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)


enzyme_display_name: 4-hydroxyproline epimerase

source_db: oed

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

column_label: Table 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)

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

data_origin: experimental

enzyme: 4-hydroxyproline epimerase

status: corrected

source: oed


organism: Brevibacillus brevis

substrate_name: L-Phe

source_db: brenda

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

substrate: L-Phe

source: brenda


verification_status: unverified

status: unverified


organism: Agrobacterium tumefaciens

verification_status: verified

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)

status: verified


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_db: skid

kcat_display: Not reported

kcat_over_km_display: Not reported

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q6L2R8

substrate: D-Aspartate

source: skid


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

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

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)

source_db: uniprot

source: uniprot


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.

mutation_type: substitution

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


km_display: Not reported

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


organism: Manihot esculenta

substrate_name: L-serine

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

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

kcat_over_km_origin: calculated

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

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

sequence_source: multiple

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.

source_databases_merged: skid uniprot

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

ki_unit: mM

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: 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


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

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

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

row_label: L-Ala-L-Tyr


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

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

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

row_label: L-Ala-L-His


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

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

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

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

row_label: L-Ala-L-Leu


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

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

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

row_label: L-Ile-L-Phe


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

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

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

row_label: L-Lys-L-Phe


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


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

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

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

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


substrate_name: L-Aspartate

substrate: L-Aspartate


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

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

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

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


organism: Homo sapiens

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D318N 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 | AspR | WT (SSS). Reaction row: d-Asp to l-Asp. Km column cell = 9.86 ± 0.56; Kcat column cell = 27,600 ± 1000; Kcat/Km column cell = 2810 ± 60. Km, Kcat and Kcat/Km are read from the one printed row of this species/enzyme block, so they are one measurement; no value comes from another row, another block, or another paper.

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

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

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


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

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

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

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


substrate_name: D-serine

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

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

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

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

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

substrate: D-serine


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

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

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

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

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


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

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

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

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

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


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

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

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

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


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

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

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

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

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


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

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

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

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


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

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

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

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


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

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

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


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

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

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

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


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

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

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

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


substrate_name: L-2-aminobutyric acid amide

assay_conditions_summary: pH 7; buffer pH 7

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

raw_value_unit_evidence: Km raw_value=1.1 raw_unit=mM

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

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

substrate: L-2-aminobutyric acid amide


substrate_name: L-Ala

substrate: L-Ala


substrate_name: D-alpha-Amino-epsilon-caprolactam

substrate: D-alpha-Amino-epsilon-caprolactam


enzyme_display_name: nocardicin-A epimerase

organism: Nocardia uniformis

substrate_name: nocardicin A

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

enzyme: nocardicin-A epimerase

substrate: nocardicin A


substrate_name: L-serine


organism: Streptomyces clavuligerus

substrate_name: pyridoxal 5'-phosphate

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

substrate: pyridoxal 5'-phosphate


substrate_name: isopenicillin N

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

raw_value_unit_evidence: Km raw_value=0.30 mM raw_unit=mM

row_label: Purified isopenicillin N epimerase / isopenicillin N substrate

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

substrate: isopenicillin N


organism: Aplysia californica


organism: Pyrococcus horikoshii

substrate_name: L-aspartate

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

source_databases_merged: brenda skid uniprot

substrate: L-aspartate


organism: Dictyostelium discoideum


substrate_name: O-ureido-D-serine

substrate: O-ureido-D-serine


substrate_name: O-ureido-L-serine

substrate: O-ureido-L-serine


organism: Roseobacter litoralis


organism: Oryza sativa subsp. japonica

substrate_name: L-serine (racemase activity)

substrate: L-serine (racemase activity)


organism: Escherichia coli

substrate_name: L-Ala-D-Asp

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

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

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

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

substrate: L-Ala-D-Asp


substrate_name: L-Ala-D-Gln

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

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

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

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

substrate: L-Ala-D-Gln