organism: Fusarium oxysporum

substrate_name: alpha-D-glucose 1-phosphate

proof_lines: in 41 mM 1,3-diaza-2,4-cyclopentadiene /HCl (pH 7.6), 5 mM MgCl2, at 25°C

substrate: alpha-D-glucose 1-phosphate


substrate_name: D-glucose 1,6-diphosphate

source_db: brenda

verification_status: unverified

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

substrate: D-glucose 1,6-diphosphate

status: unverified

source: brenda


enzyme_display_name: alanine racemase

organism: Aquifex pyrophilus

substrate_name: D-Ala

protein_accession_database: UniProt

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

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

data_origin: experimental

enzyme: alanine racemase

substrate: D-Ala


organism: Thalassiosira sp.

substrate_name: D-alanine

kcat_display: Not reported

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

substrate: D-alanine


enzyme_display_name: UniProt P10724

organism: Geobacillus stearothermophilus

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P10724

source: skid


enzyme_display_name: UniProt P94556

organism: Bacillus subtilis

substrate_name: L-alanine

enzyme: UniProt P94556

substrate: L-alanine


enzyme_display_name: UniProt P9WPW9

organism: Mycobacterium tuberculosis

enzyme: UniProt P9WPW9


enzyme_display_name: UniProt Q180W0

organism: Clostridioides difficile

proof_lines:
Raw SKiD Env: Temp=-----, pH=8.5
Raw SKiD Env: Temp=37°C, pH=7.5

enzyme: UniProt Q180W0


enzyme_display_name: UniProt Q65YW7

organism: Streptomyces lavendulae

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8.2
Raw SKiD Env: Temp=37°C, pH=8.2

enzyme: UniProt Q65YW7


enzyme_display_name: UniProt Q8RAK6

organism: Caldanaerobacter subterraneus subsp. tengcongensis

enzyme: UniProt Q8RAK6


substrate_name: D-Lysine

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

substrate: D-Lysine


enzyme_display_name: UniProt P0A2W8

organism: Streptococcus pneumoniae

enzyme: UniProt P0A2W8


enzyme_display_name: UniProt Q9A1B7

organism: Streptococcus pyogenes

substrate_name: L-glutamate

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

enzyme: UniProt Q9A1B7

substrate: L-glutamate


enzyme_display_name: UniProt H3ZMH5

organism: Thermococcus litoralis

substrate_name: L-proline

enzyme: UniProt H3ZMH5

substrate: L-proline


enzyme_display_name: cysteine-S-conjugate beta-lyase

organism: Homo sapiens

substrate_name: beta-chloro-L-alanine

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

enzyme: cysteine-S-conjugate beta-lyase

substrate: beta-chloro-L-alanine


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


enzyme_display_name: selenocysteine lyase

substrate_name: L-selenocysteine

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

enzyme: selenocysteine lyase

substrate: L-selenocysteine


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


enzyme_display_name: prostaglandin-D synthase

substrate_name: glutathione

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

enzyme: prostaglandin-D synthase

substrate: glutathione


enzyme_display_name: lactoylglutathione lyase

proof_lines: pH and temperature not specified in the publication

enzyme: lactoylglutathione lyase


enzyme_display_name: Transferred entry: 4.8.1.2

organism: Pseudomonas chlororaphis

substrate_name: Aldoxime

source_db: oed

kcat_over_km_origin: calculated

smiles: C/C=N/O

enzyme: Transferred entry: 4.8.1.2

substrate: Aldoxime

source: oed


substrate_name: n-Butyraldoxime

smiles: CCC/C=N/O

substrate: n-Butyraldoxime


verification_status: corrected

column_label: Table III; substrate row E/Z-Pyridine-2-aldoxime; columns Km, kcat, and kcat/Km

raw_value_unit_evidence: paper Table III cells: Km=3.4 mM; kcat=0.090 min^-1; kcat/Km=0.026 min^-1 mM^-1

table_label: Table III

status: corrected


enzyme_display_name: L-3-cyanoalanine synthase

organism: Glycine max

substrate_name: L-cysteine

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

enzyme: L-3-cyanoalanine synthase

substrate: L-cysteine


substrate_name: hydrogen cyanide

substrate: hydrogen cyanide


enzyme_display_name: glutamate racemase

organism: Saccoglossus kowalevskii

assay_conditions_summary: pH 8

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

enzyme: glutamate racemase


substrate_name: L-aspartate

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

substrate: L-aspartate


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

mutation_type: substitution

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


substrate_name: D-glutamate

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

substrate: D-glutamate


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


enzyme_display_name: adenylate cyclase

substrate_name: ATP

assay_conditions_summary: 303.15 K; cofactor ATP

proof_lines:
wild type isoform V, 30°C
wild type isoform VI, 30°C

enzyme: adenylate cyclase

substrate: ATP


enzyme_display_name: prostaglandin-E synthase

sequence_source: UniProtKB O14684 FASTA

proof_lines: in the presence of 0.3 mM dodecylmaltoside

enzyme: prostaglandin-E synthase


substrate_name: prostaglandine G2

substrate: prostaglandine G2


enzyme_display_name: proline racemase

organism: Ferroplasma acidarmanus

substrate_name: D-proline

enzyme: proline racemase

substrate: D-proline


enzyme_display_name: alanine racemase

organism: Acidiphilium organovorum

substrate_name: D-Ala

assay_conditions_summary: pH 9

enzyme: alanine racemase

substrate: D-Ala


organism: Candidatus Pelagibacter communis

substrate_name: L-alanine

proof_lines: recombinant MBP-tagged enzyme, pH 8.0, 37°C

substrate: L-alanine


organism: Medicago sativa

substrate_name: D-alanine

proof_lines:
Vmax = 0.44 mol/s/kg
Vmax = 1.02 mol/s/kg

substrate: D-alanine


enzyme_display_name: magnesium dechelatase

organism: Chenopodium album

substrate_name: chlorophyllin a

enzyme: magnesium dechelatase

substrate: chlorophyllin a


organism: Cellana grata


organism: Fragaria x ananassa

assay_conditions_summary: pH 8.8; 310.15 K; buffer only a paper note fragment ('in 50 mM Tris-tricine

proof_lines: in 50 mM Tris-tricine buffer, at 37°C and pH 8.8


substrate_name: L-proline

substrate: L-proline


organism: Tolypocladium inflatum


organism: Bacillus anthracis

proof_lines: D-glutamate analog, good competitive inhibitor for RacE1

proof_lines: D-glutamate analog, only weak inhibitor of RacE2

proof_lines: isozyme RacE1, pH and temperature not specified in the publication


organism: Trypanosoma vivax

sequence_source: multiple

proof_lines: 40 mM substrate in 0.2 M sodium acetate, for 30 min at 37°C


proof_lines: 0.005 mM pyrrole-2-carboxylic acid, serial concentrations of 20-160 mM L-proline


organism: Aquifex pyrophilus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D7S to reconstruct the assayed variant sequence.


substrate_name: L-glutamate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E147N to reconstruct the assayed variant sequence.

substrate: L-glutamate


enzyme_display_name: coproporphyrin ferrochelatase

organism: Bacillus subtilis (strain 168)

source_db: uniprot

proof_lines: kcat is 0.11 min(-1) with coproporphyrin III as substrate (PubMed:25646457). kcat is 78 min(-1) with Fe(2+) as substrate (PubMed:25908396).

enzyme: coproporphyrin ferrochelatase

source: uniprot


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: coproporphyrin III

proof_lines: kcat is 1.8 min(-1) with coproporphyrin III as substrate. kcat is 0.8 min(-1) with protoporphyrin IX as substrate.

substrate: coproporphyrin III


substrate_name: protoporphyrin IX

substrate: protoporphyrin IX


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

substrate_name: cystathionine (at pH 8.8 and 37 degrees Celsius)

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

proof_lines: kcat is 2.3 sec(-1) for cystathionine beta-lyase activity (at pH 8.8 and 37 degrees Celsius). kcat is 3.3 sec(-1) for cystathionine beta-lyase activity (at pH 8.0 and 37 degrees Celsius). kcat is 9.2 sec(-1) for cystathionine beta-lyase act


substrate_name: L-glutamate (at pH 8.0 and 37 degrees Celsius)


organism: Procambarus clarkii


enzyme_display_name: methionine racemase

organism: Thermococcus kodakarensis

substrate_name: L-leucine

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

assay_conditions_summary: pH 5

proof_lines: kcat is 108 sec(-1) with D-leucine as substrate. kcat is 43.3 sec(-1) with L-leucine as substrate. kcat is 86.0 sec(-1) with D-methionine as substrate. kcat is 54.4 sec(-1) with L-methionine as substrate.

source_databases_merged: brenda uniprot

enzyme: methionine racemase

substrate: L-leucine


substrate_name: L-methionine

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

substrate: L-methionine


substrate_name: D-Glutamate

substrate: D-Glutamate


substrate_name: L-Glutamate

substrate: L-Glutamate


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


organism: Lactiplantibacillus plantarum


organism: Pseudomonas aeruginosa

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

proof_lines:
23°C, enzyme DadX
Raw SKiD Env: Temp=23°C, pH=-----

source_databases_merged: brenda skid uniprot


organism: Wolbachia pipientis

assay_conditions_summary: pH 8; 310.15 K; buffer as 50 mM Tris·HCl pH 8

column_label: Table 2 (Steady state kinetic parameters for MBP-PuCBL, wMelCBL and TmCBL), Enzyme block 'wMelCBL', Function row 'ALR', Conditions column '37 C, Tris'; column 'kcat (s^-1)' = 2.3; column 'KM (mM)' = 3.8; column 'kcat/KM (s^-1 M^-1)' = 580. The ALR line is the only line this Enzyme block prints for that activity, and the block prints no second buffer or temperature for it.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.3 s^-1; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 2.3 s^(-1). Km: printed Table 2 cell 3.8 mM; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 3.8 mM. kcat/Km: printed Table 2 cell 580 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 580 / 1000 = 0.58 s^-1 mM^-1. Closure disclosure: the quotient of this row's own two printed component cells is 2.3 / 3.8 = 0.6052631578947368 s^-1 mM^-1, against the printed efficiency cell 0.58 s^-1 mM^-1 carried at the two-significant-figure precision of the printed efficiency column.

raw_value_unit_evidence: Table 2, Enzyme block 'wMelCBL', Function row 'ALR', Conditions '37 C, Tris': kcat = 2.3 s^-1; KM = 3.8 mM; printed kcat/KM = 580 s^-1 M^-1.

table_label: Table 2: Steady state kinetic parameters for MBP-PuCBL, wMelCBL and TmCBL (Mol. Microbiol. 2017, 105(4):508-524)


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: Fe(2+) (in the presence of coproporphyrin III)

proof_lines: kcat is 165 min(-1) with coproporphyrin III as substrate. kcat is 15 min(-1) with protoporphyrin IX as substrate.


organism: Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF)

proof_lines: kcat is 64 sec(-1) with L-proline as substrate.


organism: Thermotoga maritima

assay_conditions_summary: pH 8; buffer bicine

proof_lines: recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer

proof_lines: recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer


organism: Synechocystis sp. PCC 6803

sequence_variant_note: Mutation signature W385A references residue 385, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature W385V references residue 385, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature W385I references residue 385, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature W385F references residue 385, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature W385Y references residue 385, which is outside the resolved sequence length.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -14, so it is treated as a source-provided variant sequence.


organism: Mycobacterium avium

substrate_name: Unknown

substrate: Unknown


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


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


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)


organism: Trypanosoma cruzi (strain CL Brener)


organism: Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)

substrate_name: pyridoxal phosphate

proof_lines: kcat is 0.62 sec(-1) with L-leucine as substrate. kcat is 0.79 sec(-1) with D-leucine as substrate. kcat is 1.1 sec(-1) with L-methionine as substrate. kcat is 1.8 sec(-1) with D-methionine as substrate.

substrate: pyridoxal phosphate


organism: Wolbachia pipientis wMel

proof_lines: kcat is 0.001 sec(-1) for cystathionine beta-lyase activity (at pH 8.8 and 37 degrees Celsius). kcat is 2.3 sec(-1) for alanine racemase activity (at pH 8.8 and 37 degrees Celsius). kcat is 0.017 sec(-1) for glutamate racemase activity (at

substrate: cystathionine (at pH 8.8 and 37 degrees Celsius)


substrate_name: L-alanine (at pH 8.8 and 37 degrees Celsius)


organism: Staphylococcus aureus (strain Mu50 / ATCC 700699)


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)


organism: Aquifex pyrophilus


organism: Homo sapiens


organism: Clostridioides difficile

proof_lines: substrate: D-proline, Vmax= 0.000017 M/sec

proof_lines: substrate: L-proline, Vmax = 0.000027 M/sec


organism: Caldanaerobacter subterraneus subsp. tengcongensis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S173D with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature S173D/Q360Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 10.0, 65°C, recombinant mutant S173D/Q360Y


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q360I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q360Y to reconstruct the assayed variant sequence.


substrate_name: L-alanine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q360W to reconstruct the assayed variant sequence.


organism: Wolbachia pipientis

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

column_label: Table 2 (Steady state kinetic parameters for MBP-PuCBL, wMelCBL and TmCBL), Enzyme block 'wMelCBL', Function row 'GLR', Conditions column '37 C, Tris'; column 'kcat (s^-1)' = 0.017; column 'KM (mM)' = 0.80; column 'kcat/KM (s^-1 M^-1)' = 21. The GLR line is the only line this Enzyme block prints for that activity, and the block prints no second buffer or temperature for it.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.017 s^-1; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 0.017 s^(-1). Km: printed Table 2 cell 0.80 mM; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 0.8 mM. kcat/Km: printed Table 2 cell 21 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 21 / 1000 = 0.021 s^-1 mM^-1. Closure disclosure: the quotient of this row's own two printed component cells is 0.017 / 0.80 = 0.02125 s^-1 mM^-1, against the printed efficiency cell 0.021 s^-1 mM^-1 carried at the two-significant-figure precision of the printed efficiency column.

raw_value_unit_evidence: Table 2, Enzyme block 'wMelCBL', Function row 'GLR', Conditions '37 C, Tris': kcat = 0.017 s^-1; KM = 0.80 mM; printed kcat/KM = 21 s^-1 M^-1.


enzyme_display_name: sirohydrochlorin nickelchelatase

organism: Methanocaldococcus jannaschii

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

enzyme: sirohydrochlorin nickelchelatase


substrate_name: sirohydrochlorin

proof_lines: wild-type enzyme, with Ni2+, pH and temperature not specified in the publication

substrate: sirohydrochlorin


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

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


proof_lines: chimeric mutant enzyme, with Ni2+, pH and temperature not specified in the publication


organism: Escherichia coli

substrate_name: L-Alanine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D164K to reconstruct the assayed variant sequence.

substrate: L-Alanine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6B4 and applied mutation signature E165A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

column_label: Table 2, enzyme row 'E165A', L- to D-Ala block; column 'Km (mM)' = 1.562 ± 0.256; column 'kcat (min-1)' = 1348 ± 160; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1348 min-1; min^-1 to s^-1 is a division by 60, so 1348 / 60 = 22.466666666666665 s^(-1); the exported value 22.467 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 1.562 mM; the cell is already in mM, so no unit conversion applies and the paper value is 1.562 mM; the exported value is 1.562 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 14.383269312846776 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 22.466666666666665 / 1.562 of this row's own two printed cells, typed derived_same_measurement; the exported value 14.383482714468629 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'E165A', L- to D-Ala block: kcat = 1348 min-1; Km (mM) = 1.562 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'E165A', L- to D-Ala direction

table_label: Table 2: Kinetic parameters of the wild-type EcAlr and its mutants (Protein Science 2008, 17:1066-1076)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6B4 and applied mutation signature E165K to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'E165K', L- to D-Ala block; column 'Km (mM)' = 2.057 ± 0.038; column 'kcat (min-1)' = 1003 ± 51; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1003 min-1; min^-1 to s^-1 is a division by 60, so 1003 / 60 = 16.716666666666665 s^(-1); the exported value 16.717 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 2.057 mM; the cell is already in mM, so no unit conversion applies and the paper value is 2.057 mM; the exported value is 2.057 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 8.1267217630854 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 16.716666666666665 / 2.057 of this row's own two printed cells, typed derived_same_measurement; the exported value 8.126883811375789 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'E165K', L- to D-Ala block: kcat = 1003 min-1; Km (mM) = 2.057 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'E165K', L- to D-Ala direction


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6B4 and applied mutation signature E221A to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'E221A', L- to D-Ala block; column 'Km (mM)' = 1.516 ± 0.083; column 'kcat (min-1)' = 4255 ± 140; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4255 min-1; min^-1 to s^-1 is a division by 60, so 4255 / 60 = 70.91666666666667 s^(-1); the exported value 70.917 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 1.516 mM; the cell is already in mM, so no unit conversion applies and the paper value is 1.516 mM; the exported value is 1.516 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 46.7788038698329 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 70.91666666666667 / 1.516 of this row's own two printed cells, typed derived_same_measurement; the exported value 46.779023746701846 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'E221A', L- to D-Ala block: kcat = 4255 min-1; Km (mM) = 1.516 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'E221A', L- to D-Ala direction


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6B4 and applied mutation signature E221K to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'E221K', L- to D-Ala block; column 'Km (mM)' = 1.993 ± 0.269; column 'kcat (min-1)' = 4094 ± 453; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4094 min-1; min^-1 to s^-1 is a division by 60, so 4094 / 60 = 68.23333333333333 s^(-1); the exported value 68.233 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 1.993 mM; the cell is already in mM, so no unit conversion applies and the paper value is 1.993 mM; the exported value is 1.993 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 34.23649439705636 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 68.23333333333333 / 1.993 of this row's own two printed cells, typed derived_same_measurement; the exported value 34.23632714500753 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'E221K', L- to D-Ala block: kcat = 4094 min-1; Km (mM) = 1.993 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'E221K', L- to D-Ala direction


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6B4 and applied mutation signature E221P to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'E221P', L- to D-Ala block; column 'Km (mM)' = 1.401 ± 0.209; column 'kcat (min-1)' = 4024 ± 458; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4024 min-1; min^-1 to s^-1 is a division by 60, so 4024 / 60 = 67.06666666666666 s^(-1); the exported value 67.067 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 1.401 mM; the cell is already in mM, so no unit conversion applies and the paper value is 1.401 mM; the exported value is 1.401 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 47.87056864144658 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 67.06666666666666 / 1.401 of this row's own two printed cells, typed derived_same_measurement; the exported value 47.87080656673804 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'E221P', L- to D-Ala block: kcat = 4024 min-1; Km (mM) = 1.401 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'E221P', L- to D-Ala direction


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6B4 and applied mutation signature P219A to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'P219A', L- to D-Ala block; column 'Km (mM)' = 1.049 ± 0.131; column 'kcat (min-1)' = 3106 ± 364; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3106 min-1; min^-1 to s^-1 is a division by 60, so 3106 / 60 = 51.766666666666666 s^(-1); the exported value 51.767 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 1.049 mM; the cell is already in mM, so no unit conversion applies and the paper value is 1.049 mM; the exported value is 1.049 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 49.34858595487766 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 51.766666666666666 / 1.049 of this row's own two printed cells, typed derived_same_measurement; the exported value 49.34890371782651 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'P219A', L- to D-Ala block: kcat = 3106 min-1; Km (mM) = 1.049 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'P219A', L- to D-Ala direction


substrate_name: D-alanine

source_databases_merged: skid uniprot


substrate_name: D-Alanine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6B4 and applied mutation signature D164A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

column_label: Table 2, enzyme row 'D164A', D- to L-Ala block; column 'Km (mM)' = 0.615 ± 0.032; column 'kcat (min-1)' = 268 ± 12; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 268 min-1; min^-1 to s^-1 is a division by 60, so 268 / 60 = 4.466666666666667 s^(-1); the exported value 4.467 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 0.615 mM; the cell is already in mM, so no unit conversion applies and the paper value is 0.615 mM; the exported value is 0.615 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 7.262872628726288 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 4.466666666666667 / 0.615 of this row's own two printed cells, typed derived_same_measurement; the exported value 7.263414634146341 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'D164A', D- to L-Ala block: kcat = 268 min-1; Km (mM) = 0.615 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'D164A', D- to L-Ala direction

substrate: D-Alanine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A6B4 and applied mutation signature D164K to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'D164K', D- to L-Ala block; column 'Km (mM)' = 0.604 ± 0.070; column 'kcat (min-1)' = 20 ± 2; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 20 min-1; min^-1 to s^-1 is a division by 60, so 20 / 60 = 0.3333333333333333 s^(-1); the exported value 0.333 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 0.604 mM; the cell is already in mM, so no unit conversion applies and the paper value is 0.604 mM; the exported value is 0.604 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 0.5518763796909492 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.3333333333333333 / 0.604 of this row's own two printed cells, typed derived_same_measurement; the exported value 0.5513245033112584 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'D164K', D- to L-Ala block: kcat = 20 min-1; Km (mM) = 0.604 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'D164K', D- to L-Ala direction


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E165A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


column_label: Table 2, enzyme row 'E165K', D- to L-Ala block; column 'Km (mM)' = 0.528 ± 0.079; column 'kcat (min-1)' = 79 ± 6; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 79 min-1; min^-1 to s^-1 is a division by 60, so 79 / 60 = 1.3166666666666667 s^(-1); the exported value 1.317 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 0.528 mM; the cell is already in mM, so no unit conversion applies and the paper value is 0.528 mM; the exported value is 0.528 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 2.4936868686868685 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.3166666666666667 / 0.528 of this row's own two printed cells, typed derived_same_measurement; the exported value 2.4943181818181817 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'E165K', D- to L-Ala block: kcat = 79 min-1; Km (mM) = 0.528 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'E165K', D- to L-Ala direction


column_label: Table 2, enzyme row 'E221A', D- to L-Ala block; column 'Km (mM)' = 0.439 ± 0.080; column 'kcat (min-1)' = 409 ± 39; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 409 min-1; min^-1 to s^-1 is a division by 60, so 409 / 60 = 6.816666666666666 s^(-1); the exported value 6.817 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 0.439 mM; the cell is already in mM, so no unit conversion applies and the paper value is 0.439 mM; the exported value is 0.439 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 15.527714502657554 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 6.816666666666666 / 0.439 of this row's own two printed cells, typed derived_same_measurement; the exported value 15.528473804100228 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'E221A', D- to L-Ala block: kcat = 409 min-1; Km (mM) = 0.439 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'E221A', D- to L-Ala direction


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E221K to reconstruct the assayed variant sequence.


column_label: Table 2, enzyme row 'E221P', D- to L-Ala block; column 'Km (mM)' = 0.513 ± 0.084; column 'kcat (min-1)' = 457 ± 45; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 457 min-1; min^-1 to s^-1 is a division by 60, so 457 / 60 = 7.616666666666666 s^(-1); the exported value 7.617 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 0.513 mM; the cell is already in mM, so no unit conversion applies and the paper value is 0.513 mM; the exported value is 0.513 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 14.84730344379467 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 7.616666666666666 / 0.513 of this row's own two printed cells, typed derived_same_measurement; the exported value 14.847953216374268 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'E221P', D- to L-Ala block: kcat = 457 min-1; Km (mM) = 0.513 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'E221P', D- to L-Ala direction


column_label: Table 2, enzyme row 'P219A', D- to L-Ala block; column 'Km (mM)' = 0.304 ± 0.034; column 'kcat (min-1)' = 316 ± 20; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 316 min-1; min^-1 to s^-1 is a division by 60, so 316 / 60 = 5.266666666666667 s^(-1); the exported value 5.267 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 0.304 mM; the cell is already in mM, so no unit conversion applies and the paper value is 0.304 mM; the exported value is 0.304 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 17.32456140350877 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 5.266666666666667 / 0.304 of this row's own two printed cells, typed derived_same_measurement; the exported value 17.325657894736842 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'P219A', D- to L-Ala block: kcat = 316 min-1; Km (mM) = 0.304 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'P219A', D- to L-Ala direction


column_label: Table 2, enzyme row 'D164A', L- to D-Ala block; column 'Km (mM)' = 3.030 ± 0.114; column 'kcat (min-1)' = 2509 ± 156; Table 2 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2509 min-1; min^-1 to s^-1 is a division by 60, so 2509 / 60 = 41.81666666666666 s^(-1); the exported value 41.817 s^(-1) is that quotient rounded to three decimals. Km: printed Table 2 cell 3.030 mM; the cell is already in mM, so no unit conversion applies and the paper value is 3.03 mM; the exported value is 3.03 mM. kcat/Km: Table 2 has no kcat/Km column, so the paper value 13.800880088008801 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 41.81666666666666 / 3.03 of this row's own two printed cells, typed derived_same_measurement; the exported value 13.800990099009901 s^(-1)*mM^(-1) is the quotient of the rounded exported kcat and the same km.

raw_value_unit_evidence: Table 2, enzyme row 'D164A', L- to D-Ala block: kcat = 2509 min-1; Km (mM) = 3.030 mM; Table 2 prints no kcat/Km cell for this row.

row_label: Table 2, enzyme row 'D164A', L- to D-Ala direction


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

proof_lines: kcat is 37.47 sec(-1) with D-alanine as substrate. kcat is 92.0 sec(-1) with L-alanine as substrate.


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

proof_lines: kcat is 2.3 sec(-1) for cystathionine beta-lyase activity (at pH 8.8 and 37 degrees Celsius). kcat is 3.3 sec(-1) for cystathionine beta-lyase activity (at pH 8.0 and 37 degrees Celsius). kcat is 9.2 sec(-1) for cystathionine beta-lyase act


substrate: L-alanine (at pH 8.8 and 37 degrees Celsius)


organism: Bacillus subtilis (strain 168)

substrate_name: coproporphyrin III

proof_lines: kcat is 0.11 min(-1) with coproporphyrin III as substrate (PubMed:25646457). kcat is 78 min(-1) with Fe(2+) as substrate (PubMed:25908396).


substrate: L-glutamate (at pH 8.0 and 37 degrees Celsius)


organism: Rattus norvegicus

substrate_name: L-serine

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

proof_lines: kcat is 844 min(-1) for L-serine and 152 min(-1) for L-threonine.

substrate: L-serine


substrate_name: L-threonine

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

substrate: L-threonine


substrate_name: L-glutamate

substrate: L-glutamate


organism: Pyrococcus horikoshii

proof_lines: pH and temperature not specified in the publication

substrate: L-alanine


organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)

proof_lines: kcat is 1.42 sec(-1) with L-alanine as substrate. kcat is 1.16 sec(-1) with L-serine as substrate.


organism: Fusobacterium nucleatum subsp. nucleatum

substrate_name: L-2-aminoadipic acid

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

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

assay_conditions_summary: pH 8; buffer fragment

proof_lines: His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)

substrate: L-2-aminoadipic acid


substrate_name: L-glutamate / D-glutamate

proof_lines: recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)

substrate: L-glutamate / D-glutamate


organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)

verification_status: verified

column_label: Full text reports the determined KM value is 0.28 uM for Fe(II) and kcat is 7.9 min^-1.

raw_value_unit_evidence: Km raw_value=0.28 uM raw_unit=uM

row_label: LmCpfC / ferrous iron

table_label: PMC full text steady-state kinetic prose PMID 31794133

status: verified


organism: Thermococcus litoralis

substrate_name: D-proline

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

column_label: Table 2. Kinetic parameters for D-proline and C4DHyp; row TlProR F62S / D-Proline; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1*mM^-1); TlProR F62S / D-Proline: kcat 1.55 +/- 0.09 min^-1; Km 4.00 +/- 0.17 mM; kcat/Km 0.387 +/- 0.008 min^-1*mM^-1. Direct /60 conversion of kcat and kcat/Km gives kcat=0.025833333333333333 s^-1; Km=4.0 mM; kcat/Km=0.00645 s^-1*mM^-1.

row_label: TlProR F62S / D-Proline

substrate: D-proline


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

column_label: Table 2. Kinetic parameters for D-proline and C4DHyp; row TlProR F62V / D-Proline; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1*mM^-1); TlProR F62V / D-Proline: kcat 1.41 +/- 0.03 min^-1; Km 0.156 +/- 0.004 mM; kcat/Km 9.04 +/- 0.23 min^-1*mM^-1. Direct /60 conversion of kcat and kcat/Km gives kcat=0.0235 s^-1; Km=0.156 mM; kcat/Km=0.15066666666666664 s^-1*mM^-1.

row_label: TlProR F62V / D-Proline


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

column_label: Table 2. Kinetic parameters for D-proline and C4DHyp; row TlProR L221H / D-Proline; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1*mM^-1); TlProR L221H / D-Proline: kcat 17.3 +/- 2.7 min^-1; Km 2.54 +/- 0.46 mM; kcat/Km 6.84 +/- 0.19 min^-1*mM^-1. Direct /60 conversion of kcat and kcat/Km gives kcat=0.28833333333333333 s^-1; Km=2.54 mM; kcat/Km=0.114 s^-1*mM^-1.

row_label: TlProR L221H / D-Proline


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

column_label: Table 2. Kinetic parameters for D-proline and C4DHyp; row TlProR W241F / D-Proline; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1*mM^-1); TlProR W241F / D-Proline: kcat 191 +/- 5 min^-1; Km 0.194 +/- 0.020 mM; kcat/Km 990 +/- 82 min^-1*mM^-1. Direct /60 conversion of kcat and kcat/Km gives kcat=3.183333333333333 s^-1; Km=0.194 mM; kcat/Km=16.5 s^-1*mM^-1.

row_label: TlProR W241F / D-Proline


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

column_label: Table 2. Kinetic parameters for D-proline and C4DHyp; row TlProR WT / D-Proline; columns Km, kcat, kcat/Km report normalized values kcat=2.21667 s^-1, Km=0.0919 mM, kcat/Km=26.1667 s^-1*mM^-1.

raw_value_unit_evidence: TlProR WT / D-Proline; kcat raw_value=133 +/- 2 min^-1; Km raw_value=0.0919 +/- 0.006 mM; kcat/Km raw_value=1570 +/- 90 min^-1*mM^-1.

row_label: TlProR WT / D-Proline


substrate_name: L-proline

column_label: Table 1. Kinetic parameters for L-proline, T4LHyp, and T3LHyp; row TlProR F62S / L-Proline; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1*mM^-1); TlProR F62S / L-Proline: kcat 12.0 +/- 1.1 min^-1; Km 154 +/- 13 mM; kcat/Km 0.0774 +/- 0.0010 min^-1*mM^-1. Direct /60 conversion of kcat and kcat/Km gives kcat=0.2 s^-1; Km=154.0 mM; kcat/Km=0.00129 s^-1*mM^-1.

row_label: TlProR F62S / L-Proline

substrate: L-proline


column_label: Table 1. Kinetic parameters for L-proline, T4LHyp, and T3LHyp; row TlProR F62V / L-Proline; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1*mM^-1); TlProR F62V / L-Proline: kcat 5.51 +/- 0.99 min^-1; Km 1.93 +/- 0.44 mM; kcat/Km 2.88 +/- 0.15 min^-1*mM^-1. Direct /60 conversion of kcat and kcat/Km gives kcat=0.09183333333333334 s^-1; Km=1.93 mM; kcat/Km=0.048 s^-1*mM^-1.

row_label: TlProR F62V / L-Proline


column_label: Table 1. Kinetic parameters for L-proline, T4LHyp, and T3LHyp; row TlProR L221H / L-Proline; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1*mM^-1); TlProR L221H / L-Proline: kcat 55.4 +/- 6.1 min^-1; Km 20.5 +/- 2.5 mM; kcat/Km 2.71 +/- 0.05 min^-1*mM^-1. Direct /60 conversion of kcat and kcat/Km gives kcat=0.9233333333333333 s^-1; Km=20.5 mM; kcat/Km=0.04516666666666667 s^-1*mM^-1.

row_label: TlProR L221H / L-Proline


column_label: Table 1. Kinetic parameters for L-proline, T4LHyp, and T3LHyp; row TlProR W241F / L-Proline; columns Km (mM), kcat (min^-1), and kcat/Km (min^-1*mM^-1); TlProR W241F / L-Proline: kcat 190 +/- 14 min^-1; Km 1.29 +/- 0.14 mM; kcat/Km 147 +/- 5 min^-1*mM^-1. Direct /60 conversion of kcat and kcat/Km gives kcat=3.1666666666666665 s^-1; Km=1.29 mM; kcat/Km=2.45 s^-1*mM^-1.

row_label: TlProR W241F / L-Proline


column_label: Table 1. Kinetic parameters for L-proline, T4LHyp, and T3LHyp; row TlProR WT / L-Proline; columns Km, kcat, kcat/Km report normalized values kcat=2.78333 s^-1, Km=1.21 mM, kcat/Km=2.3 s^-1*mM^-1.

raw_value_unit_evidence: TlProR WT / L-Proline; kcat raw_value=167 +/- 10 min^-1; Km raw_value=1.21 +/- 0.12 mM; kcat/Km raw_value=138 +/- 4 min^-1*mM^-1.

row_label: TlProR WT / L-Proline


organism: Lactobacillus fermentum

substrate_name: L-Glutamate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D10N with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

substrate: L-Glutamate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D36N with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E152Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H186N with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


organism: Thermotoga maritima

assay_conditions_summary: pH 8.8; buffer recombinant His-tagged enzyme

proof_lines: recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer

proof_lines: recombinant His-tagged enzyme, pH 8.0, 37°C, bicine buffer

proof_lines: recombinant His-tagged enzyme, pH 8.0, 37°C, Tris buffer


organism: Treponema denticola

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH

column_label: Valid package PDF page 4 (journal page 476), Table 1, D-Alanine row within Racemization, columns Km, kcat, and kcat/Km.

normalized_value_unit_evidence: kcat=1.4 s^-1; Km=10 mM; kcat/Km=0.14 s^-1 mM^-1; exported floating representation is 0.13999999999999999.

raw_value_unit_evidence: Table 1 D-Alanine racemization row: Km=10 +/- 1 mM; kcat=1.4 +/- 0.1 s^-1; kcat/Km=0.14 +/- 0.02 mM^-1 s^-1.

row_label: D-Alanine; Racemization

table_label: Table 1. Steady-state kinetic parameters for L- and D-alanine


column_label: Valid package PDF page 4 (journal page 476), Table 1, L-Alanine row within Racemization, columns Km, kcat, and kcat/Km.

normalized_value_unit_evidence: kcat=1.05 s^-1; Km=10 mM; printed kcat/Km=0.10 s^-1 mM^-1. Exported 0.10500000000000001 is the same-row 1.05/10 quotient and lies within the printed uncertainty.

row_label: L-Alanine; Racemization


substrate_name: L-Alanine methyl ester

substrate: L-Alanine methyl ester


organism: Geobacillus stearothermophilus

substrate_name: D-Lysine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10724 and applied mutation signature I222T/Y354W to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; buffer KPB

column_label: Table I (Kinetic parameters of racemases), Alanine racemase block, enzyme form I222T/Y354W, substrate Lys, direction D to L; column kcat (min^-1) = 1.5 x 10^2; column Km (mM) = 18; column kcat/Km (min^-1 mM^-1) = 8.3.

normalized_value_unit_evidence: kcat: printed Table I cell 1.5 x 10^2 min^-1; 1 min^-1 is 1/60 s^-1, so 150.0 / 60 = 2.5 s^-1. Km: printed Table I cell 18 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 18.0 mM. kcat/Km: printed Table I cell 8.3 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 8.3 / 60 = 0.13833333333333334 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Alanine racemase block, enzyme form I222T/Y354W, substrate Lys, direction D to L: kcat = 1.5 x 10^2 min^-1; Km = 18 mM; printed kcat/Km = 8.3 min^-1 mM^-1.

row_label: Table I, Alanine racemase block, enzyme form I222T/Y354W row, substrate Lys, direction D to L

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

substrate: D-Lysine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10724 and applied mutation signature I222T to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic parameters of racemases), Alanine racemase block, enzyme form I222T, substrate Ala, direction L to D; column kcat (min^-1) = 8.5 x 10^4; column Km (mM) = 4.7; column kcat/Km (min^-1 mM^-1) = 1.8 x 10^4.

normalized_value_unit_evidence: kcat: printed Table I cell 8.5 x 10^4 min^-1; 1 min^-1 is 1/60 s^-1, so 85000.0 / 60 = 1416.6666666666667 s^-1. Km: printed Table I cell 4.7 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 4.7 mM. kcat/Km: printed Table I cell 1.8 x 10^4 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 18000.0 / 60 = 300.0 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Alanine racemase block, enzyme form I222T, substrate Ala, direction L to D: kcat = 8.5 x 10^4 min^-1; Km = 4.7 mM; printed kcat/Km = 1.8 x 10^4 min^-1 mM^-1.

row_label: Table I, Alanine racemase block, enzyme form I222T row, substrate Ala, direction L to D


column_label: Table I (Kinetic parameters of racemases), Alanine racemase block, enzyme form I222T/Y354W, substrate Ala, direction L to D; column kcat (min^-1) = 6.8 x 10^4; column Km (mM) = 8.3; column kcat/Km (min^-1 mM^-1) = 8.2 x 10^3.

normalized_value_unit_evidence: kcat: printed Table I cell 6.8 x 10^4 min^-1; 1 min^-1 is 1/60 s^-1, so 68000.0 / 60 = 1133.3333333333333 s^-1. Km: printed Table I cell 8.3 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 8.3 mM. kcat/Km: printed Table I cell 8.2 x 10^3 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 8200.0 / 60 = 136.66666666666666 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Alanine racemase block, enzyme form I222T/Y354W, substrate Ala, direction L to D: kcat = 6.8 x 10^4 min^-1; Km = 8.3 mM; printed kcat/Km = 8.2 x 10^3 min^-1 mM^-1.

row_label: Table I, Alanine racemase block, enzyme form I222T/Y354W row, substrate Ala, direction L to D


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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10724 and applied mutation signature Y354W to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic parameters of racemases), Alanine racemase block, enzyme form Y354W, substrate Ala, direction L to D; column kcat (min^-1) = 6.8 x 10^4; column Km (mM) = 4.5; column kcat/Km (min^-1 mM^-1) = 1.5 x 10^4.

normalized_value_unit_evidence: kcat: printed Table I cell 6.8 x 10^4 min^-1; 1 min^-1 is 1/60 s^-1, so 68000.0 / 60 = 1133.3333333333333 s^-1. Km: printed Table I cell 4.5 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 4.5 mM. kcat/Km: printed Table I cell 1.5 x 10^4 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 15000.0 / 60 = 250.0 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Alanine racemase block, enzyme form Y354W, substrate Ala, direction L to D: kcat = 6.8 x 10^4 min^-1; Km = 4.5 mM; printed kcat/Km = 1.5 x 10^4 min^-1 mM^-1.

row_label: Table I, Alanine racemase block, enzyme form Y354W row, substrate Ala, direction L to D


substrate_name: L-lysine

column_label: Table I (Kinetic parameters of racemases), Alanine racemase block, enzyme form I222T/Y354W, substrate Lys, direction L to D; column kcat (min^-1) = 2.5 x 10^2; column Km (mM) = 32; column kcat/Km (min^-1 mM^-1) = 7.8.

normalized_value_unit_evidence: kcat: printed Table I cell 2.5 x 10^2 min^-1; 1 min^-1 is 1/60 s^-1, so 250.0 / 60 = 4.166666666666667 s^-1. Km: printed Table I cell 32 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 32.0 mM. kcat/Km: printed Table I cell 7.8 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 7.8 / 60 = 0.13 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Alanine racemase block, enzyme form I222T/Y354W, substrate Lys, direction L to D: kcat = 2.5 x 10^2 min^-1; Km = 32 mM; printed kcat/Km = 7.8 min^-1 mM^-1.

row_label: Table I, Alanine racemase block, enzyme form I222T/Y354W row, substrate Lys, direction L to D

substrate: L-lysine


column_label: Table I (Kinetic parameters of racemases), Alanine racemase block, enzyme form I222T, substrate Ala, direction D to L; column kcat (min^-1) = 5.9 x 10^4; column Km (mM) = 2.6; column kcat/Km (min^-1 mM^-1) = 2.3 x 10^4.

normalized_value_unit_evidence: kcat: printed Table I cell 5.9 x 10^4 min^-1; 1 min^-1 is 1/60 s^-1, so 59000.0 / 60 = 983.3333333333334 s^-1. Km: printed Table I cell 2.6 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 2.6 mM. kcat/Km: printed Table I cell 2.3 x 10^4 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 23000.0 / 60 = 383.3333333333333 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Alanine racemase block, enzyme form I222T, substrate Ala, direction D to L: kcat = 5.9 x 10^4 min^-1; Km = 2.6 mM; printed kcat/Km = 2.3 x 10^4 min^-1 mM^-1.

row_label: Table I, Alanine racemase block, enzyme form I222T row, substrate Ala, direction D to L


column_label: Table I (Kinetic parameters of racemases), Alanine racemase block, enzyme form I222T/Y354W, substrate Ala, direction D to L; column kcat (min^-1) = 3.8 x 10^4; column Km (mM) = 4.0; column kcat/Km (min^-1 mM^-1) = 9.5 x 10^3.

normalized_value_unit_evidence: kcat: printed Table I cell 3.8 x 10^4 min^-1; 1 min^-1 is 1/60 s^-1, so 38000.0 / 60 = 633.3333333333334 s^-1. Km: printed Table I cell 4.0 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 4.0 mM. kcat/Km: printed Table I cell 9.5 x 10^3 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 9500.0 / 60 = 158.33333333333334 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Alanine racemase block, enzyme form I222T/Y354W, substrate Ala, direction D to L: kcat = 3.8 x 10^4 min^-1; Km = 4.0 mM; printed kcat/Km = 9.5 x 10^3 min^-1 mM^-1.

row_label: Table I, Alanine racemase block, enzyme form I222T/Y354W row, substrate Ala, direction D to L


column_label: Table I (Kinetic parameters of racemases), Alanine racemase block, enzyme form Y354W, substrate Ala, direction D to L; column kcat (min^-1) = 3.1 x 10^4; column Km (mM) = 2.3; column kcat/Km (min^-1 mM^-1) = 1.3 x 10^4.

normalized_value_unit_evidence: kcat: printed Table I cell 3.1 x 10^4 min^-1; 1 min^-1 is 1/60 s^-1, so 31000.0 / 60 = 516.6666666666666 s^-1. Km: printed Table I cell 2.3 mM; the printed unit is already the canonical millimolar unit, so no unit conversion applies and Km = 2.3 mM. kcat/Km: printed Table I cell 1.3 x 10^4 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 13000.0 / 60 = 216.66666666666666 s^-1 mM^-1.

raw_value_unit_evidence: Table I, Alanine racemase block, enzyme form Y354W, substrate Ala, direction D to L: kcat = 3.1 x 10^4 min^-1; Km = 2.3 mM; printed kcat/Km = 1.3 x 10^4 min^-1 mM^-1.

row_label: Table I, Alanine racemase block, enzyme form Y354W row, substrate Ala, direction D to L


organism: Caldanaerobacter subterraneus subsp. tengcongensis

substrate_name: L-alanine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q360I to reconstruct the assayed variant sequence.

column_label: Table 2, Kinetic parameters of wild-type and mutant AlrTt; row Q360I; columns under L-Ala to D-Ala: Km (mM), kcat (s^-1), and kcat/Km; printed cells are Km 136.00±2.88 mM, kcat 286.64±19.84 s^-1, kcat/Km 2.11 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q360W to reconstruct the assayed variant sequence.

column_label: Table 2, Kinetic parameters of wild-type and mutant AlrTt; row Q360W; columns under L-Ala to D-Ala: Km (mM), kcat (s^-1), and kcat/Km; printed cells are Km 176.11±13.22 mM, kcat 612.43±30.63 s^-1, kcat/Km 3.48 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q360Y to reconstruct the assayed variant sequence.

column_label: Table 2, Kinetic parameters of wild-type and mutant AlrTt; row Q360Y; columns under L-Ala to D-Ala: Km (mM), kcat (s^-1), and kcat/Km; printed cells are Km 87.81±8.72 mM, kcat 431.46±22.52 s^-1, kcat/Km 4.91 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S173D with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

column_label: Table 2, Kinetic parameters of wild-type and mutant AlrTt; row S173D; columns under L-Ala to D-Ala: Km (mM), kcat (s^-1), and kcat/Km; printed cells are Km 157.53±10.42 mM, kcat 34.69±1.57 s^-1, kcat/Km 0.22 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S173D/Q360Y to reconstruct the assayed variant sequence.

column_label: Table 2, Kinetic parameters of wild-type and mutant AlrTt; row Q360Y&S173D; columns under L-Ala to D-Ala: Km (mM), kcat (s^-1), and kcat/Km; printed cells are Km 83.10±8.78 mM, kcat 246.48±8.11 s^-1, kcat/Km 2.97 s^-1 mM^-1.


column_label: Table 2, Kinetic parameters of wild-type and mutant AlrTt; row WT; columns under L-Ala to D-Ala: Km (mM), kcat (s^-1), and kcat/Km; printed cells are Km 780.20±25.89 mM, kcat 212.38±4.09 s^-1, kcat/Km 0.27 s^-1 mM^-1.

row_label: WT


column_label: Table 2, Kinetic parameters of wild-type and mutant AlrTt; row Q360I; columns under D-Ala to L-Ala: Km (mM), kcat (s^-1), and kcat/Km; printed cells are Km 110.31±6.12 mM, kcat 224.98±7.80 s^-1, kcat/Km 2.04 s^-1 mM^-1.


column_label: Table 2, Kinetic parameters of wild-type and mutant AlrTt; row Q360W; columns under D-Ala to L-Ala: Km (mM), kcat (s^-1), and kcat/Km; printed cells are Km 216.09±4.28 mM, kcat 633.45±45.52 s^-1, kcat/Km 2.93 s^-1 mM^-1.


column_label: Table 2, Kinetic parameters of wild-type and mutant AlrTt; row Q360Y; columns under D-Ala to L-Ala: Km (mM), kcat (s^-1), and kcat/Km; printed cells are Km 52.03±5.41 mM, kcat 251.21±18.82 s^-1, kcat/Km 4.83 s^-1 mM^-1.


column_label: Table 2, Kinetic parameters of wild-type and mutant AlrTt; row S173D; columns under D-Ala to L-Ala: Km (mM), kcat (s^-1), and kcat/Km; printed cells are Km 160.92±13.72 mM, kcat 32.54±0.94 s^-1, kcat/Km 0.2 s^-1 mM^-1.


column_label: Table 2, Kinetic parameters of wild-type and mutant AlrTt; row Q360Y&S173D; columns under D-Ala to L-Ala: Km (mM), kcat (s^-1), and kcat/Km; printed cells are Km 58.48±7.29 mM, kcat 133.08±7.17 s^-1, kcat/Km 2.27 s^-1 mM^-1.


column_label: Table 2, Kinetic parameters of wild-type and mutant AlrTt; row WT; columns under D-Ala to L-Ala: Km (mM), kcat (s^-1), and kcat/Km; printed cells are Km 381.22±9.27 mM, kcat 96.86±10.71 s^-1, kcat/Km 0.25 s^-1 mM^-1.


organism: Streptococcus pyogenes

substrate_name: D-Glutamate

substrate: D-Glutamate


organism: Peribacillus psychrosaccharolyticus

substrate_name: pyridoxal phosphate

column_label: The abstract reports a Km value of 5.0 microM for the pyridoxal 5-phosphate cofactor.

raw_value_unit_evidence: Km raw_value=5.0 microM raw_unit=microM

row_label: Prose segment: pyridoxal 5-phosphate Km

table_label: PubMed PMID 10080917 abstract

substrate: pyridoxal phosphate


substrate_name: D-alanine

column_label: Primary PDF page 5 / printed page 337: Km values at 30 C for D-alanine and L-alanine were 12.2 and 17.9 mM, respectively.

raw_value_unit_evidence: Km raw_value=12.2 mM raw_unit=mM.

row_label: D-alanine

table_label: Primary article PDF page 5 / printed page 337, Results prose

substrate: D-alanine


organism: Escherichia coli

substrate_name: D-Alanine

substrate: D-Alanine


organism: Candidatus Pelagibacter ubique

column_label: Table 2 (Steady state kinetic parameters for MBP-PuCBL, wMelCBL and TmCBL), Enzyme block 'MBP-PuCBL', Function row 'ALR', Conditions column '37 C, Tris'; column 'kcat (s^-1)' = 0.15; column 'KM (mM)' = 12; column 'kcat/KM (s^-1 M^-1)' = 12. The ALR line is the only line this Enzyme block prints for that activity, and the block prints no second buffer or temperature for it.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.15 s^-1; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 0.15 s^(-1). Km: printed Table 2 cell 12 mM; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 12.0 mM. kcat/Km: printed Table 2 cell 12 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 12 / 1000 = 0.012 s^-1 mM^-1. Closure disclosure: the quotient of this row's own two printed component cells is 0.15 / 12 = 0.012499999999999999 s^-1 mM^-1, against the printed efficiency cell 0.012 s^-1 mM^-1 carried at the two-significant-figure precision of the printed efficiency column.

raw_value_unit_evidence: Table 2, Enzyme block 'MBP-PuCBL', Function row 'ALR', Conditions '37 C, Tris': kcat = 0.15 s^-1; KM = 12 mM; printed kcat/KM = 12 s^-1 M^-1.


organism: Mycobacterium tuberculosis


organism: Clostridioides difficile

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

column_label: Table 2: Kinetic parameters for D-proline and C4DHyp. (PLOS ONE 2015, PMID 25786142). Column heads: Enzymes | Substrates | Specific activity a (units/mg protein) | K m (mM) | k cat (min-1) | k cat/K m (min-1 mM-1) | ProRHypE. The cited row is the one whose enzyme cell reads 'CdProR' and whose substrate cell reads 'D-Proline'; in that row the column 'K m (mM)' prints 0.612, the column 'k cat (min-1)' prints 149, the column 'k cat/K m (min-1 mM-1)' prints 245, and the column 'Specific activity a (units/mg protein)' prints the activity restated in the decoded line.

normalized_value_unit_evidence: K m: printed Table 2 cell 0.612 mM; the column head is K m (mM), so no conversion is needed and the paper value is 0.612 mM (the exported value is 0.612 mM). k cat: printed Table 2 cell 149 min-1; 1 min^-1 is 1/60 s^-1, so 149 / 60 = 2.4833333333333334 s^-1 (the exported value is 2.48 s^-1). k cat/K m: printed Table 2 cell 245 min-1 mM-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 245 / 60 = 4.083333333333333 s^-1 mM^-1 (the exported value is 4.052287581699346 s^-1 mM^-1).

raw_value_unit_evidence: Table 2 (Table 2: Kinetic parameters for D-proline and C4DHyp. (PLOS ONE 2015, PMID 25786142)), enzyme row 'CdProR', substrate cell 'D-Proline': column 'K m (mM)' = 0.612; column 'k cat (min-1)' = 149; column 'k cat/K m (min-1 mM-1)' = 245.

row_label: Table 2, row with enzyme 'CdProR' and substrate 'D-Proline'


column_label: Table 1: Kinetic parameters for L-proline, T4LHyp, and T3LHyp. (PLOS ONE 2015, PMID 25786142). Column heads: Enzymes | Substrates | Specific activity a (units/mg protein) | K m (mM) | k cat (min-1) | k cat/K m (min-1 mM-1) | ProRHypE. The cited row is the one whose enzyme cell reads 'CdProR' and whose substrate cell reads 'L-Proline'; in that row the column 'K m (mM)' prints 8.53, the column 'k cat (min-1)' prints 849, the column 'k cat/K m (min-1 mM-1)' prints 99.6, and the column 'Specific activity a (units/mg protein)' prints the activity restated in the decoded line.

normalized_value_unit_evidence: K m: printed Table 1 cell 8.53 mM; the column head is K m (mM), so no conversion is needed and the paper value is 8.53 mM (the exported value is 8.53 mM). k cat: printed Table 1 cell 849 min-1; 1 min^-1 is 1/60 s^-1, so 849 / 60 = 14.15 s^-1 (the exported value is 14.15 s^-1). k cat/K m: printed Table 1 cell 99.6 min-1 mM-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 99.6 / 60 = 1.66 s^-1 mM^-1 (the exported value is 1.6588511137162956 s^-1 mM^-1).

raw_value_unit_evidence: Table 1 (Table 1: Kinetic parameters for L-proline, T4LHyp, and T3LHyp. (PLOS ONE 2015, PMID 25786142)), enzyme row 'CdProR', substrate cell 'L-Proline': column 'K m (mM)' = 8.53; column 'k cat (min-1)' = 849; column 'k cat/K m (min-1 mM-1)' = 99.6.

row_label: Table 1, row with enzyme 'CdProR' and substrate 'L-Proline'


organism: Bacillus subtilis


organism: Ferroplasma acidarmanus

column_label: Table 2. Kinetic parameters for D-proline and C4DHyp; row FaProR WT / D-Proline; columns Km, kcat, kcat/Km report normalized values kcat=0.118167 s^-1, Km=1.17 mM, kcat/Km=0.1015 s^-1*mM^-1.

raw_value_unit_evidence: FaProR WT / D-Proline; kcat raw_value=7.09 +/- 0.12 min^-1; Km raw_value=1.17 +/- 0.09 mM; kcat/Km raw_value=6.09 +/- 0.35 min^-1*mM^-1.

row_label: FaProR WT / D-Proline


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:S0APF4 and applied mutation signature F240W to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters for L-proline, T4LHyp, and T3LHyp. (PLOS ONE 2015, PMID 25786142). Column heads: Enzymes | Substrates | Specific activity a (units/mg protein) | K m (mM) | k cat (min-1) | k cat/K m (min-1 mM-1) | ProRHypE. The cited row is the one whose enzyme cell reads 'FaProRF240W' and whose substrate cell reads 'L-Proline'; in that row the column 'K m (mM)' prints 53.0, the column 'k cat (min-1)' prints 25.0, the column 'k cat/K m (min-1 mM-1)' prints 0.473, and the column 'Specific activity a (units/mg protein)' prints the activity restated in the decoded line.

normalized_value_unit_evidence: K m: printed Table 1 cell 53.0 mM; the column head is K m (mM), so no conversion is needed and the paper value is 53.0 mM (the exported value is 53.0 mM). k cat: printed Table 1 cell 25.0 min-1; 1 min^-1 is 1/60 s^-1, so 25.0 / 60 = 0.4166666666666667 s^-1 (the exported value is 0.42 s^-1). k cat/K m: printed Table 1 cell 0.473 min-1 mM-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.473 / 60 = 0.007883333333333332 s^-1 mM^-1 (the exported value is 0.007924528301886792 s^-1 mM^-1).

raw_value_unit_evidence: Table 1 (Table 1: Kinetic parameters for L-proline, T4LHyp, and T3LHyp. (PLOS ONE 2015, PMID 25786142)), enzyme row 'FaProRF240W', substrate cell 'L-Proline': column 'K m (mM)' = 53.0; column 'k cat (min-1)' = 25.0; column 'k cat/K m (min-1 mM-1)' = 0.473.

row_label: Table 1, row with enzyme 'FaProRF240W' and substrate 'L-Proline'


column_label: Table 1. Kinetic parameters for L-proline, T4LHyp, and T3LHyp; row FaProR WT / L-Proline; columns Km, kcat, kcat/Km report normalized values kcat=0.596667 s^-1, Km=31.6 mM, kcat/Km=0.0188333 s^-1*mM^-1.

raw_value_unit_evidence: FaProR WT / L-Proline; kcat raw_value=35.8 +/- 5.6 min^-1; Km raw_value=31.6 +/- 5.3 mM; kcat/Km raw_value=1.13 +/- 0.01 min^-1*mM^-1.

row_label: FaProR WT / L-Proline


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


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


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

column_label: Abstract states that at 37 degrees C the Km values for L-alanine and D-alanine are 8.2 and 2.1 mM respectively.

raw_value_unit_evidence: Km raw_value=2.1 raw_unit=mM

row_label: Salmonella typhimurium DadB alanine racemase with D-alanine

table_label: PubMed abstract PMID 6391537


substrate_name: L-Ala

substrate: L-Ala


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)


organism: Penaeus monodon

substrate_name: D-Ala

substrate: D-Ala


organism: Mycobacterium avium


organism: Staphylococcus aureus

column_label: Table 3 and Results report AlrSas D -> L direction Km = 0.89 mM.

raw_value_unit_evidence: Km raw_value=0.89 raw_unit=mM

row_label: AlrSas D -> L direction

table_label: PMC3245724 Table 3 / enzyme kinetics comparison


organism: Thermotoga maritima


organism: Trypanosoma cruzi

column_label: The JBC full text states that rTcPRACA has Km of 29 mM and Vmax of 5.3 x 10^-5 mol*s^-1 under the Figure 3 kinetic assay.

raw_value_unit_evidence: Km raw_value=29 mM raw_unit=mM

row_label: rTcPRACA L-proline Km

table_label: JBC full text Functional Analysis prose and Figure 3


organism: Limosilactobacillus fermentum

substrate_name: (R)-glutamate

column_label: Abstract states the enzyme follows Michaelis-Menten kinetics with a Km of 0.3 mM in each reaction direction.

raw_value_unit_evidence: Km raw_value=0.3 raw_unit=mM

row_label: Lactobacillus fermenti glutamate racemase in each glutamate racemization direction

table_label: PubMed abstract PMID 8385993

substrate: (R)-glutamate


organism: Homo sapiens

substrate_name: L-serine

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

substrate: L-serine


substrate_name: L-threonine

substrate: L-threonine


organism: Aquifex pyrophilus

substrate_name: D-glutamate

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=8.5

source_databases_merged: brenda skid

substrate: D-glutamate


organism: Wolbachia pipientis

column_label: Table 2 (Steady state kinetic parameters for MBP-PuCBL, wMelCBL and TmCBL), Enzyme block 'wMelCBL', Function row 'ALR', Conditions column '37 C, Tris'; column 'kcat (s^-1)' = 2.3; column 'KM (mM)' = 3.8; column 'kcat/KM (s^-1 M^-1)' = 580. The ALR line is the only line this Enzyme block prints for that activity, and the block prints no second buffer or temperature for it.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.3 s^-1; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 2.3 s^(-1). Km: printed Table 2 cell 3.8 mM; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 3.8 mM. kcat/Km: printed Table 2 cell 580 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 580 / 1000 = 0.58 s^-1 mM^-1. Closure disclosure: the quotient of this row's own two printed component cells is 2.3 / 3.8 = 0.6052631578947368 s^-1 mM^-1, against the printed efficiency cell 0.58 s^-1 mM^-1 carried at the two-significant-figure precision of the printed efficiency column.

raw_value_unit_evidence: Table 2, Enzyme block 'wMelCBL', Function row 'ALR', Conditions '37 C, Tris': kcat = 2.3 s^-1; KM = 3.8 mM; printed kcat/KM = 580 s^-1 M^-1.

substrate: L-alanine


organism: Bacillus anthracis

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

assay_conditions_summary: pH 9.2; 298.15 K; cofactor NAD+

proof_lines: recombinant wild type enzyme, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml d

proof_lines: recombinant wild type enzyme, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol

proof_lines: recombinant wild type enzyme, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/mL d


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

proof_lines: mutant Q86A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.

proof_lines: mutant Q86A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol


proof_lines: mutant Y221A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0

proof_lines: mutant Y221A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol


proof_lines: mutant K106A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0

proof_lines: mutant K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol


proof_lines: mutant R214A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0

proof_lines: mutant R214A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol


proof_lines: mutant K29A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.

proof_lines: mutant K29A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol

proof_lines: mutant K29A, in 10 mM potassium phosphate (pH 8.2)and 0.2 mM dithiothreitol


proof_lines: mutant R25A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.

proof_lines: mutant R25A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol


proof_lines: mutant P99A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.

proof_lines: mutant P99A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol


proof_lines: mutant R214A/K106A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase,

proof_lines: mutant R214A/K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol


organism: Clostridioides difficile

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


organism: Clostridium perfringens


organism: Geobacillus stearothermophilus

proof_lines: pH 8.0, 30°C, recombinant mutant I222T/Y354W


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


organism: Trypanosoma cruzi (strain CL Brener)

assay_conditions_summary: pH 6

column_label: The JBC full text states that rTcPRACB enzyme has Km of 75 mM and Vmax of 2 x 10^-4 mol*s^-1 under the Figure 3 kinetic assay.

raw_value_unit_evidence: Km raw_value=75 mM raw_unit=mM

row_label: rTcPRACB L-proline Km


organism: Helicobacter pylori


proof_lines: demonstrates a high degree of asymmetry in substrate processing with the Michaelis constant for D-glutamate approximately tenfold lower than for L-glutamate


proof_lines: value above 100 for deletion mutant E151K


substrate_name: Unknown

proof_lines: potent competitive inhibitor for RacE2 mutant V149A

substrate: Unknown


organism: Bacillus subtilis

substrate_name: protoporphyrin IX

proof_lines: pH 7.2, 30°C. The Km-value for protoporphyrin IX is the same independent of whether Zn2+ or Fe2+ is used in the reaction

substrate: protoporphyrin IX


proof_lines: RacE2 mutant enzyme S207A, pH and temperature not specified in the publication


proof_lines: RacE2 mutant enzyme K106A, pH and temperature not specified in the publication


substrate_name: L-glutamate

column_label: Table 2 (Steady state kinetic parameters for MBP-PuCBL, wMelCBL and TmCBL), Enzyme block 'wMelCBL', Function row 'GLR', Conditions column '37 C, Tris'; column 'kcat (s^-1)' = 0.017; column 'KM (mM)' = 0.80; column 'kcat/KM (s^-1 M^-1)' = 21. The GLR line is the only line this Enzyme block prints for that activity, and the block prints no second buffer or temperature for it.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.017 s^-1; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 0.017 s^(-1). Km: printed Table 2 cell 0.80 mM; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 0.8 mM. kcat/Km: printed Table 2 cell 21 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 21 / 1000 = 0.021 s^-1 mM^-1. Closure disclosure: the quotient of this row's own two printed component cells is 0.017 / 0.80 = 0.02125 s^-1 mM^-1, against the printed efficiency cell 0.021 s^-1 mM^-1 carried at the two-significant-figure precision of the printed efficiency column.

raw_value_unit_evidence: Table 2, Enzyme block 'wMelCBL', Function row 'GLR', Conditions '37 C, Tris': kcat = 0.017 s^-1; KM = 0.80 mM; printed kcat/KM = 21 s^-1 M^-1.

substrate: L-glutamate


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines: mutant T76A, at 25°C in 50 mM Tris-HCl (pH 8.0), 5 mM NAD+, 0.5 mM iodonitrotetrazolium chloride, 2.5 mM ADP, 20 units of L-glutamate dehydrogenase, 2 units of diaphorase and D-glutamate

proof_lines: mutant T76A, at 25°C in 50 mM Tris-HCl, pH 8.0, 5 mM NAD+, 0.5 mM iodonitrotetrazolium chloride, 2.5 mM ADP, 20 units of L-glutamate dehydrogenase, 2 units of diaphorase and D-glutamate


proof_lines: wild type enzyme, at 25°C in 50 mM Tris-HCl, pH 8.0, 5 mM NAD+, 0.5 mM iodonitrotetrazolium chloride, 2.5 mM ADP, 20 units of L-glutamate dehydrogenase, 2 units of diaphorase and D-glutamate

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

proof_lines: wild type enzyme, 50 mM boric acid, 100 mM KCl, 0.2 mM dithiothreitol, pH 8.0, at 25°C in the presence of 0.22 microM glutamate racemase


proof_lines:
or higher, wild-type, 37°C, pH 9.1
wild-type, 37°C, pH 9.1


proof_lines: pH 8.5, temperature not specified in the publication, recombinant wild-type enzyme

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


proof_lines: pH 8.5, temperature not specified in the publication, recombinant mutant K271T


organism: Fusobacterium nucleatum

substrate_name: D-homocysteic acid

substrate: D-homocysteic acid


assay_conditions_summary: pH 8; 303.15 K; buffer potassium phosphate

proof_lines: His-tagged recombinant BsGR, in potassium phosphate buffer (10 mM, pH 8.0)


proof_lines: pH 8, 30°C, mutant enzyme D36N and H152Q


enzyme_display_name: protoporphyrin ferrochelatase

proof_lines: no added cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin

proof_lines: 0.5% cholate, for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin

enzyme: protoporphyrin ferrochelatase


substrate_name: deuteroporphyrin IX

proof_lines: for the human ferrochelatase (R115L)-catalyzed insertion of zinc into deuteroporphyrin

substrate: deuteroporphyrin IX


enzyme_display_name: protein disulfide-isomerase

substrate_name: RNAse A

enzyme: protein disulfide-isomerase

substrate: RNAse A


proof_lines: mutant PDI without two Cys in domains a' and a


enzyme_display_name: prostaglandin-I synthase

substrate_name: 15-hydroperoxyeicosatetraenoic acid

smiles: CCCCCC(C=CC=CCC=CCC=CCCCC(=O)O)OO

proof_lines:
pH 7.5, 23°C, heterolytic cleavage
pH 7.5, 23°C, homolytic cleavage

enzyme: prostaglandin-I synthase

substrate: 15-hydroperoxyeicosatetraenoic acid


enzyme_display_name: thromboxane-A synthase

enzyme: thromboxane-A synthase


substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


organism: Lactuca sativa


substrate_name: mesoporphyrin

substrate: mesoporphyrin


organism: Hyphomicrobium sp.


enzyme_display_name: sirohydrochlorin cobaltochelatase

organism: Methanosarcina barkeri

substrate_name: sirohydrochlorin

enzyme: sirohydrochlorin cobaltochelatase

substrate: sirohydrochlorin


organism: Lathyrus oleraceus


substrate_name: alpha-D-Glucose 1,6-bisphosphate

substrate: alpha-D-Glucose 1,6-bisphosphate


organism: Leishmania donovani


enzyme_display_name: 4-hydroxyproline epimerase

organism: Thermococcus litoralis

enzyme: 4-hydroxyproline epimerase


organism: Escherichia coli

substrate_name: D-alanine

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

proof_lines: +/-0.033, Alr D164K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-0.250, Alr D164K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-0.070, Alr D164K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

substrate: D-alanine


proof_lines: +/-0.100, Alr E165K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-0.850, Alr E165K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-0.079, Alr E165K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm


proof_lines: +/-0.417, Alr E165A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-2.667, Alr E165A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-0.085, Alr E165A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm


proof_lines: +/-0.200, Alr D164A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-2.600, Alr D164A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-0.032, Alr D164A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm


proof_lines: +/-0.333, Alr P219A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-6.067, Alr P219A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-0.034, Alr P219A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm


proof_lines: +/-0.483, Alr wildtype, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-3.217, Alr wildtype, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-0.008, Alr wildtype, 30°C, pH 8.0, spectrophotometrically measured at 340 nm


proof_lines: +/-0.333, Alr E221K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-7.550, Alr E221K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-0.055, Alr E221K, 30°C, pH 8.0, spectrophotometrically measured at 340 nm


proof_lines: +/-0.650, Alr E221A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-2.333, Alr E221A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-0.080, Alr E221A, 30°C, pH 8.0, spectrophotometrically measured at 340 nm


proof_lines: +/-0.750, Alr E221P, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-7.633, Alr E221P, 30°C, pH 8.0, spectrophotometrically measured at 340 nm

proof_lines: +/-0.084, Alr E221P, 30°C, pH 8.0, spectrophotometrically measured at 340 nm


enzyme_display_name: arginine racemase

organism: Pseudomonas taetrolens

substrate_name: L-alanine / D-alanine

assay_conditions_summary: pH 10; 310.15 K; buffer 0.6 M CHES-NaOH

proof_lines: wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C

proof_lines: wild type enzyme,in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C

enzyme: arginine racemase

substrate: L-alanine / D-alanine


proof_lines: mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C

proof_lines: mutant enzyme C74A/C73A ,in 0.6 M CHES-NaOH buffer (pH 10.0). 0.1 mM pyridoxal 5'-phosphate, at 37°C

proof_lines: mutant enzyme C74A/C73A, in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C


substrate_name: D-ornithine / L-ornithine

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

substrate: D-ornithine / L-ornithine


substrate_name: D-Lysine / L-lysine

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

substrate: D-Lysine / L-lysine


proof_lines: wild type enzyme, in 0.6 M CHES-NaOH buffer (pH 10.0), 0.1 mM pyridoxal 5'-phosphate, at 37°C


substrate_name: L-arginine / D-arginine

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

substrate: L-arginine / D-arginine


enzyme_display_name: amino-acid racemase

organism: Geobacillus kaustophilus

substrate_name: N-acetyl-L-asparagine

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

enzyme: amino-acid racemase

substrate: N-acetyl-L-asparagine


substrate_name: N-acetyl-D-tryptophan

substrate: N-acetyl-D-tryptophan


substrate_name: N-acetyl-D-alanine

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

substrate: N-acetyl-D-alanine


substrate_name: N-carbamoyl-L-methionine

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

substrate: N-carbamoyl-L-methionine


substrate_name: N-succinyl-L-phenylalanine

substrate: N-succinyl-L-phenylalanine


substrate_name: N-acetyl-D-phenylalanine

substrate: N-acetyl-D-phenylalanine


substrate_name: N-acetyl-D-methionine

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

substrate: N-acetyl-D-methionine


substrate_name: N-succinyl-L-alanine

substrate: N-succinyl-L-alanine


organism: Pseudomonas graveolens

substrate_name: pyridoxal 5'-phosphate

substrate: pyridoxal 5'-phosphate


substrate_name: D-Arg

substrate: D-Arg


substrate_name: L-leucine

substrate: L-leucine


substrate_name: D-methionine

substrate: D-methionine


organism: Ferroplasma acidarmanus


organism: Leishmania mexicana


enzyme_display_name: lysine racemase

organism: uncultured bacterium

substrate_name: D-Lysine

proof_lines: in 50 mM Tris-HCl (pH 8.0), 2 mM cobalt chloride at 30°C

enzyme: lysine racemase

substrate: D-Lysine


substrate_name: N-Succinyl-L-Arg

substrate: N-Succinyl-L-Arg


organism: Mus musculus

substrate_name: L-serine

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

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

substrate: L-serine


enzyme_display_name: threonine racemase

organism: Dictyostelium discoideum

substrate_name: L-allo-threonine

enzyme: threonine racemase

substrate: L-allo-threonine


substrate_name: D-allo-threonine

substrate: D-allo-threonine


organism: Proteus mirabilis

substrate_name: L-lysine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S394Y with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

substrate: L-lysine


substrate_name: L-arginine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S394C with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

substrate: L-arginine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S394T with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S394N with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


proof_lines: kcat is 3326 min(-1) with L-lysine as substrate. kcat is 650 min(-1) with L-arginine as substrate.


enzyme_display_name: Delta(3)-Delta(2)-enoyl-CoA isomerase

organism: Homo sapiens

assay_conditions_summary: pH 8.5; 298.15 K; cofactor CoA

enzyme: Delta(3)-Delta(2)-enoyl-CoA isomerase


organism: Thermococcus kodakarensis


substrate_name: L-methionine

substrate: L-methionine


organism: Pyrococcus horikoshii

substrate_name: D-Trp

assay_conditions_summary: pH 7

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

substrate: D-Trp


substrate_name: L-Tyr

substrate: L-Tyr


substrate_name: D-Phe

substrate: D-Phe


substrate_name: L-Val

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

substrate: L-Val


substrate_name: L-Ile

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

substrate: L-Ile


substrate_name: D-Leu

substrate: D-Leu


substrate_name: L-Met

substrate: L-Met


substrate_name: D-Ala

substrate: D-Ala


organism: Oenococcus oeni

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

proof_lines: pH 8.0, 30°C, recombinant mutant T224I/W355Y


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


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


substrate_name: L-ornithine

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

substrate: L-ornithine


substrate_name: D-Lysine

substrate: D-Lysine


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

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

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

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


proof_lines: kcat is 2.1 min(-1) for L-lysine. kcat is 1.7 min(-1) for D-lysine. kcat is 1.1 min(-1) for L-ornithine. kcat is 1.1 min(-1) for D-ornithine.


proof_lines: kcat is 109.0 sec(-1) with L-lysine as substrate. kcat is 104.0 sec(-1) with D-lysine as substrate. kcat is 119.0 sec(-1) with L-arginine as substrate. kcat is 119.0 sec(-1) with D-arginine as substrate. kcat is 87.7 sec(-1) with L-ornithin


substrate_name: L-alanine

substrate: L-alanine


organism: Aplysia californica

substrate_name: L-aspartate

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

assay_conditions_summary: pH 8; buffer 50 mM Tris-HCl

proof_lines: in 50 mM Tris-HCl buffer, pH 8.0, at 30°C

substrate: L-aspartate


substrate_name: L-serine

assay_conditions_summary: pH 8.5; buffer 50 mM Tris-HCl

proof_lines: in 50 mM Tris-HCl buffer, pH 8.5, for Ser reactions, at 30°C

substrate: L-serine


organism: Latilactobacillus sakei

substrate_name: D-alanine

proof_lines: pH 10.0, 35°C, recombinant His-tagged enzyme

substrate: D-alanine


organism: Pseudomonas putida

proof_lines: kcat is 4238 min(-1) with L-alanine as substrate (PubMed:22806802). kcat is 3545 min(-1) with L-lysine as substrate. kcat is 2228 min(-1) with L-arginine as substrate (PubMed:23118975).


organism: Escherichia coli (strain K12)

substrate_name: L-homoserine

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

proof_lines: kcat is 7.84 min(-1) with L-homoserine as substrate. kcat is 1.15 min(-1) with D-homoserine as substrate.

substrate: L-homoserine


enzyme_display_name: diaminopimelate epimerase

organism: Mycobacterium tuberculosis

substrate_name: meso-diaminoheptanedioate

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

proof_lines: recombinant DapF consisting of silent mutation of the first 10 codons of the open reading frame

enzyme: diaminopimelate epimerase

substrate: meso-diaminoheptanedioate


enzyme_display_name: ornithine racemase

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

substrate_name: L-lysine

proof_lines: kcat is 693 sec(-1) with L-lysine as substrate. kcat is 669 sec(-1) with D-lysine as substrate. kcat is 537 sec(-1) with L-ornithine as substrate. kcat is 447 sec(-1) with D-ornithine as substrate. kcat is 965 sec(-1) with L-alanine as subs

enzyme: ornithine racemase

substrate: L-lysine


organism: Haemophilus influenzae

proof_lines: kcat is 128 and 82 sec(-1) for L,L-DAP and D,L-DAP, respectively.


organism: Paracoccus denitrificans (strain Pd 1222)


organism: Acetoanaerobium sticklandii

proof_lines: kcat is 1660 sec(-1) for L-ornithine as substrate (PubMed:19251850). kcat is 980 sec(-1) for L-ornithine as substrate (PubMed:10715017).


organism: Pseudomonas putida (strain ATCC 700007 / DSM 6899 / JCM 31910 / BCRC 17059 / LMG 24140 / F1)

proof_lines: kcat is 26 sec(-1) for t4LHyp epimerization. kcat is 4.8 sec(-1) for t3LHyp epimerization. kcat is 2.8 sec(-1) for L-proline racemization.


substrate_name: L-proline

substrate: L-proline


organism: Rhizobium etli (strain ATCC 51251 / DSM 11541 / JCM 21823 / NBRC 15573 / CFN 42)

proof_lines: kcat is 1.9 sec(-1) for t4LHyp epimerization. kcat is 0.94 sec(-1) for t3LHyp epimerization.


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

column_label: Table 2: Kinetic constants for 3/4HypE and t3HypD activities of the screened PRS targets; row Cluster 3 / BMEI1586 / D0B556 / 4HypE; Km raw 4.5 ± 1 mM normalized 4.5 mM; kcat raw 0.082 ± 0.005 s^-1 normalized 0.082 s^-1; kcat/KM raw 18 M^-1 s^-1 normalized 0.018 s^-1 mM^-1.

row_label: Cluster 3 / BMEI1586 / D0B556 / 4HypE


proof_lines: kcat is 0.082 sec(-1) for t4LHyp epimerization. kcat is 0.085 sec(-1) for t3LHyp epimerization.


organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)

proof_lines: kcat is 1.68 sec(-1) with L-alanine as substrate. kcat is 4.68 sec(-1) with L-serine as substrate. kcat is 2.94 sec(-1) with L-methionine as substrate. kcat is 2.30 sec(-1) with L-leucine as substrate. kcat is 2.59 sec(-1) with L-glutamine


substrate_name: L-methionine

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

substrate: L-methionine


substrate_name: L-leucine

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

substrate: L-leucine


substrate_name: L-glutamine

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

substrate: L-glutamine


substrate_name: L-asparagine

substrate: L-asparagine


substrate_name: L-arginine

substrate: L-arginine


organism: Burkholderia multivorans (strain ATCC 17616 / 249)

proof_lines: kcat is 5.6 sec(-1) for trans-4-hydroxy-L-proline epimerization. kcat is 0.34 sec(-1) for trans-3-hydroxy-L-proline epimerization.


organism: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)

proof_lines: kcat is 28 sec(-1) for t4LHyp epimerization. kcat is 1.3 sec(-1) for t3LHyp epimerization.


organism: Roseibium alexandrii (strain DSM 17067 / NCIMB 14079 / DFL-11)

proof_lines: kcat is 67 sec(-1) for t4LHyp epimerization.


organism: Proteus mirabilis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T391Y/S394Y to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 50°C, recombinant His-tagged mutant T391Y/S394Y


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T391Y to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 50°C, recombinant His-tagged mutant T391Y


assay_conditions_summary: pH 9

column_label: Table 4; row Wild-type Lyr; L-Arg columns kcat (min^-1), Km (mM), and kcat/Km (B); cells 650, 14.9, and 43.6; assay at 50 C and pH 9.0.

raw_value_unit_evidence: Table 4 Wild-type Lyr L-Arg cells: kcat 650 min^-1; Km 14.9 mM; kcat/Km 43.6 min^-1*mM^-1.

row_label: Wild-type Lyr | L-Arg

table_label: Table 4. Kinetic Parameters for Wild-type Lyr and Bar, and Their Mutants


column_label: Table 4; row Wild-type Lyr; L-Lys columns kcat (min^-1), Km (mM), and kcat/Km (A); cells 3326, 21.8, and 152.6; assay at 50 C and pH 9.0.

raw_value_unit_evidence: Table 4 Wild-type Lyr L-Lys cells: kcat 3326 min^-1; Km 21.8 mM; kcat/Km 152.6 min^-1*mM^-1.

row_label: Wild-type Lyr | L-Lys


organism: Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37)

proof_lines: kcat is 89 sec(-1) for t4LHyp epimerization. kcat is 2.4 sec(-1) for t3LHyp epimerization.


proof_lines: kcat is 0.064 sec(-1) for t4LHyp epimerization.


proof_lines: kcat is 4238 min(-1) with L-alanine as substrate (PubMed:22806802). kcat is 3545 min(-1) with L-lysine as substrate. kcat is 2228 min(-1) with L-arginine as substrate (PubMed:23118975).


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

substrate_name: D-lysine

proof_lines: kcat is 274.5 sec(-1) with D-lysine as substrate. kcat is 1681.7 sec(-1) with L-lysine as substrate. kcat is 8.83 sec(-1) with D-alanine as substrate. kcat is 7.33 sec(-1) with L-alanine as substrate. Thus, the catalytic efficiency with lys

substrate: D-lysine


organism: Bacillus subtilis (strain 168)

proof_lines: kcat is 0.08 min(-1) with L-lysine as substrate. kcat is 0.224 min(-1) with D-lysine as substrate.


organism: Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / KCTC 9067 / NCIMB 10171 / NRRL 2505 / NI 9100)

proof_lines: kcat is 14 sec(-1) for t4LHyp epimerization.


substrate_name: L,L-DAP

proof_lines: kcat is 56.2 sec(-1) with L,L-DAP as substrate. kcat is 79.1 sec(-1) with meso-DAP as substrate. kcat is 10.1 sec(-1) with L-Lys as substrate. kcat is 11.2 sec(-1) with D-Lys as substrate.

substrate: L,L-DAP


substrate_name: L-Lys

substrate: L-Lys


substrate_name: Unknown

substrate: Unknown


organism: Escherichia coli (strain K12)

proof_lines: kcat is 7.84 min(-1) with L-homoserine as substrate. kcat is 1.15 min(-1) with D-homoserine as substrate.


organism: Pseudomonas putida


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


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

proof_lines: kcat is 693 sec(-1) with L-lysine as substrate. kcat is 669 sec(-1) with D-lysine as substrate. kcat is 537 sec(-1) with L-ornithine as substrate. kcat is 447 sec(-1) with D-ornithine as substrate. kcat is 965 sec(-1) with L-alanine as subs


organism: Roseibium aggregatum (strain ATCC 25650 / DSM 13394 / JCM 20685 / NBRC 16684 / NCIMB 2208 / IAM 12614 / B1)

column_label: Table 2, SIAM614_28492 / A0NXQ7 / 4HypE row reports K_M 3.2 +/- 0.5.

normalized_value_unit_evidence: K_M 3.2 mM

table_label: Table 2


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


organism: Brucella suis biovar 1 (strain 1330)


organism: Burkholderia pseudomallei (strain K96243)


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


organism: Shewanella loihica (strain ATCC BAA-1088 / PV-4)


organism: Agrobacterium fabrum (strain C58 / ATCC 33970)

proof_lines: kcat is 27 sec(-1) for t3LHyp dehydration. kcat is 0.40 sec(-1) for t4LHyp epimerization.


proof_lines: kcat is 0.86 sec(-1) for t4LHyp epimerization. kcat is 4.0 sec(-1) for t3LHyp epimerization.


organism: Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264)

column_label: Table 2, BTH_II2067 / Q2T3J4 / 4HypE row reports K_M 1.4 +/- 0.4.

normalized_value_unit_evidence: K_M 1.4 mM

row_label: BTH_II2067 / Q2T3J4 / 4HypE


enzyme_display_name: trans-L-3-hydroxyproline dehydratase

column_label: Table 2, BTH_II2067 / Q2T3J4 / t3HypD row reports K_M 26 +/- 9.

normalized_value_unit_evidence: K_M 26 mM

row_label: BTH_II2067 / Q2T3J4 / t3HypD

enzyme: trans-L-3-hydroxyproline dehydratase


organism: Latilactobacillus sakei

substrate_name: L-alanine

column_label: Table 4 columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 mM^-1); row Racemase / L-Ala.

normalized_value_unit_evidence: kcat 2.31 x 10^3 s^-1 = 2310 s^-1; Km 169 mM; kcat/Km table value 13.7 s^-1 mM^-1, consistent with expected 13.668639053254438 by displayed rounding.

row_label: Racemase; L-Ala

table_label: Table 4: Kinetic parameters of racemase and beta-lyase reactions

substrate: L-alanine


substrate_name: D-Alanine

column_label: Table 4 columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 mM^-1); row Racemase / D-Ala.

row_label: Racemase; D-Ala

substrate: D-Alanine


organism: Allorhizobium ampelinum (strain ATCC BAA-846 / DSM 112012 / S4)

proof_lines: kcat is 1.3 sec(-1) for t4LHyp epimerization. kcat is 0.75 sec(-1) for t3LHyp epimerization.


organism: Proteus mirabilis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T391Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T391Y/S394Y to reconstruct the assayed variant sequence.

column_label: Table 4 row Lyr-T391Y/ S394Y; L-Lys columns kcat = 154 min^-1, Km = 34.3 mM, kcat/Km (A) = 4.5 min^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=2.566666666666667 normalized_unit=s^-1; km normalized_value=34.3 normalized_unit=mM; kcat_over_km normalized_value=0.075 normalized_unit=s^-1*mM^-1; conversions=154/60 and 4.5/60

raw_value_unit_evidence: kcat raw_value=154 raw_unit=min^-1; Km raw_value=34.3 raw_unit=mM; kcat/Km raw_value=4.5 raw_unit=min^-1*mM^-1


column_label: Table 4 row Wild-type Lyr; L-Lys columns kcat = 3326 min^-1, Km = 21.8 mM, kcat/Km (A) = 152.6 min^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=55.43333333333333 normalized_unit=s^-1; km normalized_value=21.8 normalized_unit=mM; kcat_over_km normalized_value=2.5433333333333333 normalized_unit=s^-1*mM^-1; conversions=3326/60 and 152.6/60

raw_value_unit_evidence: kcat raw_value=3326 raw_unit=min^-1; Km raw_value=21.8 raw_unit=mM; kcat/Km raw_value=152.6 raw_unit=min^-1*mM^-1

row_label: Wild-type Lyr


substrate_name: L-Arginine

substrate: L-Arginine


column_label: Table 4 row Lyr-T391Y/ S394Y; L-Arg columns kcat = 23 min^-1, Km = 75.5 mM, kcat/Km (B) = 0.3 min^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.38333333333333336 normalized_unit=s^-1; km normalized_value=75.5 normalized_unit=mM; kcat_over_km normalized_value=0.005 normalized_unit=s^-1*mM^-1; conversions=23/60 and 0.3/60

raw_value_unit_evidence: kcat raw_value=23 raw_unit=min^-1; Km raw_value=75.5 raw_unit=mM; kcat/Km raw_value=0.3 raw_unit=min^-1*mM^-1