sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13000 and applied mutation signature S41C with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters (Km, kcat) for the Wild-Type and Mutant DTBS Enzymes (pH 7.5, 25 C) Measured by Spectrophotometric Assay and [14C]CO2 Fixation Assay (Biochemistry 1997, 36, 4751-4760); printed column heads enzymes | kcat (min-1) | Km (DAPA) (uM) | kcat/Km(DAPA) (M-1 s-1) | Km(ATP) (uM) | kcat/Km(ATP) (M-1 s-1). Table 2, enzyme row S41C; column kcat (min-1) = 3.29; column Km(ATP) (uM) = 1.45; column kcat/Km(ATP) (M-1 s-1) = 3.78 x 10^4. captured primary segment: ATP | S41C DTBS | Km 1.45 uM | kcat 3.29 min^-1 | kcat/Km 3.78 x 10^4 M^-1 s^-1

raw_value_unit_evidence: Table 2, enzyme row S41C, substrate column set ATP: Km(ATP) (uM) = 1.45 uM; kcat (min-1) = 3.29 min^-1; kcat/Km(ATP) (M-1 s-1) = 3.78 x 10^4 M^-1 s^-1.

row_label: Table 2, enzyme row S41C, column set for substrate ATP


enzyme_display_name: dethiobiotin synthase

organism: Escherichia coli

substrate_name: ATP

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13000 and applied mutation signature T11V with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

column_label: Table 2: Kinetic Parameters (Km, kcat) for the Wild-Type and Mutant DTBS Enzymes (pH 7.5, 25 C) Measured by Spectrophotometric Assay and [14C]CO2 Fixation Assay (Biochemistry 1997, 36, 4751-4760); printed column heads enzymes | kcat (min-1) | Km (DAPA) (uM) | kcat/Km(DAPA) (M-1 s-1) | Km(ATP) (uM) | kcat/Km(ATP) (M-1 s-1). Table 2, enzyme row T11V; column kcat (min-1) = 1.51; column Km(ATP) (uM) = 9.47 x 10^3; column kcat/Km(ATP) (M-1 s-1) = 2.65 x 10^0. captured primary segment: ATP | T11V DTBS | Km 9.47 x 10^3 uM | kcat 1.51 min^-1 | kcat/Km 2.65 x 10^0 M^-1 s^-1

raw_value_unit_evidence: Table 2, enzyme row T11V, substrate column set ATP: Km(ATP) (uM) = 9.47 x 10^3 uM; kcat (min-1) = 1.51 min^-1; kcat/Km(ATP) (M-1 s-1) = 2.65 x 10^0 M^-1 s^-1.

row_label: Table 2, enzyme row T11V, column set for substrate ATP

data_origin: experimental

enzyme: dethiobiotin synthase

substrate: ATP

status: corrected

source: oed


mutation_signature: Unknown

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

column_label: Table 2: Kinetic Parameters (Km, kcat) for the Wild-Type and Mutant DTBS Enzymes (pH 7.5, 25 C) Measured by Spectrophotometric Assay and [14C]CO2 Fixation Assay (Biochemistry 1997, 36, 4751-4760); printed column heads enzymes | kcat (min-1) | Km (DAPA) (uM) | kcat/Km(DAPA) (M-1 s-1) | Km(ATP) (uM) | kcat/Km(ATP) (M-1 s-1). Table 2, enzyme row wild-type; column kcat (min-1) = 3.73; column Km(ATP) (uM) = 0.39; column kcat/Km(ATP) (M-1 s-1) = 1.59 x 10^5. captured primary segment: ATP | wild-type DTBS | Km 0.39 uM | kcat 3.73 min^-1 | kcat/Km 1.59 x 10^5 M^-1 s^-1

raw_value_unit_evidence: Table 2, enzyme row wild-type, substrate column set ATP: Km(ATP) (uM) = 0.39 uM; kcat (min-1) = 3.73 min^-1; kcat/Km(ATP) (M-1 s-1) = 1.59 x 10^5 M^-1 s^-1.

row_label: Table 2, enzyme row wild-type, column set for substrate ATP


organism: Cryptococcus neoformans (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)

substrate_name: ATP (at 37 degrees Celsius)

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

assay_conditions_summary: cofactor ATP

proof_lines: kcat is 27.3 sec(-1) for phosphoribosylamine--glycine ligase activity (at 37 degrees Celsius).

substrate: ATP (at 37 degrees Celsius)

source: uniprot


substrate_name: glycine (at 37 degrees Celsius)

verification_status: verified

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

column_label: Results text reports Km_app_glycine values of 496 +/- 20 microM for bifunctional GARs/AIRs and 364 +/- 9 microM for single unit GARs.

raw_value_unit_evidence: Km raw_value=496 microM raw_unit=microM

row_label: C. neoformans bifunctional GARs/AIRs / glycine

table_label: PMC full-text PMID 34416230 / Figure 4B and Table 1 kinetics text

substrate: glycine (at 37 degrees Celsius)

status: verified


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13000 and applied mutation signature E12A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

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

column_label: Table 2: Kinetic Parameters (Km, kcat) for the Wild-Type and Mutant DTBS Enzymes (pH 7.5, 25 C) Measured by Spectrophotometric Assay and [14C]CO2 Fixation Assay (Biochemistry 1997, 36, 4751-4760); printed column heads enzymes | kcat (min-1) | Km (DAPA) (uM) | kcat/Km(DAPA) (M-1 s-1) | Km(ATP) (uM) | kcat/Km(ATP) (M-1 s-1). Table 2, enzyme row E12A; column kcat (min-1) = 4.61; column Km (DAPA) (uM) = 1.13; column kcat/Km(DAPA) (M-1 s-1) = 6.82 x 10^4. captured primary segment: DAPA | E12A DTBS | Km 1.13 uM | kcat 4.61 min^-1 | kcat/Km 6.82 x 10^4 M^-1 s^-1

raw_value_unit_evidence: Table 2, enzyme row E12A, substrate column set DAPA: Km (DAPA) (uM) = 1.13 uM; kcat (min-1) = 4.61 min^-1; kcat/Km(DAPA) (M-1 s-1) = 6.82 x 10^4 M^-1 s^-1.

row_label: Table 2, enzyme row E12A, column set for substrate DAPA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13000 and applied mutation signature E12D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters (Km, kcat) for the Wild-Type and Mutant DTBS Enzymes (pH 7.5, 25 C) Measured by Spectrophotometric Assay and [14C]CO2 Fixation Assay (Biochemistry 1997, 36, 4751-4760); printed column heads enzymes | kcat (min-1) | Km (DAPA) (uM) | kcat/Km(DAPA) (M-1 s-1) | Km(ATP) (uM) | kcat/Km(ATP) (M-1 s-1). Table 2, enzyme row E12D; column kcat (min-1) = 6.97; column Km (DAPA) (uM) = 0.23; column kcat/Km(DAPA) (M-1 s-1) = 5.05 x 10^5. captured primary segment: DAPA | E12D DTBS | Km 0.23 uM | kcat 6.97 min^-1 | kcat/Km 5.05 x 10^5 M^-1 s^-1

raw_value_unit_evidence: Table 2, enzyme row E12D, substrate column set DAPA: Km (DAPA) (uM) = 0.23 uM; kcat (min-1) = 6.97 min^-1; kcat/Km(DAPA) (M-1 s-1) = 5.05 x 10^5 M^-1 s^-1.

row_label: Table 2, enzyme row E12D, column set for substrate DAPA


kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K37L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13000 and applied mutation signature K37Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters (Km, kcat) for the Wild-Type and Mutant DTBS Enzymes (pH 7.5, 25 C) Measured by Spectrophotometric Assay and [14C]CO2 Fixation Assay (Biochemistry 1997, 36, 4751-4760); printed column heads enzymes | kcat (min-1) | Km (DAPA) (uM) | kcat/Km(DAPA) (M-1 s-1) | Km(ATP) (uM) | kcat/Km(ATP) (M-1 s-1). Table 2, enzyme row K37Q; column kcat (min-1) = 3.2 x 10^-2; column Km (DAPA) (uM) = 30.4; column kcat/Km(DAPA) (M-1 s-1) = 1.75 x 10^1. captured primary segment: DAPA | K37Q DTBS | Km 30.4 uM | kcat 3.2 x 10^-2 min^-1 | kcat/Km 1.75 x 10^1 M^-1 s^-1

raw_value_unit_evidence: Table 2, enzyme row K37Q, substrate column set DAPA: Km (DAPA) (uM) = 30.4 uM; kcat (min-1) = 3.2 x 10^-2 min^-1; kcat/Km(DAPA) (M-1 s-1) = 1.75 x 10^1 M^-1 s^-1.

row_label: Table 2, enzyme row K37Q, column set for substrate DAPA


sequence_variant_note: Mutation signature S41A matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


column_label: Table 2: Kinetic Parameters (Km, kcat) for the Wild-Type and Mutant DTBS Enzymes (pH 7.5, 25 C) Measured by Spectrophotometric Assay and [14C]CO2 Fixation Assay (Biochemistry 1997, 36, 4751-4760); printed column heads enzymes | kcat (min-1) | Km (DAPA) (uM) | kcat/Km(DAPA) (M-1 s-1) | Km(ATP) (uM) | kcat/Km(ATP) (M-1 s-1). Table 2, enzyme row S41C; column kcat (min-1) = 3.29; column Km (DAPA) (uM) = 1.68; column kcat/Km(DAPA) (M-1 s-1) = 3.27 x 10^4. captured primary segment: DAPA | S41C DTBS | Km 1.68 uM | kcat 3.29 min^-1 | kcat/Km 3.27 x 10^4 M^-1 s^-1

raw_value_unit_evidence: Table 2, enzyme row S41C, substrate column set DAPA: Km (DAPA) (uM) = 1.68 uM; kcat (min-1) = 3.29 min^-1; kcat/Km(DAPA) (M-1 s-1) = 3.27 x 10^4 M^-1 s^-1.

row_label: Table 2, enzyme row S41C, column set for substrate DAPA


column_label: Table 2: Kinetic Parameters (Km, kcat) for the Wild-Type and Mutant DTBS Enzymes (pH 7.5, 25 C) Measured by Spectrophotometric Assay and [14C]CO2 Fixation Assay (Biochemistry 1997, 36, 4751-4760); printed column heads enzymes | kcat (min-1) | Km (DAPA) (uM) | kcat/Km(DAPA) (M-1 s-1) | Km(ATP) (uM) | kcat/Km(ATP) (M-1 s-1). Table 2, enzyme row T11V; column kcat (min-1) = 1.51; column Km (DAPA) (uM) = 0.34; column kcat/Km(DAPA) (M-1 s-1) = 7.40 x 10^4. captured primary segment: DAPA | T11V DTBS | Km 0.34 uM | kcat 1.51 min^-1 | kcat/Km 7.40 x 10^4 M^-1 s^-1

raw_value_unit_evidence: Table 2, enzyme row T11V, substrate column set DAPA: Km (DAPA) (uM) = 0.34 uM; kcat (min-1) = 1.51 min^-1; kcat/Km(DAPA) (M-1 s-1) = 7.40 x 10^4 M^-1 s^-1.

row_label: Table 2, enzyme row T11V, column set for substrate DAPA


column_label: Table 2: Kinetic Parameters (Km, kcat) for the Wild-Type and Mutant DTBS Enzymes (pH 7.5, 25 C) Measured by Spectrophotometric Assay and [14C]CO2 Fixation Assay (Biochemistry 1997, 36, 4751-4760); printed column heads enzymes | kcat (min-1) | Km (DAPA) (uM) | kcat/Km(DAPA) (M-1 s-1) | Km(ATP) (uM) | kcat/Km(ATP) (M-1 s-1). Table 2, enzyme row E12A; column kcat (min-1) = 4.61; column Km(ATP) (uM) = 0.33; column kcat/Km(ATP) (M-1 s-1) = 2.33 x 10^5. captured primary segment: ATP | E12A DTBS | Km 0.33 uM | kcat 4.61 min^-1 | kcat/Km 2.33 x 10^5 M^-1 s^-1

raw_value_unit_evidence: Table 2, enzyme row E12A, substrate column set ATP: Km(ATP) (uM) = 0.33 uM; kcat (min-1) = 4.61 min^-1; kcat/Km(ATP) (M-1 s-1) = 2.33 x 10^5 M^-1 s^-1.

row_label: Table 2, enzyme row E12A, column set for substrate ATP


column_label: Table 2: Kinetic Parameters (Km, kcat) for the Wild-Type and Mutant DTBS Enzymes (pH 7.5, 25 C) Measured by Spectrophotometric Assay and [14C]CO2 Fixation Assay (Biochemistry 1997, 36, 4751-4760); printed column heads enzymes | kcat (min-1) | Km (DAPA) (uM) | kcat/Km(DAPA) (M-1 s-1) | Km(ATP) (uM) | kcat/Km(ATP) (M-1 s-1). Table 2, enzyme row E12D; column kcat (min-1) = 6.97; column Km(ATP) (uM) = 2.38; column kcat/Km(ATP) (M-1 s-1) = 4.88 x 10^4. captured primary segment: ATP | E12D DTBS | Km 2.38 uM | kcat 6.97 min^-1 | kcat/Km 4.88 x 10^4 M^-1 s^-1

raw_value_unit_evidence: Table 2, enzyme row E12D, substrate column set ATP: Km(ATP) (uM) = 2.38 uM; kcat (min-1) = 6.97 min^-1; kcat/Km(ATP) (M-1 s-1) = 4.88 x 10^4 M^-1 s^-1.

row_label: Table 2, enzyme row E12D, column set for substrate ATP


substrate_name: GTP

source_db: skid

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

sequence_source: multiple

source_databases_merged: skid uniprot

substrate: GTP

source: skid


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


substrate_name: CTP

substrate: CTP


enzyme_display_name: carbapenam-3-carboxylate synthase

organism: Pectobacterium carotovorum

enzyme: carbapenam-3-carboxylate synthase


assay_conditions_summary: pH 7.8; 295.15 K; cofactor ATP


enzyme_display_name: 5-formyltetrahydrofolate cyclo-ligase

organism: Lacticaseibacillus casei

substrate_name: ATPgammaS

source_db: brenda

enzyme: 5-formyltetrahydrofolate cyclo-ligase

substrate: ATPgammaS

source: brenda


substrate_name: dATP

substrate: dATP


substrate_name: UTP

substrate: UTP


substrate_name: dTTP

substrate: dTTP


substrate_name: ITP

substrate: ITP


enzyme_display_name: 4-phosphopantoate--beta-alanine ligase

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

substrate_name: beta-alanine

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

enzyme: 4-phosphopantoate--beta-alanine ligase

substrate: beta-alanine


organism: Streptomyces clavuligerus

substrate_name: L-cysteine

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

substrate: L-cysteine


substrate_name: L-valine

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

substrate: L-valine


substrate_name: L-aminoadipate

substrate: L-aminoadipate


organism: Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255)

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

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


column_label: Abstract states the Km values for the three precursor substrates L-alpha-aminoadipic acid, L-cysteine and L-valine were determined as 45, 80 and 80 microM respectively.

raw_value_unit_evidence: Km raw_value=80 raw_unit=microM

row_label: Penicillium chrysogenum ACVS with L-cysteine

table_label: PubMed abstract PMID 9355751


enzyme_display_name: tenuazonic acid synthetase

organism: Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)

substrate_name: isoleucine

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

assay_conditions_summary: cofactor CoA

column_label: Results section 'Substrate specificity of TAS1' for Isoleucine: KM(app) raw_value=44.3 +/- 3.1 x 10^-2 raw_unit=mM expression with x 10^-2 multiplier; kcat context raw_value=14.9 +/- 0.3 x 10^-3 raw_unit=min^-1 expression with x 10^-3 multiplier. KM(app) normalized_value=0.443 normalized_unit=mM after applying x 10^-2; CatLog value=44.3 mM; CatLog/paper ratio=100.

row_label: Isoleucine

table_label: Results prose: Substrate specificity of TAS1; Supplementary Fig. 6 cited

enzyme: tenuazonic acid synthetase

substrate: isoleucine


substrate_name: acetoacetyl-CoA

column_label: Results section 'Substrate specificity of TAS1' for Acetoacetyl-CoA: KM(app) raw_value=1.2 +/- 0.1 x 10^-2 raw_unit=mM expression with x 10^-2 multiplier; kcat context raw_value=13.1 +/- 0.2 x 10^-3 raw_unit=min^-1 expression with x 10^-3 multiplier. KM(app) normalized_value=0.012 normalized_unit=mM after applying x 10^-2; CatLog value=1.2 mM; CatLog/paper ratio=100.

row_label: Acetoacetyl-CoA

substrate: acetoacetyl-CoA


column_label: Results section 'Substrate specificity of TAS1' for ATP: KM(app) raw_value=8.1 +/- 0.5 x 10^-2 raw_unit=mM expression with x 10^-2 multiplier; kcat context raw_value=15.3 +/- 0.2 x 10^-3 raw_unit=min^-1 expression with x 10^-3 multiplier. KM(app) normalized_value=0.081 normalized_unit=mM after applying x 10^-2; CatLog value=8.1 mM; CatLog/paper ratio=100.

row_label: ATP


organism: Arabidopsis thaliana


organism: Streptococcus pyogenes serotype M1

substrate_name: 5-CHO-THF-Glu3 (at pH 7.3 and 30 degrees Celsius)

proof_lines: kcat is 0.13 sec(-1) for formyltransferase with 5-CHO-THF or 5-CHO-THF-Glu3 as substrates (at pH 7.3 and 30 degrees Celsius).


organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

substrate_name: 5-CHO-THF (at pH 7.3 and 30 degrees Celsius)

proof_lines: kcat is 0.27 sec(-1) for formyltransferase with 5-CHO-THF or 5-CHO-THF-Glu3 as substrates (at pH 7.3 and 30 degrees Celsius).


substrate_name: Unknown

km_display: Not reported

proof_lines: kcat is 0.072 min(-1) for 7,8-diamino-pelargonic acid aminotransferase + dethiobiotin synthetase activities, and 1.85 min(-1) for 7,8-diamino-pelargonic acid aminotransferase activity only (at pH 7.5 and 30 degrees Celsius).

substrate: Unknown


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13000 and applied mutation signature K37R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters (Km, kcat) for the Wild-Type and Mutant DTBS Enzymes (pH 7.5, 25 C) Measured by Spectrophotometric Assay and [14C]CO2 Fixation Assay (Biochemistry 1997, 36, 4751-4760); printed column heads enzymes | kcat (min-1) | Km (DAPA) (uM) | kcat/Km(DAPA) (M-1 s-1) | Km(ATP) (uM) | kcat/Km(ATP) (M-1 s-1). Table 2, enzyme row K37R; column kcat (min-1) = 2.9 x 10^-3; column Km(ATP) (uM) = 7.44; column kcat/Km(ATP) (M-1 s-1) = 6.50 x 10^0. captured primary segment: ATP | K37R DTBS | Km 7.44 uM | kcat 2.9 x 10^-3 min^-1 | kcat/Km 6.50 x 10^0 M^-1 s^-1

raw_value_unit_evidence: Table 2, enzyme row K37R, substrate column set ATP: Km(ATP) (uM) = 7.44 uM; kcat (min-1) = 2.9 x 10^-3 min^-1; kcat/Km(ATP) (M-1 s-1) = 6.50 x 10^0 M^-1 s^-1.

row_label: Table 2, enzyme row K37R, column set for substrate ATP

substrate: ATP


column_label: Table 2: Kinetic Parameters (Km, kcat) for the Wild-Type and Mutant DTBS Enzymes (pH 7.5, 25 C) Measured by Spectrophotometric Assay and [14C]CO2 Fixation Assay (Biochemistry 1997, 36, 4751-4760); printed column heads enzymes | kcat (min-1) | Km (DAPA) (uM) | kcat/Km(DAPA) (M-1 s-1) | Km(ATP) (uM) | kcat/Km(ATP) (M-1 s-1). Table 2, enzyme row K37R; column kcat (min-1) = 2.9 x 10^-3; column Km (DAPA) (uM) = 143; column kcat/Km(DAPA) (M-1 s-1) = 3.38 x 10^-1. captured primary segment: DAPA | K37R DTBS | Km 143 uM | kcat 2.9 x 10^-3 min^-1 | kcat/Km 3.38 x 10^-1 M^-1 s^-1

raw_value_unit_evidence: Table 2, enzyme row K37R, substrate column set DAPA: Km (DAPA) (uM) = 143 uM; kcat (min-1) = 2.9 x 10^-3 min^-1; kcat/Km(DAPA) (M-1 s-1) = 3.38 x 10^-1 M^-1 s^-1.

row_label: Table 2, enzyme row K37R, column set for substrate DAPA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13000 and applied mutation signature K15Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters (Km, kcat) for the Wild-Type and Mutant DTBS Enzymes (pH 7.5, 25 C) Measured by Spectrophotometric Assay and [14C]CO2 Fixation Assay (Biochemistry 1997, 36, 4751-4760); printed column heads enzymes | kcat (min-1) | Km (DAPA) (uM) | kcat/Km(DAPA) (M-1 s-1) | Km(ATP) (uM) | kcat/Km(ATP) (M-1 s-1). Table 2, enzyme row K15Q; column kcat (min-1) = 5.4 x 10^-4; column Km (DAPA) (uM) = 11.1; column kcat/Km(DAPA) (M-1 s-1) = 8.10 x 10^-1. captured primary segment: DAPA | K15Q DTBS | Km 11.1 uM | kcat 5.4 x 10^-4 min^-1 | kcat/Km 8.10 x 10^-1 M^-1 s^-1

raw_value_unit_evidence: Table 2, enzyme row K15Q, substrate column set DAPA: Km (DAPA) (uM) = 11.1 uM; kcat (min-1) = 5.4 x 10^-4 min^-1; kcat/Km(DAPA) (M-1 s-1) = 8.10 x 10^-1 M^-1 s^-1.

row_label: Table 2, enzyme row K15Q, column set for substrate DAPA


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


enzyme_display_name: dapdiamide synthase

organism: Pantoea agglomerans

enzyme: dapdiamide synthase


organism: Homo sapiens

column_label: Table 1 row KmA under Human (A = CTP); Table 2 row CTP column Km

raw_value_unit_evidence: Table 1 Human (A = CTP): KmA 265 +/- 20 uM; Table 2 CTP: Km 265 +/- 20 uM

row_label: Table 1 column Human (A = CTP); Table 2 row CTP

table_label: ScienceDirect Table 1; ScienceDirect Table 2


assay_conditions_summary: pH 7.6; cofactor ATP

column_label: Table 1 row KmA under Human (A = ATP); Table 2 row ATP column Km

raw_value_unit_evidence: Table 1 Human (A = ATP): KmA 269 +/- 14 uM; Table 2 ATP: Km 269 +/- 14 uM

row_label: Table 1 column Human (A = ATP); Table 2 row ATP


substrate_name: fumarate

substrate: fumarate


substrate_name: succinate

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

assay_conditions_summary: pH 8; 295.15 K; cofactor ATP

substrate: succinate


organism: Mycoplasma pneumoniae

assay_conditions_summary: pH 6; 310.15 K; cofactor ATP


enzyme_display_name: O-ureido-D-serine cyclo-ligase

organism: Streptomyces lavendulae

substrate_name: D-homocysteine

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

column_label: Table 2 (Kinetic parameters of DcsG), substrate row D-Homocysteine; column Mean Km (mM) = 19; column Mean kcat (s^-1) = 860; column Mean kcat/Km (M^-1 s^-1) = 45,000; column Mean Kmapp for ATP (uM) = 23.

normalized_value_unit_evidence: Km: printed Table 2 cell 19 mM; the column head prints mM, so no unit conversion applies and the value carried here is 19.0 mM. kcat: printed Table 2 cell 860 s^-1; the column head prints s^-1, so no unit conversion applies and the value carried here is 860.0 s^(-1). kcat/Km: printed Table 2 cell 4.5 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell converts to 45.0 s^-1 mM^-1. Quotient disclosure for this cell group: 860 / 19 = 45.26315789473684 s^-1 mM^-1, and the printed efficiency cell is that same quotient carried to the two significant figures Table 2 uses.

raw_value_unit_evidence: Table 2, substrate row D-Homocysteine: Km = 19 mM; kcat = 860 s^-1; printed kcat/Km = 4.5 x 10^4 M^-1 s^-1 (the cell prints 45,000 with a printed standard deviation of 9,000).

row_label: Table 2, substrate row D-Homocysteine

table_label: Table 2: Kinetic parameters of DcsG (Antimicrobial Agents and Chemotherapy 2013, volume 57, number 6, pages 2603-2612); printed columns Mean Km (mM), Mean kcat (s^-1), Mean kcat/Km (M^-1 s^-1) and Mean Kmapp for ATP (uM)

enzyme: O-ureido-D-serine cyclo-ligase

substrate: D-homocysteine


substrate_name: O-ureido-D-serine

column_label: Table 2 (Kinetic parameters of DcsG), substrate row D-OUS; column Mean Km (mM) = 10; column Mean kcat (s^-1) = 2,200; column Mean kcat/Km (M^-1 s^-1) = 210,000; column Mean Kmapp for ATP (uM) = 73.

normalized_value_unit_evidence: Km: printed Table 2 cell 10 mM; the column head prints mM, so no unit conversion applies and the value carried here is 10.0 mM. kcat: printed Table 2 cell 2,200 s^-1; the column head prints s^-1, so no unit conversion applies and the value carried here is 2200.0 s^(-1). kcat/Km: printed Table 2 cell 210,000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 210,000 / 1000 = 210.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate row D-OUS: Km = 10 mM; kcat = 2,200 s^-1; printed kcat/Km = 210,000 M^-1 s^-1.

row_label: Table 2, substrate row D-OUS

substrate: O-ureido-D-serine


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


enzyme_display_name: coenzyme F420-0:L-glutamate ligase

column_label: The ACS full text states that at 50 C, apparent kinetic parameters of CofE using F420-0 as substrate were Km = 1.0 +/- 0.15 uM and Vmax = 2.4 +/- 0.09 nmol min^-1 mg^-1.

raw_value_unit_evidence: Km raw_value=1.0 +/- 0.15 raw_unit=uM

row_label: CofE using F420-0 as substrate to produce F420-2

table_label: ACS Biochemistry full text kinetic-parameter prose following Table 2

enzyme: coenzyme F420-0:L-glutamate ligase


column_label: The ACS full text states that using F420-1 as substrate, the parameters were Km = 0.21 +/- 0.05 uM and Vmax = 0.96 +/- 0.07 nmol min^-1 mg^-1.

raw_value_unit_evidence: Km raw_value=0.21 +/- 0.05 raw_unit=uM

row_label: CofE using F420-1 as substrate to produce F420-2


organism: Geminocystis herdmanii PCC 6308

substrate_name: L-arginine

verification_status: unverified

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

source_databases_merged: brenda uniprot

substrate: L-arginine

status: unverified


organism: Methanocaldococcus jannaschii

substrate_name: coenzyme gamma-F420-2

substrate: coenzyme gamma-F420-2


organism: Geminocystis herdmanii (strain PCC 6308)

substrate_name: L-aspartic acid

substrate: L-aspartic acid


assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines:
pH 7.5
Raw SKiD Env: Temp=-----, pH=7.5

source_databases_merged: brenda skid


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


enzyme_display_name: D-alanine--D-serine ligase

organism: Enterococcus casseliflavus

enzyme: D-alanine--D-serine ligase


enzyme_display_name: jasmonoyl--L-amino acid ligase

substrate_name: (-)-jasmonate

enzyme: jasmonoyl--L-amino acid ligase

substrate: (-)-jasmonate


organism: Bacillus cereus


organism: Hapsidospora chrysogena


enzyme_display_name: tetrahydrofolate synthase

organism: Escherichia coli

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

enzyme: tetrahydrofolate synthase


substrate_name: 5,6,7,8-tetrahydrofolic acid

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

substrate: 5,6,7,8-tetrahydrofolic acid


assay_conditions_summary: pH 9.8; cofactor ATP

proof_lines: mutant D154A, pH 9.8 cosubstrate 7,8-dihydropteroate

proof_lines: mutant D154A, pH 9.8, cosubstrate 5,6,7,8-tetrahydrofolic acid


proof_lines: mutant A155H, pH 9.8 cosubstrate 7,8-dihydropteroate

proof_lines: mutant A155H, pH 9.8, cosubstrate 5,6,7,8-tetrahydrofolic acid


substrate_name: L-Glu

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

proof_lines: mutant A155H, pH 9.8, cosubstrate 7,8-dihydropteroate

substrate: L-Glu


proof_lines: chimera containing N-terminal residues 1-81 of Escherichia coli enzyme, residues 72-82 of Lactobacillus casei enzyme, and residues 93-422 of Escherichia coli enzyme, pH 9.8


proof_lines: chimera containing N-terminal residues 1-298 of Lactobacillus casei enzyme, residues 288-422 of Escherichia coli enzyme, pH 9.8


proof_lines: mutant A155W, pH 9.8 cosubstrate 7,8-dihydropteroate


organism: Lacticaseibacillus casei

assay_conditions_summary: pH 6; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K120A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


enzyme_display_name: L-alanine--L-anticapsin ligase

organism: Bacillus subtilis

substrate_name: L-alanine

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

proof_lines:
pH 7.1, 37°C, mutant enzyme Y75F
pH 7.7, 37°C, mutant enzyme Y75F

enzyme: L-alanine--L-anticapsin ligase

substrate: L-alanine


substrate_name: L-phenylalanine

proof_lines:
pH 7.1, 37°C, mutant enzyme
pH 7.7, 37°C, mutant enzyme

substrate: L-phenylalanine


proof_lines:
pH 7.1, 37°C, wild-type enzyme
pH 7.7, 37°C, wild-type enzyme


ki_unit: mM


substrate_name: L-Ala-D-Glu

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

substrate: L-Ala-D-Glu


substrate_name: L-Ala-gamma-D-Glu-L-Lys

substrate: L-Ala-gamma-D-Glu-L-Lys


substrate_name: L-Ala-gamma-D-Glu-L-Lys-D-Ala

substrate: L-Ala-gamma-D-Glu-L-Lys-D-Ala


assay_conditions_summary: pH 8.4; 310.15 K; cofactor ATP


substrate_name: UDP-N-alpha-D-acetylmuramate

substrate: UDP-N-alpha-D-acetylmuramate


substrate_name: methotrexate

proof_lines:
wild type enzyme from mitochondrion
wild type enzyme from cytosol

substrate: methotrexate


substrate_name: Glu

substrate: Glu


organism: Mycobacterium tuberculosis

substrate_name: ATP

substrate: ATP


assay_conditions_summary: pH 7.7; cofactor ATP


substrate_name: succinate

substrate: succinate


substrate_name: fumarate

substrate: fumarate


substrate_name: L-valine

substrate: L-valine


substrate_name: L-isoleucine

substrate: L-isoleucine


substrate_name: L-leucine

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

substrate: L-leucine


smiles: CC(C(CCCCCC(=O)[O-])N)N


substrate_name: TTP

substrate: TTP


substrate_name: GTP

substrate: GTP


substrate_name: UTP

substrate: UTP


substrate_name: CTP

substrate: CTP


substrate_name: ITP

substrate: ITP


organism: Salmonella enterica


assay_conditions_summary: pH 7.7; 310.15 K; cofactor ATP


organism: Lysinibacillus sphaericus


enzyme_display_name: tubulin--tyrosine ligase

organism: Bos taurus

substrate_name: untyrosinated tubulin

enzyme: tubulin--tyrosine ligase

substrate: untyrosinated tubulin


substrate_name: L-Tyr

substrate: L-Tyr


enzyme_display_name: N-acetylaspartylglutamate synthase

organism: Mus musculus

substrate_name: N-acetyl-L-aspartate

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

proof_lines:
pH 8.0, 30°C
at pH 8.0 and 37°C

enzyme: N-acetylaspartylglutamate synthase

substrate: N-acetyl-L-aspartate


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines:
pH 8.0, 30°C
with 5 mM MgATP, at pH 8.0 and 37°C


substrate_name: L-glutamate

substrate: L-glutamate


substrate_name: citrate

substrate: citrate


substrate_name: L-glutamine

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

assay_conditions_summary: pH 9; 310.15 K; cofactor ATP

substrate: L-glutamine


substrate_name: ATP

substrate: ATP


substrate_name: L-alanine

substrate: L-alanine


substrate_name: (7R,8S)-7,8-diaminopelargonic acid

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

substrate: (7R,8S)-7,8-diaminopelargonic acid


organism: Lathyrus oleraceus


substrate_name: L-Glu

substrate: L-Glu


proof_lines: mutant enzyme Y152A, in 100 mM MES, pH 6.0, at 37°C


proof_lines: wild type enzyme, in 100 mM MES, pH 6.0, at 37°C


proof_lines: mutant enzyme Y152F, in 100 mM MES, pH 6.0, at 37°C


organism: Homo sapiens


substrate_name: aminopterin

substrate: aminopterin


substrate_name: L-Phe

substrate: L-Phe


substrate_name: tyramine

substrate: tyramine


organism: Penicillium chrysogenum

substrate_name: L-aminoadipate

substrate: L-aminoadipate


substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: L-valine

substrate: L-valine


substrate_name: ATPgammaS

substrate: ATPgammaS


organism: Oryctolagus cuniculus


substrate_name: CTP

substrate: CTP


substrate_name: UTP

substrate: UTP


proof_lines: chimera containing N-terminal residues 1-71 of Lactobacillus casei enzyme, residues 82-93 of Escherichia coli enzyme, and residues 83-428 of Lactobacillus casei enzyme, pH 9.8


assay_conditions_summary: pH 9.75; cofactor ATP

proof_lines: reaction with 10-formyl-5,6,7,8-tetrahydropteroyl-Glu + Glu

proof_lines: pH 9.75, temperature conditions not mentioned


substrate_name: (6RS)-5,6,7,8-tetrahydrofolic acid

substrate: (6RS)-5,6,7,8-tetrahydrofolic acid


organism: Gallus gallus


assay_conditions_summary: cofactor ATP


proof_lines: Km-value is constant over the pH-range 5.0-7.5


assay_conditions_summary: pH 6; 301.15 K; cofactor ATP


organism: Ovis aries


organism: Rattus norvegicus


organism: Saccharomyces cerevisiae


assay_conditions_summary: pH 7; 303.15 K; cofactor ATP


proof_lines:
cytosolic enzyme
mitochondrial enzyme
at 37°C in 100 mM MES, pH 6.0


organism: Synechocystis sp. PCC 6803

assay_conditions_summary: pH 8.2; 301.15 K; cofactor ATP


substrate_name: L-aspartic acid

substrate: L-aspartic acid


organism: Sus scrofa

substrate_name: dihydroaminopterin

substrate: dihydroaminopterin


substrate_name: pteroylmonoglutamate

substrate: pteroylmonoglutamate


organism: Arabidopsis thaliana

mutation_signature: truncated recombinant enzyme

mutation_type: truncation

proof_lines: truncated recombinant enzyme, pH 6.0, 23°C


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: Glu

substrate: Glu


enzyme_display_name: staphyloferrin B synthase

organism: Staphylococcus aureus

enzyme: staphyloferrin B synthase


organism: Corynebacterium sp.

substrate_name: Tetrahydropteroyl-L-glutamate; n-1 n-1 n-1 L-Glutamate; n-1 n-1 n-1 ATP

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

proof_lines: ATP L-Glu


substrate_name: ATP

substrate: ATP


assay_conditions_summary: pH 8.7; cofactor ATP

proof_lines:
pH 8.7
reaction with aminopterin + ATP


substrate_name: methotrexate-Glu

substrate: methotrexate-Glu


organism: Escherichia coli

substrate_name: Unknown

substrate: Unknown


substrate_name: methotrexate

substrate: methotrexate


proof_lines:
cytosolic enzyme
mitochondrial enzyme


organism: Pantoea agglomerans


enzyme_display_name: oxalate--CoA ligase

substrate_name: oxalate

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: oxalate--CoA ligase

substrate: oxalate


enzyme_display_name: lanosterol synthase

enzyme: lanosterol synthase


organism: Lacticaseibacillus casei

proof_lines: chimera containing N-terminal residues 1-81 of Escherichia coli enzyme, residues 72-82 of Lactobacillus casei enzyme, and residues 93-422 of Escherichia coli enzyme, pH 9.8


enzyme_display_name: arginine--tRNA ligase

substrate_name: Arg

proof_lines:
aminoacylation of tRNAArg-C-C-A(3'NH2)
aminoacylation of tRNAArg-C-C-A
aminoacylation of tRNAArg-C-C-A, Arg

enzyme: arginine--tRNA ligase

substrate: Arg


enzyme_display_name: glucose-6-phosphate isomerase

substrate_name: fructose 6-phosphate

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

proof_lines: values of 0.11 mM, 0.15 mM and 0.23 mM are determined by different autors

enzyme: glucose-6-phosphate isomerase

substrate: fructose 6-phosphate


enzyme_display_name: phosphoribosylanthranilate isomerase

proof_lines: pH 7.5, 25°C, recombinant xPRAI, expressed in E. coli

proof_lines: pH 7.5, 25°C, recombinant xPRAI, expressed in Escherichia coli

enzyme: phosphoribosylanthranilate isomerase


enzyme_display_name: inositol-3-phosphate synthase

proof_lines:
at pH 7.0 and 37°C
pH 5.5

enzyme: inositol-3-phosphate synthase


enzyme_display_name: serine--tRNA ligase

substrate_name: L-seryl-tRNASer

enzyme: serine--tRNA ligase

substrate: L-seryl-tRNASer


enzyme_display_name: leucine--tRNA ligase

enzyme: leucine--tRNA ligase


substrate_name: D-glucose 6-phosphate

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

substrate: D-glucose 6-phosphate


enzyme_display_name: methionine--tRNA ligase

substrate_name: Met

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

enzyme: methionine--tRNA ligase

substrate: Met


enzyme_display_name: mannose-6-phosphate isomerase

substrate_name: mannose 6-phosphate

enzyme: mannose-6-phosphate isomerase

substrate: mannose 6-phosphate


enzyme_display_name: DNA 5'-3' helicase

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

enzyme: DNA 5'-3' helicase


proof_lines: recombinant xPRAI, expressed in Escherichia coli


enzyme_display_name: adenylate cyclase

enzyme: adenylate cyclase


substrate_name: dATP

substrate: dATP


enzyme_display_name: tyrosine--tRNA ligase

substrate_name: tRNACUA

proof_lines: mutant P320A/D321A, 37°C, pH not specified in the publication

enzyme: tyrosine--tRNA ligase

substrate: tRNACUA


enzyme_display_name: cellobiose epimerase

organism: Saccharophagus degradans

substrate_name: lactose

proof_lines: pH and temperature not specified in the publication

enzyme: cellobiose epimerase

substrate: lactose


enzyme_display_name: methylmalonyl-CoA mutase

organism: Saccharopolyspora erythraea

assay_conditions_summary: cofactor CoA

enzyme: methylmalonyl-CoA mutase


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

organism: Sagittula stellata

smiles: CSCCC(=O)[O-]

assay_conditions_summary: pH 8; 313.15 K; cofactor CoA

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


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

organism: Salmonella enterica

proof_lines:
pH 7.0, 25°C
native

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


enzyme_display_name: glutamine synthetase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

enzyme: glutamine synthetase


enzyme_display_name: acetate--CoA ligase

substrate_name: acetate

assay_conditions_summary: pH 7.7; 310.15 K; cofactor CoA

proof_lines:
isoform Acs2, at pH 7.7 and 37°C
isoform Acs3, at pH 7.7 and 37°C
isoform Acs1, at pH 7.7 and 37°C

enzyme: acetate--CoA ligase

substrate: acetate


enzyme_display_name: alanine racemase

organism: Salmonella enteritidis PT4 P125109

substrate_name: D-alanine

enzyme: alanine racemase

substrate: D-alanine


substrate_name: D-Ala

proof_lines:
dadB encoded enzyme
alr encoded enzyme
alr gene encoded

substrate: D-Ala


enzyme_display_name: D-cysteine desulfhydrase

substrate_name: D-cysteine

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

proof_lines: recombinant His6-tagged enzyme, pH and temperature not specified in the publication

enzyme: D-cysteine desulfhydrase

substrate: D-cysteine


enzyme_display_name: triose-phosphate isomerase

organism: Schistosoma japonicum

substrate_name: D-glyceraldehyde 3-phosphate

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

enzyme: triose-phosphate isomerase

substrate: D-glyceraldehyde 3-phosphate


enzyme_display_name: cysteine-S-conjugate beta-lyase

substrate_name: cystathionine

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

enzyme: cysteine-S-conjugate beta-lyase

substrate: cystathionine


enzyme_display_name: chorismate mutase

organism: Selaginella moellendorffii

substrate_name: chorismate

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication, recombinant enzyme

enzyme: chorismate mutase

substrate: chorismate


organism: Shigella dysenteriae


organism: Schizosaccharomyces pombe

substrate_name: ATP

assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP

substrate: ATP


enzyme_display_name: alkylmercury lyase

organism: Serratia marcescens

substrate_name: p-hydroxymercuribenzoate

proof_lines:
pH 8.0, in presence of glutathione
pH 8.0, in presence of cysteine

enzyme: alkylmercury lyase

substrate: p-hydroxymercuribenzoate


enzyme_display_name: 4-hydroxyproline epimerase

organism: Sinorhizobium meliloti

proof_lines: pH not specified in the publication, 30°C, recombinant enzyme

enzyme: 4-hydroxyproline epimerase


organism: Solanum chacoense

proof_lines:
plastidic triosephosphate isomerase
cytoplasmic triosephosphate isomerase


sequence_source: UniProtKB O59828 FASTA

assay_conditions_summary: pH 9


enzyme_display_name: serine racemase

organism: Solanum lycopersicum

substrate_name: L-serine

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

proof_lines: pH 8.0, temperature not specified in the publication

enzyme: serine racemase

substrate: L-serine


enzyme_display_name: L-3-cyanoalanine synthase

organism: Solanum tuberosum

substrate_name: Sulfide

enzyme: L-3-cyanoalanine synthase

substrate: Sulfide


enzyme_display_name: isopentenyl-diphosphate Delta-isomerase

substrate_name: isopentenyl diphosphate

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

enzyme: isopentenyl-diphosphate Delta-isomerase

substrate: isopentenyl diphosphate


enzyme_display_name: hydantoin racemase

substrate_name: L-benzylhydantoin

enzyme: hydantoin racemase

substrate: L-benzylhydantoin


substrate_name: Chorismate

proof_lines:
in presence of Trp
in absence of Trp

substrate: Chorismate


enzyme_display_name: holocytochrome-c synthase

organism: Saccharomyces cerevisiae

substrate_name: Unknown

enzyme: holocytochrome-c synthase

substrate: Unknown


enzyme_display_name: ribose-5-phosphate isomerase

organism: Spinacia oleracea

substrate_name: D-ribose 5-phosphate

enzyme: ribose-5-phosphate isomerase

substrate: D-ribose 5-phosphate


organism: Sorghum sp.


enzyme_display_name: phosphomannomutase

organism: Sphingomonas sanxanigenens

substrate_name: alpha-D-mannose 1-phosphate

proof_lines: recombinant His-tagged enzyme, pH 7.6, temperature not specified in the publication

enzyme: phosphomannomutase

substrate: alpha-D-mannose 1-phosphate


enzyme_display_name: ribulose-phosphate 3-epimerase

enzyme: ribulose-phosphate 3-epimerase


substrate_name: D-ribulose 5-phosphate

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

substrate: D-ribulose 5-phosphate


substrate_name: S-adenosyl-L-methionine

proof_lines:
at pH 8.5 and 30°C
Km increases from pH 7.5 to 9.5

substrate: S-adenosyl-L-methionine


enzyme_display_name: glutamate racemase

organism: Staphylococcus aureus

substrate_name: D-glutamate

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

enzyme: glutamate racemase

substrate: D-glutamate


enzyme_display_name: methionine--tRNA ligase

enzyme: methionine--tRNA ligase


assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH

proof_lines: aerobic, presence of dithionite, pH 7.0, 37°C

proof_lines: anaerobic, presence of NADPH, pH 7.0, 37°C


enzyme_display_name: adenylate cyclase

organism: Spodoptera frugiperda

enzyme: adenylate cyclase


substrate_name: D-alanine

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

substrate: D-alanine


enzyme_display_name: isoleucine--tRNA ligase

substrate_name: tRNAIle

proof_lines: below, tRNAIle aminoacylation reaction, pH 7.9, 22°C

proof_lines: pH 7.9, 22°C, in complex with the enzyme and Ile, in analogy to the reaction intermediate

enzyme: isoleucine--tRNA ligase

substrate: tRNAIle


substrate_name: alpha-D-Glucose 1-phosphate

proof_lines:
peak I enzyme
peak II enzyme

substrate: alpha-D-Glucose 1-phosphate


organism: Staphylococcus haemolyticus

substrate_name: L-cystathionine

proof_lines: pH 8.0, 37°C, purified recombinant enzyme

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

substrate: L-cystathionine


enzyme_display_name: UDP-N-acetylmuramate--L-alanine ligase

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

enzyme: UDP-N-acetylmuramate--L-alanine ligase


organism: Streptococcus mutans


enzyme_display_name: alanine--tRNA ligase

organism: Streptococcus pneumoniae

substrate_name: lipid II L-Ser

proof_lines:
strain 159
strain Pn16

enzyme: alanine--tRNA ligase

substrate: lipid II L-Ser


enzyme_display_name: asparagine--tRNA ligase

substrate_name: tRNAAsn

enzyme: asparagine--tRNA ligase

substrate: tRNAAsn


enzyme_display_name: o-succinylbenzoate--CoA ligase

proof_lines: pH and temperature not specified in the publication

enzyme: o-succinylbenzoate--CoA ligase


enzyme_display_name: acetate--CoA ligase

substrate_name: acetate

enzyme: acetate--CoA ligase

substrate: acetate


enzyme_display_name: alanine racemase

enzyme: alanine racemase


organism: Streptococcus pyogenes


enzyme_display_name: UDP-glucose 4-epimerase

substrate_name: UDPgalactose

enzyme: UDP-glucose 4-epimerase

substrate: UDPgalactose


enzyme_display_name: nephthenol synthase

organism: Streptomyces sp.

substrate_name: geranylgeranyl diphosphate

enzyme: nephthenol synthase

substrate: geranylgeranyl diphosphate


enzyme_display_name: xylose isomerase

organism: Streptomyces corchorusii

substrate_name: D-glucose

enzyme: xylose isomerase

substrate: D-glucose


organism: Streptococcus iniae


enzyme_display_name: chorismate mutase

organism: Streptomyces venezuelae

substrate_name: chorismate

enzyme: chorismate mutase

substrate: chorismate


enzyme_display_name: N-acylglucosamine 2-epimerase

organism: Sus scrofa

substrate_name: N-acetyl-D-mannosamine

proof_lines: in presence of saturating concentrations of ATP

enzyme: N-acylglucosamine 2-epimerase

substrate: N-acetyl-D-mannosamine


enzyme_display_name: selenocysteine lyase

substrate_name: L-selenocysteine

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

enzyme: selenocysteine lyase

substrate: L-selenocysteine


enzyme_display_name: isopentenyl-diphosphate Delta-isomerase

substrate_name: isopentenyl diphosphate

enzyme: isopentenyl-diphosphate Delta-isomerase

substrate: isopentenyl diphosphate


enzyme_display_name: inositol-3-phosphate synthase

substrate_name: glucose 6-phosphate

enzyme: inositol-3-phosphate synthase

substrate: glucose 6-phosphate


substrate_name: ATP

substrate: ATP


organism: Streptomyces violaceoruber

substrate_name: D-xylose

proof_lines:
with 1 mM Co2+
with 10 mM Mg2+

substrate: D-xylose


enzyme_display_name: succinate--CoA ligase (GDP-forming)

substrate_name: succinate

assay_conditions_summary: pH 7.4; 294.15 K; cofactor CoA

enzyme: succinate--CoA ligase (GDP-forming)

substrate: succinate


enzyme_display_name: tubulin--tyrosine ligase

substrate_name: L-Dopa

enzyme: tubulin--tyrosine ligase

substrate: L-Dopa


enzyme_display_name: tetrahydrofolate synthase

proof_lines: reaction with 5,6,7,8-tetrahydropteroyl-Glu + ATP

enzyme: tetrahydrofolate synthase


enzyme_display_name: microtubule-severing ATPase

organism: Strongylocentrotus purpuratus

enzyme: microtubule-severing ATPase


enzyme_display_name: thromboxane-A synthase

enzyme: thromboxane-A synthase


substrate_name: L-Phe

substrate: L-Phe


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: mannose-6-phosphate isomerase

substrate_name: mannose 6-phosphate

enzyme: mannose-6-phosphate isomerase

substrate: mannose 6-phosphate


enzyme_display_name: cellobiose epimerase

organism: Teredinibacter turnerae

substrate_name: cellobiose

enzyme: cellobiose epimerase

substrate: cellobiose


enzyme_display_name: phosphoacetylglucosamine mutase

substrate_name: N-acetylglucosamine 1-phosphate

enzyme: phosphoacetylglucosamine mutase

substrate: N-acetylglucosamine 1-phosphate


substrate_name: glucose 1-phosphate

substrate: glucose 1-phosphate


enzyme_display_name: glutamate--tRNA ligase

organism: Tetradesmus obliquus

substrate_name: Glu

enzyme: glutamate--tRNA ligase

substrate: Glu


enzyme_display_name: aldose 1-epimerase

substrate_name: alpha-D-glucose

proof_lines: alpha-D-glucose, kidney, embryo and adult

enzyme: aldose 1-epimerase

substrate: alpha-D-glucose


enzyme_display_name: guanylate cyclase

organism: Tetrahymena pyriformis

substrate_name: GTP

enzyme: guanylate cyclase

substrate: GTP


substrate_name: lactose

substrate: lactose


enzyme_display_name: methionine racemase

organism: Thermococcus litoralis

substrate_name: L-methionine

enzyme: methionine racemase

substrate: L-methionine


enzyme_display_name: arginine--tRNA ligase

organism: Thermus thermophilus

substrate_name: tRNAArg

proof_lines: adenine at position 20 of the tRNAArg is required for activity, pH 7.5, 65°C

enzyme: arginine--tRNA ligase

substrate: tRNAArg


enzyme_display_name: chaperonin ATPase

organism: Thermoplasma acidophilum

assay_conditions_summary: pH 7.5; 328.15 K; cofactor ATP

proof_lines: wild type enzyme, with rhamnose dehydrogenase as protein substrate, at pH 7.5 and 55°C

enzyme: chaperonin ATPase


enzyme_display_name: alanine--tRNA ligase

substrate_name: tmRNA

enzyme: alanine--tRNA ligase

substrate: tmRNA


enzyme_display_name: isopentenyl-diphosphate Delta-isomerase

substrate_name: isopentenyl diphosphate

enzyme: isopentenyl-diphosphate Delta-isomerase

substrate: isopentenyl diphosphate


substrate_name: ATP

proof_lines: ATPase rate per unit mass of chaperonin, in the absence of K+, only alpha subunits

proof_lines: ATPase rate per unit mass of chaperonin, in the absence of K+, alpha,beta subunits

proof_lines: ATPase rate per unit mass of chaperonin, 100 mM KCl, only alpha subunits

substrate: ATP


enzyme_display_name: aspartate--tRNA ligase

substrate_name: tRNAAsn

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

enzyme: aspartate--tRNA ligase

substrate: tRNAAsn


enzyme_display_name: maltose alpha-D-glucosyltransferase

substrate_name: maltose

proof_lines: recombinant immobilized enzyme, pH 8.0, 50°C

enzyme: maltose alpha-D-glucosyltransferase

substrate: maltose


enzyme_display_name: threonine--tRNA ligase

substrate_name: tRNAThr

proof_lines: of Thermus thermophilus, , depending on temperature

enzyme: threonine--tRNA ligase

substrate: tRNAThr


enzyme_display_name: glycine--tRNA ligase

substrate_name: tRNAGly

proof_lines:
native substrate from E. coli
native substrate from yeast

enzyme: glycine--tRNA ligase

substrate: tRNAGly


proof_lines: in 200 mM HEPES (pH 7.0) containing 2 mM MgCl2, 0.04 mM FMN, 2 mM NADPH, at 37°C


enzyme_display_name: isoleucine--tRNA ligase

substrate_name: tRNAIle

enzyme: isoleucine--tRNA ligase

substrate: tRNAIle


enzyme_display_name: methionine gamma-lyase

organism: Treponema denticola

enzyme: methionine gamma-lyase


substrate_name: Asp

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines: 37°C and 70°C, tRNA aminoacylation, enzyme form AspRS2

proof_lines: 37°C, tRNA aminoacylation, enzyme form AspRS1

substrate: Asp


substrate_name: L-cysteine

substrate: L-cysteine


enzyme_display_name: glutamate racemase

substrate_name: D-glutamate

enzyme: glutamate racemase

substrate: D-glutamate


enzyme_display_name: triose-phosphate isomerase

organism: Trichomonas vaginalis

substrate_name: D-glyceraldehyde 3-phosphate

enzyme: triose-phosphate isomerase

substrate: D-glyceraldehyde 3-phosphate


organism: Trichormus variabilis ATCC 29413

substrate_name: L-Arg

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

substrate: L-Arg


enzyme_display_name: glutamine synthetase

organism: Triticum aestivum

assay_conditions_summary: cofactor ATP

proof_lines: in the presence of 1 mM L-glutamate, pH and temperature not specified in the publication

proof_lines: in the presence of 3.5 mM L-glutamate, pH and temperature not specified in the publication

proof_lines: in the presence of 8 mM L-glutamate, pH and temperature not specified in the publication

enzyme: glutamine synthetase


enzyme_display_name: glucose-6-phosphate isomerase

substrate_name: fructose 6-phosphate

proof_lines: fructose 6-phosphate, enzyme form PGI II

enzyme: glucose-6-phosphate isomerase

substrate: fructose 6-phosphate


organism: Trichormus variabilis

substrate_name: Glu

proof_lines:
enzyme from strain SA0, pH 6.8
enzyme from strain SA0, pH 7.5
enzyme from strain SA1, pH 6.8

substrate: Glu


organism: Trypanosoma brucei

substrate_name: Variant-surface-glycoprotein

proof_lines:
37°C, deacylated enzyme
37°C, acylated enzyme
pH 8

substrate: Variant-surface-glycoprotein


enzyme_display_name: long-chain-fatty-acid--CoA ligase

substrate_name: tetradecanoate

smiles: CCCCCCCCCCCCCC(=O)[O-]

proof_lines:
enzyme TbACS1
enzyme TbACS3
enzyme TbACS4

enzyme: long-chain-fatty-acid--CoA ligase

substrate: tetradecanoate


enzyme_display_name: UniProt Q9NRF8

organism: Homo sapiens

substrate_name: L-Gln

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt Q9NRF8

substrate: L-Gln


substrate_name: UTP

substrate: UTP


enzyme_display_name: UniProt P0A7D4

organism: Escherichia coli

substrate_name: hydroxylamine

smiles: NO

enzyme: UniProt P0A7D4

substrate: hydroxylamine


enzyme_display_name: lysine--tRNA ligase

substrate_name: Unknown

enzyme: lysine--tRNA ligase

substrate: Unknown


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


enzyme_display_name: serine--tRNA ligase

substrate_name: tRNASecUCA

enzyme: serine--tRNA ligase

substrate: tRNASecUCA


organism: Trypanosoma brucei brucei


organism: Oryctolagus cuniculus

substrate_name: 5-phosphoribosyl diphosphate

substrate: 5-phosphoribosyl diphosphate


substrate_name: ATP

substrate: ATP


substrate_name: imidazoleacetate

substrate: imidazoleacetate


enzyme_display_name: adenylate cyclase

organism: Trypanosoma cruzi

enzyme: adenylate cyclase


enzyme_display_name: ribose-5-phosphate--ammonia ligase

organism: Gallus gallus

enzyme: ribose-5-phosphate--ammonia ligase


enzyme_display_name: adenylosuccinate synthase

organism: Rattus norvegicus

substrate_name: Asp

proof_lines:
L-Asp
skeletal muscle
muscle enzyme

enzyme: adenylosuccinate synthase

substrate: Asp


substrate_name: GTP

proof_lines:
muscle enzyme
liver acidic type L isozyme
heart enzyme

substrate: GTP


substrate_name: IMP

proof_lines:
liver acidic type L isozyme
heart enzyme
muscle enzyme

substrate: IMP


enzyme_display_name: urea carboxylase

organism: Oleomonas sagaranensis

substrate_name: ATP; Urea; Hydrogencarbonate

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

enzyme: urea carboxylase

substrate: ATP; Urea; Hydrogencarbonate


sequence_variant_note: Mutation signature V273N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.7, 25°C, mutant V273N, hydroxylamine as substrate


sequence_variant_note: Mutation signature V273T could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature V273A 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_ec_organism_consensus_sequence and applied mutation signature T301A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature T129A to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature T128A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


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


proof_lines: pH 7.7, 25°C, mutant V273A, hydroxylamine as substrate


proof_lines: pH 7.7, 25°C, mutant V273T, hydroxylamine as substrate


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


proof_lines: pH 7.7, 25°C, mutant T301A, hydroxylamine as substrate


substrate_name: L-aspartate

substrate: L-aspartate


sequence_variant_note: Mutation signature N38A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature H41N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
pH 7.7, 25°C, mutant H41N
mutant H41N


sequence_variant_note: Mutation signature N38D could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
pH 7.7, 25°C, mutant N38D
pH 5.6, 25°C, mutant N38D


sequence_variant_note: Mutation signature N38E could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +7, so it is treated as a source-provided variant sequence.


proof_lines:
pH 5.6, 25°C, wild-type
pH 7.7, 25°C, wild-type
pH 7.8, 25°C, wild-type


sequence_variant_note: Mutation signature R419L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature T42A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: aspartate

substrate: aspartate


proof_lines:
pH 5.6, 25°C, mutant N38D
pH 7.7, 25°C, mutant N38D


substrate_name: alpha-D-glucose 6-phosphate

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

proof_lines: glucose 6-phosphate, enzyme form PGI I and PGI II

substrate: alpha-D-glucose 6-phosphate


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -2, so it is treated as a source-provided variant sequence.

proof_lines:
IMP, mutant Q224E
Asp, mutant Q224E


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -4, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q34E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature S240A 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_ec_organism_consensus_sequence and applied mutation signature L228A to reconstruct the assayed variant sequence.


proof_lines:
GTP, mutant S240A
mutant S240A


enzyme_display_name: CTP synthase (glutamine hydrolyzing)

sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature K306A to reconstruct the assayed variant sequence.

smiles: N

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: mutant K306A, presence of 3 mM ATP, 2 mM UTP

proof_lines: mutant K306A, presence of 1 mM ATP, 1 mM UTP

source_databases_merged: brenda oed

enzyme: CTP synthase (glutamine hydrolyzing)


substrate_name: glutamine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K306A to reconstruct the assayed variant sequence.

substrate: glutamine


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature K297A to reconstruct the assayed variant sequence.

proof_lines: mutant K297A, presence of 1 mM ATP, 1 mM UTP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K297A 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.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature V60F to reconstruct the assayed variant sequence.

proof_lines: mutant V60F, modified by 6-diazo-5-oxo-L-norleucine, pH 8, 37°C


substrate_name: L-glutamine

substrate: L-glutamine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature V60W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature V60D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature V60A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature V60C to reconstruct the assayed variant sequence.


organism: Kluyveromyces lactis

substrate_name: Urea

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S177A to reconstruct the assayed variant sequence.

proof_lines: mutant S177A, pH 8.0, temperature not specified in the publication

substrate: Urea


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K1605A to reconstruct the assayed variant sequence.

proof_lines: mutant K1605A, pH 8.0, temperature not specified in the publication

proof_lines: mutant enzyme K1605A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G559E/G572E to reconstruct the assayed variant sequence.

proof_lines: mutant G559E/G572E, pH 8.0, temperature not specified in the publication


proof_lines: isolated urea carboxyxlase domain plus allophanate hydrolase domain, pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S177A/K1605A to reconstruct the assayed variant sequence.

proof_lines: mixture of mutants S177A and mutant K1605A, pH 8.0, temperature not specified in the publication


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

proof_lines: wild type enzyme, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C


proof_lines:
wild-type
pH 7.7, 25°C, wild-type
pH 7.7, 25°C, wild-type and mutant N38E


sequence_variant_note: Mutation signature G15V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
mutant G15V
IMP, mutant G15V


sequence_variant_note: Mutation signature K331L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature K331R could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
IMP, mutant K331R
Asp, mutant K331R


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature R305L to reconstruct the assayed variant sequence.

proof_lines:
Asp, mutant R305L
mutant R305L


sequence_variant_note: Mutation signature R303L 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_ec_organism_consensus_sequence and applied mutation signature R304L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6CP22 and applied mutation signature D1321A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 295.15 K; cofactor NAD+

column_label: Table 2, body row 'D1321A': column 'kcat (s-1)' = 3.16; column 'Km for urea (mM)' = 78; column 'kcat/Km (s-1 mM-1)' = 0.041. The value printed after the plus/minus sign in each of those three cells is the printed S.D. and is not an exported metric, and the parenthesised number beside each cell is the printed ratio of that cell to the wild-type value of the same column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.16 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 3.16 s^(-1). Km: printed Table 2 cell 78 in a column headed Km for urea (mM); mM is already canonical, so no unit conversion applies and the value is 78.0 mM. kcat/Km: printed Table 2 cell 0.041 in a column headed kcat/Km (s-1 mM-1); 1 s^-1 mM^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 0.041 s^(-1)*mM^(-1). The exported values are kcat 3.16 s^(-1), Km 78.0 mM and kcat_over_km 0.04051282051282051 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'D1321A': kcat = 3.16 in a column headed kcat (s-1); Km for urea = 78 in a column headed Km for urea (mM); printed kcat/Km = 0.041 in a column headed kcat/Km (s-1 mM-1).

row_label: Table 2, row D1321A

table_label: Table 2: Summary of the KlUC kinetic parameters (J. Biol. Chem. 2012, 287(12):9389-9398). Printed column heads: Mutation; kcat (s-1); Km for urea (mM); kcat/Km (s-1 mM-1). The printed caption states that the numbers in the parentheses are ratios to the wild-type values and that the S.D. values were obtained from fitting the experimental data to the Michaelis-Menten equation.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6CP22 and applied mutation signature Y1324F to reconstruct the assayed variant sequence.

column_label: Table 2, body row 'Y1324F': column 'kcat (s-1)' = 45.8; column 'Km for urea (mM)' = 7.7; column 'kcat/Km (s-1 mM-1)' = 5.9. The value printed after the plus/minus sign in each of those three cells is the printed S.D. and is not an exported metric, and the parenthesised number beside each cell is the printed ratio of that cell to the wild-type value of the same column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 45.8 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 45.8 s^(-1). Km: printed Table 2 cell 7.7 in a column headed Km for urea (mM); mM is already canonical, so no unit conversion applies and the value is 7.7 mM. kcat/Km: printed Table 2 cell 5.9 in a column headed kcat/Km (s-1 mM-1); 1 s^-1 mM^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 5.9 s^(-1)*mM^(-1). The exported values are kcat 45.8 s^(-1), Km 7.7 mM and kcat_over_km 5.948051948051948 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'Y1324F': kcat = 45.8 in a column headed kcat (s-1); Km for urea = 7.7 in a column headed Km for urea (mM); printed kcat/Km = 5.9 in a column headed kcat/Km (s-1 mM-1).

row_label: Table 2, row Y1324F


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D1564N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D1564N, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6CP22 and applied mutation signature Y1628F to reconstruct the assayed variant sequence.

column_label: Table 2, body row 'Y1628F': column 'kcat (s-1)' = 64.9; column 'Km for urea (mM)' = 15.0; column 'kcat/Km (s-1 mM-1)' = 4.3. The value printed after the plus/minus sign in each of those three cells is the printed S.D. and is not an exported metric, and the parenthesised number beside each cell is the printed ratio of that cell to the wild-type value of the same column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 64.9 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 64.9 s^(-1). Km: printed Table 2 cell 15.0 in a column headed Km for urea (mM); mM is already canonical, so no unit conversion applies and the value is 15.0 mM. kcat/Km: printed Table 2 cell 4.3 in a column headed kcat/Km (s-1 mM-1); 1 s^-1 mM^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 4.3 s^(-1)*mM^(-1). The exported values are kcat 64.9 s^(-1), Km 15.0 mM and kcat_over_km 4.326666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'Y1628F': kcat = 64.9 in a column headed kcat (s-1); Km for urea = 15.0 in a column headed Km for urea (mM); printed kcat/Km = 4.3 in a column headed kcat/Km (s-1 mM-1).

row_label: Table 2, row Y1628F


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6CP22 and applied mutation signature E1792A to reconstruct the assayed variant sequence.

column_label: Table 2, body row 'E1792A': column 'kcat (s-1)' = 68.7; column 'Km for urea (mM)' = 0.39; column 'kcat/Km (s-1 mM-1)' = 176. The value printed after the plus/minus sign in each of those three cells is the printed S.D. and is not an exported metric, and the parenthesised number beside each cell is the printed ratio of that cell to the wild-type value of the same column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 68.7 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 68.7 s^(-1). Km: printed Table 2 cell 0.39 in a column headed Km for urea (mM); mM is already canonical, so no unit conversion applies and the value is 0.39 mM. kcat/Km: printed Table 2 cell 176 in a column headed kcat/Km (s-1 mM-1); 1 s^-1 mM^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 176.0 s^(-1)*mM^(-1). The exported values are kcat 68.7 s^(-1), Km 0.39 mM and kcat_over_km 176.15384615384616 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'E1792A': kcat = 68.7 in a column headed kcat (s-1); Km for urea = 0.39 in a column headed Km for urea (mM); printed kcat/Km = 176 in a column headed kcat/Km (s-1 mM-1).

row_label: Table 2, row E1792A


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

proof_lines: wild-type protein, presence of 3 mM ATP, 2 mM UTP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature L109A to reconstruct the assayed variant sequence.


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


substrate_name: UTP

substrate: UTP


substrate_name: XTP

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +8, so it is treated as a source-provided variant sequence.

substrate: XTP


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: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -12, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D33Q with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


substrate_name: ITP

substrate: ITP


organism: Plasmodium falciparum

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R155A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R155L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R155K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N429V to reconstruct the assayed variant sequence.


proof_lines: wild type enzyme, in 30 mM sodium phosphate, pH 7.4 and at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K62L with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T307V to reconstruct the assayed variant sequence.


substrate_name: L-Asp

substrate: L-Asp


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature H118A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E103A to reconstruct the assayed variant sequence.


substrate_name: Gln

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature L109F with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

substrate: Gln


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature R105A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature L109A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

proof_lines:
pH 8.0, mutant enzyme L109A
37°C, pH 8.0, mutant enzyme L109A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature R104A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature G110A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D107A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K102A 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.

proof_lines: wild-type protein, presence of 1 mM ATP, 1 mM UTP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C328S/C368S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C328S/C368S, in 30 mM sodium phosphate, pH 7.4 and at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C368D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C368D/C368D, in 30 mM sodium phosphate, pH 7.4 and at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C328S with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C328S, in 30 mM sodium phosphate, pH 7.4 and at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C368S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C368S, in 30 mM sodium phosphate, pH 7.4 and at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C328D with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C328D, in 30 mM sodium phosphate, pH 7.4 and at 25°C


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


organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: L-glutamine (at unsaturating levels of ATP and UTP (0.5 mM))

proof_lines: kcat is 7.4 sec(-1) toward L-glutamine at unsaturating levels of ATP and UTP (0.5 mM) and 40 sec(-1) in the presence of GTP. kcat is 260 sec(-1) toward UTP.


enzyme_display_name: formate--tetrahydrofolate ligase

organism: Clostridium cylindrosporum

substrate_name: ADP

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K71Q with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ADP

enzyme: formate--tetrahydrofolate ligase

substrate: ADP


substrate_name: tetrahydrofolate

proof_lines:
MgATP2-, wild-type enzyme
wild-type enzyme

substrate: tetrahydrofolate


substrate_name: ATP

substrate: ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H131S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H125S to reconstruct the assayed variant sequence.


substrate_name: formate

substrate: formate


substrate_name: GTP

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -5, so it is treated as a source-provided variant sequence.

substrate: GTP


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


sequence_variant_note: Mutation signature R131L could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
IMP, mutant R131L
GTP, mutant R131L


substrate_name: IMP

sequence_variant_note: Mutation signature H41N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
mutant H41N
pH 7.7, 25°C, mutant H41N

substrate: IMP


substrate_name: Asp

substrate: Asp


organism: Dictyostelium discoideum


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature G142A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 37°C, mutant G142A with L-glutamine, in presence of 0.25 mM GTP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature G143A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 37°C, mutant G143A with L-glutamine, in presence of 0.25 mM GTP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature G146A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 37°C, mutant G146A with L-glutamine, in presence of 0.25 mM GTP


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

proof_lines: pH 8.0, 37°C, wild-type enzyme with L-glutamine, in presence of 0.25 mM GTP


proof_lines:
IMP, wild-type
wild-type
Asp, wild-type


sequence_variant_note: Mutation signature R143L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: guanosine 5'-tetraphosphate

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

substrate: guanosine 5'-tetraphosphate


proof_lines:
0.2 mM guanosine
0.1 mM guanosine
no guanosine


substrate_name: 6-thioguanosine 5'-triphosphate

proof_lines: no guanosine, kact: 8.5/sec, KA: 0.035 mM, Ki: 0.27 mM

substrate: 6-thioguanosine 5'-triphosphate


substrate_name: glutamine

proof_lines: kcat is 13 sec(-1) with ammonia as substrate. kcat is 6.6 sec(-1) with L-glutamine as substrate (in the presence of 0.25 mM GTP).

substrate: glutamine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C379A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C379S to reconstruct the assayed variant sequence.


proof_lines:
pH 8.0, 25°C, without GTP
pH 8.0, 25°C, activation with GTP


assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


enzyme_display_name: argininosuccinate synthase

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

substrate_name: citrulline (at 38 degrees Celsius and pH 9.0)

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

assay_conditions_summary: pH 9; cofactor ATP

column_label: PMC10937788 Table 1 reports Citrulline Km = 0.35 +/- 0.01 mM under optimum conditions; this matches the current row value.

raw_value_unit_evidence: Km raw_value=0.35 +/- 0.01 mM raw_unit=mM

row_label: Row: Citrulline

enzyme: argininosuccinate synthase


substrate_name: aspartate (at 38 degrees Celsius and pH 9.0)

column_label: PMC10937788 Table 1 reports Aspartate Km = 0.36 +/- 0.04 mM under optimum conditions; this matches the current row value.

raw_value_unit_evidence: Km raw_value=0.36 +/- 0.04 mM raw_unit=mM

row_label: Row: Aspartate


substrate_name: ATP (at 38 degrees Celsius and pH 9.0)

column_label: PMC10937788 Table 1 reports ATP Km = 0.26 +/- 0.01 mM under optimum conditions; this matches the current row value.

raw_value_unit_evidence: Km raw_value=0.26 +/- 0.01 mM raw_unit=mM

row_label: Row: ATP

substrate: ATP (at 38 degrees Celsius and pH 9.0)


organism: Leishmania major

substrate_name: Formate; ATP; 5,6,7,8-Tetrahydrofolate

substrate: Formate; ATP; 5,6,7,8-Tetrahydrofolate


organism: Methylobacterium extorquens


organism: Mus musculus


organism: Schizosaccharomyces pombe

substrate_name: GTP; IMP; L-Aspartate

substrate: GTP; IMP; L-Aspartate


organism: Zea mays

substrate_name: GTP; L-Aspartate; IMP

substrate: GTP; L-Aspartate; IMP


organism: Bos taurus

substrate_name: L-Citrulline; ATP; L-Aspartate

substrate: L-Citrulline; ATP; L-Aspartate


organism: Homo sapiens

substrate_name: L-Aspartate; ATP; L-Citrulline

substrate: L-Aspartate; ATP; L-Citrulline


organism: Escherichia coli

substrate_name: Unknown

sequence_variant_note: Mutation signature V273N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: Unknown


sequence_variant_note: Mutation signature V273A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature V273T could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: allopurinol ribonucleotide

substrate: allopurinol ribonucleotide


substrate_name: IMP; GTP; L-Aspartate

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

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

proof_lines:
22°C
22°C, reaction with IMP
pH 7.7, 30°C

source_databases_merged: sabio_rk brenda skid

substrate: IMP; GTP; L-Aspartate


substrate_name: Gln-OH

substrate: Gln-OH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature L109A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


substrate_name: NH3; UTP; ATP

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines:
in the presence of 10 mM UTP
no guanosine
Kinact: 0.48/min

substrate: NH3; UTP; ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K306A to reconstruct the assayed variant sequence.

proof_lines: K306A: replacement of lysine 306 by alanine reduces the rate of 2',3'-dialdehyde adenosine 5'-triphosphate-dependent inactivation


substrate_name: One carbon pool; 5,6,7,8-Tetrahydrofolate


substrate_name: ADP

proof_lines:
ATP synthesis from carbamoylphosphate
formyltetrahydrofolate synthesis

substrate: ADP


substrate_name: tetrahydrofolate

proof_lines:
ATP synthesis
formyltretrahydrofolate synthesis

substrate: tetrahydrofolate


organism: Toxoplasma gondii

substrate_name: UTP

proof_lines: K0.5 value, Hill coefficient 1.6, pH 8.0, 37°C

substrate: UTP


organism: Methanocaldococcus jannaschii

proof_lines: pH 6.0, 70°C, competitive inhibition of GTP

proof_lines: pH 6.0, 70°C, competitive inhibition of IMP

proof_lines: pH 6.0, 70°C, competitive inhibition of asparate


organism: Saccharolobus solfataricus


organism: Kluyveromyces lactis

substrate_name: Urea

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6CP22 and applied mutation signature D1321A to reconstruct the assayed variant sequence.

smiles: N=C(N)O

substrate: Urea


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D1564N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6CP22 and applied mutation signature E1792A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6CP22 and applied mutation signature K1605A to reconstruct the assayed variant sequence.

column_label: Table 2, body row 'K1605A': column 'kcat (s-1)' = 1.44; column 'Km for urea (mM)' = 493; column 'kcat/Km (s-1 mM-1)' = 0.0029. The value printed after the plus/minus sign in each of those three cells is the printed S.D. and is not an exported metric, and the parenthesised number beside each cell is the printed ratio of that cell to the wild-type value of the same column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.44 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 1.44 s^(-1). Km: printed Table 2 cell 493 in a column headed Km for urea (mM); mM is already canonical, so no unit conversion applies and the value is 493.0 mM. kcat/Km: printed Table 2 cell 0.0029 in a column headed kcat/Km (s-1 mM-1); 1 s^-1 mM^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 0.0029 s^(-1)*mM^(-1). The exported values are kcat 1.44 s^(-1), Km 493.0 mM and kcat_over_km 0.002920892494929006 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'K1605A': kcat = 1.44 in a column headed kcat (s-1); Km for urea = 493 in a column headed Km for urea (mM); printed kcat/Km = 0.0029 in a column headed kcat/Km (s-1 mM-1).

row_label: Table 2, row K1605A


column_label: Table 2, body row 'Wild type': column 'kcat (s-1)' = 210.8; column 'Km for urea (mM)' = 0.32; column 'kcat/Km (s-1 mM-1)' = 659. The value printed after the plus/minus sign in each of those three cells is the printed S.D. and is not an exported metric, and the parenthesised number beside each cell is the printed ratio of that cell to the wild-type value of the same column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 210.8 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 210.8 s^(-1). Km: printed Table 2 cell 0.32 in a column headed Km for urea (mM); mM is already canonical, so no unit conversion applies and the value is 0.32 mM. kcat/Km: printed Table 2 cell 659 in a column headed kcat/Km (s-1 mM-1); 1 s^-1 mM^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 659.0 s^(-1)*mM^(-1). The exported values are kcat 210.8 s^(-1), Km 0.32 mM and kcat_over_km 658.75 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row 'Wild type': kcat = 210.8 in a column headed kcat (s-1); Km for urea = 0.32 in a column headed Km for urea (mM); printed kcat/Km = 659 in a column headed kcat/Km (s-1 mM-1).

row_label: Table 2, row Wild type


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6CP22 and applied mutation signature Y1324F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q6CP22 and applied mutation signature Y1628F to reconstruct the assayed variant sequence.


organism: Lactococcus lactis subsp. cremoris

substrate_name: UTP; H2O; ATP; L-Glutamine

substrate: UTP; H2O; ATP; L-Glutamine


organism: Lactococcus lactis subsp. lactis

substrate_name: H2O; L-Glutamine; ATP; UTP

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

substrate: H2O; L-Glutamine; ATP; UTP


organism: Mycobacterium tuberculosis


organism: Saccharomyces cerevisiae

substrate_name: H2O; UTP; L-Glutamine; ATP

substrate: H2O; UTP; L-Glutamine; ATP


organism: Clostridium cylindrosporum


substrate_name: THF monoglutamate

substrate: THF monoglutamate


organism: Lactococcus lactis

substrate_name: L-Glutamine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E362Q with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

substrate: L-Glutamine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G360A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R359M 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 R359P 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 G360P to reconstruct the assayed variant sequence.


substrate_name: L-Asp

proof_lines:
22°C, cosubstrate: 2'-dIMP
22°C, cosubstrate: IMP
22°C, cosubstrate: dIMP

substrate: L-Asp


substrate_name: GTP

sequence_variant_note: Mutation signature H41N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: GTP


substrate_name: L-Aspartate

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

substrate: L-Aspartate


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -5, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature R131L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: L-aspartate

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

substrate: L-aspartate


sequence_variant_note: Mutation signature V273A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature V273N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: ATP

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

substrate: ATP


substrate_name: formate

substrate: formate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V186G to reconstruct the assayed variant sequence.


substrate_name: IMP

substrate: IMP


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

column_label: PubMed abstract reports URA8-encoded CTP synthetase UTP Km = 74 microM; this normalizes to 0.074 mM.

raw_value_unit_evidence: Km raw_value=74 microM raw_unit=microM

row_label: Prose segment: UTP Km

table_label: PubMed PMID 7559626 abstract


column_label: PubMed abstract reports URA8-encoded CTP synthetase ATP Km = 22 microM; this normalizes to 0.022 mM.

raw_value_unit_evidence: Km raw_value=22 microM raw_unit=microM

row_label: Prose segment: ATP Km


substrate_name: L-glutamine

column_label: PubMed abstract reports URA8-encoded CTP synthetase glutamine Km = 0.14 mM; this matches the current row value.

raw_value_unit_evidence: Km raw_value=0.14 mM raw_unit=mM

row_label: Prose segment: glutamine Km

substrate: L-glutamine


organism: Azotobacter vinelandii


substrate_name: Asp

substrate: Asp


organism: Ovis aries


substrate_name: tetrahydrofolate

substrate: tetrahydrofolate


proof_lines:
pH 7.7, 30°C
22°C, cosubstrate: 2'-dIMP
22°C, cosubstrate: IMP


organism: Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)

column_label: Kinetic prose reports the apparent K_m for formate as 22 mM for purified FtfL from M. extorquens AM1.

raw_value_unit_evidence: Km raw_value=22 raw_unit=mM

row_label: purified FtfL from M. extorquens AM1 / formate substrate

table_label: PMC full text PMID 14645277 FtfL kinetic prose


organism: Schizosaccharomyces pombe


substrate_name: L-citrulline

substrate: L-citrulline


organism: Zea mays


organism: Plasmodium falciparum

proof_lines:
pH 7.5
pH 7.5, 37°C
Raw SKiD Env: Temp=37°C, pH=7

source_databases_merged: brenda skid uniprot


proof_lines:
pH 7.5
pH 7.5, 37°C
Raw SKiD Env: Temp=25°C, pH=7


assay_conditions_summary: pH 6


organism: Lactococcus lactis subsp. cremoris (strain MG1363)


substrate_name: ammonia

substrate: ammonia


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K306A to reconstruct the assayed variant sequence.


organism: Leishmania major

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


substrate_name: Formate

smiles: O=CO

substrate: Formate


organism: Toxoplasma gondii

assay_conditions_summary: pH 8; cofactor ATP

column_label: Article Table 1 columns Substrate=ATP; Km (mM)=0.54 +/- 0.05; kcat (s^-1)=36; kcat/Km (s^-1 mM^-1)=66.7.

raw_value_unit_evidence: Table 1 ATP row reports Km 0.54 +/- 0.05 mM; kcat 36 s^-1; kcat/Km 66.7 s^-1 mM^-1.

row_label: T. gondii (full length refolded) - ATP

table_label: Table 1


assay_conditions_summary: pH 8

column_label: Article Table 1 columns Substrate=L-Gln; Km (mM)=0.26 +/- 0.04; kcat (s^-1)=29.6; kcat/Km (s^-1 mM^-1)=114.

normalized_value_unit_evidence: Normalized values: Km 0.26 mM; kcat 29.6 s^-1; kcat/Km 113.84615384615385 s^-1*mM^-1 from 29.6 / 0.26. The table-displayed kcat/Km cell is 114 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 L-Gln row reports Km 0.26 +/- 0.04 mM; kcat 29.6 s^-1; kcat/Km 114 s^-1 mM^-1.

row_label: T. gondii (full length refolded) - L-Gln


organism: Dictyostelium discoideum

column_label: Abstract reports apparent Km values for IMP, GTP, and aspartate of 36, 23, and 714 microM, respectively.

raw_value_unit_evidence: Km raw_value=23 microM raw_unit=microM

row_label: Dictyostelium adenylosuccinate synthetase / GTP

table_label: PubMed XML abstract PMID 6703692


raw_value_unit_evidence: Km raw_value=36 microM raw_unit=microM

row_label: Dictyostelium adenylosuccinate synthetase / IMP


organism: Homo sapiens

substrate_name: citrulline (at pH 7.0 and 37 degrees Celsius)

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


substrate_name: aspartate (at pH 7.0 and 37 degrees Celsius)


organism: Oleomonas sagaranensis

substrate_name: Formamide

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

smiles: C(=O)N

column_label: Table 4; row Formamide; columns kcat (s^-1), Km (mM), kcat/Km (s^-1 mM^-1)

row_label: Formamide

table_label: Table 4

substrate: Formamide


substrate_name: acetamide

smiles: CC(=O)N

column_label: Official PMC article HTML Table 4, row Acetamide, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1): 126 +/- 7; 40.3 +/- 0.8; 0.32.

normalized_value_unit_evidence: Table units are already canonical: Km=126 mM; kcat=40.3 s^-1; kcat/Km=0.32 s^-1 mM^-1.

raw_value_unit_evidence: Official PMC Table 4, Acetamide row: Km 126 +/- 7 mM; kcat 40.3 +/- 0.8 s^-1; kcat/Km 0.32 s^-1 mM^-1.

row_label: Acetamide

substrate: acetamide


substrate_name: Urea

column_label: Table 4; row Urea; columns kcat (s^-1), Km (mM), kcat/Km (s^-1 mM^-1)

row_label: Urea

substrate: Urea


substrate_name: Carbamoyl phosphate

column_label: Table I, Comparison of Km and Kd values of substrates in the two enzymatic activities, lists Carbamyl phosphate with Km (mM), ATP synthesis = 11.9 and footnote a.

raw_value_unit_evidence: Km raw_value=11.9 raw_unit=mM

row_label: Carbamyl phosphate

table_label: Table I

substrate: Carbamoyl phosphate


proof_lines:
22°C
Raw SKiD Env: Temp=22°C, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.7


organism: Lactococcus lactis subsp. lactis

substrate_name: GTP


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.


substrate_name: Unknown

substrate: Unknown


organism: Clostridium cylindrosporum

substrate_name: phosphate

substrate: phosphate


substrate_name: L-Gln

substrate: L-Gln


substrate_name: UTP

substrate: UTP


mutation_signature: C-terminal deletion mutant

mutation_type: deletion

proof_lines: C-terminal deletion mutant, pH 8.1, 37°C


substrate_name: ATP

substrate: ATP


substrate_name: citrulline

substrate: citrulline


substrate_name: Asp


organism: Cyberlindnera jadinii


organism: Neomoorella thermoacetica

assay_conditions_summary: pH 7; 300.15 K; cofactor ATP


substrate_name: formate

substrate: formate


organism: Clostridium perfringens

assay_conditions_summary: pH 8.2; cofactor ATP

proof_lines: recombinant His6-tagged enzyme, pH 8.2, temperature not specified in the publication


proof_lines: pH 8.2, temperature not specified in the publication


organism: Gallus gallus

proof_lines:
muscle enzyme
liver enzyme
Asp, liver enzyme

substrate: GTP


substrate: Asp


substrate_name: IMP

substrate: IMP


organism: Helicobacter pylori


substrate_name: L-aspartate

substrate: L-aspartate


organism: Rattus norvegicus

substrate_name: diphosphate

substrate: diphosphate


proof_lines:
enzyme form ASSI
Asp


substrate_name: AMP

substrate: AMP


substrate_name: argininosuccinate

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

substrate: argininosuccinate


organism: Lactococcus lactis


proof_lines:
recombinant enzyme, 30°C
above, recombinant enzyme, 30°C


assay_conditions_summary: 303.15 K; cofactor ATP

proof_lines: recombinant enzyme, 30°C, with substrate (6R,S)-tetrahydrofolate pteroyltriglutamate or (6R,S)-tetrahydrofolate pteroylpentaglutamate and formate

proof_lines: above, recombinant enzyme, 30°C, with substrate (6R,S)-tetrahydrofolate monoglutamate and formate


proof_lines: recombinant enzyme, 30°C, with substrate (6R,S)-tetrahydrofolate pteroylpentaglutamate

proof_lines: recombinant enzyme, 30°C, with substrate (6R,S)-tetrahydrofolate pteroyltriglutamate

proof_lines: recombinant enzyme, 30°C, with substrate (6R,S)-tetrahydrofolate monoglutamate


organism: Lathyrus oleraceus

proof_lines: ATP, reaction with tetrahydropteroyl-Glu4


proof_lines: ATP, reaction with tetrahydropteroyl-Glu2


substrate_name: tetrahydrofolate

substrate: tetrahydrofolate


organism: Trypanosoma brucei


substrate_name: L-glutamine

substrate: L-glutamine


organism: Mus musculus

substrate_name: aspartate

proof_lines:
in presence of 0.0005 mM Bj-BPP-10c
in presence of 0.1 mM Bj-BPP-10c

substrate: aspartate


organism: Saccharomyces cerevisiae


proof_lines: normal liver and from patients with citrullinemia


organism: Zea mays

substrate_name: GTP


organism: Methylorubrum extorquens

assay_conditions_summary: pH 8; 296.15 K; cofactor ATP


organism: Bacillus subtilis


substrate_name: Unknown

substrate: Unknown


proof_lines:
pH 8.0, 25°C, native enzyme
pH 8.0, 25°C, recombinant enzyme


proof_lines:
pH 8.0, 25°C, recombinant enzyme
pH 8.0, 25°C, native enzyme


substrate_name: Gln

proof_lines: 30°C, pH 8.0, inhibition of hydroxylamine-dependent N4-OH CTP synthesis in presence of GTP

substrate: Gln


proof_lines: 30°C, pH 8.0, inhibition of N4-OH-CTP synthesis


organism: Bos taurus

substrate_name: L-Asp

substrate: L-Asp


substrate_name: threo-beta-methyl-L-Asp

substrate: threo-beta-methyl-L-Asp


organism: Sus scrofa

substrate_name: ATP

substrate: ATP


substrate_name: UTP

substrate: UTP


proof_lines:
pH 6.7, 22°C, AdSS1-Tr
pH 6.7, 22°C, AdSS2-Tr
pH 6.7, 22°C, AdSS2


proof_lines:
pH 6.7, 22°C, AdSS2-Tr
pH 6.7, 22°C, AdSS2
pH 6.7, 22°C, AdSS1-Tr


organism: Leishmania donovani


substrate_name: Asp


organism: Oryctolagus cuniculus


proof_lines:
22°C
reaction with IMP
pH 6.7, 22°C, AdSS1


proof_lines:
22°C, cosubstrate: 2'-dIMP
pH 6.7, 22°C, AdSS1
pH 7.2, 22°C


organism: Oryza sativa

proof_lines:
isoform AdSS2, pH 7.7, 30°C
isoform AdSS1, pH 7.7, 30°C


proof_lines:
isoform AdSS1, pH 7.7, 30°C
isoform AdSS2, pH 7.7, 30°C


organism: Homo sapiens


organism: Triticum aestivum


proof_lines: pH 8.0, mutant enzyme S354A, kinetic constant determined with 0.5 mM ATP


proof_lines: pH 8.0, mutant enzyme S330A, kinetic constant determined with 0.5 mM ATP


organism: Anoxybacillus gonensis


substrate_name: citrulline

substrate: citrulline


substrate: GTP


substrate: Asp


column_label: Table II, Km (uM) column, Parent enzyme subcolumn, MgATP row shows 67; Synthetase fragment subcolumn shows 65.

raw_value_unit_evidence: Km = 67 uM

row_label: 10-Formyltetrahydrofolate synthetase; substrate MgATP

table_label: Table II: Kinetic constants for C1-tetrahydrofolate synthase reactions and the two purified fragments


substrate_name: formate

column_label: Table II, Km (uM) column, Parent enzyme subcolumn, Formate row shows 166; Synthetase fragment subcolumn shows 160.

raw_value_unit_evidence: Km = 166 uM

row_label: 10-Formyltetrahydrofolate synthetase; substrate Formate

substrate: formate


substrate_name: IMP

substrate: IMP


organism: Chlamydia trachomatis