3.4 x 10^-1 under the unit-less column head kcat/Km, in min^-1 mM^-1 by construction from the Km (mM) and kcat (min^-1) columns. Cells printed with a bare ten are written with their implicit exponent made explicit (printed 3.1 x 10, written 3.1 x 10^1; printed 1.1 x 10, written 1.1 x 10^1); the value is unchanged.

row_label: Table I, D to L Direction, row K164R


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N83G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58403 and applied mutation signature R48A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters of Mutant PhAspRs), journal page 505 (PDF page 4), D to L Direction group, row R48A; column Km (mM) = 1.5 x 10^2; column kcat (min^-1) = 1.1 x 10^1; column kcat/Km = 7.7 x 10^-2, the kcat/Km head printing no unit and the cell being in min^-1 mM^-1 by construction from the two neighbouring columns; the other three cells of the same printed row belong to the L to D Direction group, which is the L-Aspartate export row. Cells printed with a bare ten are written with their implicit exponent made explicit (printed 1.1 x 10, written 1.1 x 10^1); the value is unchanged.

normalized_value_unit_evidence: Km: printed Table I cell 1.5 x 10^2 mM = 150 mM, already in mM, no conversion applies; the export stores 150.0 mM. kcat: printed cell 1.1 x 10^1 min^-1 = 11 min^-1; the printed turnover column is per MINUTE, so 11 / 60 = 0.18333333333333332 s^(-1); the export stores 0.183 s^(-1). kcat/Km: printed cell 7.7 x 10^-2 = 0.077 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.077 / 60 = 0.0012833333333333334 s^(-1)*mM^(-1); the export stores 0.00122 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I (journal page 505, PDF page 4), D to L Direction, row R48A: Km = 1.5 x 10^2 mM; kcat = 1.1 x 10^1 min^-1; kcat/Km = 7.7 x 10^-2 under the unit-less column head kcat/Km, in min^-1 mM^-1 by construction from the Km (mM) and kcat (min^-1) columns. Cells printed with a bare ten are written with their implicit exponent made explicit (printed 1.1 x 10, written 1.1 x 10^1); the value is unchanged.

row_label: Table I, D to L Direction, row R48A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R48I with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R48K with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T124A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58403 and applied mutation signature T124A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters of Mutant PhAspRs), journal page 505 (PDF page 4), L to D Direction group, row T124A; column Km (mM) = 1.8 x 10^-1; column kcat (min^-1) = 1.8 x 10^3; column kcat/Km = 9.7 x 10^3, the kcat/Km head printing no unit and the cell being in min^-1 mM^-1 by construction from the two neighbouring columns; the other three cells of the same printed row belong to the D to L Direction group, which is the D-Aspartate export row.

normalized_value_unit_evidence: Km: printed Table I cell 1.8 x 10^-1 mM = 0.18 mM, already in mM, no conversion applies; the export stores 0.18 mM. kcat: printed cell 1.8 x 10^3 min^-1 = 1800 min^-1; the printed turnover column is per MINUTE, so 1800 / 60 = 30.0 s^(-1); the export stores 30.0 s^(-1). kcat/Km: printed cell 9.7 x 10^3 = 9700 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 9700 / 60 = 161.66666666666666 s^(-1)*mM^(-1); the export stores 166.66666666666669 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I (journal page 505, PDF page 4), L to D Direction, row T124A: Km = 1.8 x 10^-1 mM; kcat = 1.8 x 10^3 min^-1; kcat/Km = 9.7 x 10^3 under the unit-less column head kcat/Km, in min^-1 mM^-1 by construction from the Km (mM) and kcat (min^-1) columns.

row_label: Table I, L to D Direction, row T124A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58403 and applied mutation signature T127A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic Parameters of Mutant PhAspRs), journal page 505 (PDF page 4), L to D Direction group, row T127A; column Km (mM) = 1.4 x 10^-1; column kcat (min^-1) = 3.5 x 10^3; column kcat/Km = 2.4 x 10^4, the kcat/Km head printing no unit and the cell being in min^-1 mM^-1 by construction from the two neighbouring columns; the other three cells of the same printed row belong to the D to L Direction group, which is the D-Aspartate export row.

normalized_value_unit_evidence: Km: printed Table I cell 1.4 x 10^-1 mM = 0.14 mM, already in mM, no conversion applies; the export stores 0.14 mM. kcat: printed cell 3.5 x 10^3 min^-1 = 3500 min^-1; the printed turnover column is per MINUTE, so 3500 / 60 = 58.333333333333336 s^(-1); the export stores 58.333 s^(-1). kcat/Km: printed cell 2.4 x 10^4 = 24000 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 24000 / 60 = 400.0 s^(-1)*mM^(-1); the export stores 416.66428571428565 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I (journal page 505, PDF page 4), L to D Direction, row T127A: Km = 1.4 x 10^-1 mM; kcat = 3.5 x 10^3 min^-1; kcat/Km = 2.4 x 10^4 under the unit-less column head kcat/Km, in min^-1 mM^-1 by construction from the Km (mM) and kcat (min^-1) columns.

row_label: Table I, L to D Direction, row T127A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T84A 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: Mus musculus

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


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 'l-Ser to d-Ser' of the Mus musculus SerR H150S/P151S/N152S (SSS) block: Km = 53.4, Kcat = 277, Kcat/Km = 5.18, v = 3.94.

normalized_value_unit_evidence: Km: printed Table 1 cell 53.4 under the column head 'Km (mM)'; the printed unit is already mM, so no conversion is applied and the normalized value is 53.4 mM. kcat: printed Table 1 cell 277 under the column head 'Kcat (10^-3 s^-1)'; 277 x 10^-3 = 0.277 s^(-1). kcat/Km: printed Table 1 cell 5.18 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 5.18 M^-1 s^-1, and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.18 x 0.001 = 0.00518 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 'l-Ser to d-Ser': printed Km cell 53.4 under the column head 'Km (mM)'; printed Kcat cell 277 under the column head 'Kcat (10^-3 s^-1)'; printed Kcat/Km cell 5.18 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; printed v cell 3.94 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/P151S/N152S (SSS) block


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


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 'l-Ser to d-Ser' of the Mus musculus SerR P151S (HSN) block: Km = 30.0, Kcat = 5710, Kcat/Km = 191, v = 132.

normalized_value_unit_evidence: Km: printed Table 1 cell 30.0 under the column head 'Km (mM)'; the printed unit is already mM, so no conversion is applied and the normalized value is 30.0 mM. kcat: printed Table 1 cell 5710 under the column head 'Kcat (10^-3 s^-1)'; 5710 x 10^-3 = 5.71 s^(-1). kcat/Km: printed Table 1 cell 191 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 191 M^-1 s^-1, and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 191 x 0.001 = 0.191 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 'l-Ser to d-Ser': printed Km cell 30.0 under the column head 'Km (mM)'; printed Kcat cell 5710 under the column head 'Kcat (10^-3 s^-1)'; printed Kcat/Km cell 191 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; printed v cell 132 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 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 'l-Ser to d-Ser' of the Mus musculus SerR P151S/N152S (HSS) block: Km = 38.1, Kcat = 1880, Kcat/Km = 49.5, v = 39.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 38.1 under the column head 'Km (mM)'; the printed unit is already mM, so no conversion is applied and the normalized value is 38.1 mM. kcat: printed Table 1 cell 1880 under the column head 'Kcat (10^-3 s^-1)'; 1880 x 10^-3 = 1.88 s^(-1). kcat/Km: printed Table 1 cell 49.5 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 49.5 M^-1 s^-1, and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 49.5 x 0.001 = 0.0495 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 'l-Ser to d-Ser': printed Km cell 38.1 under the column head 'Km (mM)'; printed Kcat cell 1880 under the column head 'Kcat (10^-3 s^-1)'; printed Kcat/Km cell 49.5 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; printed v cell 39.5 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 P151S/N152S (HSS) block


assay_conditions_summary: pH 8.5; 310.15 K; cofactor NADH

column_label: Table 2; row label: L-Ala-D-Asp; column block: YkfB (B. subtilis); column labels include kcat (s^-1), kcat/KM (M^-1 s^-1), KM (M); kcat = 0.053 +/- 0.009 s^-1; kcat/Km = 1.9 x 10^3 M^-1 s^-1; Km = (2.8 +/- 1.2) x 10^-5 M; normalized kcat=0.053 s^-1; kcat/Km=1.9 s^-1 mM^-1; Km=0.028 mM.

row_label: Substrate row: L-Ala-D-Asp; enzyme/column block: YkfB (B. subtilis); metric columns: kcat (s^-1), kcat/KM (M^-1 s^-1), KM (M).

table_label: Table 2: Kinetic Parameters for the Reactions Catalyzed by YcjG and YkfB


column_label: Table label: Table 2:  Kinetic Parameters for the Reactions Catalyzed by YcjG and YkfB. Row: l-Ala-d-Glu. Enzyme column group: YkfB (B. subtilis). Columns read: KM (M) cell (3.2 ± 1.1) × 10-4, kcat (s-1) cell 15 ± 2.7, kcat/KM (M-1 s-1) cell 4.7 × 104. KM (3.2 ± 1.1) × 10-4 M normalizes to 0.32 mM and equals the exported km; kcat 15 ± 2.7 s^-1 normalizes to 15 s^-1 and equals the exported kcat; the exported kcat_over_km 46.875 s^-1 mM^-1 is the exact quotient of those two printed cells and agrees with the printed kcat/KM cell 4.7 × 104 M-1 s-1 at its two-significant-figure precision.

normalized_value_unit_evidence: YkfB (B. subtilis) columns of row l-Ala-d-Glu: KM (3.2 ± 1.1) × 10-4 M = 0.32 mM; kcat 15 ± 2.7 s^-1 = 15 s^-1; kcat/KM taken as the quotient of those two printed cells, 15 s^-1 / 0.32 mM = 46.875 s^-1 mM^-1, which the table prints rounded to two significant figures as 4.7 × 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: YkfB (B. subtilis) | l-Ala-d-Glu


column_label: Table 2; row label: L-Ala-D-Met; column block: YkfB (B. subtilis); column labels include kcat (s^-1), kcat/KM (M^-1 s^-1), KM (M); kcat = 1.1 +/- 0.1 s^-1; kcat/Km = 2.2 x 10^3 M^-1 s^-1; Km = (5.1 +/- 1.7) x 10^-4 M; normalized kcat=1.1 s^-1; kcat/Km=2.2 s^-1 mM^-1; Km=0.51 mM.

normalized_value_unit_evidence: normalized: kcat=1.1 s^-1; kcat/Km=2.2 s^-1 mM^-1; Km=0.51 mM

row_label: Substrate row: L-Ala-D-Met; enzyme/column block: YkfB (B. subtilis); metric columns: kcat (s^-1), kcat/KM (M^-1 s^-1), KM (M).


substrate_name: L-Alanyl-D-aspartate

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADH

column_label: Table 2; row label: L-Alanyl-D-aspartate; column block: YkfB (B. subtilis); column labels include kcat (s^-1), kcat/KM (M^-1 s^-1), KM (M); kcat = 0.053 +/- 0.009 s^-1; kcat/Km = 1.9 x 10^3 M^-1 s^-1; Km = (2.8 +/- 1.2) x 10^-5 M; normalized kcat=0.053 s^-1; kcat/Km=1.9 s^-1 mM^-1; Km=0.028 mM.

row_label: Substrate row: L-Alanyl-D-aspartate; enzyme/column block: YkfB (B. subtilis); metric columns: kcat (s^-1), kcat/KM (M^-1 s^-1), KM (M).

substrate: L-Alanyl-D-aspartate


substrate_name: L-Alanyl-D-methionine

column_label: Table 2; row label: L-Alanyl-D-methionine; column block: YkfB (B. subtilis); column labels include kcat (s^-1), kcat/KM (M^-1 s^-1), KM (M); kcat = 1.1 +/- 0.1 s^-1; kcat/Km = 2.2 x 10^3 M^-1 s^-1; Km = (5.1 +/- 1.7) x 10^-4 M; normalized kcat=1.1 s^-1; kcat/Km=2.2 s^-1 mM^-1; Km=0.51 mM.

row_label: Substrate row: L-Alanyl-D-methionine; enzyme/column block: YkfB (B. subtilis); metric columns: kcat (s^-1), kcat/KM (M^-1 s^-1), KM (M).

substrate: L-Alanyl-D-methionine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H150S/P151S/F152S with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


column_label: Table label: Table 1 Comparison of kinetic constants of SerRs and AspRs. Species/enzyme block: Penaeus monodon | SerR | WT (HPF). Reaction row: d-Ser to l-Ser. Km column cell = 119 ± 16; Kcat column cell = 7.72 ± 1.13; Kcat/Km column cell = 0.0651 ± 0.0012. 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 119 ± 16 mM is already in mM and normalizes to 119.0 mM. Kcat 7.72 ± 1.13 is printed in the column unit 10^-3 s^-1, so it normalizes to 0.00772 s^-1 (multiply by 0.001). kcat/Km = 0.00772 s^-1 / 119.0 mM = 0.00006487394957983193 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, 0.0651 ± 0.0012 (10^-3 s^-1 mM^-1) = 0.00006510000000000001 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 (0.00772 s^-1 / 119.0 mM = 0.00006487394957983193 s^-1 mM^-1), and that quotient lies inside the printed cell's own stated standard deviation (± 0.0000012 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 | SerR | WT (HPF) | reaction row: d-Ser to l-Ser | columns: Km (mM); Kcat (10^-3 s^-1); Kcat/Km (10^-3 s^-1 mM^-1) | row as printed: d-Ser to l-Ser     (Uda et al. 2016)   119 ± 16          7.72 ± 1.13        0.0651 ± 0.0012   0.103 ± 0.011 | Km cell = 119 ± 16 mM; Kcat cell = 7.72 ± 1.13 (10^-3 s^-1); Kcat/Km cell = 0.0651 ± 0.0012 (10^-3 s^-1 mM^-1).

row_label: Penaeus monodon | SerR | WT (HPF) | d-Ser to l-Ser


substrate_name: L-serine

substrate: L-serine


column_label: Table label: Table 1 Comparison of kinetic constants of SerRs and AspRs. Species/enzyme block: Penaeus monodon | SerR | WT (HPF). Reaction row: l-Ser to d-Ser. Km column cell = 146 ± 5; Kcat column cell = 8.17 ± 0.56; Kcat/Km column cell = 0.0559 ± 0.0038. 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 146 ± 5 mM is already in mM and normalizes to 146.0 mM. Kcat 8.17 ± 0.56 is printed in the column unit 10^-3 s^-1, so it normalizes to 0.00817 s^-1 (multiply by 0.001). kcat/Km = 0.00817 s^-1 / 146.0 mM = 0.00005595890410958904 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, 0.0559 ± 0.0038 (10^-3 s^-1 mM^-1) = 0.0000559 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 (0.00817 s^-1 / 146.0 mM = 0.00005595890410958904 s^-1 mM^-1), and that quotient lies inside the printed cell's own stated standard deviation (± 0.0000038 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 | SerR | WT (HPF) | reaction row: l-Ser to d-Ser | columns: Km (mM); Kcat (10^-3 s^-1); Kcat/Km (10^-3 s^-1 mM^-1) | row as printed: l-Ser to d-Ser     (Uda et al. 2016)   146 ± 5           8.17 ± 0.56        0.0559 ± 0.0038   0.0805 ± 0.0070 | Km cell = 146 ± 5 mM; Kcat cell = 8.17 ± 0.56 (10^-3 s^-1); Kcat/Km cell = 0.0559 ± 0.0038 (10^-3 s^-1 mM^-1).

row_label: Penaeus monodon | SerR | WT (HPF) | l-Ser to d-Ser


organism: Crassostrea gigas

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0U5AKI6 and applied mutation signature P150S/P151S/Y152S 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 Crassostrea gigas SerR P150S/P151S/Y152S (SSS) block: Km = 12.7, Kcat = 4.23, Kcat/Km = 0.338, v = 0.253.

normalized_value_unit_evidence: Km: printed Table 1 cell 12.7 under the column head 'Km (mM)'; the printed unit is already mM, so no conversion is applied and the normalized value is 12.7 mM. kcat: printed Table 1 cell 4.23 under the column head 'Kcat (10^-3 s^-1)'; 4.23 x 10^-3 = 0.00423 s^(-1). kcat/Km: printed Table 1 cell 0.338 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 0.338 M^-1 s^-1, and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.338 x 0.001 = 0.000338 s^(-1)*mM^(-1). No min^-1, uM or M cell is involved in this row.

raw_value_unit_evidence: Table 1, Crassostrea gigas SerR P150S/P151S/Y152S (SSS) block, reaction row 'd-Ser to l-Ser': printed Km cell 12.7 under the column head 'Km (mM)'; printed Kcat cell 4.23 under the column head 'Kcat (10^-3 s^-1)'; printed Kcat/Km cell 0.338 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; printed v cell 0.253 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 Crassostrea gigas SerR P150S/P151S/Y152S (SSS) 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 Crassostrea gigas SerR P150S/P151S/Y152S (SSS) block: Km = 15.1, Kcat = 4.88, Kcat/Km = 0.324, v = 0.236.

normalized_value_unit_evidence: Km: printed Table 1 cell 15.1 under the column head 'Km (mM)'; the printed unit is already mM, so no conversion is applied and the normalized value is 15.1 mM. kcat: printed Table 1 cell 4.88 under the column head 'Kcat (10^-3 s^-1)'; 4.88 x 10^-3 = 0.00488 s^(-1). kcat/Km: printed Table 1 cell 0.324 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 0.324 M^-1 s^-1, and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.324 x 0.001 = 0.000324 s^(-1)*mM^(-1). No min^-1, uM or M cell is involved in this row.

raw_value_unit_evidence: Table 1, Crassostrea gigas SerR P150S/P151S/Y152S (SSS) block, reaction row 'l-Ser to d-Ser': printed Km cell 15.1 under the column head 'Km (mM)'; printed Kcat cell 4.88 under the column head 'Kcat (10^-3 s^-1)'; printed Kcat/Km cell 0.324 under the column head 'Kcat/Km (10^-3 s^-1 mM^-1)'; printed v cell 0.236 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 Crassostrea gigas SerR P150S/P151S/Y152S (SSS) block


organism: Escherichia coli (strain K12)

substrate_name: L-Ala-D-Glu (at pH 8.5)

column_label: Table 2; row label: L-Ala-D-Glu; column block: YcjG (E. coli); column labels include KM (M); Km = (1.3 +/- 0.3) x 10^-4 M; normalized Km=0.13 mM.

normalized_value_unit_evidence: normalized: Km=0.13 mM

row_label: Substrate row: L-Ala-D-Glu; enzyme/column block: YcjG (E. coli); metric columns: KM (M).

substrate: L-Ala-D-Glu (at pH 8.5)


substrate_name: L-Ala-D-Asp (at pH 8.5)

column_label: Table 2; row label: L-Ala-D-Asp; column block: YcjG (E. coli); column labels include KM (M); Km = (1.9 +/- 0.7) x 10^-4 M; normalized Km=0.19 mM.

normalized_value_unit_evidence: normalized: Km=0.19 mM

row_label: Substrate row: L-Ala-D-Asp; enzyme/column block: YcjG (E. coli); metric columns: KM (M).

substrate: L-Ala-D-Asp (at pH 8.5)


substrate_name: L-Ala-D-Met (at pH 8.5)

column_label: Table 2; row label: L-Ala-D-Met; column block: YcjG (E. coli); column labels include KM (M); Km = (6.9 +/- 0.4) x 10^-4 M; normalized Km=0.69 mM.

normalized_value_unit_evidence: normalized: Km=0.69 mM

row_label: Substrate row: L-Ala-D-Met; enzyme/column block: YcjG (E. coli); metric columns: KM (M).

substrate: L-Ala-D-Met (at pH 8.5)


substrate_name: L-Ala-D-Gln (at pH 8.5)

column_label: Table 2; row label: L-Ala-D-Gln; column block: YcjG (E. coli); column labels include KM (M); Km = (1.8 +/- 0.2) x 10^-3 M; normalized Km=1.8 mM.

normalized_value_unit_evidence: normalized: Km=1.8 mM

row_label: Substrate row: L-Ala-D-Gln; enzyme/column block: YcjG (E. coli); metric columns: KM (M).

substrate: L-Ala-D-Gln (at pH 8.5)


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

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

column_label: Table 3; TM0006; row L-Ala-L-Glu; column K_M (x10^-3 M); raw Km 2.8 +/- 0.96 x10^-3 M; normalized Km=2.8 mM.

raw_value_unit_evidence: Table 3 gives L-Ala-L-Glu K_M 2.8 +/- 0.96 x10^-3 M.

row_label: L-Ala-L-Glu

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


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

column_label: Table 3; TM0006; row L-Ala-L-Phe 28 C; column K_M (x10^-3 M); raw Km 1.3 +/- 0.56 x10^-3 M; normalized Km=1.3 mM.

raw_value_unit_evidence: Table 3 gives L-Ala-L-Phe 28 C K_M 1.3 +/- 0.56 x10^-3 M.

row_label: L-Ala-L-Phe 28 C