column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row D317A; column kcat (min^-1) = 1.3; column Km D-Glu (uM) = 44; column kcat/Km D-Glu (min^-1 uM^-1) = 0.029.

raw_value_unit_evidence: Table 2, protein row D317A, D-Glu column group: kcat = 1.3 min^-1; Km D-Glu = 44 uM; printed kcat/Km D-Glu = 0.029 min^-1 uM^-1.


organism: Escherichia coli

substrate_name: D-Glutamate

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:P14900 and applied mutation signature D35A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 9.4; 310.15 K; buffer 0.1 M Tris-HCl; cofactor ATP

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row D35A; column kcat (min^-1) = 256; column Km D-Glu (uM) = 95; column kcat/Km D-Glu (min^-1 uM^-1) = 2.69.

raw_value_unit_evidence: Table 2, protein row D35A, D-Glu column group: kcat = 256 min^-1; Km D-Glu = 95 uM; printed kcat/Km D-Glu = 2.69 min^-1 uM^-1.

table_label: Table 2: Kinetic Constants of the MurD Mutant Proteins (Biochemistry 1999, 38(38):12240-12247)

data_origin: experimental

substrate: D-Glutamate

status: corrected

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature E157K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row E157K; column kcat (min^-1) = 0.022; column Km D-Glu (uM) = 56; column kcat/Km D-Glu (min^-1 uM^-1) = 0.00039.

raw_value_unit_evidence: Table 2, protein row E157K, D-Glu column group: kcat = 0.022 min^-1; Km D-Glu = 56 uM; printed kcat/Km D-Glu = 0.00039 min^-1 uM^-1. the kcat/Km D-Glu cell is set by the journal with a digit-grouping space as 0.000 39 and reads 0.00039.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature H183A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row H183A; column kcat (min^-1) = 5.6; column Km D-Glu (uM) = 806; column kcat/Km D-Glu (min^-1 uM^-1) = 0.0069.

raw_value_unit_evidence: Table 2, protein row H183A, D-Glu column group: kcat = 5.6 min^-1; Km D-Glu = 806 uM; printed kcat/Km D-Glu = 0.0069 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature H301A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row H301A; column kcat (min^-1) = 46; column Km D-Glu (uM) = 95; column kcat/Km D-Glu (min^-1 uM^-1) = 0.48.

raw_value_unit_evidence: Table 2, protein row H301A, D-Glu column group: kcat = 46 min^-1; Km D-Glu = 95 uM; printed kcat/Km D-Glu = 0.48 min^-1 uM^-1.


substrate_name: UDP-N-acetylmuramoyl-L-alanine

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row D35A; column kcat (min^-1) = 256; column Km UMA (uM) = 84; column kcat/Km UMA (min^-1 uM^-1) = 3.05.

raw_value_unit_evidence: Table 2, protein row D35A, UMA column group: kcat = 256 min^-1; Km UMA = 84 uM; printed kcat/Km UMA = 3.05 min^-1 uM^-1.

substrate: UDP-N-acetylmuramoyl-L-alanine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature E157A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row E157A; column kcat (min^-1) = 0.020; column Km UMA (uM) = 304; column kcat/Km UMA (min^-1 uM^-1) = 0.000066.

raw_value_unit_evidence: Table 2, protein row E157A, UMA column group: kcat = 0.020 min^-1; Km UMA = 304 uM; printed kcat/Km UMA = 0.000066 min^-1 uM^-1. the kcat/Km UMA cell is set by the journal with a digit-grouping space as 0.000 066 and reads 0.000066.


column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row E157K; column kcat (min^-1) = 0.022; column Km UMA (uM) = 218; column kcat/Km UMA (min^-1 uM^-1) = 0.00010.

raw_value_unit_evidence: Table 2, protein row E157K, UMA column group: kcat = 0.022 min^-1; Km UMA = 218 uM; printed kcat/Km UMA = 0.00010 min^-1 uM^-1. the kcat/Km UMA cell is set by the journal with a digit-grouping space as 0.000 10 and reads 0.00010.


column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row H183A; column kcat (min^-1) = 5.6; column Km UMA (uM) = 59; column kcat/Km UMA (min^-1 uM^-1) = 0.095.

raw_value_unit_evidence: Table 2, protein row H183A, UMA column group: kcat = 5.6 min^-1; Km UMA = 59 uM; printed kcat/Km UMA = 0.095 min^-1 uM^-1.


column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row H301A; column kcat (min^-1) = 46; column Km UMA (uM) = 40; column kcat/Km UMA (min^-1 uM^-1) = 1.15.

raw_value_unit_evidence: Table 2, protein row H301A, UMA column group: kcat = 46 min^-1; Km UMA = 40 uM; printed kcat/Km UMA = 1.15 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature K115A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row K115A; column kcat (min^-1) = 0.26; column Km UMA (uM) = 46; column kcat/Km UMA (min^-1 uM^-1) = 0.0056.

raw_value_unit_evidence: Table 2, protein row K115A, UMA column group: kcat = 0.26 min^-1; Km UMA = 46 uM; printed kcat/Km UMA = 0.0056 min^-1 uM^-1.


kcat_over_km_origin: calculated

sequence_variant_note: Mutation signature K198A 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.


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.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature N268A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row N268A; column kcat (min^-1) = 307; column Km UMA (uM) = 12; column kcat/Km UMA (min^-1 uM^-1) = 25.6.

raw_value_unit_evidence: Table 2, protein row N268A, UMA column group: kcat = 307 min^-1; Km UMA = 12 uM; printed kcat/Km UMA = 25.6 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature N271A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row N271A; column kcat (min^-1) = 18; column Km UMA (uM) = 16; column kcat/Km UMA (min^-1 uM^-1) = 1.12.

raw_value_unit_evidence: Table 2, protein row N271A, UMA column group: kcat = 18 min^-1; Km UMA = 16 uM; printed kcat/Km UMA = 1.12 min^-1 uM^-1.


enzyme_display_name: carnosine synthase

organism: Gallus gallus

substrate_name: beta-Alanine

source_db: brenda

kcat_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

sequence_source: multiple

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

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

source_databases_merged: brenda uniprot

enzyme: carnosine synthase

substrate: beta-Alanine

source: brenda


substrate_name: L-histidine

substrate: L-histidine


substrate_name: ATP

assay_conditions_summary: pH 7.5; cofactor ATP

substrate: ATP


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


substrate_name: L-lysine

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

substrate: L-lysine


substrate_name: L-ornithine

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

substrate: L-ornithine


substrate_name: N-methylhistidine

source_db: uniprot

substrate: N-methylhistidine

source: uniprot


organism: Erysipelothrix rhusiopathiae

assay_conditions_summary: pH 9.6; 310.15 K; cofactor ATP


substrate_name: L-alanine

substrate: L-alanine


enzyme_display_name: dihydrofolate synthase

organism: Escherichia coli (strain K12)

proof_lines: kcat is 25 min(-1) with 7,8-dihydropteroate as substrate (at 30 degrees Celsius).

enzyme: dihydrofolate synthase


substrate_name: tetrahydrofolate

substrate: tetrahydrofolate


organism: Homo sapiens

verification_status: verified

column_label: Km column under Human ATPGD1

normalized_value_unit_evidence: Table 4 Human ATPGD1 column supports Km 0.09 mM for beta-Alanine.

raw_value_unit_evidence: Table 4 beta-Alanine row, Human ATPGD1 Km column reports 0.09 +/- 0.01 mM.

row_label: Human ATPGD1; beta-Alanine substrate

table_label: Table 4: Kinetic properties of mouse human and chicken carnosine synthase

status: verified


normalized_value_unit_evidence: Table 4 Human ATPGD1 column supports Km 0.37 mM for L-histidine.

raw_value_unit_evidence: Table 4 L-Histidine row, Human ATPGD1 Km column reports 0.37 +/- 0.05 mM.

row_label: Human ATPGD1; L-Histidine substrate


normalized_value_unit_evidence: Table 4 Human ATPGD1 column supports Km 1.84 mM for gamma-Aminobutyrate, synonym 4-aminobutanoate.

raw_value_unit_evidence: Table 4 gamma-Aminobutyrate row, Human ATPGD1 Km column reports 1.84 +/- 0.11 mM.

row_label: Human ATPGD1; gamma-Aminobutyrate substrate


normalized_value_unit_evidence: Table 4 Human ATPGD1 column supports Km 4.67 mM for L-lysine.

raw_value_unit_evidence: Table 4 L-Lysine row, Human ATPGD1 Km column reports 4.67 mM.

row_label: Human ATPGD1; L-Lysine substrate


normalized_value_unit_evidence: Table 4 Human ATPGD1 column supports Km 7.66 mM for L-ornithine.

raw_value_unit_evidence: Table 4 L-Ornithine row, Human ATPGD1 Km column reports 7.66 mM.

row_label: Human ATPGD1; L-Ornithine substrate


normalized_value_unit_evidence: Table 4 Human ATPGD1 column supports Km 24.7 mM for N-pi-Methylhistidine, a specific N-methylhistidine isomer.

raw_value_unit_evidence: Table 4 N-pi-Methylhistidine row, Human ATPGD1 Km column reports 24.7 mM.

row_label: Human ATPGD1; N-pi-Methylhistidine substrate


organism: Mus musculus

substrate_name: beta-alanine

assay_conditions_summary: cofactor ATP

column_label: Km column under Mouse ATPGD1

normalized_value_unit_evidence: Km 0.46 mM

raw_value_unit_evidence: Table 4 row beta-Alanine, Mouse ATPGD1 Km column reports 0.46 +/- 0.04 mM.

row_label: beta-Alanine; Mouse ATPGD1

table_label: Table 4: Kinetic properties of mouse, human, and chicken carnosine synthase

substrate: beta-alanine


normalized_value_unit_evidence: Km 6.44 mM for gamma-aminobutyrate, synonym 4-aminobutanoate/GABA.

raw_value_unit_evidence: Table 4 row gamma-Aminobutyrate, Mouse ATPGD1 Km column reports 6.44 +/- 0.33 mM.

row_label: gamma-Aminobutyrate; Mouse ATPGD1


normalized_value_unit_evidence: Km 0.11 mM

raw_value_unit_evidence: Table 4 row L-Histidine, Mouse ATPGD1 Km column reports 0.11 +/- 0.01 mM.

row_label: L-Histidine; Mouse ATPGD1


normalized_value_unit_evidence: Km 1.59 mM

raw_value_unit_evidence: Table 4 row L-Lysine, Mouse ATPGD1 Km column reports 1.59 mM.

row_label: L-Lysine; Mouse ATPGD1


normalized_value_unit_evidence: Km 0.52 mM

raw_value_unit_evidence: Table 4 row L-Ornithine, Mouse ATPGD1 Km column reports 0.52 mM.

row_label: L-Ornithine; Mouse ATPGD1


normalized_value_unit_evidence: Km 4.51 mM for the paper row N-pi-Methylhistidine, a specific N-methylhistidine isomer.

raw_value_unit_evidence: Table 4 row N-pi-Methylhistidine, Mouse ATPGD1 Km column reports 4.51 mM.

row_label: N-pi-Methylhistidine; Mouse ATPGD1


organism: Plasmodium falciparum

substrate_name: dihydropteroate

assay_conditions_summary: pH 10; cofactor ATP

column_label: PMID 20350571 abstract: DHFS activity under lower co-substrate concentrations yielded apparent Km values of 0.88 microM for dihydropteroate, 22.8 microM for ATP, and 5.97 microM for glutamate.

raw_value_unit_evidence: The abstract reports apparent Km 0.88 microM for dihydropteroate in the DHFS assay.

row_label: PfDHFS-FPGS DHFS activity under lower co-substrate concentrations, dihydropteroate

table_label: PubMed abstract prose, PMID 20350571

substrate: dihydropteroate


substrate_name: glutamate

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

raw_value_unit_evidence: The abstract reports apparent Km 5.97 microM for glutamate in the DHFS assay.

row_label: PfDHFS-FPGS DHFS activity under lower co-substrate concentrations, glutamate

substrate: glutamate


raw_value_unit_evidence: The abstract reports apparent Km 22.8 microM for ATP in the DHFS assay.

row_label: PfDHFS-FPGS DHFS activity under lower co-substrate concentrations, ATP


enzyme_display_name: enterobactin synthase

substrate_name: isochorismate (at pH 7 and 37 degrees Celsius)

assay_conditions_summary: pH 7

proof_lines: kcat is 600 min(-1) for isochorismatase activity with isochorismate as substrate (at pH 7 and 37 degrees Celsius). kcat is 540 min(-1) for isochorismatase activity with 3-[(1-carboxylatoethenyl)oxy]-cyclohepta-1,6-diene-1-carboxylate as sub

enzyme: enterobactin synthase


substrate_name: meso-diaminopimelate

substrate: meso-diaminopimelate


substrate_name: meso-lanthionine

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

substrate: meso-lanthionine


assay_conditions_summary: pH 8; cofactor ATP


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

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


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

column_label: Table 6; row Km, ATP; column MurF Sa Km (mM); raw 0.11 mM; normalized 0.11 mM.

raw_value_unit_evidence: Table 6 row Km, ATP gives MurF Sa Km 0.11 mM.

row_label: Km, ATP (MurF Sa; UniProt Q2FWH4)

table_label: PMID 20659527, Table 6: kinetic parameters of MurF Sa ligase from Staphylococcus aureus


substrate_name: D-alanyl-D-alanine

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

column_label: Table 6; row Km, D-Ala-D-Ala; column MurF Sa Km (mM); raw 0.24 mM; normalized 0.24 mM.

raw_value_unit_evidence: Table 6 row Km, D-Ala-D-Ala gives MurF Sa Km 0.24 mM.

row_label: Km, D-Ala-D-Ala (MurF Sa; UniProt Q2FWH4)

substrate: D-alanyl-D-alanine


substrate_name: D-glutamate

column_label: Table 3; row Km, D-Glu; column MurD Sa Km (mM); raw 0.13 mM; normalized 0.13 mM.

raw_value_unit_evidence: Table 3 row Km, D-Glu gives MurD Sa Km 0.13 mM.

row_label: Km, D-Glu (MurD Sa; UniProt Q2FZ92)

table_label: PMID 20659527, Table 3: kinetic parameters of MurD Sa ligase from Staphylococcus aureus

substrate: D-glutamate


column_label: Table 3; row Km, ATP; column MurD Sa Km (mM); raw 5.4 mM; normalized 5.4 mM.

normalized_value_unit_evidence: Km 5.4 mM.

raw_value_unit_evidence: Table 3 row Km, ATP gives MurD Sa Km 5.4 mM.

row_label: Km, ATP (MurD Sa; UniProt Q2FZ92)


organism: Mycobacterium tuberculosis

verification_status: unverified

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

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

proof_lines: mutant N449D, pH 8.5, 37°C, co-substrate: UDP-MurNAc-L-Ala-D-Glu, meso-2,6-diaminoheptanedioate

status: unverified


proof_lines: mutant R451A, pH 8.5, 37°C, co-substrate: UDP-MurNAc-L-Ala-D-Glu, meso-2,6-diaminoheptanedioate


proof_lines: mutant K157A, pH 8.5, 37°C, co-substrate: UDP-MurNAc-L-Ala-D-Glu, meso-2,6-diaminoheptanedioate


proof_lines: mutant D392A, pH 8.5, 37°C, co-substrate: UDP-MurNAc-L-Ala-D-Glu, meso-2,6-diaminoheptanedioate


proof_lines: mutant E220A, pH 8.5, 37°C, co-substrate: UDP-MurNAc-L-Ala-D-Glu, meso-2,6-diaminoheptanedioate


km_display: Not reported

mutation_signature: N-terminal deletion mutant

mutation_type: deletion

proof_lines: N-terminal deletion mutant, pH 8.5, 37°C, co-substrate: UDP-MurNAc-L-Ala-D-Glu, meso-2,6-diaminoheptanedioate


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

proof_lines: wild-type, pH 8.5, 37°C, co-substrate: UDP-MurNAc-L-Ala-D-Glu, meso-2,6-diaminoheptanedioate


substrate_name: UDP-MurNAc-L-Ala-D-Glu

substrate: UDP-MurNAc-L-Ala-D-Glu


mutation_signature: Δ1

proof_lines: DELTA1-24 (N-terminal deletion mutant), pH 8.5, 37°C


substrate_name: beta-Alanine


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


organism: Bacillus cereus


substrate_name: UDP-N-MurNAc-L-Ala-D-Glu

substrate: UDP-N-MurNAc-L-Ala-D-Glu


substrate_name: ATP


substrate_name: Glu

substrate: Glu


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


substrate_name: UDP-N-acetylmuramoyl-L-Ala-D-Glu

substrate: UDP-N-acetylmuramoyl-L-Ala-D-Glu


substrate_name: meso-diaminopimelic acid

substrate: meso-diaminopimelic acid


organism: Pseudomonas aeruginosa


substrate: ATP


organism: Staphylococcus aureus

substrate_name: UDP-N-acetylmuramoyl-L-Ala

substrate: UDP-N-acetylmuramoyl-L-Ala


substrate_name: D-Glu

substrate: D-Glu


assay_conditions_summary: pH 8.8; 310.15 K; cofactor ATP


organism: Corynebacterium sp.


substrate_name: L-Glu

substrate: L-Glu


organism: Neisseria gonorrhoeae


assay_conditions_summary: pH 8.6; 310.15 K; cofactor ATP

column_label: Table IV row D-Ala-D-HBut; columns Km (mM), kcat (min^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table IV row D-Ala-D-HBut: Km 2.6 mM; kcat 550 min^-1; kcat/Km 3.5 x 10^3 M^-1 s^-1.

row_label: D-Ala-D-HBut

table_label: Table IV, Substrate Specificity Data for E. coli D-Ala-D-Ala Adding Enzyme


substrate_name: D-Alanyl-D-alanine

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

raw_value_unit_evidence: Table IV row D-Ala-D-Ala: Km 0.054 mM; kcat 1080 min^-1; kcat/Km 3.3 x 10^5 M^-1 s^-1.

row_label: D-Ala-D-Ala

substrate: D-Alanyl-D-alanine


substrate_name: D-Alanyl-D-lactate

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

column_label: Table IV row D-Ala-D-Lac; columns Km (mM), kcat (min^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table IV row D-Ala-D-Lac: Km 0.095 mM; kcat 830 min^-1; kcat/Km 1.5 x 10^5 M^-1 s^-1.

row_label: D-Ala-D-Lac

substrate: D-Alanyl-D-lactate


substrate_name: D-Alanyl-D-methionine

column_label: Table IV row D-Ala-D-Met; columns Km (mM), kcat (min^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table IV row D-Ala-D-Met: Km 21 mM; kcat 34 min^-1; kcat/Km 27 M^-1 s^-1.

row_label: D-Ala-D-Met

substrate: D-Alanyl-D-methionine


substrate_name: D-Alanyl-D-phenylalanine

column_label: Table IV row D-Ala-D-Phe; columns Km (mM), kcat (min^-1), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table IV row D-Ala-D-Phe: Km 32 mM; kcat 55 min^-1; kcat/Km 29 M^-1 s^-1.

row_label: D-Ala-D-Phe

substrate: D-Alanyl-D-phenylalanine


substrate_name: L-Histidine; ATP; beta-Alanine

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

ki_unit: mM

substrate: L-Histidine; ATP; beta-Alanine


substrate_name: L-His

proof_lines:
olfactory bulb
olfactory epithelium
pH 7.5, 37°C

substrate: L-His


organism: Acinetobacter baumannii

substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


substrate_name: L-Ser

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

substrate: L-Ser


enzyme_display_name: glutamine--tRNA ligase

substrate_name: L-glutamine

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

enzyme: glutamine--tRNA ligase

substrate: L-glutamine


assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP


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


proof_lines:
wild-type enzyme, pH 7.2, 37°C
wild-type enzyme, strain UT172


enzyme_display_name: isoleucine--tRNA ligase

substrate_name: L-isoleucine

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

proof_lines: pH 7.5, 37°C, recombinant mutant Y59T/D342A

enzyme: isoleucine--tRNA ligase

substrate: L-isoleucine


proof_lines: pH 7.5, 37°C, recombinant mutant Y59F/D342A


enzyme_display_name: chorismate mutase

substrate_name: chorismate

enzyme: chorismate mutase

substrate: chorismate


proof_lines:
30°C, pH 7.2, wild-type
wild type
wild-type enzyme


enzyme_display_name: steroid Delta-isomerase

enzyme: steroid Delta-isomerase


enzyme_display_name: acetate--CoA ligase (ADP-forming)

organism: Archaeoglobus fulgidus

substrate_name: ADP

assay_conditions_summary: 323.15 K; cofactor ADP

proof_lines: 50°C, pH not specified in the publication

enzyme: acetate--CoA ligase (ADP-forming)

substrate: ADP


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: phosphate

substrate: phosphate


enzyme_display_name: 4-chlorobenzoate--CoA ligase

organism: Arthrobacter sp.

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

enzyme: 4-chlorobenzoate--CoA ligase


substrate_name: ATP

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

substrate: ATP


substrate_name: CoA

substrate: CoA


enzyme_display_name: NAD(P)H-hydrate epimerase

organism: Arabidopsis thaliana

enzyme: NAD(P)H-hydrate epimerase


enzyme_display_name: phosphoglucosamine mutase

organism: Methanococcus maripaludis

substrate_name: alpha-D-glucose 1-phosphate

enzyme: phosphoglucosamine mutase

substrate: alpha-D-glucose 1-phosphate


substrate_name: alpha-D-glucosamine 1-phosphate

substrate: alpha-D-glucosamine 1-phosphate


substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


substrate_name: dehydroepiandrosterone

proof_lines:
wild-type, isoform 1, 27°C, pH 7.4
wild-type, isoform 2, 27°C, pH 7.4

substrate: dehydroepiandrosterone


proof_lines:
wild-type, isoform 1, 27°C, pH 7.4
wild-type, 27°C, pH 7.4
wild-type, isoform 2, 27°C, pH 7.4


organism: Escherichia coli

substrate_name: D-Glu

substrate: D-Glu


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature D317A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row D317A; column kcat (min^-1) = 1.3; column Km ATP (uM) = 2180; column kcat/Km ATP (min^-1 uM^-1) = 0.00060.

raw_value_unit_evidence: Table 2, protein row D317A, ATP column group: kcat = 1.3 min^-1; Km ATP = 2180 uM; printed kcat/Km ATP = 0.00060 min^-1 uM^-1. the kcat/Km ATP cell is set by the journal with a digit-grouping space as 0.000 60 and reads 0.00060.


column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row D35A; column kcat (min^-1) = 256; column Km ATP (uM) = 114; column kcat/Km ATP (min^-1 uM^-1) = 2.25.

raw_value_unit_evidence: Table 2, protein row D35A, ATP column group: kcat = 256 min^-1; Km ATP = 114 uM; printed kcat/Km ATP = 2.25 min^-1 uM^-1.


column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row E157A; column kcat (min^-1) = 0.020; column Km ATP (uM) = 30; column kcat/Km ATP (min^-1 uM^-1) = 0.00067.

raw_value_unit_evidence: Table 2, protein row E157A, ATP column group: kcat = 0.020 min^-1; Km ATP = 30 uM; printed kcat/Km ATP = 0.00067 min^-1 uM^-1. the kcat/Km ATP cell is set by the journal with a digit-grouping space as 0.000 67 and reads 0.00067.


column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row E157K; column kcat (min^-1) = 0.022; column Km ATP (uM) = 85; column kcat/Km ATP (min^-1 uM^-1) = 0.00026.

raw_value_unit_evidence: Table 2, protein row E157K, ATP column group: kcat = 0.022 min^-1; Km ATP = 85 uM; printed kcat/Km ATP = 0.00026 min^-1 uM^-1. the kcat/Km ATP cell is set by the journal with a digit-grouping space as 0.000 26 and reads 0.00026.


column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row H183A; column kcat (min^-1) = 5.6; column Km ATP (uM) = 130; column kcat/Km ATP (min^-1 uM^-1) = 0.043.

raw_value_unit_evidence: Table 2, protein row H183A, ATP column group: kcat = 5.6 min^-1; Km ATP = 130 uM; printed kcat/Km ATP = 0.043 min^-1 uM^-1.


column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row H301A; column kcat (min^-1) = 46; column Km ATP (uM) = 153; column kcat/Km ATP (min^-1 uM^-1) = 0.30.

raw_value_unit_evidence: Table 2, protein row H301A, ATP column group: kcat = 46 min^-1; Km ATP = 153 uM; printed kcat/Km ATP = 0.30 min^-1 uM^-1.


column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row K115A; column kcat (min^-1) = 0.26; column Km ATP (uM) = 328; column kcat/Km ATP (min^-1 uM^-1) = 0.00079.

raw_value_unit_evidence: Table 2, protein row K115A, ATP column group: kcat = 0.26 min^-1; Km ATP = 328 uM; printed kcat/Km ATP = 0.00079 min^-1 uM^-1. the kcat/Km ATP cell is set by the journal with a digit-grouping space as 0.000 79 and reads 0.00079.


column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row N268A; column kcat (min^-1) = 307; column Km ATP (uM) = 140; column kcat/Km ATP (min^-1 uM^-1) = 2.19.

raw_value_unit_evidence: Table 2, protein row N268A, ATP column group: kcat = 307 min^-1; Km ATP = 140 uM; printed kcat/Km ATP = 2.19 min^-1 uM^-1.


enzyme_display_name: isochorismate synthase

substrate_name: isochorismate

enzyme: isochorismate synthase

substrate: isochorismate


assay_conditions_summary: 310.15 K; cofactor ATP


substrate_name: UDP-N-MurNAc-L-Ala-D-Glu

substrate: UDP-N-MurNAc-L-Ala-D-Glu


substrate_name: meso-lanthionine

substrate: meso-lanthionine


substrate_name: UDP-N-acetylmuramoyl-L-Ala

proof_lines:
37°C
pH 8.6, 37°C
versus D-Glu

substrate: UDP-N-acetylmuramoyl-L-Ala


substrate_name: UDP-N-acetylmuramoyl-L-alanine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature R302A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9.4; 310.15 K; buffer 0.1 M Tris-HCl; cofactor ATP

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row R302A; column kcat (min^-1) = 188; column Km UMA (uM) = 65; column kcat/Km UMA (min^-1 uM^-1) = 2.89.

raw_value_unit_evidence: Table 2, protein row R302A, UMA column group: kcat = 188 min^-1; Km UMA = 65 uM; printed kcat/Km UMA = 2.89 min^-1 uM^-1.

substrate: UDP-N-acetylmuramoyl-L-alanine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature R425A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row R425A; column kcat (min^-1) = 32; column Km UMA (uM) = 53; column kcat/Km UMA (min^-1 uM^-1) = 0.60.

raw_value_unit_evidence: Table 2, protein row R425A, UMA column group: kcat = 32 min^-1; Km UMA = 53 uM; printed kcat/Km UMA = 0.60 min^-1 uM^-1.


column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row wild-type; column kcat (min^-1) = 403; column Km UMA (uM) = 5; column kcat/Km UMA (min^-1 uM^-1) = 80.6.

raw_value_unit_evidence: Table 2, protein row wild-type, UMA column group: kcat = 403 min^-1; Km UMA = 5 uM; printed kcat/Km UMA = 80.6 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14900 and applied mutation signature Y194F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Constants of the MurD Mutant Proteins), protein row Y194F; column kcat (min^-1) = 32; column Km UMA (uM) = 111; column kcat/Km UMA (min^-1 uM^-1) = 0.29.

raw_value_unit_evidence: Table 2, protein row Y194F, UMA column group: kcat = 32 min^-1; Km UMA = 111 uM; printed kcat/Km UMA = 0.29 min^-1 uM^-1.


proof_lines: leaderless MtCM with C-terminal His tag, at 30°C and pH 7.5


enzyme_display_name: glutamate racemase

substrate_name: Unknown

enzyme: glutamate racemase

substrate: Unknown


substrate_name: D-glutamate

substrate: D-glutamate


substrate_name: UDP-N-acetylmuramoyl L-alanine

substrate: UDP-N-acetylmuramoyl L-alanine


assay_conditions_summary: pH 9.4; 310.15 K; cofactor ATP


enzyme_display_name: D-alanine--D-alanine ligase

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: competitive inhibition with respect to ATP, at pH 8.0 and 37°C

proof_lines: competitive inhibition with respect to D-alanine, at pH 8.0 and 37°C

enzyme: D-alanine--D-alanine ligase


enzyme_display_name: methionine--tRNA ligase

substrate_name: tRNAMet

enzyme: methionine--tRNA ligase

substrate: tRNAMet


organism: Homo sapiens

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +1, so it is treated as a source-provided variant sequence.


proof_lines:
27°C, pH 7.4, wild-type enzyme
wild-type, 27°C, pH 7.4
22°C, pH 7.4, wild-type enzyme


organism: Mycolicibacterium smegmatis

substrate_name: L-cysteine

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

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

substrate: L-cysteine


enzyme_display_name: L-arabinose isomerase

substrate_name: L-arabinose

proof_lines:
D-galactose induced enzyme
L-arabinose induced enzyme

enzyme: L-arabinose isomerase

substrate: L-arabinose


enzyme_display_name: prokaryotic ubiquitin-like protein ligase

substrate_name: [IdeR]-L-lysine

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

substrate: [IdeR]-L-lysine


enzyme_display_name: adenylate cyclase

organism: Mytilus galloprovincialis

substrate_name: ATP

assay_conditions_summary: pH 7.4; 295.15 K; cofactor ATP

enzyme: adenylate cyclase

substrate: ATP


enzyme_display_name: glutamine synthetase

substrate_name: Glu

enzyme: glutamine synthetase

substrate: Glu


enzyme_display_name: maltose alpha-D-glucosyltransferase

organism: Myxococcus sp. V11

substrate_name: maltose

enzyme: maltose alpha-D-glucosyltransferase

substrate: maltose


organism: Neurospora crassa

assay_conditions_summary: cofactor ATP


enzyme_display_name: glucose-6-phosphate isomerase

organism: Oryctolagus cuniculus

substrate_name: fructose 6-phosphate

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

proof_lines: muscle enzyme, values of 0.01 mM, 0.12 mM and 0.17 mM are determined by different authors

enzyme: glucose-6-phosphate isomerase

substrate: fructose 6-phosphate


enzyme_display_name: aldose 1-epimerase

substrate_name: alpha-D-glucose

enzyme: aldose 1-epimerase

substrate: alpha-D-glucose


enzyme_display_name: 4-coumarate--CoA ligase

organism: Nicotiana tabacum

substrate_name: 4-coumaric acid

assay_conditions_summary: cofactor CoA

enzyme: 4-coumarate--CoA ligase

substrate: 4-coumaric acid


enzyme_display_name: inositol-3-phosphate synthase

organism: Oryza coarctata

substrate_name: D-glucose 6-phosphate

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

proof_lines:
native enzyme
recombinant enzyme

enzyme: inositol-3-phosphate synthase

substrate: D-glucose 6-phosphate


organism: Oryza sativa


enzyme_display_name: cysteine-S-conjugate beta-lyase

enzyme: cysteine-S-conjugate beta-lyase


enzyme_display_name: lactoylglutathione lyase

organism: Oryza sativa Japonica Group

proof_lines:
25°C, pH 7.0, native Glb33
25°C, pH 7.0, recombinant Glb33

enzyme: lactoylglutathione lyase


enzyme_display_name: chorismate mutase

organism: Nicotiana sylvestris

substrate_name: chorismate

proof_lines: enzyme form CM1, weak positive cooperativity

enzyme: chorismate mutase

substrate: chorismate


substrate_name: (R)-S-lactoylglutathione

substrate: (R)-S-lactoylglutathione


proof_lines: recombinant enzyme, pH 7.2, temperature not specified in the publication


enzyme_display_name: D-cysteine desulfhydrase

substrate_name: D-cysteine

enzyme: D-cysteine desulfhydrase

substrate: D-cysteine


enzyme_display_name: mannose-6-phosphate isomerase

substrate_name: D-mannose 6-phosphate

enzyme: mannose-6-phosphate isomerase

substrate: D-mannose 6-phosphate


enzyme_display_name: GDP-mannose 3,5-epimerase

substrate_name: GDP-D-mannose

assay_conditions_summary: cofactor NAD+

proof_lines: pH and temperature not specified in the publication

enzyme: GDP-mannose 3,5-epimerase

substrate: GDP-D-mannose


organism: Ovis aries

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: xylose isomerase

organism: Parabacteroides sp.

substrate_name: alpha-D-xylopyranose

enzyme: xylose isomerase

substrate: alpha-D-xylopyranose


enzyme_display_name: prostaglandin-E synthase

substrate_name: prostaglandin H2

proof_lines:
IgG1(hei-7)-reactive protein
IgG1(hei-26)-reactive protein

enzyme: prostaglandin-E synthase

substrate: prostaglandin H2


organism: Paramecium tetraurelia


enzyme_display_name: L-arabinose isomerase

organism: Pediococcus pentosaceus

substrate_name: D-galactose

proof_lines:
at 50°C and pH 6.0
pH 6.0, 50°C, recombinant enzyme

substrate: D-galactose


enzyme_display_name: serine racemase

organism: Penaeus monodon

substrate_name: D-serine

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

enzyme: serine racemase

substrate: D-serine


enzyme_display_name: alanine racemase

organism: Peribacillus psychrosaccharolyticus

substrate_name: D-Ala

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

enzyme: alanine racemase

substrate: D-Ala


enzyme_display_name: glutamine synthetase

organism: Phaseolus vulgaris

substrate_name: L-glutamate

substrate: L-glutamate


organism: Parageobacillus thermoglucosidasius

proof_lines:
at pH 7.0 and 40°C
pH 7.0, 40°C, recombinant enzyme

enzyme: L-arabinose isomerase


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

organism: Photinus pyralis

substrate_name: lauric acid

smiles: CCCCCCCCCCCC(=O)O

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

substrate: lauric acid


organism: Paracoccus denitrificans

substrate_name: cystathionine

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

substrate: cystathionine


enzyme_display_name: steroid Delta-isomerase

organism: Bos taurus

enzyme: steroid Delta-isomerase


enzyme_display_name: adenylate cyclase

organism: Phycomyces blakesleeanus

substrate_name: ATP

enzyme: adenylate cyclase

substrate: ATP


enzyme_display_name: leucine--tRNA ligase

substrate_name: Leu-tRNALeu

proof_lines:
substrate from E. coli
unfractionated substrate of E. coli

enzyme: leucine--tRNA ligase

substrate: Leu-tRNALeu


organism: Piromyces sp. E2


organism: Plasmodium falciparum

proof_lines: recombinant AC expressed from synthetic AC gene PfAC526-884


organism: Physcomitrium patens

assay_conditions_summary: pH 8

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


enzyme_display_name: tyrosine--tRNA ligase

substrate_name: tRNATyr

enzyme: tyrosine--tRNA ligase

substrate: tRNATyr


organism: Piromyces sp.

substrate_name: D-xylose

substrate: D-xylose


enzyme_display_name: glucose-6-phosphate isomerase

substrate_name: fructose 6-phosphate

enzyme: glucose-6-phosphate isomerase

substrate: fructose 6-phosphate


enzyme_display_name: methylmalonyl-CoA mutase

organism: Propionibacterium freudenreichii subsp. shermanii

substrate_name: succinyl-CoA

enzyme: methylmalonyl-CoA mutase

substrate: succinyl-CoA


enzyme_display_name: glutamate--cysteine ligase

organism: Proteus mirabilis

enzyme: glutamate--cysteine ligase


assay_conditions_summary: 303.15 K; cofactor CoA

proof_lines: 30°C, with 5'-deoxyadenosylcobinamide GDP as cofactor

proof_lines: 30°C, with 5'-adenosylcobalamin as cofactor


organism: Pseudomonas aeruginosa

substrate_name: L-cysteine

substrate: L-cysteine


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


enzyme_display_name: triose-phosphate isomerase

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: methionine gamma-lyase

organism: Porphyromonas gingivalis

enzyme: methionine gamma-lyase


enzyme_display_name: isochorismate synthase

substrate_name: chorismate

enzyme: isochorismate synthase

substrate: chorismate


enzyme_display_name: UDP-glucose 4-epimerase

substrate_name: UDP-alpha-D-glucose

enzyme: UDP-glucose 4-epimerase

substrate: UDP-alpha-D-glucose


enzyme_display_name: phenylalanine--tRNA ligase

organism: Plasmodium vivax

substrate_name: Unknown

enzyme: phenylalanine--tRNA ligase

substrate: Unknown


enzyme_display_name: 4-hydroxyproline epimerase

enzyme: 4-hydroxyproline epimerase


enzyme_display_name: anthranilate--CoA ligase

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

enzyme: anthranilate--CoA ligase


assay_conditions_summary: pH 8.5; 313.15 K; cofactor ATP


enzyme_display_name: mannose-6-phosphate isomerase

substrate_name: mannose 6-phosphate

proof_lines: bifunctional enzyme: phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase

enzyme: mannose-6-phosphate isomerase

substrate: mannose 6-phosphate


enzyme_display_name: alanine racemase

enzyme: alanine racemase


enzyme_display_name: glutamate--tRNA ligase

substrate_name: tRNAGlu

enzyme: glutamate--tRNA ligase

substrate: tRNAGlu


enzyme_display_name: aspartate--tRNA(Asn) ligase

substrate_name: tRNAAsn

proof_lines:
at pH 7.2 and 37°C
tRNAAsp aspartylation
tRNAAsn aspartylation

enzyme: aspartate--tRNA(Asn) ligase

substrate: tRNAAsn


proof_lines: in 50 mM HEPES, pH 8.0, with 2 mM beta-mercaptoethanol,1 mM EDTA, at 37°C


substrate_name: D-galactose

substrate: D-galactose


substrate_name: mannose 1-phosphate

substrate: mannose 1-phosphate


enzyme_display_name: glutamine--tRNA ligase

substrate_name: tRNAGln

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

enzyme: glutamine--tRNA ligase

substrate: tRNAGln


organism: Pseudomonas fluorescens

substrate_name: D-alanine

substrate: D-alanine


organism: Pseudomonas putida

substrate_name: L-alanine

assay_conditions_summary: pH 9; 310.15 K; buffer pH 7

substrate: L-alanine


enzyme_display_name: 2-hydroxymuconate tautomerase

proof_lines:
D-4OT enantiomer, pH 7.3, 30°C
L-4OT enantiomer, pH 7.3, 30°C
pH 7.3, 30°C

enzyme: 2-hydroxymuconate tautomerase


enzyme_display_name: amino-acid racemase

substrate_name: D-Met

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

proof_lines: crude lyophilisates, 30°C, pH 7, Vmax: 2075 micromol/min/g

proof_lines: crude lyophilisates, 25°C, pH 7, Vmax: 2150 micromol/min/g

enzyme: amino-acid racemase

substrate: D-Met


substrate_name: D-mannose 6-phosphate

substrate: D-mannose 6-phosphate


substrate_name: D-ornithine

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

proof_lines: pH and temperature not specified in the publication, in 40% methanol

proof_lines: pH and temperature not specified in the publication, in 20% methanol

proof_lines: pH and temperature not specified in the publication, in 10% methanol

substrate: D-ornithine


proof_lines:
at pH 7.3 and 22°C
pH 7.3, 30°C


substrate_name: L-Ala

substrate: L-Ala


enzyme_display_name: maleate isomerase

substrate_name: Maleate

enzyme: maleate isomerase

substrate: Maleate


proof_lines:
solvent H2O
2-2H-4-hydroxy-L-Pro
solvent 2H2O


enzyme_display_name: steroid Delta-isomerase

organism: Pseudomonas sp.

enzyme: steroid Delta-isomerase


enzyme_display_name: muconate cycloisomerase

organism: Pseudomonas reinekei

substrate_name: cis,cis-muconate

enzyme: muconate cycloisomerase

substrate: cis,cis-muconate


enzyme_display_name: prostaglandin-D synthase

organism: Rattus norvegicus

enzyme: prostaglandin-D synthase


enzyme_display_name: lanosterol synthase

enzyme: lanosterol synthase


enzyme_display_name: methylmalonyl-CoA epimerase

organism: Pyrococcus horikoshii

substrate_name: methylmalonyl-CoA

enzyme: methylmalonyl-CoA epimerase

substrate: methylmalonyl-CoA


enzyme_display_name: alkylmercury lyase

substrate_name: p-chloromercuribenzoic acid

enzyme: alkylmercury lyase

substrate: p-chloromercuribenzoic acid


enzyme_display_name: cholate--CoA ligase

substrate_name: cholate

enzyme: cholate--CoA ligase

substrate: cholate


enzyme_display_name: glutamate--cysteine ligase

substrate_name: glutamate

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

proof_lines: enzyme from visceral yolk sac homogenate

enzyme: glutamate--cysteine ligase

substrate: glutamate


enzyme_display_name: alpha-methylacyl-CoA racemase

substrate_name: (S)-ibuprofenoyl-CoA

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

enzyme: alpha-methylacyl-CoA racemase

substrate: (S)-ibuprofenoyl-CoA


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: glutamine synthetase

enzyme: glutamine synthetase


enzyme_display_name: guanylate cyclase

enzyme: guanylate cyclase


substrate_name: Prostaglandin H2

substrate: Prostaglandin H2


enzyme_display_name: selenocysteine lyase

enzyme: selenocysteine lyase


enzyme_display_name: DNA topoisomerase (ATP-hydrolyzing)

substrate_name: ATP

proof_lines: pH and temperature not specified in the publication

enzyme: DNA topoisomerase (ATP-hydrolyzing)

substrate: ATP


substrate_name: CoA

substrate: CoA


substrate_name: L-Cys

proof_lines: ATP, holoenzyme and recombinant heavy subunit

substrate: L-Cys


substrate_name: guanyl-imidodiphosphate

substrate: guanyl-imidodiphosphate


enzyme_display_name: lysine--tRNA ligase

substrate_name: tRNALys

proof_lines:
18S synthetase complex
free enzyme
lysylation, free enzyme

enzyme: lysine--tRNA ligase

substrate: tRNALys


enzyme_display_name: arachidonate--CoA ligase

substrate_name: arachidonate

smiles: CCCCCC=CCC=CCC=CCC=CCCCC(=O)[O-]

proof_lines:
pH 8, 37°C, 10-day-old rats
pH 8, 37°C, 70-day-old rats

enzyme: arachidonate--CoA ligase

substrate: arachidonate


enzyme_display_name: inositol-3-phosphate synthase

substrate_name: glucose 6-phosphate

enzyme: inositol-3-phosphate synthase

substrate: glucose 6-phosphate


enzyme_display_name: glutathione synthase

substrate_name: N-acetyl-L-Cys

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

enzyme: glutathione synthase

substrate: N-acetyl-L-Cys


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

substrate_name: eicosapentaenoate

smiles: CCC=CCC=CCC=CCC=CCC=CCCCC(=O)O

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

substrate: eicosapentaenoate


enzyme_display_name: pancreatic ribonuclease

substrate_name: cyclic 2',3'-UMP

enzyme: pancreatic ribonuclease

substrate: cyclic 2',3'-UMP


substrate_name: GTP

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: 30°C, pH 8.0, in the presence of N-(beta-D-glucopyranosyl-N2-acetyl-S-nitroso-D,L-penicillaminamide) and YC-1

proof_lines: 30°C, pH 8.0, in the presence of N-(beta-D-glucopyranosyl-N2-acetyl-S-nitroso-D,L-peniciiaminamide)

substrate: GTP


substrate_name: AMP

substrate: AMP


enzyme_display_name: leukotriene-C4 synthase

substrate_name: leukotriene A4

enzyme: leukotriene-C4 synthase

substrate: leukotriene A4


substrate_name: D-glucose 6-phosphate

substrate: D-glucose 6-phosphate


enzyme_display_name: medium-chain acyl-CoA ligase

substrate_name: Butyrate

smiles: CCCC(=O)[O-]

enzyme: medium-chain acyl-CoA ligase

substrate: Butyrate


substrate_name: stearate

smiles: CCCCCCCCCCCCCCCCCC(=O)[O-]

substrate: stearate


proof_lines:
recombinant heavy subunit
L-Glu, holoenzyme
L-Glu, kidney enzyme


enzyme_display_name: adenylate cyclase

proof_lines: VC1-IIC2 in the presence of 0.1 mM forskolin and GTPgammaS-activated Galphas

enzyme: adenylate cyclase


enzyme_display_name: prostaglandin-E synthase

substrate_name: Prostaglandin H2

proof_lines:
cPGES plus casein kinase II plus Hsp90
GSH-dependent enzyme from deferent duct
cPGES plus casein kinase II

enzyme: prostaglandin-E synthase

substrate: Prostaglandin H2


enzyme_display_name: phosphomannomutase

substrate_name: mannose 1-phosphate

enzyme: phosphomannomutase

substrate: mannose 1-phosphate


substrate_name: Coenzyme A; ATP; Palmitate

substrate: Coenzyme A; ATP; Palmitate


enzyme_display_name: triose-phosphate isomerase

organism: Rhipicephalus microplus

substrate_name: D-glyceraldehyde 3-phosphate

proof_lines: in 100 mM triethanolamine, pH 7.4, at 25°C

enzyme: triose-phosphate isomerase

substrate: D-glyceraldehyde 3-phosphate


enzyme_display_name: serine racemase

substrate_name: L-serine

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

enzyme: serine racemase

substrate: L-serine


organism: Rhizobium etli

substrate_name: ATP

substrate: ATP


enzyme_display_name: chaperonin ATPase

organism: Rhizobium leguminosarum

assay_conditions_summary: 293.15 K; cofactor ATP

enzyme: chaperonin ATPase


enzyme_display_name: aldose 1-epimerase

organism: Rhizopus stolonifer

substrate_name: alpha-D-glucose

enzyme: aldose 1-epimerase

substrate: alpha-D-glucose


enzyme_display_name: maleate isomerase

organism: Rhodococcus jostii

substrate_name: Maleate

proof_lines: pH 8.0, 40°C, recombinant enzyme mutant MaiR-D48/49-304AA

enzyme: maleate isomerase

substrate: Maleate


enzyme_display_name: muconate cycloisomerase

enzyme: muconate cycloisomerase


enzyme_display_name: muconolactone Delta-isomerase

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

substrate_name: muconolactone

enzyme: muconolactone Delta-isomerase

substrate: muconolactone


enzyme_display_name: ribose-5-phosphate isomerase

organism: Rhodospirillum rubrum

substrate_name: D-ribose 5-phosphate

enzyme: ribose-5-phosphate isomerase

substrate: D-ribose 5-phosphate


enzyme_display_name: cellobiose epimerase

organism: Roseburia intestinalis

substrate_name: cellobiose

enzyme: cellobiose epimerase

substrate: cellobiose


enzyme_display_name: L-cysteate sulfo-lyase

organism: Ruegeria pomeroyi

substrate_name: L-cysteate

enzyme: L-cysteate sulfo-lyase

substrate: L-cysteate


organism: Rhodothermus marinus


organism: Ruminococcus albus

substrate_name: lactose

proof_lines: recombinant enzyme, 100 mM sodium phosphate, 20 mM lactose, pH 7.5, 30°C

substrate: lactose


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

smiles: CSCCC(=O)[O-]

assay_conditions_summary: pH 8; 313.15 K; cofactor CoA

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


organism: Saccharolobus shibatae

substrate_name: maltohexaose

substrate: maltohexaose


enzyme_display_name: DNA 3'-5' helicase

organism: Saccharolobus solfataricus

proof_lines: pH and temperature not specified in the publication, mutant enzyme L189D/D191R

enzyme: DNA 3'-5' helicase


enzyme_display_name: aliphatic aldoxime dehydratase

organism: Rhodococcus sp. N-771

proof_lines:
ferric oxidation state, pH 7.0, 23°C
ferrous oxidation state, pH 7.0, 23°C

enzyme: aliphatic aldoxime dehydratase


enzyme_display_name: aspartate--tRNA ligase

organism: Saccharomyces cerevisiae

substrate_name: tRNAAsp

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

enzyme: aspartate--tRNA ligase

substrate: tRNAAsp


enzyme_display_name: tyrosine--tRNA ligase

substrate_name: native yeast tRNATyr

enzyme: tyrosine--tRNA ligase

substrate: native yeast tRNATyr


enzyme_display_name: glutamate--cysteine ligase

organism: Rattus norvegicus

enzyme: glutamate--cysteine ligase


enzyme_display_name: phenylalanine--tRNA ligase

substrate_name: L-phenylalanine

enzyme: phenylalanine--tRNA ligase

substrate: L-phenylalanine


substrate_name: Glucose 1-phosphate

proof_lines: recombinant His-tagged Pgm2, pH 7.5, 30°C

proof_lines: recombinant His-tagged Pgm3, pH 7.5, 30°C

substrate: Glucose 1-phosphate


enzyme_display_name: lactoylglutathione lyase

enzyme: lactoylglutathione lyase


enzyme_display_name: glutamine synthetase

enzyme: glutamine synthetase


enzyme_display_name: lanosterol synthase

substrate_name: Unknown

enzyme: lanosterol synthase

substrate: Unknown


proof_lines:
mutant H181A
H181A mutant


enzyme_display_name: peptidylprolyl isomerase

proof_lines: 20°C, pH 7.4, wild-type Ypa2, presence of 1 mM MgATP

enzyme: peptidylprolyl isomerase


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: pH 7.6, 30°C, in presence of M13mp18 single-stranded circular DNA


enzyme_display_name: tetrahydrofolate synthase

organism: Neurospora crassa

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

enzyme: tetrahydrofolate synthase


substrate_name: glutathione

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

proof_lines: the apparent kinetic parameters are determined by using hemithioacetal as substrate, which is obtained by the nonenzymatic reaction between glutathione and methylglyoxal

substrate: glutathione


substrate_name: L-Tyr

sequence_source: UniProtKB/Swiss-Prot

substrate: L-Tyr


enzyme_display_name: glucose-6-phosphate 1-epimerase

substrate_name: beta-D-glucose 6-phosphate

enzyme: glucose-6-phosphate 1-epimerase

substrate: beta-D-glucose 6-phosphate


enzyme_display_name: leucine--tRNA ligase

substrate_name: tRNALeu

enzyme: leucine--tRNA ligase

substrate: tRNALeu


substrate_name: Glycerate 3-phosphate

proof_lines:
phosphatase activity
mutase activity

substrate: Glycerate 3-phosphate


enzyme_display_name: glutamate--tRNA ligase

substrate_name: tRNAGlu

proof_lines: pH and temperature not specified in the publication

enzyme: glutamate--tRNA ligase

substrate: tRNAGlu


organism: Datura inoxia


substrate_name: ATP

substrate: ATP


substrate_name: L-Glu

substrate: L-Glu


organism: Escherichia coli

source_db: skid

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

assay_conditions_summary: pH 9.8; cofactor ATP

proof_lines: kcat is 25 min(-1) with 7,8-dihydropteroate as substrate (at 30 degrees Celsius).

source_databases_merged: skid uniprot

source: skid


organism: Homo sapiens

substrate_name: aminopterin

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D378A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

proof_lines: pH 8.9, 37°C, charcoal assay, D378A mutant

substrate: aminopterin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D376A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.9; 310.15 K; cofactor ATP

proof_lines: pH 8.9, 37°C, charcoal assay, D376A mutant


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D335A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


substrate_name: L-Glutamic acid

substrate: L-Glutamic acid


enzyme_display_name: phosphopentomutase

substrate_name: alpha-D-ribose 1-phosphate

enzyme: phosphopentomutase

substrate: alpha-D-ribose 1-phosphate


substrate_name: n-1 n-1 n-1 ATP; 10-Formyltetrahydrofolyl L-glutamate; n-1 n-1 n-1 L-Glutamate

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

source_databases_merged: sabio_rk skid uniprot


organism: Mus musculus

proof_lines:
L1210 isoform
liver isoform
pH 8.9, 37°C, L1210 isoform


organism: Plasmodium falciparum


organism: Escherichia coli (strain K12)


substrate_name: tetrahydrofolate

substrate: tetrahydrofolate


organism: Lacticaseibacillus casei

source_license: CC BY-NC-ND 4.0


assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.5
Raw SKiD Env: Temp=-----, pH=9.8


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7.5
Raw SKiD Env: Temp=-----, pH=9.8


organism: Lactobacillus casei

substrate_name: n-1 n-1 n-1 L-Glutamate; (6R)-5,10-Methylene-5,6,7,8-tetrahydropteroyl-diglutamate; n-1 n-1 n-1 ATP

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


column_label: Abstract reports tetrahydrofolate (THF) exhibited standard kinetics with an apparent K(m) of 0.96 microM.

raw_value_unit_evidence: Km raw_value=0.96 microM raw_unit=microM

row_label: Plasmodium falciparum PfDHFS-FPGS FPGS assay / THF

table_label: PubMed XML abstract PMID 20350571


proof_lines: pH 8.9, 37°C, charcoal assay, wild type recombinant enzyme


proof_lines: pH 8.9, 37°C, charcoal assay, K384A mutant


proof_lines: pH 8.9, 37°C, charcoal assay, C346A mutant


substrate_name: glutamic acid

substrate: glutamic acid


organism: Hapsidospora chrysogena

substrate_name: L-aminoadipate

substrate: L-aminoadipate


substrate_name: L-valine

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

substrate: L-valine


enzyme_display_name: UniProt Q5JIZ8

organism: Thermococcus kodakarensis

substrate_name: beta-Alanine

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

enzyme: UniProt Q5JIZ8

substrate: beta-Alanine


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

proof_lines:
pH 7.5, wild type enzyme
wild-type

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


proof_lines:
pH 7.5, wild type enzyme
wild-type, pH 9.8


organism: Bos taurus


substrate_name: methotrexate

substrate: methotrexate


assay_conditions_summary: pH 6.5; 358.15 K; cofactor ATP


organism: Sus scrofa

assay_conditions_summary: cofactor ATP

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


substrate_name: dATP

substrate: dATP


substrate_name: ITP

substrate: ITP


substrate_name: UTP

substrate: UTP


organism: Acinetobacter calcoaceticus

substrate_name: ATP

assay_conditions_summary: pH 8.2; 303.15 K; cofactor ATP

proof_lines: 30°C, pH 8.2, for the L-aspartic acid-ATP binding site alone


substrate_name: L-aspartic acid

substrate: L-aspartic acid


proof_lines: 30°C, pH 8.2, for the L-arginine-ATP binding site alone


substrate_name: L-arginine

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

substrate: L-arginine


substrate_name: L-glutamate (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)

column_label: General Properties prose states the Km values for L-glutamate and MgATP were 201 uM and 200 uM; L-glutamate maps to 201 uM.

raw_value_unit_evidence: Km raw_value=201 raw_unit=uM

row_label: L-glutamate Km prose

table_label: PMID 8662720 JBC General Properties prose


substrate_name: MgATP (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)

column_label: General Properties prose states the Km values for L-glutamate and MgATP were 201 uM and 200 uM; MgATP maps to 200 uM.

raw_value_unit_evidence: Km raw_value=200 raw_unit=uM

row_label: MgATP Km prose


substrate_name: pteroylglutamic acid (PteGlu) (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)


substrate_name: aminopterin (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)

column_label: Table III columns are Substrate, Km, Vmax (rel), Vmax/Km (rel); row Aminopterin has Km 4.4 uM, Vmax 118, Vmax/Km 118.

raw_value_unit_evidence: Km raw_value=4.4 raw_unit=uM

row_label: Aminopterin

table_label: PMID 8662720 JBC Table III


substrate_name: methotrexate (isoform 2, at 37 degrees Celsius in the presence of 10 mM ATP and pH 8.5)


substrate: ATP


substrate_name: glutamate

substrate: glutamate


substrate_name: UDP-N-acetyl-alpha-D-muramate

substrate: UDP-N-acetyl-alpha-D-muramate


enzyme_display_name: dapdiamide synthase

organism: Enterobacter agglomerans

substrate_name: valine

proof_lines: kcat is 8.1 min(-1) with valine as substrate. kcat is 9.5 min(-1) with isoleucine as substrate. kcat is 11.2 min(-1) with leucine as substrate (PubMed:19807062). kcat is 21 min(-1) with N-beta-fumaramoyl-DAP as substrate. kcat is 181 min(-1

enzyme: dapdiamide synthase

substrate: valine


substrate_name: isoleucine

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

substrate: isoleucine


substrate_name: leucine

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

substrate: leucine


substrate_name: 5,10-dideazatetrahydrofolic acid

substrate: 5,10-dideazatetrahydrofolic acid


substrate_name: aminopterin

substrate: aminopterin


enzyme_display_name: D-alanine--D-serine ligase

organism: Enterococcus casseliflavus

substrate_name: D-serine

proof_lines: kcat is 490 min(-1) with D-serine as substrate (at pH 7.5) (PubMed:9294159). kcat is 1092 min(-1) with D-serine as substrate (at pH 7.5) (PubMed:9545431). kcat is 178 min(-1) with D-alanine as substrate (at pH 7.5) (PubMed:9545431). kcat is

enzyme: D-alanine--D-serine ligase

substrate: D-serine


substrate_name: D-asparagine

substrate: D-asparagine


organism: Enterococcus faecalis

substrate_name: CTP

substrate: CTP


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


substrate_name: L-cysteine

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

substrate: L-cysteine


substrate_name: fumarate

proof_lines: kcat is 11.6 sec(-1) with fumarate as substrate. kcat is 3.8 sec(-1) with succinate as substrate.

substrate: fumarate


substrate_name: succinate

substrate: succinate


enzyme_display_name: jasmonoyl--L-amino acid ligase

organism: Arabidopsis thaliana

substrate_name: L-Ile

assay_conditions_summary: pH 8.6; cofactor ATP

proof_lines: All results obtained at pH 8.6 and 25 degrees Celsius (PubMed:18247047). kcat is 2.72 sec(-1) with ATP as substrate (in the presence of JA). kcat is 6.32 sec(-1) with ATP as substrate (in the presence of JA and when in complex with GSTU20/F

enzyme: jasmonoyl--L-amino acid ligase

substrate: L-Ile


substrate_name: L-Phe

substrate: L-Phe


substrate_name: L-Leu

substrate: L-Leu


substrate_name: L-Val

substrate: L-Val


enzyme_display_name: L-2,3-diaminopropanoate--citrate ligase

organism: Staphylococcus aureus

substrate_name: citrate

proof_lines: pH 7.4, temperature not specified in the publication

proof_lines: kcat is 16.08 min(-1) with citrate as substrate.

enzyme: L-2,3-diaminopropanoate--citrate ligase

substrate: citrate


organism: Geminocystis herdmanii PCC 6308

substrate_name: ATP

assay_conditions_summary: pH 8.2; cofactor ATP

proof_lines: pH and temperature not specified in the publication

substrate: ATP


substrate_name: D-alanine (at pH 7.5)

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

substrate: D-alanine (at pH 7.5)


substrate_name: D-threonine (at pH 7.5)

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

substrate: D-threonine (at pH 7.5)


substrate_name: D-homoserine (at pH 7.5)

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

substrate: D-homoserine (at pH 7.5)


organism: Methanocaldococcus jannaschii

substrate_name: ATP; Coenzyme gamma-F420-2; L-Glutamate

substrate: ATP; Coenzyme gamma-F420-2; L-Glutamate


substrate_name: GTP; L-Glutamate; Coenzyme F420-1

source_databases_merged: sabio_rk brenda uniprot

substrate: GTP; L-Glutamate; Coenzyme F420-1


enzyme_display_name: [amino-group carrier protein]--L-2-aminoadipate ligase

organism: Thermus thermophilus


enzyme_display_name: tenuazonic acid synthetase

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

substrate_name: N-acetoacetyl-L-Ile-SNAC (for the KS domain)

enzyme: tenuazonic acid synthetase


enzyme_display_name: beta-tubulin-glutamate ligase

organism: Mus musculus

substrate_name: [beta-tubulin]-L-glutamate

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines: pH 7.0, 30°C, enzyme from adult brain, 0.006 mM L-glutamate

proof_lines: pH 7.0, 30°C, enzyme from newborn brain, 0.05 mM L-glutamate

enzyme: beta-tubulin-glutamate ligase

substrate: [beta-tubulin]-L-glutamate


substrate_name: L-glutamate

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

proof_lines: pH 7.0, 30°C, enzyme from newborn brain, 0.05 mM ATP

proof_lines: pH 7.0, 30°C, enzyme from adult brain, 0.05 mM ATP

substrate: L-glutamate


enzyme_display_name: tubulin-glutamate ligase

organism: Crithidia fasciculata

substrate_name: [alpha/beta-tubulin]-L-glutamate

assay_conditions_summary: pH 9

proof_lines: at pH 9.0, temperature not specified in the publication

enzyme: tubulin-glutamate ligase

substrate: [alpha/beta-tubulin]-L-glutamate


substrate_name: [modified porcine brain tubulin]-L-glutamate


assay_conditions_summary: pH 8.7; 303.15 K; cofactor ATP


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

substrate_name: L-lysine (at pH 9.4)

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

proof_lines: The catalytic efficiency for the L-lysine adding activity is 4-fold and 10-fold higher than that for the D-lysine and meso-diaminopimelate adding activity, respectively.

substrate: L-lysine (at pH 9.4)


substrate_name: meso-diaminopimelate (at pH 9.4)

substrate: meso-diaminopimelate (at pH 9.4)


substrate_name: L-ornithine (at pH 9.4)

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

substrate: L-ornithine (at pH 9.4)


organism: Hapsidospora chrysogena

substrate_name: cysteine

substrate: cysteine


enzyme_display_name: 4-phosphopantoate--beta-alanine ligase

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

substrate_name: Unknown

enzyme: 4-phosphopantoate--beta-alanine ligase

substrate: Unknown


substrate_name: UDP-N-acetylmuramoyl-L-Ala-D-Glu

substrate: UDP-N-acetylmuramoyl-L-Ala-D-Glu


organism: Escherichia coli (strain K12)


substrate_name: N-beta-fumaramoyl-DAP

substrate: N-beta-fumaramoyl-DAP


enzyme_display_name: L-alanine--L-anticapsin ligase

organism: Bacillus subtilis (strain 168)

proof_lines: kcat is 9.32 sec(-1) for ligase activity with alanine as substrate (PubMed:24702628). kcat is 10.4 sec(-1) for ligase activity with phenylalanine as substrate (PubMed:24702628). kcat is 630 min(-1) for ligase activity with alanine and pheny

enzyme: L-alanine--L-anticapsin ligase


organism: Homo sapiens


enzyme_display_name: UniProt P13000

organism: Escherichia coli

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

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

enzyme: UniProt P13000

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


enzyme_display_name: UniProt P9WPQ5

organism: Mycobacterium tuberculosis

enzyme: UniProt P9WPQ5


enzyme_display_name: UniProt P0DJQ7

organism: Streptomyces clavuligerus

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

enzyme: UniProt P0DJQ7


substrate_name: L-Arg

substrate: L-Arg


substrate_name: ATP

substrate: ATP


enzyme_display_name: tetrahydrofolate synthase

substrate_name: H(2)PteGlu (isoform 2 at 37 degrees Celsius in the presence of 1 mM ATP and 2 mM L-glutamate)

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

enzyme: tetrahydrofolate synthase


organism: Lacticaseibacillus casei


organism: Neurospora crassa


organism: Synechocystis sp.

substrate_name: [L-Asp(4-L-Arg)]n; L-Aspartate; ATP

substrate: [L-Asp(4-L-Arg)]n; L-Aspartate; ATP


enzyme_display_name: coenzyme F420-0:L-glutamate ligase

organism: Methanocaldococcus jannaschii

substrate_name: GTP; Coenzyme F420-0; L-Glutamate

enzyme: coenzyme F420-0:L-glutamate ligase

substrate: GTP; Coenzyme F420-0; L-Glutamate


organism: Thermus thermophilus

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

assay_conditions_summary: pH 8

enzyme: [amino-group carrier protein]--L-2-aminoadipate ligase


assay_conditions_summary: pH 8; cofactor ATP


assay_conditions_summary: pH 8; 333.15 K; cofactor ATP


organism: Arabidopsis thaliana


organism: Bacillus subtilis

substrate_name: L-alanine

assay_conditions_summary: pH 7.1; 310.15 K; cofactor ATP

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.1
Raw SKiD Env: Temp=37°C, pH=7.7
Raw SKiD Env: Temp=37°C, pH=9

substrate: L-alanine


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


organism: Amycolatopsis lactamdurans

substrate_name: L-cysteine

assay_conditions_summary: pH 7; cofactor ATP

column_label: Fig. 3D/Michaelis-Menten prose; substrate L-cysteine; apparent KM value 40 +/- 1 uM.

normalized_value_unit_evidence: 40 uM normalizes to 0.04 mM.

raw_value_unit_evidence: Results prose reports apparent KM values of 40 +/- 1 uM for L-cysteine.

row_label: L-cysteine

table_label: Results prose and Fig. 3D: Enzymatic characterization of ACVS

substrate: L-cysteine


substrate_name: L-valine

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

column_label: Fig. 3D/Michaelis-Menten prose; substrate L-valine; apparent KM value 150 +/- 4 uM.

normalized_value_unit_evidence: 150 uM normalizes to 0.15 mM.

raw_value_unit_evidence: Results prose reports apparent KM values of 150 +/- 4 uM for L-valine.

row_label: L-valine

substrate: L-valine


column_label: Fig. 3D/Michaelis-Menten prose; substrate L-alpha-aminoadipic acid; apparent KM value 640 +/- 16 uM.

normalized_value_unit_evidence: L-2-aminohexanedioate is L-alpha-aminoadipic acid; 640 uM normalizes to 0.64 mM.

raw_value_unit_evidence: Results prose reports apparent KM values of 640 +/- 16 uM for L-alpha-aminoadipic acid.

row_label: L-alpha-aminoadipic acid


enzyme_display_name: 5-formyltetrahydrofolate cyclo-ligase

organism: Mycoplasmoides pneumoniae

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R7A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6

proof_lines: mutant enzyme R7A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C

enzyme: 5-formyltetrahydrofolate cyclo-ligase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K3D/D151K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K3D/D151K, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K3A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K3A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R125A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R125A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D81A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D81A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W153A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W153A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D151A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D151A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C


assay_conditions_summary: pH 6; cofactor ATP


proof_lines: mutant enzyme K3A, Km above 5 mM, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C


proof_lines: mutant enzyme R7A, Km above 5 mM, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C


proof_lines: mutant enzyme R125A, Km above 5 mM, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C


proof_lines: mutant enzyme W153A, Km above 5 mM, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C


enzyme_display_name: dethiobiotin synthase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G169N to reconstruct the assayed variant sequence.

enzyme: dethiobiotin synthase


substrate_name: CTP

substrate: CTP


substrate_name: GTP

substrate: GTP


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


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

assay_conditions_summary: pH 7.5; buffer FP; cofactor ATP

column_label: TABLE 1 row NaHCO3 inside the MtDTBS enzyme block supplies both metric cells: Km = 3074.3 ± 352.4 under the column header Km (μM) and kcat = 9.9 ± 0.6 under the column header kcat (s-1) (x 10-3). Both cells lie on that single printed row, so the tuple spans no second row, no second column and no second enzyme block.

normalized_value_unit_evidence: metric: Km; raw value: 3074.3 ± 352.4 μM; raw unit: uM; normalized value: 3.074 mM; metric: kcat; raw value: 9.9 ± 0.6 (x 10-3) s-1; raw unit: s^-1 (column scaled by x 10-3); normalized value: 0.0099 s^(-1); metric: kcat/Km; normalized value: 0.0032205595315549776 s^(-1)*mM^(-1); assay condition: 37 degC in FP buffer: 50 mM Tris (pH 7.5), 150 mM NaCl, 5 mM MgCl2, 10 mM NaHCO3, supplemented with 0.3 mM ATP and 0.1 mM DAPA; steady-state analysis varying one substrate with the other two at saturating concentrations; mean +/- SEM of three independent experiments.

raw_value_unit_evidence: TABLE 1, MtDTBS enzyme block, substrate row NaHCO3: the Km (μM) cell prints 3074.3 ± 352.4 and the kcat (s-1) (x 10-3) cell prints 9.9 ± 0.6. TABLE 1 prints no kcat/Km column.

row_label: MtDTBS block, substrate row NaHCO3

table_label: TABLE 1. Kinetic analysis of substrates.


substrate_name: ITP

column_label: TABLE 1 row ITP inside the MtDTBS enzyme block supplies both metric cells: Km = 17.7 ± 1.7 under the column header Km (μM) and kcat = 10.2 ± 1.2 under the column header kcat (s-1) (x 10-3). Both cells lie on that single printed row, so the tuple spans no second row, no second column and no second enzyme block.

normalized_value_unit_evidence: metric: Km; raw value: 17.7 ± 1.7 μM; raw unit: uM; normalized value: 0.018 mM; metric: kcat; raw value: 10.2 ± 1.2 (x 10-3) s-1; raw unit: s^-1 (column scaled by x 10-3); normalized value: 0.0102 s^(-1); metric: kcat/Km; normalized value: 0.5666666666666668 s^(-1)*mM^(-1); assay condition: 37 degC in FP buffer: 50 mM Tris (pH 7.5), 150 mM NaCl, 5 mM MgCl2, 10 mM NaHCO3, supplemented with 0.3 mM ATP and 0.1 mM DAPA; steady-state analysis varying one substrate with the other two at saturating concentrations; mean +/- SEM of three independent experiments.

raw_value_unit_evidence: TABLE 1, MtDTBS enzyme block, substrate row ITP: the Km (μM) cell prints 17.7 ± 1.7 and the kcat (s-1) (x 10-3) cell prints 10.2 ± 1.2. TABLE 1 prints no kcat/Km column.

row_label: MtDTBS block, substrate row ITP

substrate: ITP


column_label: TABLE 1 row GTP inside the MtDTBS enzyme block supplies both metric cells: Km = 26.3 ± 0.5 under the column header Km (μM) and kcat = 11.1 ± 0.1 under the column header kcat (s-1) (x 10-3). Both cells lie on that single printed row, so the tuple spans no second row, no second column and no second enzyme block.

normalized_value_unit_evidence: metric: Km; raw value: 26.3 ± 0.5 μM; raw unit: uM; normalized value: 0.026 mM; metric: kcat; raw value: 11.1 ± 0.1 (x 10-3) s-1; raw unit: s^-1 (column scaled by x 10-3); normalized value: 0.0111 s^(-1); metric: kcat/Km; normalized value: 0.42692307692307696 s^(-1)*mM^(-1); assay condition: 37 degC in FP buffer: 50 mM Tris (pH 7.5), 150 mM NaCl, 5 mM MgCl2, 10 mM NaHCO3, supplemented with 0.3 mM ATP and 0.1 mM DAPA; steady-state analysis varying one substrate with the other two at saturating concentrations; mean +/- SEM of three independent experiments.

raw_value_unit_evidence: TABLE 1, MtDTBS enzyme block, substrate row GTP: the Km (μM) cell prints 26.3 ± 0.5 and the kcat (s-1) (x 10-3) cell prints 11.1 ± 0.1. TABLE 1 prints no kcat/Km column.

row_label: MtDTBS block, substrate row GTP


substrate_name: UTP

column_label: TABLE 1 row UTP inside the MtDTBS enzyme block supplies both metric cells: Km = 26.1 ± 0.5 under the column header Km (μM) and kcat = 11.4 ± 0.8 under the column header kcat (s-1) (x 10-3). Both cells lie on that single printed row, so the tuple spans no second row, no second column and no second enzyme block.

normalized_value_unit_evidence: metric: Km; raw value: 26.1 ± 0.5 μM; raw unit: uM; normalized value: 0.026 mM; metric: kcat; raw value: 11.4 ± 0.8 (x 10-3) s-1; raw unit: s^-1 (column scaled by x 10-3); normalized value: 0.0114 s^(-1); metric: kcat/Km; normalized value: 0.4384615384615385 s^(-1)*mM^(-1); assay condition: 37 degC in FP buffer: 50 mM Tris (pH 7.5), 150 mM NaCl, 5 mM MgCl2, 10 mM NaHCO3, supplemented with 0.3 mM ATP and 0.1 mM DAPA; steady-state analysis varying one substrate with the other two at saturating concentrations; mean +/- SEM of three independent experiments.

raw_value_unit_evidence: TABLE 1, MtDTBS enzyme block, substrate row UTP: the Km (μM) cell prints 26.1 ± 0.5 and the kcat (s-1) (x 10-3) cell prints 11.4 ± 0.8. TABLE 1 prints no kcat/Km column.

row_label: MtDTBS block, substrate row UTP

substrate: UTP


column_label: TABLE 1 row ATP inside the MtDTBS enzyme block supplies both metric cells: Km = 30.2 ± 1.7 under the column header Km (μM) and kcat = 11.7 ± 0.2 under the column header kcat (s-1) (x 10-3). Both cells lie on that single printed row, so the tuple spans no second row, no second column and no second enzyme block.

normalized_value_unit_evidence: metric: Km; raw value: 30.2 ± 1.7 μM; raw unit: uM; normalized value: 0.03 mM; metric: kcat; raw value: 11.7 ± 0.2 (x 10-3) s-1; raw unit: s^-1 (column scaled by x 10-3); normalized value: 0.0117 s^(-1); metric: kcat/Km; normalized value: 0.39 s^(-1)*mM^(-1); assay condition: 37 degC in FP buffer: 50 mM Tris (pH 7.5), 150 mM NaCl, 5 mM MgCl2, 10 mM NaHCO3, supplemented with 0.3 mM ATP and 0.1 mM DAPA; steady-state analysis varying one substrate with the other two at saturating concentrations; mean +/- SEM of three independent experiments.

raw_value_unit_evidence: TABLE 1, MtDTBS enzyme block, substrate row ATP: the Km (μM) cell prints 30.2 ± 1.7 and the kcat (s-1) (x 10-3) cell prints 11.7 ± 0.2. TABLE 1 prints no kcat/Km column.

row_label: MtDTBS block, substrate row ATP


substrate_name: TTP

column_label: TABLE 1 row TTP inside the MtDTBS enzyme block supplies both metric cells: Km = 23.2 ± 1.4 under the column header Km (μM) and kcat = 11.8 ± 0.8 under the column header kcat (s-1) (x 10-3). Both cells lie on that single printed row, so the tuple spans no second row, no second column and no second enzyme block.

normalized_value_unit_evidence: metric: Km; raw value: 23.2 ± 1.4 μM; raw unit: uM; normalized value: 0.023 mM; metric: kcat; raw value: 11.8 ± 0.8 (x 10-3) s-1; raw unit: s^-1 (column scaled by x 10-3); normalized value: 0.0118 s^(-1); metric: kcat/Km; normalized value: 0.5130434782608696 s^(-1)*mM^(-1); assay condition: 37 degC in FP buffer: 50 mM Tris (pH 7.5), 150 mM NaCl, 5 mM MgCl2, 10 mM NaHCO3, supplemented with 0.3 mM ATP and 0.1 mM DAPA; steady-state analysis varying one substrate with the other two at saturating concentrations; mean +/- SEM of three independent experiments.

raw_value_unit_evidence: TABLE 1, MtDTBS enzyme block, substrate row TTP: the Km (μM) cell prints 23.2 ± 1.4 and the kcat (s-1) (x 10-3) cell prints 11.8 ± 0.8. TABLE 1 prints no kcat/Km column.

row_label: MtDTBS block, substrate row TTP

substrate: TTP


column_label: TABLE 1 row DAPA inside the MtDTBS enzyme block supplies both metric cells: Km = 30.2 ± 1.1 under the column header Km (μM) and kcat = 13.3 ± 0.7 under the column header kcat (s-1) (x 10-3). Both cells lie on that single printed row, so the tuple spans no second row, no second column and no second enzyme block.

normalized_value_unit_evidence: metric: Km; raw value: 30.2 ± 1.1 μM; raw unit: uM; normalized value: 0.03 mM; metric: kcat; raw value: 13.3 ± 0.7 (x 10-3) s-1; raw unit: s^-1 (column scaled by x 10-3); normalized value: 0.0133 s^(-1); metric: kcat/Km; normalized value: 0.4433333333333333 s^(-1)*mM^(-1); assay condition: 37 degC in FP buffer: 50 mM Tris (pH 7.5), 150 mM NaCl, 5 mM MgCl2, 10 mM NaHCO3, supplemented with 0.3 mM ATP and 0.1 mM DAPA; steady-state analysis varying one substrate with the other two at saturating concentrations; mean +/- SEM of three independent experiments.

raw_value_unit_evidence: TABLE 1, MtDTBS enzyme block, substrate row DAPA: the Km (μM) cell prints 30.2 ± 1.1 and the kcat (s-1) (x 10-3) cell prints 13.3 ± 0.7. TABLE 1 prints no kcat/Km column.

row_label: MtDTBS block, substrate row DAPA


column_label: TABLE 1 row CTP inside the MtDTBS enzyme block supplies both metric cells: Km = 25.2 ± 1.7 under the column header Km (μM) and kcat = 15.2 ± 0.3 under the column header kcat (s-1) (x 10-3). Both cells lie on that single printed row, so the tuple spans no second row, no second column and no second enzyme block.

normalized_value_unit_evidence: metric: Km; raw value: 25.2 ± 1.7 μM; raw unit: uM; normalized value: 0.025 mM; metric: kcat; raw value: 15.2 ± 0.3 (x 10-3) s-1; raw unit: s^-1 (column scaled by x 10-3); normalized value: 0.0152 s^(-1); metric: kcat/Km; normalized value: 0.608 s^(-1)*mM^(-1); assay condition: 37 degC in FP buffer: 50 mM Tris (pH 7.5), 150 mM NaCl, 5 mM MgCl2, 10 mM NaHCO3, supplemented with 0.3 mM ATP and 0.1 mM DAPA; steady-state analysis varying one substrate with the other two at saturating concentrations; mean +/- SEM of three independent experiments.

raw_value_unit_evidence: TABLE 1, MtDTBS enzyme block, substrate row CTP: the Km (μM) cell prints 25.2 ± 1.7 and the kcat (s-1) (x 10-3) cell prints 15.2 ± 0.3. TABLE 1 prints no kcat/Km column.

row_label: MtDTBS block, substrate row CTP


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

organism: Streptomyces lavendulae

substrate_name: D-homocysteine

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

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

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

proof_lines: kcat is 2200 sec(-1) with D-OUS as substrate. kcat is 0.86 sec(-1) with D-homocysteine as substrate.

substrate: O-ureido-D-serine


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: pH 8.0, 30°C, cosubstrate: D-homocysteine

proof_lines: pH 8.0, 30°C, cosubstrate: beta-aminooxy-D-alanine

proof_lines: pH 8.0, 30°C, cosubstrate: D-2,4-diaminobutyrate


assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines: with CTP as cosubstrate, at pH 7.6 and 37°C

proof_lines: with ATP as cosubstrate, at pH 7.6 and 37°C


substrate_name: L-phenylalanine

proof_lines: kcat is 9.32 sec(-1) for ligase activity with alanine as substrate (PubMed:24702628). kcat is 10.4 sec(-1) for ligase activity with phenylalanine as substrate (PubMed:24702628). kcat is 630 min(-1) for ligase activity with alanine and pheny

substrate: L-phenylalanine


enzyme_display_name: carbapenam-3-carboxylate synthase

organism: Pectobacterium carotovorum

assay_conditions_summary: pH 7.8; 295.15 K; cofactor ATP

proof_lines:
pH 7.8, 22°C
Raw SKiD Env: Temp=22°C, pH=7.8
kcat is 0.28 sec(-1).

source_databases_merged: brenda skid uniprot

enzyme: carbapenam-3-carboxylate synthase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature H447A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H447A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature V446G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V446G, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature V446A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V446A, pH and temperature not specified in the publication


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


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

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

assay_conditions_summary: pH 7.5; buffer 50 mM Tris pH 7; cofactor NADH

column_label: PMC3503319 Results paragraph under Biochemical characterization of Mtb DTBS reports K_m and V_max for DAPA as 2 uM and 6 uM min^-1 mg^-1, respectively.

raw_value_unit_evidence: Km raw_value=2 raw_unit=uM; Vmax raw_value=6 raw_unit=uM min^-1 mg^-1

row_label: Mtb DTBS DAPA kinetic parameter

table_label: PMC3503319 Results prose, Biochemical characterization of Mtb DTBS


assay_conditions_summary: pH 7.5; buffer 50 mM Tris pH 7; cofactor ATP

column_label: PMC3503319 Results paragraph under Biochemical characterization of Mtb DTBS reports K_m and V_max for ATP as 29 uM and 3.5 uM min^-1 mg^-1, respectively.

raw_value_unit_evidence: Km raw_value=29 raw_unit=uM; Vmax raw_value=3.5 raw_unit=uM min^-1 mg^-1

row_label: Mtb DTBS ATP kinetic parameter


organism: Mus musculus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y151A with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y151A, in 100 mM MES, pH 6.0, at 37°C


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


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

substrate_name: phosphoribosyl-amine (at 37 degrees Celsius)

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


substrate_name: Unknown

substrate: Unknown


substrate_name: 5-FTHF (at pH 6 and 37 degrees Celsius)

assay_conditions_summary: pH 6; 310.15 K; cofactor ATP

proof_lines: kcat is 0.94 sec(-1) for cyclo-ligase activity with 5-FTHF (at pH 6 and 37 degrees Celsius). kcat is 0.99 sec(-1) for cyclo-ligase activity with ATP (at pH 6 and 37 degrees Celsius).

substrate: 5-FTHF (at pH 6 and 37 degrees Celsius)


organism: Oryctolagus cuniculus

proof_lines: kcat is 2 sec(-1) for cyclo-ligase activity with 5-CHO-H(4)Pte. kcat is 3 sec(-1) for cyclo-ligase activity with 5-CHO-H(4)PteHis. kcat is 5 sec(-1) for cyclo-ligase activity with 5-CHO-H(4)PteGlu and 5-CHO-H(4)PteGlu(5).


organism: Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)

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

proof_lines: kcat is 1.16 sec(-1) for formyltransferase with 5-CHO-THF or 5-CHO-THF-Glu3 as substrates (at pH 7.3 and 30 degrees Celsius).


proof_lines: kcat is 2200 sec(-1) with D-OUS as substrate. kcat is 0.86 sec(-1) with D-homocysteine as substrate.


proof_lines: pH 7.8, 22°C, variable substrate: (2S,5R)-carboxymethylproline, Ki(slope)

proof_lines: pH 7.8, 22°C, variable substrate: ATP, Ki(slope)

source_databases_merged: brenda skid


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y345F/E380A to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature Y345F/E380D 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_rest_accession:Q9XB61 and applied mutation signature E380A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; buffer system for CPS; cofactor ATP

column_label: Table 1, CPS block, single-point mutant row E380A; column kcat (s-1) = 0.0067; column Km,s (mM) = 0.49; column kcat/Km,s (mM-1 s-1) = 0.014; column -Delta kcat = 54; column +Delta Km = 1.4; column -Delta (kcat/Km) = 74

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.0067 s-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.0067 s^(-1). Km: printed Table 1 cell 0.49 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 0.49 mM. kcat/Km: printed Table 1 cell 0.014 mM-1 s-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.014 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, CPS block, single-point mutant row E380A: kcat = 0.0067 s-1; Km = 0.49 mM; printed kcat/Km = 0.014 mM-1 s-1; printed fold-change cells -Delta kcat = 54, +Delta Km = 1.4, -Delta (kcat/Km) = 74.

table_label: Table 1: CPS and beta-LS Mutant Kinetic Parameters Compared to Wild-Type Proteins (Biochemistry 2009, 48(22):4959-4971, NIH Public Access author manuscript)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9XB61 and applied mutation signature Y345A to reconstruct the assayed variant sequence.

column_label: Table 1, CPS block, single-point mutant row Y345A; column kcat (s-1) = 0.011; column Km,s (mM) = 1.7; column kcat/Km,s (mM-1 s-1) = 0.0063; column -Delta kcat = 33; column +Delta Km = 5; column -Delta (kcat/Km) = 170

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.011 s-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.011 s^(-1). Km: printed Table 1 cell 1.7 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 1.7 mM. kcat/Km: printed Table 1 cell 0.0063 mM-1 s-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.0063 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, CPS block, single-point mutant row Y345A: kcat = 0.011 s-1; Km = 1.7 mM; printed kcat/Km = 0.0063 mM-1 s-1; printed fold-change cells -Delta kcat = 33, +Delta Km = 5, -Delta (kcat/Km) = 170.


sequence_variant_note: Mutation signature Y345F/E380Q 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_rest_accession:Q9XB61 and applied mutation signature E380Q to reconstruct the assayed variant sequence.

column_label: Table 1, CPS block, single-point mutant row E380Q; column kcat (s-1) = 0.020; column Km,s (mM) = 0.075; column kcat/Km,s (mM-1 s-1) = 0.27; column -Delta kcat = 18; column +Delta Km = 0.21; column -Delta (kcat/Km) = 4

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.020 s-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.02 s^(-1). Km: printed Table 1 cell 0.075 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 0.075 mM. kcat/Km: printed Table 1 cell 0.27 mM-1 s-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.27 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, CPS block, single-point mutant row E380Q: kcat = 0.020 s-1; Km = 0.075 mM; printed kcat/Km = 0.27 mM-1 s-1; printed fold-change cells -Delta kcat = 18, +Delta Km = 0.21, -Delta (kcat/Km) = 4.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9XB61 and applied mutation signature Y345F to reconstruct the assayed variant sequence.

column_label: Table 1, CPS block, single-point mutant row Y345F; column kcat (s-1) = 0.17; column Km,s (mM) = 0.27; column kcat/Km,s (mM-1 s-1) = 0.63; column -Delta kcat = 2; column +Delta Km = 0.77; column -Delta (kcat/Km) = 1.7

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.17 s-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.17 s^(-1). Km: printed Table 1 cell 0.27 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 0.27 mM. kcat/Km: printed Table 1 cell 0.63 mM-1 s-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.63 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, CPS block, single-point mutant row Y345F: kcat = 0.17 s-1; Km = 0.27 mM; printed kcat/Km = 0.63 mM-1 s-1; printed fold-change cells -Delta kcat = 2, +Delta Km = 0.77, -Delta (kcat/Km) = 1.7.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9XB61 and applied mutation signature E380D to reconstruct the assayed variant sequence.

column_label: Table 1, CPS block, single-point mutant row E380D; column kcat (s-1) = 0.26; column Km,s (mM) = 0.36; column kcat/Km,s (mM-1 s-1) = 0.72; column -Delta kcat = 1.4; column +Delta Km = 1; column -Delta (kcat/Km) = 1.4

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.26 s-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.26 s^(-1). Km: printed Table 1 cell 0.36 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 0.36 mM. kcat/Km: printed Table 1 cell 0.72 mM-1 s-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 0.72 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, CPS block, single-point mutant row E380D: kcat = 0.26 s-1; Km = 0.36 mM; printed kcat/Km = 0.72 mM-1 s-1; printed fold-change cells -Delta kcat = 1.4, +Delta Km = 1, -Delta (kcat/Km) = 1.4.


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

proof_lines:
pH 8.0, 25°C, wild-type enzyme
pH 8.0, 25?, wild-type enzyme


proof_lines: wild type enzyme, in 200 mM MES pH 6.0, with 30 mM NaCl, 10 mM MgCl2, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol, at 37°C

proof_lines: wild type enzyme, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C


substrate_name: ATP

substrate: ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K120A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K120A, in 200 mM MES pH 6.0, with 30 mM NaCl, 10 mM MgCl2, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol, at 37°C

proof_lines: mutant enzyme K120A, in 200 mM MES (pH 6.0), 30 mM sodium chloride, 10 mM magnesium chloride, 0.1% (v/v) Triton X-100, and 0.01% (v/v) 2-mercaptoethanol at 37°C


organism: Escherichia coli

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.

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 K15Q; column kcat (min-1) = 5.4 x 10^-4; column Km(ATP) (uM) = 7.01 x 10^2; column kcat/Km(ATP) (M-1 s-1) = 1.29 x 10^-2. captured primary segment: ATP | K15Q DTBS | Km 7.01 x 10^2 uM | kcat 5.4 x 10^-4 min^-1 | kcat/Km 1.29 x 10^-2 M^-1 s^-1

raw_value_unit_evidence: Table 2, enzyme row K15Q, substrate column set ATP: Km(ATP) (uM) = 7.01 x 10^2 uM; kcat (min-1) = 5.4 x 10^-4 min^-1; kcat/Km(ATP) (M-1 s-1) = 1.29 x 10^-2 M^-1 s^-1.

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


organism: Mycobacterium tuberculosis


organism: Streptomyces clavuligerus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature V446G with inferred residue-numbering offset -7 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 V446A with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature H447A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H447A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F118A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y122A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y123F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y122F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q144A to reconstruct the assayed variant sequence.


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

proof_lines:
pH 6.0, 37°C, recombinant enzyme
Raw SKiD Env: Temp=37°C, pH=6


organism: Geminocystis herdmanii PCC 6308

substrate_name: L-Asp

proof_lines: pH and temperature not specified in the publication

substrate: L-Asp


organism: Lacticaseibacillus casei

substrate_name: araATP

substrate: araATP


organism: Escherichia coli (strain K12)

substrate_name: DAPA (at pH 7.5, 37 degrees Celsius)

column_label: Table 1 row EcDTBS DAPA; KM cell 15.2 +/- 1.7 uM.

normalized_value_unit_evidence: EcDTBS DAPA KM = 0.0152 mM.

raw_value_unit_evidence: EcDTBS DAPA KM = 15.2 +/- 1.7 uM.

row_label: EcDTBS; DAPA

table_label: Table 1: Kinetic analysis of substrates

substrate: DAPA (at pH 7.5, 37 degrees Celsius)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: DAPA (at pH 8.5 and at 20 degrees Celsius)

assay_conditions_summary: cofactor ATP


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


organism: Streptococcus pyogenes serotype M1

substrate_name: Glu (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).

substrate: Glu (at pH 7.3 and 30 degrees Celsius)


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

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).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P13000 and applied mutation signature K37L 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 K37L; column kcat (min-1) = 2.6 x 10^-2; column Km(ATP) (uM) = 4.30; column kcat/Km(ATP) (M-1 s-1) = 1.01 x 10^2. captured primary segment: ATP | K37L DTBS | Km 4.30 uM | kcat 2.6 x 10^-2 min^-1 | kcat/Km 1.01 x 10^2 M^-1 s^-1

raw_value_unit_evidence: Table 2, enzyme row K37L, substrate column set ATP: Km(ATP) (uM) = 4.30 uM; kcat (min-1) = 2.6 x 10^-2 min^-1; kcat/Km(ATP) (M-1 s-1) = 1.01 x 10^2 M^-1 s^-1.

row_label: Table 2, enzyme row K37L, column set for substrate ATP


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(ATP) (uM) = 4.53; column kcat/Km(ATP) (M-1 s-1) = 1.18 x 10^2. captured primary segment: ATP | K37Q DTBS | Km 4.53 uM | kcat 3.2 x 10^-2 min^-1 | kcat/Km 1.18 x 10^2 M^-1 s^-1

raw_value_unit_evidence: Table 2, enzyme row K37Q, substrate column set ATP: Km(ATP) (uM) = 4.53 uM; kcat (min-1) = 3.2 x 10^-2 min^-1; kcat/Km(ATP) (M-1 s-1) = 1.18 x 10^2 M^-1 s^-1.

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


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.