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', 'L307V' genotype block: Km = 0.48 ± 0.036; kcat = 0.91 ± 0.020; kcat/Km = 1.9.

normalized_value_unit_evidence: Km: printed cell 0.48 ± 0.036 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 0.48 mM. kcat: printed cell 0.91 ± 0.020 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 0.91 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 0.91 / 0.48 = 1.8958333333333335 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-Norvaline', 'L307V' genotype block: column 'Km +/- SEM (mM)' prints 0.48 ± 0.036; column 'kcat +/- SEM (s^-1)' prints 0.91 ± 0.020; column 'kcat/Km (s^-1 mM^-1)' prints 1.9.

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


enzyme_display_name: phenylalanine dehydrogenase

organism: Lysinibacillus sphaericus

substrate_name: L-Phenylalanine

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

mutation_type: substitution

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-Phenylalanine', 'G124A' genotype block: Km = 8.1 ± 0.48; kcat = 4.2 ± 0.11; kcat/Km = 0.52.

normalized_value_unit_evidence: Km: printed cell 8.1 ± 0.48 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 8.1 mM. kcat: printed cell 4.2 ± 0.11 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 4.2 s^(-1). kcat/Km: Printed Table 1 kcat/Km cell 0.52 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 0.52 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 4.2 / 8.1 = 0.5185185185185186 s^-1 mM^-1, and the paper's own efficiency cell is printed as 0.52 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-Phenylalanine', 'G124A' genotype block: column 'Km +/- SEM (mM)' prints 8.1 ± 0.48; column 'kcat +/- SEM (s^-1)' prints 4.2 ± 0.11; column 'kcat/Km (s^-1 mM^-1)' prints 0.52.

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

data_origin: experimental

enzyme: phenylalanine dehydrogenase

substrate: L-Phenylalanine

status: corrected

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23307 and applied mutation signature G124A/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-Phenylalanine', 'G124A/L307V' genotype block: Km = 7.2 ± 0.81; kcat = 5.1 ± 0.25; kcat/Km = 0.71.

normalized_value_unit_evidence: Km: printed cell 7.2 ± 0.81 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 7.2 mM. kcat: printed cell 5.1 ± 0.25 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 5.1 s^(-1). kcat/Km: Printed Table 1 kcat/Km cell 0.71 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 0.71 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 5.1 / 7.2 = 0.7083333333333333 s^-1 mM^-1, and the paper's own efficiency cell is printed as 0.71 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-Phenylalanine', 'G124A/L307V' genotype block: column 'Km +/- SEM (mM)' prints 7.2 ± 0.81; column 'kcat +/- SEM (s^-1)' prints 5.1 ± 0.25; column 'kcat/Km (s^-1 mM^-1)' prints 0.71.

row_label: Table 1, substrate line 'L-Phenylalanine', 'G124A/L307V' genotype block


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-Phenylalanine', 'L307V' genotype block: Km = 0.53 ± 0.039; kcat = 18 ± 0.45; kcat/Km = 34.

normalized_value_unit_evidence: Km: printed cell 0.53 ± 0.039 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 0.53 mM. kcat: printed cell 18 ± 0.45 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 18.0 s^(-1). kcat/Km: Printed Table 1 kcat/Km cell 34 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 34.0 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 18.0 / 0.53 = 33.9622641509434 s^-1 mM^-1, and the paper's own efficiency cell is printed as 34 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-Phenylalanine', 'L307V' genotype block: column 'Km +/- SEM (mM)' prints 0.53 ± 0.039; column 'kcat +/- SEM (s^-1)' prints 18 ± 0.45; column 'kcat/Km (s^-1 mM^-1)' prints 34.

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


substrate_name: L-Tyrosine

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-Tyrosine', 'L307V' genotype block: Km = 0.49 ± 0.014; kcat = 21 ± 0.17; kcat/Km = 43.

normalized_value_unit_evidence: Km: printed cell 0.49 ± 0.014 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 0.49 mM. kcat: printed cell 21 ± 0.17 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 21.0 s^(-1). kcat/Km: Printed Table 1 kcat/Km cell 43 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 43.0 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 21.0 / 0.49 = 42.85714285714286 s^-1 mM^-1, and the paper's own efficiency cell is printed as 43 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-Tyrosine', 'L307V' genotype block: column 'Km +/- SEM (mM)' prints 0.49 ± 0.014; column 'kcat +/- SEM (s^-1)' prints 21 ± 0.17; column 'kcat/Km (s^-1 mM^-1)' prints 43.

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

substrate: L-Tyrosine


substrate_name: L-Valine

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-Valine', 'G124A' genotype block: Km = 0.13 ± 0.012; kcat = 0.97 ± 0.030; kcat/Km = 7.5.

normalized_value_unit_evidence: Km: printed cell 0.13 ± 0.012 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 0.13 mM. kcat: printed cell 0.97 ± 0.030 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 0.97 s^(-1). kcat/Km: Printed Table 1 kcat/Km cell 7.5 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 7.5 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 0.97 / 0.13 = 7.461538461538461 s^-1 mM^-1, and the paper's own efficiency cell is printed as 7.5 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-Valine', 'G124A' genotype block: column 'Km +/- SEM (mM)' prints 0.13 ± 0.012; column 'kcat +/- SEM (s^-1)' prints 0.97 ± 0.030; column 'kcat/Km (s^-1 mM^-1)' prints 7.5.

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

substrate: L-Valine


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-Valine', 'G124A/L307V' genotype block: Km = 0.27 ± 0.019; kcat = 1.9 ± 0.044; kcat/Km = 7.0.

normalized_value_unit_evidence: Km: printed cell 0.27 ± 0.019 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 0.27 mM. kcat: printed cell 1.9 ± 0.044 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 1.9 s^(-1). kcat/Km: Printed Table 1 kcat/Km cell 7.0 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 7.0 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 1.9 / 0.27 = 7.037037037037036 s^-1 mM^-1, and the paper's own efficiency cell is printed as 7.0 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-Valine', 'G124A/L307V' genotype block: column 'Km +/- SEM (mM)' prints 0.27 ± 0.019; column 'kcat +/- SEM (s^-1)' prints 1.9 ± 0.044; column 'kcat/Km (s^-1 mM^-1)' prints 7.0.

row_label: Table 1, substrate line 'L-Valine', 'G124A/L307V' genotype block


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-Valine', 'L307V' genotype block: Km = 2.2 ± 0.19; kcat = 1.4 ± 0.048; kcat/Km = 0.64.

normalized_value_unit_evidence: Km: printed cell 2.2 ± 0.19 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 2.2 mM. kcat: printed cell 1.4 ± 0.048 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 0.64 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 0.64 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 1.4 / 2.2 = 0.6363636363636362 s^-1 mM^-1, and the paper's own efficiency cell is printed as 0.64 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-Valine', 'L307V' genotype block: column 'Km +/- SEM (mM)' prints 2.2 ± 0.19; column 'kcat +/- SEM (s^-1)' prints 1.4 ± 0.048; column 'kcat/Km (s^-1 mM^-1)' prints 0.64.

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


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

assay_conditions_summary: pH 8.6; 298.15 K; cofactor NADH

column_label: Table 2: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various ketoacid 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 'DL-a-Keto-b-methyl-n-valerate', 'G124A' genotype block: Km = 1.3 ± 0.15; kcat = 16 ± 0.91; kcat/Km = 12.

normalized_value_unit_evidence: Km: printed cell 1.3 ± 0.15 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 1.3 mM. kcat: printed cell 16 ± 0.91 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 16.0 s^(-1). kcat/Km: Printed Table 2 kcat/Km cell 12 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 12.0 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 16.0 / 1.3 = 12.307692307692307 s^-1 mM^-1, and the paper's own efficiency cell is printed as 12 at the two-figure precision this table uses.

raw_value_unit_evidence: Table 2: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various ketoacid substrates (Eur. J. Biochem. 270, 4628-4634 (2003)), substrate line 'DL-a-Keto-b-methyl-n-valerate', 'G124A' genotype block: column 'Km +/- SEM (mM)' prints 1.3 ± 0.15; column 'kcat +/- SEM (s^-1)' prints 16 ± 0.91; column 'kcat/Km (s^-1 mM^-1)' prints 12.

row_label: Table 2, substrate line 'DL-a-Keto-b-methyl-n-valerate', 'G124A' genotype block


column_label: Table 2: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various ketoacid 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 'DL-a-Keto-b-methyl-n-valerate', 'G124A/L307V' genotype block: Km = 0.42 ± 0.041; kcat = 13 ± 00.57; kcat/Km = 31.

normalized_value_unit_evidence: Km: printed cell 0.42 ± 0.041 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 0.42 mM. kcat: printed cell 13 ± 00.57 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 13.0 s^(-1). kcat/Km: Printed Table 2 kcat/Km cell 31 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 31.0 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 13.0 / 0.42 = 30.952380952380953 s^-1 mM^-1, and the paper's own efficiency cell is printed as 31 at the two-figure precision this table uses.

raw_value_unit_evidence: Table 2: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various ketoacid substrates (Eur. J. Biochem. 270, 4628-4634 (2003)), substrate line 'DL-a-Keto-b-methyl-n-valerate', 'G124A/L307V' genotype block: column 'Km +/- SEM (mM)' prints 0.42 ± 0.041; column 'kcat +/- SEM (s^-1)' prints 13 ± 00.57; column 'kcat/Km (s^-1 mM^-1)' prints 31.

row_label: Table 2, substrate line 'DL-a-Keto-b-methyl-n-valerate', 'G124A/L307V' genotype block


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

substrate_name: NAD+

source_db: brenda

verification_status: unverified

kcat_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

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

assay_conditions_summary: cofactor NAD+

proof_lines:
ordered NAD+ binding
phenylalanine dehydrogenase
Rhodococcus sp. M4

substrate: NAD+

status: unverified

source: brenda


enzyme_display_name: diaminopimelate dehydrogenase

organism: Corynebacterium glutamicum

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 CgDapDH / NADPH / Amination / THDPA; columns Km (mmol/L), Kcat (/s), Kcat/Km; cells Km 0.27 +/- 0.02, Kcat 41.9 +/- 4.4, Kcat/Km 155.2.

normalized_value_unit_evidence: Km normalized_value=0.27 normalized_unit=mM; kcat normalized_value=41.9 normalized_unit=s^-1; kcat/Km normalized_value=155.2 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row CgDapDH / NADPH / Amination / THDPA: Km 0.27 +/- 0.02 mmol/L; Kcat 41.9 +/- 4.4 /s; Kcat/Km 155.2.

row_label: CgDapDH / NADPH / Amination / THDPA

enzyme: diaminopimelate dehydrogenase


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 CgDapDH / NADP+ / Deamination / meso-DAP; columns Km (mmol/L), Kcat (/s), Kcat/Km; cells Km 2.8 +/- 0.3, Kcat 115.4 +/- 15.8, Kcat/Km 41.2.

normalized_value_unit_evidence: Km normalized_value=2.8 normalized_unit=mM; kcat normalized_value=115.4 normalized_unit=s^-1; kcat/Km normalized_value=41.2 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row CgDapDH / NADP+ / Deamination / meso-DAP: Km 2.8 +/- 0.3 mmol/L; Kcat 115.4 +/- 15.8 /s; Kcat/Km 41.2.


column_label: Table 1. The kinetic parameter (±SD) of different DapDH for different substrate with NADPH or NADP+ as cofactora.; row CgDapDH / NADPH / Amination / NH4+; columns Km (mmol/L), Kcat (/s), Kcat/Km; cells Km 39.2 +/- 6.5, Kcat 768.3 +/- 62.5, Kcat/Km 23.8.

normalized_value_unit_evidence: Km normalized_value=39.2 normalized_unit=mM; kcat normalized_value=768.3 normalized_unit=s^-1; kcat/Km normalized_value=23.8 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row CgDapDH / NADPH / Amination / NH4+: Km 39.2 +/- 6.5 mmol/L; Kcat 768.3 +/- 62.5 /s; Kcat/Km 23.8.

row_label: CgDapDH / NADPH / Amination / NH4+


verification_status: verified

assay_conditions_summary: pH 8; cofactor NAD+

column_label: Abstract reports Km values for L-phenylalanine and NAD+ were 0.21 and 0.13 mM respectively.

raw_value_unit_evidence: Km raw_value=0.13 mM raw_unit=mM

row_label: Bacillus sphaericus recombinant PheDH / NAD+

table_label: PubMed XML abstract PMID 18506218

status: verified


column_label: Table 2: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various ketoacid 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 'DL-a-Keto-b-methyl-n-valerate', 'L307V' genotype block: Km = 8.5 ± 0.70; kcat = 10 ± 0.46; kcat/Km = 1.2.

normalized_value_unit_evidence: Km: printed cell 8.5 ± 0.70 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 8.5 mM. kcat: printed cell 10 ± 0.46 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 10.0 s^(-1). kcat/Km: Printed Table 2 kcat/Km cell 1.2 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 1.2 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 10.0 / 8.5 = 1.1764705882352942 s^-1 mM^-1, and the paper's own efficiency cell is printed as 1.2 at the two-figure precision this table uses.

raw_value_unit_evidence: Table 2: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various ketoacid substrates (Eur. J. Biochem. 270, 4628-4634 (2003)), substrate line 'DL-a-Keto-b-methyl-n-valerate', 'L307V' genotype block: column 'Km +/- SEM (mM)' prints 8.5 ± 0.70; column 'kcat +/- SEM (s^-1)' prints 10 ± 0.46; column 'kcat/Km (s^-1 mM^-1)' prints 1.2.

row_label: Table 2, substrate line 'DL-a-Keto-b-methyl-n-valerate', 'L307V' genotype block


substrate_name: phenylpyruvate

column_label: Table 2: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various ketoacid 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 'Phenylpyruvate', 'G124A' genotype block: Km = 7.3 ± 1.2; kcat = 31 ± 2.3; kcat/Km = 4.2.

normalized_value_unit_evidence: Km: printed cell 7.3 ± 1.2 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 7.3 mM. kcat: printed cell 31 ± 2.3 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 31.0 s^(-1). kcat/Km: Printed Table 2 kcat/Km cell 4.2 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 4.2 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 31.0 / 7.3 = 4.2465753424657535 s^-1 mM^-1, and the paper's own efficiency cell is printed as 4.2 at the two-figure precision this table uses.

raw_value_unit_evidence: Table 2: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various ketoacid substrates (Eur. J. Biochem. 270, 4628-4634 (2003)), substrate line 'Phenylpyruvate', 'G124A' genotype block: column 'Km +/- SEM (mM)' prints 7.3 ± 1.2; column 'kcat +/- SEM (s^-1)' prints 31 ± 2.3; column 'kcat/Km (s^-1 mM^-1)' prints 4.2.

row_label: Table 2, substrate line 'Phenylpyruvate', 'G124A' genotype block

substrate: phenylpyruvate


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


column_label: Table 2: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various ketoacid 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 'Phenylpyruvate', 'L307V' genotype block: Km = 0.22 ± 0.019; kcat = 49 ± 1.6; kcat/Km = 223.

normalized_value_unit_evidence: Km: printed cell 0.22 ± 0.019 in the column head 'Km +/- SEM (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 0.22 mM. kcat: printed cell 49 ± 1.6 in the column head 'kcat +/- SEM (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 49.0 s^(-1). kcat/Km: Printed Table 2 kcat/Km cell 223 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 223.0 s^(-1)*mM^(-1). Closure reading: the quotient of the two printed component cells is 49.0 / 0.22 = 222.72727272727272 s^-1 mM^-1, and the paper's own efficiency cell is printed as 223 at the two-figure precision this table uses.

raw_value_unit_evidence: Table 2: Apparent Km and kcat values of wild-type and mutant phenylalanine dehydrogenase (PheDH) for various ketoacid substrates (Eur. J. Biochem. 270, 4628-4634 (2003)), substrate line 'Phenylpyruvate', 'L307V' genotype block: column 'Km +/- SEM (mM)' prints 0.22 ± 0.019; column 'kcat +/- SEM (s^-1)' prints 49 ± 1.6; column 'kcat/Km (s^-1 mM^-1)' prints 223.

row_label: Table 2, substrate line 'Phenylpyruvate', 'L307V' genotype block


proof_lines: DapDH THDPA meso-DAP


proof_lines: DapDH meso-DAP THDPA


proof_lines: DapDH NH4+ ammonium


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

organism: Homo sapiens

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

proof_lines:
hGDH1, mutant C323Y
hGDH2, mutant C323Y

enzyme: glutamate dehydrogenase [NAD(P)+]


proof_lines:
hGDH1, mutant C323R
hGDH2, mutant C323R


proof_lines:
hGDH1, mutant C323G
hGDH2, mutant C323G


proof_lines:
hGDH1, mutant C323L
hGDH2, mutant C323L


proof_lines:
hGDH1, mutant C323M
hGDH2, mutant C323M


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23307 and applied mutation signature N145L to reconstruct the assayed variant sequence.

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

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 'R-keto-γ-methiobutyrate', enzyme row 'N145L'; column Km (mM) = 0.28; column kcat (s-1) = 25; column kcat/Km (s-1 mM-1) = 89. captured primary segment: alpha-keto-gamma-methiobutyrate | N145L | Km 0.28 mM | kcat 25 s^-1 | kcat/Km 89 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 5 Km cell 0.28 mM; the printed column is already in mM, so no unit conversion applies and the value is 0.28 mM. kcat: printed Table 5 kcat cell 25 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 25.0 s^(-1). kcat/Km: printed Table 5 kcat/Km cell 89 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 89.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 25.0 / 0.28 = 89.28571428571428 s^-1 mM^-1, against the printed efficiency cell 89.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 5, substrate block 'R-keto-γ-methiobutyrate', enzyme row 'N145L': Km = 0.28 mM; kcat = 25 s^-1; kcat/Km = 89 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23307 and applied mutation signature N145V 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 'R-keto-γ-methiobutyrate', enzyme row 'N145V'; column Km (mM) = 0.29; column kcat (s-1) = 34; column kcat/Km (s-1 mM-1) = 117. captured primary segment: alpha-keto-gamma-methiobutyrate | N145V | Km 0.29 mM | kcat 34 s^-1 | kcat/Km 117 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 5 Km cell 0.29 mM; the printed column is already in mM, so no unit conversion applies and the value is 0.29 mM. kcat: printed Table 5 kcat cell 34 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 34.0 s^(-1). kcat/Km: printed Table 5 kcat/Km cell 117 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 117.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 34.0 / 0.29 = 117.24137931034484 s^-1 mM^-1, against the printed efficiency cell 117.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 5, substrate block 'R-keto-γ-methiobutyrate', enzyme row 'N145V': Km = 0.29 mM; kcat = 34 s^-1; kcat/Km = 117 s^-1 mM^-1.


kcat_over_km_origin: calculated


substrate_name: alpha-Ketovaline

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

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

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 'R-ketoisovalerate', enzyme row 'N145A'; column Km (mM) = 3.3; column kcat (s-1) = 54; column kcat/Km (s-1 mM-1) = 16. captured primary segment: alpha-ketoisovalerate | N145A | Km 3.3 mM | kcat 54 s^-1 | kcat/Km 16 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 5 Km cell 3.3 mM; the printed column is already in mM, so no unit conversion applies and the value is 3.3 mM. kcat: printed Table 5 kcat cell 54 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 54.0 s^(-1). kcat/Km: printed Table 5 kcat/Km cell 16 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 16.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 54.0 / 3.3 = 16.363636363636363 s^-1 mM^-1, against the printed efficiency cell 16.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 5, substrate block 'R-ketoisovalerate', enzyme row 'N145A': Km = 3.3 mM; kcat = 54 s^-1; kcat/Km = 16 s^-1 mM^-1.

substrate: alpha-Ketovaline


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23307 and applied mutation signature N145I 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 'R-ketoisovalerate', enzyme row 'N145I'; column Km (mM) = 4.3; column kcat (s-1) = 59; column kcat/Km (s-1 mM-1) = 14. captured primary segment: alpha-ketoisovalerate | N145I | Km 4.3 mM | kcat 59 s^-1 | kcat/Km 14 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 5 Km cell 4.3 mM; the printed column is already in mM, so no unit conversion applies and the value is 4.3 mM. kcat: printed Table 5 kcat cell 59 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 59.0 s^(-1). kcat/Km: printed Table 5 kcat/Km cell 14 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 14.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 59.0 / 4.3 = 13.72093023255814 s^-1 mM^-1, against the printed efficiency cell 14.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 5, substrate block 'R-ketoisovalerate', enzyme row 'N145I': Km = 4.3 mM; kcat = 59 s^-1; kcat/Km = 14 s^-1 mM^-1.


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 'R-ketoisovalerate', enzyme row 'N145L'; column Km (mM) = 7.4; column kcat (s-1) = 36; column kcat/Km (s-1 mM-1) = 4.9. captured primary segment: alpha-ketoisovalerate | N145L | Km 7.4 mM | kcat 36 s^-1 | kcat/Km 4.9 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 5 Km cell 7.4 mM; the printed column is already in mM, so no unit conversion applies and the value is 7.4 mM. kcat: printed Table 5 kcat cell 36 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 36.0 s^(-1). kcat/Km: printed Table 5 kcat/Km cell 4.9 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 4.9 s^(-1)*mM^(-1). Quotient disclosure for this row: 36.0 / 7.4 = 4.864864864864865 s^-1 mM^-1, against the printed efficiency cell 4.9 s^-1 mM^-1.

raw_value_unit_evidence: Table 5, substrate block 'R-ketoisovalerate', enzyme row 'N145L': Km = 7.4 mM; kcat = 36 s^-1; kcat/Km = 4.9 s^-1 mM^-1.


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 'R-ketoisovalerate', enzyme row 'N145V'; column Km (mM) = 4.2; column kcat (s-1) = 46; column kcat/Km (s-1 mM-1) = 11. captured primary segment: alpha-ketoisovalerate | N145V | Km 4.2 mM | kcat 46 s^-1 | kcat/Km 11 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 5 Km cell 4.2 mM; the printed column is already in mM, so no unit conversion applies and the value is 4.2 mM. kcat: printed Table 5 kcat cell 46 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 46.0 s^(-1). kcat/Km: printed Table 5 kcat/Km cell 11 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 11.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 46.0 / 4.2 = 10.952380952380953 s^-1 mM^-1, against the printed efficiency cell 11.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 5, substrate block 'R-ketoisovalerate', enzyme row 'N145V': Km = 4.2 mM; kcat = 46 s^-1; kcat/Km = 11 s^-1 mM^-1.


substrate_name: L-Isoleucine

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

column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids 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 4, substrate block 'L-isoleucine', enzyme row 'N145A'; column Km (mM) = 0.017; column kcat (s-1) = 0.50; column kcat/Km (s-1 mM-1) = 29. captured primary segment: L-isoleucine | N145A | Km 0.017 mM | kcat 0.50 s^-1 | kcat/Km 29 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 4 Km cell 0.017 mM; the printed column is already in mM, so no unit conversion applies and the value is 0.017 mM. kcat: printed Table 4 kcat cell 0.50 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.5 s^(-1). kcat/Km: printed Table 4 kcat/Km cell 29 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 29.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.5 / 0.017 = 29.41176470588235 s^-1 mM^-1, against the printed efficiency cell 29.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, substrate block 'L-isoleucine', enzyme row 'N145A': Km = 0.017 mM; kcat = 0.50 s^-1; kcat/Km = 29 s^-1 mM^-1.

substrate: L-Isoleucine


column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids 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 4, substrate block 'L-isoleucine', enzyme row 'N145I'; column Km (mM) = 0.014; column kcat (s-1) = 0.19; column kcat/Km (s-1 mM-1) = 14. captured primary segment: L-isoleucine | N145I | Km 0.014 mM | kcat 0.19 s^-1 | kcat/Km 14 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 4 Km cell 0.014 mM; the printed column is already in mM, so no unit conversion applies and the value is 0.014 mM. kcat: printed Table 4 kcat cell 0.19 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.19 s^(-1). kcat/Km: printed Table 4 kcat/Km cell 14 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 14.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.19 / 0.014 = 13.571428571428571 s^-1 mM^-1, against the printed efficiency cell 14.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, substrate block 'L-isoleucine', enzyme row 'N145I': Km = 0.014 mM; kcat = 0.19 s^-1; kcat/Km = 14 s^-1 mM^-1.


column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids 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 4, substrate block 'L-isoleucine', enzyme row 'N145L'; column Km (mM) = 0.0082; column kcat (s-1) = 0.11; column kcat/Km (s-1 mM-1) = 13. captured primary segment: L-isoleucine | N145L | Km 0.0082 mM | kcat 0.11 s^-1 | kcat/Km 13 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 4 Km cell 0.0082 mM; the printed column is already in mM, so no unit conversion applies and the value is 0.0082 mM. kcat: printed Table 4 kcat cell 0.11 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.11 s^(-1). kcat/Km: printed Table 4 kcat/Km cell 13 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 13.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.11 / 0.0082 = 13.414634146341463 s^-1 mM^-1, against the printed efficiency cell 13.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, substrate block 'L-isoleucine', enzyme row 'N145L': Km = 0.0082 mM; kcat = 0.11 s^-1; kcat/Km = 13 s^-1 mM^-1.


enzyme_display_name: leucine dehydrogenase

organism: Bacillus subtilis

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

enzyme: leucine dehydrogenase


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


substrate_name: L-Leu

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

proof_lines: competitive inhibition of the reductive amination of 4-methylthio-2-oxobutanoate

substrate: L-Leu


substrate_name: L-Ile

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

substrate: L-Ile


substrate_name: L-Val

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

substrate: L-Val


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


substrate_name: L-Met

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

substrate: L-Met


organism: Symbiobacterium thermophilum

column_label: Table 1. The kinetic parameter (±SD) of different DapDH for different substrate with NADPH or NADP+ as cofactora.; row StDapDH / NADPH / Amination / THDPA; columns Km (mmol/L), Kcat (/s), Kcat/Km; cells Km 0.24 +/- 0.3, Kcat 52.8 +/- 4.5, Kcat/Km 220.0.

normalized_value_unit_evidence: Km normalized_value=0.24 normalized_unit=mM; kcat normalized_value=52.8 normalized_unit=s^-1; kcat/Km normalized_value=220.0 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row StDapDH / NADPH / Amination / THDPA: Km 0.24 +/- 0.3 mmol/L; Kcat 52.8 +/- 4.5 /s; Kcat/Km 220.0.

row_label: StDapDH / NADPH / Amination / THDPA


column_label: Table 1. The kinetic parameter (±SD) of different DapDH for different substrate with NADPH or NADP+ as cofactora.; row StDapDH / NADP+ / Deamination / meso-DAP; columns Km (mmol/L), Kcat (/s), Kcat/Km; cells Km 1.8 +/- 0.08, Kcat 145.7 +/- 1.4, Kcat/Km 80.9.

normalized_value_unit_evidence: Km normalized_value=1.8 normalized_unit=mM; kcat normalized_value=145.7 normalized_unit=s^-1; kcat/Km normalized_value=80.9 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row StDapDH / NADP+ / Deamination / meso-DAP: Km 1.8 +/- 0.08 mmol/L; Kcat 145.7 +/- 1.4 /s; Kcat/Km 80.9.


column_label: Table 1. The kinetic parameter (±SD) of different DapDH for different substrate with NADPH or NADP+ as cofactora.; row StDapDH / NADPH / Amination / NH4+; columns Km (mmol/L), Kcat (/s), Kcat/Km; cells Km 6.3 +/- 0.7, Kcat 387.4 +/- 45.3, Kcat/Km 61.5.

normalized_value_unit_evidence: Km normalized_value=6.3 normalized_unit=mM; kcat normalized_value=387.4 normalized_unit=s^-1; kcat/Km normalized_value=61.5 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row StDapDH / NADPH / Amination / NH4+: Km 6.3 +/- 0.7 mmol/L; Kcat 387.4 +/- 45.3 /s; Kcat/Km 61.5.

row_label: StDapDH / NADPH / Amination / NH4+


enzyme_display_name: alanine dehydrogenase

organism: Bradyrhizobium japonicum

enzyme: alanine dehydrogenase


substrate_name: pyruvate

substrate: pyruvate


substrate_name: L-norvaline

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

substrate: L-norvaline


substrate_name: L-Ala

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

substrate: L-Ala


substrate_name: L-Ser

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

substrate: L-Ser


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


substrate_name: glyoxylate

substrate: glyoxylate


organism: Archaeoglobus fulgidus


assay_conditions_summary: pH 8.5; 355.15 K; cofactor NAD+


substrate_name: oxaloacetate

substrate: oxaloacetate


assay_conditions_summary: pH 8.5; 355.15 K; cofactor NADH


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


enzyme_display_name: glutamate dehydrogenase (NADP+)

organism: Escherichia coli

substrate_name: L-glutamate

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

enzyme: glutamate dehydrogenase (NADP+)

substrate: L-glutamate


substrate_name: NADP+

assay_conditions_summary: pH 8; 295.15 K; cofactor NADP+

substrate: NADP+


proof_lines: pH 8.0, 22°C, recombinant wild-type enzyme

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

proof_lines: wild-type EcGDH, Vmax: 45.6 micromol/min/mg, pH 8.0, 25°C


proof_lines: wild-type EcGDH, Vmax: 37.9 micromol/min/mg, pH 8.0, 25°C


enzyme_display_name: secondary-alkyl amine dehydrogenase [NAD(P)+]

organism: Streptomyces virginiae

sequence_source: multiple

proof_lines:
pH 7, 25°C
pH 9, 25°C

source_databases_merged: brenda uniprot


substrate_name: NAD+

proof_lines:
pH 9, 25°C
pH 8, 25°C

enzyme: secondary-alkyl amine dehydrogenase [NAD(P)+]

substrate: NAD+


substrate_name: dihydroxyacetone

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

substrate: dihydroxyacetone


substrate_name: serinol

smiles: C(C(CO)N)O

substrate: serinol


smiles: N


enzyme_display_name: UniProt A9BHL2

organism: Petrotoga mobilis

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt A9BHL2

source: skid


enzyme_display_name: UniProt S9Q235

organism: Cystobacter fuscus

substrate_name: NADH

enzyme: UniProt S9Q235

substrate: NADH


substrate_name: NADPH

substrate: NADPH


substrate_name: Isobutanal

smiles: CC(C)C=O

substrate: Isobutanal


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

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

source_databases_merged: skid uniprot


substrate_name: cyclohexanone

substrate: cyclohexanone


enzyme_display_name: secondary-alkyl amine dehydrogenase [NAD(P)(+)]

organism: Geobacillus stearothermophilus

smiles: CCC(=O)CO


enzyme: secondary-alkyl amine dehydrogenase [NAD(P)(+)]


organism: Sporosarcina psychrophila


organism: Thermoactinomyces intermedius


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E102A to reconstruct the assayed variant sequence.


enzyme_display_name: Amine dehydrogenase

source_db: uniprot

enzyme: Amine dehydrogenase

source: uniprot


organism: Petrotoga mobilis (strain DSM 10674 / SJ95)


enzyme_display_name: D-aspartate oxidase

organism: Vanrija humicola

substrate_name: D-Asp

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R243D to reconstruct the assayed variant sequence.

enzyme: D-aspartate oxidase

substrate: D-Asp


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R243E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R243K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R243M to reconstruct the assayed variant sequence.


assay_conditions_summary: 298.15 K; cofactor NADH


organism: Lysinibacillus sphaericus

substrate_name: L-Isoleucine

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.

assay_conditions_summary: pH 10.4; 298.15 K; cofactor NAD+

column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs, row L-isoleucine / N145V, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.0095, 0.15, and 16.

raw_value_unit_evidence: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs row L-isoleucine / N145V: Km = 0.0095 mM; kcat = 0.15 s^-1; kcat/Km = 16 s^-1 mM^-1.

row_label: L-isoleucine / N145V

substrate: L-Isoleucine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N142V/N145V to reconstruct the assayed variant sequence.

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_name: L-Leucine

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

column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs, row L-leucine / N145A, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.032, 0.98, and 31.

raw_value_unit_evidence: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs row L-leucine / N145A: Km = 0.032 mM; kcat = 0.98 s^-1; kcat/Km = 31 s^-1 mM^-1.

row_label: L-leucine / N145A

substrate: L-Leucine


sequence_variant_note: Resolved canonical sequence from uniprotkb:P23307 and applied mutation signature N145I to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs, row L-leucine / N145I, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.015, 1.2, and 80.

raw_value_unit_evidence: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs row L-leucine / N145I: Km = 0.015 mM; kcat = 1.2 s^-1; kcat/Km = 80 s^-1 mM^-1.

row_label: L-leucine / N145I


sequence_variant_note: Resolved canonical sequence from uniprotkb:P23307 and applied mutation signature N145L to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs, row L-leucine / N145L, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.021, 0.45, and 21.

raw_value_unit_evidence: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs row L-leucine / N145L: Km = 0.021 mM; kcat = 0.45 s^-1; kcat/Km = 21 s^-1 mM^-1.

row_label: L-leucine / N145L


column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs, row L-leucine / N145V, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.013, 0.84, and 65.

raw_value_unit_evidence: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs row L-leucine / N145V: Km = 0.013 mM; kcat = 0.84 s^-1; kcat/Km = 65 s^-1 mM^-1.

row_label: L-leucine / N145V


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_name: L-Methionine

column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs, row L-methionine / N145A, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.078, 3.1, and 40.

raw_value_unit_evidence: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs row L-methionine / N145A: Km = 0.078 mM; kcat = 3.1 s^-1; kcat/Km = 40 s^-1 mM^-1.

row_label: L-methionine / N145A

substrate: L-Methionine


column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs, row L-methionine / N145I, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.14, 3.1, and 22.

raw_value_unit_evidence: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs row L-methionine / N145I: Km = 0.14 mM; kcat = 3.1 s^-1; kcat/Km = 22 s^-1 mM^-1.

row_label: L-methionine / N145I


column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs, row L-methionine / N145L, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.15, 1.8, and 12.

raw_value_unit_evidence: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs row L-methionine / N145L: Km = 0.15 mM; kcat = 1.8 s^-1; kcat/Km = 12 s^-1 mM^-1.

row_label: L-methionine / N145L


organism: Bacillus cereus

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


assay_conditions_summary: pH 9.5; 308.15 K; cofactor NADH

proof_lines:
wild-type, pH 9.5, 35°C
wild-type, pH 8.5, 30°C
pH 10.0, 30°C, wild-type enzyme


proof_lines:
mutant E116V, pH 9.5, 35°C
mutant E116V, pH 8.5, 30°C


assay_conditions_summary: pH 8.3; 303.15 K; cofactor NADPH


assay_conditions_summary: pH 8.3; 303.15 K; cofactor NADH


substrate_name: L-norleucine

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

assay_conditions_summary: pH 10; 298.15 K; buffer 100 mM glycine-KCl-KOH

proof_lines: in 100 mM glycine-KCl-KOH buffer (pH 10), at 25°C

substrate: L-norleucine


substrate_name: L-norvaline

substrate: L-norvaline


substrate_name: L-Ile

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

substrate: L-Ile


substrate_name: L-Leu

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

substrate: L-Leu


enzyme_display_name: glutamate dehydrogenase

enzyme: glutamate dehydrogenase


substrate_name: oxaloacetate

substrate: oxaloacetate


organism: Thermomyces dupontii

substrate_name: D-glutamine

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

substrate: D-glutamine


substrate_name: D-Aspartate

substrate: D-Aspartate


substrate_name: D-glutamate

substrate: D-glutamate


substrate_name: N-Methyl-D-aspartate

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

substrate: N-Methyl-D-aspartate


organism: Mus musculus

substrate_name: D-proline

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

assay_conditions_summary: pH 8.3; 298.15 K; cofactor FAD

column_label: Table 2, mDASPO columns, D-Pro row: Km,app=169.0 +/- 25.5 mM; kcat,app=5.5 +/- 0.3 s^-1; kcat/Km=0.03 s^-1 mM^-1.

row_label: D-Pro

table_label: Table 2

substrate: D-proline


substrate_name: D-histidine

column_label: Table 2, mDASPO columns, D-His row: Km,app=8.8 +/- 2.0 mM; kcat,app=0.71 +/- 0.03 s^-1; kcat/Km=0.08 s^-1 mM^-1.

row_label: D-His

substrate: D-histidine


substrate_name: D-Asparagine

column_label: Table 2, mDASPO columns, D-Asn row: Km,app=101.4 +/- 13.5 mM; kcat,app=11.4 +/- 0.8 s^-1; kcat/Km=0.11 s^-1 mM^-1.

row_label: D-Asn

substrate: D-Asparagine


substrate_name: D-Glutamate

column_label: Table 2, mDASPO columns, D-Glu row: Km,app=68.4 +/- 12.8 mM; kcat,app=16.8 +/- 1.7 s^-1; kcat/Km=0.25 s^-1 mM^-1.

row_label: D-Glu

substrate: D-Glutamate


organism: Microbacterium sp. MA1

substrate_name: cyclohexanone

substrate: cyclohexanone


substrate_name: isobutanal

substrate: isobutanal


organism: Mycolicibacterium smegmatis

substrate_name: NADPH

assay_conditions_summary: pH 9.5; 296.15 K; cofactor NADPH

substrate: NADPH


substrate_name: Isobutanal

substrate: Isobutanal


substrate_name: NADH

assay_conditions_summary: pH 9.5; 296.15 K; cofactor NADH

substrate: NADH


enzyme_display_name: glycine dehydrogenase (cytochrome)

organism: Nitrobacter winogradskyi

substrate_name: ferricytochrome c

enzyme: glycine dehydrogenase (cytochrome)

substrate: ferricytochrome c


substrate_name: glycine

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

substrate: glycine


organism: Pelophylax lessonae

substrate_name: N-methyl-D-Asp

proof_lines:
pH 8.2, 37°C, kidney
pH 8.2, 37°C, brain
pH 8.2, 37°C, liver

substrate: N-methyl-D-Asp


substrate_name: D-Asp

substrate: D-Asp


substrate_name: D-Glu

substrate: D-Glu


enzyme_display_name: glycine cleavage system

organism: Gallus gallus

substrate_name: tetrahydrofolate

enzyme: glycine cleavage system

substrate: tetrahydrofolate


organism: Fervidobacterium nodosum

assay_conditions_summary: pH 8.5; 328.15 K; cofactor NAD+

proof_lines: with NAD+ as cosubstrate, at pH 8.5 and 55°C


substrate_name: NADP+

assay_conditions_summary: pH 8.5; 328.15 K; cofactor NADP+

substrate: NADP+


substrate_name: NAD+

substrate: NAD+


substrate_name: Unknown

substrate: Unknown


organism: Rattus norvegicus


smiles: CCC=O


sequence_source: uniprot


substrate_name: N-Methyl-D-aspartate

substrate: N-Methyl-D-aspartate


proof_lines: value for the isolated P-protein, pH 6.6, 37°C


organism: Synechocystis sp. PCC 6803

substrate_name: lipoic acid

substrate: lipoic acid


substrate_name: D-Leu

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q75WF1 and applied mutation signature H56N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM potassium phosphate; cofactor FAD

column_label: Table I: Apparent kinetic parameters of the wild-type and the His56 mutants of ChDDO (J. Biochem. 2016, 159(3):371-378); each enzyme column group prints the column heads kcat (s^-1), Km (mM) and kcat/Km (s^-1 M^-1). Table I, H56N column group, substrate row D-Leu; column kcat (s^-1) = 0.7; column Km (mM) = 8.8; column kcat/Km (s^-1 M^-1) = 74. captured primary segment: D-Leu | H56N mutant of ChDDO | kcat 0.7 s^-1 | Km 8.8 mM | kcat/Km 74 s^-1 M^-1

normalized_value_unit_evidence: kcat: printed Table I cell 0.7 s^-1; the printed turnover column is per second, so no conversion applies and the paper-side value is 0.7 s^(-1). Km: printed Table I cell 8.8 mM; the printed Michaelis column is already in mM, so no conversion applies and the paper-side value is 8.8 mM. kcat/Km: printed Table I cell 74 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 74 / 1000 = 0.074 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, H56N column group, substrate row D-Leu: kcat = 0.7 s^-1; Km = 8.8 mM; printed kcat/Km = 74 s^-1 M^-1.

substrate: D-Leu


substrate_name: D-Gln

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q75WF1 and applied mutation signature H56A to reconstruct the assayed variant sequence.

column_label: Table I: Apparent kinetic parameters of the wild-type and the His56 mutants of ChDDO (J. Biochem. 2016, 159(3):371-378); each enzyme column group prints the column heads kcat (s^-1), Km (mM) and kcat/Km (s^-1 M^-1). Table I, H56A column group, substrate row D-Gln; column kcat (s^-1) = 2.2; column Km (mM) = 39.4; column kcat/Km (s^-1 M^-1) = 55. captured primary segment: D-Gln | H56A mutant of ChDDO | kcat 2.2 s^-1 | Km 39.4 mM | kcat/Km 55 s^-1 M^-1

normalized_value_unit_evidence: kcat: printed Table I cell 2.2 s^-1; the printed turnover column is per second, so no conversion applies and the paper-side value is 2.2 s^(-1). Km: printed Table I cell 39.4 mM; the printed Michaelis column is already in mM, so no conversion applies and the paper-side value is 39.4 mM. kcat/Km: printed Table I cell 55 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 55 / 1000 = 0.055 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, H56A column group, substrate row D-Gln: kcat = 2.2 s^-1; Km = 39.4 mM; printed kcat/Km = 55 s^-1 M^-1.

substrate: D-Gln


proof_lines: pH 7.0, 20°C, recombinant wild-type enzyme


substrate_name: D-Phe

column_label: Table I: Apparent kinetic parameters of the wild-type and the His56 mutants of ChDDO (J. Biochem. 2016, 159(3):371-378); each enzyme column group prints the column heads kcat (s^-1), Km (mM) and kcat/Km (s^-1 M^-1). Table I, H56A column group, substrate row D-Phe; column kcat (s^-1) = 3.1; column Km (mM) = 14.3; column kcat/Km (s^-1 M^-1) = 218. captured primary segment: D-Phe | H56A mutant of ChDDO | kcat 3.1 s^-1 | Km 14.3 mM | kcat/Km 218 s^-1 M^-1

normalized_value_unit_evidence: kcat: printed Table I cell 3.1 s^-1; the printed turnover column is per second, so no conversion applies and the paper-side value is 3.1 s^(-1). Km: printed Table I cell 14.3 mM; the printed Michaelis column is already in mM, so no conversion applies and the paper-side value is 14.3 mM. kcat/Km: printed Table I cell 218 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 218 / 1000 = 0.218 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, H56A column group, substrate row D-Phe: kcat = 3.1 s^-1; Km = 14.3 mM; printed kcat/Km = 218 s^-1 M^-1.

substrate: D-Phe


substrate_name: D-Asn

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H56N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: D-Asn


substrate_name: D-Met

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

column_label: Table I: Apparent kinetic parameters of the wild-type and the His56 mutants of ChDDO (J. Biochem. 2016, 159(3):371-378); each enzyme column group prints the column heads kcat (s^-1), Km (mM) and kcat/Km (s^-1 M^-1). Table I, H56N column group, substrate row D-Met; column kcat (s^-1) = 4.0; column Km (mM) = 31.8; column kcat/Km (s^-1 M^-1) = 125. captured primary segment: D-Met | H56N mutant of ChDDO | kcat 4.0 s^-1 | Km 31.8 mM | kcat/Km 125 s^-1 M^-1

normalized_value_unit_evidence: kcat: printed Table I cell 4.0 s^-1; the printed turnover column is per second, so no conversion applies and the paper-side value is 4.0 s^(-1). Km: printed Table I cell 31.8 mM; the printed Michaelis column is already in mM, so no conversion applies and the paper-side value is 31.8 mM. kcat/Km: printed Table I cell 125 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 125 / 1000 = 0.125 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, H56N column group, substrate row D-Met: kcat = 4.0 s^-1; Km = 31.8 mM; printed kcat/Km = 125 s^-1 M^-1.

substrate: D-Met


column_label: Table I: Apparent kinetic parameters of the wild-type and the His56 mutants of ChDDO (J. Biochem. 2016, 159(3):371-378); each enzyme column group prints the column heads kcat (s^-1), Km (mM) and kcat/Km (s^-1 M^-1). Table I, H56N column group, substrate row D-Phe; column kcat (s^-1) = 4.1; column Km (mM) = 34.8; column kcat/Km (s^-1 M^-1) = 119. captured primary segment: D-Phe | H56N mutant of ChDDO | kcat 4.1 s^-1 | Km 34.8 mM | kcat/Km 119 s^-1 M^-1

normalized_value_unit_evidence: kcat: printed Table I cell 4.1 s^-1; the printed turnover column is per second, so no conversion applies and the paper-side value is 4.1 s^(-1). Km: printed Table I cell 34.8 mM; the printed Michaelis column is already in mM, so no conversion applies and the paper-side value is 34.8 mM. kcat/Km: printed Table I cell 119 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 119 / 1000 = 0.119 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, H56N column group, substrate row D-Phe: kcat = 4.1 s^-1; Km = 34.8 mM; printed kcat/Km = 119 s^-1 M^-1.


column_label: Table I: Apparent kinetic parameters of the wild-type and the His56 mutants of ChDDO (J. Biochem. 2016, 159(3):371-378); each enzyme column group prints the column heads kcat (s^-1), Km (mM) and kcat/Km (s^-1 M^-1). Table I, H56N column group, substrate row D-Gln; column kcat (s^-1) = 4.5; column Km (mM) = 21.0; column kcat/Km (s^-1 M^-1) = 213. captured primary segment: D-Gln | H56N mutant of ChDDO | kcat 4.5 s^-1 | Km 21.0 mM | kcat/Km 213 s^-1 M^-1

normalized_value_unit_evidence: kcat: printed Table I cell 4.5 s^-1; the printed turnover column is per second, so no conversion applies and the paper-side value is 4.5 s^(-1). Km: printed Table I cell 21.0 mM; the printed Michaelis column is already in mM, so no conversion applies and the paper-side value is 21.0 mM. kcat/Km: printed Table I cell 213 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 213 / 1000 = 0.213 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, H56N column group, substrate row D-Gln: kcat = 4.5 s^-1; Km = 21.0 mM; printed kcat/Km = 213 s^-1 M^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H56A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7


substrate_name: D-Aspartate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S308G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.3; buffer 40 mM sodium diphosphate

proof_lines: mutant enzyme S308G fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

proof_lines: His-tagged mutant enzyme S308G, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

substrate: D-Aspartate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S308A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S308A fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S308Y to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S308Y, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)


proof_lines: mutant enzyme S308Y fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)


organism: Caenorhabditis elegans

proof_lines: The values given are for the recombinant protein.


proof_lines:
pH 8.3, 37°C, recombinant DDO-2
pH 8.3, 37°C,recombinant DDO-2


enzyme_display_name: D-aspartate oxidase 3

substrate_name: N-methyl D-aspartate

enzyme: D-aspartate oxidase 3

substrate: N-methyl D-aspartate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R243E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R243K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R243M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R243D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R243A to reconstruct the assayed variant sequence.


organism: Petrotoga mobilis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E102A to reconstruct the assayed variant sequence.


source_databases_merged: brenda oed


substrate_name: NADH

assay_conditions_summary: pH 9.5; cofactor NADH

substrate: NADH


organism: Bos taurus

substrate_name: D-homocysteic acid (at 25 degrees Celsius and at pH 7.4)

proof_lines: kcat is 4.7 sec(-1) with D-aspartate as substrate (at 25 degrees Celsius and at pH 7) (PubMed:7915543). kcat is 11.1 sec(-1) with D-aspartate as substrate (at 4 degrees Celsius and at pH 7.4) (PubMed:2901415). kcat is 43.5 sec(-1) with D-as


substrate_name: D-alpha-aminoadipic acid (at 25 degrees Celsius and at pH 7.4)

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


substrate_name: glycyl-D-aspartic acid (at 25 degrees Celsius and at pH 7.4)

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


substrate_name: cis-2,3-piperidine dicarboxylic acid (at 25 degrees Celsius and at pH 7.4)


organism: Homo sapiens

substrate_name: D-glutamate (at 25 degrees Celsius and at pH 8.3)

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

proof_lines: kcat is 81.3 sec(-1) with D-aspartate as substrate (at 25 degrees Celsius and at pH 8.3) (PubMed:32553892, PubMed:31914658). kcat is 229 sec(-1) with D-aspartate as substrate (at 25 degrees Celsius) (PubMed:31914658). kcat is 68.4 sec(-1) w


substrate_name: D-asparagine (at 25 degrees Celsius and at pH 8.3)


substrate_name: D-histidine (at 25 degrees Celsius and at pH 8.3)


substrate_name: D-proline (at 25 degrees Celsius and at pH 8.3)


substrate_name: D-glutamate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F18E with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

proof_lines: recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C

substrate: D-glutamate


substrate_name: N-Methyl-D-aspartate


substrate_name: D-asparagine

substrate: D-asparagine


organism: Octopus vulgaris

column_label: Table 2 header Octopus hepatopancreas Km(mM); row 2 D-Glutamic acid; value 6.2

raw_value_unit_evidence: Table 2 Octopus hepatopancreas row 2 D-Glutamic acid, Km(mM) column = 6.2

row_label: row 2 D-Glutamic acid

table_label: ScienceDirect PDF Table 2. Substrate specificity of D-aspartate oxidase purified from hepatopancreas of Octopus vulgaris and beef kidney


column_label: Table 2 header Octopus hepatopancreas Km(mM); row 3 N-Methyl-D-Asp; value 42

normalized_value_unit_evidence: 42 mM

raw_value_unit_evidence: Table 2 Octopus hepatopancreas row 3 N-Methyl-D-Asp, Km(mM) column = 42

row_label: row 3 N-Methyl-D-Asp


column_label: Table 2 header Octopus hepatopancreas Km(mM); row 4 D-Asparagine; value 53

normalized_value_unit_evidence: 53 mM

raw_value_unit_evidence: Table 2 Octopus hepatopancreas row 4 D-Asparagine, Km(mM) column = 53

row_label: row 4 D-Asparagine


substrate_name: D-glutamine

column_label: Table 2 header Octopus hepatopancreas Km(mM); row 6 D-Glutamine; value 600

raw_value_unit_evidence: Table 2 Octopus hepatopancreas row 6 D-Glutamine, Km(mM) column = 600

row_label: row 6 D-Glutamine

substrate: D-glutamine


proof_lines: kcat is 9.83 sec(-1) with D-aspartate as substrate (at 37 degrees Celsius and at pH 8.3) (PubMed:25747990). kcat is 12.2 sec(-1) with D-aspartate as substrate (at 37 degrees Celsius and at pH 8.3) (PubMed:20567862). kcat is 58.4 sec(-1) wit

substrate: D-asparagine (at 25 degrees Celsius and at pH 8.3)


substrate: D-histidine (at 25 degrees Celsius and at pH 8.3)


substrate: D-proline (at 25 degrees Celsius and at pH 8.3)


organism: Sus scrofa

substrate_name: D-aspartate (at 37 degrees Celsius and at pH 8.3)

proof_lines: kcat is 172 sec(-1) with D-aspartate as substrate (at 37 degrees Celsius and at pH 8.3) (PubMed:17234685). kcat is 46.7 sec(-1) with D-aspartate as substrate (at 25 degrees Celsius and at pH 8.3) (PubMed:16751595). kcat is 30 sec(-1) with D


substrate_name: D-glutamate (at 37 degrees Celsius and at pH 8.3)


substrate_name: N-methyl D-aspartate (at 37 degrees Celsius and at pH 8.3)


substrate_name: D-aspartate (at pH 8.3)

proof_lines: kcat is 27.4 sec(-1) with D-aspartate as substrate (at 25 degrees Celsius and at pH 8.3).

proof_lines: kcat is 27.8 sec(-1) with D-aspartate as substrate (at 25 degrees Celsius and at pH 8.3).

substrate: D-aspartate (at pH 8.3)


substrate_name: N-methyl D-aspartate (at pH 8.3)

substrate: N-methyl D-aspartate (at pH 8.3)


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

substrate: N-methyl D-aspartate (at 37 degrees Celsius and at pH 8.3)


substrate: D-glutamate (at 37 degrees Celsius and at pH 8.3)


enzyme_display_name: 2,4-diaminopentanoate dehydrogenase

organism: Unknown prokaryotic organism

substrate_name: NAD

assay_conditions_summary: cofactor NAD+

column_label: Table 1 row DAPDH / NAD+ column Km

row_label: DAPDH / NAD+

table_label: Table 1

enzyme: 2,4-diaminopentanoate dehydrogenase

substrate: NAD


substrate_name: NADP

assay_conditions_summary: cofactor NADP+

column_label: Table 1 row DAPDH / NADP+ column Km

normalized_value_unit_evidence: Km 2.56 mM

row_label: DAPDH / NADP+

substrate: NADP


substrate_name: D-aspartate (at 25 degrees Celsius and at pH 7)


substrate_name: D-glutamate (at 25 degrees Celsius and at pH 7)


substrate_name: N-methyl D-aspartate (at 25 degrees Celsius and at pH 7)


substrate_name: D-proline (at 25 degrees Celsius and at pH 7)


organism: Vanrija humicola

substrate_name: D-alanine

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

proof_lines: pH and temperature not specified in the publication

substrate: D-alanine


substrate_name: D-Aspartate

proof_lines: kcat is 82.6 sec(-1) with D-aspartate as substrate (at 37 degrees Celsius) (PubMed:15115779). kcat is 54.2 sec(-1) with D-aspartate as substrate (at 37 degrees Celsius and at pH 7.5) (PubMed:8645733). kcat is 127.7 sec(-1) with D-aspartate


substrate_name: D-glutamate


substrate_name: N-Methyl-D-aspartate

substrate: N-Methyl-D-aspartate


enzyme_display_name: nicotine dehydrogenase

organism: Pseudomonas putida

substrate_name: (S)-nicotine

proof_lines: 37°C, pH not specified in the publication

proof_lines: kcat is 0.00664 sec(-1) with O(2) as electron acceptor (at room temperature) (PubMed:26237398). kcat is 0.0132 sec(-1) with O(2) as electron acceptor (at 37 degrees Celsius) (PubMed:26237398). kcat is 0.00611 sec(-1) with O(2) as electron a

enzyme: nicotine dehydrogenase

substrate: (S)-nicotine


organism: Talaromyces thermophilus

substrate_name: D-aspartate (at 60 degrees Celsius and at pH 7.5)

proof_lines: kcat is 123 sec(-1) with D-aspartate as substrate (at 37 degrees Celsius and at pH 7.5) (PubMed:30937498). kcat is 217 sec(-1) with D-glutamate as substrate (at 37 degrees Celsius and at pH 7.5) (PubMed:30937498). kcat is 155 sec(-1) with N


substrate_name: D-glutamate (at 60 degrees Celsius and at pH 7.5)


substrate_name: N-methyl D-aspartate (at 60 degrees Celsius and at pH 7.5)


substrate_name: D-glutamine (at 60 degrees Celsius and at pH 7.5)


proof_lines: kcat is 6.8 sec(-1) with D-aspartate as substrate (at 25 degrees Celsius and at pH 7) (PubMed:7915543). kcat is 11 sec(-1) with D-glutamate as substrate (at 25 degrees Celsius and at pH 7) (PubMed:7915543). kcat is 2.4 sec(-1) with D-prolin

substrate: D-Aspartate


substrate_name: D-proline

substrate: D-proline


enzyme_display_name: pseudooxynicotine dehydrogenase

organism: Pseudomonas sp.

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication

proof_lines: kcat is 151 sec(-1) with pseudooxynicotine as substrate.

enzyme: pseudooxynicotine dehydrogenase


organism: Oryctolagus cuniculus

proof_lines:
O2 as acceptor
ferricyanide as acceptor


proof_lines:
ferricyanide as acceptor
O2 as acceptor

substrate: D-glutamate


organism: Mus musculus

substrate_name: D-aspartate (at 37 degrees Celsius and at pH 8.3)


substrate_name: ferricytochrome c protein CycN

substrate: ferricytochrome c protein CycN


substrate_name: D-aspartate dimethylester

column_label: Table 2 header Octopus hepatopancreas Km(mM); row 5 D-Asp-dimethylester; value 150

raw_value_unit_evidence: Table 2 Octopus hepatopancreas row 5 D-Asp-dimethylester, Km(mM) column = 150

row_label: row 5 D-Asp-dimethylester

substrate: D-aspartate dimethylester


substrate_name: pseudooxynicotine

proof_lines: kcat is 0.790 sec(-1) (at 30 degrees Celsius).

substrate: pseudooxynicotine


substrate_name: H2O; D-Aspartate; O2

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

substrate: H2O; D-Aspartate; O2


substrate_name: D-aspartate using GHS-tagged enzyme (at 37 degrees Celsius and at pH 8.3)


substrate_name: Unknown

substrate: Unknown


substrate_name: N-methyl-D-Asp

proof_lines: pH 7.0, 20°C, recombinant wild-type enzyme

substrate: N-methyl-D-Asp


substrate_name: D,L-cysteic acid (at 25 degrees Celsius and at pH 7.4)

proof_lines: kcat is 4.7 sec(-1) with D-aspartate as substrate (at 25 degrees Celsius and at pH 7) (PubMed:7915543). kcat is 11.1 sec(-1) with D-aspartate as substrate (at 4 degrees Celsius and at pH 7.4) (PubMed:2901415). kcat is 43.5 sec(-1) with D-as


substrate_name: D-Aspartate; H2O; O2

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

source_databases_merged: sabio_rk brenda uniprot

substrate: D-Aspartate; H2O; O2


substrate_name: D-Aspartate; O2; H2O

substrate: D-Aspartate; O2; H2O


substrate_name: N-methyl-D-asparagine

assay_conditions_summary: pH 8.3; 310.15 K; buffer 40 mM sodium diphosphate

proof_lines: recombinant F18Ep protein, in 40 mM sodium diphosphate buffer (pH 8.3), at 37°C

substrate: N-methyl-D-asparagine


substrate_name: O2; H2O; D-Aspartate

substrate: O2; H2O; D-Aspartate


substrate_name: D-Asn

sequence_variant_note: Resolved canonical sequence from uniprot_reviewed_accession:Q75WF1 and applied mutation signature H56N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor FAD

column_label: Table I; H56N block; D-Asn row; columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1); kcat/Km normalized by dividing by 1000.

normalized_value_unit_evidence: kcat paper=3.9 s^-1; km paper=83.4 mM; kcat/Km paper=0.047 s^-1*mM^-1.

row_label: H56N / D-Asn

table_label: Table I | Apparent kinetic parameters of the wild-type, H56A and H56N mutants of ChDDO

substrate: D-Asn


substrate_name: D-Asp

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

column_label: Table I; wild type block; D-Asp row; columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1); kcat/Km normalized by dividing by 1000.

normalized_value_unit_evidence: kcat paper=74.5 s^-1; km paper=2.5 mM; kcat/Km paper=29.8 s^-1*mM^-1.

raw_value_unit_evidence: Table I wild type D-Asp: kcat 74.5 s^-1; Km 2.5 +/- 0.3 mM; kcat/Km 29,800 s^-1 M^-1.

row_label: wild type / D-Asp

substrate: D-Asp


substrate_name: D-Gln

sequence_variant_note: Resolved canonical sequence from uniprot_reviewed_accession:Q75WF1 and applied mutation signature H56A to reconstruct the assayed variant sequence.

column_label: Table I; H56A block; D-Gln row; columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1); kcat/Km normalized by dividing by 1000.

normalized_value_unit_evidence: kcat paper=2.2 s^-1; km paper=39.4 mM; kcat/Km paper=0.055 s^-1*mM^-1.

row_label: H56A / D-Gln

substrate: D-Gln


column_label: Table I; H56N block; D-Gln row; columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1); kcat/Km normalized by dividing by 1000.

normalized_value_unit_evidence: kcat paper=4.5 s^-1; km paper=21.0 mM; kcat/Km paper=0.213 s^-1*mM^-1.

row_label: H56N / D-Gln


substrate_name: D-Glu

column_label: Table I; wild type block; D-Glu row; columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1); kcat/Km normalized by dividing by 1000.

normalized_value_unit_evidence: kcat paper=2.6 s^-1; km paper=106 mM; kcat/Km paper=0.024 s^-1*mM^-1.

raw_value_unit_evidence: Table I wild type D-Glu: kcat 2.6 s^-1; Km 106 +/- 9.4 mM; kcat/Km 24 s^-1 M^-1.

row_label: wild type / D-Glu

substrate: D-Glu


substrate_name: D-Leu

column_label: Table I; H56N block; D-Leu row; columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1); kcat/Km normalized by dividing by 1000.

normalized_value_unit_evidence: kcat paper=0.7 s^-1; km paper=8.8 mM; kcat/Km paper=0.074 s^-1*mM^-1.

row_label: H56N / D-Leu

substrate: D-Leu


substrate_name: D-Met

column_label: Table I; H56A block; D-Met row; columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1); kcat/Km normalized by dividing by 1000.

normalized_value_unit_evidence: kcat paper=11.5 s^-1; km paper=8.5 mM; kcat/Km paper=1.35 s^-1*mM^-1.

row_label: H56A / D-Met

substrate: D-Met


column_label: Table I; H56N block; D-Met row; columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1); kcat/Km normalized by dividing by 1000.

normalized_value_unit_evidence: kcat paper=4.0 s^-1; km paper=31.8 mM; kcat/Km paper=0.125 s^-1*mM^-1.

row_label: H56N / D-Met


substrate_name: D-Phe

column_label: Table I; H56A block; D-Phe row; columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1); kcat/Km normalized by dividing by 1000.

normalized_value_unit_evidence: kcat paper=3.1 s^-1; km paper=14.3 mM; kcat/Km paper=0.218 s^-1*mM^-1.

row_label: H56A / D-Phe

substrate: D-Phe


column_label: Table I; H56N block; D-Phe row; columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1); kcat/Km normalized by dividing by 1000.

normalized_value_unit_evidence: kcat paper=4.1 s^-1; km paper=34.8 mM; kcat/Km paper=0.119 s^-1*mM^-1.

row_label: H56N / D-Phe


enzyme_display_name: putrescine oxidase

organism: Kocuria rosea

substrate_name: spermidine

smiles: C(CCNCCCN)CN

enzyme: putrescine oxidase

substrate: spermidine


enzyme_display_name: UniProt B0F9F6

organism: Rhodococcus erythropolis

enzyme: UniProt B0F9F6


substrate_name: putrescine

smiles: C(CCN)CN

proof_lines:
Raw SKiD Env: Temp=25°C, pH=9
Raw SKiD Env: Temp=25°C, pH=8.3
Raw SKiD Env: Temp=25°C, pH=8

substrate: putrescine


smiles: C(CN)C(CN)O


substrate_name: cadaverine

smiles: C(CCN)CCN

substrate: cadaverine


substrate_name: spermine

smiles: C(CCNCCCN)CNCCCN

substrate: spermine


substrate_name: L-ornithine

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

substrate: L-ornithine


enzyme_display_name: L-lysine oxidase

organism: Trichoderma viride

substrate_name: L-arginine

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

enzyme: L-lysine oxidase

substrate: L-arginine


enzyme_display_name: UniProt A0A0G4DCU0

substrate_name: L-lysine

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

proof_lines:
Raw SKiD Env: Temp=50°C, pH=4
Raw SKiD Env: Temp=50°C, pH=7.4

enzyme: UniProt A0A0G4DCU0

substrate: L-lysine


organism: Rattus norvegicus

substrate_name: D-aspartate (at 37 degrees Celsius and at pH 8.3)

proof_lines: kcat is 31.1 sec(-1) with D-aspartate as substrate (at 37 degrees Celsius and at pH 8.3).


enzyme_display_name: glutamate dehydrogenase (NADP+)

organism: Trichurus sp.

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

smiles: N

enzyme: glutamate dehydrogenase (NADP+)


organism: Caenorhabditis elegans

substrate_name: D-Aspartate

substrate: D-Aspartate


substrate_name: D-Glutamate

substrate: D-Glutamate


substrate_name: N-Methyl-D-aspartic acid

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

substrate: N-Methyl-D-aspartic acid


enzyme_display_name: D-aspartate oxidase 1

substrate_name: N-methyl D-aspartate

assay_conditions_summary: pH 8.3; buffer pH 8; cofactor FAD

column_label: Table 2. Kinetic parameters of purified recombinant Y69Ap, C47Ap, and F18Ep; row C47Ap / NMDA; column(s) Km (mM)

raw_value_unit_evidence: Km raw_value=0.84 raw_unit=mM

row_label: C47Ap / NMDA

enzyme: D-aspartate oxidase 1

substrate: N-methyl D-aspartate


enzyme_display_name: D-aspartate oxidase 2

column_label: Table 2. Kinetic parameters of purified recombinant Y69Ap, C47Ap, and F18Ep; row F18Ep / NMDA; column(s) Km (mM)

raw_value_unit_evidence: Km raw_value=1.84 raw_unit=mM

row_label: F18Ep / NMDA

enzyme: D-aspartate oxidase 2


enzyme_display_name: phenylalanine dehydrogenase

organism: Lysinibacillus sphaericus

substrate_name: L-Norvaline

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.

assay_conditions_summary: pH 10.4; 298.15 K; cofactor NAD+

column_label: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs, row L-norvaline / N145V, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.18, 1.9, and 11.

raw_value_unit_evidence: Table 4: Kinetic Parameters for Aliphatic Amino Acids in B. sphaericus PheDHs row L-norvaline / N145V: Km = 0.18 mM; kcat = 1.9 s^-1; kcat/Km = 11 s^-1 mM^-1.

row_label: L-norvaline / N145V

enzyme: phenylalanine dehydrogenase

substrate: L-Norvaline


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N142V/N145V to reconstruct the assayed variant sequence.

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_name: L-Phenylalanine

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

column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates, row L-phenylalanine / N145A, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.042, 34, and 809.

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 L-phenylalanine / N145A: Km = 0.042 mM; kcat = 34 s^-1; kcat/Km = 809 s^-1 mM^-1.

row_label: L-phenylalanine / N145A

substrate: L-Phenylalanine


sequence_variant_note: Resolved canonical sequence from uniprotkb:P23307 and applied mutation signature N145I to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates, row L-phenylalanine / N145I, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.014, 13, and 929.

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 L-phenylalanine / N145I: Km = 0.014 mM; kcat = 13 s^-1; kcat/Km = 929 s^-1 mM^-1.

row_label: L-phenylalanine / N145I


sequence_variant_note: Resolved canonical sequence from uniprotkb:P23307 and applied mutation signature N145L to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates, row L-phenylalanine / N145L, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.032, 8.5, and 266.

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 L-phenylalanine / N145L: Km = 0.032 mM; kcat = 8.5 s^-1; kcat/Km = 266 s^-1 mM^-1.

row_label: L-phenylalanine / N145L


sequence_variant_note: Resolved canonical sequence from uniprotkb:P23307 and applied mutation signature N145V to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates, row L-phenylalanine / N145V, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.021, 17, and 810.

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 L-phenylalanine / N145V: Km = 0.021 mM; kcat = 17 s^-1; kcat/Km = 810 s^-1 mM^-1.

row_label: L-phenylalanine / N145V


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N142V/N145V/G193K/K194G to reconstruct the assayed variant sequence.

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

normalized_value_unit_evidence: normalized: Km=1.1 mM; kcat=68 s^-1; kcat/Km=62 s^-1 mM^-1

row_label: Lysinibacillus sphaericus / wt / L-Phenylalanine


substrate_name: L-Tyrosine

column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates, row L-tyrosine / N145A, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 2.0, 31, and 15.

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 L-tyrosine / N145A: Km = 2.0 mM; kcat = 31 s^-1; kcat/Km = 15 s^-1 mM^-1.

row_label: L-tyrosine / N145A

substrate: L-Tyrosine


column_label: Table 2: Kinetic Parameters of Wild-Type and Mutant B. sphaericus and Wild-Type B. badius PheDH Enzymes for Aromatic Substrates, row L-tyrosine / N145I, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 1.3, 21, and 16.

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 L-tyrosine / N145I: Km = 1.3 mM; kcat = 21 s^-1; kcat/Km = 16 s^-1 mM^-1.

row_label: L-tyrosine / 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 L-tyrosine / N145L, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1), cells 0.69, 9.4, and 14.

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 L-tyrosine / N145L: Km = 0.69 mM; kcat = 9.4 s^-1; kcat/Km = 14 s^-1 mM^-1.

row_label: L-tyrosine / N145L


enzyme_display_name: cyclohexylamine oxidase

organism: Erythrobacteraceae bacterium

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

enzyme: cyclohexylamine oxidase


organism: Trichoderma pseudokoningii


substrate_name: L-phenylalanine

substrate: L-phenylalanine


organism: Aspergillus nidulans


enzyme_display_name: L-glutamate oxidase

organism: Streptomyces hygroscopicus subsp. hygroscopicus

substrate_name: L-glutamate

enzyme: L-glutamate oxidase

substrate: L-glutamate


smiles: O=O


organism: Bos taurus


substrate_name: spermidine


substrate_name: Unknown

substrate: Unknown


organism: Microbacterium oxydans


substrate_name: cyclooctanamine

substrate: cyclooctanamine


substrate_name: Cyclohexylamine

substrate: Cyclohexylamine


organism: Pseudomonas putida

substrate_name: putrescine

substrate: putrescine


organism: Streptomyces violascens

assay_conditions_summary: pH 5


substrate_name: L-His

substrate: L-His


substrate_name: L-Gln

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

substrate: L-Gln


organism: Pseudomonas sp.


organism: Trichoderma reesei


organism: Meyerozyma guilliermondii


substrate: spermidine


substrate_name: cadaverine

substrate: cadaverine


organism: Trichoderma aureoviride

substrate_name: L-lysine

proof_lines:
at pH 7.5 and 37°C
at pH and ?C

substrate: L-lysine


organism: Arthrobacter sp. TYUT010-15


organism: Rhodococcus erythropolis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P15I/A394C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme P15I/A394C, at pH 8.3 and 25°C


sequence_variant_note: Mutation signature A394C/A396T/Q431G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme A394C/A396T/Q431G, at pH 8.3 and 25°C


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


assay_conditions_summary: pH 8.3; buffer 50 mM Tris-HCl

proof_lines: wild type enzyme, in 50 mM Tris-HCl buffer, pH 9.0, at 25°C

proof_lines: wild type enzyme, in 50 mM Tris-HCl buffer, pH 8.0, at 25°C


organism: Scomber japonicus


organism: Trichoderma viride

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0J9X1X3 and applied mutation signature D212A/D315A to reconstruct the assayed variant sequence.

column_label: Table 2 columns read for the row 'LysOX D212A/D315A'; column 'Specific activity (U/mg)' = 6.4; column 'Km (mM)' = 7.6; column 'kcat (s-1)' = 17.0; column 'kcat/Km' = 2.2.

normalized_value_unit_evidence: Km: printed Table 2 cell 7.6 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 7.6 mM. kcat: printed Table 2 cell 17.0 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 17.0 s^(-1). kcat/Km: the printed Table 2 cell 2.2 s^-1 mM^-1 is the paper's rounded rendering of the same row's own quotient 17.0 / 7.6 = 2.236842105263158 s^-1 mM^-1, and that full-precision quotient is the exported value; the printed cell is carried as its rounded corroboration.

raw_value_unit_evidence: Table 2, row 'LysOX D212A/D315A': Km = 7.6 mM; kcat = 17.0 s^-1; printed kcat/Km = 2.2 s^-1 mM^-1.

row_label: Table 2, row LysOX D212A/D315A

table_label: Table 2: Kinetic parameters of LysOX and LysOX mutant variants for L-lysine (Protein Science 2020, 29:2213-2225)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0J9X1X3 and applied mutation signature D315A to reconstruct the assayed variant sequence.

column_label: Table 2 columns read for the row 'LysOX D315A'; column 'Specific activity (U/mg)' = 22.2; column 'Km (mM)' = 0.28; column 'kcat (s-1)' = 24.3; column 'kcat/Km' = 87.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.28 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 0.28 mM. kcat: printed Table 2 cell 24.3 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 24.3 s^(-1). kcat/Km: the printed Table 2 cell 87 s^-1 mM^-1 is the paper's rounded rendering of the same row's own quotient 24.3 / 0.28 = 86.78571428571428 s^-1 mM^-1, and that full-precision quotient is the exported value; the printed cell is carried as its rounded corroboration.

raw_value_unit_evidence: Table 2, row 'LysOX D315A': Km = 0.28 mM; kcat = 24.3 s^-1; printed kcat/Km = 87 s^-1 mM^-1.

row_label: Table 2, row LysOX D315A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0J9X1X3 and applied mutation signature D212A to reconstruct the assayed variant sequence.

column_label: Table 2 columns read for the row 'LysOX D212A'; column 'Specific activity (U/mg)' = 18.5; column 'Km (mM)' = 0.56; column 'kcat (s-1)' = 26.4; column 'kcat/Km' = 47.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.56 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 0.56 mM. kcat: printed Table 2 cell 26.4 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 26.4 s^(-1). kcat/Km: the printed Table 2 cell 47 s^-1 mM^-1 is the paper's rounded rendering of the same row's own quotient 26.4 / 0.56 = 47.14285714285714 s^-1 mM^-1, and that full-precision quotient is the exported value; the printed cell is carried as its rounded corroboration.

raw_value_unit_evidence: Table 2, row 'LysOX D212A': Km = 0.56 mM; kcat = 26.4 s^-1; printed kcat/Km = 47 s^-1 mM^-1.

row_label: Table 2, row LysOX D212A


organism: Acinetobacter sp. YT-02

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


enzyme_display_name: D-glutamate(D-aspartate) oxidase

organism: Aspergillus ustus

substrate_name: D-glutamate

enzyme: D-glutamate(D-aspartate) oxidase

substrate: D-glutamate


enzyme_display_name: L-aspartate oxidase

organism: Bacillus subtilis (strain 168)

substrate_name: L-aspartate (for L-aspartate:oxygen oxidoreductase activity)

proof_lines: kcat is 0.18 sec(-1) for L-aspartate:oxygen oxidoreductase activity. kcat is 15.4 sec(-1) for fumarate reductase activity. kcat is 0.50 sec(-1) for L-aspartate:fumarate oxidoreductase activity.

enzyme: L-aspartate oxidase


substrate_name: fumarate (for fumarate reductase activity)


substrate_name: L-ornithine

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tris-HCl

column_label: Table 1 Steady-state kinetic parameters of PuORh at pH 8.0. Substrate row 'L-Ornithine'; column 'kcat (s-1)' = 0.0198; column 'Km (uM)' = 330; column 'kcat / Km (s-1 mM-1)' = 0.06.

normalized_value_unit_evidence: kcat: printed cell 0.0198 s-1 -> 0.0198 s^(-1); the exported value is 0.0198. Km: printed cell 330 uM -> 0.33 mM; the exported value is 0.33. kcat/Km: printed cell 0.06 s-1 mM-1 -> 0.06 s^(-1)*mM^(-1); the exported value is 0.060000000000000005.

raw_value_unit_evidence: Table 1, decoded plain-numeral transcription (journal page 460), substrate row 'L-Ornithine': kcat = 0.0198 s-1; Km = 330 uM; printed kcat / Km = 0.06 s-1 mM-1.

substrate: L-ornithine


substrate_name: spermine

assay_conditions_summary: pH 8; buffer 50 mM Tris-HCl

substrate: spermine


column_label: Table 1 Steady-state kinetic parameters of PuORh at pH 8.0. Substrate row 'Spermidine'; column 'kcat (s-1)' = 1.4; column 'Km (uM)' = 100; column 'kcat / Km (s-1 mM-1)' = 14.

normalized_value_unit_evidence: kcat: printed cell 1.4 s-1 -> 1.4 s^(-1); the exported value is 1.4. Km: printed cell 100 uM -> 0.1 mM; the exported value is 0.1. kcat/Km: printed cell 14 s-1 mM-1 -> 14.0 s^(-1)*mM^(-1); the exported value is 13.999999999999998.

raw_value_unit_evidence: Table 1, decoded plain-numeral transcription (journal page 460), substrate row 'Spermidine': kcat = 1.4 s-1; Km = 100 uM; printed kcat / Km = 14 s-1 mM-1.


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

assay_conditions_summary: pH 9; buffer 50 mM Tris-HCl

proof_lines: mutant enzyme E324L, in 50 mM Tris-HCl buffer, pH 9.0, at 25°C


proof_lines: mutant enzyme E324A, in 50 mM Tris-HCl buffer, pH 9.0, at 25°C


organism: Escherichia coli (strain K12)

substrate_name: N-acetyl-L-aspartate

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

proof_lines: kcat is 29.4 min(-1) for L-aspartate oxidase activity with oxygen as electron acceptor. kcat is 16.0 min(-1) for reduced benzyl viologen:fumarate oxidoreductase activity (PubMed:11294641). kcat is 40.0 min(-1) with L-aspartate as substrate.

substrate: N-acetyl-L-aspartate


substrate_name: N-formyl-L-aspartate

substrate: N-formyl-L-aspartate


organism: Streptomyces mobaraensis

substrate_name: L-glutamate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S280T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H533L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S280T/H533L to reconstruct the assayed variant sequence.


substrate_name: L-aspartate (at substrate concentrations between 0.25 and 1.25 mM)

assay_conditions_summary: cofactor FAD


substrate_name: FAD

substrate: FAD


organism: Streptomyces sp.

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


enzyme_display_name: Lysyl oxidase homolog 2

organism: Homo sapiens

proof_lines: kcat is 2.04 min(-1) with tropoelastin as substrate (without the first three SRCR domains). kcat is 0.62 min(-1) with tropoelastin as substrate (without all four SRCR domains).

enzyme: Lysyl oxidase homolog 2


proof_lines: pH 8.0, 25°C, self-assembled enzyme PutOx-AuBP bound to gold nanoparticles


organism: Streptomyces diastatochromogenes

proof_lines: proteinase K treated enzyme, at pH 8.0 and 30°C


organism: Sulfurisphaera tokodaii

substrate_name: L-aspartate

proof_lines:
pH 8, 37°C
apparent value, at pH 8.0 and 37°C
recombinant enzyme, at 37°C

source_databases_merged: brenda skid uniprot

substrate: L-aspartate


substrate_name: L-asparagine

proof_lines:
apparent value, at pH 8.0 and 37°C
Raw SKiD Env: Temp=37°C, pH=8

substrate: L-asparagine


organism: Kocuria rosea

substrate_name: putrescine

proof_lines: enzyme immobilized by cross-linking on screen-printed carbon electrodes containing tetrathiafulvalene as mediator, pH not specified in the publication, at 20°C

proof_lines: free enzyme, pH not specified in the publication, at 20°C


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: L-amino-acid oxidase 4

organism: Hebeloma cylindrosporum

enzyme: L-amino-acid oxidase 4


enzyme_display_name: L-glutamate oxidase precursor

enzyme: L-glutamate oxidase precursor


substrate_name: tropoelastin (without the first three SRCR domains)


enzyme_display_name: Lysyl oxidase homolog 3

proof_lines: kcat is 0.058 sec(-1) with STAT3 acetylated at 'Lys-685' (for deacetylation activity). kcat is 0.022 sec(-1) with STAT3 acetylated at 'Lys-685' (for lysine 6-oxidase activity).

enzyme: Lysyl oxidase homolog 3


substrate_name: semicarbazide

smiles: C(=O)(N)NN

substrate: semicarbazide