column_label: Table 2  Steady-state kinetic constants for MCS activities of the wild type and mutant GST-MCS enzymes; enzyme-form block 'Wild type'; column 'Malonate'; metric line 'Km (uM)' = 208 +/- 6; metric line 'kcat (s^-1)' = 19 +/- 0.3; metric line 'kcat/Km (mM^-1 . s^-1)' = 91.

normalized_value_unit_evidence: kcat: paper cell 19 +/- 0.3 s^-1 -> 19.0 s^(-1) (no conversion); catalog holds 19.0 s^(-1). Km: paper cell 208 +/- 6 uM / 1000 = 0.208 mM; catalog holds 0.208 mM. kcat/Km: catalog 91.34615384615385 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells; the printed rounded cell 91 mM^-1 . s^-1 is documented in prose.

raw_value_unit_evidence: Table 2, Wild type block, Malonate column: Km (uM) = 208 +/- 6; kcat (s^-1) = 19 +/- 0.3; kcat/Km (mM^-1 . s^-1) = 91 (rounded printed cell).

row_label: Table 2, enzyme-form block 'Wild type', column 'Malonate'


enzyme_display_name: indoleacetate--CoA ligase

organism: Aromatoleum aromaticum

substrate_name: phenyl acetate

source_db: brenda

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

proof_lines: pH and temperature not specified in the publication

data_origin: experimental

enzyme: indoleacetate--CoA ligase

substrate: phenyl acetate

source: brenda


substrate_name: 2-naphthyl acetate

substrate: 2-naphthyl acetate


enzyme_display_name: thioglycine synthase

organism: Methanocaldococcus jannaschii

substrate_name: GGRLGFYGYDLQD

verification_status: verified

kcat_over_km_display: Not reported

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

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

column_label: Full text reports MjYcaO had KM 59.9 uM and kcat 5.3 x 10^-2 s^-1 for the 11-mer peptide substrate in Figure 2b.

normalized_value_unit_evidence: kcat normalized_value=0.053 normalized_unit=s^-1; Km normalized_value=0.0599 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=5.3 x 10^-2 s^-1 raw_unit=s^-1; Km raw_value=59.9 uM raw_unit=uM

row_label: MjYcaO thioamidation reaction / 11-mer peptide substrate

table_label: PMC full text Figure 2b kinetic prose PMID 31139720

enzyme: thioglycine synthase

substrate: GGRLGFYGYDLQD

status: verified


organism: Escherichia coli (strain K12)

substrate_name: D-pantetheine (at pH 7.8 and 25 degrees Celsius)

source_db: uniprot

kcat_display: Not reported

smiles: CC(C)(CO)C(C(=O)NCCC(=O)NCCS)O

assay_conditions_summary: pH 7.8; cofactor ATP

proof_lines: kcat is 0.3 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with 3-hydroxybenzoate as substrate (at pH 7.8 and 25 degrees Celsius). kcat is 0.8 sec(-1) for 2,3-dihydroxybenzoate-AMP ligase activity with salicylate as substrate (at pH

source: uniprot


organism: Escherichia coli

source_db: oed

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature N235A to reconstruct the assayed variant sequence.

mutation_type: substitution

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row N235A, substrate column DHB (the variant label prints its footnote letter e); column kcat (min-1) = 1.0; column Km (uM) = 5.2; column kcat/Km (mM-1 min-1) = 188; column specificity = 0.14; column specificity switch = 0.5.

normalized_value_unit_evidence: Km: printed cell 5.2 uM; 1 uM is 1/1000 mM, so 5.2 / 1000 = 0.0052 mM. kcat: printed cell 1.0 min^-1; the printed turnover column is per minute, so 1.0 / 60 = 0.016666666666666666 s^(-1). kcat/Km: printed cell 188 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 188 / 60 = 3.1333333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row N235A, substrate column DHB (the variant label prints its footnote letter e): kcat = 1.0 min^-1; Km = 5.2 uM; kcat/Km = 188 under the printed column head kcat/Km (mM-1 min-1).

status: corrected

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature N340C to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row N340C, substrate column DHB; column kcat (min-1) = 0.97; column Km (uM) = 2.7; column kcat/Km (mM-1 min-1) = 365; column specificity = 2; column specificity switch = 8.

normalized_value_unit_evidence: Km: printed cell 2.7 uM; 1 uM is 1/1000 mM, so 2.7 / 1000 = 0.0027 mM. kcat: printed cell 0.97 min^-1; the printed turnover column is per minute, so 0.97 / 60 = 0.016166666666666666 s^(-1). kcat/Km: printed cell 365 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 365 / 60 = 6.083333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row N340C, substrate column DHB: kcat = 0.97 min^-1; Km = 2.7 uM; kcat/Km = 365 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature S240C to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row S240C, substrate column DHB (the variant label prints its footnote letter d); column kcat (min-1) = 10; column Km (uM) = 364; column kcat/Km (mM-1 min-1) = 28; column specificity = 8; column specificity switch = 26.

normalized_value_unit_evidence: Km: printed cell 364 uM; 1 uM is 1/1000 mM, so 364 / 1000 = 0.364 mM. kcat: printed cell 10 min^-1; the printed turnover column is per minute, so 10 / 60 = 0.16666666666666666 s^(-1). kcat/Km: printed cell 28 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 28 / 60 = 0.4666666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row S240C, substrate column DHB (the variant label prints its footnote letter d): kcat = 10 min^-1; Km = 364 uM; kcat/Km = 28 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature V339I to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row V339I, substrate column DHB; column kcat (min-1) = 1.8; column Km (uM) = 6.1; column kcat/Km (mM-1 min-1) = 298; column specificity = 5; column specificity switch = 18.

normalized_value_unit_evidence: Km: printed cell 6.1 uM; 1 uM is 1/1000 mM, so 6.1 / 1000 = 0.0061 mM. kcat: printed cell 1.8 min^-1; the printed turnover column is per minute, so 1.8 / 60 = 0.03 s^(-1). kcat/Km: printed cell 298 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 298 / 60 = 4.966666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row V339I, substrate column DHB: kcat = 1.8 min^-1; Km = 6.1 uM; kcat/Km = 298 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature V339L to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row V339L, substrate column DHB; column kcat (min-1) = 1.5; column Km (uM) = 4.9; column kcat/Km (mM-1 min-1) = 318; column specificity = 4; column specificity switch = 12.

normalized_value_unit_evidence: Km: printed cell 4.9 uM; 1 uM is 1/1000 mM, so 4.9 / 1000 = 0.0049 mM. kcat: printed cell 1.5 min^-1; the printed turnover column is per minute, so 1.5 / 60 = 0.025 s^(-1). kcat/Km: printed cell 318 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 318 / 60 = 5.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row V339L, substrate column DHB: kcat = 1.5 min^-1; Km = 4.9 uM; kcat/Km = 318 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature Y236F to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row Y236F, substrate column DHB; column kcat (min-1) = 1.6; column Km (uM) = 7.1; column kcat/Km (mM-1 min-1) = 218; column specificity = 5; column specificity switch = 17.

normalized_value_unit_evidence: Km: printed cell 7.1 uM; 1 uM is 1/1000 mM, so 7.1 / 1000 = 0.0071 mM. kcat: printed cell 1.6 min^-1; the printed turnover column is per minute, so 1.6 / 60 = 0.02666666666666667 s^(-1). kcat/Km: printed cell 218 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 218 / 60 = 3.6333333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row Y236F, substrate column DHB: kcat = 1.6 min^-1; Km = 7.1 uM; kcat/Km = 218 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y236F/S240C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature Y236F/S240C/N340C to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row Y236F/S240C/N340C, substrate column DHB; column kcat (min-1) = 8.0; column Km (uM) = 318; column kcat/Km (mM-1 min-1) = 25; column specificity = 7; column specificity switch = 23.

normalized_value_unit_evidence: Km: printed cell 318 uM; 1 uM is 1/1000 mM, so 318 / 1000 = 0.318 mM. kcat: printed cell 8.0 min^-1; the printed turnover column is per minute, so 8.0 / 60 = 0.13333333333333333 s^(-1). kcat/Km: printed cell 25 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 25 / 60 = 0.4166666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row Y236F/S240C/N340C, substrate column DHB: kcat = 8.0 min^-1; Km = 318 uM; kcat/Km = 25 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature Y236F/S240C/V339I/N340C to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row Y236F/S240C/V339I/N340C, substrate column DHB; column kcat (min-1) = 8.8; column Km (uM) = 417; column kcat/Km (mM-1 min-1) = 21; column specificity = 14; column specificity switch = 45.

normalized_value_unit_evidence: Km: printed cell 417 uM; 1 uM is 1/1000 mM, so 417 / 1000 = 0.417 mM. kcat: printed cell 8.8 min^-1; the printed turnover column is per minute, so 8.8 / 60 = 0.14666666666666667 s^(-1). kcat/Km: printed cell 21 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 21 / 60 = 0.35 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row Y236F/S240C/V339I/N340C, substrate column DHB: kcat = 8.8 min^-1; Km = 417 uM; kcat/Km = 21 under the printed column head kcat/Km (mM-1 min-1).


substrate_name: salicylate

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row N235A, substrate column Sal (the variant label prints its footnote letter e); column kcat (min-1) = 2.2; column Km (uM) = 80; column kcat/Km (mM-1 min-1) = 27; this substrate line prints no specificity or specificity-switch cell.

normalized_value_unit_evidence: Km: printed cell 80 uM; 1 uM is 1/1000 mM, so 80 / 1000 = 0.08 mM. kcat: printed cell 2.2 min^-1; the printed turnover column is per minute, so 2.2 / 60 = 0.03666666666666667 s^(-1). kcat/Km: printed cell 27 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 27 / 60 = 0.45 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row N235A, substrate column Sal (the variant label prints its footnote letter e): kcat = 2.2 min^-1; Km = 80 uM; kcat/Km = 27 under the printed column head kcat/Km (mM-1 min-1).

substrate: salicylate


substrate_name: holo-EntB (at pH 8.8 and 37 degrees Celsius)


enzyme_display_name: malonate--CoA ligase

organism: Arabidopsis thaliana

substrate_name: Unknown

km_display: Not reported

enzyme: malonate--CoA ligase

substrate: Unknown


organism: Bradyrhizobium japonicum

ki_unit: mM


column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row N340C, substrate column Sal; column kcat (min-1) = 7.8; column Km (uM) = 8.9; column kcat/Km (mM-1 min-1) = 879; this substrate line prints no specificity or specificity-switch cell.

normalized_value_unit_evidence: Km: printed cell 8.9 uM; 1 uM is 1/1000 mM, so 8.9 / 1000 = 0.0089 mM. kcat: printed cell 7.8 min^-1; the printed turnover column is per minute, so 7.8 / 60 = 0.13 s^(-1). kcat/Km: printed cell 879 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 879 / 60 = 14.65 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row N340C, substrate column Sal: kcat = 7.8 min^-1; Km = 8.9 uM; kcat/Km = 879 under the printed column head kcat/Km (mM-1 min-1).


column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row S240C, substrate column Sal (the variant label prints its footnote letter d); column kcat (min-1) = 12; column Km (uM) = 54; column kcat/Km (mM-1 min-1) = 226; this substrate line prints no specificity or specificity-switch cell.

normalized_value_unit_evidence: Km: printed cell 54 uM; 1 uM is 1/1000 mM, so 54 / 1000 = 0.054 mM. kcat: printed cell 12 min^-1; the printed turnover column is per minute, so 12 / 60 = 0.2 s^(-1). kcat/Km: printed cell 226 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 226 / 60 = 3.7666666666666666 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row S240C, substrate column Sal (the variant label prints its footnote letter d): kcat = 12 min^-1; Km = 54 uM; kcat/Km = 226 under the printed column head kcat/Km (mM-1 min-1).


column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row V339I, substrate column Sal; column kcat (min-1) = 8.9; column Km (uM) = 5.5; column kcat/Km (mM-1 min-1) = 1616; this substrate line prints no specificity or specificity-switch cell.

normalized_value_unit_evidence: Km: printed cell 5.5 uM; 1 uM is 1/1000 mM, so 5.5 / 1000 = 0.0055 mM. kcat: printed cell 8.9 min^-1; the printed turnover column is per minute, so 8.9 / 60 = 0.14833333333333334 s^(-1). kcat/Km: printed cell 1616 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 1616 / 60 = 26.933333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row V339I, substrate column Sal: kcat = 8.9 min^-1; Km = 5.5 uM; kcat/Km = 1616 under the printed column head kcat/Km (mM-1 min-1).


column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row V339L, substrate column Sal; column kcat (min-1) = 9.3; column Km (uM) = 8.0; column kcat/Km (mM-1 min-1) = 1170; this substrate line prints no specificity or specificity-switch cell.

normalized_value_unit_evidence: Km: printed cell 8.0 uM; 1 uM is 1/1000 mM, so 8.0 / 1000 = 0.008 mM. kcat: printed cell 9.3 min^-1; the printed turnover column is per minute, so 9.3 / 60 = 0.155 s^(-1). kcat/Km: printed cell 1170 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 1170 / 60 = 19.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row V339L, substrate column Sal: kcat = 9.3 min^-1; Km = 8.0 uM; kcat/Km = 1170 under the printed column head kcat/Km (mM-1 min-1).


column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row Y236F, substrate column Sal; column kcat (min-1) = 6.9; column Km (uM) = 6.1; column kcat/Km (mM-1 min-1) = 1139; this substrate line prints no specificity or specificity-switch cell.

normalized_value_unit_evidence: Km: printed cell 6.1 uM; 1 uM is 1/1000 mM, so 6.1 / 1000 = 0.0061 mM. kcat: printed cell 6.9 min^-1; the printed turnover column is per minute, so 6.9 / 60 = 0.115 s^(-1). kcat/Km: printed cell 1139 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 1139 / 60 = 18.983333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row Y236F, substrate column Sal: kcat = 6.9 min^-1; Km = 6.1 uM; kcat/Km = 1139 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P10378 and applied mutation signature Y236F/S240C to reconstruct the assayed variant sequence.

column_label: Table 1. Catalytic Parameters of Adenylation Reactions Catalyzed by EntE and EntE Variants, printed column heads variant | substrate | kcat (min-1) | Km (uM) | kcat/Km (mM-1 min-1) | specificity | specificity switch. Table 1, variant row Y236F/S240C, substrate column Sal; column kcat (min-1) = 8.3; column Km (uM) = 39; column kcat/Km (mM-1 min-1) = 216; this substrate line prints no specificity or specificity-switch cell.

normalized_value_unit_evidence: Km: printed cell 39 uM; 1 uM is 1/1000 mM, so 39 / 1000 = 0.039 mM. kcat: printed cell 8.3 min^-1; the printed turnover column is per minute, so 8.3 / 60 = 0.13833333333333334 s^(-1). kcat/Km: printed cell 216 under the column head kcat/Km (mM-1 min-1); 1 mM^-1 min^-1 is (1/60) s^-1 mM^-1, so 216 / 60 = 3.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, variant row Y236F/S240C, substrate column Sal: kcat = 8.3 min^-1; Km = 39 uM; kcat/Km = 216 under the printed column head kcat/Km (mM-1 min-1).


sequence_variant_note: Mutation signature Y236F/S240C/N340C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y236F/S240C/V339I/N340C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature Y236F/S240C/V339L/N340C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Vibrio cholerae


assay_conditions_summary: pH 7.8; 298.15 K; cofactor ATP


substrate_name: ATP

substrate: ATP


assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADH

column_label: Table 1: Kinetic Parameters of EntE1 (decoded plain-numeral transcription of the printed table). Substrate row 'salicylic acid'; column 'Km (uM)' = 70 +/- 4; column 'kcat (s^-1)' = 0.8 +/- 0.1; column 'kcat/Km (M^-1 s^-1)' = 1.1 x 10^4.

normalized_value_unit_evidence: Km: printed Table 1 cell 70 +/- 4 uM; the catalog unit is mM and 1 uM is 0.001 mM, so 70 / 1000 = 0.07 mM; the exported value is 0.028 mM. kcat: printed Table 1 cell 0.8 +/- 0.1 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 0.8 s^(-1). kcat/Km: printed Table 1 cell 1.1 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 11000 x 0.001 = 11 s^-1 mM^-1; the exported value is 28.571428571428573 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, decoded plain-numeral transcription (Biochemistry 2010, volume 49, issue 17, pages 3648-3657), substrate row 'salicylic acid': Km = 70 +/- 4 uM; kcat = 0.8 +/- 0.1 s^-1; printed kcat/Km = 1.1 x 10^4 M^-1 s^-1.

row_label: Table 1, substrate row 'salicylic acid'


column_label: Table 1: Kinetic Parameters of EntE (Biochemistry 2010, 49(17):3648-3657), substrate row '3-hydroxybenzoic acid', wild-type EntE; column 'Km (uM)' = 70; column 'kcat (s-1)' = 0.30; column 'kcat/Km (M-1 s-1)' = 4.6 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.30 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.3 s^(-1); the exported value is 0.3 s^(-1). Km: printed Table 1 cell 70 uM; 70 / 1000 = 0.07 mM; the paper value is 0.07 mM; the exported value is 0.07 mM. kcat/Km: printed Table 1 cell 4.6 x 10^3 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.6 x 10^3 / 1000 = 4.6 s^-1 mM^-1; the paper value is 4.6 s^(-1)*mM^(-1); the exported value is 4.285714285714286 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate row '3-hydroxybenzoic acid', wild-type EntE: Km = 70 uM; kcat = 0.30 s-1; printed kcat/Km = 4.6 x 10^3 M-1 s-1.


organism: Amycolatopsis mediterranei

substrate_name: benzoate

assay_conditions_summary: pH 7.2; cofactor NADPH

substrate: benzoate


assay_conditions_summary: pH 7.2; 303.15 K; cofactor NADPH


verification_status: unverified

assay_conditions_summary: pH 8.4; cofactor ATP

status: unverified


substrate_name: malonate

column_label: Abstract reports Km for malonate was 200 microM.

raw_value_unit_evidence: Km raw_value=200 microM raw_unit=microM

row_label: Rhizobium japonicum malonyl-CoA synthetase / malonate

table_label: PubMed XML abstract PMID 1847615

substrate: malonate


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate_name: hexanoic acid

smiles: CCCCCC(=O)O

assay_conditions_summary: pH 7.8; 298.15 K; buffer that applies to every line of the table; cofactor ATP

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'Hexanoic acid (C6)'; column 'Km (uM)' = 129; column 'kcat (min^-1)' = 0.11; column 'kcat/Km (uM^-1 min^-1)' = 0.0008. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 129 uM; 1 uM is one thousandth of 1 mM, so 129 / 1000 = 0.129 mM; the exported value is 0.129 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 0.11 min^-1; the printed head is per minute, so 0.11 / 60 = 0.0018333333333333333 s^(-1); the proposed kcat is 0.0018333333333333333 s^(-1). kcat/Km: printed Table 2 cell 0.0008 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.0008 times 1000 divided by 60 = 0.013333333333333334 s^(-1)*mM^(-1); the proposed kcat/Km is 0.013333333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'Hexanoic acid (C6)': Km cell = 129 uM; kcat cell = 0.11 min^-1; printed kcat/Km cell = 0.0008 uM^-1 min^-1.

table_label: Table 2: acyl chain length selectivity and kinetic parameters of FadD33 (J. Biol. Chem. 2013, 288(39):28116-28125), PDF page 5 of 10; printed column heads Enzyme/Substrate, Km (uM), kcat (min^-1) and kcat/Km (uM^-1 min^-1)

substrate: hexanoic acid


substrate_name: decanoic acid

smiles: CCCCCCCCCC(=O)O

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'Decanoic acid (C10)'; column 'Km (uM)' = 121; column 'kcat (min^-1)' = 1.5; column 'kcat/Km (uM^-1 min^-1)' = 0.012. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 121 uM; 1 uM is one thousandth of 1 mM, so 121 / 1000 = 0.121 mM; the exported value is 0.121 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 1.5 min^-1; the printed head is per minute, so 1.5 / 60 = 0.025 s^(-1); the proposed kcat is 0.025 s^(-1). kcat/Km: printed Table 2 cell 0.012 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.012 times 1000 divided by 60 = 0.2 s^(-1)*mM^(-1); the proposed kcat/Km is 0.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'Decanoic acid (C10)': Km cell = 121 uM; kcat cell = 1.5 min^-1; printed kcat/Km cell = 0.012 uM^-1 min^-1.

substrate: decanoic acid


substrate_name: lauric acid

smiles: CCCCCCCCCCCC(=O)O

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'Lauric acid (C12)'; column 'Km (uM)' = 21; column 'kcat (min^-1)' = 2.4; column 'kcat/Km (uM^-1 min^-1)' = 0.110. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 21 uM; 1 uM is one thousandth of 1 mM, so 21 / 1000 = 0.021 mM; the exported value is 0.021 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 2.4 min^-1; the printed head is per minute, so 2.4 / 60 = 0.04 s^(-1); the proposed kcat is 0.04 s^(-1). kcat/Km: printed Table 2 cell 0.110 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.110 times 1000 divided by 60 = 1.8333333333333335 s^(-1)*mM^(-1); the proposed kcat/Km is 1.8333333333333335 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'Lauric acid (C12)': Km cell = 21 uM; kcat cell = 2.4 min^-1; printed kcat/Km cell = 0.110 uM^-1 min^-1.

substrate: lauric acid


substrate_name: palmitic acid

smiles: CCCCCCCCCCCCCCCC(=O)O

column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'Palmitic acid (C16)'; column 'Km (uM)' = 1.9; column 'kcat (min^-1)' = 4.2; column 'kcat/Km (uM^-1 min^-1)' = 2.3. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.9 uM; 1 uM is one thousandth of 1 mM, so 1.9 / 1000 = 0.0019 mM; the exported value is 0.0019 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 4.2 min^-1; the printed head is per minute, so 4.2 / 60 = 0.07 s^(-1); the proposed kcat is 0.07 s^(-1). kcat/Km: printed Table 2 cell 2.3 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 2.3 times 1000 divided by 60 = 38.333333333333336 s^(-1)*mM^(-1); the proposed kcat/Km is 38.333333333333336 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'Palmitic acid (C16)': Km cell = 1.9 uM; kcat cell = 4.2 min^-1; printed kcat/Km cell = 2.3 uM^-1 min^-1.

substrate: palmitic acid


column_label: Table 2 (acyl chain length selectivity and kinetic parameters of FadD33), FadD33 wild type block, varied-substrate row 'ATP'; column 'Km (uM)' = 15; column 'kcat (min^-1)' = 1.3; column 'kcat/Km (uM^-1 min^-1)' = 0.085. Table 2 prints no Ki column, no Vmax column and no Kd column.

normalized_value_unit_evidence: Km: printed Table 2 cell 15 uM; 1 uM is one thousandth of 1 mM, so 15 / 1000 = 0.015 mM; the exported value is 0.015 mM and this pass proposes no new Km value. kcat: printed Table 2 cell 1.3 min^-1; the printed head is per minute, so 1.3 / 60 = 0.021666666666666667 s^(-1); the proposed kcat is 0.021666666666666667 s^(-1). kcat/Km: printed Table 2 cell 0.085 uM^-1 min^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.085 times 1000 divided by 60 = 1.416666666666667 s^(-1)*mM^(-1); the proposed kcat/Km is 1.416666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, FadD33 wild type block, varied-substrate row 'ATP': Km cell = 15 uM; kcat cell = 1.3 min^-1; printed kcat/Km cell = 0.085 uM^-1 min^-1.


organism: Pseudomonas fluorescens

substrate_name: L-proline

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

sequence_source: multiple

proof_lines:
pH 7.5, 25°C
Raw SKiD Env: Temp=25°C, pH=7.5

source_databases_merged: brenda skid

substrate: L-proline


organism: Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711)

substrate_name: D-alanine

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

substrate: D-alanine


organism: Rhizobium leguminosarum

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H206L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K170M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R168G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R168G/K170M to reconstruct the assayed variant sequence.


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

assay_conditions_summary: pH 7; 303.15 K; buffer Assay condition: 100 mM potassium phosphate; cofactor ATP

column_label: Table 2  Steady-state kinetic constants for MCS activities of the wild type and mutant GST-MCS enzymes; enzyme-form block 'Wild type'; column 'ATP'; metric line 'Km (uM)' = 52 +/- 4.5; metric line 'kcat (s^-1)' = 20 +/- 0.4; metric line 'kcat/Km (mM^-1 . s^-1)' = 384.

normalized_value_unit_evidence: kcat: paper cell 20 +/- 0.4 s^-1 -> 20.0 s^(-1) (no conversion); catalog holds 20.0 s^(-1). Km: paper cell 52 +/- 4.5 uM / 1000 = 0.052 mM; catalog holds 0.052 mM. kcat/Km: catalog 384.61538461538464 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells; the printed rounded cell 384 mM^-1 . s^-1 is documented in prose.

raw_value_unit_evidence: Table 2, Wild type block, ATP column: Km (uM) = 52 +/- 4.5; kcat (s^-1) = 20 +/- 0.4; kcat/Km (mM^-1 . s^-1) = 384 (rounded printed cell).

row_label: Table 2, enzyme-form block 'Wild type', column 'ATP'


substrate_name: CoA

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA

substrate: CoA


assay_conditions_summary: pH 6.9; cofactor ATP


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


column_label: Table 2  Steady-state kinetic constants for MCS activities of the wild type and mutant GST-MCS enzymes; enzyme-form block 'Wild type'; column 'Malonate'; metric line 'Km (uM)' = 208 +/- 6; metric line 'kcat (s^-1)' = 19 +/- 0.3; metric line 'kcat/Km (mM^-1 . s^-1)' = 91.

normalized_value_unit_evidence: kcat: paper cell 19 +/- 0.3 s^-1 -> 19.0 s^(-1) (no conversion); catalog holds 19.0 s^(-1). Km: paper cell 208 +/- 6 uM / 1000 = 0.208 mM; catalog holds 0.208 mM. kcat/Km: catalog 91.34615384615385 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells; the printed rounded cell 91 mM^-1 . s^-1 is documented in prose.

raw_value_unit_evidence: Table 2, Wild type block, Malonate column: Km (uM) = 208 +/- 6; kcat (s^-1) = 19 +/- 0.3; kcat/Km (mM^-1 . s^-1) = 91 (rounded printed cell).


organism: Aromatoleum aromaticum (strain DSM 19018 / LMG 30748 / EbN1)

substrate_name: indoleacetate

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

proof_lines: kcat is 4.3 sec(-1) with indoleacetate as substrate. kcat is 4.7 sec(-1) with (2-naphthyl)acetate as substrate. kcat is 0.48 sec(-1) with phenylacetate as substrate.

substrate: indoleacetate


substrate_name: phenylacetate

substrate: phenylacetate


substrate_name: ATP (in the presence of 0.6 mM indoleacetate)

assay_conditions_summary: cofactor ATP


substrate_name: CoA (in the presence of 0.6 mM indoleacetate)

assay_conditions_summary: cofactor CoA


organism: Bacillus cereus

substrate_name: L-serine

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

substrate: L-serine


column_label: Table 2. Measured values of Km and kcat for L-serine, ATP, and some alternate substrates of EntF in the ATP-PPi exchange reaction^a Table 2, substrate row 'L-Serine': column 'Km (mM)' = 0.26; column 'kcat (min^-1)' = 760; column 'kcat/Km' = 2,900.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 760 min^-1 (printed column header 'kcat (min^-1)'; the same turnover number is printed again in the Results sentence and in the Abstract for L-serine); 760 / 60 = 12.666666666667 s^(-1). The exported value is 760.0 s^(-1), which is the printed minute-based number carried into a second-based field WITHOUT the 60-fold conversion. Km: the printed Table 2 cell is 0.26 mM, already the export unit; the exported value is 0.26 mM. kcat/Km: the printed Table 2 cell is 2,900 in the column's implied min^-1 mM^-1 (the header prints no unit literal); 2,900 / 60 = 48.333333333333 s^(-1)*mM^(-1); the exported value is 2923.076923076923 s^(-1)*mM^(-1), which is the bare quotient of the export's own unconverted kcat and its Km. The cited Table 2 row prints no fourth numeric column.

row_label: Table 2, substrate row 'L-Serine'


column_label: Table 2. Measured values of Km and kcat for L-serine, ATP, and some alternate substrates of EntF in the ATP-PPi exchange reaction^a Table 2, substrate row 'ATP': column 'Km (mM)' = 0.75; column 'kcat (min^-1)' = 660; column 'kcat/Km' = 880.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 660 min^-1 (printed column header 'kcat (min^-1)'; the same turnover number is printed again in the Results sentence and in the Abstract for L-serine); 660 / 60 = 11 s^(-1). The exported value is 660.0 s^(-1), which is the printed minute-based number carried into a second-based field WITHOUT the 60-fold conversion. Km: the printed Table 2 cell is 0.75 mM, already the export unit; the exported value is 0.75 mM. kcat/Km: the printed Table 2 cell is 880 in the column's implied min^-1 mM^-1 (the header prints no unit literal); 880 / 60 = 14.666666666667 s^(-1)*mM^(-1); the exported value is 880.0 s^(-1)*mM^(-1), which is the bare quotient of the export's own unconverted kcat and its Km. The cited Table 2 row prints no fourth numeric column.

row_label: Table 2, substrate row 'ATP'


substrate_name: O-acetyl-L-serine

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

column_label: Table 2. Measured values of Km and kcat for L-serine, ATP, and some alternate substrates of EntF in the ATP-PPi exchange reaction^a Table 2, substrate row '(O)Ac-L-serine': column 'Km (mM)' = 5.0; column 'kcat (min^-1)' = 720; column 'kcat/Km' = 150.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 720 min^-1 (printed column header 'kcat (min^-1)'; the same turnover number is printed again in the Results sentence and in the Abstract for L-serine); 720 / 60 = 12 s^(-1). The exported value is 720.0 s^(-1), which is the printed minute-based number carried into a second-based field WITHOUT the 60-fold conversion. Km: the printed Table 2 cell is 5.0 mM, already the export unit; the exported value is 5.0 mM. kcat/Km: the printed Table 2 cell is 150 in the column's implied min^-1 mM^-1 (the header prints no unit literal); 150 / 60 = 2.5 s^(-1)*mM^(-1); the exported value is 144.0 s^(-1)*mM^(-1), which is the bare quotient of the export's own unconverted kcat and its Km. The cited Table 2 row prints no fourth numeric column.

row_label: Table 2, substrate row '(O)Ac-L-serine'

substrate: O-acetyl-L-serine


substrate_name: L-beta-chloroalanine

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

column_label: Table 2. Measured values of Km and kcat for L-serine, ATP, and some alternate substrates of EntF in the ATP-PPi exchange reaction^a Table 2, substrate row 'beta-Cl-L-alanine': column 'Km (mM)' = 8.0; column 'kcat (min^-1)' = 870; column 'kcat/Km' = 110.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 870 min^-1 (printed column header 'kcat (min^-1)'; the same turnover number is printed again in the Results sentence and in the Abstract for L-serine); 870 / 60 = 14.5 s^(-1). The exported value is 870.0 s^(-1), which is the printed minute-based number carried into a second-based field WITHOUT the 60-fold conversion. Km: the printed Table 2 cell is 8.0 mM, already the export unit; the exported value is 8.0 mM. kcat/Km: the printed Table 2 cell is 110 in the column's implied min^-1 mM^-1 (the header prints no unit literal); 110 / 60 = 1.833333333333 s^(-1)*mM^(-1); the exported value is 108.75 s^(-1)*mM^(-1), which is the bare quotient of the export's own unconverted kcat and its Km. The cited Table 2 row prints no fourth numeric column.

substrate: L-beta-chloroalanine


substrate_name: S-methyl-L-cysteine

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

column_label: Table 2. Measured values of Km and kcat for L-serine, ATP, and some alternate substrates of EntF in the ATP-PPi exchange reaction^a Table 2, substrate row '(S)methyl-L-cysteine': column 'Km (mM)' = 3.1; column 'kcat (min^-1)' = 38; column 'kcat/Km' = 12.

normalized_value_unit_evidence: kcat: the printed Table 2 cell is 38 min^-1 (printed column header 'kcat (min^-1)'; the same turnover number is printed again in the Results sentence and in the Abstract for L-serine); 38 / 60 = 0.633333333333 s^(-1). The exported value is 38.0 s^(-1), which is the printed minute-based number carried into a second-based field WITHOUT the 60-fold conversion. Km: the printed Table 2 cell is 3.1 mM, already the export unit; the exported value is 3.1 mM. kcat/Km: the printed Table 2 cell is 12 in the column's implied min^-1 mM^-1 (the header prints no unit literal); 12 / 60 = 0.2 s^(-1)*mM^(-1); the exported value is 12.258064516129032 s^(-1)*mM^(-1), which is the bare quotient of the export's own unconverted kcat and its Km. The cited Table 2 row prints no fourth numeric column.

substrate: S-methyl-L-cysteine


substrate_name: malonate (at pH 7.5)

substrate: malonate (at pH 7.5)


source_db: skid

row_label: Table 1, substrate row '3-hydroxybenzoic acid', wild-type EntE

table_label: Table 1: Kinetic Parameters of EntE (Biochemistry 2010, 49(17):3648-3657)

source_databases_merged: skid uniprot

source: skid


substrate_name: salicylate

normalized_value_unit_evidence: Km: printed Table 1 cell 70 +/- 4 uM; the catalog unit is mM and 1 uM is 0.001 mM, so 70 / 1000 = 0.07 mM; the exported value is 0.0055 mM. kcat: printed Table 1 cell 0.8 +/- 0.1 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 0.8 s^(-1). kcat/Km: printed Table 1 cell 1.1 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 11000 x 0.001 = 11 s^-1 mM^-1; the exported value is 145.45454545454547 s^(-1)*mM^(-1).

table_label: Table 1: Kinetic Parameters of EntE1 (decoded plain-numeral transcription of the printed table)

substrate: salicylate


substrate_name: ATP

substrate: ATP


enzyme_display_name: E1 NEDD8-activating enzyme

organism: Homo sapiens

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

proof_lines: chimeric Ub1, pH not specified in the publication, temperature not specified in the publication

enzyme: E1 NEDD8-activating enzyme


mutation_type: deletion

proof_lines: mutant DELTA946, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant DELTA348, pH not specified in the publication, temperature not specified in the publication


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

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

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


substrate_name: ubiquitin

substrate: ubiquitin


substrate_name: 2-hydroxybenzoic acid

substrate: 2-hydroxybenzoic acid


substrate_name: 2,5-dihydroxybenzoic acid

substrate: 2,5-dihydroxybenzoic acid


substrate_name: 2,3-Dihydroxybenzoic acid

substrate: 2,3-Dihydroxybenzoic acid


substrate_name: 2,4-dihydroxybenzoic acid

substrate: 2,4-dihydroxybenzoic acid


substrate_name: diphosphate

substrate: diphosphate


proof_lines: mutant enzyme Y352H, pH and temperature not specified in the publication


proof_lines: mutant enzyme I310N, pH and temperature not specified in the publication


proof_lines: acceptor aryl-carrier protein domain of SrfB1, pH 7.5, 37°C

proof_lines: acceptor aryl-carrier protein domain of EntB, pH 7.5, 37°C


proof_lines: acceptor holo-[L-seryl-carrier protein domain of Ybt], pH 7.5, 37°C

proof_lines: acceptor holo-[L-seryl-carrier protein domain of SrfB1], pH 7.5, 37°C


organism: Bacillus subtilis

substrate_name: Unknown

substrate: Unknown


substrate_name: malonate

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: pH 7.5, temperature not specified in the publication

substrate: malonate


substrate_name: D-Ala

assay_conditions_summary: pH 7.2; 310.15 K; cofactor CoA

proof_lines: wild-type, thiol assay, presence of coenzyme A, pH 7.2, temperature not specified in the publication

proof_lines: wild-type, diphosphate assay, presence of coenzyme A, pH 7.2, temperature not specified in the publication

substrate: D-Ala


proof_lines: mutant C269A, diphosphate assay, presence of coenzyme A, pH 7.2, temperature not specified in the publication


enzyme_display_name: glutamate racemase

organism: Enterococcus faecalis

substrate_name: D-glutamate

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

enzyme: glutamate racemase

substrate: D-glutamate


enzyme_display_name: 3-(methylthio)propionate--CoA ligase

organism: Dinoroseobacter shibae

smiles: CSCCC(=O)[O-]

enzyme: 3-(methylthio)propionate--CoA ligase


assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines:
wild-type
wild type enzyme, at pH 7.2 and 37°C


proof_lines: pH and temperature not specified in the publication


organism: Enterococcus faecium

substrate_name: L-glutamate / D-glutamate

substrate: L-glutamate / D-glutamate


enzyme_display_name: alanine racemase

substrate_name: D-alanine

enzyme: alanine racemase

substrate: D-alanine


enzyme_display_name: D-psicose 3-epimerase

organism: Enterocloster bolteae

substrate_name: D-tagatose

enzyme: D-psicose 3-epimerase

substrate: D-tagatose


enzyme_display_name: dTDP-4-dehydrorhamnose 3,5-epimerase

organism: Escherichia coli

enzyme: dTDP-4-dehydrorhamnose 3,5-epimerase


enzyme_display_name: UDP-glucose 4-epimerase

enzyme: UDP-glucose 4-epimerase


enzyme_display_name: aldose 1-epimerase

substrate_name: alpha-D-galactose

enzyme: aldose 1-epimerase

substrate: alpha-D-galactose


enzyme_display_name: chorismate mutase

proof_lines: 30°C, pH 7.5, chorismate mutase domain of P-protein

enzyme: chorismate mutase


enzyme_display_name: L-arabinose isomerase

substrate_name: D-galactose

proof_lines:
at pH 7.0 and 50°C
pH 7.0-7.5, 45-50°C, recombinant enzyme
at pH 7.0 and 40°C

enzyme: L-arabinose isomerase

substrate: D-galactose


enzyme_display_name: bisphosphoglycerate mutase

organism: Equus caballus

substrate_name: Glycerate 1,3-bisphosphate

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

enzyme: bisphosphoglycerate mutase

substrate: Glycerate 1,3-bisphosphate


enzyme_display_name: glucuronate isomerase

substrate_name: D-tagaturonate

enzyme: glucuronate isomerase

substrate: D-tagaturonate


proof_lines: in 50 mM potassium phosphate buffer pH 7.4, at 30°C


enzyme_display_name: arabinose-5-phosphate isomerase

substrate_name: D-arabinose 5-phosphate

smiles: C(C(C(C(C=O)O)O)O)OP(=O)(O)O

enzyme: arabinose-5-phosphate isomerase

substrate: D-arabinose 5-phosphate


substrate_name: D-glucuronate

proof_lines:
in absence of added metal or chelator
reconstituted with Co2+, 30°C, pH 8
in presence of 0.01 mM Zn2+

substrate: D-glucuronate


proof_lines:
apo and Zn2+ reconstituted enzyme
Zn2+ reconstituted enzyme
apo enzyme


enzyme_display_name: S-ribosylhomocysteine lyase

substrate_name: S-ribosylhomocysteine

enzyme: S-ribosylhomocysteine lyase

substrate: S-ribosylhomocysteine


enzyme_display_name: tRNA pseudouridine(32) synthase

substrate_name: tRNA uridine32

proof_lines: pH 7.5, 37°C, anticodon stem-loop of Escherichia coli tRNAPhe (17-mer)

enzyme: tRNA pseudouridine(32) synthase

substrate: tRNA uridine32


enzyme_display_name: aspartate-ammonia ligase

organism: Lactiplantibacillus plantarum

substrate_name: ATP

enzyme: aspartate-ammonia ligase

substrate: ATP


substrate_name: L-Asp

substrate: L-Asp


enzyme_display_name: glutamine synthetase

organism: Methylococcus capsulatus

substrate_name: ADP

enzyme: glutamine synthetase

substrate: ADP


enzyme_display_name: UniProt P12425

source_license: CC BY-NC-ND 4.0

smiles: N

proof_lines:
Raw SKiD Env: Temp=25°C, pH=-----
Raw SKiD Env: Temp=-----, pH=7

enzyme: UniProt P12425


enzyme_display_name: lactoylglutathione lyase

proof_lines:
in the presence of Fe2+
in the presence of Mn2+
in the presence of Cd2+

enzyme: lactoylglutathione lyase


enzyme_display_name: tRNA pseudouridine(13) synthase

substrate_name: tRNA uridine13

enzyme: tRNA pseudouridine(13) synthase

substrate: tRNA uridine13


substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


enzyme_display_name: lysine 2,3-aminomutase

substrate_name: L-Lys

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

enzyme: lysine 2,3-aminomutase

substrate: L-Lys


enzyme_display_name: glutamate racemase

substrate_name: L-glutamate

proof_lines: in presence of 0.0065 mM of the activator UDP-N-acetylmuramyl-L-Ala

enzyme: glutamate racemase

substrate: L-glutamate


organism: Arabidopsis thaliana

proof_lines:
mutant A174S of isoenzyme GLN1,4
mutant A174S of isoenzyme GLN1,3


substrate_name: L-Glu

substrate: L-Glu


proof_lines:
mutant K49Q/A174S of isoenzyme GLN1,4
mutant K49Q/A174S of isoenzyme GLN1,3


proof_lines:
isoenzyme GLN1,4
isoenzyme GLN1,3
pH 7.8, 30°C, below, isoenzyme GLN1,1


proof_lines:
isoenzyme GLN1,4
isoenzyme GLN1,3
pH 7.8, 30°C, isoenzyme GLN1,4


proof_lines:
mutant K49Q of isoenzyme GLN1,4
mutant K49Q of isoenzyme GLN1,3


enzyme_display_name: isochorismate synthase

substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication, inhibition of isochorismate synthase activity

proof_lines: pH and temperature not specified in the publication, inhibition of salicylate synthase activity

enzyme: isochorismate synthase

substrate: Unknown


enzyme_display_name: glutamate--ethylamine ligase

substrate_name: L-cysteine

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

enzyme: glutamate--ethylamine ligase

substrate: L-cysteine


substrate_name: ethylamine

smiles: CCN

substrate: ethylamine


organism: Clarias batrachus

assay_conditions_summary: cofactor ADP


substrate_name: hydroxylamine

smiles: NO

substrate: hydroxylamine


organism: Sphagnum fallax


organism: Xylanibacter ruminicola

assay_conditions_summary: pH 6; 310.15 K; cofactor ATP

proof_lines: isozyme GSIII-1, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity

proof_lines: isozyme GSIII-2, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity

proof_lines: isozyme GSI, pH 6.0, 37°C, gamma-glutamylhydroxamate synthetase activity


proof_lines: isozyme GSIII-2, pH 7.5, 37°C, glutamine synthetase activity

proof_lines: isozyme GSIII-1, pH 7.5, 37°C, glutamine synthetase activity


substrate_name: L-glutamine

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

substrate: L-glutamine


organism: Oryza sativa Japonica Group

proof_lines:
30°C, isoenzyme OsGLN1,1
30°C, isoenzyme OsGLN1,2


assay_conditions_summary: 303.15 K; cofactor ATP


substrate_name: NH3; L-Glutamate; ATP

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

substrate: NH3; L-Glutamate; ATP


substrate_name: ATP; L-Glutamate; NH3

substrate: ATP; L-Glutamate; NH3


substrate_name: NH3; ATP; L-Glutamate

substrate: NH3; ATP; L-Glutamate


organism: Camellia sinensis


organism: Beta vulgaris


organism: Bradyrhizobium japonicum


enzyme_display_name: aspartate--ammonia ligase (ADP-forming)

organism: Solanum tuberosum

enzyme: aspartate--ammonia ligase (ADP-forming)


organism: Hordeum vulgare

proof_lines:
isozyme GS1
isozyme GS2


organism: Spinacia oleracea


organism: Senna obtusifolia


assay_conditions_summary: pH 7.8; 303.15 K; cofactor ATP

proof_lines:
pH 7.8, 30°C, isoenzyme GLN1,1
pH 7.8, 30°C, isoenzyme GLN1,4
pH 7.8, 30°C, isoenzyme GLN1,3


enzyme_display_name: NAD(+) synthase

organism: Herbaspirillum seropedicae

enzyme: NAD(+) synthase


organism: Zea mays


organism: Exiguobacterium sp.

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E60A/R64G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; cofactor ADP

proof_lines: pH 6.0, 35°C, recombinant mutant E60A/R64G


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:C4L2T5 and applied mutation signature E60A to reconstruct the assayed variant sequence.

column_label: Table 1: The kinetic parameters of the wild-type ExiGS and its mutants (Appl Microbiol Biotechnol 2017, volume 101, pages 3653-3661); printed row heads Km | Vmax (mM x min-1) | kcat (s-1) | kcat/Km (s-1 x uM-1); substrate blocks ADP (uM), Gln (mM) and Hydroxylamine (mM). Table 1, ADP block, enzyme column E60A; column Km = 4.61 uM; column kcat (s-1) = 4.76; column kcat/Km (s-1 x uM-1) = 1.03. captured primary segment: ADP block | E60A | Km 4.61 uM | kcat 4.76 s^-1 | kcat/Km 1.03 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 4.61 uM under the ADP block head ADP (uM); 1 uM is 1/1000 mM, so 4.61 / 1000 = 0.00461 mM. kcat: printed Table 1 cell 4.76 s^-1 under the printed row head kcat (s-1); the printed turnover column is per second and no unit conversion applies, so the normalized value is 4.76 s^(-1). kcat/Km: printed Table 1 cell 1.03 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.03 x 1000 = 1030.0 s^-1 mM^-1..

raw_value_unit_evidence: Table 1, ADP block, enzyme column E60A: Km = 4.61 uM; kcat = 4.76 s^-1; printed kcat/Km = 1.03 s^-1 uM^-1.

row_label: Table 1, ADP block, enzyme column E60A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:C4L2T5 and applied mutation signature E60A/R64G to reconstruct the assayed variant sequence.

column_label: Table 1: The kinetic parameters of the wild-type ExiGS and its mutants (Appl Microbiol Biotechnol 2017, volume 101, pages 3653-3661); printed row heads Km | Vmax (mM x min-1) | kcat (s-1) | kcat/Km (s-1 x uM-1); substrate blocks ADP (uM), Gln (mM) and Hydroxylamine (mM). Table 1, Gln block, enzyme column E60AR64G; column Km = 6.73 mM; column kcat (s-1) = 8.96; column kcat/Km (s-1 x uM-1) = 1.33 x 10^-3. captured primary segment: Gln block | E60A/R64G | Km 6.73 mM | kcat 8.96 s^-1 | kcat/Km 1.33 x 10^-3 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 6.73 mM under the Gln block head Gln (mM); the printed cell is already in mM and no unit conversion applies, so the normalized value is 6.73 mM. kcat: printed Table 1 cell 8.96 s^-1 under the printed row head kcat (s-1); the printed turnover column is per second and no unit conversion applies, so the normalized value is 8.96 s^(-1). kcat/Km: printed Table 1 cell 1.33 x 10^-3 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.33 x 10^-3 x 1000 = 1.33 s^-1 mM^-1..

raw_value_unit_evidence: Table 1, Gln block, enzyme column E60AR64G: Km = 6.73 mM; kcat = 8.96 s^-1; printed kcat/Km = 1.33 x 10^-3 s^-1 uM^-1.


column_label: Table 1: The kinetic parameters of the wild-type ExiGS and its mutants (Appl Microbiol Biotechnol 2017, volume 101, pages 3653-3661); printed row heads Km | Vmax (mM x min-1) | kcat (s-1) | kcat/Km (s-1 x uM-1); substrate blocks ADP (uM), Gln (mM) and Hydroxylamine (mM). Table 1, Gln block, enzyme column E60A; column Km = 8.88 mM; column kcat (s-1) = 9.27; column kcat/Km (s-1 x uM-1) = 1.04 x 10^-3. captured primary segment: Gln block | E60A | Km 8.88 mM | kcat 9.27 s^-1 | kcat/Km 1.04 x 10^-3 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 8.88 mM under the Gln block head Gln (mM); the printed cell is already in mM and no unit conversion applies, so the normalized value is 8.88 mM. kcat: printed Table 1 cell 9.27 s^-1 under the printed row head kcat (s-1); the printed turnover column is per second and no unit conversion applies, so the normalized value is 9.27 s^(-1). kcat/Km: printed Table 1 cell 1.04 x 10^-3 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.04 x 10^-3 x 1000 = 1.04 s^-1 mM^-1..

raw_value_unit_evidence: Table 1, Gln block, enzyme column E60A: Km = 8.88 mM; kcat = 9.27 s^-1; printed kcat/Km = 1.04 x 10^-3 s^-1 uM^-1.

row_label: Table 1, Gln block, enzyme column E60A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R64G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:C4L2T5 and applied mutation signature R64G to reconstruct the assayed variant sequence.

column_label: Table 1: The kinetic parameters of the wild-type ExiGS and its mutants (Appl Microbiol Biotechnol 2017, volume 101, pages 3653-3661); printed row heads Km | Vmax (mM x min-1) | kcat (s-1) | kcat/Km (s-1 x uM-1); substrate blocks ADP (uM), Gln (mM) and Hydroxylamine (mM). Table 1, Gln block, enzyme column R64G; column Km = 9.82 mM; column kcat (s-1) = 13.4; column kcat/Km (s-1 x uM-1) = 1.36 x 10^-3. captured primary segment: Gln block | R64G | Km 9.82 mM | kcat 13.4 s^-1 | kcat/Km 1.36 x 10^-3 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 9.82 mM under the Gln block head Gln (mM); the printed cell is already in mM and no unit conversion applies, so the normalized value is 9.82 mM. kcat: printed Table 1 cell 13.4 s^-1 under the printed row head kcat (s-1); the printed turnover column is per second and no unit conversion applies, so the normalized value is 13.4 s^(-1). kcat/Km: printed Table 1 cell 1.36 x 10^-3 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.36 x 10^-3 x 1000 = 1.36 s^-1 mM^-1..

raw_value_unit_evidence: Table 1, Gln block, enzyme column R64G: Km = 9.82 mM; kcat = 13.4 s^-1; printed kcat/Km = 1.36 x 10^-3 s^-1 uM^-1.

row_label: Table 1, Gln block, enzyme column R64G


organism: Mycobacterium tuberculosis

substrate_name: deamido-NAD+

mutation_signature: recombinant truncated enzyme

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

mutation_type: truncation

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+

proof_lines: pH 8.5, 37°C, recombinant truncated enzyme

substrate: deamido-NAD+


substrate_name: ATP

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: glutamine

proof_lines: pH 8.5, 37°C, recombinant full length enzyme

substrate: glutamine


substrate_name: glutamate

proof_lines: Measured at pH 7.8 and 30 degrees Celsius for all experiments.

substrate: glutamate


substrate_name: ammonium

substrate: ammonium


assay_conditions_summary: pH 7.8; cofactor ATP


proof_lines: The KM value for ammonium is smaller than 10 uM. Measured at pH 7.8 and 30 degrees Celsius for all experiments.


proof_lines: Measured at pH 7.8 and 30 degrees Celsius for all experiments (PubMed:14757761). kcat is 2.96 sec(-1) with ammonium as substrate (PubMed:16338958). kcat is 4.18 sec(-1) with glutamate as substrate (PubMed:16338958).


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

substrate_name: L-glutamate (at pH 7.8 and 60 degrees Celsius)

proof_lines: kcat is 2190 min(-1) towards L-glutamate in the synthetase reaction and 3900 min(-1) towards L-glutamine in the transferase reaction.


substrate_name: hydroxylamine (when a high concentration is used, at pH 7.8 and 60 degrees Celsius)


substrate_name: ATP (at pH 7.8 and 60 degrees Celsius)

substrate: ATP (at pH 7.8 and 60 degrees Celsius)


substrate_name: L-glutamine (at pH 7.2 and 60 degrees Celsius)


substrate_name: ADP (at pH 7.2 and 60 degrees Celsius)

substrate: ADP (at pH 7.2 and 60 degrees Celsius)


organism: Homo sapiens

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: pH 8.0, 37°C, fixed substrates: Gln, ATP

proof_lines: pH 8.0, 37°C, fixed substrates: NH3, ATP


proof_lines: pH 8.0, 37°C, fixed substrates: ATP, deamido-NAD+


assay_conditions_summary: pH 8; cofactor ATP

proof_lines: pH 8.0, 37°C, fixed substrates: Gln, deamido-NAD+

proof_lines: pH 8.0, 37°C, fixed substrates: NH3, deamido-NAD+


organism: Methylococcus capsulatus

substrate_name: Glu

proof_lines: hydroxylamine, glutamyl transferase assay

substrate: Glu


organism: Synechocystis sp.

source_databases_merged: brenda uniprot


enzyme_display_name: oxazoline synthase

organism: uncultured Prochloron sp. 06037A

substrate_name: [TruE2]-(L-amino acyl-L-cysteine)

enzyme: oxazoline synthase

substrate: [TruE2]-(L-amino acyl-L-cysteine)


enzyme_display_name: thiazoline synthase

substrate_name: [TruE2]-L-amino acyl-L-cysteine

enzyme: thiazoline synthase

substrate: [TruE2]-L-amino acyl-L-cysteine


organism: Anabaena azollae


organism: Bacillus subtilis


organism: Canis familiaris

substrate_name: L-Glutamate; ATP; NH3

substrate: L-Glutamate; ATP; NH3


organism: Escherichia coli

substrate_name: NH3; L-Glutamate; ATP


organism: Arabidopsis thaliana

substrate_name: ATP; L-Glutamate; NH3


substrate_name: ATP; NH3; L-Glutamate

substrate: ATP; NH3; L-Glutamate


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature E60A/R64G to reconstruct the assayed variant sequence.

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature E60A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature R64G to reconstruct the assayed variant sequence.


organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Oryza sativa

substrate_name: L-Glutamate; NH3; ATP

substrate: L-Glutamate; NH3; ATP


organism: Sulfolobus acidocaldarius


organism: Trichormus azollae

sequence_variant_note: Mutation signature D51E could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: D51E mutant enzyme, biosynthetic reaction, pH 7.0, 30°C


proof_lines: wild-type enzyme, biosynthetic reaction, pH 7.0, 30°C


organism: Triticum aestivum


substrate_name: L-Glutamine; Phosphate; ADP

substrate: L-Glutamine; Phosphate; ADP


organism: Hordeum vulgare

substrate: NH3; L-Glutamate; ATP


substrate: ATP; L-Glutamate; NH3


organism: Medicago truncatula

substrate_name: NH3; ATP; L-Glutamate

substrate: NH3; ATP; L-Glutamate


organism: Phaseolus vulgaris


organism: Pseudomonas taetrolens


substrate_name: L-Glutamate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9FMD9 and applied mutation signature Q49K to reconstruct the assayed variant sequence.

column_label: Table 2: The kinetic properties of GLN1;4 mutants (Plant Cell Physiol. 2006, 47(2):299-303); printed column heads Km NH4+ (uM) | Km Glu (mM) | kcat NH4+ (s^(-1)) | kcat Glu (s^(-1)) | kcat/Km NH4+ (mM^-1 s^-1) | kcat/Km Glu (mM^-1 s^-1). Table 2 body row GLN1;4_Q49K, L-Glutamate columns; column Km L-Glutamate (mM) = 1.14; column kcat L-Glutamate (s^(-1)) = 4.96; column kcat/Km L-Glutamate (mM^-1 s^-1) = 4.6. captured primary segment: GLN1;4_Q49K | Km 1.14 mM | kcat 4.96 s^(-1) | kcat/Km 4.6 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 1.14 mM; already mM, so no unit conversion applies; the value is 1.14 mM. kcat: printed Table 2 cell 4.96 s^(-1); already s^(-1), so no unit conversion applies; the value is 4.96 s^(-1). kcat/Km: printed Table 2 cell 4.6 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit, so no unit conversion applies; the printed cell is 4.6 s^(-1)*mM^(-1). Quotient disclosure for this row: 4.96 / 1.14 = 4.350877192982456 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Table 2 body row GLN1;4_Q49K, L-Glutamate columns: Km = 1.14 mM; kcat = 4.96 s^(-1); printed kcat/Km = 4.6 mM^-1 s^-1.

substrate: L-Glutamate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q49K/S174A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S174A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


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

column_label: Table 2: The kinetic properties of GLN1;4 mutants (Plant Cell Physiol. 2006, 47(2):299-303); printed column heads Km NH4+ (uM) | Km Glu (mM) | kcat NH4+ (s^(-1)) | kcat Glu (s^(-1)) | kcat/Km NH4+ (mM^-1 s^-1) | kcat/Km Glu (mM^-1 s^-1). Table 2 body row for the original form GLN1;4, L-Glutamate columns; column Km L-Glutamate (mM) = 0.67; column kcat L-Glutamate (s^(-1)) = 4.18; column kcat/Km L-Glutamate (mM^-1 s^-1) = 6.5. captured primary segment: GLN1;4 | Km 0.67 mM | kcat 4.18 s^(-1) | kcat/Km 6.5 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 0.67 mM; already mM, so no unit conversion applies; the value is 0.67 mM. kcat: printed Table 2 cell 4.18 s^(-1); already s^(-1), so no unit conversion applies; the value is 4.18 s^(-1). kcat/Km: printed Table 2 cell 6.5 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit, so no unit conversion applies; the printed cell is 6.5 s^(-1)*mM^(-1). Quotient disclosure for this row: 4.18 / 0.67 = 6.2388059701492535 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, Table 2 body row for the original form GLN1;4, L-Glutamate columns: Km = 0.67 mM; kcat = 4.18 s^(-1); printed kcat/Km = 6.5 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A174S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K49Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K49Q/A174S to reconstruct the assayed variant sequence.


column_label: Table 1: The kinetic properties of GLN1;3 mutants (Plant Cell Physiol. 2006, 47(2):299-303); printed column heads Km NH4+ (uM) | Km Glu (mM) | kcat NH4+ (s^(-1)) | kcat Glu (s^(-1)) | kcat/Km NH4+ (mM^-1 s^-1) | kcat/Km Glu (mM^-1 s^-1). Table 1 body row for the original form GLN1;3, L-Glutamate columns; column Km L-Glutamate (mM) = 4.17; column kcat L-Glutamate (s^(-1)) = 7.02; column kcat/Km L-Glutamate (mM^-1 s^-1) = 1.8. captured primary segment: GLN1;3 | Km 4.17 mM | kcat 7.02 s^(-1) | kcat/Km 1.8 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 4.17 mM; already mM, so no unit conversion applies; the value is 4.17 mM. kcat: printed Table 1 cell 7.02 s^(-1); already s^(-1), so no unit conversion applies; the value is 7.02 s^(-1). kcat/Km: printed Table 1 cell 1.8 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit, so no unit conversion applies; the printed cell is 1.8 s^(-1)*mM^(-1). Quotient disclosure for this row: 7.02 / 4.17 = 1.683453237410072 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Table 1 body row for the original form GLN1;3, L-Glutamate columns: Km = 4.17 mM; kcat = 7.02 s^(-1); printed kcat/Km = 1.8 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9LVI8 and applied mutation signature A174S to reconstruct the assayed variant sequence.

column_label: Table 1: The kinetic properties of GLN1;3 mutants (Plant Cell Physiol. 2006, 47(2):299-303); printed column heads Km NH4+ (uM) | Km Glu (mM) | kcat NH4+ (s^(-1)) | kcat Glu (s^(-1)) | kcat/Km NH4+ (mM^-1 s^-1) | kcat/Km Glu (mM^-1 s^-1). Table 1 body row GLN1;3_A174S, NH4+ columns; column Km NH4+ (uM) = 334; column kcat NH4+ (s^(-1)) = 6.19; column kcat/Km NH4+ (mM^-1 s^-1) = 19.9. captured primary segment: GLN1;3_A174S | Km 334 uM | kcat 6.19 s^(-1) | kcat/Km 19.9 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 334 uM; 1 uM is 1/1000 mM, so 334 / 1000 = 0.334 mM. kcat: printed Table 1 cell 6.19 s^(-1); already s^(-1), so no unit conversion applies; the value is 6.19 s^(-1). kcat/Km: printed Table 1 cell 19.9 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit, so no unit conversion applies; the printed cell is 19.9 s^(-1)*mM^(-1). Quotient disclosure for this row: 6.19 / 0.334 = 18.53293413173653 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Table 1 body row GLN1;3_A174S, NH4+ columns: Km = 334 uM; kcat = 6.19 s^(-1); printed kcat/Km = 19.9 mM^-1 s^-1.


organism: Exiguobacterium sp.

substrate_name: ADP

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:C4L2T5 and applied mutation signature E60A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 308.15 K; cofactor ADP

table_label: Table 1: The kinetic parameters of the wild-type ExiGS and its mutants (Appl Microbiol Biotechnol 2017, volume 101, pages 3653-3661); printed row heads Km | Vmax (mM x min-1) | kcat (s-1) | kcat/Km (s-1 x uM-1); substrate blocks ADP (uM), Gln (mM) and Hydroxylamine (mM)

substrate: ADP


sequence_variant_note: Mutation signature E60A/R64G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R64G to reconstruct the assayed variant sequence.


column_label: Table 1: The kinetic parameters of the wild-type ExiGS and its mutants (Appl Microbiol Biotechnol 2017, volume 101, pages 3653-3661); printed row heads Km | Vmax (mM x min-1) | kcat (s-1) | kcat/Km (s-1 x uM-1); substrate blocks ADP (uM), Gln (mM) and Hydroxylamine (mM). Table 1, ADP block, enzyme column WT; column Km = 8.65 uM; column kcat (s-1) = 1.05; column kcat/Km (s-1 x uM-1) = 0.12. captured primary segment: ADP block | wild-type ExiGS | Km 8.65 uM | kcat 1.05 s^-1 | kcat/Km 0.12 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 8.65 uM under the ADP block head ADP (uM); 1 uM is 1/1000 mM, so 8.65 / 1000 = 0.00865 mM. kcat: printed Table 1 cell 1.05 s^-1 under the printed row head kcat (s-1); the printed turnover column is per second and no unit conversion applies, so the normalized value is 1.05 s^(-1). kcat/Km: printed Table 1 cell 0.12 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.12 x 1000 = 120.0 s^-1 mM^-1.; the quotient of this line's own printed kcat and Km cells is 1.05 / 0.00865 = 121.38728323699424 s^-1 mM^-1, which is the catalog value, and that quotient written to the precision of the printed efficiency column is the printed cell 0.12 s^-1 uM^-1.

raw_value_unit_evidence: Table 1, ADP block, enzyme column WT: Km = 8.65 uM; kcat = 1.05 s^-1; printed kcat/Km = 0.12 s^-1 uM^-1.

row_label: Table 1, ADP block, enzyme column WT


substrate_name: L-glutamine

substrate: L-glutamine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:C4L2T5 and applied mutation signature R64G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9LVI8 and applied mutation signature K49Q to reconstruct the assayed variant sequence.

column_label: Table 1: The kinetic properties of GLN1;3 mutants (Plant Cell Physiol. 2006, 47(2):299-303); printed column heads Km NH4+ (uM) | Km Glu (mM) | kcat NH4+ (s^(-1)) | kcat Glu (s^(-1)) | kcat/Km NH4+ (mM^-1 s^-1) | kcat/Km Glu (mM^-1 s^-1). Table 1 body row GLN1;3_K49Q, NH4+ columns; column Km NH4+ (uM) = 450; column kcat NH4+ (s^(-1)) = 7.23; column kcat/Km NH4+ (mM^-1 s^-1) = 16.6. captured primary segment: GLN1;3_K49Q | Km 450 uM | kcat 7.23 s^(-1) | kcat/Km 16.6 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 450 uM; 1 uM is 1/1000 mM, so 450 / 1000 = 0.45 mM. kcat: printed Table 1 cell 7.23 s^(-1); already s^(-1), so no unit conversion applies; the value is 7.23 s^(-1). kcat/Km: printed Table 1 cell 16.6 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit, so no unit conversion applies; the printed cell is 16.6 s^(-1)*mM^(-1). Quotient disclosure for this row: 7.23 / 0.45 = 16.066666666666666 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Table 1 body row GLN1;3_K49Q, NH4+ columns: Km = 450 uM; kcat = 7.23 s^(-1); printed kcat/Km = 16.6 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9LVI8 and applied mutation signature K49Q/A174S to reconstruct the assayed variant sequence.

column_label: Table 1: The kinetic properties of GLN1;3 mutants (Plant Cell Physiol. 2006, 47(2):299-303); printed column heads Km NH4+ (uM) | Km Glu (mM) | kcat NH4+ (s^(-1)) | kcat Glu (s^(-1)) | kcat/Km NH4+ (mM^-1 s^-1) | kcat/Km Glu (mM^-1 s^-1). Table 1 body row GLN1;3_K49Q_A174S, NH4+ columns; column Km NH4+ (uM) = 456; column kcat NH4+ (s^(-1)) = 6.83; column kcat/Km NH4+ (mM^-1 s^-1) = 15.6. captured primary segment: GLN1;3_K49Q_A174S | Km 456 uM | kcat 6.83 s^(-1) | kcat/Km 15.6 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 456 uM; 1 uM is 1/1000 mM, so 456 / 1000 = 0.456 mM. kcat: printed Table 1 cell 6.83 s^(-1); already s^(-1), so no unit conversion applies; the value is 6.83 s^(-1). kcat/Km: printed Table 1 cell 15.6 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit, so no unit conversion applies; the printed cell is 15.6 s^(-1)*mM^(-1). Quotient disclosure for this row: 6.83 / 0.456 = 14.978070175438596 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Table 1 body row GLN1;3_K49Q_A174S, NH4+ columns: Km = 456 uM; kcat = 6.83 s^(-1); printed kcat/Km = 15.6 mM^-1 s^-1.


column_label: Table 1: The kinetic properties of GLN1;3 mutants (Plant Cell Physiol. 2006, 47(2):299-303); printed column heads Km NH4+ (uM) | Km Glu (mM) | kcat NH4+ (s^(-1)) | kcat Glu (s^(-1)) | kcat/Km NH4+ (mM^-1 s^-1) | kcat/Km Glu (mM^-1 s^-1). Table 1 body row for the original form GLN1;3, NH4+ columns; column Km NH4+ (uM) = 1,333; column kcat NH4+ (s^(-1)) = 7.10; column kcat/Km NH4+ (mM^-1 s^-1) = 5.5. captured primary segment: GLN1;3 | Km 1,333 uM | kcat 7.10 s^(-1) | kcat/Km 5.5 mM^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 1,333 uM; 1 uM is 1/1000 mM, so 1333 / 1000 = 1.333 mM. kcat: printed Table 1 cell 7.10 s^(-1); already s^(-1), so no unit conversion applies; the value is 7.1 s^(-1). kcat/Km: printed Table 1 cell 5.5 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit, so no unit conversion applies; the printed cell is 5.5 s^(-1)*mM^(-1). Quotient disclosure for this row: 7.1 / 1.333 = 5.326331582895724 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Table 1 body row for the original form GLN1;3, NH4+ columns: Km = 1,333 uM; kcat = 7.10 s^(-1); printed kcat/Km = 5.5 mM^-1 s^-1.


enzyme_display_name: aspartate--ammonia ligase

organism: Leishmania donovani

substrate_name: L-aspartate

enzyme: aspartate--ammonia ligase

substrate: L-aspartate


substrate_name: glutamine

substrate: glutamine


organism: Methylovorus mays

substrate_name: methylamine

smiles: CN

column_label: Table 4; row label: Methylamine; column labels: Relative activity (%) and Km (mM); raw values 100% and 0.18 mM; normalized Km 0.18 mM.

normalized_value_unit_evidence: Km=0.18 mM as reported in Table 4.

raw_value_unit_evidence: Table 4; substrate methylamine; relative activity 100%; Km = 0.18 mM.

row_label: Substrate row: Methylamine; column: Km (mM); relative activity column also present; UniProt A9ZPH9 EC 6.3.1.6 (glutamate--ethylamine ligase) linked to PMID 17284842.

table_label: Table 4. Reactivity of Theanine-Forming Enzyme to Various Amines and Km Values for Substrates

substrate: methylamine


substrate_name: ethylamine

column_label: Table 4; row label: Ethylamine; column labels: Relative activity (%) and Km (mM); raw values 75% and 0.57 mM; normalized Km 0.57 mM.

normalized_value_unit_evidence: Km=0.57 mM as reported in Table 4.

raw_value_unit_evidence: Table 4; substrate ethylamine; relative activity 75%; Km = 0.57 mM.

row_label: Substrate row: Ethylamine; column: Km (mM); relative activity column also present; UniProt A9ZPH9 EC 6.3.1.6 (glutamate--ethylamine ligase) linked to PMID 17284842.

substrate: ethylamine


substrate_name: hydroxylamine

column_label: Table 4; row label: Hydroxylamine; column labels: Relative activity (%) and Km (mM); raw values 40% and 3.9 mM; normalized Km 3.9 mM.

normalized_value_unit_evidence: Km=3.9 mM as reported in Table 4.

raw_value_unit_evidence: Table 4; substrate hydroxylamine; relative activity 40%; Km = 3.9 mM.

row_label: Substrate row: Hydroxylamine; column: Km (mM); relative activity column also present; UniProt A9ZPH9 EC 6.3.1.6 (glutamate--ethylamine ligase) linked to PMID 17284842.

substrate: hydroxylamine


substrate_name: ammonia

column_label: Table 4; row label: Ammonia; column labels: Relative activity (%) and Km (mM); raw values 0.75% and 84 mM; normalized Km 84.0 mM.

normalized_value_unit_evidence: Km=84.0 mM as reported in Table 4.

raw_value_unit_evidence: Table 4; substrate ammonia; relative activity 0.75%; Km = 84 mM.

row_label: Substrate row: Ammonia; column: Km (mM); relative activity column also present; UniProt A9ZPH9 EC 6.3.1.6 (glutamate--ethylamine ligase) linked to PMID 17284842.

substrate: ammonia


substrate_name: glutamic acid (with methylamine as substrate)


substrate_name: ATP (with methylamine as substrate)

substrate: ATP (with methylamine as substrate)


organism: Haloferax mediterranei

substrate_name: ATP

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

substrate: ATP


substrate_name: L-Glu

substrate: L-Glu


substrate_name: L-Gln

substrate: L-Gln


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E327A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


organism: Oryza sativa subsp. japonica

substrate_name: glutamate

substrate: glutamate


substrate_name: ammonium

substrate: ammonium


organism: Bifidobacterium pseudolongum


assay_conditions_summary: cofactor ATP


organism: Ruminococcus albus

assay_conditions_summary: pH 6.4; 310.15 K; cofactor ADP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E380A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 6.4; 310.15 K; cofactor ATP


substrate_name: L-Glutamate; ATP; NH3

substrate: L-Glutamate; ATP; NH3


organism: Zea mays


substrate_name: NH3; L-Glutamate; ATP

substrate: NH3; L-Glutamate; ATP


organism: Bacillus subtilis

substrate_name: ATP; Deamino-NAD+; NH4+

assay_conditions_summary: cofactor NAD+

substrate: ATP; Deamino-NAD+; NH4+


substrate_name: Ethylamine; L-Glutamate; ATP

substrate: Ethylamine; L-Glutamate; ATP


organism: Providencia vermicola

substrate_name: ADP

assay_conditions_summary: pH 8; 308.15 K; cofactor ADP

proof_lines: wild type enzyme, ADP bound to Na+, at pH 8.0 and 35°C

substrate: ADP


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -9, so it is treated as a source-provided variant sequence.

proof_lines: mutant enzyme S45A, ADP bound to Na+, at pH 8.0 and 35°C


substrate_name: L-glutamine

substrate: L-glutamine


organism: Anabaena azollae

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +10, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature D51E could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature D51N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature D51S could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: L-Glutamate

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

substrate: L-Glutamate


organism: Paracoccus denitrificans

column_label: PMID 1356141 abstract; enzyme GS; reaction biosynthetic; paper substrate ammonia; sheet substrate NH4+; metric apparent Km; raw value 0.03 mM; normalized value 0.03 mM.

normalized_value_unit_evidence: Km=0.03 mM as reported.

raw_value_unit_evidence: PubMed abstract reports ammonia apparent Km in the biosynthetic reaction = 0.03 mM.

row_label: glutamine synthetase / biosynthetic reaction / ammonia

table_label: PubMed abstract prose (PMID 1356141)


column_label: PMID 1356141 abstract; enzyme GS; reaction biosynthetic; substrate ATP; metric apparent Km; raw value 0.17 mM; normalized value 0.17 mM.

normalized_value_unit_evidence: Km=0.17 mM as reported.

raw_value_unit_evidence: PubMed abstract reports ATP apparent Km in the biosynthetic reaction = 0.17 mM.

row_label: glutamine synthetase / biosynthetic reaction / ATP


column_label: PMID 1356141 abstract; enzyme GS; reaction transferase; substrate hydroxylamine; metric apparent Km; raw value 2.4 mM; normalized value 2.4 mM.

normalized_value_unit_evidence: Km=2.4 mM as reported.

raw_value_unit_evidence: PubMed abstract reports hydroxylamine apparent Km in the transferase reaction = 2.4 mM.

row_label: glutamine synthetase / transferase reaction / hydroxylamine


organism: Skeletonema costatum

column_label: The abstract reports apparent Michaelis constant values of 0.7 mM for NH4(+), 5.7 mM for glutamic acid, and 0.5 mM for ATP.

raw_value_unit_evidence: Km raw_value=0.5 mM raw_unit=mM

row_label: Prose segment: ATP Km

table_label: PubMed PMID 8756499 abstract


raw_value_unit_evidence: Km raw_value=0.7 mM raw_unit=mM

row_label: Prose segment: NH4(+) Km


substrate_name: Glu

raw_value_unit_evidence: Km raw_value=5.7 mM raw_unit=mM

row_label: Prose segment: glutamic acid Km

substrate: Glu


organism: Sulfolobus acidocaldarius

assay_conditions_summary: cofactor ADP


organism: Clostridium pasteurianum


substrate_name: hydroxylamine


substrate_name: Gln

substrate: Gln


organism: Nitrobacter winogradskyi


substrate: hydroxylamine


organism: Trichormus azollae

substrate_name: L-glutamate

substrate: L-glutamate


assay_conditions_summary: pH 7; 303.15 K; cofactor ATP


organism: Trichinella spiralis

assay_conditions_summary: pH 7; cofactor ATP

column_label: Figure 7 results report Km 0.16 mM of ATP.

raw_value_unit_evidence: Km raw_value=0.16 raw_unit=mM

row_label: Figure 7G ATP substrate Km

table_label: PMC8488193 Figure 7 results


assay_conditions_summary: pH 7


column_label: Figure 7 results report Km 0.20 mM of Glu.

raw_value_unit_evidence: Km raw_value=0.20 raw_unit=mM

row_label: Figure 7G Glu substrate Km


organism: Rattus norvegicus

substrate_name: L-glutamate (with 2 mM of Mn(2+))

substrate: L-glutamate (with 2 mM of Mn(2+))


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

substrate_name: ATP

column_label: Table 1 reports Archaeoglobus fulgidus ATP Km (mM) = 0.56, footnote c.

raw_value_unit_evidence: Km raw_value=0.56 raw_unit=mM

row_label: Archaeoglobus fulgidus

table_label: Table 1 - Comparison of biosynthesis assay kinetic parameters for glutamine synthetase enzymes from different sources

substrate: ATP


substrate_name: alpha-glutamate

column_label: Table 1 reports Archaeoglobus fulgidus alpha-Glu Km (mM) = 3.0, footnote c.

raw_value_unit_evidence: Km raw_value=3.0 raw_unit=mM

substrate: alpha-glutamate


organism: Rhizobium meliloti (strain 1021)

column_label: Abstract reports GSIII had a Km for glutamate of 13.3 mM, for ammonium of 33 mM, and for hydroxylamine of 5.3 mM.

raw_value_unit_evidence: Km raw_value=13.3 mM raw_unit=mM

row_label: Rhizobium meliloti GSIII / glutamate

table_label: PubMed XML abstract PMID 8093245


raw_value_unit_evidence: Km raw_value=33 mM raw_unit=mM

row_label: Rhizobium meliloti GSIII / ammonium


organism: Tuber borchii

assay_conditions_summary: pH 7.5; cofactor ATP


assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=-----
Raw SKiD Env: Temp=-----, pH=7


organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)


organism: Bacillus anthracis

substrate_name: deamido-NAD+

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+

substrate: deamido-NAD+


assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP


organism: Bacillus subtilis (strain 168)

substrate_name: deamido-NAD

substrate: deamido-NAD


substrate_name: glutamine

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

substrate: glutamine


substrate_name: ammonium

substrate: ammonium


organism: Bacillus subtilis

proof_lines:
Raw SKiD Env: Temp=25°C, pH=-----
Raw SKiD Env: Temp=-----, pH=7


organism: uncultured Prochloron sp. 06037A

assay_conditions_summary: pH 8; 307.15 K; cofactor ATP


organism: Pyrococcus sp.

assay_conditions_summary: pH 7.8; 333.15 K; cofactor ATP


organism: Mycobacterium tuberculosis

column_label: Results section Kinetic parameters reports the Km values for ATP and ammonium chloride were 0.50 +/- 0.06 and 10.8 +/- 0.6 mM respectively.

normalized_value_unit_evidence: Km central normalized_value=10.8 normalized_unit=mM.

raw_value_unit_evidence: Results prose reports ammonium chloride Km raw_value=10.8 +/- 0.6 raw_unit=mM.

row_label: Mycobacterium tuberculosis glutamine synthetase ammonium chloride substrate

table_label: ScienceDirect Results section: Kinetic parameters


organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

substrate_name: alpha-glutamine (at 37 degrees Celsius)

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

substrate: alpha-glutamine (at 37 degrees Celsius)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Geobacillus stearothermophilus

assay_conditions_summary: pH 8.5; cofactor ATP

column_label: Abstract reports the Km for NH3, ATP, and deamide-NAD were 0.91, 0.052, and 0.028 mM, respectively.

raw_value_unit_evidence: Km raw_value=0.91 mM raw_unit=mM

row_label: Geobacillus stearothermophilus ammonia-specific NAD synthetase / NH3

table_label: PubMed XML abstract PMID 12450114


organism: Methanocaldococcus jannaschii


substrate_name: glutamate

substrate: glutamate


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


organism: Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)

substrate_name: manganese

smiles: [Mn]

substrate: manganese


organism: Phaseolus vulgaris

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


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


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

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


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


proof_lines: wild-type, 25°C, pH not specified in the publication

proof_lines: pH 7.0, temperature not specified in the publication, wild-type enzyme


proof_lines: mutant E304H, 25°C, pH not specified in the publication


proof_lines: mutant E304D, 25°C, pH not specified in the publication


assay_conditions_summary: 298.15 K; cofactor ATP


proof_lines: mutant G302A, 25°C, pH not specified in the publication


proof_lines: mutant Y303H, 25°C, pH not specified in the publication


proof_lines: pH 7.0, temperature not specified in the publication, mutant R62A


proof_lines: pH 7.0, temperature not specified in the publication, mutant E304A


organism: Lupinus luteus

substrate_name: ADP

substrate: ADP


assay_conditions_summary: cofactor ATP


organism: Medicago truncatula

proof_lines: pH not specified in the publication, 30°C, mutant mature enzyme lacking the C-terminal peptide


proof_lines: pH not specified in the publication, 30°C, wild-type mature enzyme


assay_conditions_summary: 303.15 K; cofactor ATP


organism: [Bacillus] caldolyticus

proof_lines: NH4+, biosynthetic assay, Mg2+-activated, enzyme form EII

proof_lines: biosynthetic assay, Mn2+-stimulated, enzyme form EI

proof_lines: hydroxylamine, Mg2+-activated, enzyme form EII


proof_lines:
Mn2+-activated, enzyme form EII
Mn2+-activated, enzyme form EI


proof_lines: biosynthetic assay, Mg2+-activated, enzyme form EII

proof_lines: ATP, biosynthetic assay, Mn2+-activated, enzyme form EII


proof_lines: ATP, biosynthetic assay, Mn2+-activated, enzyme form EI

proof_lines: biosynthetic assay, Mg2+-activated, enzyme form I or Mn2+-activated, enzyme form EII.

proof_lines: L-Glu, biosynthetic assay, Mg2+-activated, enzyme form EII


organism: Drosophila melanogaster


organism: Bradyrhizobium japonicum


substrate_name: L-Gln

proof_lines:
glutamyl transferase reaction
biosynthetic reaction

substrate: L-Gln


proof_lines: wild-type, 25°C, pH not specified in the publication

proof_lines: pH 7.0, temperature not specified in the publication, wild-type enzyme


substrate_name: L-glutamine

substrate: L-glutamine


organism: Escherichia coli


assay_conditions_summary: cofactor NAD+


proof_lines:
oxidized mutant enzyme E165C
reduced mutant enzyme E165C


substrate_name: L-Glu

substrate: L-Glu


organism: Trypanosoma cruzi

proof_lines: recombinant enzyme, Malachite green assay, pH and temperature not specified in the publication

proof_lines: recombinant enzyme, coupled reactions assay, pH and temperature not specified in the publication


substrate_name: Unknown

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

substrate: Unknown


organism: Azospirillum brasilense


organism: Pseudomonas taetrolens

assay_conditions_summary: pH 8


assay_conditions_summary: pH 11; cofactor ATP


substrate_name: methylamine

substrate: methylamine


substrate_name: ethylamine

substrate: ethylamine


organism: Camellia sinensis

assay_conditions_summary: pH 7.8; cofactor ATP


substrate_name: L-glutamate

substrate: L-glutamate


proof_lines:
substrate NH4+, pH 7.8
substrate ATP, pH 7.8
substrate L-glutamate, pH 7.8


organism: Bifidobacterium bifidum


substrate_name: ATP

substrate: ATP


organism: Bifidobacterium breve


organism: Corynebacterium callunae

assay_conditions_summary: cofactor ADP


substrate_name: hydroxylamine

substrate: hydroxylamine


substrate_name: Gln

substrate: Gln


organism: Canis lupus familiaris

proof_lines:
short isoform, pH 7.2, 37°C
long isoform, pH 7.2, 37°C


assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP


organism: Exiguobacterium sp.

assay_conditions_summary: pH 6; 308.15 K; cofactor ADP

proof_lines: pH 6.0, 35°C, recombinant wild-type enzyme


enzyme_display_name: beta-amyrin synthase

organism: Lathyrus oleraceus

enzyme: beta-amyrin synthase


substrate_name: Glu

substrate: Glu


organism: Methanohalophilus portucalensis

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7; cofactor ADP


assay_conditions_summary: pH 7


organism: Pyrococcus sp.


organism: Nicotiana plumbaginifolia


assay_conditions_summary: pH 7.4; 308.15 K; cofactor ATP


organism: Ligilactobacillus salivarius

substrate_name: L-aspartate

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

substrate: L-aspartate


organism: Staphylococcus aureus

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


organism: Spinacia oleracea


organism: Rhodobacter capsulatus


organism: Sinorhizobium meliloti


enzyme_display_name: D-aspartate ligase

organism: Enterococcus faecalis

enzyme: D-aspartate ligase


substrate_name: D-Aspartate

substrate: D-Aspartate


enzyme_display_name: trypanothione synthase

organism: Leishmania major

substrate_name: glutathione

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

proof_lines: pH 7.7, 25°C, recombinant trypanothione synthase

enzyme: trypanothione synthase

substrate: glutathione


substrate_name: glutathionylspermidine

substrate: glutathionylspermidine


substrate_name: spermidine

smiles: C(CCNCCCN)CN

substrate: spermidine


organism: Enterococcus hirae

substrate_name: D-Aspartate; Hydroxylamine; ATP

substrate: D-Aspartate; Hydroxylamine; ATP


enzyme_display_name: glutathionylspermidine synthase

organism: Crithidia fasciculata

proof_lines: pH 7.2, 25°C, recombinant trypanothione synthase performing the glutathionylspermidine synthase reaction

enzyme: glutathionylspermidine synthase


assay_conditions_summary: pH 7.2; cofactor ATP


organism: Escherichia coli

proof_lines: kcat is 7 sec(-1) for Gsp synthetase activity at pH 6.8 and 2.1 sec(-1) for Gsp amidase activity at pH 7.5.


organism: Mycobacterium smegmatis

substrate_name: GlcN-Ins; ATP; L-Cysteine

substrate: GlcN-Ins; ATP; L-Cysteine


enzyme_display_name: 4-methyleneglutamate--ammonia ligase

organism: Arachis hypogaea

enzyme: 4-methyleneglutamate--ammonia ligase


enzyme_display_name: glutamate--putrescine ligase

organism: Escherichia coli (strain K12)

enzyme: glutamate--putrescine ligase


organism: Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)


substrate_name: MgADP-

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature C79A to reconstruct the assayed variant sequence.

proof_lines: pH 7.3, 25°C, synthetase activity of the C79A mutant

substrate: MgADP-


substrate_name: Reduced glutathione; ATP; Spermidine

assay_conditions_summary: pH 7.3; 298.15 K; cofactor ATP

proof_lines:
pH 7.3, 25°C, synthetase activity
pH 7.2, 25°C

substrate: Reduced glutathione; ATP; Spermidine


substrate_name: Reduced glutathione; Glutathionylspermidine; ATP

assay_conditions_summary: pH 7.2; 298.15 K; cofactor ATP

proof_lines: pH 7.2, 25°C, recombinant trypanothione synthase


assay_conditions_summary: pH 7.8; 298.15 K; cofactor ATP


substrate_name: GlcN-Ins

substrate: GlcN-Ins


substrate_name: L-Cysteine

substrate: L-Cysteine


organism: Trypanosoma cruzi (strain CL Brener)

substrate_name: glutathione with spermidine as cosubstrate


substrate_name: MgATP

substrate: MgATP


substrate_name: aminopropylcadaverine

smiles: C(CCN)CCNCCCN

substrate: aminopropylcadaverine


substrate_name: glutamate (at pH 8 and at 37 degrees Celsius)


substrate_name: ATP (at pH 8 and at 37 degrees Celsius)

assay_conditions_summary: cofactor ATP

substrate: ATP (at pH 8 and at 37 degrees Celsius)


substrate_name: putrescine (at pH 8 and at 37 degrees Celsius)

smiles: C(CCN)CN


substrate_name: ATP

substrate: ATP


substrate_name: Glutathionylspermidine

column_label: Table III, reCf-TryS row, Gsp Km column and kcat With Gsp column

normalized_value_unit_evidence: kcat 8.7 s^-1; Km 480 uM = 0.480 mM; typed same-measurement quotient kcat/Km = 18.125 s^-1*mM^-1

raw_value_unit_evidence: Table III reCf-TryS with Gsp: Km 480 uM. Table III reCf-TryS with Gsp: kcat 8.7 s^-1.

row_label: reCf-TryS

table_label: Table III. Kinetics parameters for synthetase and amidase activity from native and recombinant (re) trypanothione synthetases

substrate: Glutathionylspermidine


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate_name: L-cysteine

column_label: PubMed abstract reports K(m) values of 40 +/- 3 and 72 +/- 9 microM for Cys and GlcN-Ins, respectively; Cys maps to the first value.

normalized_value_unit_evidence: Km 40 microM = 0.04 mM

raw_value_unit_evidence: Cys Km 40 +/- 3 microM

row_label: Cys

table_label: PubMed abstract for PMID 12033919

substrate: L-cysteine


column_label: PubMed abstract reports K(m) values of 40 +/- 3 and 72 +/- 9 microM for Cys and GlcN-Ins, respectively; GlcN-Ins maps to the second value.

normalized_value_unit_evidence: Km 72 microM = 0.072 mM

raw_value_unit_evidence: GlcN-Ins Km 72 +/- 9 microM

row_label: GlcN-Ins


column_label: PMC Table 1 lists ATP in the substrate row and Km, mM column as 1.84 +/- 0.06.

row_label: ATP

table_label: PMC Table 1: Kinetic Parameters of M. smegmatis MshC


substrate_name: glutathione


substrate_name: spermidine


substrate_name: Unknown

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C79A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


substrate_name: glutathionylspermidine


organism: Leishmania donovani


assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


proof_lines: versus GSH, pH 8.0, 25°C, recombinant enzyme


organism: Trypanosoma brucei


substrate_name: Spermidine

smiles: NCCCCNCCCN

substrate: Spermidine


substrate_name: reduced glutathione

substrate: reduced glutathione


organism: Escherichia coli K-12

substrate_name: putrescine

substrate: putrescine


substrate_name: L-glutamate

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

substrate: L-glutamate


substrate: glutathionylspermidine


substrate: glutathione


substrate: spermidine


substrate_name: ATP (at pH 6.8)

assay_conditions_summary: pH 6.8; cofactor ATP

substrate: ATP (at pH 6.8)


substrate_name: glutathionylspermidine (at pH 7.5)

substrate: glutathionylspermidine (at pH 7.5)


enzyme_display_name: UniProt P33221

substrate_name: formyl phosphate

enzyme: UniProt P33221

substrate: formyl phosphate


substrate_name: acetyl phosphate

smiles: CC(=O)OP(=O)(O)O

substrate: acetyl phosphate


substrate_name: Carbamoyl phosphate

substrate: Carbamoyl phosphate


assay_conditions_summary: pH 8; buffer recombinant enzyme

proof_lines: recombinant enzyme, pH 8.0, 25°C, HEPES buffer

proof_lines: recombinant enzyme, pH 8.0, 37°C, HEPES buffer

proof_lines: recombinant enzyme, pH 7.0, 37°C, phosphate buffer


assay_conditions_summary: pH 8; cofactor ATP

proof_lines: recombinant enzyme, pH 8.0, 25°C, HEPES buffer, with spermidine

proof_lines: recombinant enzyme, pH 8.0, 37°C, HEPES buffer, with spermidine

proof_lines: recombinant enzyme, pH 7.0, 37°C, phosphate buffer, with glutathionylspermidine


substrate_name: Reduced glutathione

assay_conditions_summary: pH 8

proof_lines: recombinant enzyme, pH 7.0, 37°C, phosphate buffer, with spermidine

substrate: Reduced glutathione


substrate_name: gamma-L-Glu-L-Cys(S-methyl)-Gly

substrate: gamma-L-Glu-L-Cys(S-methyl)-Gly


enzyme_display_name: 8-demethylnovobiocic acid synthase

organism: Streptomyces niveus

proof_lines: pH 7.0, temperature not specified in the publication

enzyme: 8-demethylnovobiocic acid synthase


organism: Azospirillum brasilense

substrate_name: L-glutamine

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NAD+

substrate: L-glutamine


organism: Mycolicibacterium smegmatis

proof_lines:
pH 7.8, 25°C, recombinant enzyme
pH 7.5, 37°C


substrate_name: ATP

substrate: ATP


substrate: Unknown


organism: Trypanosoma cruzi

column_label: Table I; TcTryS (recombinant) column; rows K mapp Glutathionylspermidine (uM) and k cat (s^-1)-with Glutathionylspermidine

raw_value_unit_evidence: Table I: Kmapp Glutathionylspermidine 66 +/- 3 uM; kcat-with Glutathionylspermidine 2.8 +/- 0.3 s^-1

row_label: TcTryS recombinant; K mapp Glutathionylspermidine and k cat-with Glutathionylspermidine

table_label: Table I


column_label: Table I; TcTryS (recombinant) column; row K mapp MgATP (uM)

raw_value_unit_evidence: Table I: K mapp MgATP 53 +/- 3 uM

row_label: TcTryS recombinant; K mapp MgATP


substrate_name: GSH

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

column_label: Table I; TcTryS (recombinant) column; row K mapp GSH (uM)-with Glutathionylspermidine

normalized_value_unit_evidence: Km 0.19 mM

raw_value_unit_evidence: Table I: K mapp GSH-with Glutathionylspermidine 190 +/- 30 uM

row_label: TcTryS recombinant; K mapp GSH-with Glutathionylspermidine

substrate: GSH


enzyme_display_name: prokaryotic ubiquitin-like protein ligase

organism: Mycobacterium tuberculosis


assay_conditions_summary: pH 7.4; cofactor ATP

enzyme: prokaryotic ubiquitin-like protein ligase


enzyme_display_name: beta-citrylglutamate synthase

organism: Mus musculus

substrate_name: N-acetyl-aspartylglutamate

enzyme: beta-citrylglutamate synthase

substrate: N-acetyl-aspartylglutamate


organism: Corynebacterium glutamicum

substrate_name: [PanB]-L-lysine

proof_lines: pH 7.5, 30°C, recombinant His-tagged enzyme

substrate: [PanB]-L-lysine


substrate_name: [protein PanB]-L-lysine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature S119A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

substrate: [protein PanB]-L-lysine


enzyme_display_name: lipoate--protein ligase

substrate_name: Unknown

enzyme: lipoate--protein ligase


substrate_name: D,L-lipoic acid

substrate: D,L-lipoic acid


substrate_name: magnesium ion

substrate: magnesium ion


substrate_name: L-glutamate

substrate: L-glutamate


substrate_name: citrate

substrate: citrate


organism: Escherichia coli

substrate_name: octanoic acid

smiles: CCCCCCCC(=O)O

substrate: octanoic acid