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

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

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

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


enzyme_display_name: glutamine synthetase

organism: Exiguobacterium sp.

substrate_name: L-glutamine

source_db: brenda

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:C4L2T5 and applied mutation signature E60A to reconstruct the assayed variant sequence.

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

mutation_type: substitution

assay_conditions_summary: pH 6; cofactor ADP

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

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

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

row_label: Table 1, Gln block, enzyme column E60A

data_origin: experimental

enzyme: glutamine synthetase

substrate: L-glutamine

status: corrected

source: brenda


substrate_name: ADP

kcat_over_km_origin: calculated

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

substrate: ADP


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

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

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

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

row_label: Table 1, Gln block, enzyme column R64G


enzyme_display_name: NAD(+) synthase

organism: Mycobacterium tuberculosis

substrate_name: deamido-NAD+

kcat_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: recombinant truncated enzyme

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

mutation_type: truncation

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+

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

enzyme: NAD(+) synthase

substrate: deamido-NAD+


substrate_name: ATP

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: glutamine

mutation_signature: Unknown

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

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

substrate: glutamine


organism: Arabidopsis thaliana

substrate_name: glutamate

source_db: uniprot

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

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

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

substrate: glutamate

source: uniprot


substrate_name: ammonium

substrate: ammonium


assay_conditions_summary: pH 7.8; cofactor ATP


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


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


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

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

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


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

smiles: NO


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

assay_conditions_summary: cofactor ATP

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


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


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

assay_conditions_summary: cofactor ADP

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


organism: Homo sapiens

assay_conditions_summary: pH 8; cofactor NAD+

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

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


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


assay_conditions_summary: pH 8; cofactor ATP

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

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


smiles: N


organism: Methylococcus capsulatus

substrate_name: Glu

proof_lines: hydroxylamine, glutamyl transferase assay

substrate: Glu


organism: Synechocystis sp.

sequence_source: multiple

source_databases_merged: brenda uniprot


enzyme_display_name: oxazoline synthase

organism: uncultured Prochloron sp. 06037A

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

enzyme: oxazoline synthase

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


enzyme_display_name: thiazoline synthase

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

enzyme: thiazoline synthase

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


organism: Anabaena azollae

substrate_name: NH3; ATP; L-Glutamate

km_display: Not reported

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

ki_unit: mM

substrate: NH3; ATP; L-Glutamate


organism: Bacillus subtilis

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


organism: Canis familiaris

substrate_name: L-Glutamate; ATP; NH3

substrate: L-Glutamate; ATP; NH3


organism: Escherichia coli

substrate_name: NH3; L-Glutamate; ATP

substrate: NH3; L-Glutamate; ATP


substrate_name: ATP; L-Glutamate; NH3

substrate: ATP; L-Glutamate; NH3


substrate_name: ATP; NH3; L-Glutamate

substrate: ATP; NH3; L-Glutamate


substrate_name: Unknown

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

substrate: Unknown


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


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


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


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Oryza sativa

substrate_name: L-Glutamate; NH3; ATP

substrate: L-Glutamate; NH3; ATP


organism: Sulfolobus acidocaldarius


organism: Trichormus azollae

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

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


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


organism: Triticum aestivum


substrate_name: L-Glutamine; Phosphate; ADP

substrate: L-Glutamine; Phosphate; ADP


organism: Hordeum vulgare


organism: Medicago truncatula


organism: Phaseolus vulgaris


organism: Pseudomonas taetrolens


organism: Arabidopsis thaliana

substrate_name: L-Glutamate

source_db: oed

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

assay_conditions_summary: pH 7.8; 303.15 K; cofactor ATP

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

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

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

substrate: L-Glutamate

source: oed


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


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


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

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

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


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


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


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


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

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

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


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

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

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

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


organism: Exiguobacterium sp.

substrate_name: ADP

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

assay_conditions_summary: pH 6; 308.15 K; cofactor ADP

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

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

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

row_label: Table 1, ADP block, enzyme column E60A

substrate: ADP


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


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


verification_status: verified

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

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

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

row_label: Table 1, ADP block, enzyme column WT

status: verified


substrate_name: L-glutamine

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

substrate: L-glutamine


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


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

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

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

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


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

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

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

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


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

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

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

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


enzyme_display_name: aspartate--ammonia ligase

organism: Leishmania donovani

substrate_name: L-aspartate

enzyme: aspartate--ammonia ligase

substrate: L-aspartate


substrate_name: glutamine

substrate: glutamine


enzyme_display_name: glutamate--ethylamine ligase

organism: Methylovorus mays

substrate_name: methylamine

smiles: CN

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

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

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

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

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

enzyme: glutamate--ethylamine ligase

substrate: methylamine


substrate_name: ethylamine

smiles: CCN

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

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

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

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

substrate: ethylamine


substrate_name: hydroxylamine

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

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

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

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

substrate: hydroxylamine


substrate_name: ammonia

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

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

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

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

substrate: ammonia


substrate_name: glutamic acid (with methylamine as substrate)


substrate_name: ATP (with methylamine as substrate)

substrate: ATP (with methylamine as substrate)


organism: Haloferax mediterranei

substrate_name: ATP

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

substrate: ATP


substrate_name: L-Glu

substrate: L-Glu


substrate_name: L-Gln

substrate: L-Gln


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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


organism: Oryza sativa subsp. japonica

substrate_name: glutamate

substrate: glutamate


substrate_name: ammonium

substrate: ammonium


organism: Bifidobacterium pseudolongum


organism: Ruminococcus albus

assay_conditions_summary: pH 6.4; 310.15 K; cofactor ADP


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


assay_conditions_summary: pH 6.4; 310.15 K; cofactor ATP


substrate_name: L-Glutamate; ATP; NH3

substrate: L-Glutamate; ATP; NH3


organism: Zea mays


substrate_name: NH3; L-Glutamate; ATP

substrate: NH3; L-Glutamate; ATP


organism: Bacillus subtilis

substrate_name: ATP; Deamino-NAD+; NH4+

assay_conditions_summary: cofactor NAD+

substrate: ATP; Deamino-NAD+; NH4+


substrate_name: Ethylamine; L-Glutamate; ATP

substrate: Ethylamine; L-Glutamate; ATP


organism: Providencia vermicola

substrate_name: ADP

assay_conditions_summary: pH 8; 308.15 K; cofactor ADP

column_label: Table 1 (kinetic parameters of PveGS), ADP-Na2 block, enzyme column 'WT'; row 'Km(mM)' = 25.2 x 10^-5; row 'Vmax(mM/min)' = 0.20; row 'kcat(s^-1)' = 9.14; row 'kcat/Km(s^-1 mM^-1)' = 3.63 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 1 cell 9.14 s^-1; already in s^-1, so no unit conversion applies; the catalog value is 9.14 s^(-1). Km: printed Table 1 cell 25.2 x 10^-5 mM; already in mM, so no unit conversion applies; the catalog value is 0.000252 mM. kcat/Km: printed Table 1 cell 3.63 x 10^4 s^-1 mM^-1; already in the export's canonical s^-1 mM^-1, so no unit conversion applies; the printed cell is 36300.0 s^-1 mM^-1. The quotient of the two printed component cells is 9.14 / 0.000252 = 36269.84126984127 s^-1 mM^-1, which is the catalog value, and it lies inside the rounding interval of the printed cell.

row_label: Table 1, ADP-Na2 block, column WT

table_label: Table 1, kinetic parameters of PveGS (Scientific Reports 2018, 8:15640)

substrate: ADP


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

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


column_label: Table 1 (kinetic parameters of PveGS), Hydroxylamine block, enzyme column 'WT'; row 'Km(mM)' = 15.7; row 'Vmax(mM/min)' = 0.37; row 'kcat(s^-1)' = 17.0; row 'kcat/Km(s^-1 mM^-1)' = 1.08.

normalized_value_unit_evidence: kcat: printed Table 1 cell 17.0 s^-1; already in s^-1, so no unit conversion applies; the catalog value is 17.0 s^(-1). Km: printed Table 1 cell 15.7 mM; already in mM, so no unit conversion applies; the catalog value is 15.7 mM. kcat/Km: printed Table 1 cell 1.08 s^-1 mM^-1; already in the export's canonical s^-1 mM^-1, so no unit conversion applies; the printed cell is 1.08 s^-1 mM^-1. The quotient of the two printed component cells is 17.0 / 15.7 = 1.0828025477707006 s^-1 mM^-1, which is the catalog value, and it lies inside the rounding interval of the printed cell.

raw_value_unit_evidence: Table 1, Hydroxylamine block, column WT: Km(mM) = 15.7; Vmax(mM/min) = 0.37; kcat(s^-1) = 17.0; kcat/Km(s^-1 mM^-1) = 1.08.

row_label: Table 1, Hydroxylamine block, column WT


substrate_name: L-glutamine

column_label: Table 1 (kinetic parameters of PveGS), L-Glutamine block, enzyme column 'WT'; row 'Km(mM)' = 32.6; row 'Vmax(mM/min)' = 0.66; row 'kcat(s^-1)' = 30.5; row 'kcat/Km(s^-1 mM^-1)' = 0.936.

normalized_value_unit_evidence: kcat: printed Table 1 cell 30.5 s^-1; already in s^-1, so no unit conversion applies; the catalog value is 30.5 s^(-1). Km: printed Table 1 cell 32.6 mM; already in mM, so no unit conversion applies; the catalog value is 32.6 mM. kcat/Km: printed Table 1 cell 0.936 s^-1 mM^-1; already in the export's canonical s^-1 mM^-1, so no unit conversion applies; the printed cell is 0.936 s^-1 mM^-1. The quotient of the two printed component cells is 30.5 / 32.6 = 0.9355828220858895 s^-1 mM^-1, which is the catalog value, and it lies inside the rounding interval of the printed cell.

raw_value_unit_evidence: Table 1, L-Glutamine block, column WT: Km(mM) = 32.6; Vmax(mM/min) = 0.66; kcat(s^-1) = 30.5; kcat/Km(s^-1 mM^-1) = 0.936.

row_label: Table 1, L-Glutamine block, column WT

substrate: L-glutamine


organism: Anabaena azollae

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


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


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


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


substrate_name: L-Glutamate

substrate: L-Glutamate


organism: Paracoccus denitrificans

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

normalized_value_unit_evidence: Km=0.03 mM as reported.

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

row_label: glutamine synthetase / biosynthetic reaction / ammonia

table_label: PubMed abstract prose (PMID 1356141)


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

normalized_value_unit_evidence: Km=0.17 mM as reported.

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

row_label: glutamine synthetase / biosynthetic reaction / ATP


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

normalized_value_unit_evidence: Km=2.4 mM as reported.

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

row_label: glutamine synthetase / transferase reaction / hydroxylamine


organism: Skeletonema costatum

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

raw_value_unit_evidence: Km raw_value=0.5 mM raw_unit=mM

row_label: Prose segment: ATP Km

table_label: PubMed PMID 8756499 abstract


raw_value_unit_evidence: Km raw_value=0.7 mM raw_unit=mM

row_label: Prose segment: NH4(+) Km


substrate_name: Glu

raw_value_unit_evidence: Km raw_value=5.7 mM raw_unit=mM

row_label: Prose segment: glutamic acid Km

substrate: Glu


organism: Sulfolobus acidocaldarius


organism: Clostridium pasteurianum


substrate_name: hydroxylamine


substrate_name: Gln

substrate: Gln


organism: Nitrobacter winogradskyi


substrate: hydroxylamine


organism: Trichormus azollae

substrate_name: L-glutamate

substrate: L-glutamate


assay_conditions_summary: pH 7; 303.15 K; cofactor ATP


organism: Trichinella spiralis

assay_conditions_summary: pH 7; cofactor ATP

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

raw_value_unit_evidence: Km raw_value=0.16 raw_unit=mM

row_label: Figure 7G ATP substrate Km

table_label: PMC8488193 Figure 7 results


verification_status: unverified

assay_conditions_summary: pH 7

status: unverified


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

raw_value_unit_evidence: Km raw_value=0.20 raw_unit=mM

row_label: Figure 7G Glu substrate Km


organism: Rattus norvegicus

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

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


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

substrate_name: ATP

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

raw_value_unit_evidence: Km raw_value=0.56 raw_unit=mM

row_label: Archaeoglobus fulgidus

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

substrate: ATP


substrate_name: alpha-glutamate

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

raw_value_unit_evidence: Km raw_value=3.0 raw_unit=mM

substrate: alpha-glutamate


organism: Rhizobium meliloti (strain 1021)

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

raw_value_unit_evidence: Km raw_value=13.3 mM raw_unit=mM

row_label: Rhizobium meliloti GSIII / glutamate

table_label: PubMed XML abstract PMID 8093245


raw_value_unit_evidence: Km raw_value=33 mM raw_unit=mM

row_label: Rhizobium meliloti GSIII / ammonium


organism: Tuber borchii

assay_conditions_summary: pH 7.5; cofactor ATP


source_db: skid

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

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

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

source_databases_merged: skid uniprot

source: skid


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


organism: Bacillus anthracis

substrate_name: deamido-NAD+

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+

substrate: deamido-NAD+


assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP


organism: Bacillus subtilis (strain 168)

substrate_name: deamido-NAD

substrate: deamido-NAD


assay_conditions_summary: cofactor ATP


substrate_name: glutamine

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

substrate: glutamine


substrate_name: ammonium

substrate: ammonium


organism: Bacillus subtilis

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


organism: uncultured Prochloron sp. 06037A

assay_conditions_summary: pH 8; 307.15 K; cofactor ATP


assay_conditions_summary: cofactor ADP


organism: Pyrococcus sp.

assay_conditions_summary: pH 7.8; 333.15 K; cofactor ATP


organism: Mycobacterium tuberculosis

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

normalized_value_unit_evidence: Km central normalized_value=10.8 normalized_unit=mM.

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

row_label: Mycobacterium tuberculosis glutamine synthetase ammonium chloride substrate

table_label: ScienceDirect Results section: Kinetic parameters


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

substrate_name: alpha-glutamine (at 37 degrees Celsius)

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

substrate: alpha-glutamine (at 37 degrees Celsius)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Geobacillus stearothermophilus

assay_conditions_summary: pH 8.5; cofactor ATP

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

raw_value_unit_evidence: Km raw_value=0.91 mM raw_unit=mM

row_label: Geobacillus stearothermophilus ammonia-specific NAD synthetase / NH3

table_label: PubMed XML abstract PMID 12450114


organism: Methanocaldococcus jannaschii


substrate_name: glutamate

substrate: glutamate


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


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

substrate_name: manganese

smiles: [Mn]

substrate: manganese


organism: Phaseolus vulgaris

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


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


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

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


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


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

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


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


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


assay_conditions_summary: 298.15 K; cofactor ATP


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


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


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


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


organism: Lupinus luteus

substrate_name: ADP

substrate: ADP


organism: Medicago truncatula

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


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


assay_conditions_summary: 303.15 K; cofactor ATP


organism: [Bacillus] caldolyticus

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

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

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


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


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

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


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

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

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


organism: Drosophila melanogaster


organism: Bradyrhizobium japonicum


substrate_name: L-Gln

proof_lines:
glutamyl transferase reaction
biosynthetic reaction

substrate: L-Gln


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

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


substrate_name: L-glutamine

substrate: L-glutamine


organism: Escherichia coli


assay_conditions_summary: cofactor NAD+


proof_lines:
oxidized mutant enzyme E165C
reduced mutant enzyme E165C


substrate_name: L-Glu

substrate: L-Glu


organism: Trypanosoma cruzi

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

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


substrate_name: Unknown

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

substrate: Unknown


organism: Azospirillum brasilense


organism: Pseudomonas taetrolens

assay_conditions_summary: pH 8


assay_conditions_summary: pH 11; cofactor ATP


substrate_name: methylamine

substrate: methylamine


substrate_name: ethylamine

substrate: ethylamine


organism: Camellia sinensis

assay_conditions_summary: pH 7.8; cofactor ATP


substrate_name: L-glutamate

substrate: L-glutamate


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


organism: Bifidobacterium bifidum


substrate_name: ATP

substrate: ATP


organism: Bifidobacterium breve


organism: Corynebacterium callunae


substrate_name: hydroxylamine

substrate: hydroxylamine


substrate_name: Gln

substrate: Gln


organism: Canis lupus familiaris

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


assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP


organism: Exiguobacterium sp.

assay_conditions_summary: pH 6; 308.15 K; cofactor ADP

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


enzyme_display_name: beta-amyrin synthase

organism: Lathyrus oleraceus

enzyme: beta-amyrin synthase


substrate_name: Glu

substrate: Glu


organism: Methanohalophilus portucalensis

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7; cofactor ADP


assay_conditions_summary: pH 7


organism: Pyrococcus sp.


organism: Nicotiana plumbaginifolia


assay_conditions_summary: pH 7.4; 308.15 K; cofactor ATP


organism: Ligilactobacillus salivarius

substrate_name: L-aspartate

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

substrate: L-aspartate


organism: Staphylococcus aureus

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


organism: Spinacia oleracea

assay_conditions_summary: cofactor ATP


organism: Rhodobacter capsulatus

assay_conditions_summary: cofactor ADP


organism: Sinorhizobium meliloti


enzyme_display_name: D-aspartate ligase

organism: Enterococcus faecalis

enzyme: D-aspartate ligase


substrate_name: D-Aspartate

substrate: D-Aspartate


enzyme_display_name: trypanothione synthase

organism: Leishmania major

substrate_name: glutathione

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

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

enzyme: trypanothione synthase

substrate: glutathione


substrate_name: glutathionylspermidine

substrate: glutathionylspermidine


substrate_name: spermidine

smiles: C(CCNCCCN)CN

substrate: spermidine


organism: Enterococcus hirae

substrate_name: D-Aspartate; Hydroxylamine; ATP

substrate: D-Aspartate; Hydroxylamine; ATP


enzyme_display_name: glutathionylspermidine synthase

organism: Crithidia fasciculata

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

enzyme: glutathionylspermidine synthase


assay_conditions_summary: pH 7.2; cofactor ATP


organism: Escherichia coli

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


organism: Mycobacterium smegmatis

substrate_name: GlcN-Ins; ATP; L-Cysteine

substrate: GlcN-Ins; ATP; L-Cysteine


enzyme_display_name: 4-methyleneglutamate--ammonia ligase

organism: Arachis hypogaea

enzyme: 4-methyleneglutamate--ammonia ligase


enzyme_display_name: glutamate--putrescine ligase

organism: Escherichia coli (strain K12)

enzyme: glutamate--putrescine ligase


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


substrate_name: MgADP-

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

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

substrate: MgADP-


substrate_name: Reduced glutathione; ATP; Spermidine

assay_conditions_summary: pH 7.3; 298.15 K; cofactor ATP

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

substrate: Reduced glutathione; ATP; Spermidine


substrate_name: Reduced glutathione; Glutathionylspermidine; ATP

assay_conditions_summary: pH 7.2; 298.15 K; cofactor ATP

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


assay_conditions_summary: pH 7.8; 298.15 K; cofactor ATP


substrate_name: GlcN-Ins

substrate: GlcN-Ins


substrate_name: L-Cysteine

substrate: L-Cysteine


organism: Trypanosoma cruzi (strain CL Brener)

substrate_name: glutathione with spermidine as cosubstrate


substrate_name: MgATP

substrate: MgATP


substrate_name: aminopropylcadaverine

smiles: C(CCN)CCNCCCN

substrate: aminopropylcadaverine


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


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

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


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

smiles: C(CCN)CN


substrate_name: ATP

substrate: ATP


substrate_name: Glutathionylspermidine

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

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

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

row_label: reCf-TryS

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

substrate: Glutathionylspermidine


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

substrate_name: L-cysteine

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

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

normalized_value_unit_evidence: Km 40 microM = 0.04 mM

raw_value_unit_evidence: Cys Km 40 +/- 3 microM

row_label: Cys

table_label: PubMed abstract for PMID 12033919

substrate: L-cysteine


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

normalized_value_unit_evidence: Km 72 microM = 0.072 mM

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

row_label: GlcN-Ins


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

row_label: ATP

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


substrate_name: glutathione


substrate_name: spermidine


substrate_name: Unknown

substrate: Unknown


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


substrate_name: glutathionylspermidine


organism: Leishmania donovani


assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


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


organism: Trypanosoma brucei


substrate_name: Spermidine

smiles: NCCCCNCCCN

substrate: Spermidine


substrate_name: reduced glutathione

substrate: reduced glutathione


organism: Escherichia coli K-12

substrate_name: putrescine

substrate: putrescine


substrate_name: L-glutamate

substrate: L-glutamate


substrate: glutathionylspermidine


substrate: glutathione


substrate: spermidine


substrate_name: ATP (at pH 6.8)

assay_conditions_summary: pH 6.8; cofactor ATP

substrate: ATP (at pH 6.8)


substrate_name: glutathionylspermidine (at pH 7.5)

substrate: glutathionylspermidine (at pH 7.5)


enzyme_display_name: UniProt P33221

substrate_name: formyl phosphate

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P33221

substrate: formyl phosphate


substrate_name: acetyl phosphate

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

substrate: acetyl phosphate


substrate_name: Carbamoyl phosphate

substrate: Carbamoyl phosphate


assay_conditions_summary: pH 8; buffer recombinant enzyme

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

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

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


assay_conditions_summary: pH 8; cofactor ATP

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

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

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


substrate_name: Reduced glutathione

assay_conditions_summary: pH 8

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

substrate: Reduced glutathione


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

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


enzyme_display_name: 8-demethylnovobiocic acid synthase

organism: Streptomyces niveus

proof_lines: pH 7.0, temperature not specified in the publication

enzyme: 8-demethylnovobiocic acid synthase


organism: Azospirillum brasilense

substrate_name: L-glutamine

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NAD+

substrate: L-glutamine


organism: Mycolicibacterium smegmatis

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


substrate_name: ATP

substrate: ATP


substrate: Unknown


organism: Trypanosoma cruzi

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

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

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

table_label: Table I


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

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

row_label: TcTryS recombinant; K mapp MgATP


substrate_name: GSH

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

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

normalized_value_unit_evidence: Km 0.19 mM

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

row_label: TcTryS recombinant; K mapp GSH-with Glutathionylspermidine

substrate: GSH


enzyme_display_name: prokaryotic ubiquitin-like protein ligase

organism: Mycobacterium tuberculosis


assay_conditions_summary: pH 7.4; cofactor ATP

enzyme: prokaryotic ubiquitin-like protein ligase


enzyme_display_name: beta-citrylglutamate synthase

organism: Mus musculus

substrate_name: N-acetyl-aspartylglutamate

enzyme: beta-citrylglutamate synthase

substrate: N-acetyl-aspartylglutamate


organism: Corynebacterium glutamicum

substrate_name: [PanB]-L-lysine

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

substrate: [PanB]-L-lysine


substrate_name: [protein PanB]-L-lysine

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

substrate: [protein PanB]-L-lysine


enzyme_display_name: lipoate--protein ligase

substrate_name: Unknown

enzyme: lipoate--protein ligase


substrate_name: D,L-lipoic acid

substrate: D,L-lipoic acid


substrate_name: magnesium ion

substrate: magnesium ion


substrate_name: L-glutamate

substrate: L-glutamate


substrate_name: citrate

substrate: citrate


organism: Escherichia coli

substrate_name: octanoic acid

smiles: CCCCCCCC(=O)O

substrate: octanoic acid


substrate_name: ADP

assay_conditions_summary: pH 8; 298.15 K; cofactor ADP

proof_lines: recombinant enzyme, pH 8.0, 25°C, reaction with formyl phosphate

proof_lines: recombinant enzyme, pH 8.0, 25°C, reaction with acetyl phosphate

proof_lines: recombinant enzyme, pH 8.0, 25°C, reaction with carbamoyl phosphate

substrate: ADP


proof_lines: recombinant enzyme, pH 8.0, 25°C, with formate

proof_lines: recombinant enzyme, pH 8.0, 25°C, with acetate


substrate_name: acetyl phosphate

proof_lines: recombinant enzyme, pH 8.0, 25°C, reaction with ADP

substrate: acetyl phosphate


substrate_name: Carbamoyl phosphate

substrate: Carbamoyl phosphate


substrate_name: formyl phosphate

substrate: formyl phosphate


substrate_name: octanoyl-[CoA]

assay_conditions_summary: pH 7.8; 298.15 K; cofactor CoA

proof_lines: mutant enzyme K135A, with glycine cleavage system H protein as cosubstrate, at pH 7.8 and 25°C

substrate: octanoyl-[CoA]


proof_lines: mutant enzyme R71A, with glycine cleavage system H protein as cosubstrate, at pH 7.8 and 25°C


proof_lines: mutant enzyme G72A/G73A, with glycine cleavage system H protein as cosubstrate, at pH 7.8 and 25°C


proof_lines: wild type enzyme, with glycine cleavage system H protein as cosubstrate, at pH 7.8 and 25°C


substrate_name: R-lipoic acid

substrate: R-lipoic acid


substrate_name: ATP

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: apoH-protein

substrate: apoH-protein


substrate_name: DL-lipoic acid

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

substrate: DL-lipoic acid


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


organism: Bacillus anthracis

substrate_name: deamido-NAD+

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+

proof_lines: in 60 mM EPPS pH 8.5 with 20 mM ammonium chloride, 20 mM potassium chloride, and 10 mM magnesium chloride, at 37°C

substrate: deamido-NAD+


enzyme_display_name: glutamine synthetase

organism: Chlorella sorokiniana

enzyme: glutamine synthetase


assay_conditions_summary: cofactor ATP


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


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


enzyme_display_name: NAD(+) synthase

organism: Francisella tularensis

assay_conditions_summary: cofactor NAD+

enzyme: NAD(+) synthase


substrate_name: deamido-NMN

substrate: deamido-NMN


organism: Medicago truncatula

substrate_name: L-Glu

proof_lines: non-phosphorylated GS1a, in the presence of 0.0005 mM microcystin

substrate: L-Glu


proof_lines: phosphorylated GS1a, in the presence of 0.0005 mM microcystin


assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines:
pH 7.5
Gln


substrate_name: formate

proof_lines: kcat is 37.6 sec(-1) for transformylase activity (at pH 8). kcat is 0.309 sec(-1) for acetate kinase activity (at pH 8).

substrate: formate


organism: Nocardia asteroides


substrate_name: Glu

substrate: Glu


organism: Homo sapiens


substrate_name: L-glutamate

substrate: L-glutamate


organism: Escherichia coli (strain K12)

substrate_name: acetate (at pH 8)

assay_conditions_summary: pH 8; cofactor ADP

substrate: acetate (at pH 8)


organism: Ovis aries


organism: Staphylococcus aureus

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: in 60 mM Tris-HCl pH 8.0, 10 mM NH4Cl, 10 mM MgCl2, 10 mM KCl


organism: Trypanosoma brucei

substrate_name: ATP; Reduced glutathione; Spermidine

assay_conditions_summary: pH 8; 298.15 K; buffer recombinant enzyme

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

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

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

substrate: ATP; Reduced glutathione; Spermidine


organism: Streptococcus equinus


substrate_name: L-Asp

substrate: L-Asp


organism: Chlorella sp.

substrate_name: Unknown

substrate: Unknown


organism: Trichormus variabilis

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


assay_conditions_summary: pH 6.8; cofactor ATP

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


substrate_name: beta-Citryl-L-glutamate

substrate: beta-Citryl-L-glutamate


proof_lines:
at pH 7.4 and 37°C
above


organism: Columba sp.


organism: Bacillus subtilis


substrate_name: LplA acceptor peptide 2

substrate: LplA acceptor peptide 2


enzyme_display_name: o-succinylbenzoate--CoA ligase

proof_lines: pH and temperature not specified in the publication

enzyme: o-succinylbenzoate--CoA ligase


enzyme_display_name: peptidylprolyl isomerase

substrate_name: RNase T1

proof_lines: mutant Y15A, pH not specified in the publication, temperature not specified in the publication

enzyme: peptidylprolyl isomerase

substrate: RNase T1


enzyme_display_name: L-arabinose isomerase

substrate_name: L-arabinose

enzyme: L-arabinose isomerase

substrate: L-arabinose


enzyme_display_name: amino-acid racemase

substrate_name: D-homoserine

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

enzyme: amino-acid racemase

substrate: D-homoserine


proof_lines: mutant A82P, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: sulfoquinovose isomerase

substrate_name: beta-sulfoquinovose

proof_lines: formation of 6-deoxy-6-sulfo-D-fructose, pH and temperature not specified in the publication

enzyme: sulfoquinovose isomerase

substrate: beta-sulfoquinovose


proof_lines:
pH 7.0
pH 7.0, 30°C, isomerase acitivity


enzyme_display_name: UDP-glucose 4-epimerase

substrate_name: UDP-alpha-D-glucose

proof_lines: pH 6.2, temperature not specified in the publication, recombinant mutant K153M

enzyme: UDP-glucose 4-epimerase

substrate: UDP-alpha-D-glucose


enzyme_display_name: L-ribulose-5-phosphate 4-epimerase

substrate_name: L-ribulose 5-phosphate

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

enzyme: L-ribulose-5-phosphate 4-epimerase

substrate: L-ribulose 5-phosphate


enzyme_display_name: UniProt Q2FV22

substrate_name: beta-Alanine

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

enzyme: UniProt Q2FV22

substrate: beta-Alanine


substrate_name: (R)-pantoate

substrate: (R)-pantoate


enzyme_display_name: UniProt P0A6W9

substrate_name: L-alpha-aminobutyrate

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

enzyme: UniProt P0A6W9

substrate: L-alpha-aminobutyrate


substrate_name: L-cysteine

substrate: L-cysteine


enzyme_display_name: UniProt P32477

organism: Saccharomyces cerevisiae

substrate_name: ATP

enzyme: UniProt P32477

substrate: ATP


substrate_name: L-Glu

substrate: L-Glu


organism: Escherichia coli


substrate_name: L-glutamate

substrate: L-glutamate


substrate_name: L-Cys

substrate: L-Cys


enzyme_display_name: Glutathione biosynthesis bifunctional protein GshAB

organism: Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)


enzyme: Glutathione biosynthesis bifunctional protein GshAB


substrate_name: ATP (in the reaction with gamma-GCS)

substrate: ATP (in the reaction with gamma-GCS)


substrate_name: gamma-L-glutamyl-L-cysteine

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

substrate: gamma-L-glutamyl-L-cysteine


substrate_name: glycine

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

substrate: glycine


enzyme_display_name: glutathione synthase

organism: Spinacia oleracea

enzyme: glutathione synthase


organism: [Candida] boidinii

substrate_name: gamma-Glu-Cys

substrate: gamma-Glu-Cys


substrate_name: Gly

substrate: Gly


enzyme_display_name: UniProt P48637

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8.2
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P48637


enzyme_display_name: UniProt Q9M426

organism: Glycine max

substrate_name: beta-Ala

enzyme: UniProt Q9M426

substrate: beta-Ala


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=37°C, pH=8.2


enzyme_display_name: UniProt P07862

substrate_name: D-alanine

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

proof_lines:
Raw SKiD Env: Temp=37°C, pH=9.2
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=6

enzyme: UniProt P07862

substrate: D-alanine


enzyme_display_name: UniProt Q5SHZ3

organism: Thermus thermophilus

enzyme: UniProt Q5SHZ3


enzyme_display_name: UniProt Q2N4T5

organism: Helicobacter pylori

proof_lines:
Raw SKiD Env: Temp=30°C, pH=9
Raw SKiD Env: Temp=30°C, pH=8

enzyme: UniProt Q2N4T5


proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=30°C, pH=9


enzyme_display_name: UniProt Q5HEB7

enzyme: UniProt Q5HEB7


smiles: N


organism: Streptococcus pyogenes


substrate_name: L-Lysine

substrate: L-Lysine


organism: Streptococcus pyogenes serotype M1

substrate_name: L-lysine

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

substrate: L-lysine


enzyme_display_name: glucose-6-phosphate isomerase

substrate_name: fructose 6-phosphate

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

enzyme: glucose-6-phosphate isomerase

substrate: fructose 6-phosphate


enzyme_display_name: xylose isomerase

substrate_name: D-glucose

proof_lines: pH 7.0, 50°C, with 0.5 mM Mn2+ and 10 mM Mg2+

enzyme: xylose isomerase

substrate: D-glucose


enzyme_display_name: arabinose-5-phosphate isomerase

substrate_name: D-ribulose 5-phosphate

enzyme: arabinose-5-phosphate isomerase

substrate: D-ribulose 5-phosphate


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


enzyme_display_name: adenylate cyclase

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: pH 8.0, 37°C, recombinant catalytic domain, 10 mM Mg2+

enzyme: adenylate cyclase


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

proof_lines: in presence of 1 mM UDP-N-acetylglucosamine

proof_lines: in presence of 0.5 mM UDP-N-acetylglucosamine

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


organism: Mycobacterium tuberculosis


smiles: NCCCCC(=O)O


substrate_name: Taurine

substrate: Taurine


substrate_name: methylamine

smiles: CN

substrate: methylamine


smiles: NCCCC(=O)O


substrate_name: cysteamine

smiles: NCCS

substrate: cysteamine


substrate_name: ethylamine

smiles: CCN

substrate: ethylamine


substrate_name: glycolate

smiles: O=C(O)CO

substrate: glycolate


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

organism: Verrucomicrobium spinosum

substrate_name: L-alanine

proof_lines: pH 9.0, 37°C, recombinnant enzyme MurB/CVs

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

substrate: L-alanine


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

proof_lines: pH 9.0, 37°C, recombinant enzyme MurB/CVs

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


substrate_name: ATP

assay_conditions_summary: pH 9; 310.15 K; cofactor ATP

substrate: ATP


organism: Rattus norvegicus

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


organism: Lysinibacillus sphaericus

substrate_name: Lys

proof_lines:
in presence of 30 mM K2HPO4
in presence of 2 mM K2HPO4
in presence of 60 mM KCl

substrate: Lys


proof_lines:
in presence of 2 mM K2HPO4
in presence of 30 mM K2HPO4


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

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


organism: Setaria cervi

substrate_name: Gly

assay_conditions_summary: 310.15 K; cofactor ATP

substrate: Gly


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


substrate_name: beta-Alanine

substrate: beta-Alanine


assay_conditions_summary: pH 7.8; 298.15 K; cofactor ATP


substrate_name: Carbamate

substrate: Carbamate


substrate_name: D-Pantoate

substrate: D-Pantoate


enzyme_display_name: glutamate--cysteine ligase

enzyme: glutamate--cysteine ligase


substrate_name: ATP; L-alpha-Aminobutyrate; L-alpha-Methyl glutamate


substrate_name: ATP; L-Glutamate; 3-Cyano-L-alanine

substrate: ATP; L-Glutamate; 3-Cyano-L-alanine


substrate_name: L-Glutamate; L-alpha-Aminobutyrate; ATP

substrate: L-Glutamate; L-alpha-Aminobutyrate; ATP


substrate_name: L-alpha-Aminobutyrate; ATP; L-alpha-Ethyl glutamate


substrate_name: D-Glutamate; ATP; L-alpha-Aminobutyrate

substrate: D-Glutamate; ATP; L-alpha-Aminobutyrate


substrate_name: L-alpha-Aminobutyrate; ATP; L-Glutamate

substrate: L-alpha-Aminobutyrate; ATP; L-Glutamate


organism: Synechocystis sp.

substrate_name: L-glutamate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P74515 and applied mutation signature R248K to reconstruct the assayed variant sequence.

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

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row R248K, substrate Glutamate; column V/Etot (min^-1) = 0.5 ± 0.1; column Km (uM) = 3760 ± 427; column V/Km (M^-1·s^-1) = 2.2. captured primary segment: Table 2 | SynGCL mutant R248K | substrate Glutamate | V/Etot (kcat) 0.5 ± 0.1 min^-1 | Km 3760 ± 427 uM | V/Km (kcat/Km) 2.2 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row R248K, substrate Glutamate: V/Etot = 0.5 ± 0.1 min^-1 (the turnover cell, kcat); Km = 3760 ± 427 uM; printed V/Km = 2.2 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row R248K, substrate Glutamate

table_label: Table 2: Steady-state kinetic parameters of mutant SynGCL (Biochem. J. 2013, 450: 63-72), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1)

substrate: L-glutamate


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row R248K, substrate ATP; column V/Etot (min^-1) = 0.5 ± 0.1; column Km (uM) = 969 ± 77; column V/Km (M^-1·s^-1) = 8.6. captured primary segment: Table 2 | SynGCL mutant R248K | substrate ATP | V/Etot (kcat) 0.5 ± 0.1 min^-1 | Km 969 ± 77 uM | V/Km (kcat/Km) 8.6 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row R248K, substrate ATP: V/Etot = 0.5 ± 0.1 min^-1 (the turnover cell, kcat); Km = 969 ± 77 uM; printed V/Km = 8.6 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row R248K, substrate ATP


substrate_name: L-cysteine

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

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row R248K, substrate Cysteine; column V/Etot (min^-1) = 0.6 ± 0.1; column Km (uM) = 857 ± 10; column V/Km (M^-1·s^-1) = 11.7. captured primary segment: Table 2 | SynGCL mutant R248K | substrate Cysteine | V/Etot (kcat) 0.6 ± 0.1 min^-1 | Km 857 ± 10 uM | V/Km (kcat/Km) 11.7 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 2 V/Etot cell 0.6 min^-1; the printed turnover column is per MINUTE, so 0.6 / 60 = 0.01 s^(-1); the exported value is 0.01 s^(-1). Km: printed Table 2 Km cell 857 uM; 1 uM is 1/1000 mM, so 857 / 1000 = 0.857 mM; the exported value is 0.857 mM. kcat/Km: printed Table 2 V/Km cell 11.7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 11.7 / 1000 = 0.0117 s^(-1)*mM^(-1); the exported value is 0.011668611435239206 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.01 / 0.857 = 0.011668611435239206 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row R248K, substrate Cysteine: V/Etot = 0.6 ± 0.1 min^-1 (the turnover cell, kcat); Km = 857 ± 10 uM; printed V/Km = 11.7 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row R248K, substrate Cysteine

substrate: L-cysteine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P74515 and applied mutation signature R167K to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row R167K, substrate Cysteine; column V/Etot (min^-1) = 1.5 ± 0.2; column Km (uM) = 1950 ± 180; column V/Km (M^-1·s^-1) = 12.8. captured primary segment: Table 2 | SynGCL mutant R167K | substrate Cysteine* (asterisk: reaction performed at sub-saturating 50 mM glutamate) | V/Etot (kcat) 1.5 ± 0.2 min^-1 | Km 1950 ± 180 uM | V/Km (kcat/Km) 12.8 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 2 V/Etot cell 1.5 min^-1; the printed turnover column is per MINUTE, so 1.5 / 60 = 0.025 s^(-1); the exported value is 0.025 s^(-1). Km: printed Table 2 Km cell 1950 uM; 1 uM is 1/1000 mM, so 1950 / 1000 = 1.95 mM; the exported value is 1.95 mM. kcat/Km: printed Table 2 V/Km cell 12.8 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 12.8 / 1000 = 0.0128 s^(-1)*mM^(-1); the exported value is 0.012820512820512822 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.025 / 1.95 = 0.012820512820512822 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row R167K, substrate Cysteine: V/Etot = 1.5 ± 0.2 min^-1 (the turnover cell, kcat); Km = 1950 ± 180 uM; printed V/Km = 12.8 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row R167K, substrate Cysteine


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row R167K, substrate ATP; column V/Etot (min^-1) = 2.3 ± 0.3; column Km (uM) = 445 ± 71; column V/Km (M^-1·s^-1) = 86.1. captured primary segment: Table 2 | SynGCL mutant R167K | substrate ATP* (asterisk: reaction performed at sub-saturating 50 mM glutamate) | V/Etot (kcat) 2.3 ± 0.3 min^-1 | Km 445 ± 71 uM | V/Km (kcat/Km) 86.1 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row R167K, substrate ATP: V/Etot = 2.3 ± 0.3 min^-1 (the turnover cell, kcat); Km = 445 ± 71 uM; printed V/Km = 86.1 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row R167K, substrate ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R167K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P74515 and applied mutation signature H121A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121A, substrate Cysteine; column V/Etot (min^-1) = 5.4 ± 0.1; column Km (uM) = 707 ± 49; column V/Km (M^-1·s^-1) = 127. captured primary segment: Table 2 | SynGCL mutant H121A | substrate Cysteine* (asterisk: reaction performed at sub-saturating 50 mM glutamate) | V/Etot (kcat) 5.4 ± 0.1 min^-1 | Km 707 ± 49 uM | V/Km (kcat/Km) 127 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 2 V/Etot cell 5.4 min^-1; the printed turnover column is per MINUTE, so 5.4 / 60 = 0.09 s^(-1); the exported value is 0.09 s^(-1). Km: printed Table 2 Km cell 707 uM; 1 uM is 1/1000 mM, so 707 / 1000 = 0.707 mM; the exported value is 0.707 mM. kcat/Km: printed Table 2 V/Km cell 127 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 127 / 1000 = 0.127 s^(-1)*mM^(-1); the exported value is 0.1272984441301273 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.09 / 0.707 = 0.1272984441301273 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121A, substrate Cysteine: V/Etot = 5.4 ± 0.1 min^-1 (the turnover cell, kcat); Km = 707 ± 49 uM; printed V/Km = 127 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121A, substrate Cysteine


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121A, substrate ATP; column V/Etot (min^-1) = 5.9 ± 0.2; column Km (uM) = 310 ± 18; column V/Km (M^-1·s^-1) = 317. captured primary segment: Table 2 | SynGCL mutant H121A | substrate ATP* (asterisk: reaction performed at sub-saturating 50 mM glutamate) | V/Etot (kcat) 5.9 ± 0.2 min^-1 | Km 310 ± 18 uM | V/Km (kcat/Km) 317 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 2 V/Etot cell 5.9 min^-1; the printed turnover column is per MINUTE, so 5.9 / 60 = 0.09833333333333333 s^(-1); the exported value is 0.098 s^(-1). Km: printed Table 2 Km cell 310 uM; 1 uM is 1/1000 mM, so 310 / 1000 = 0.31 mM; the exported value is 0.31 mM. kcat/Km: printed Table 2 V/Km cell 317 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 317 / 1000 = 0.317 s^(-1)*mM^(-1); the exported value is 0.31612903225806455 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.09833333333333333 / 0.31 = 0.3172043010752688 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121A, substrate ATP: V/Etot = 5.9 ± 0.2 min^-1 (the turnover cell, kcat); Km = 310 ± 18 uM; printed V/Km = 317 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121A, substrate ATP


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121A, substrate Glutamate; column V/Etot (min^-1) = 7.6 ± 2.4; column Km (uM) = 15200 ± 4900; column V/Km (M^-1·s^-1) = 8.3. captured primary segment: Table 2 | SynGCL mutant H121A | substrate Glutamate | V/Etot (kcat) 7.6 ± 2.4 min^-1 | Km 15200 ± 4900 uM | V/Km (kcat/Km) 8.3 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121A, substrate Glutamate: V/Etot = 7.6 ± 2.4 min^-1 (the turnover cell, kcat); Km = 15200 ± 4900 uM; printed V/Km = 8.3 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121A, substrate Glutamate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P74515 and applied mutation signature T117S to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row T117S, substrate Cysteine; column V/Etot (min^-1) = 8.0 ± 1.3; column Km (uM) = 186 ± 6.1; column V/Km (M^-1·s^-1) = 717. captured primary segment: Table 2 | SynGCL mutant T117S | substrate Cysteine | V/Etot (kcat) 8.0 ± 1.3 min^-1 | Km 186 ± 6.1 uM | V/Km (kcat/Km) 717 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row T117S, substrate Cysteine: V/Etot = 8.0 ± 1.3 min^-1 (the turnover cell, kcat); Km = 186 ± 6.1 uM; printed V/Km = 717 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row T117S, substrate Cysteine


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

column_label: Table 1 (Steady-state kinetic parameters of SynGCL), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 66, PDF page 4. substrate row ATP (wild-type SynGCL); column V/Etot (min^-1) = 30.6 ± 1.9; column Km (uM) = 145 ± 13; column V/Km (M^-1·s^-1) = 3520. captured primary segment: Table 1 | wild-type SynGCL | substrate ATP | V/Etot (kcat) 30.6 ± 1.9 min^-1 | Km 145 ± 13 uM | V/Km (kcat/Km) 3520 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 V/Etot cell 30.6 min^-1; the printed turnover column is per MINUTE, so 30.6 / 60 = 0.51 s^(-1); the exported value is 0.137 s^(-1). Km: printed Table 1 Km cell 145 uM; 1 uM is 1/1000 mM, so 145 / 1000 = 0.145 mM; the exported value is 0.145 mM. kcat/Km: printed Table 1 V/Km cell 3520 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3520 / 1000 = 3.52 s^(-1)*mM^(-1); the exported value is 0.9448275862068967 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.51 / 0.145 = 3.517241379310345 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 66, Table 1 (Steady-state kinetic parameters of SynGCL), substrate row ATP (wild-type SynGCL): V/Etot = 30.6 ± 1.9 min^-1 (the turnover cell, kcat); Km = 145 ± 13 uM; printed V/Km = 3520 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 1, substrate row ATP (wild-type SynGCL)

table_label: Table 1: Steady-state kinetic parameters of SynGCL (Biochem. J. 2013, 450: 63-72), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1)


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row T117S, substrate Glutamate; column V/Etot (min^-1) = 8.2 ± 0.6; column Km (uM) = 6100 ± 150; column V/Km (M^-1·s^-1) = 22.4. captured primary segment: Table 2 | SynGCL mutant T117S | substrate Glutamate | V/Etot (kcat) 8.2 ± 0.6 min^-1 | Km 6100 ± 150 uM | V/Km (kcat/Km) 22.4 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row T117S, substrate Glutamate: V/Etot = 8.2 ± 0.6 min^-1 (the turnover cell, kcat); Km = 6100 ± 150 uM; printed V/Km = 22.4 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row T117S, substrate Glutamate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P74515 and applied mutation signature H121Q to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121Q, substrate Glutamate; column V/Etot (min^-1) = 11.3 ± 1.4; column Km (uM) = 1180 ± 135; column V/Km (M^-1·s^-1) = 160. captured primary segment: Table 2 | SynGCL mutant H121Q | substrate Glutamate | V/Etot (kcat) 11.3 ± 1.4 min^-1 | Km 1180 ± 135 uM | V/Km (kcat/Km) 160 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121Q, substrate Glutamate: V/Etot = 11.3 ± 1.4 min^-1 (the turnover cell, kcat); Km = 1180 ± 135 uM; printed V/Km = 160 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121Q, substrate Glutamate


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row T117S, substrate ATP; column V/Etot (min^-1) = 13.5 ± 1.5; column Km (uM) = 352 ± 19; column V/Km (M^-1·s^-1) = 639. captured primary segment: Table 2 | SynGCL mutant T117S | substrate ATP | V/Etot (kcat) 13.5 ± 1.5 min^-1 | Km 352 ± 19 uM | V/Km (kcat/Km) 639 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 2 V/Etot cell 13.5 min^-1; the printed turnover column is per MINUTE, so 13.5 / 60 = 0.225 s^(-1); the exported value is 0.225 s^(-1). Km: printed Table 2 Km cell 352 uM; 1 uM is 1/1000 mM, so 352 / 1000 = 0.352 mM; the exported value is 0.352 mM. kcat/Km: printed Table 2 V/Km cell 639 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 639 / 1000 = 0.639 s^(-1)*mM^(-1); the exported value is 0.6392045454545455 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.225 / 0.352 = 0.6392045454545455 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row T117S, substrate ATP: V/Etot = 13.5 ± 1.5 min^-1 (the turnover cell, kcat); Km = 352 ± 19 uM; printed V/Km = 639 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row T117S, substrate ATP


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121Q, substrate Cysteine; column V/Etot (min^-1) = 20.1 ± 2.7; column Km (uM) = 116 ± 16; column V/Km (M^-1·s^-1) = 2890. captured primary segment: Table 2 | SynGCL mutant H121Q | substrate Cysteine | V/Etot (kcat) 20.1 ± 2.7 min^-1 | Km 116 ± 16 uM | V/Km (kcat/Km) 2890 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 2 V/Etot cell 20.1 min^-1; the printed turnover column is per MINUTE, so 20.1 / 60 = 0.335 s^(-1); the exported value is 0.335 s^(-1). Km: printed Table 2 Km cell 116 uM; 1 uM is 1/1000 mM, so 116 / 1000 = 0.116 mM; the exported value is 0.116 mM. kcat/Km: printed Table 2 V/Km cell 2890 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2890 / 1000 = 2.89 s^(-1)*mM^(-1); the exported value is 2.8879310344827585 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.335 / 0.116 = 2.8879310344827585 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121Q, substrate Cysteine: V/Etot = 20.1 ± 2.7 min^-1 (the turnover cell, kcat); Km = 116 ± 16 uM; printed V/Km = 2890 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121Q, substrate Cysteine


column_label: Table 1 (Steady-state kinetic parameters of SynGCL), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 66, PDF page 4. substrate row Glutamate (wild-type SynGCL); column V/Etot (min^-1) = 21.0 ± 1.3; column Km (uM) = 953 ± 16; column V/Km (M^-1·s^-1) = 367. captured primary segment: Table 1 | wild-type SynGCL | substrate Glutamate | V/Etot (kcat) 21.0 ± 1.3 min^-1 | Km 953 ± 16 uM | V/Km (kcat/Km) 367 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 V/Etot cell 21.0 min^-1; the printed turnover column is per MINUTE, so 21.0 / 60 = 0.35 s^(-1); the exported value is 0.35 s^(-1). Km: printed Table 1 Km cell 953 uM; 1 uM is 1/1000 mM, so 953 / 1000 = 0.953 mM; the exported value is 0.953 mM. kcat/Km: printed Table 1 V/Km cell 367 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 367 / 1000 = 0.367 s^(-1)*mM^(-1); the exported value is 0.3672612801678909 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.35 / 0.953 = 0.3672612801678909 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 66, Table 1 (Steady-state kinetic parameters of SynGCL), substrate row Glutamate (wild-type SynGCL): V/Etot = 21.0 ± 1.3 min^-1 (the turnover cell, kcat); Km = 953 ± 16 uM; printed V/Km = 367 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 1, substrate row Glutamate (wild-type SynGCL)


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121Q, substrate ATP; column V/Etot (min^-1) = 22.9 ± 2.2; column Km (uM) = 279 ± 66; column V/Km (M^-1·s^-1) = 1370. captured primary segment: Table 2 | SynGCL mutant H121Q | substrate ATP | V/Etot (kcat) 22.9 ± 2.2 min^-1 | Km 279 ± 66 uM | V/Km (kcat/Km) 1370 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121Q, substrate ATP: V/Etot = 22.9 ± 2.2 min^-1 (the turnover cell, kcat); Km = 279 ± 66 uM; printed V/Km = 1370 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121Q, substrate ATP


column_label: Table 1 (Steady-state kinetic parameters of SynGCL), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 66, PDF page 4. substrate row Cysteine (wild-type SynGCL); column V/Etot (min^-1) = 25.2 ± 1.7; column Km (uM) = 59 ± 0.5; column V/Km (M^-1·s^-1) = 7120. captured primary segment: Table 1 | wild-type SynGCL | substrate Cysteine | V/Etot (kcat) 25.2 ± 1.7 min^-1 | Km 59 ± 0.5 uM | V/Km (kcat/Km) 7120 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 V/Etot cell 25.2 min^-1; the printed turnover column is per MINUTE, so 25.2 / 60 = 0.42 s^(-1); the exported value is 0.42 s^(-1). Km: printed Table 1 Km cell 59 uM; 1 uM is 1/1000 mM, so 59 / 1000 = 0.059 mM; the exported value is 0.059 mM. kcat/Km: printed Table 1 V/Km cell 7120 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7120 / 1000 = 7.12 s^(-1)*mM^(-1); the exported value is 7.11864406779661 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.42 / 0.059 = 7.11864406779661 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 66, Table 1 (Steady-state kinetic parameters of SynGCL), substrate row Cysteine (wild-type SynGCL): V/Etot = 25.2 ± 1.7 min^-1 (the turnover cell, kcat); Km = 59 ± 0.5 uM; printed V/Km = 7120 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 1, substrate row Cysteine (wild-type SynGCL)


organism: Trypanosoma brucei

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E489A with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

proof_lines: mutant E489A, pH 8.0, 37°C, in presence of Mn2+

proof_lines: mutant E489A, pH 8.0, 37°C, in presence of Mg2+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E93A to reconstruct the assayed variant sequence.

proof_lines: mutant E93A, pH 8.0, 37°C, in presence of Mg2+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q321A to reconstruct the assayed variant sequence.


proof_lines: mutant Q321A, pH 8.0, 37°C, in presence of Mn2+


proof_lines: wild-type and mutant enzyme, pH 8.0, 37°C

proof_lines: wild-type enzyme, pH 8.0, 37°C, in presence of Mn2+


proof_lines: mutant Q321A, pH 8.0, 37°C, in presence of Mg2+


substrate_name: L-alpha-aminobutyrate

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

substrate: L-alpha-aminobutyrate


organism: Arabidopsis thaliana

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R454A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R454A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


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

assay_conditions_summary: pH 7.5; cofactor NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K456M with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K456M, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R274K with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R274K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N376A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N376A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R454K with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S155A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S153A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


organism: Allium cepa

proof_lines: in the absence of Cd2+, pH and temperature not specified in the publication

proof_lines: in the presence of 0.1 mM Cd2+, pH and temperature not specified in the publication


organism: Pseudoalteromonas haloplanktis


assay_conditions_summary: pH 8; 288.15 K; cofactor ATP


enzyme_display_name: D-alanine--D-alanine ligase

assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8
kcat is 9.7 sec(-1) (at pH 7.3).

enzyme: D-alanine--D-alanine ligase


substrate_name: D-alanine

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

substrate: D-alanine


substrate_name: ATP

assay_conditions_summary: pH 7.8; cofactor ATP

proof_lines: pH 7.8, 10°C, recombinant enzyme, ATPase activity

proof_lines: pH 7.8, 15°C, recombinant enzyme, ATPase activity

proof_lines: pH 7.8, 20°C, recombinant enzyme, ATPase activity


substrate_name: gamma-L-glutamyl-L-cysteine

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

substrate: gamma-L-glutamyl-L-cysteine


substrate_name: glycine

substrate: glycine


substrate_name: L-Glu

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C319A to reconstruct the assayed variant sequence.

substrate: L-Glu


substrate_name: L-2-aminobutyric acid

substrate: L-2-aminobutyric acid


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q26820 and applied mutation signature R491A to reconstruct the assayed variant sequence.

column_label: Table 1, Table 1, enzyme row 'R491A'; column 'kcat (s-1)' = 0.055; column 'Kmapp(L-Glu) (mM)' = 0.61; column 'Kmapp(L-Aba) (mM)' = nd; column 'Kmapp(ATP) (mM)' = 0.11; Table 1 carries no kcat/Km column. The printed cells carry error terms that this pdftotext rendering shows with the plus-minus sign decoded as an opening parenthesis, and only the leading value of each cell is transcribed here.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.055 s-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 0.055 s^(-1). Km: printed Table 1 cell 0.61 mM; already in mM, so no unit conversion applies; the paper value is 0.61 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 0.09016393442622951 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.055 / 0.61 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Table 1, enzyme row 'R491A': kcat = 0.055 s-1; apparent Km = 0.61 mM; Table 1 prints no kcat/Km cell for this measurement.

row_label: Table 1, enzyme row 'R491A'

table_label: Table 1: Steady-State Kinetic Analysis of T. brucei gamma-GCS Mutant Enzymes (Biochemistry 2002, 41(8):2741-2750)


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

column_label: Table 3, Table 3, wild-type gamma-GCS column, rows 'kcat(GABA) (s-1)' and 'Kmapp(GABA) (mM)'; row 'kcat(GABA) (s-1)' = 0.14; row 'Kmapp(GABA) (mM)' = 150; row 'kcat(L-Glu) (s-1)' = 3.9; row 'Kmapp(L-Glu) (mM)' = 0.24; Table 3 carries no kcat/Km column. The printed cells carry error terms that this pdftotext rendering shows with the plus-minus sign decoded as an opening parenthesis, and only the leading value of each cell is transcribed here.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.14 s-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 0.14 s^(-1). Km: printed Table 3 cell 150 mM; already in mM, so no unit conversion applies; the paper value is 150.0 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 0.0009333333333333334 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.14 / 150 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, Table 3, wild-type gamma-GCS column, rows 'kcat(GABA) (s-1)' and 'Kmapp(GABA) (mM)': kcat = 0.14 s-1; apparent Km = 150 mM; Table 3 prints no kcat/Km cell for this measurement.

table_label: Table 3: Comparison of Wild-Type and R366A gamma-GCS Steady-State Kinetics for ATP Hydrolysis with L-Glu versus GABA as Substrates (Biochemistry 2002, 41(8):2741-2750)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q26820 and applied mutation signature R474A to reconstruct the assayed variant sequence.

column_label: Table 1, Table 1, enzyme row 'R474A'; column 'kcat (s-1)' = 0.24; column 'Kmapp(L-Glu) (mM)' = 1.6; column 'Kmapp(L-Aba) (mM)' = 56; column 'Kmapp(ATP) (mM)' = 1.3; Table 1 carries no kcat/Km column. The printed cells carry error terms that this pdftotext rendering shows with the plus-minus sign decoded as an opening parenthesis, and only the leading value of each cell is transcribed here.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.24 s-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 0.24 s^(-1). Km: printed Table 1 cell 1.6 mM; already in mM, so no unit conversion applies; the paper value is 1.6 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 0.15 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.24 / 1.6 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Table 1, enzyme row 'R474A': kcat = 0.24 s-1; apparent Km = 1.6 mM; Table 1 prints no kcat/Km cell for this measurement.

row_label: Table 1, enzyme row 'R474A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q26820 and applied mutation signature R366A to reconstruct the assayed variant sequence.

column_label: Table 1, Table 1, enzyme row 'R366A'; column 'kcat (s-1)' = 0.32; column 'Kmapp(L-Glu) (mM)' = 130; column 'Kmapp(L-Aba) (mM)' = 34; column 'Kmapp(ATP) (mM)' = 2.8; Table 1 carries no kcat/Km column. The printed cells carry error terms that this pdftotext rendering shows with the plus-minus sign decoded as an opening parenthesis, and only the leading value of each cell is transcribed here.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.32 s-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 0.32 s^(-1). Km: printed Table 1 cell 130 mM; already in mM, so no unit conversion applies; the paper value is 130.0 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 0.0024615384615384616 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.32 / 130 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Table 1, enzyme row 'R366A': kcat = 0.32 s-1; apparent Km = 130 mM; Table 1 prints no kcat/Km cell for this measurement.

row_label: Table 1, enzyme row 'R366A'


column_label: Table 3, Table 3, R366A gamma-GCS column, rows 'kcat(GABA) (s-1)' and 'Kmapp(GABA) (mM)'; row 'kcat(GABA) (s-1)' = 0.59; row 'Kmapp(GABA) (mM)' = 20; row 'kcat(L-Glu) (s-1)' = 0.32; row 'Kmapp(L-Glu) (mM)' = 130; Table 3 carries no kcat/Km column. The printed cells carry error terms that this pdftotext rendering shows with the plus-minus sign decoded as an opening parenthesis, and only the leading value of each cell is transcribed here.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.59 s-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 0.59 s^(-1). Km: printed Table 3 cell 20 mM; already in mM, so no unit conversion applies; the paper value is 20.0 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 0.0295 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.59 / 20 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, Table 3, R366A gamma-GCS column, rows 'kcat(GABA) (s-1)' and 'Kmapp(GABA) (mM)': kcat = 0.59 s-1; apparent Km = 20 mM; Table 3 prints no kcat/Km cell for this measurement.