enzyme_display_name: Phenylalanine dehydrogenase

organism: Caldalkalibacillus thermarum (strain TA2.A1)

substrate_name: phenylpyruvate

proof_lines: kcat is 74.8 sec(-1) with phenylpyruvate as substrate. kcat is 56.2 sec(-1) with ketoleucine as substrate. kcat is 2.2 sec(-1) with 2-oxo-4-phenylbutyrate as substrate.

enzyme: Phenylalanine dehydrogenase

substrate: phenylpyruvate


substrate_name: ketoleucine

source_db: uniprot

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

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

data_origin: experimental

substrate: ketoleucine

status: unverified

source: uniprot


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


smiles: N


enzyme_display_name: Meso-diaminopimelate D-dehydrogenase

organism: Lysinibacillus sphaericus

verification_status: verified

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

assay_conditions_summary: pH 7.5; cofactor NADP+

column_label: The official JBC article abstract lists the Michaelis constant for meso-2,6-diaminoheptanedioate; the exported Km value matches after microM-to-mM normalization where needed.

table_label: Official JBC article abstract: Michaelis constants prose

enzyme: Meso-diaminopimelate D-dehydrogenase

status: verified


substrate_name: NADP(+)

column_label: The official JBC article abstract lists the Michaelis constant for NADP(+); the exported Km value matches after microM-to-mM normalization where needed.

raw_value_unit_evidence: NADP+ (83 microM).

row_label: NADP+ Michaelis constant

substrate: NADP(+)


substrate_name: NADPH

assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: The official JBC article abstract lists the Michaelis constant for NADPH; the exported Km value matches after microM-to-mM normalization where needed.

raw_value_unit_evidence: NADPH (0.2 mM).

row_label: NADPH Michaelis constant

substrate: NADPH


column_label: The official JBC article abstract lists the Michaelis constant for L-2-amino-6-oxoheptanedioate; the exported Km value matches after microM-to-mM normalization where needed.


substrate_name: ammonia

column_label: The official JBC article abstract lists the Michaelis constant for ammonia; the exported Km value matches after microM-to-mM normalization where needed.

raw_value_unit_evidence: ammonia (12.5 mM).

row_label: ammonia Michaelis constant

substrate: ammonia


enzyme_display_name: phenylalanine dehydrogenase

substrate_name: L-phenylalanine

source_db: brenda

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E313G to reconstruct the assayed variant sequence.

mutation_type: substitution

enzyme: phenylalanine dehydrogenase

substrate: L-phenylalanine

source: brenda


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D209G with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


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


organism: Bacillus badius

assay_conditions_summary: pH 10.4; 298.15 K; buffer pH 10; cofactor NAD+

column_label: Table 1; row Wild-Type; exact primary cells km=0.08 mM; kcat=50 s^-1; kcat_over_km=609 s^-1 mM^-1; printed page 46.

raw_value_unit_evidence: Table 1 row Wild-Type: km=0.08 mM; kcat=50 s^-1; kcat_over_km=609 s^-1 mM^-1.

row_label: Wild-Type

table_label: Table 1


substrate_name: L-tyrosine

column_label: Table 2; row Wild-Type; exact primary cells km=8.6 mM; kcat=58 s^-1; kcat_over_km=6.7 s^-1 mM^-1; printed page 46.

raw_value_unit_evidence: Table 2 row Wild-Type: km=8.6 mM; kcat=58 s^-1; kcat_over_km=6.7 s^-1 mM^-1.

table_label: Table 2

substrate: L-tyrosine


enzyme_display_name: Valine dehydrogenase

organism: Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858)

substrate_name: L-valine

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

proof_lines: kcat is 47.5 sec(-1) for the oxidative deamination of L-valine. kcat is 314.5 sec(-1) for the reductive amination of 3-methyl-2-oxobutanoate.

enzyme: Valine dehydrogenase

substrate: L-valine


substrate_name: NAD(+)

assay_conditions_summary: cofactor NAD+

substrate: NAD(+)


enzyme_display_name: aspartate dehydrogenase

organism: Thermotoga maritima

substrate_name: L-Asp

sequence_source: multiple

proof_lines:
cofactor NAD+
+/- 0.02, with NAD+
cofactor NADP+

source_databases_merged: brenda uniprot

enzyme: aspartate dehydrogenase

substrate: L-Asp


substrate_name: NAD+

proof_lines: pH and temperature not specified in the publication

substrate: NAD+


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


organism: Bacillus thermotolerans

substrate_name: 2-oxo-4-phenylbutyric acid

proof_lines: kcat is 0.53 sec(-1) with 2-oxo-4-phenylbutyric acid as substrate. kcat is 58.91 sec(-1) with CPOA as substrate. kcat is 0.048 sec(-1) with benzoylformic acid as substrate. kcat is 146.30 sec(-1) with NADH as substrate.

substrate: 2-oxo-4-phenylbutyric acid


substrate_name: benzoylformic acid

substrate: benzoylformic acid


organism: Thermoactinomyces intermedius

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K69A/K81A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K81A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K69A to reconstruct the assayed variant sequence.


substrate_name: L-Phe

substrate: L-Phe


organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)

substrate_name: phenylacetone

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K66Q/S149G/N262C with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K66Q/S149G/N262C, at pH 9.6 and 30°C

substrate: phenylacetone


organism: Sporosarcina ureae

proof_lines:
pH 10.4, 25°C, native enzyme
pH 10.4, 30°C, native enzyme
pH 10.4, 25°C, immobilized enzyme


assay_conditions_summary: pH 10.4; cofactor NAD+

proof_lines:
pH 10.4, 25°C, immobilized enzyme
pH 10.4, 25°C, native enzyme


substrate_name: L-Leu

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

substrate: L-Leu


enzyme_display_name: UniProt P04964

organism: Corynebacterium glutamicum

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P04964

source: skid


enzyme_display_name: UniProt Q67PI3

organism: Symbiobacterium thermophilum

enzyme: UniProt Q67PI3


enzyme_display_name: diaminopimelate dehydrogenase

organism: Ureibacillus thermosphaericus

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

proof_lines:
pH 8.5, 30°C
Raw SKiD Env: Temp=30°C, pH=8.5

source_databases_merged: brenda skid

enzyme: diaminopimelate dehydrogenase


organism: Pseudomonas putida


substrate_name: NAD+; L-Phenylalanine; H2O

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

substrate: NAD+; L-Phenylalanine; H2O


substrate_name: oxidized beta-nicotinamide hypoxanthine dinucleotide


enzyme_display_name: L-tryptophan dehydrogenase

organism: Nostoc punctiforme

proof_lines: kcat is 4.2 sec(-1) with L-tryptophan as substrate. kcat is 4.3 sec(-1) with NAD(+) as substrate. kcat is 16 sec(-1) with indole-3-pyruvate as substrate. kcat is 21 sec(-1) with NADH as substrate. kcat is 17 sec(-1) with NH4(+) as substrate

enzyme: L-tryptophan dehydrogenase


substrate_name: NADP+; H2O; L-Aspartate

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

substrate: NADP+; H2O; L-Aspartate


km_display: Not reported

ki_unit: mM


enzyme_display_name: valine dehydrogenase (NAD+)

organism: Kitasatospora aureofaciens

proof_lines: pH 10.4, temperature not specified in the publication

enzyme: valine dehydrogenase (NAD+)


substrate_name: pyruvate

substrate: pyruvate


substrate_name: L-norleucine

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

substrate: L-norleucine


organism: Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)

substrate_name: Unknown

substrate: Unknown


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


organism: Nostoc punctiforme (strain ATCC 29133 / PCC 73102)


substrate_name: CPOA

substrate: CPOA


organism: Lysinibacillus sphaericus

substrate_name: NAD+; H2O; L-Phenylalanine

assay_conditions_summary: pH 10.4; 298.15 K; cofactor NAD+

substrate: NAD+; H2O; L-Phenylalanine


sequence_variant_note: Mutation signature N145A/H4C could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 8.5; 298.15 K; buffer 50mM pH 8; cofactor NADH

proof_lines: mutant enzyme N145A, at 25°C inTris buffer 50mM pH 8.5, with NADH (0.1 mM), KCl (100 mM) and NH4Cl (400 mM)


substrate_name: L-isoleucine

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

column_label: Table 4; substrate row L-isoleucine; enzyme row wt; metric columns Km, kcat, kcat/Km

normalized_value_unit_evidence: normalized: Km=0.14 mM; kcat=0.14 s^-1; kcat/Km=1 s^-1 mM^-1

row_label: Lysinibacillus sphaericus / wt / L-isoleucine

table_label: Table 4

substrate: L-isoleucine


substrate_name: L-leucine

verification_status: corrected

column_label: Table 4; substrate row L-leucine; enzyme row wt; metric columns Km, kcat, kcat/Km

normalized_value_unit_evidence: normalized: Km=0.55 mM; kcat=0.7 s^-1; kcat/Km=1.3 s^-1 mM^-1

row_label: Lysinibacillus sphaericus / wt / L-leucine

substrate: L-leucine

status: corrected


substrate_name: L-valine

column_label: Table 4; substrate row L-valine; enzyme row wt; metric columns Km, kcat, kcat/Km

normalized_value_unit_evidence: normalized: Km=2 mM; kcat=0.91 s^-1; kcat/Km=0.46 s^-1 mM^-1

row_label: Lysinibacillus sphaericus / wt / L-valine

substrate: L-valine


substrate_name: L-methionine

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

column_label: Table 4; substrate row L-methionine; enzyme row wt; metric columns Km, kcat, kcat/Km

normalized_value_unit_evidence: normalized: Km=2.7 mM; kcat=1.2 s^-1; kcat/Km=0.44 s^-1 mM^-1

row_label: Lysinibacillus sphaericus / wt / L-methionine

substrate: L-methionine


substrate_name: L-norvaline

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

column_label: Table 4; substrate row L-norvaline; enzyme row wt; metric columns Km, kcat, kcat/Km

normalized_value_unit_evidence: normalized: Km=3.3 mM; kcat=1.4 s^-1; kcat/Km=0.42 s^-1 mM^-1

row_label: Lysinibacillus sphaericus / wt / L-norvaline

substrate: L-norvaline


column_label: Table 4; substrate row L-norleucine; enzyme row wt; metric columns Km, kcat, kcat/Km

normalized_value_unit_evidence: normalized: Km=0.79 mM; kcat=3.2 s^-1; kcat/Km=4 s^-1 mM^-1

row_label: Lysinibacillus sphaericus / wt / L-norleucine


assay_conditions_summary: pH 10.4; buffer pH 10; cofactor NAD+

column_label: Table 5; row alpha-ketoisocaproate / WT; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1); PDF page 5/8, article page 11394.

normalized_value_unit_evidence: Paper normalized required metrics: kcat=27.0 s^-1; Km=20.0 mM; kcat/Km=1.4 s^-1 mM^-1. Exported required metrics: kcat=27.0 s^-1; Km=20.0 mM; kcat/Km=1.35 s^-1 mM^-1.

raw_value_unit_evidence: Table 5 cells: Km=20 mM; kcat=27 s^-1; kcat/Km=1.4 s^-1 mM^-1.

row_label: alpha-ketoisocaproate / WT

table_label: Table 5


substrate_name: alpha-keto-gamma-methiobutyrate

column_label: Table 5; substrate row alpha-keto-gamma-methiobutyrate; enzyme row wt; metric columns Km, kcat, kcat/Km

normalized_value_unit_evidence: normalized: Km=11 mM; kcat=27 s^-1; kcat/Km=3.7 s^-1 mM^-1

row_label: Lysinibacillus sphaericus / wt / alpha-keto-gamma-methiobutyrate

substrate: alpha-keto-gamma-methiobutyrate


substrate_name: alpha-ketovalerate

column_label: Table 5; row alpha-ketovalerate / WT; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1); PDF page 5/8, article page 11394.

normalized_value_unit_evidence: Paper normalized required metrics: kcat=33.0 s^-1; Km=52.0 mM; kcat/Km=0.63 s^-1 mM^-1. Exported required metrics: kcat=33.0 s^-1; Km=52.0 mM; kcat/Km=0.6346153846153846 s^-1 mM^-1.

raw_value_unit_evidence: Table 5 cells: Km=52 mM; kcat=33 s^-1; kcat/Km=0.63 s^-1 mM^-1.

row_label: alpha-ketovalerate / WT

substrate: alpha-ketovalerate


substrate_name: alpha-Ketocaproate

smiles: CCCCC(=O)C(=O)O

column_label: Table 5; row alpha-ketocaproate / WT; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1); PDF page 5/8, article page 11394.

normalized_value_unit_evidence: Paper normalized required metrics: kcat=51.0 s^-1; Km=13.0 mM; kcat/Km=3.9 s^-1 mM^-1. Exported required metrics: kcat=51.0 s^-1; Km=13.0 mM; kcat/Km=3.923076923076923 s^-1 mM^-1.

raw_value_unit_evidence: Table 5 cells: Km=13 mM; kcat=51 s^-1; kcat/Km=3.9 s^-1 mM^-1.

row_label: alpha-ketocaproate / WT

substrate: alpha-Ketocaproate


substrate_name: H2O; L-Phenylalanine; NAD+

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

substrate: H2O; L-Phenylalanine; NAD+


organism: Archaeoglobus fulgidus

substrate_name: H2O; L-Aspartate; NAD+

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

substrate: H2O; L-Aspartate; NAD+


organism: Thermosyntropha lipolytica

assay_conditions_summary: pH 10.5; buffer pH 10; cofactor NADP+

column_label: Table 2, meso-DAP row: turnover number 4.42 x 10^3 min^-1; Km 5.68 mM; catalytic efficiency 7.78 x 10^2 min^-1 mM^-1.

normalized_value_unit_evidence: kcat normalized_value=73.66666666666667 normalized_unit=s^-1; Km normalized_value=5.68 normalized_unit=mM; kcat/Km normalized_value=12.966666666666667 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: meso-DAP row: kcat raw_value=4.42 x 10^3 raw_unit=min^-1; Km raw_value=5.68 raw_unit=mM; kcat/Km raw_value=7.78 x 10^2 raw_unit=min^-1*mM^-1.

row_label: meso-DAP

table_label: Table 2, PDF page 3


substrate_name: NAD+

column_label: Table 2, NAD+ row: turnover number 4.65 x 10^3 min^-1; Km 14.8 mM; catalytic efficiency 3.13 x 10^2 min^-1 mM^-1.

normalized_value_unit_evidence: kcat normalized_value=77.5 normalized_unit=s^-1; Km normalized_value=14.8 normalized_unit=mM; kcat/Km normalized_value=5.216666666666667 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: NAD+ row: kcat raw_value=4.65 x 10^3 raw_unit=min^-1; Km raw_value=14.8 raw_unit=mM; kcat/Km raw_value=3.13 x 10^2 raw_unit=min^-1*mM^-1.

row_label: NAD+

substrate: NAD+


substrate_name: NADP+

column_label: Table 2, NADP+ row: turnover number 4.98 x 10^3 min^-1; Km 0.828 mM; catalytic efficiency 6.01 x 10^3 min^-1 mM^-1.

normalized_value_unit_evidence: kcat normalized_value=83 normalized_unit=s^-1; Km normalized_value=0.828 normalized_unit=mM; kcat/Km normalized_value=100.16666666666667 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: NADP+ row: kcat raw_value=4.98 x 10^3 raw_unit=min^-1; Km raw_value=0.828 raw_unit=mM; kcat/Km raw_value=6.01 x 10^3 raw_unit=min^-1*mM^-1.

row_label: NADP+

substrate: NADP+


source_db: oed

assay_conditions_summary: pH 10.5; 323.15 K; buffer pH 10; cofactor NADP+

source: oed


organism: Bacillus badius

substrate_name: L-tyrosine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q59224 and applied mutation signature V144D to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type and mutant B. badius PheDH enzymes for L-tyrosine substrates (Archives of Biochemistry and Biophysics 635 (2017) 44-51), enzyme row 'V144D'; column 'Km L-tyrosine (mM)' = 27; column 'K Cat (s^-1)' = 28; column 'K cat/Km (S^-1/mM^-1)' = 1.

normalized_value_unit_evidence: Km: printed Table 2 cell 27 mM; the printed unit is already mM, so no unit conversion applies and the normalized value is 27.0 mM. kcat: printed Table 2 cell 28 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 28.0 s^(-1). kcat/Km: printed Table 2 cell 1 s^-1 mM^-1 (the decoded form of the printed head S^-1/mM^-1); the printed unit is already the canonical ratio unit, so no unit conversion applies and the normalized value is 1.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row V144D, substrate L-tyrosine: Km = 27 mM; kcat = 28 s^-1; printed kcat/Km = 1 s^-1 mM^-1.

row_label: Table 2, enzyme row 'V144D', substrate column 'L-tyrosine'

substrate: L-tyrosine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q59224 and applied mutation signature V144L to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type and mutant B. badius PheDH enzymes for L-tyrosine substrates (Archives of Biochemistry and Biophysics 635 (2017) 44-51), enzyme row 'V144L'; column 'Km L-tyrosine (mM)' = 11.9; column 'K Cat (s^-1)' = 26; column 'K cat/Km (S^-1/mM^-1)' = 2.2.

normalized_value_unit_evidence: Km: printed Table 2 cell 11.9 mM; the printed unit is already mM, so no unit conversion applies and the normalized value is 11.9 mM. kcat: printed Table 2 cell 26 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 26.0 s^(-1). kcat/Km: printed Table 2 cell 2.2 s^-1 mM^-1 (the decoded form of the printed head S^-1/mM^-1); the printed unit is already the canonical ratio unit, so no unit conversion applies and the normalized value is 2.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row V144L, substrate L-tyrosine: Km = 11.9 mM; kcat = 26 s^-1; printed kcat/Km = 2.2 s^-1 mM^-1.

row_label: Table 2, enzyme row 'V144L', substrate column 'L-tyrosine'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q59224 and applied mutation signature V144N to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type and mutant B. badius PheDH enzymes for L-tyrosine substrates (Archives of Biochemistry and Biophysics 635 (2017) 44-51), enzyme row 'V144N'; column 'Km L-tyrosine (mM)' = 4.7; column 'K Cat (s^-1)' = 57; column 'K cat/Km (S^-1/mM^-1)' = 11.9.

normalized_value_unit_evidence: Km: printed Table 2 cell 4.7 mM; the printed unit is already mM, so no unit conversion applies and the normalized value is 4.7 mM. kcat: printed Table 2 cell 57 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 57.0 s^(-1). kcat/Km: printed Table 2 cell 11.9 s^-1 mM^-1 (the decoded form of the printed head S^-1/mM^-1); the printed unit is already the canonical ratio unit, so no unit conversion applies and the normalized value is 11.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row V144N, substrate L-tyrosine: Km = 4.7 mM; kcat = 57 s^-1; printed kcat/Km = 11.9 s^-1 mM^-1.

row_label: Table 2, enzyme row 'V144N', substrate column 'L-tyrosine'


column_label: Table 2 Wild-Type L-tyrosine row: Km 8.6 mM; kcat 58 s^-1; kcat/Km 6.7 s^-1 mM^-1.

normalized_value_unit_evidence: Km 8.6 mM; kcat 58 s^(-1); independently printed kcat/Km 6.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Wild-Type row: Km 8.6 mM; kcat 58 s^-1; independently printed kcat/Km 6.7 s^-1 mM^-1.

row_label: Wild-Type

table_label: Table 2. Kinetic parameters of wild-type and mutant PheDHs toward L-tyrosine


substrate_name: L-Phenylalanine

column_label: Table 1: Kinetic parameters of wild type and Mutant B. badius PheDH enzymes for L-phenylalanine substrates (Archives of Biochemistry and Biophysics 635 (2017) 44-51), enzyme row 'V144D'; column 'Km L-phenylalanine (mM)' = 0.06; column 'K Cat (s^-1)' = 13.5; column 'K cat/Km (S^-1/mM^-1)' = 204.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.06 mM; the printed unit is already mM, so no unit conversion applies and the normalized value is 0.06 mM. kcat: printed Table 1 cell 13.5 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 13.5 s^(-1). kcat/Km: printed Table 1 cell 204 s^-1 mM^-1 (the decoded form of the printed head S^-1/mM^-1); the printed unit is already the canonical ratio unit, so no unit conversion applies and the normalized value is 204.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row V144D, substrate L-phenylalanine: Km = 0.06 mM; kcat = 13.5 s^-1; printed kcat/Km = 204 s^-1 mM^-1.

row_label: Table 1, enzyme row 'V144D', substrate column 'L-phenylalanine'

substrate: L-Phenylalanine


column_label: Table 1: Kinetic parameters of wild type and Mutant B. badius PheDH enzymes for L-phenylalanine substrates (Archives of Biochemistry and Biophysics 635 (2017) 44-51), enzyme row 'V144L'; column 'Km L-phenylalanine (mM)' = 0.04; column 'K Cat (s^-1)' = 36; column 'K cat/Km (S^-1/mM^-1)' = 800.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.04 mM; the printed unit is already mM, so no unit conversion applies and the normalized value is 0.04 mM. kcat: printed Table 1 cell 36 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 36.0 s^(-1). kcat/Km: printed Table 1 cell 800 s^-1 mM^-1 (the decoded form of the printed head S^-1/mM^-1); the printed unit is already the canonical ratio unit, so no unit conversion applies and the normalized value is 800.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row V144L, substrate L-phenylalanine: Km = 0.04 mM; kcat = 36 s^-1; printed kcat/Km = 800 s^-1 mM^-1.

row_label: Table 1, enzyme row 'V144L', substrate column 'L-phenylalanine'


column_label: Table 1: Kinetic parameters of wild type and Mutant B. badius PheDH enzymes for L-phenylalanine substrates (Archives of Biochemistry and Biophysics 635 (2017) 44-51), enzyme row 'V144N'; column 'Km L-phenylalanine (mM)' = 0.19; column 'K Cat (s^-1)' = 23; column 'K cat/Km (S^-1/mM^-1)' = 118.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.19 mM; the printed unit is already mM, so no unit conversion applies and the normalized value is 0.19 mM. kcat: printed Table 1 cell 23 s^-1; the printed unit is already s^-1, so no unit conversion applies and the normalized value is 23.0 s^(-1). kcat/Km: printed Table 1 cell 118 s^-1 mM^-1 (the decoded form of the printed head S^-1/mM^-1); the printed unit is already the canonical ratio unit, so no unit conversion applies and the normalized value is 118.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row V144N, substrate L-phenylalanine: Km = 0.19 mM; kcat = 23 s^-1; printed kcat/Km = 118 s^-1 mM^-1.

row_label: Table 1, enzyme row 'V144N', substrate column 'L-phenylalanine'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P22823 and applied mutation signature F124M/V125D/H126I/A127I/A128Y/R129Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9.5; 295.15 K; cofactor NADH

column_label: Table III (Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase), reductive amination rows, substrate row 'a-Ketocaproate', CS2 columns; column 'Km (mM)' = 47; column 'kcat (s^-1)' = 22; column 'kcat/Km (mM^-1 s^-1)' = 0.47; the CS2 efficiency column also prints the parenthesised percentage of the wild-type efficiency, 1.5, which is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table III cell 47 in the column headed Km (mM); mM is already the export unit, so no unit conversion applies; the exported value is 47.0 mM. kcat: printed Table III cell 22 in the column headed kcat (s^-1); s^-1 is already the export unit, so no unit conversion applies; the exported value is 22.0 s^(-1). kcat/Km: printed Table III cell 0.47 in the column headed kcat/Km (mM^-1 s^-1); mM^-1 s^-1 is the export unit s^(-1)*mM^(-1), so no unit conversion applies; the exported value is 0.46808510638297873 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, reductive amination rows, substrate row 'a-Ketocaproate', CS2 columns: Km = 47 mM; kcat = 22 s^-1; printed kcat/Km = 0.47 mM^-1 s^-1.

row_label: Table III, reductive amination rows, substrate row 'a-Ketocaproate', CS2 mutant enzyme columns

table_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase (J. Biochem. 1993, 114(1):69-75)


assay_conditions_summary: pH 9.5; 295.15 K; cofactor NAD+

column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row alpha-ketocaproate / PheDH, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row alpha-ketocaproate, enzyme PheDH: Km 2.5 mM; kcat 79 s^-1; kcat/Km 31 mM^-1 s^-1.

normalized_value_unit_evidence: km 2.5 mM; kcat 79 s^-1; kcat_over_km 31 mM^-1 s^-1

row_label: alpha-ketocaproate / PheDH


column_label: Table III (Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase), reductive amination rows, substrate row 'a-Ketovalerate', CS2 columns; column 'Km (mM)' = 107; column 'kcat (s^-1)' = 4.8; column 'kcat/Km (mM^-1 s^-1)' = 0.045; the CS2 efficiency column also prints the parenthesised percentage of the wild-type efficiency, 2.0, which is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table III cell 107 in the column headed Km (mM); mM is already the export unit, so no unit conversion applies; the exported value is 107.0 mM. kcat: printed Table III cell 4.8 in the column headed kcat (s^-1); s^-1 is already the export unit, so no unit conversion applies; the exported value is 4.8 s^(-1). kcat/Km: printed Table III cell 0.045 in the column headed kcat/Km (mM^-1 s^-1); mM^-1 s^-1 is the export unit s^(-1)*mM^(-1), so no unit conversion applies; the exported value is 0.044859813084112146 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, reductive amination rows, substrate row 'a-Ketovalerate', CS2 columns: Km = 107 mM; kcat = 4.8 s^-1; printed kcat/Km = 0.045 mM^-1 s^-1.

row_label: Table III, reductive amination rows, substrate row 'a-Ketovalerate', CS2 mutant enzyme columns


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F124M/V125D/H126I/A127I/A128Y/R129Q to reconstruct the assayed variant sequence.

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

column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row alpha-keto-beta-methyl-valerate / CS2, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row alpha-keto-beta-methyl-valerate, enzyme CS2: Km 50 mM; kcat 2.5 s^-1; kcat/Km 0.05 mM^-1 s^-1.

normalized_value_unit_evidence: km 50 mM; kcat 2.5 s^-1; kcat_over_km 0.05 mM^-1 s^-1

row_label: alpha-keto-beta-methyl-valerate / CS2


assay_conditions_summary: pH 9.5; 295.15 K; buffer Gly-KCl-KOH; cofactor NAD+

column_label: TABLE III. Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase; substrate row 'alpha-Keto-beta-methyl-valerate'; column group 'Km (mM)' sub-column 'PheDH' = 13; column group 'kcat (s^-1)' sub-column 'PheDH' = 26; column group 'kcat/Km (mM^-1 s^-1)' sub-column 'PheDH' = 2.0.

normalized_value_unit_evidence: Km: printed cell 13 mM, already the catalog unit mM (no uM/1000 step applies). kcat: printed cell 26 s^-1, already the catalog unit s^(-1) (no min^-1/60 step applies). kcat/Km: printed cell 2.0 mM^-1 s^-1 is already s^(-1)*mM^(-1); the exact quotient of this row's own printed cells is 26 / 13 = 2.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III (printed page 74), row 'alpha-Keto-beta-methyl-valerate', wild-type PheDH sub-columns: Km = 13 mM; kcat = 26 s^-1; printed kcat/Km = 2.0 mM^-1 s^-1. Printed line: alpha-Keto-beta-methyl-valerate | 13 | 50 | 26 | 2.5 | 2.0 | 0.050 (2.5)

row_label: Table III, substrate row 'alpha-Keto-beta-methyl-valerate', wild-type PheDH column group


column_label: Table III (Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase), reductive amination rows, substrate row 'a-Ketoisocaproate', CS2 columns; column 'Km (mM)' = 56; column 'kcat (s^-1)' = 7.4; column 'kcat/Km (mM^-1 s^-1)' = 0.13; the CS2 efficiency column also prints the parenthesised percentage of the wild-type efficiency, 2.1, which is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table III cell 56 in the column headed Km (mM); mM is already the export unit, so no unit conversion applies; the exported value is 56.0 mM. kcat: printed Table III cell 7.4 in the column headed kcat (s^-1); s^-1 is already the export unit, so no unit conversion applies; the exported value is 7.4 s^(-1). kcat/Km: printed Table III cell 0.13 in the column headed kcat/Km (mM^-1 s^-1); mM^-1 s^-1 is the export unit s^(-1)*mM^(-1), so no unit conversion applies; the exported value is 0.13214285714285715 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, reductive amination rows, substrate row 'a-Ketoisocaproate', CS2 columns: Km = 56 mM; kcat = 7.4 s^-1; printed kcat/Km = 0.13 mM^-1 s^-1.

row_label: Table III, reductive amination rows, substrate row 'a-Ketoisocaproate', CS2 mutant enzyme columns


column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row alpha-ketoisocaproate / PheDH, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row alpha-ketoisocaproate, enzyme PheDH: Km 9.1 mM; kcat 57 s^-1; kcat/Km 6.2 mM^-1 s^-1.

normalized_value_unit_evidence: km 9.1 mM; kcat 57 s^-1; kcat_over_km 6.2 mM^-1 s^-1

row_label: alpha-ketoisocaproate / PheDH


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

column_label: Table III (Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase), reductive amination rows, substrate row 'a-Keto-y-methyl-thiobutyrate', CS2 columns; column 'Km (mM)' = 87; column 'kcat (s^-1)' = 18; column 'kcat/Km (mM^-1 s^-1)' = 0.21; the CS2 efficiency column also prints the parenthesised percentage of the wild-type efficiency, 1.6, which is not a kinetic constant.

normalized_value_unit_evidence: Km: printed Table III cell 87 in the column headed Km (mM); mM is already the export unit, so no unit conversion applies; the exported value is 87.0 mM. kcat: printed Table III cell 18 in the column headed kcat (s^-1); s^-1 is already the export unit, so no unit conversion applies; the exported value is 18.0 s^(-1). kcat/Km: printed Table III cell 0.21 in the column headed kcat/Km (mM^-1 s^-1); mM^-1 s^-1 is the export unit s^(-1)*mM^(-1), so no unit conversion applies; the exported value is 0.20689655172413793 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, reductive amination rows, substrate row 'a-Keto-y-methyl-thiobutyrate', CS2 columns: Km = 87 mM; kcat = 18 s^-1; printed kcat/Km = 0.21 mM^-1 s^-1.

row_label: Table III, reductive amination rows, substrate row 'a-Keto-y-methyl-thiobutyrate', CS2 mutant enzyme columns


substrate_name: L-Ethionine

assay_conditions_summary: pH 10.8; 295.15 K; cofactor NAD+

column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row L-Ethionine / CS2, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row L-Ethionine, enzyme CS2: Km 4.0 mM; kcat 0.1 s^-1; kcat/Km 0.025 mM^-1 s^-1.

row_label: L-Ethionine / CS2

substrate: L-Ethionine


column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row L-Ethionine / PheDH, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row L-Ethionine, enzyme PheDH: Km 0.27 mM; kcat 1.1 s^-1; kcat/Km 4.0 mM^-1 s^-1.

row_label: L-Ethionine / PheDH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G124A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.6; 298.15 K; cofactor NADH

column_label: Table 2; row=a-Ketocaproate; mutant column=G124A; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 2.1 mM; kcat 64.0 s^-1; kcat/Km 30.476190476190474 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 2 row a-Ketocaproate, mutant column G124A: Km 2.1 mM; kcat 64.0 s^-1; kcat/Km 30.0 s^-1 mM^-1.

row_label: a-Ketocaproate


sequence_variant_note: Resolved canonical sequence from uniprotkb:P23307 and applied mutation signature G124A/L307V to reconstruct the assayed variant sequence.

column_label: Table 2; row=a-Ketocaproate; mutant column=G124A/L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 0.94 mM; kcat 66.0 s^-1; kcat/Km 70.2127659574468 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 2 row a-Ketocaproate, mutant column G124A/L307V: Km 0.94 mM; kcat 66.0 s^-1; kcat/Km 70.0 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L307V to reconstruct the assayed variant sequence.

column_label: Table 2; row=a-Ketocaproate; mutant column=L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 0.69 mM; kcat 17.0 s^-1; kcat/Km 24.637681159420293 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 2 row a-Ketocaproate, mutant column L307V: Km 0.69 mM; kcat 17.0 s^-1; kcat/Km 25.0 s^-1 mM^-1.


column_label: Table 2; row=a-Ketovalerate; mutant column=G124A; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 2.5 mM; kcat 53.0 s^-1; kcat/Km 21.2 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 2 row a-Ketovalerate, mutant column G124A: Km 2.5 mM; kcat 53.0 s^-1; kcat/Km 21.0 s^-1 mM^-1.

row_label: a-Ketovalerate


column_label: Table 2; row=a-Ketovalerate; mutant column=G124A/L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 0.82 mM; kcat 51.0 s^-1; kcat/Km 62.19512195121951 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 2 row a-Ketovalerate, mutant column G124A/L307V: Km 0.82 mM; kcat 51.0 s^-1; kcat/Km 62.0 s^-1 mM^-1.


column_label: Table 2; row=a-Ketovalerate; mutant column=L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 11.0 mM; kcat 33.0 s^-1; kcat/Km 3.0 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 2 row a-Ketovalerate, mutant column L307V: Km 11.0 mM; kcat 33.0 s^-1; kcat/Km 3.0 s^-1 mM^-1.


column_label: Table 2; row=Hydroxyphenylpyruvate; mutant column=L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 0.23 mM; kcat 55.0 s^-1; kcat/Km 239.1304347826087 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 2 row Hydroxyphenylpyruvate, mutant column L307V: Km 0.23 mM; kcat 55.0 s^-1; kcat/Km 239.0 s^-1 mM^-1.

row_label: Hydroxyphenylpyruvate


column_label: Table 2; row=a-Ketoisocaproate; mutant column=G124A; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 0.63 mM; kcat 25.0 s^-1; kcat/Km 39.682539682539684 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 2 row a-Ketoisocaproate, mutant column G124A: Km 0.63 mM; kcat 25.0 s^-1; kcat/Km 40.0 s^-1 mM^-1.

row_label: a-Ketoisocaproate


column_label: Table 2; row=a-Ketoisocaproate; mutant column=G124A/L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 0.36 mM; kcat 24.0 s^-1; kcat/Km 66.66666666666667 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 2 row a-Ketoisocaproate, mutant column G124A/L307V: Km 0.36 mM; kcat 24.0 s^-1; kcat/Km 67.0 s^-1 mM^-1.


column_label: Table 2; row=a-Ketoisocaproate; mutant column=L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 1.4 mM; kcat 7.8 s^-1; kcat/Km 5.571428571428572 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 2 row a-Ketoisocaproate, mutant column L307V: Km 1.4 mM; kcat 7.8 s^-1; kcat/Km 5.6 s^-1 mM^-1.


substrate_name: NADH

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

assay_conditions_summary: pH 9; cofactor NADH

column_label: Prose below Table 4 gives Km values 18.2 mM for NH4+ and 0.023 mM for NADH under standard alpha-ketoisovalerate assay

raw_value_unit_evidence: Km 0.023 mM for NADH

row_label: standard assay with alpha-ketoisovalerate; NADH

table_label: Scanned page 5194 prose after Table 4

substrate: NADH


column_label: Prose: standard alpha-ketoisovalerate assay gives NH4+ 18.2 and NADH 0.023 mM; oxidative deamination prose gives NAD+ 0.10 mM

normalized_value_unit_evidence: sheet NAD+ 0.023 mM not supported; supported NAD+ value is 0.10 mM in a different reaction direction

raw_value_unit_evidence: Paper gives NADH Km 0.023 mM and NAD+ Km 0.10 mM

row_label: standard assay with alpha-ketoisovalerate; NAD+ oxidative cofactor prose


column_label: Table 4 row alpha-Keto-beta-methyl-n-valerate; Km column 6.7 mM; relative activity 22.3%

raw_value_unit_evidence: Km 6.7 mM

row_label: alpha-Keto-beta-methyl-n-valerate

table_label: Table 4. Substrate specificity for reductive amination


proof_lines: L-valine alpha-ketoisovalerate NH4Cl


proof_lines: NH4Cl alpha-ketoisovalerate NADH


enzyme_display_name: L-aspartate dehydrogenase

organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

substrate_name: L-aspartate (in the presence of NAD)

enzyme: L-aspartate dehydrogenase

substrate: L-aspartate (in the presence of NAD)


substrate_name: NAD

substrate: NAD


substrate_name: NADP

substrate: NADP


substrate_name: oxaloacetate (in the presence of NADH and NH(3))

assay_conditions_summary: cofactor NADH

column_label: Abstract metric sentence maps oxaloacetate to 1.2 mM Km

raw_value_unit_evidence: Km raw_value=1.2 raw_unit=mM

row_label: oxaloacetate item in reductive amination Km sentence

table_label: PMID 16731057 PubMed abstract


substrate_name: NADH (in the presence of oxaloacetate and NH(3))

column_label: Abstract metric sentence maps NADH to 0.014 mM Km

raw_value_unit_evidence: Km raw_value=0.014 raw_unit=mM

row_label: NADH item in reductive amination Km sentence


substrate_name: NH(3) (in the presence of oxaloacetate and NADH)

column_label: Abstract metric sentence maps ammonia/NH(3) to 167 mM Km

raw_value_unit_evidence: Km raw_value=167 raw_unit=mM

row_label: ammonia item in reductive amination Km sentence


substrate_name: meso-2,6-diaminoheptanedioate (at 30 degrees Celsius and pH 10.5)


substrate_name: NADP(+) (at 30 degrees Celsius and pH 10.5)

assay_conditions_summary: pH 10.5; cofactor NADP+


substrate_name: L-2-amino-6-oxoheptanedioate (at 30 degrees Celsius and pH 10.5)

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


substrate_name: NADPH (at 30 degrees Celsius and pH 10.5)

assay_conditions_summary: pH 10.5; cofactor NADPH


substrate_name: ammonia (at 30 degrees Celsius and pH 10.5)


raw_value_unit_evidence: Km 18.2 mM for NH4+

row_label: standard assay with alpha-ketoisovalerate; NH4+


enzyme_display_name: tryptophan dehydrogenase

substrate_name: L-tryptophan

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature A69L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 11; 298.15 K; cofactor NAD+

column_label: Table 2 | A69L NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 1.1 +/- 0.047 mM | kcat 1.2 +/- 0.090 s^-1 | kcat/Km 1.1 mM^-1 s^-1

normalized_value_unit_evidence: kcat=1.2 s^(-1); km=1.1 mM; kcat_over_km=1.1 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row A69L, non-parenthetical L-tryptophan cells

table_label: Table 2: kinetic constants of NpTrpDH mutants

enzyme: tryptophan dehydrogenase

substrate: L-tryptophan


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature A69M to reconstruct the assayed variant sequence.

column_label: Table 2 | A69M NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.82 +/- 0.071 mM | kcat 1.2 +/- 0.058 s^-1 | kcat/Km 1.5 mM^-1 s^-1

normalized_value_unit_evidence: kcat=1.2 s^(-1); km=0.82 mM; kcat_over_km=1.5 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row A69M, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature I296A to reconstruct the assayed variant sequence.

column_label: Table 2 | I296A NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.059 +/- 0.0070 mM | kcat 10 +/- 1.0 s^-1 | kcat/Km 170 mM^-1 s^-1

normalized_value_unit_evidence: kcat=10 s^(-1); km=0.059 mM; kcat_over_km=170 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row I296A, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L288M with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature M295A to reconstruct the assayed variant sequence.

column_label: Table 2 | M295A NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.047 +/- 0.0025 mM | kcat 8.0 +/- 0.58 s^-1 | kcat/Km 170 mM^-1 s^-1

normalized_value_unit_evidence: kcat=8 s^(-1); km=0.047 mM; kcat_over_km=170 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row M295A, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature M40L to reconstruct the assayed variant sequence.

column_label: Table 2 | M40L NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.047 +/- 0.0036 mM | kcat 12 +/- 0.63 s^-1 | kcat/Km 260 mM^-1 s^-1

normalized_value_unit_evidence: kcat=12 s^(-1); km=0.047 mM; kcat_over_km=260 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row M40L, non-parenthetical L-tryptophan cells


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:W8CV45 and applied mutation signature V132A to reconstruct the assayed variant sequence.

column_label: Table 2 | V132A NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.017 +/- 0.0010 mM | kcat 4.6 +/- 0.20 s^-1 | kcat/Km 270 mM^-1 s^-1

normalized_value_unit_evidence: kcat=4.6 s^(-1); km=0.017 mM; kcat_over_km=270 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row V132A, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature V133A to reconstruct the assayed variant sequence.

column_label: Table 2 | V133A NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.019 +/- 0.0019 mM | kcat 2.6 +/- 0.18 s^-1 | kcat/Km 140 mM^-1 s^-1

normalized_value_unit_evidence: kcat=2.6 s^(-1); km=0.019 mM; kcat_over_km=140 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row V133A, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature V291A to reconstruct the assayed variant sequence.

column_label: Table 2 | V291A NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.047 +/- 0.0030 mM | kcat 2.9 +/- 0.12 s^-1 | kcat/Km 62 mM^-1 s^-1

normalized_value_unit_evidence: kcat=2.9 s^(-1); km=0.047 mM; kcat_over_km=62 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row V291A, non-parenthetical L-tryptophan cells


proof_lines:
pH 10, 30°C
Raw SKiD Env: Temp=30°C, pH=10

source_databases_merged: brenda skid uniprot


assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADP+

column_label: Table 1. The kinetic parameter (±SD) of different DapDH for different substrate with NADPH or NADP+ as cofactora.; row UtDapDH / NADPH / Amination / NH4+; columns Km (mmol/L), Kcat (/s), Kcat/Km; cells Km 6.5 +/- 0.5, Kcat 347.7 +/- 25.8, Kcat/Km 53.4.

normalized_value_unit_evidence: Km normalized_value=6.5 normalized_unit=mM; kcat normalized_value=347.7 normalized_unit=s^-1; kcat/Km normalized_value=53.4 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row UtDapDH / NADPH / Amination / NH4+: Km 6.5 +/- 0.5 mmol/L; Kcat 347.7 +/- 25.8 /s; Kcat/Km 53.4.

row_label: UtDapDH / NADPH / Amination / NH4+


column_label: Table 1. The kinetic parameter (±SD) of different DapDH for different substrate with NADPH or NADP+ as cofactora.; row UtDapDH / NADPH / Amination / THDPA; columns Km (mmol/L), Kcat (/s), Kcat/Km; cells Km 0.26 +/- 0.3, Kcat 50.6 +/- 4.5, Kcat/Km 194.6.

normalized_value_unit_evidence: Km normalized_value=0.26 normalized_unit=mM; kcat normalized_value=50.6 normalized_unit=s^-1; kcat/Km normalized_value=194.6 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row UtDapDH / NADPH / Amination / THDPA: Km 0.26 +/- 0.3 mmol/L; Kcat 50.6 +/- 4.5 /s; Kcat/Km 194.6.

row_label: UtDapDH / NADPH / Amination / THDPA


assay_conditions_summary: pH 10; 303.15 K; cofactor NADP+

column_label: Table 1. The kinetic parameter (±SD) of different DapDH for different substrate with NADPH or NADP+ as cofactora.; row UtDapDH / NADP+ / Deamination / meso-DAP; columns Km (mmol/L), Kcat (/s), Kcat/Km; cells Km 1.9 +/- 0.2, Kcat 123.3 +/- 9.4, Kcat/Km 64.9.

normalized_value_unit_evidence: Km normalized_value=1.9 normalized_unit=mM; kcat normalized_value=123.3 normalized_unit=s^-1; kcat/Km normalized_value=64.9 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row UtDapDH / NADP+ / Deamination / meso-DAP: Km 1.9 +/- 0.2 mmol/L; Kcat 123.3 +/- 9.4 /s; Kcat/Km 64.9.


table_label: Table 1. The kinetic parameter (±SD) of different DapDH for different substrate with NADPH or NADP+ as cofactora.


organism: Thermoactinomyces intermedius

substrate_name: L-Isoleucine

column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row L-Isoleucine / CS2, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row L-Isoleucine, enzyme CS2: Km 10 mM; kcat 0.28 s^-1; kcat/Km 0.028 mM^-1 s^-1.

row_label: L-Isoleucine / CS2

substrate: L-Isoleucine


column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row L-Isoleucine / PheDH, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row L-Isoleucine, enzyme PheDH: Km 0.09 mM; kcat 0.24 s^-1; kcat/Km 2.6 mM^-1 s^-1.

row_label: L-Isoleucine / PheDH


substrate_name: L-Leucine

column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row L-Leucine / CS2, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row L-Leucine, enzyme CS2: Km 4.7 mM; kcat 0.21 s^-1; kcat/Km 0.045 mM^-1 s^-1.

row_label: L-Leucine / CS2

substrate: L-Leucine


column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row L-Leucine / PheDH, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row L-Leucine, enzyme PheDH: Km 0.09 mM; kcat 3.6 s^-1; kcat/Km 40 mM^-1 s^-1.

normalized_value_unit_evidence: km 0.09 mM; kcat 3.6 s^-1; kcat_over_km 40 mM^-1 s^-1

row_label: L-Leucine / PheDH


substrate_name: L-Methionine

column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row L-Methionine / CS2, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row L-Methionine, enzyme CS2: Km 7.5 mM; kcat 0.16 s^-1; kcat/Km 0.021 mM^-1 s^-1.

row_label: L-Methionine / CS2

substrate: L-Methionine


column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row L-Methionine / PheDH, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row L-Methionine, enzyme PheDH: Km 0.34 mM; kcat 0.84 s^-1; kcat/Km 2.5 mM^-1 s^-1.

row_label: L-Methionine / PheDH


substrate_name: L-Norleucine

column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row L-Norleucine / CS2, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row L-Norleucine, enzyme CS2: Km 2.1 mM; kcat 0.17 s^-1; kcat/Km 0.081 mM^-1 s^-1.

row_label: L-Norleucine / CS2

substrate: L-Norleucine


column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row L-Norleucine / PheDH, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row L-Norleucine, enzyme PheDH: Km 0.22 mM; kcat 1.9 s^-1; kcat/Km 8.6 mM^-1 s^-1.

row_label: L-Norleucine / PheDH


substrate_name: L-Norvaline

column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row L-Norvaline / CS2, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row L-Norvaline, enzyme CS2: Km 10 mM; kcat 0.15 s^-1; kcat/Km 0.015 mM^-1 s^-1.

row_label: L-Norvaline / CS2

substrate: L-Norvaline


column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row L-Norvaline / PheDH, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row L-Norvaline, enzyme PheDH: Km 0.53 mM; kcat 0.59 s^-1; kcat/Km 1.1 mM^-1 s^-1.

row_label: L-Norvaline / PheDH


substrate_name: L-tyrosine

assay_conditions_summary: pH 10.4; cofactor NAD+

column_label: Table 2; substrate row L-tyrosine; enzyme row wt; metric columns Km, kcat, kcat/Km

normalized_value_unit_evidence: normalized: Km=1.3 mM; kcat=68 s^-1; kcat/Km=52 s^-1 mM^-1

row_label: Lysinibacillus sphaericus / wt / L-tyrosine


column_label: Table 2; row L-tyrosine / WT; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1); PDF page 4/8, article page 11393.

normalized_value_unit_evidence: Paper normalized required metrics: Km=1.3 mM. Exported required metrics: Km=0.48 mM.

raw_value_unit_evidence: Table 2 cells: Km=1.3 mM; kcat=68 s^-1; kcat/Km=52 s^-1 mM^-1.

row_label: L-tyrosine / WT


substrate_name: L-phenylalanine

assay_conditions_summary: pH 10.4; 298.15 K; buffer pH 10; cofactor NAD+

column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates (Biochemistry 2002, 41(38):11390-11397); printed column heads substrate | enzyme | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 2, substrate block 'L-phenylalanine', enzyme row 'wt'; column Km (mM) = 1.1; column kcat (s-1) = 68; column kcat/Km (s-1 mM-1) = 62. captured primary segment: L-phenylalanine | wt | Km 1.1 mM | kcat 68 s^-1 | kcat/Km 62 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 1.1 mM; the printed column is already in mM, so no unit conversion applies and the value is 1.1 mM. kcat: printed Table 2 kcat cell 68 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 68.0 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 62 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 62.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 68.0 / 1.1 = 61.81818181818181 s^-1 mM^-1, against the printed efficiency cell 62.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate block 'L-phenylalanine', enzyme row 'wt': Km = 1.1 mM; kcat = 68 s^-1; kcat/Km = 62 s^-1 mM^-1.

substrate: L-phenylalanine


substrate_name: phenylpyruvate

assay_conditions_summary: pH 10.4; buffer pH 10; cofactor NAD+

column_label: Table 2; row phenylpyruvate / WT; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1); PDF page 4/8, article page 11393.

normalized_value_unit_evidence: Paper normalized required metrics: kcat=113.0 s^-1; Km=0.37 mM; kcat/Km=305.0 s^-1 mM^-1. Exported required metrics: kcat=113.0 s^-1; Km=0.37 mM; kcat/Km=305.4054054054054 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 cells: Km=0.37 mM; kcat=113 s^-1; kcat/Km=305 s^-1 mM^-1.

row_label: phenylpyruvate / WT

substrate: phenylpyruvate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N145A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.6; 298.15 K; buffer pH 10; cofactor NAD+

column_label: Table 5; row alpha-ketocaproate / N145A; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1); PDF page 5/8, article page 11394.

normalized_value_unit_evidence: Paper normalized required metrics: kcat=66.0 s^-1; Km=0.25 mM; kcat/Km=264.0 s^-1 mM^-1. Exported required metrics: kcat=66.0 s^-1; Km=0.25 mM; kcat/Km=264.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 5 cells: Km=0.25 mM; kcat=66 s^-1; kcat/Km=264 s^-1 mM^-1.

row_label: alpha-ketocaproate / N145A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N145I with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

column_label: Table 5; row alpha-ketocaproate / N145I; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1); PDF page 5/8, article page 11394.

normalized_value_unit_evidence: Paper normalized required metrics: kcat=61.0 s^-1; Km=0.25 mM; kcat/Km=244.0 s^-1 mM^-1. Exported required metrics: kcat=61.0 s^-1; Km=0.25 mM; kcat/Km=244.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 5 cells: Km=0.25 mM; kcat=61 s^-1; kcat/Km=244 s^-1 mM^-1.

row_label: alpha-ketocaproate / N145I


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N145L with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.6; 298.15 K; cofactor NAD+

column_label: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs, row R-ketocaproate / N145L, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.22, 42, and 191.

raw_value_unit_evidence: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs row R-ketocaproate / N145L: Km = 0.22 mM; kcat = 42 s^-1; kcat/Km = 191 s^-1 mM^-1.

row_label: R-ketocaproate / N145L


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N145V with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

column_label: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs, row R-ketocaproate / N145V, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.15, 40, and 267.

raw_value_unit_evidence: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs row R-ketocaproate / N145V: Km = 0.15 mM; kcat = 40 s^-1; kcat/Km = 267 s^-1 mM^-1.

row_label: R-ketocaproate / N145V


column_label: Table 5; substrate row 2-Oxohexanoate; enzyme row wt; metric columns Km, kcat, kcat/Km

normalized_value_unit_evidence: normalized: Km=13 mM; kcat=51 s^-1; kcat/Km=3.9 s^-1 mM^-1

row_label: Lysinibacillus sphaericus / wt / 2-Oxohexanoate


column_label: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs, row R-ketovalerate / N145A, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 1.4, 54, and 39.

raw_value_unit_evidence: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs row R-ketovalerate / N145A: Km = 1.4 mM; kcat = 54 s^-1; kcat/Km = 39 s^-1 mM^-1.

row_label: R-ketovalerate / N145A


column_label: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs, row R-ketovalerate / N145I, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 2.6, 61, and 23.

raw_value_unit_evidence: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs row R-ketovalerate / N145I: Km = 2.6 mM; kcat = 61 s^-1; kcat/Km = 23 s^-1 mM^-1.

row_label: R-ketovalerate / N145I


organism: Pseudothermotoga thermarum

substrate_name: NADPH

assay_conditions_summary: pH 8.2; cofactor NADH

substrate: NADPH


substrate_name: NADH


assay_conditions_summary: pH 8.2; 310.15 K; cofactor NADH


organism: Sporosarcina ureae


column_label: Table VI, phenylpyruvate row, S. ureae SCRC-R04 column, Km 0.16 mM; Table V reports the same cell.

normalized_value_unit_evidence: Km=0.16 mM for phenylpyruvate.

raw_value_unit_evidence: Tables V and VI phenylpyruvate row: S. ureae Km 0.16 mM.

row_label: Phenylpyruvate

table_label: Tables V and VI


smiles: CCCCC(=O)C(=O)[O-]

column_label: Table V, alpha-ketocaproate row, S. ureae Km column, 2.44 mM.

normalized_value_unit_evidence: Km=2.44 mM for 2-oxohexanoate.

raw_value_unit_evidence: Table V alpha-ketocaproate row: Km 2.44 mM.

row_label: alpha-Ketocaproate (2-oxohexanoate)

table_label: Table V. Substrate specificity of S. ureae phenylalanine dehydrogenase


enzyme_display_name: lysine 6-dehydrogenase

organism: Geobacillus stearothermophilus

substrate_name: NAD+

assay_conditions_summary: pH 10; cofactor NAD+

column_label: Prose metric statement maps respectively: L-lysine 0.73 mM; NAD 0.088 mM; NADP 0.48 mM. Row uses NAD value 0.088 mM.

normalized_value_unit_evidence: Km for NAD = 0.088 mM.

raw_value_unit_evidence: Abstract/results prose states: The Km values for L-lysine, NAD, and NADP at 50 C and pH 10.0 were 0.73, 0.088, and 0.48 mM, respectively.

row_label: NAD Km statement

table_label: Abstract/results prose kinetic parameter statement

enzyme: lysine 6-dehydrogenase

substrate: NAD+


substrate_name: NADP+

assay_conditions_summary: pH 10; cofactor NADP+

column_label: Prose metric statement maps respectively: L-lysine 0.73 mM; NAD 0.088 mM; NADP 0.48 mM. Row uses NADP value 0.48 mM.

normalized_value_unit_evidence: Km for NADP = 0.48 mM.

row_label: NADP Km statement

substrate: NADP+


substrate_name: L-lysine

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

assay_conditions_summary: pH 10

column_label: Prose metric statement maps respectively: L-lysine 0.73 mM; NAD 0.088 mM; NADP 0.48 mM. Row uses L-lysine value 0.73 mM.

normalized_value_unit_evidence: Km for L-lysine = 0.73 mM.

row_label: L-lysine Km statement

substrate: L-lysine


enzyme_display_name: Lysine 6-dehydrogenase

substrate_name: NADP(+)

enzyme: Lysine 6-dehydrogenase

substrate: NADP(+)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G124A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.6; 298.15 K; cofactor NADH

column_label: Table 2; row=a-Keto-gamma-methiobutyrate; mutant column=G124A; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 2.4 mM; kcat 38.0 s^-1; kcat/Km 15.833333333333334 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 2 row a-Keto-gamma-methiobutyrate, mutant column G124A: Km 2.4 mM; kcat 38.0 s^-1; kcat/Km 16.0 s^-1 mM^-1.

row_label: a-Keto-gamma-methiobutyrate


sequence_variant_note: Resolved canonical sequence from uniprotkb:P23307 and applied mutation signature G124A/L307V to reconstruct the assayed variant sequence.

column_label: Table 2; row=a-Keto-gamma-methiobutyrate; mutant column=G124A/L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 1.1 mM; kcat 52.0 s^-1; kcat/Km 47.272727272727266 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 2 row a-Keto-gamma-methiobutyrate, mutant column G124A/L307V: Km 1.1 mM; kcat 52.0 s^-1; kcat/Km 47.0 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L307V to reconstruct the assayed variant sequence.

column_label: Table 2; row=a-Keto-gamma-methiobutyrate; mutant column=L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 1.5 mM; kcat 34.0 s^-1; kcat/Km 22.666666666666668 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 2 row a-Keto-gamma-methiobutyrate, mutant column L307V: Km 1.5 mM; kcat 34.0 s^-1; kcat/Km 23.0 s^-1 mM^-1.


substrate_name: alpha-Ketovaline

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

column_label: Table 2; row=a-Ketoisovalerate; mutant column=G124A; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 3.0 mM; kcat 51.0 s^-1; kcat/Km 17.0 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 2 row a-Ketoisovalerate, mutant column G124A: Km 3.0 mM; kcat 51.0 s^-1; kcat/Km 17.0 s^-1 mM^-1.

row_label: a-Ketoisovalerate

substrate: alpha-Ketovaline


column_label: Table 2; row=a-Ketoisovalerate; mutant column=G124A/L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 2.0 mM; kcat 53.0 s^-1; kcat/Km 26.5 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 2 row a-Ketoisovalerate, mutant column G124A/L307V: Km 2.0 mM; kcat 53.0 s^-1; kcat/Km 27.0 s^-1 mM^-1.


column_label: Table 2; row=a-Ketoisovalerate; mutant column=L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 14.0 mM; kcat 25.0 s^-1; kcat/Km 1.7857142857142858 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 2 row a-Ketoisovalerate, mutant column L307V: Km 14.0 mM; kcat 25.0 s^-1; kcat/Km 1.8 s^-1 mM^-1.


assay_conditions_summary: pH 10.4; 298.15 K; cofactor NAD+

column_label: Table 1; row=L-Isoleucine; mutant column=G124A; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 0.11 mM; kcat 1.1 s^-1; kcat/Km 10.0 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 1 row L-Isoleucine, mutant column G124A: Km 0.11 mM; kcat 1.1 s^-1; kcat/Km 10.0 s^-1 mM^-1.

row_label: L-Isoleucine


column_label: Table 1; row=L-Isoleucine; mutant column=G124A/L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 0.11 mM; kcat 2.3 s^-1; kcat/Km 20.909090909090907 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 1 row L-Isoleucine, mutant column G124A/L307V: Km 0.11 mM; kcat 2.3 s^-1; kcat/Km 21.0 s^-1 mM^-1.


column_label: Table 1; row=L-Isoleucine; mutant column=L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 0.19 mM; kcat 0.27 s^-1; kcat/Km 1.4210526315789473 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 1 row L-Isoleucine, mutant column L307V: Km 0.19 mM; kcat 0.27 s^-1; kcat/Km 1.4 s^-1 mM^-1.


column_label: Table 1; row=L-Leucine; mutant column=G124A; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 0.057 mM; kcat 1.0 s^-1; kcat/Km 17.543859649122805 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 1 row L-Leucine, mutant column G124A: Km 0.057 mM; kcat 1.0 s^-1; kcat/Km 18.0 s^-1 mM^-1.

row_label: L-Leucine


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

column_label: Table 2; row None (wild type); non-parenthetical L-tryptophan cells Km=0.045 mM, kcat=20 s^-1, kcat/Km=440 s^-1*mM^-1.

raw_value_unit_evidence: Table 2 row None (wild type); Km=0.045 mM; kcat=20 s^-1; kcat/Km=440 mM^-1*s^-1.

row_label: None (wild type) / L-tryptophan

table_label: Table 2. Kinetic constants of NpTrpDH mutants


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature Y292F to reconstruct the assayed variant sequence.

column_label: Table 2 | Y292F NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.039 +/- 0.0030 mM | kcat 21 +/- 1.5 s^-1 | kcat/Km 540 mM^-1 s^-1

normalized_value_unit_evidence: kcat=21 s^(-1); km=0.039 mM; kcat_over_km=540 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row Y292F, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature Y292H to reconstruct the assayed variant sequence.

column_label: Table 2 | Y292H NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.021 +/- 0.0030 mM | kcat 3.5 +/- 0.41 s^-1 | kcat/Km 170 mM^-1 s^-1

normalized_value_unit_evidence: kcat=3.5 s^(-1); km=0.021 mM; kcat_over_km=170 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row Y292H, non-parenthetical L-tryptophan cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:W8CV45 and applied mutation signature Y292W to reconstruct the assayed variant sequence.

column_label: Table 2 | Y292W NpTrpDH | substrate L-tryptophan, non-parenthetical cells | condition 200 mM Gly-KOH pH 11.0, varied L-Trp, 1.25 mM NAD+, 25-100 nM NpTrpDH, 25 C, three independent experiments, Michaelis-Menten fit | Km 0.030 +/- 0.0050 mM | kcat 8.5 +/- 0.58 s^-1 | kcat/Km 280 mM^-1 s^-1

normalized_value_unit_evidence: kcat=8.5 s^(-1); km=0.03 mM; kcat_over_km=280 s^(-1)*mM^(-1). Each central value is copied from a separate printed Table 2 cell; no scale conversion is needed.

row_label: Table 2, row Y292W, non-parenthetical L-tryptophan cells


assay_conditions_summary: pH 8; cofactor NADPH

column_label: Table IV reports Km(B) (microM) under column (B) Pip2C as 15; 15 microM = 0.015 mM.

raw_value_unit_evidence: Km raw_value=15 raw_unit=microM

row_label: Km(B)

table_label: Table IV - Kinetic parameters of DpkA in the forward direction


substrate_name: L-proline

column_label: Table V reports Km(P) (microM) under column (P) L-Proline as 144,000; 144,000 microM = 144.0 mM.

raw_value_unit_evidence: Km raw_value=144,000 raw_unit=microM

row_label: Km(P)

table_label: Table V - Kinetic parameters of DpkA in the reverse direction

substrate: L-proline


substrate_name: L-pipecolate

column_label: Table V reports Km(P) (microM) under column (P) L-Pipecolate as 32,400; 32,400 microM = 32.4 mM.

raw_value_unit_evidence: Km raw_value=32,400 raw_unit=microM

substrate: L-pipecolate


substrate_name: NADPH (with Pyr2C as cosubstrate)

assay_conditions_summary: cofactor NADPH

column_label: Table IV reports Km(NADPH) (microM) under column (B) Pyr2C as 34; 34 microM = 0.034 mM.

raw_value_unit_evidence: Km raw_value=34 raw_unit=microM

row_label: Km(NADPH)

substrate: NADPH (with Pyr2C as cosubstrate)


substrate_name: NADP(+) (with L-proline as cosubstrate)

assay_conditions_summary: cofactor NADP+

substrate: NADP(+) (with L-proline as cosubstrate)


organism: Acetivibrio thermocellus

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADPH

column_label: Table 1. The kinetic parameter (±SD) of different DapDH for different substrate with NADPH or NADP+ as cofactora.; row CtDapDH / NADPH / Amination / THDPA; columns Km (mmol/L), Kcat (/s), Kcat/Km; cells Km 0.11 +/- 0.03, Kcat 278.2 +/- 25.3, Kcat/Km 2318.3.

normalized_value_unit_evidence: Km normalized_value=0.11 normalized_unit=mM; kcat normalized_value=278.2 normalized_unit=s^-1; kcat/Km normalized_value=2318.3 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row CtDapDH / NADPH / Amination / THDPA: Km 0.11 +/- 0.03 mmol/L; Kcat 278.2 +/- 25.3 /s; Kcat/Km 2318.3.

row_label: CtDapDH / NADPH / Amination / THDPA


assay_conditions_summary: pH 10; 303.15 K; cofactor NADP+

column_label: Table 1. The kinetic parameter (±SD) of different DapDH for different substrate with NADPH or NADP+ as cofactora.; row CtDapDH / NADP+ / Deamination / meso-DAP; columns Km (mmol/L), Kcat (/s), Kcat/Km; cells Km 0.21 +/- 0.05, Kcat 344.3 +/- 31.4, Kcat/Km 1638.6.

normalized_value_unit_evidence: Km normalized_value=0.21 normalized_unit=mM; kcat normalized_value=344.3 normalized_unit=s^-1; kcat/Km normalized_value=1638.6 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row CtDapDH / NADP+ / Deamination / meso-DAP: Km 0.21 +/- 0.05 mmol/L; Kcat 344.3 +/- 31.4 /s; Kcat/Km 1638.6.


column_label: Table 1. The kinetic parameter (±SD) of different DapDH for different substrate with NADPH or NADP+ as cofactora.; row CtDapDH / NADPH / Amination / NH4+; columns Km (mmol/L), Kcat (/s), Kcat/Km; cells Km 8.5 +/- 14.2, Kcat 1815.6 +/- 125.3, Kcat/Km 205.4.

normalized_value_unit_evidence: Km normalized_value=8.5 normalized_unit=mM; kcat normalized_value=1815.6 normalized_unit=s^-1; kcat/Km normalized_value=205.4 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row CtDapDH / NADPH / Amination / NH4+: Km 8.5 +/- 14.2 mmol/L; Kcat 1815.6 +/- 125.3 /s; Kcat/Km 205.4.

row_label: CtDapDH / NADPH / Amination / NH4+


substrate_name: L-2-amino-6-oxoheptanedioate (at 30 degrees Celsius and pH 10.5)


substrate_name: NADPH (at 30 degrees Celsius and pH 10.5)

assay_conditions_summary: pH 10.5; cofactor NADPH


substrate_name: ammonia (at 30 degrees Celsius and pH 10.5)


substrate_name: L-Phenylalanine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F124M/V125D/H126I/A127I/A128Y/R129Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 10.8; 295.15 K; cofactor NAD+

column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row L-Phenylalanine / CS2, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row L-Phenylalanine, enzyme CS2: Km 23 mM; kcat 0.75 s^-1; kcat/Km 0.033 mM^-1 s^-1.

row_label: L-Phenylalanine / CS2

substrate: L-Phenylalanine


column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row L-Phenylalanine / PheDH, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row L-Phenylalanine, enzyme PheDH: Km 0.11 mM; kcat 45 s^-1; kcat/Km 410 mM^-1 s^-1.

normalized_value_unit_evidence: km 0.11 mM; kcat 45 s^-1; kcat_over_km 410 mM^-1 s^-1

row_label: L-Phenylalanine / PheDH


assay_conditions_summary: pH 9.5; 295.15 K; cofactor NAD+

column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row phenylpyruvate / CS2, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row phenylpyruvate, enzyme CS2: Km 23 mM; kcat 12 s^-1; kcat/Km 0.52 mM^-1 s^-1.

normalized_value_unit_evidence: km 23 mM; kcat 12 s^-1; kcat_over_km 0.52 mM^-1 s^-1

row_label: phenylpyruvate / CS2


column_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase, row phenylpyruvate / PheDH, columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1): Table III row phenylpyruvate, enzyme PheDH: Km 0.06 mM; kcat 91 s^-1; kcat/Km 1500 mM^-1 s^-1.

row_label: phenylpyruvate / PheDH


assay_conditions_summary: cofactor NADH

substrate: NADH


assay_conditions_summary: pH 8.6; 298.15 K; cofactor NAD+

column_label: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs, row R-ketovalerate / N145L, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 2.9, 40, and 14.

raw_value_unit_evidence: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs row R-ketovalerate / N145L: Km = 2.9 mM; kcat = 40 s^-1; kcat/Km = 14 s^-1 mM^-1.

row_label: R-ketovalerate / N145L


column_label: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs, row R-ketovalerate / N145V, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 2.2, 40, and 18.

raw_value_unit_evidence: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs row R-ketovalerate / N145V: Km = 2.2 mM; kcat = 40 s^-1; kcat/Km = 18 s^-1 mM^-1.

row_label: R-ketovalerate / N145V


column_label: Table 5; substrate row 2-Oxopentanoate; enzyme row wt; metric columns Km, kcat, kcat/Km

normalized_value_unit_evidence: normalized: Km=52 mM; kcat=33 s^-1; kcat/Km=0.63 s^-1 mM^-1

row_label: Lysinibacillus sphaericus / wt / 2-Oxopentanoate


column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates, row p-hydroxyphenylpyruvate / N145A, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.099, 14, and 141.

raw_value_unit_evidence: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates row p-hydroxyphenylpyruvate / N145A: Km = 0.099 mM; kcat = 14 s^-1; kcat/Km = 141 s^-1 mM^-1.

row_label: p-hydroxyphenylpyruvate / N145A


column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates, row p-hydroxyphenylpyruvate / N145I, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.55, 80, and 145.

raw_value_unit_evidence: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates row p-hydroxyphenylpyruvate / N145I: Km = 0.55 mM; kcat = 80 s^-1; kcat/Km = 145 s^-1 mM^-1.

row_label: p-hydroxyphenylpyruvate / N145I


column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates, row p-hydroxyphenylpyruvate / N145L, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.22, 30, and 136.

raw_value_unit_evidence: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates row p-hydroxyphenylpyruvate / N145L: Km = 0.22 mM; kcat = 30 s^-1; kcat/Km = 136 s^-1 mM^-1.

row_label: p-hydroxyphenylpyruvate / N145L


column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates, row p-hydroxyphenylpyruvate / N145V, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.61, 88, and 144.

raw_value_unit_evidence: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates row p-hydroxyphenylpyruvate / N145V: Km = 0.61 mM; kcat = 88 s^-1; kcat/Km = 144 s^-1 mM^-1.

row_label: p-hydroxyphenylpyruvate / N145V


column_label: Table 2; substrate row 3-(4-Hydroxyphenyl)pyruvate; enzyme row wt; metric columns Km, kcat, kcat/Km

normalized_value_unit_evidence: normalized: Km=0.19 mM; kcat=90 s^-1; kcat/Km=474 s^-1 mM^-1

row_label: Lysinibacillus sphaericus / wt / 3-(4-Hydroxyphenyl)pyruvate

table_label: Table 2


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23307 and applied mutation signature N145A to reconstruct the assayed variant sequence.

column_label: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs (Biochemistry 2002, 41(38):11390-11397); printed column heads substrates | enzyme | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 5, substrate block 'DL-R-keto-β-methyl-n-valerate', enzyme row 'N145A'; column Km (mM) = 0.74; column kcat (s-1) = 19; column kcat/Km (s-1 mM-1) = 26. captured primary segment: DL-alpha-keto-beta-methyl-n-valerate | N145A | Km 0.74 mM | kcat 19 s^-1 | kcat/Km 26 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 5 Km cell 0.74 mM; the printed column is already in mM, so no unit conversion applies and the value is 0.74 mM. kcat: printed Table 5 kcat cell 19 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 19.0 s^(-1). kcat/Km: printed Table 5 kcat/Km cell 26 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 26.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 19.0 / 0.74 = 25.675675675675677 s^-1 mM^-1, against the printed efficiency cell 26.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 5, substrate block 'DL-R-keto-β-methyl-n-valerate', enzyme row 'N145A': Km = 0.74 mM; kcat = 19 s^-1; kcat/Km = 26 s^-1 mM^-1.


organism: Ureibacillus thermosphaericus

substrate_name: NADP(+) (at 50 degrees Celsius and pH 10.5)


organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)

substrate_name: L-Phe

substrate: L-Phe


substrate_name: L-Tyr

proof_lines:
Rhodococcus sp. M4
L-phenylalanine dehydrogenase
L-phenylalanine

substrate: L-Tyr


substrate_name: L-tryptophan

proof_lines:
L-tryptophan dehydrogenase
stability
specific activity

substrate: L-tryptophan


substrate_name: L-Leucine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G124A/L307V to reconstruct the assayed variant sequence.

column_label: Table 1; row=L-Leucine; mutant column=G124A/L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 0.046 mM; kcat 1.1 s^-1; kcat/Km 23.91304347826087 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 1 row L-Leucine, mutant column G124A/L307V: Km 0.046 mM; kcat 1.1 s^-1; kcat/Km 24.0 s^-1 mM^-1.

row_label: L-Leucine

table_label: Table 1

substrate: L-Leucine


substrate_name: L-Methionine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23307 and applied mutation signature G124A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 10.4; 298.15 K; buffer 1 mL containing 50 lmol glycine/KOH; cofactor NAD+

column_label: Table 1: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various amino acid substrates (Eur. J. Biochem. 270, 4628-4634 (2003)). Column 1 is the substrate; the four genotype blocks run across the page in the printed order Wild type, L307V, G124A, G124A/L307V, each carrying the three column heads 'Km +/- SEM (mM)', 'kcat +/- SEM (s^-1)' and 'kcat/Km (s^-1 mM^-1)'. Substrate line 'L-Methionine', 'G124A' genotype block: Km = 0.73 ± 0.042; kcat = 1.4 ± 0.027; kcat/Km = 1.9.

normalized_value_unit_evidence: Km: printed cell 0.73 ± 0.042 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 0.73 mM. kcat: printed cell 1.4 ± 0.027 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 1.4 s^(-1). kcat/Km: Printed Table 1 kcat/Km cell 1.9 in the column head 'kcat/Km (s^-1 mM^-1)'; that unit is already the canonical catalog unit s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 1.9 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 1.4 / 0.73 = 1.917808219178082 s^-1 mM^-1, and the paper's own efficiency cell is printed as 1.9 at the two-figure precision this table uses.

raw_value_unit_evidence: Table 1: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various amino acid substrates (Eur. J. Biochem. 270, 4628-4634 (2003)), substrate line 'L-Methionine', 'G124A' genotype block: column 'Km +/- SEM (mM)' prints 0.73 ± 0.042; column 'kcat +/- SEM (s^-1)' prints 1.4 ± 0.027; column 'kcat/Km (s^-1 mM^-1)' prints 1.9.

row_label: Table 1, substrate line 'L-Methionine', 'G124A' genotype block

substrate: L-Methionine


column_label: Table 1; row=L-Methionine; mutant column=G124A/L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 0.16 mM; kcat 1.0 s^-1; kcat/Km 6.25 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 1 row L-Methionine, mutant column G124A/L307V: Km 0.16 mM; kcat 1.0 s^-1; kcat/Km 6.3 s^-1 mM^-1.

row_label: L-Methionine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23307 and applied mutation signature L307V to reconstruct the assayed variant sequence.

column_label: Table 1: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various amino acid substrates (Eur. J. Biochem. 270, 4628-4634 (2003)). Column 1 is the substrate; the four genotype blocks run across the page in the printed order Wild type, L307V, G124A, G124A/L307V, each carrying the three column heads 'Km +/- SEM (mM)', 'kcat +/- SEM (s^-1)' and 'kcat/Km (s^-1 mM^-1)'. Substrate line 'L-Methionine', 'L307V' genotype block: Km = 0.29 ± 0.018; kcat = 1.2 ± 0.023; kcat/Km = 4.1.

normalized_value_unit_evidence: Km: printed cell 0.29 ± 0.018 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 0.29 mM. kcat: printed cell 1.2 ± 0.023 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 1.2 s^(-1). kcat/Km: Printed Table 1 kcat/Km cell 4.1 in the column head 'kcat/Km (s^-1 mM^-1)'; that unit is already the canonical catalog unit s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 4.1 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 1.2 / 0.29 = 4.137931034482759 s^-1 mM^-1, and the paper's own efficiency cell is printed as 4.1 at the two-figure precision this table uses.

raw_value_unit_evidence: Table 1: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various amino acid substrates (Eur. J. Biochem. 270, 4628-4634 (2003)), substrate line 'L-Methionine', 'L307V' genotype block: column 'Km +/- SEM (mM)' prints 0.29 ± 0.018; column 'kcat +/- SEM (s^-1)' prints 1.2 ± 0.023; column 'kcat/Km (s^-1 mM^-1)' prints 4.1.

row_label: Table 1, substrate line 'L-Methionine', 'L307V' genotype block


substrate_name: L-Norleucine

column_label: Table 1: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various amino acid substrates (Eur. J. Biochem. 270, 4628-4634 (2003)). Column 1 is the substrate; the four genotype blocks run across the page in the printed order Wild type, L307V, G124A, G124A/L307V, each carrying the three column heads 'Km +/- SEM (mM)', 'kcat +/- SEM (s^-1)' and 'kcat/Km (s^-1 mM^-1)'. Substrate line 'L-Norleucine', 'G124A' genotype block: Km = 0.096 ± 0.010; kcat = 1.6 ± 0.063; kcat/Km = 17.

normalized_value_unit_evidence: Km: printed cell 0.096 ± 0.010 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 0.096 mM. kcat: printed cell 1.6 ± 0.063 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 1.6 s^(-1). kcat/Km: Printed Table 1 kcat/Km cell 17 in the column head 'kcat/Km (s^-1 mM^-1)'; that unit is already the canonical catalog unit s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 17.0 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 1.6 / 0.096 = 16.666666666666668 s^-1 mM^-1, and the paper's own efficiency cell is printed as 17 at the two-figure precision this table uses.

raw_value_unit_evidence: Table 1: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various amino acid substrates (Eur. J. Biochem. 270, 4628-4634 (2003)), substrate line 'L-Norleucine', 'G124A' genotype block: column 'Km +/- SEM (mM)' prints 0.096 ± 0.010; column 'kcat +/- SEM (s^-1)' prints 1.6 ± 0.063; column 'kcat/Km (s^-1 mM^-1)' prints 17.

row_label: Table 1, substrate line 'L-Norleucine', 'G124A' genotype block

substrate: L-Norleucine


column_label: Table 1; row=L-Norleucine; mutant column=G124A/L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 0.088 mM; kcat 2.2 s^-1; kcat/Km 25.000000000000004 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 1 row L-Norleucine, mutant column G124A/L307V: Km 0.088 mM; kcat 2.2 s^-1; kcat/Km 25.0 s^-1 mM^-1.

row_label: L-Norleucine


column_label: Table 1: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various amino acid substrates (Eur. J. Biochem. 270, 4628-4634 (2003)). Column 1 is the substrate; the four genotype blocks run across the page in the printed order Wild type, L307V, G124A, G124A/L307V, each carrying the three column heads 'Km +/- SEM (mM)', 'kcat +/- SEM (s^-1)' and 'kcat/Km (s^-1 mM^-1)'. Substrate line 'L-Norleucine', 'L307V' genotype block: Km = 0.077 ± 0.0052; kcat = 1.3 ± 0.029; kcat/Km = 17.

normalized_value_unit_evidence: Km: printed cell 0.077 ± 0.0052 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 0.077 mM. kcat: printed cell 1.3 ± 0.029 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 1.3 s^(-1). kcat/Km: Printed Table 1 kcat/Km cell 17 in the column head 'kcat/Km (s^-1 mM^-1)'; that unit is already the canonical catalog unit s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 17.0 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 1.3 / 0.077 = 16.883116883116884 s^-1 mM^-1, and the paper's own efficiency cell is printed as 17 at the two-figure precision this table uses.

raw_value_unit_evidence: Table 1: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various amino acid substrates (Eur. J. Biochem. 270, 4628-4634 (2003)), substrate line 'L-Norleucine', 'L307V' genotype block: column 'Km +/- SEM (mM)' prints 0.077 ± 0.0052; column 'kcat +/- SEM (s^-1)' prints 1.3 ± 0.029; column 'kcat/Km (s^-1 mM^-1)' prints 17.

row_label: Table 1, substrate line 'L-Norleucine', 'L307V' genotype block


substrate_name: L-Norvaline

column_label: Table 1: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various amino acid substrates (Eur. J. Biochem. 270, 4628-4634 (2003)). Column 1 is the substrate; the four genotype blocks run across the page in the printed order Wild type, L307V, G124A, G124A/L307V, each carrying the three column heads 'Km +/- SEM (mM)', 'kcat +/- SEM (s^-1)' and 'kcat/Km (s^-1 mM^-1)'. Substrate line 'L-Norvaline', 'G124A' genotype block: Km = 0.19 ± 0.017; kcat = 1.5 ± 0.041; kcat/Km = 7.9.

normalized_value_unit_evidence: Km: printed cell 0.19 ± 0.017 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 0.19 mM. kcat: printed cell 1.5 ± 0.041 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 1.5 s^(-1). kcat/Km: Printed Table 1 kcat/Km cell 7.9 in the column head 'kcat/Km (s^-1 mM^-1)'; that unit is already the canonical catalog unit s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 7.9 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 1.5 / 0.19 = 7.894736842105263 s^-1 mM^-1, and the paper's own efficiency cell is printed as 7.9 at the two-figure precision this table uses.

raw_value_unit_evidence: Table 1: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various amino acid substrates (Eur. J. Biochem. 270, 4628-4634 (2003)), substrate line 'L-Norvaline', 'G124A' genotype block: column 'Km +/- SEM (mM)' prints 0.19 ± 0.017; column 'kcat +/- SEM (s^-1)' prints 1.5 ± 0.041; column 'kcat/Km (s^-1 mM^-1)' prints 7.9.

row_label: Table 1, substrate line 'L-Norvaline', 'G124A' genotype block

substrate: L-Norvaline


column_label: Table 1; row=L-Norvaline; mutant column=G124A/L307V; metric columns=Km +/- SEM (mM), kcat +/- SEM (s^-1), kcat/Km (s^-1 mM^-1).

normalized_value_unit_evidence: Expected row normalized values: Km 0.081 mM; kcat 1.4 s^-1; kcat/Km 17.28395061728395 s^-1 mM^-1. Paper kcat/Km is rounded in table; ratio recomputes from table kcat/Km cells where needed.

raw_value_unit_evidence: Table 1 row L-Norvaline, mutant column G124A/L307V: Km 0.081 mM; kcat 1.4 s^-1; kcat/Km 17.0 s^-1 mM^-1.

row_label: L-Norvaline


organism: Bacteroides fragilis

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADP+

column_label: Table 1. The kinetic parameter (±SD) of different DapDH for different substrate with NADPH or NADP+ as cofactora.; row BfDapDH / NADPH / Amination / THDPA; columns Km (mmol/L), Kcat (/s), Kcat/Km; cells Km 0.57 +/- 0.14, Kcat 4.9 +/- 0.3, Kcat/Km 8.6.

normalized_value_unit_evidence: Km normalized_value=0.57 normalized_unit=mM; kcat normalized_value=4.9 normalized_unit=s^-1; kcat/Km normalized_value=8.6 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row BfDapDH / NADPH / Amination / THDPA: Km 0.57 +/- 0.14 mmol/L; Kcat 4.9 +/- 0.3 /s; Kcat/Km 8.6.

row_label: BfDapDH / NADPH / Amination / THDPA


column_label: Table 1. The kinetic parameter (±SD) of different DapDH for different substrate with NADPH or NADP+ as cofactora.; row BfDapDH / NADP+ / Deamination / meso-DAP; columns Km (mmol/L), Kcat (/s), Kcat/Km; cells Km 0.11 +/- 0.02, Kcat 7.7 +/- 0.4, Kcat/Km 70.0.

normalized_value_unit_evidence: Km normalized_value=0.11 normalized_unit=mM; kcat normalized_value=7.7 normalized_unit=s^-1; kcat/Km normalized_value=70.0 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row BfDapDH / NADP+ / Deamination / meso-DAP: Km 0.11 +/- 0.02 mmol/L; Kcat 7.7 +/- 0.4 /s; Kcat/Km 70.0.


column_label: Table 1. The kinetic parameter (±SD) of different DapDH for different substrate with NADPH or NADP+ as cofactora.; row BfDapDH / NADPH / Amination / NH4+; columns Km (mmol/L), Kcat (/s), Kcat/Km; cells Km 4.2 +/- 0.5, Kcat 160.8 +/- 21.2, Kcat/Km 38.3.

normalized_value_unit_evidence: Km normalized_value=4.2 normalized_unit=mM; kcat normalized_value=160.8 normalized_unit=s^-1; kcat/Km normalized_value=38.3 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row BfDapDH / NADPH / Amination / NH4+: Km 4.2 +/- 0.5 mmol/L; Kcat 160.8 +/- 21.2 /s; Kcat/Km 38.3.

row_label: BfDapDH / NADPH / Amination / NH4+


organism: Thermotoga maritima

substrate_name: L-Aspartate

substrate: L-Aspartate


substrate_name: NAD+

assay_conditions_summary: pH 8.5; 343.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NADP+

assay_conditions_summary: pH 8.5; 343.15 K; cofactor NADP+

substrate: NADP+


assay_conditions_summary: cofactor NAD+

proof_lines:
phenylalanine dehydrogenase
NAD+
Thermoactinomyces intermedius


column_label: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs, row DL-R-keto-beta-methyl-n-valerate / N145L, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 1.6, 13, and 8.1.

raw_value_unit_evidence: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs row DL-R-keto-beta-methyl-n-valerate / N145L: Km = 1.6 mM; kcat = 13 s^-1; kcat/Km = 8.1 s^-1 mM^-1.


column_label: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs, row DL-R-keto-beta-methyl-n-valerate / N145V, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.76, 9.6, and 13.

raw_value_unit_evidence: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs row DL-R-keto-beta-methyl-n-valerate / N145V: Km = 0.76 mM; kcat = 9.6 s^-1; kcat/Km = 13 s^-1 mM^-1.


assay_conditions_summary: pH 8.6; 298.15 K; cofactor NADH

column_label: Table 5; substrate row 3-Methyl-2-oxopentanoate; enzyme row wt; metric columns Km, kcat, kcat/Km

normalized_value_unit_evidence: normalized: Km=13 mM; kcat=7.2 s^-1; kcat/Km=0.55 s^-1 mM^-1

row_label: Lysinibacillus sphaericus / wt / 3-Methyl-2-oxopentanoate

table_label: Table 5


column_label: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs, row R-ketoisocaproate / N145A, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.22, 24, and 109.

raw_value_unit_evidence: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs row R-ketoisocaproate / N145A: Km = 0.22 mM; kcat = 24 s^-1; kcat/Km = 109 s^-1 mM^-1.

row_label: R-ketoisocaproate / N145A


column_label: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs, row R-ketoisocaproate / N145I, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.21, 28, and 133.

raw_value_unit_evidence: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs row R-ketoisocaproate / N145I: Km = 0.21 mM; kcat = 28 s^-1; kcat/Km = 133 s^-1 mM^-1.

row_label: R-ketoisocaproate / N145I


column_label: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs, row R-ketoisocaproate / N145L, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.22, 15, and 68.

raw_value_unit_evidence: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs row R-ketoisocaproate / N145L: Km = 0.22 mM; kcat = 15 s^-1; kcat/Km = 68 s^-1 mM^-1.

row_label: R-ketoisocaproate / N145L


column_label: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs, row R-ketoisocaproate / N145V, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.21, 18, and 86.

raw_value_unit_evidence: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs row R-ketoisocaproate / N145V: Km = 0.21 mM; kcat = 18 s^-1; kcat/Km = 86 s^-1 mM^-1.

row_label: R-ketoisocaproate / N145V


column_label: Table 5; substrate row 4-Methyl-2-oxopentanoate; enzyme row wt; metric columns Km, kcat, kcat/Km

normalized_value_unit_evidence: normalized: Km=20 mM; kcat=27 s^-1; kcat/Km=1.4 s^-1 mM^-1

row_label: Lysinibacillus sphaericus / wt / 4-Methyl-2-oxopentanoate


column_label: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs, row R-keto-gamma-methiobutyrate / N145A, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.26, 61, and 235.

raw_value_unit_evidence: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs row R-keto-gamma-methiobutyrate / N145A: Km = 0.26 mM; kcat = 61 s^-1; kcat/Km = 235 s^-1 mM^-1.

row_label: R-keto-gamma-methiobutyrate / N145A


column_label: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs, row R-keto-gamma-methiobutyrate / N145I, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.43, 47, and 109.

raw_value_unit_evidence: Table 5: Kinetic Parameters for Aliphatic Oxoacids in B. sphaericus PheDHs row R-keto-gamma-methiobutyrate / N145I: Km = 0.43 mM; kcat = 47 s^-1; kcat/Km = 109 s^-1 mM^-1.

row_label: R-keto-gamma-methiobutyrate / N145I