proof_lines:
reaction with tetrahydropteroyl-Glu5
reaction with tetrahydropteroyl-Glu3
reaction with tetrahydropteroyl-Glu2


enzyme_display_name: CTP synthase (glutamine hydrolyzing)

organism: Homo sapiens

substrate_name: ATP

source_db: brenda

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: cofactor ATP

data_origin: experimental

enzyme: CTP synthase (glutamine hydrolyzing)

substrate: ATP

status: unverified

source: brenda


enzyme_display_name: adenylosuccinate synthase

organism: Oryctolagus cuniculus

substrate_name: GTP

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

enzyme: adenylosuccinate synthase

substrate: GTP


organism: Mus musculus

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


enzyme_display_name: argininosuccinate synthase

organism: Rattus norvegicus

proof_lines:
enzyme form ASSI
enzyme form ASSII

enzyme: argininosuccinate synthase


substrate_name: L-Asp

proof_lines:
enzyme form ASSII
enzyme form ASSI

substrate: L-Asp


enzyme_display_name: urea carboxylase

organism: Saccharomyces cerevisiae

substrate_name: Urea

enzyme: urea carboxylase

substrate: Urea


organism: Helicobacter pylori


substrate_name: citrulline

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

proof_lines:
reaction with 5 mM Asp
normal liver
reaction with 0.5 mM Asp

substrate: citrulline


substrate_name: arabinosylIMP

substrate: arabinosylIMP


enzyme_display_name: phosphoenolpyruvate mutase

organism: Trypanosoma cruzi

substrate_name: Phosphonopyruvate

enzyme: phosphoenolpyruvate mutase

substrate: Phosphonopyruvate


enzyme_display_name: peptidylprolyl isomerase

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

assay_conditions_summary: pH 7.8; 283.15 K; buffer 35 mM sodium HEPES

proof_lines: at 10°C in 35 mM sodium HEPES buffer, pH 7.8

enzyme: peptidylprolyl isomerase


enzyme_display_name: cellobiose epimerase

organism: uncultured bacterium

substrate_name: cellobiose

proof_lines:
recombinant enzyme, pH 7.5, 30°C
recombinant enzyme, pH 7.5, 25°C

enzyme: cellobiose epimerase

substrate: cellobiose


enzyme_display_name: methionine--tRNA ligase

assay_conditions_summary: 296.15 K; cofactor ATP

proof_lines: substrate ATP, 23°C, pH not specified in the publication

proof_lines: substrate L-methionine, 23°C, pH not specified in the publication

enzyme: methionine--tRNA ligase


enzyme_display_name: triose-phosphate isomerase

substrate_name: D-glyceraldehyde 3-phosphate

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

proof_lines: in 100 mM TEA, 10 mM EDTA, pH 7.4, at 25°C

proof_lines: in complex with monomer from Trypanosoma brucei, pH 7.4, 25°C

enzyme: triose-phosphate isomerase

substrate: D-glyceraldehyde 3-phosphate


enzyme_display_name: maleylacetoacetate isomerase

organism: Vibrio sp.

substrate_name: maleylacetone

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

enzyme: maleylacetoacetate isomerase

substrate: maleylacetone


substrate_name: GSH

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

substrate: GSH


enzyme_display_name: S-ribosylhomocysteine lyase

organism: Vibrio harveyi

enzyme: S-ribosylhomocysteine lyase


substrate_name: 6-Oxo-2(E),4(Z)-heptanedienoic acid

substrate: 6-Oxo-2(E),4(Z)-heptanedienoic acid


enzyme_display_name: UDP-glucose 4-epimerase

organism: Vicia faba

substrate_name: UDPgalactose

enzyme: UDP-glucose 4-epimerase

substrate: UDPgalactose


enzyme_display_name: glutamine synthetase

organism: Vigna radiata

enzyme: glutamine synthetase


substrate_name: S-ribosylhomocysteine

substrate: S-ribosylhomocysteine


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Winmispira thermophila

proof_lines:
pH 7.5, 30°C, recombinant enzyme
pH 7.0, 60°C


substrate_name: UTP

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: pH 8.0, 30°C, phosphorylated enzyme, in presence of 2 mM ATP

proof_lines: pH 8.0, 30°C, native enzyme, in presence of 2 mM ATP

proof_lines: pH 8.0, 30°C, native enzyme or phosphorylated enzyme, in presence of 0.5 mM ATP

substrate: UTP


enzyme_display_name: chorismate mutase

organism: Yersinia pestis

substrate_name: chorismate

enzyme: chorismate mutase

substrate: chorismate


enzyme_display_name: (S)-beta-macrocarpene synthase

organism: Zea mays

substrate_name: geranyl diphosphate

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

proof_lines: recombinant enzyme, in the presence of 0.05 mM Mn2+, pH and temperature not specified in the publication

enzyme: (S)-beta-macrocarpene synthase

substrate: geranyl diphosphate


organism: Equus caballus

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


enzyme_display_name: cysteine--tRNA ligase

organism: Vigna radiata var. radiata

substrate_name: ATP

enzyme: cysteine--tRNA ligase

substrate: ATP


enzyme_display_name: cycloartenol synthase

enzyme: cycloartenol synthase


enzyme_display_name: mannose-6-phosphate isomerase

organism: Xanthomonas campestris

substrate_name: mannose 6-phosphate

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

enzyme: mannose-6-phosphate isomerase

substrate: mannose 6-phosphate


organism: Oryctolagus cuniculus


organism: Onchocerca volvulus


enzyme_display_name: adenylosuccinate synthase

organism: Leishmania donovani

enzyme: adenylosuccinate synthase


organism: Micrococcus luteus

substrate_name: alpha-D-Glucose 1-phosphate

substrate: alpha-D-Glucose 1-phosphate


enzyme_display_name: bisphosphoglycerate mutase

substrate_name: 2,3-Bisphosphoglycerate; H2O

enzyme: bisphosphoglycerate mutase

substrate: 2,3-Bisphosphoglycerate; H2O


organism: Bacillus cereus


organism: Rattus norvegicus


enzyme_display_name: phosphomannomutase

substrate_name: D-Mannose 6-phosphate

enzyme: phosphomannomutase

substrate: D-Mannose 6-phosphate


organism: Triticum aestivum

substrate_name: Glucose 1-phosphate

substrate: Glucose 1-phosphate


organism: Sus scrofa


organism: Phaseolus aureus

substrate_name: ATP; tRNA(Cys); L-Cysteine

substrate: ATP; tRNA(Cys); L-Cysteine


enzyme_display_name: beta-phosphoglucomutase

organism: Neisseria meningitidis

substrate_name: beta-D-Glucose 1-phosphate

enzyme: beta-phosphoglucomutase

substrate: beta-D-Glucose 1-phosphate


enzyme_display_name: aspartate--tRNA ligase

organism: Lactobacillus plantarum

substrate_name: L-Aspartate; ATP; tRNA(Asp)

enzyme: aspartate--tRNA ligase

substrate: L-Aspartate; ATP; tRNA(Asp)


enzyme_display_name: acetate--CoA ligase

organism: Methanothermobacter thermautotrophicus

substrate_name: Coenzyme A; ATP; Acetate

enzyme: acetate--CoA ligase

substrate: Coenzyme A; ATP; Acetate


enzyme_display_name: propionate--CoA ligase

organism: Bos taurus

substrate_name: ATP; Coenzyme A; Propanoate

enzyme: propionate--CoA ligase

substrate: ATP; Coenzyme A; Propanoate


organism: Homo sapiens

substrate_name: Butanoate; ATP; Coenzyme A

assay_conditions_summary: cofactor CoA

substrate: Butanoate; ATP; Coenzyme A


enzyme_display_name: medium-chain acyl-CoA ligase

substrate_name: Benzoate; ATP; Coenzyme A

enzyme: medium-chain acyl-CoA ligase

substrate: Benzoate; ATP; Coenzyme A


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

organism: Escherichia coli

substrate_name: Coenzyme A; Oleate; ATP

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

substrate: Coenzyme A; Oleate; ATP


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

organism: Mycobacterium bovis

substrate_name: Phosphate; Succinyl-CoA; ADP

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

substrate: Phosphate; Succinyl-CoA; ADP


enzyme_display_name: histidine--tRNA ligase

organism: Salmonella typhimurium

substrate_name: L-Histidine; tRNA(His); ATP

enzyme: histidine--tRNA ligase

substrate: L-Histidine; tRNA(His); ATP


substrate_name: ATP; Propanoate; Coenzyme A

substrate: ATP; Propanoate; Coenzyme A


organism: Saccharomyces cerevisiae

substrate_name: Glucose 6-phosphate

substrate: Glucose 6-phosphate


enzyme_display_name: glutamine synthetase

organism: Bacillus caldolyticus

substrate_name: L-Glutamate; ATP; NH3

enzyme: glutamine synthetase

substrate: L-Glutamate; ATP; NH3


substrate_name: Phosphate; ADP; Succinyl-CoA

substrate: Phosphate; ADP; Succinyl-CoA


organism: Mycobacterium tuberculosis

substrate_name: ADP; Phosphate; Succinyl-CoA

substrate: ADP; Phosphate; Succinyl-CoA


organism: Mycobacterium smegmatis


enzyme_display_name: D-alanine--D-alanine ligase

substrate_name: D-Alanine; ATP

enzyme: D-alanine--D-alanine ligase

substrate: D-Alanine; ATP


enzyme_display_name: formate--tetrahydrofolate ligase

organism: Pisum sativum

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

enzyme: formate--tetrahydrofolate ligase

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


organism: Enterococcus faecalis


substrate_name: ADP; Succinyl-CoA; Phosphate

assay_conditions_summary: cofactor ADP

substrate: ADP; Succinyl-CoA; Phosphate


enzyme_display_name: CTP synthase (glutamine hydrolyzing)

substrate_name: ATP; NH3; UTP

enzyme: CTP synthase (glutamine hydrolyzing)

substrate: ATP; NH3; UTP


enzyme_display_name: carnosine synthase

substrate_name: ATP; L-Histidine; beta-Alanine

enzyme: carnosine synthase

substrate: ATP; L-Histidine; beta-Alanine


enzyme_display_name: argininosuccinate synthase

substrate_name: L-Aspartate; L-Citrulline; ATP

enzyme: argininosuccinate synthase

substrate: L-Aspartate; L-Citrulline; ATP


enzyme_display_name: D-tagatose 3-epimerase

organism: Pseudomonas cichorii

substrate_name: L-ribulose

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

enzyme: D-tagatose 3-epimerase

substrate: L-ribulose


enzyme_display_name: cholestenol Delta-isomerase

organism: Rattus norvegicus

enzyme: cholestenol Delta-isomerase


organism: Lactococcus lactis subsp. cremoris

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


organism: Ustilago maydis


substrate_name: alpha-D-Ribose 1-phosphate

substrate: alpha-D-Ribose 1-phosphate


organism: Pseudomonas aeruginosa

substrate_name: D-Ribose 1-phosphate

substrate: D-Ribose 1-phosphate


organism: Sus scrofa

substrate_name: ATP; L-Aspartate; L-Citrulline

substrate: ATP; L-Aspartate; L-Citrulline


enzyme_display_name: trypanothione synthase

organism: Trypanosoma brucei

substrate_name: Glutathionylspermidine

assay_conditions_summary: pH 7

enzyme: trypanothione synthase

substrate: Glutathionylspermidine


substrate_name: ADP

substrate: ADP


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

organism: Streptomyces lavendulae

substrate_name: D-homoserine

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

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

substrate: D-homoserine


substrate_name: beta-aminooxy-D-alanine

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

substrate: beta-aminooxy-D-alanine


substrate_name: D-ornithine

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

substrate: D-ornithine


substrate_name: 2-Deoxyglucose 6-phosphate

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

substrate: 2-Deoxyglucose 6-phosphate


enzyme_display_name: phosphopentomutase

enzyme: phosphopentomutase


enzyme_display_name: isobutyryl-CoA mutase

organism: Xanthobacter autotrophicus

enzyme: isobutyryl-CoA mutase


enzyme_display_name: chorismate mutase

substrate_name: Chorismate

enzyme: chorismate mutase

substrate: Chorismate


enzyme_display_name: lanosterol synthase

organism: Mus musculus

enzyme: lanosterol synthase


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

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


enzyme_display_name: UniProt A0A0H3KFM7

organism: Staphylococcus aureus

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt A0A0H3KFM7

source: skid


enzyme_display_name: UniProt A1CII2

organism: Aspergillus clavatus

enzyme: UniProt A1CII2


substrate_name: ATP

substrate: ATP


enzyme_display_name: UniProt O67728

organism: Aquifex aeolicus

enzyme: UniProt O67728


substrate_name: L-lysine

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

substrate: L-lysine


enzyme_display_name: UniProt O28025

organism: Archaeoglobus fulgidus

substrate_name: agmatine

smiles: C(CCN=C(N)N)CN

enzyme: UniProt O28025

substrate: agmatine


enzyme_display_name: formate--dihydrofolate ligase

organism: Homo sapiens

substrate_name: dihydrofolate

enzyme: formate--dihydrofolate ligase

substrate: dihydrofolate


mutation_type: substitution


organism: Lacticaseibacillus casei


proof_lines: mutant enzyme R271K, in 50 mM HEPES, pH 7.8, at 37°C


proof_lines: mutant enzyme Y152A, in 50 mM HEPES, pH 7.8, at 37°C


proof_lines: mutant enzyme Y152F, in 50 mM HEPES, pH 7.8, at 37°C


proof_lines: wild type enzyme, in 50 mM HEPES, pH 7.8, at 37°C


proof_lines: mutant enzyme R155A, in 50 mM HEPES, pH 7.8, at 37°C


proof_lines: mutant enzyme D153A, in 50 mM HEPES, pH 7.8, at 37°C


proof_lines: mutant enzyme E73A, in 50 mM HEPES, pH 7.8, at 37°C


organism: Escherichia coli

substrate_name: Hydrogencarbonate; ATP; Aminoimidazole ribotide


substrate_name: ATP; Hydrogencarbonate; Aminoimidazole ribotide


enzyme_display_name: tRNA(Ile)-lysidine synthetase

organism: Geobacillus kaustophilus

substrate_name: precursor [tRNAIle2]-cytidine34

enzyme: tRNA(Ile)-lysidine synthetase

substrate: precursor [tRNAIle2]-cytidine34


enzyme_display_name: nicotinate phosphoribosyltransferase

enzyme: nicotinate phosphoribosyltransferase


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

substrate_name: nicotinate in the absence of ATP

source_db: uniprot

substrate: nicotinate in the absence of ATP

source: uniprot


substrate_name: Aminoimidazole ribotide

source_db: oed

kcat_over_km_origin: calculated

substrate: Aminoimidazole ribotide

source: oed


assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


enzyme_display_name: tyramine--L-glutamate ligase

organism: Methanocaldococcus fervens (strain DSM 4213 / JCM 15782 / AG86)

substrate_name: tyramine

proof_lines: kcat is 4.8 sec(-1) toward tyramine. kcat is 5.8 sec(-1) toward L-glutamate. kcat is 5.9 sec(-1) toward ATP.

enzyme: tyramine--L-glutamate ligase

substrate: tyramine


substrate_name: L-glutamate

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

substrate: L-glutamate


enzyme_display_name: tRNA(Ile)(2)-agmatinylcytidine synthase

smiles: N=C(N)NCCCCN

assay_conditions_summary: pH 8.8; 343.15 K; cofactor ATP

enzyme: tRNA(Ile)(2)-agmatinylcytidine synthase


substrate_name: nicotinate in the presence of ATP

substrate: nicotinate in the presence of ATP


substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate in the presence of ATP


organism: Methanocaldococcus fervens

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E21Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.7; 343.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R251A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T253V to reconstruct the assayed variant sequence.


verification_status: verified

column_label: Table 1 (Apparent Steady-State Kinetic Parameters of MfnD and Its Variants), ATP-Dependent Apparent Kinetic Parameters block, enzyme column 'wild-type'; row 'kcat(app) (s^-1)' = 5.9; row 'KM(app) (mM)' = 1.5; row 'kcat(app)/KM(app) (M^-1 s^-1)' = 3.9 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.9 s^-1; already in s^-1, so no unit conversion applies; the catalog value is 5.9 s^(-1). Km: printed Table 1 cell 1.5 mM; already in mM, so no unit conversion applies; the catalog value is 1.5 mM. kcat/Km: printed Table 1 cell 3.9 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.9 x 10^3 x 0.001 = 3.9 s^-1 mM^-1. The quotient of the two printed component cells is 5.9 / 1.5 = 3.933333333333333 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, ATP-Dependent Apparent Kinetic Parameters block, column wild-type: kcat(app) = 5.9 s^-1; KM(app) = 1.5 mM; kcat(app)/KM(app) = 3.9 x 10^3 M^-1 s^-1.

table_label: Table 1. Apparent Steady-State Kinetic Parameters of MfnD and Its Variants (Biochemistry 2014, 53(39):6220-6230)

status: verified


column_label: Table 1 (Apparent Steady-State Kinetic Parameters of MfnD and Its Variants), Glutamate-Dependent Apparent Kinetic Parameters block, enzyme column 'wild-type'; row 'kcat(app) (s^-1)' = 5.8; row 'KM(app) (mM)' = 2.3; row 'kcat(app)/KM(app) (M^-1 s^-1)' = 2.5 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.8 s^-1; already in s^-1, so no unit conversion applies; the catalog value is 5.8 s^(-1). Km: printed Table 1 cell 2.3 mM; already in mM, so no unit conversion applies; the catalog value is 2.3 mM. kcat/Km: printed Table 1 cell 2.5 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.5 x 10^3 x 0.001 = 2.5 s^-1 mM^-1. The quotient of the two printed component cells is 5.8 / 2.3 = 2.5217391304347827 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, Glutamate-Dependent Apparent Kinetic Parameters block, column wild-type: kcat(app) = 5.8 s^-1; KM(app) = 2.3 mM; kcat(app)/KM(app) = 2.5 x 10^3 M^-1 s^-1.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:C7P8V7 and applied mutation signature E21Q to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent Steady-State Kinetic Parameters of MfnD and Its Variants), Tyramine-Dependent Apparent Kinetic Parameters block, enzyme column 'E21Q'; row 'kcat(app) (s^-1)' = 1.7; row 'KM(app) (mM)' = 1.1; row 'kcat(app)/KM(app) (M^-1 s^-1)' = 1.7 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.7 s^-1; already in s^-1, so no unit conversion applies; the catalog value is 1.7 s^(-1). Km: printed Table 1 cell 1.1 mM; already in mM, so no unit conversion applies; the catalog value is 1.1 mM. kcat/Km: printed Table 1 cell 1.7 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.7 x 10^3 x 0.001 = 1.7 s^-1 mM^-1. The quotient of the two printed component cells is 1.7 / 1.1 = 1.5454545454545454 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, Tyramine-Dependent Apparent Kinetic Parameters block, column E21Q: kcat(app) = 1.7 s^-1; KM(app) = 1.1 mM; kcat(app)/KM(app) = 1.7 x 10^3 M^-1 s^-1.

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:C7P8V7 and applied mutation signature R251A to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent Steady-State Kinetic Parameters of MfnD and Its Variants), Tyramine-Dependent Apparent Kinetic Parameters block, enzyme column 'R251A'; row 'kcat(app) (s^-1)' = 0.05; row 'KM(app) (mM)' = 0.80; row 'kcat(app)/KM(app) (M^-1 s^-1)' = 6.0 x 10^1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.05 s^-1; already in s^-1, so no unit conversion applies; the catalog value is 0.05 s^(-1). Km: printed Table 1 cell 0.80 mM; already in mM, so no unit conversion applies; the catalog value is 0.8 mM. kcat/Km: printed Table 1 cell 6.0 x 10^1 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.0 x 10^1 x 0.001 = 0.06 s^-1 mM^-1. The quotient of the two printed component cells is 0.05 / 0.80 = 0.0625 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, Tyramine-Dependent Apparent Kinetic Parameters block, column R251A: kcat(app) = 0.05 s^-1; KM(app) = 0.80 mM; kcat(app)/KM(app) = 6.0 x 10^1 M^-1 s^-1.


assay_conditions_summary: pH 7.8; 333.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D153A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E73A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R155A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R271K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y152A with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y152F with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


organism: Bacillus subtilis

substrate_name: nicotinate

substrate: nicotinate


substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


substrate_name: GTP

substrate: GTP


substrate_name: nicotinic acid (in the presence of 3 mM ATP)


substrate_name: 5-phosphoribosyl-1-pyrophosphate (in the presence of 3 mM ATP)


proof_lines: mutant enzyme F78I, in 50 mM HEPES, 80 mM KCl, 20 mM MgCl2, at 22°C, pH not specified in the publication


proof_lines: mutant enzyme F78W, in 50 mM HEPES, 80 mM KCl, 20 mM MgCl2, at 22°C, pH not specified in the publication


proof_lines: wild type enzyme, in 50 mM HEPES, 80 mM KCl, 20 mM MgCl2, at 22°C, pH not specified in the publication


substrate_name: ATP

assay_conditions_summary: 295.15 K; cofactor ATP


proof_lines:
unmodified tRNAIle2, pH 7.8, 37°C
pH 8.5, 21°C


assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP


substrate_name: L-lysine


substrate_name: agmatine


row_label: Table 1, Tyramine-Dependent Apparent Kinetic Parameters block, column R251A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R251A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T253V to reconstruct the assayed variant sequence.


row_label: Table 1, Tyramine-Dependent Apparent Kinetic Parameters block, column E21Q


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E21Q to reconstruct the assayed variant sequence.


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

column_label: Table 1 (Apparent Steady-State Kinetic Parameters of MfnD and Its Variants), Tyramine-Dependent Apparent Kinetic Parameters block, enzyme column 'wild-type'; row 'kcat(app) (s^-1)' = 4.8; row 'KM(app) (mM)' = 0.80; row 'kcat(app)/KM(app) (M^-1 s^-1)' = 6.0 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 4.8 s^-1; already in s^-1, so no unit conversion applies; the catalog value is 4.8 s^(-1). Km: printed Table 1 cell 0.80 mM; already in mM, so no unit conversion applies; the catalog value is 0.8 mM. kcat/Km: printed Table 1 cell 6.0 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.0 x 10^3 x 0.001 = 6.0 s^-1 mM^-1. The quotient of the two printed component cells is 4.8 / 0.80 = 6.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, Tyramine-Dependent Apparent Kinetic Parameters block, column wild-type: kcat(app) = 4.8 s^-1; KM(app) = 0.80 mM; kcat(app)/KM(app) = 6.0 x 10^3 M^-1 s^-1.


row_label: Table 1, Glutamate-Dependent Apparent Kinetic Parameters block, column wild-type


row_label: Table 1, ATP-Dependent Apparent Kinetic Parameters block, column wild-type


organism: Salmonella enterica subsp. enterica serovar Typhimurium

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

proof_lines: in the coupled reaction, 200fold lower than in the uncoupled reaction


substrate_name: ITP

substrate: ITP


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+

proof_lines: in the presence of phosphate, pH 7.5, 37°C

proof_lines: +/-0.07 microM, in presence of 1 mM NAD+, 20 ng enzyme, 40 microM nicotinamide, 0.14-1 microM PRPP, 15 min, 37°C, TLC-based quantification


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


organism: Bos taurus


organism: Rattus norvegicus

proof_lines: reduced to 0.002 mM in the presence of ATP


proof_lines: reduced to 0.053 mM in the presence of ATP


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

proof_lines: pH 8.0, 25°C, chimeric mutant with PurK activity


organism: Sus scrofa


organism: Saccharomyces cerevisiae


row_label: Table 1, Tyramine-Dependent Apparent Kinetic Parameters block, column wild-type


proof_lines:
pncB gene, in the coupled reaction
pncB gene, in the uncoupled reaction


substrate_name: nicotinic acid

assay_conditions_summary: 310.15 K; cofactor NAD+

proof_lines: +/-3.6 microM, in presence of 1 mM NAD+, 80 ng enzyme, 10-70 microM nicotinamide, 0.3 mM PRPP, 30 min, 37°C, TLC-based quantification

proof_lines: +/-3.4 microM, 80 ng enzyme, 10-70 microM nicotinamide, 0.3 mM PRPP, 30 min, 37°C, TLC-based quantification

substrate: nicotinic acid


organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)

column_label: Table 3 PncB/Na row reports Km 0.0002, kcat 0.40, and kcat/Km 2.0 x 10^3 in the table units.

normalized_value_unit_evidence: Km normalized 0.0002 mM; kcat normalized 0.40 s^-1; kcat/Km normalized 2000 s^-1 mM^-1.

row_label: PncB row; variable substrate Na; fixed substrates PRPP and ATP

table_label: Table 3 steady-state kinetic parameters of the A. baylyi NAD biosynthesis enzymes


substrate_name: nicotinamide

column_label: Table 3 PncB/Nm row reports Km 6.9, kcat 0.004, and kcat/Km 5.8 x 10^-4 in the table units.

normalized_value_unit_evidence: Km normalized 6.9 mM; kcat normalized 0.004 s^-1; kcat/Km normalized 0.00058 s^-1 mM^-1.

row_label: PncB row; variable substrate Nm; fixed substrates PRPP and ATP

substrate: nicotinamide


enzyme_display_name: UniProt Q6IA69

smiles: N

enzyme: UniProt Q6IA69


enzyme_display_name: UniProt P04079

substrate_name: XMP

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8.5
Raw SKiD Env: Temp=40°C, pH=8

enzyme: UniProt P04079

substrate: XMP


substrate_name: L-glutamine

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

substrate: L-glutamine


substrate: ATP


enzyme_display_name: UniProt P49915

enzyme: UniProt P49915


organism: Clarias batrachus


substrate_name: ammonia

substrate: ammonia


substrate_name: L-Glutamine

substrate: L-Glutamine


substrate_name: Carbamoyl phosphate

smiles: NC(=O)OP(=O)(O)O

substrate: Carbamoyl phosphate


smiles: O=C=O


assay_conditions_summary: pH 7.6; 295.15 K; cofactor ATP


organism: Geobacillus stearothermophilus

substrate_name: L-Glutamine; ATP; H2O; Hydrogencarbonate

assay_conditions_summary: cofactor ATP


organism: Leishmania donovani

substrate_name: L-aspartate

substrate: L-aspartate


enzyme_display_name: NAD(+) synthase (glutamine-hydrolyzing)

organism: Acinetobacter baumannii

substrate_name: deamido-NMN

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

enzyme: NAD(+) synthase (glutamine-hydrolyzing)

substrate: deamido-NMN


substrate_name: deamido-NAD+

substrate: deamido-NAD+


substrate_name: ATP; H2O; Hydrogencarbonate; L-Glutamine

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


substrate_name: H2O; L-Glutamine; ATP; Hydrogencarbonate


substrate_name: H2O; ATP; Hydrogencarbonate; L-Glutamine


substrate_name: ATP

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP


substrate_name: Hydrogencarbonate; ATP; H2O; L-Glutamine


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature S209A to reconstruct the assayed variant sequence.


organism: Zea mays

proof_lines: pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn2

proof_lines: pH 7.6, temperature not specified in the publication, recombinant nontagged soluble isozyme ZmAsn2


proof_lines: pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn3

proof_lines: pH 7.6, temperature not specified in the publication, recombinant His-tagged isozyme ZmAsn1


substrate_name: Unknown

substrate: Unknown


organism: Mammalia

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


organism: Crithidia fasciculata

substrate_name: L-Gln

proof_lines: at 8.6% dimethyl sulfoxide plus 1.4% glycerol

proof_lines: at 2.0% dimethyl sulfoxide plus 8.0% glycerol

proof_lines: at 2.0% dimethyl sulfoxide plus 0.3% glycerol

substrate: L-Gln


proof_lines: HCO3-, at 8.6% dimethyl sulfoxide plus 1.4% glycerol


proof_lines: HCO3-, at 2.0% dimethyl sulfoxide plus 0.3% glycerol or 8.0% glycerol


organism: Escherichia coli


organism: Gallus gallus


enzyme_display_name: pyruvate carboxylase

organism: Ancylobacter novellus

enzyme: pyruvate carboxylase


substrate_name: pyruvate

substrate: pyruvate


enzyme_display_name: UniProt Q2K340

organism: Rhizobium etli

enzyme: UniProt Q2K340


substrate_name: oxaloacetate

substrate: oxaloacetate


enzyme_display_name: UniProt A0A0H3JRU9

organism: Staphylococcus aureus

enzyme: UniProt A0A0H3JRU9


enzyme_display_name: UniProt Q00955

enzyme: UniProt Q00955


enzyme_display_name: UniProt O00763

organism: Brassica napus

enzyme: UniProt O00763


organism: Helicobacter pylori

substrate_name: L-aspartyl-tRNAAsn

proof_lines: in 100 mM Na-HEPES buffer pH 7.2, 30 mM KCl, 12 mM MgCl2, at 37°C

substrate: L-aspartyl-tRNAAsn


substrate_name: Gln

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines: 37°C, pH 7.2, cosubstrate Asp-tRNAAsn + ATP, glutaminase activity

substrate: Gln


enzyme_display_name: acetyl-CoA carboxylase

substrate_name: ATP; Hydrogencarbonate; Acetyl-CoA

enzyme: acetyl-CoA carboxylase

substrate: ATP; Hydrogencarbonate; Acetyl-CoA


enzyme_display_name: hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolyzing)

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: cobyrinic acid c-monoamide

substrate: cobyrinic acid c-monoamide


enzyme: hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolyzing)


assay_conditions_summary: pH 7.7; cofactor ATP


substrate_name: cobyrinic acid

substrate: cobyrinic acid


substrate_name: glutamine

substrate: glutamine


enzyme_display_name: cobyrinate a,c-diamide synthase (glutamine-hydrolyzing)

organism: Pseudomonas denitrificans (nom. rej.)

substrate_name: hydrogenobyrinate c-monoamide

proof_lines:
pH 7.6, 30°C
or above, pH 7.6, 30°C

substrate: hydrogenobyrinate c-monoamide


substrate_name: Hydrogenobyrinate

enzyme: cobyrinate a,c-diamide synthase (glutamine-hydrolyzing)

substrate: Hydrogenobyrinate


substrate_name: L-glutamine

substrate: L-glutamine


substrate_name: (CN,aq)cobyrinate

substrate: (CN,aq)cobyrinate


substrate_name: ammonia

substrate: ammonia


enzyme_display_name: adenosylcobyric acid synthase (glutamine-hydrolyzing)

substrate_name: adenosylcobyrinic acid a,c-diamide

substrate: adenosylcobyrinic acid a,c-diamide


substrate_name: adenosylcobyrinic acid tetraamide

enzyme: adenosylcobyric acid synthase (glutamine-hydrolyzing)

substrate: adenosylcobyrinic acid tetraamide


substrate_name: ATP

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: pH 7.5, adenosylcobyrinic acid a,c-diamide as substrate

proof_lines: pH 7.5, adenosylcobyrinic acid triamide as substrate

proof_lines: pH 7.5, adenosylcobyrinic acid pentaamide as substrate

substrate: ATP


organism: Schistocerca gregaria


assay_conditions_summary: pH 8; cofactor ATP


substrate_name: propionyl-CoA

assay_conditions_summary: pH 8; cofactor CoA

substrate: propionyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


organism: Anser anser


assay_conditions_summary: cofactor CoA


substrate_name: butyryl-CoA

substrate: butyryl-CoA


organism: Acidianus brierleyi

assay_conditions_summary: pH 7.5; 343.15 K; cofactor ATP

proof_lines: with acetyl-CoA as cosubstrate, at pH 7.5 and 70°C

proof_lines: with propionyl-CoA as cosubstrate, at pH 7.5 and 70°C


assay_conditions_summary: pH 7.5; 343.15 K; cofactor CoA


organism: Metallosphaera sedula

assay_conditions_summary: pH 7.5; 338.15 K; cofactor CoA


assay_conditions_summary: pH 7.5; 338.15 K; cofactor ATP


organism: Leptosphaeria michotii

substrate_name: pyruvate

substrate: pyruvate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00968 and applied mutation signature P690Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NADH

column_label: Table 4: ATP-dependent kinetic parameters for wild-type and mutant CPS (Protein Science 2004, 13:466-475); the table prints three column groups, 'Glutamine-dependent ATPase', 'HCO3−-dependent ATPase' and 'CP-dependent ATP synthesis', each with the three column heads 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (mM-1 s-1)'. This record reads the HCO3−-dependent ATPase reaction group, row 'P690Q': Km (mM) = 0.009, kcat (s-1) = 0.09, kcat/Km (mM-1 s-1) = 10.4.

normalized_value_unit_evidence: Km: printed cell 0.009 mM; the export unit is already mM, so no unit conversion applies and the value is 0.009 mM. kcat: printed cell 0.09 s^-1; the export unit is already s^(-1), so no unit conversion applies and the value is 0.09 s^(-1). kcat/Km: printed cell 10.4 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit written in the two orders, so no unit conversion applies and the value is 10.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, HCO3−-dependent ATPase column group, row 'P690Q': column 'Km (mM)' = 0.009; column 'kcat (s-1)' = 0.09; column 'kcat/Km (mM-1 s-1)' = 10.4.

row_label: Table 4, HCO3−-dependent ATPase column group, row label 'P690Q'


substrate_name: Carbamoyl phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00968 and applied mutation signature D207A to reconstruct the assayed variant sequence.

column_label: Table 4: ATP-dependent kinetic parameters for wild-type and mutant CPS (Protein Science 2004, 13:466-475); the table prints three column groups, 'Glutamine-dependent ATPase', 'HCO3−-dependent ATPase' and 'CP-dependent ATP synthesis', each with the three column heads 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (mM-1 s-1)'. This record reads the CP-dependent ATP synthesis reaction group, row 'D207A': Km (mM) = 0.006, kcat (s-1) = 0.26, kcat/Km (mM-1 s-1) = 44.6.

normalized_value_unit_evidence: Km: printed cell 0.006 mM; the export unit is already mM, so no unit conversion applies and the value is 0.006 mM. kcat: printed cell 0.26 s^-1; the export unit is already s^(-1), so no unit conversion applies and the value is 0.26 s^(-1). kcat/Km: printed cell 44.6 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit written in the two orders, so no unit conversion applies and the value is 44.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, CP-dependent ATP synthesis column group, row 'D207A': column 'Km (mM)' = 0.006; column 'kcat (s-1)' = 0.26; column 'kcat/Km (mM-1 s-1)' = 44.6.

row_label: Table 4, CP-dependent ATP synthesis column group, row label 'D207A'

substrate: Carbamoyl phosphate


substrate_name: L-Glutamine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00968 and applied mutation signature D207N to reconstruct the assayed variant sequence.

column_label: Table 4: ATP-dependent kinetic parameters for wild-type and mutant CPS (Protein Science 2004, 13:466-475); the table prints three column groups, 'Glutamine-dependent ATPase', 'HCO3−-dependent ATPase' and 'CP-dependent ATP synthesis', each with the three column heads 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (mM-1 s-1)'. This record reads the glutamine-dependent ATPase reaction group, row 'D207N': Km (mM) = 0.020, kcat (s-1) = 1.65, kcat/Km (mM-1 s-1) = 84.2.

normalized_value_unit_evidence: Km: printed cell 0.020 mM; the export unit is already mM, so no unit conversion applies and the value is 0.02 mM. kcat: printed cell 1.65 s^-1; the export unit is already s^(-1), so no unit conversion applies and the value is 1.65 s^(-1). kcat/Km: printed cell 84.2 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit written in the two orders, so no unit conversion applies and the value is 84.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Glutamine-dependent ATPase column group, row 'D207N': column 'Km (mM)' = 0.020; column 'kcat (s-1)' = 1.65; column 'kcat/Km (mM-1 s-1)' = 84.2.

row_label: Table 4, Glutamine-dependent ATPase column group, row label 'D207N'

substrate: L-Glutamine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00968 and applied mutation signature D753A to reconstruct the assayed variant sequence.

column_label: Table 4: ATP-dependent kinetic parameters for wild-type and mutant CPS (Protein Science 2004, 13:466-475); the table prints three column groups, 'Glutamine-dependent ATPase', 'HCO3−-dependent ATPase' and 'CP-dependent ATP synthesis', each with the three column heads 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (mM-1 s-1)'. This record reads the HCO3−-dependent ATPase reaction group, row 'D753A': Km (mM) = 0.007, kcat (s-1) = 0.14, kcat/Km (mM-1 s-1) = 19.4.

normalized_value_unit_evidence: Km: printed cell 0.007 mM; the export unit is already mM, so no unit conversion applies and the value is 0.007 mM. kcat: printed cell 0.14 s^-1; the export unit is already s^(-1), so no unit conversion applies and the value is 0.14 s^(-1). kcat/Km: printed cell 19.4 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit written in the two orders, so no unit conversion applies and the value is 19.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, HCO3−-dependent ATPase column group, row 'D753A': column 'Km (mM)' = 0.007; column 'kcat (s-1)' = 0.14; column 'kcat/Km (mM-1 s-1)' = 19.4.

row_label: Table 4, HCO3−-dependent ATPase column group, row label 'D753A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00968 and applied mutation signature F755A to reconstruct the assayed variant sequence.

column_label: Table 4: ATP-dependent kinetic parameters for wild-type and mutant CPS (Protein Science 2004, 13:466-475); the table prints three column groups, 'Glutamine-dependent ATPase', 'HCO3−-dependent ATPase' and 'CP-dependent ATP synthesis', each with the three column heads 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (mM-1 s-1)'. This record reads the glutamine-dependent ATPase reaction group, row 'F755A': Km (mM) = 0.135, kcat (s-1) = 5.18, kcat/Km (mM-1 s-1) = 38.3.

normalized_value_unit_evidence: Km: printed cell 0.135 mM; the export unit is already mM, so no unit conversion applies and the value is 0.135 mM. kcat: printed cell 5.18 s^-1; the export unit is already s^(-1), so no unit conversion applies and the value is 5.18 s^(-1). kcat/Km: printed cell 38.3 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit written in the two orders, so no unit conversion applies and the value is 38.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Glutamine-dependent ATPase column group, row 'F755A': column 'Km (mM)' = 0.135; column 'kcat (s-1)' = 5.18; column 'kcat/Km (mM-1 s-1)' = 38.3.

row_label: Table 4, Glutamine-dependent ATPase column group, row label 'F755A'


column_label: Table 4: ATP-dependent kinetic parameters for wild-type and mutant CPS (Protein Science 2004, 13:466-475); the table prints three column groups, 'Glutamine-dependent ATPase', 'HCO3−-dependent ATPase' and 'CP-dependent ATP synthesis', each with the three column heads 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (mM-1 s-1)'. This record reads the HCO3−-dependent ATPase reaction group, row 'F755A': Km (mM) = 0.004, kcat (s-1) = 0.07, kcat/Km (mM-1 s-1) = 14.8.

normalized_value_unit_evidence: Km: printed cell 0.004 mM; the export unit is already mM, so no unit conversion applies and the value is 0.004 mM. kcat: printed cell 0.07 s^-1; the export unit is already s^(-1), so no unit conversion applies and the value is 0.07 s^(-1). kcat/Km: printed cell 14.8 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit written in the two orders, so no unit conversion applies and the value is 14.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, HCO3−-dependent ATPase column group, row 'F755A': column 'Km (mM)' = 0.004; column 'kcat (s-1)' = 0.07; column 'kcat/Km (mM-1 s-1)' = 14.8.

row_label: Table 4, HCO3−-dependent ATPase column group, row label 'F755A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00968 and applied mutation signature D753N to reconstruct the assayed variant sequence.

column_label: Table 4: ATP-dependent kinetic parameters for wild-type and mutant CPS (Protein Science 2004, 13:466-475); the table prints three column groups, 'Glutamine-dependent ATPase', 'HCO3−-dependent ATPase' and 'CP-dependent ATP synthesis', each with the three column heads 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (mM-1 s-1)'. This record reads the glutamine-dependent ATPase reaction group, row 'D753N': Km (mM) = 0.121, kcat (s-1) = 5.60, kcat/Km (mM-1 s-1) = 46.2.

normalized_value_unit_evidence: Km: printed cell 0.121 mM; the export unit is already mM, so no unit conversion applies and the value is 0.121 mM. kcat: printed cell 5.60 s^-1; the export unit is already s^(-1), so no unit conversion applies and the value is 5.6 s^(-1). kcat/Km: printed cell 46.2 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit written in the two orders, so no unit conversion applies and the value is 46.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Glutamine-dependent ATPase column group, row 'D753N': column 'Km (mM)' = 0.121; column 'kcat (s-1)' = 5.60; column 'kcat/Km (mM-1 s-1)' = 46.2.

row_label: Table 4, Glutamine-dependent ATPase column group, row label 'D753N'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00968 and applied mutation signature A144Q/D207A to reconstruct the assayed variant sequence.

column_label: Table 4: ATP-dependent kinetic parameters for wild-type and mutant CPS (Protein Science 2004, 13:466-475); the table prints three column groups, 'Glutamine-dependent ATPase', 'HCO3−-dependent ATPase' and 'CP-dependent ATP synthesis', each with the three column heads 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (mM-1 s-1)'. This record reads the glutamine-dependent ATPase reaction group, row 'A144Q/D207A': Km (mM) = 0.154, kcat (s-1) = 1.70, kcat/Km (mM-1 s-1) = 11.0.

normalized_value_unit_evidence: Km: printed cell 0.154 mM; the export unit is already mM, so no unit conversion applies and the value is 0.154 mM. kcat: printed cell 1.70 s^-1; the export unit is already s^(-1), so no unit conversion applies and the value is 1.7 s^(-1). kcat/Km: printed cell 11.0 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit written in the two orders, so no unit conversion applies and the value is 11.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Glutamine-dependent ATPase column group, row 'A144Q/D207A': column 'Km (mM)' = 0.154; column 'kcat (s-1)' = 1.70; column 'kcat/Km (mM-1 s-1)' = 11.0.

row_label: Table 4, Glutamine-dependent ATPase column group, row label 'A144Q/D207A'


organism: Streptomyces coelicolor

assay_conditions_summary: pH 7.6; 303.15 K; cofactor CoA

proof_lines: wild type subunit AccB, in 100 mM potassium phosphate, pH 7.6, at 30°C


organism: Acinetobacter baumannii

assay_conditions_summary: pH 8; 293.15 K; cofactor CoA

proof_lines:
co-substrate: ATP, HCO3-, pH 8, 20°C
pH 8, 20°C


assay_conditions_summary: pH 8; 293.15 K; cofactor ATP


organism: Bacillus thermodenitrificans

substrate_name: ATP; Hydrogencarbonate; Pyruvate

assay_conditions_summary: cofactor ATP

substrate: ATP; Hydrogencarbonate; Pyruvate


substrate_name: Gln

substrate: Gln


organism: Euglena gracilis


organism: Bacillus subtilis (strain 168)

substrate_name: ATP (FGAM synthase activity at pH 7.2 and 37 degrees Celsius)

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: kcat is 2.49 sec(-1) for FGAM synthase activity (at pH 7.2 and 37 degrees Celsius). kcat is 0.002 sec(-1) for glutaminase activity (at pH 7.2 and 37 degrees Celsius).


substrate_name: FGAR (FGAM synthase activity at pH 7.2 and 37 degrees Celsius)


substrate_name: glutamine (FGAM synthase activity at pH 7.2 and 37 degrees Celsius)


proof_lines: kcat is 2.49 sec(-1) for FGAM synthase activity with FGAR as substrate (at pH 7.2 and 37 degrees Celsius). kcat is 0.044 sec(-1) for glutamine amidotransferase activity with NH3 as substrate (at pH 7.2 and 37 degrees Celsius).

substrate: ATP (FGAM synthase activity at pH 7.2 and 37 degrees Celsius)


substrate: FGAR (FGAM synthase activity at pH 7.2 and 37 degrees Celsius)


substrate: glutamine (FGAM synthase activity at pH 7.2 and 37 degrees Celsius)


substrate_name: NH3 (Glutamine amidotransferase activity at pH 7.2 and 37 degrees Celsius)


substrate_name: ATP (at pH 7.2 and 37 degrees Celsius)

proof_lines: kcat is 2.49 sec(-1) for FGAM synthase activity (at pH 7.2 and 37 degrees Celsius).

substrate: ATP (at pH 7.2 and 37 degrees Celsius)


substrate_name: FGAR (at pH 7.2 and 37 degrees Celsius)

substrate: FGAR (at pH 7.2 and 37 degrees Celsius)


substrate_name: glutamine (at pH 7.2 and 37 degrees Celsius)


organism: Escherichia coli

column_label: Table 4: ATP-dependent kinetic parameters for wild-type and mutant CPS (Protein Science 2004, 13:466-475); the table prints three column groups, 'Glutamine-dependent ATPase', 'HCO3−-dependent ATPase' and 'CP-dependent ATP synthesis', each with the three column heads 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (mM-1 s-1)'. This record reads the CP-dependent ATP synthesis reaction group, row 'P690Q': Km (mM) = 0.039, kcat (s-1) = 0.28, kcat/Km (mM-1 s-1) = 7.1.

normalized_value_unit_evidence: Km: printed cell 0.039 mM; the export unit is already mM, so no unit conversion applies and the value is 0.039 mM. kcat: printed cell 0.28 s^-1; the export unit is already s^(-1), so no unit conversion applies and the value is 0.28 s^(-1). kcat/Km: printed cell 7.1 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit written in the two orders, so no unit conversion applies and the value is 7.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, CP-dependent ATP synthesis column group, row 'P690Q': column 'Km (mM)' = 0.039; column 'kcat (s-1)' = 0.28; column 'kcat/Km (mM-1 s-1)' = 7.1.

row_label: Table 4, CP-dependent ATP synthesis column group, row label 'P690Q'


sequence_variant_note: Mutation signature A144Q matches the mutant residue at offset +0 and the reference residue at offset +16; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


column_label: Table 4: ATP-dependent kinetic parameters for wild-type and mutant CPS (Protein Science 2004, 13:466-475); the table prints three column groups, 'Glutamine-dependent ATPase', 'HCO3−-dependent ATPase' and 'CP-dependent ATP synthesis', each with the three column heads 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (mM-1 s-1)'. This record reads the glutamine-dependent ATPase reaction group, row 'P690Q': Km (mM) = 0.383, kcat (s-1) = 9.01, kcat/Km (mM-1 s-1) = 23.5.

normalized_value_unit_evidence: Km: printed cell 0.383 mM; the export unit is already mM, so no unit conversion applies and the value is 0.383 mM. kcat: printed cell 9.01 s^-1; the export unit is already s^(-1), so no unit conversion applies and the value is 9.01 s^(-1). kcat/Km: printed cell 23.5 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit written in the two orders, so no unit conversion applies and the value is 23.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Glutamine-dependent ATPase column group, row 'P690Q': column 'Km (mM)' = 0.383; column 'kcat (s-1)' = 9.01; column 'kcat/Km (mM-1 s-1)' = 23.5.

row_label: Table 4, Glutamine-dependent ATPase column group, row label 'P690Q'


sequence_variant_note: Mutation signature D753A matches the mutant residue at offset +0 and the reference residue at offset +16; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00968 and applied mutation signature I211S to reconstruct the assayed variant sequence.

column_label: Table 4: ATP-dependent kinetic parameters for wild-type and mutant CPS (Protein Science 2004, 13:466-475); the table prints three column groups, 'Glutamine-dependent ATPase', 'HCO3−-dependent ATPase' and 'CP-dependent ATP synthesis', each with the three column heads 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (mM-1 s-1)'. This record reads the CP-dependent ATP synthesis reaction group, row 'I211S': Km (mM) = 0.011, kcat (s-1) = 0.48, kcat/Km (mM-1 s-1) = 44.0.

normalized_value_unit_evidence: Km: printed cell 0.011 mM; the export unit is already mM, so no unit conversion applies and the value is 0.011 mM. kcat: printed cell 0.48 s^-1; the export unit is already s^(-1), so no unit conversion applies and the value is 0.48 s^(-1). kcat/Km: printed cell 44.0 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit written in the two orders, so no unit conversion applies and the value is 44.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, CP-dependent ATP synthesis column group, row 'I211S': column 'Km (mM)' = 0.011; column 'kcat (s-1)' = 0.48; column 'kcat/Km (mM-1 s-1)' = 44.0.

row_label: Table 4, CP-dependent ATP synthesis column group, row label 'I211S'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00968 and applied mutation signature S209A to reconstruct the assayed variant sequence.

column_label: Table 4: ATP-dependent kinetic parameters for wild-type and mutant CPS (Protein Science 2004, 13:466-475); the table prints three column groups, 'Glutamine-dependent ATPase', 'HCO3−-dependent ATPase' and 'CP-dependent ATP synthesis', each with the three column heads 'Km (mM)', 'kcat (s-1)' and 'kcat/Km (mM-1 s-1)'. This record reads the glutamine-dependent ATPase reaction group, row 'S209A': Km (mM) = 0.031, kcat (s-1) = 2.43, kcat/Km (mM-1 s-1) = 78.0.

normalized_value_unit_evidence: Km: printed cell 0.031 mM; the export unit is already mM, so no unit conversion applies and the value is 0.031 mM. kcat: printed cell 2.43 s^-1; the export unit is already s^(-1), so no unit conversion applies and the value is 2.43 s^(-1). kcat/Km: printed cell 78.0 mM^-1 s^-1; mM^-1 s^-1 and s^(-1)*mM^(-1) are the same unit written in the two orders, so no unit conversion applies and the value is 78.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, Glutamine-dependent ATPase column group, row 'S209A': column 'Km (mM)' = 0.031; column 'kcat (s-1)' = 2.43; column 'kcat/Km (mM-1 s-1)' = 78.0.

row_label: Table 4, Glutamine-dependent ATPase column group, row label 'S209A'


organism: Homo sapiens

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

sequence_source: multiple

assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP

proof_lines:
37°C, pH 7.8, liver enzyme
37°C, pH 7.8, recombinant enzyme
Raw SKiD Env: Temp=37°C, pH=7.8

source_databases_merged: brenda skid


proof_lines:
37°C, pH 7.8, recombinant enzyme
37°C, pH 7.8, liver enzyme
Raw SKiD Env: Temp=37°C, pH=7.8


organism: Drosophila melanogaster

substrate_name: L-glutamine

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

substrate: L-glutamine


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


organism: Leishmania infantum

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

column_label: Table 1. Kinetic parameters of LiAS-A for aspartate, ATP, ammonia and glutamine. Table 1, substrate row 'Ammonia': column 'Km (mM)' = 1.12 +/- 0.16; column 'kcat (s^-1)' = 7.46 +/- 0.33; column 'Ksp (kcat/Km) (M^-1 s^-1)' = 6.66 x 10^3.

normalized_value_unit_evidence: kcat: the printed Table 1 cell is 7.46 +/- 0.33 s^-1, already the export unit; the base value is 7.46 s^(-1) and the exported value is 4.18 s^(-1). Km: the printed Table 1 cell is 1.12 +/- 0.16 mM, already the export unit; the base value is 1.12 mM and the exported value is 1.12 mM. kcat/Km: the printed Table 1 Ksp cell is 6.66 x 10^3 M^-1 s^-1, the paper's own specificity constant per its table footnote; 6660.0 / 1000 = 6.66 s^(-1)*mM^(-1); the exported value is 3.7321428571428563 s^(-1)*mM^(-1). The cited Table 1 row prints no fourth numeric column; the plus-or-minus figures are standard deviations of the same three cells, not separate metrics.

row_label: Table 1, substrate row 'Ammonia'


substrate_name: ATP

column_label: Table 1. Kinetic parameters of LiAS-A for aspartate, ATP, ammonia and glutamine. Table 1, substrate row 'ATP': column 'Km (mM)' = 1.47 +/- 0.04; column 'kcat (s^-1)' = 4.18 +/- 0.02; column 'Ksp (kcat/Km) (M^-1 s^-1)' = 2.84 x 10^3.

normalized_value_unit_evidence: kcat: the printed Table 1 cell is 4.18 +/- 0.02 s^-1, already the export unit; the base value is 4.18 s^(-1) and the exported value is 7.46 s^(-1). Km: the printed Table 1 cell is 1.47 +/- 0.04 mM, already the export unit; the base value is 1.47 mM and the exported value is 1.47 mM. kcat/Km: the printed Table 1 Ksp cell is 2.84 x 10^3 M^-1 s^-1, the paper's own specificity constant per its table footnote; 2840.0 / 1000 = 2.84 s^(-1)*mM^(-1); the exported value is 5.074829931972789 s^(-1)*mM^(-1). The cited Table 1 row prints no fourth numeric column; the plus-or-minus figures are standard deviations of the same three cells, not separate metrics.

row_label: Table 1, substrate row 'ATP'


substrate_name: L-aspartate

substrate: L-aspartate


organism: Mycobacterium tuberculosis

proof_lines: kcat is 0.55 sec(-1) for glutamine-dependent activity. kcat is 2.8 sec(-1) for ammonia-dependent activity.

source_databases_merged: skid uniprot


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

substrate_name: cobyrinate

substrate: cobyrinate


substrate: ATP


substrate_name: glutamine

substrate: glutamine


substrate_name: ammonia

substrate: ammonia


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: deamido-NAD(+) (with glutamine as a nitrogen source)


organism: Methanosarcina barkeri (strain Fusaro / DSM 804)

proof_lines: kcat is 1.03 min(-1) for ATP as substrate. kcat is 0.78 min(-1) for L-glutamine as substrate.


enzyme_display_name: GMP synthase (glutamine-hydrolyzing)

organism: Plasmodium falciparum

substrate_name: XMP

assay_conditions_summary: pH 8.5; cofactor ATP

proof_lines: kcat is 0.43 sec(-1) for XMP as substrate (at pH 8.5 and 25 degrees Celsius) (PubMed:17868038). kcat is 44 min(-1) for XMP as substrate (at pH 8.5 and 25 degrees Celsius) (PubMed:26592566). kcat is 0.74 sec(-1) for XMP as substrate (at pH 8

source_databases_merged: brenda uniprot

enzyme: GMP synthase (glutamine-hydrolyzing)

substrate: XMP


organism: Geobacillus thermodenitrificans

substrate_name: pyruvate

sequence_variant_note: Mutation signature D762N references residue 762, which is outside the resolved sequence length.

substrate: pyruvate


sequence_variant_note: Mutation signature D762E references residue 762, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature K712R references residue 712, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature E576D references residue 576, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature E592Q references residue 592, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature D713E references residue 713, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature D713N references residue 713, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature D649N references residue 649, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature E576Q references residue 576, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature D543E references residue 543, which is outside the resolved sequence length.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature C175S with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

assay_conditions_summary: 310.15 K; cofactor ATP


substrate_name: deamido-NAD+

assay_conditions_summary: 310.15 K; cofactor NAD+

substrate: deamido-NAD+


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

substrate_name: XMP (at pH 7.5 and at 40 degrees Celsius)

assay_conditions_summary: pH 7.5; cofactor ATP

column_label: Table 1: Comparison of kinetic parameters of GMP synthase from different organisms row C. neoformans: Km (XMP) raw_value=65.9 +/- 13 raw_unit=uM; reference=This work. Km normalized_value=0.0659 normalized_unit=mM after uM-to-mM conversion; CatLog value=0.0659 mM.

row_label: C. neoformans


substrate_name: ATP (at pH 7.5 and at 40 degrees Celsius)

column_label: Table 1: Comparison of kinetic parameters of GMP synthase from different organisms row C. neoformans: Km (ATP) raw_value=77.5 +/- 6 raw_unit=uM; reference=This work. Km normalized_value=0.0775 normalized_unit=mM after uM-to-mM conversion; CatLog value=0.0775 mM.


substrate_name: glutamine (at pH 7.5 and at 40 degrees Celsius)

column_label: Table 1: Comparison of kinetic parameters of GMP synthase from different organisms row C. neoformans: Km (Gln) raw_value=1130 +/- 162 raw_unit=uM; reference=This work. Km normalized_value=1.13 normalized_unit=mM after uM-to-mM conversion; CatLog value=1.13 mM.


enzyme_display_name: lipid II isoglutaminyl synthase (glutamine-hydrolyzing)

organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

substrate_name: lipid II

proof_lines: kcat is 4 sec(-1) with lipid II as substrate.

substrate: lipid II


enzyme: lipid II isoglutaminyl synthase (glutamine-hydrolyzing)


organism: Petroselinum crispum

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


substrate_name: acetyl-CoA

assay_conditions_summary: cofactor CoA

substrate: acetyl-CoA


proof_lines: wild-type enzyme after retroviral expression


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A610T to reconstruct the assayed variant sequence.

proof_lines: A610T mutant after retroviral expression


column_label: Public PMC results paragraph reports glutamine variable-substrate Km 46 uM with ATP fixed at 0.5 mM.

normalized_value_unit_evidence: Km normalized 0.046 mM.

raw_value_unit_evidence: Km raw 46 uM for glutamine.

row_label: glutamine varied; ATP fixed at 0.5 mM

table_label: Results prose, CfbE kinetic parameters paragraph


column_label: Public PMC results paragraph reports ATP variable-substrate Km 28 uM with glutamine fixed at 1 mM.

normalized_value_unit_evidence: Km normalized 0.028 mM.

raw_value_unit_evidence: Km raw 28 uM for ATP.

row_label: ATP varied; glutamine fixed at 1 mM


organism: Pseudomonas denitrificans (nom. rej.)

proof_lines: pH 7.5, 20°C, adenosyl-cobyrinic acid triamide as substrate

proof_lines: pH 7.5, 20°C, adenosyl-cobyrinic acid a,c-diamide as substrate


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

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

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: kcat is 0.39 sec(-1) for FGAM synthase activity with NH(4)Cl as substrate (at pH 8 and 37 degrees Celsius). kcat is 0.40 sec(-1) for FGAM synthase activity with FGAR as substrate (at pH 8 and 37 degrees Celsius). kcat is 0.41 sec(-1) for FG

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


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

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


proof_lines: kcat is 2.3 sec(-1) for XMP. kcat is 2.39 sec(-1) for ATP. kcat is 3.05 sec(-1) for glutamine.


proof_lines: pH 8, 30°C, ATP-cleavage in absence of pyruvate


organism: Gallus gallus

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

assay_conditions_summary: pH 7.8; cofactor ATP

proof_lines: presence of 2' -3' -O-(2,4,6-trinitrophenyl) adenosine 5' -diphosphate, pH 7.8, 30°C

proof_lines: presence of 2' -3' -O-(2,4,6-trinitrophenyl) adenosine 5' -triphosphate, pH 7.8, 30°C


organism: Mus musculus

substrate_name: Gln

substrate: Gln


organism: Saccharomyces cerevisiae

substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y83A to reconstruct the assayed variant sequence.

proof_lines: mutant Y83A, pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q608R to reconstruct the assayed variant sequence.

proof_lines: mutant Q608R, pH 7.5, temperature not specified in the publication


organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)

substrate_name: magnesium (at pH 7.5 and at 40 degrees Celsius)

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

smiles: [Mg]

proof_lines: kcat is 1657 sec(-1) for ATP (at pH 7.5 and at 40 degrees Celsius).


organism: Aspergillus nidulans

assay_conditions_summary: pH 7.8; 303.15 K; cofactor CoA

proof_lines: wild-type, presence of acetyl-CoA, pH 7.8, 30°C

proof_lines: hybrid tetramers between wild-type and Rhizobiium etli mutant E218A, pH 7.8, 30°C


substrate_name: oxaloacetate

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines: wild-type, presence of acetyl-CoA, pH 7.5, 25°C

substrate: oxaloacetate


proof_lines: pH 7.5, 20°C, adenosyl-cobyrinic acid pentaamide as substrate


proof_lines: pH 7.8, 30°C, absence of acetyl CoA, 0.24 mM Mg2+

proof_lines: pH 7.8, 30°C, absence of acetyl CoA, 10 mM Mg2+

proof_lines: pH 7.8, 30°C, absence of acetyl CoA, 1 mM Mg2+


proof_lines:
MgATP2-
with 10 mM free Mg2+
with 2 mM free Mg2+


organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)

substrate_name: deamido-NAD

proof_lines: kcat is 0.57 sec(-1) with deamido-NAD as substrate. kcat is 0.0032 sec(-1) with nicotinate mononucleotide as substrate.

substrate: deamido-NAD


substrate_name: nicotinate mononucleotide

substrate: nicotinate mononucleotide


substrate_name: hydrogenobyrinic acid c-monoamide

substrate: hydrogenobyrinic acid c-monoamide


organism: Homo sapiens

substrate_name: Hydrogencarbonate; Pyruvate; ATP

substrate: Hydrogencarbonate; Pyruvate; ATP


substrate_name: Pyruvate; ATP; Hydrogencarbonate

substrate: Pyruvate; ATP; Hydrogencarbonate


substrate_name: Hydrogencarbonate; Acetyl-CoA; ATP

substrate: Hydrogencarbonate; Acetyl-CoA; ATP


substrate_name: ATP; Hydrogencarbonate; Acetyl-CoA

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

substrate: ATP; Hydrogencarbonate; Acetyl-CoA


organism: Bacillus sp. (in: firmicutes)

proof_lines: with saturating concentrations of the activator acetyl-CoA


organism: Rattus norvegicus

substrate_name: Hydrogencarbonate; ATP; Acetyl-CoA

substrate: Hydrogencarbonate; ATP; Acetyl-CoA


organism: Bacillus thermodenitrificans

substrate_name: Pyruvate; Hydrogencarbonate; ATP

assay_conditions_summary: pH 7.8; 303.15 K; cofactor ATP

proof_lines:
pH 7.8, 30°C, in absence of acetyl-CoA
pH 7.8, 30°C, in presence of acetyl-CoA

substrate: Pyruvate; Hydrogencarbonate; ATP


organism: Methanocaldococcus jannaschii

substrate_name: Unknown

substrate: Unknown


organism: Elaeis guineensis


organism: Mycosarcoma maydis


substrate_name: ATP; L-Glutamine; H2O; Deamino-NAD+

assay_conditions_summary: cofactor NAD+

substrate: ATP; L-Glutamine; H2O; Deamino-NAD+


organism: Methanosarcina barkeri

substrate_name: L-Glutamine; Nickel-sirohydrochlorin; H2O; ATP


substrate_name: ATP; XMP; H2O; L-Glutamine

substrate: ATP; XMP; H2O; L-Glutamine


organism: Escherichia coli

substrate_name: ATP; H2O; L-Glutamine; 5'-Phosphoribosyl-N-formylglycinamide


organism: Pseudomonas denitrificans

substrate_name: L-Glutamine; ATP; Hydrogenobyrinate c-monoamide; H2O

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


organism: Geobacillus thermodenitrificans

substrate_name: biotin

proof_lines:
pH 7.8, 30°C, in presence of acetyl-CoA
pH 7.8, 30°C, in absence of acetyl-CoA

substrate: biotin


organism: Rhizobium etli

substrate_name: ADP

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ADP

substrate: ADP


substrate_name: ATP

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

substrate: ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T882A to reconstruct the assayed variant sequence.


substrate_name: pyruvate

substrate: pyruvate


organism: Aspergillus fumigatus

assay_conditions_summary: pH 7.5; 313.15 K; cofactor ATP


substrate_name: L-glutamine

substrate: L-glutamine


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C249A to reconstruct the assayed variant sequence.


substrate_name: hydrogencarbonate

substrate: hydrogencarbonate


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


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

assay_conditions_summary: cofactor ATP

proof_lines: kcat is 2.3 sec(-1) for XMP. kcat is 2.39 sec(-1) for ATP. kcat is 3.05 sec(-1) for glutamine.


organism: Plasmodium falciparum

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

proof_lines: 37°C, pH 8.5, with ATP as variable substrate

proof_lines: 37°C, pH 8.5, with XMP as variable substrate


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

substrate_name: NH(4)Cl (at pH 8 and 37 degrees Celsius)

proof_lines: kcat is 0.39 sec(-1) for FGAM synthase activity with NH(4)Cl as substrate (at pH 8 and 37 degrees Celsius). kcat is 0.40 sec(-1) for FGAM synthase activity with FGAR as substrate (at pH 8 and 37 degrees Celsius). kcat is 0.41 sec(-1) for FG


organism: Mesocricetus auratus

substrate_name: Hydrogencarbonate; L-Glutamine; H2O; ATP


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Bacillus subtilis (strain 168)


substrate_name: acetyl-CoA

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

substrate: acetyl-CoA


organism: Tenebrio molitor


organism: Thermotoga maritima

assay_conditions_summary: pH 8.3; cofactor ATP

column_label: Primary PDF page 3 (journal p. 1650), Table 1 columns Assay, Variable substrate, Fixed substrates, Km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1); NAD+/ATP/Gln, NaAD+ row

row_label: Assay NAD+; variable substrate ATP; fixed substrates Gln and NaAD+

table_label: Table 1 - Steady-state kinetic parameters of the NAD+ synthetaseTM catalyzed reactions


substrate_name: deamido-NAD+

assay_conditions_summary: pH 8.3; cofactor NAD+

column_label: Primary PDF page 3 (journal p. 1650), Table 1 columns Assay, Variable substrate, Fixed substrates, Km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1); NAD+/NaAD+/Gln, ATP row

row_label: Assay NAD+; variable substrate NaAD+ (nicotinic acid adenine dinucleotide, deamido-NAD+); fixed substrates Gln and ATP

substrate: deamido-NAD+


column_label: Primary PDF page 3 (journal p. 1650), Table 1 columns Assay, Variable substrate, Fixed substrates, Km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1); NAD+/NH3/NaAD+, ATP row

row_label: Assay NAD+; variable substrate NH3; fixed substrates NaAD+ and ATP


substrate_name: L-Gln

column_label: Primary PDF page 3 (journal p. 1650), Table 1 columns Assay, Variable substrate, Fixed substrates, Km (mM), kcat (s^-1), kcat/Km (s^-1 mM^-1); NAD+/Gln/NaAD+, ATP row

row_label: Assay NAD+; variable substrate Gln; fixed substrates NaAD+ and ATP

substrate: L-Gln


organism: Mus musculus

substrate_name: XMP

substrate: XMP


substrate_name: Gln

substrate: Gln


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E383A to reconstruct the assayed variant sequence.

column_label: Table 2 row E383A gives K m, Gln 3.2 mM, k cat 3.2 s^-1, and k cat/Km 1.0 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=3.2 normalized_unit=mM; kcat normalized_value=3.2 normalized_unit=s^-1; kcat/Km normalized_value=1.0 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=3.2 mM; kcat raw_value=3.2 s^-1; kcat/Km raw_value=1.0 x 10^3 M^-1 s^-1

row_label: E. coli GMPS E383A mutant / L-glutamine

table_label: Official PMC full-text Table 2: GMPS Kinetic Parameters


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04079 and applied mutation signature H186A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

column_label: Official NCBI Table 2 row H186A, glutamine column group.

normalized_value_unit_evidence: Km 80 mM; kcat 16 s^-1; printed kcat/Km 0.21 s^-1 mM^-1; exported derived ratio 0.2.

table_label: Table 2: E. coli GMPS Synthetase Kinetic Parameters


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H186A/E383A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

column_label: Official NCBI Table 2 row H186A/E383A, glutamine column group.

normalized_value_unit_evidence: Km 99 mM; kcat 4.8 s^-1; printed kcat/Km 0.049 s^-1 mM^-1; exported derived ratio 0.048484848484848485.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H186E/E383H with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

column_label: Official NCBI Table 2 row H186E/E383H, glutamine column group.

normalized_value_unit_evidence: Km 67 mM; kcat 4.7 s^-1; printed kcat/Km 0.070 s^-1 mM^-1; exported derived ratio 0.07014925373134329.


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


column_label: Official NCBI Table 2 row E383A, XMP(NH4+) column group.

normalized_value_unit_evidence: Km 0.056 mM; kcat 7.0 s^-1; printed kcat/Km 120 s^-1 mM^-1; exported derived ratio 125.


column_label: Official NCBI Table 2 row H186A, XMP(NH4+) column group.

normalized_value_unit_evidence: Km 0.050 mM; kcat 15.6 s^-1; printed kcat/Km 310 s^-1 mM^-1; exported derived ratio 312.


column_label: Official NCBI Table 2 row H186A/E383A, XMP(NH4+) column group.

normalized_value_unit_evidence: Km 0.074 mM; kcat 9.0 s^-1; printed kcat/Km 120 s^-1 mM^-1; exported derived ratio 121.62162162162163.


column_label: Official NCBI Table 2 row H186E/E383H, XMP(NH4+) column group.

normalized_value_unit_evidence: Km 0.050 mM; kcat 6.1 s^-1; printed kcat/Km 120 s^-1 mM^-1; exported derived ratio 121.99999999999999.


column_label: Official NCBI Table 2 row Wild Type, XMP(Gln) column group.

normalized_value_unit_evidence: Km 0.053 mM; kcat 23 s^-1; printed kcat/Km 430 s^-1 mM^-1; exported derived ratio 433.9622641509434.

row_label: Wild Type


organism: Sinorhizobium sp

substrate_name: hydrogenobyrinate

substrate: hydrogenobyrinate


substrate_name: glutamine

substrate: glutamine


substrate_name: ammonia

substrate: ammonia


substrate_name: cobyrinate

substrate: cobyrinate


organism: Pseudomonas denitrificans (nom. rej.)

substrate_name: Hydrogenobyrinic acid

assay_conditions_summary: pH 7.6; cofactor ATP

column_label: The article abstract/prose states that hydrogenobyrinic acid has Km = 0.41 microM.

raw_value_unit_evidence: Km = 0.41 microM

row_label: Hydrogenobyrinic acid

table_label: Abstract/prose page 6239

substrate: Hydrogenobyrinic acid


substrate_name: (CN,aq)cobyrinic acid c-monoamide

column_label: The article abstract/prose states that Km values for (CN,aq)cobyrinic acid, (aq)2cobyrinic acid, and (CN,aq)cobyrinic acid c-monoamide were 160, >=250, and 71 microM, respectively.

raw_value_unit_evidence: Km = 71 microM

row_label: (CN,aq)cobyrinic acid c-monoamide

substrate: (CN,aq)cobyrinic acid c-monoamide


substrate_name: (CN,aq)cobyrinic acid

raw_value_unit_evidence: Km = 160 microM

row_label: (CN,aq)cobyrinic acid

substrate: (CN,aq)cobyrinic acid


organism: Salmonella phage PMBT28

substrate_name: dGMP

substrate: dGMP


substrate_name: ATP

substrate: ATP


substrate_name: Asp

substrate: Asp


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R427K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R427S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R472K with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R472S with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


organism: Acinetobacter phage SH-Ab 15497

assay_conditions_summary: pH 8.5; cofactor ATP

column_label: The extracted supplement text shows Table S3 column dGMP and row ApPurZ with KM 5.1+/-0.7 uM, matching expected dGMP Km 0.0051 mM after uM-to-mM normalization.

raw_value_unit_evidence: Km raw_value=5.1 raw_unit=uM

row_label: ApPurZ

table_label: Table S3. Kinetic parameters of PurZs


column_label: The extracted supplement text shows Table S3 column ATP and row ApPurZ with KM 21.1+/-3.8 uM, matching expected ATP Km 0.0211 mM after uM-to-mM normalization.

raw_value_unit_evidence: Km raw_value=21.1 raw_unit=uM


column_label: The extracted supplement text shows Table S3 column Asp and row ApPurZ with KM 90.9+/-9.9 uM, matching expected Asp Km 0.0909 mM after uM-to-mM normalization.

raw_value_unit_evidence: Km raw_value=90.9 raw_unit=uM


organism: Leishmania infantum

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP


substrate_name: L-glutamine

column_label: PMC4714757 Table 1 row Glutamine dependent activity / Glutamine columns Km, kcat, and Ksp report 1.71 +/- 0.28 mM, 4.51 +/- 0.19 s^-1, and 2.64 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=4.51 s^-1; Km normalized_value=1.71 mM; paper-rounded kcat/Km normalized_value=2.64 s^-1 mM^-1. CatLog stores computed kcat/Km=2.6374269005847952 from kcat and Km cells.

raw_value_unit_evidence: Table 1 reports Glutamine dependent activity / Glutamine: Km raw_value=1.71 mM, kcat raw_value=4.51 s^-1, Ksp raw_value=2.64 x 10^3 M^-1 s^-1.

table_label: PMC4714757 Table 1

substrate: L-glutamine


substrate_name: L-Aspartate

substrate: L-Aspartate


organism: Methanocaldococcus jannaschii

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

assay_conditions_summary: pH 7


assay_conditions_summary: pH 7; cofactor ATP


organism: Rattus norvegicus


organism: Escherichia coli (strain K12)


substrate_name: aspartate (when assaying the ammonia-dependent synthetase reaction)


substrate_name: ATP (when assaying the glutamine-dependent synthetase reaction)


substrate_name: glutamine (when assaying the glutamine-dependent synthetase reaction)


organism: Homo sapiens

assay_conditions_summary: 310.15 K; cofactor ATP

column_label: Table I row NADsyn1 / ATP, column Km (mM), reports 0.089 +/- 0.023.

row_label: NADsyn1 / ATP

table_label: Table I. Kinetic parameters in NAD synthetase reactions catalyzed by the wild-type and mutant NADsyn1 and NADsyn2, PMID 12547821


substrate_name: deamido-NAD+

assay_conditions_summary: 310.15 K; cofactor NAD+


column_label: Table I row NADsyn1 / Glutamine, column Km (mM), reports 1.44 +/- 0.17.

raw_value_unit_evidence: NADsyn1 Glutamine Km 1.44 +/- 0.17 mM

row_label: NADsyn1 / Glutamine


substrate_name: ammonium

column_label: Table I row NADsyn1 / NH4Cl, column Km (mM), reports 13.1 +/- 1.2; NH4Cl is the ammonium donor for the package ammonium row.

raw_value_unit_evidence: NADsyn1 NH4Cl Km 13.1 +/- 1.2 mM

row_label: NADsyn1 / NH4Cl

substrate: ammonium


substrate_name: hydrogencarbonate

substrate: hydrogencarbonate


column_label: The abstract reports apparent Michaelis constants at pH 7.5 of 1.25 mM for glutamine and 75 mM for NH4Cl.

raw_value_unit_evidence: Km raw_value=75 mM raw_unit=mM

row_label: Prose segment: NH4Cl Km

table_label: PubMed PMID 206535 abstract


substrate_name: glutamine

raw_value_unit_evidence: Km raw_value=1.25 mM raw_unit=mM

row_label: Prose segment: glutamine Km


substrate_name: glutamine (at pH 7.25 and 37 degrees Celsius)


substrate_name: ATP (at pH 7.25 and 37 degrees Celsius)

substrate: ATP (at pH 7.25 and 37 degrees Celsius)


substrate_name: FGAR (formylglycinamide ribonucleotide at pH 7.25 and 37 degrees Celsius)


substrate_name: pyruvate

substrate: pyruvate


organism: Arthrobacter globiformis

assay_conditions_summary: pH 7.8; cofactor ATP

column_label: Printed page 449, Results prose: The apparent Km values were HCO3-, 0.33 mM; MgATP, 0.08 mM; Mg2+, 0.70 mM; pyruvate, 1.86 mM.

normalized_value_unit_evidence: MgATP Km normalized_value=0.08 normalized_unit=mM.

raw_value_unit_evidence: Apparent Km values sentence: MgATP raw_value=0.08 raw_unit=mM.

row_label: Apparent Km values sentence / MgATP

table_label: Results prose, Requirements of the A. globiformis Pyruvate Carboxylase Reaction, printed page 449


assay_conditions_summary: pH 7.8; cofactor NADH

normalized_value_unit_evidence: Pyruvate Km normalized_value=1.86 normalized_unit=mM.

raw_value_unit_evidence: Apparent Km values sentence: pyruvate raw_value=1.86 raw_unit=mM.

row_label: Apparent Km values sentence / pyruvate


enzyme_display_name: UniProt Q9X4K7

organism: Streptomyces coelicolor

substrate_name: propionyl-CoA

enzyme: UniProt Q9X4K7

substrate: propionyl-CoA


substrate_name: butyryl-CoA

substrate: butyryl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: ATP

assay_conditions_summary: pH 8; cofactor ATP

column_label: Page 490 abstract Km sentence; metric=Km; segment=ATP; raw value=1.5 x 10^-3 M; normalized value=1.5 mM.

raw_value_unit_evidence: Page 490 abstract gives ATP Km = 1.5 x 10^-3 M and ammonium chloride Km = 7.5 x 10^-3 M.

row_label: ATP

table_label: Abstract, page 490


column_label: Page 490 abstract Km sentence; metric=Km; segment=ammonium chloride; raw value=7.5 x 10^-3 M; normalized value=7.5 mM.

row_label: ammonium chloride nitrogen donor (export substrate normalized as NH4+)


organism: Vibrio phage phiVC8

substrate_name: dGMP


substrate_name: Asp


organism: Klebsiella aerogenes


substrate_name: Gln

substrate: Gln


organism: Cyclotella cryptica

column_label: Abstract metric sentence maps MgATP to 65 uM Km

raw_value_unit_evidence: Km raw_value=65 raw_unit=uM

row_label: MgATP item in ordered Km sentence

table_label: PMID 16667268 OUP/PubMed abstract


assay_conditions_summary: cofactor CoA

column_label: Abstract metric sentence maps acetyl-CoA to 233 uM Km

raw_value_unit_evidence: Km raw_value=233 raw_unit=uM

row_label: acetyl-CoA item in ordered Km sentence


column_label: Abstract metric sentence maps HCO3- to 750 uM Km

raw_value_unit_evidence: Km raw_value=750 raw_unit=uM

row_label: HCO3- item in ordered Km sentence


enzyme_display_name: propionyl-CoA carboxylase

organism: Leptospira interrogans

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

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

enzyme: propionyl-CoA carboxylase


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


substrate_name: dihydroorotate

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

assay_conditions_summary: pH 8

column_label: ScienceDirect article prose reports reverse reaction KmDHO = 27.8 +/- 4.1 uM at pH 8.

normalized_value_unit_evidence: Km normalized_value=0.0278 normalized_unit=mM; exported rounded value=0.028 mM

raw_value_unit_evidence: Km raw_value=27.8+/-4.1 raw_unit=uM

row_label: huDHOase reverse reaction / DHO

table_label: ScienceDirect PMID 24332717 article prose, Figure 4A kinetic discussion

substrate: dihydroorotate


substrate_name: N-carbamoyl-L-aspartate

column_label: ScienceDirect article prose reports forward reaction KmCA-asp = 241.2 +/- 53.7 uM at pH 5.5.

normalized_value_unit_evidence: Km normalized_value=0.2412 normalized_unit=mM; exported rounded value=0.241 mM

raw_value_unit_evidence: Km raw_value=241.2+/-53.7 raw_unit=uM

row_label: huDHOase forward reaction / CA-asp

substrate: N-carbamoyl-L-aspartate


enzyme_display_name: methylcrotonoyl-CoA carboxylase

organism: Pseudomonas aeruginosa

proof_lines: beta-subunit beta-subunit mutant R51A, pH and temperature not specified in the publication

enzyme: methylcrotonoyl-CoA carboxylase


proof_lines: beta-subunit mutant G423A, pH and temperature not specified in the publication


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


proof_lines: beta-subunit mutant F417Y/G423A, pH and temperature not specified in the publication


proof_lines: beta-subunit mutant F417Y, pH and temperature not specified in the publication


enzyme_display_name: acetone carboxylase

organism: Xanthobacter versatilis

substrate_name: acetone

smiles: CC(=O)C

enzyme: acetone carboxylase

substrate: acetone


assay_conditions_summary: cofactor ATP


organism: Metallosphaera sedula

substrate_name: propanoyl-CoA

assay_conditions_summary: pH 7.5; 338.15 K; cofactor CoA

substrate: propanoyl-CoA


assay_conditions_summary: pH 7.5; 338.15 K; cofactor ATP


organism: Mycolicibacterium phlei


proof_lines: pH 8.0, 30°C, recombinant methylcrotonyl-CoA carboxylase


proof_lines: pH 8.0, 30°C, recombinant geranyl-CoA carboxylase

proof_lines: Vmax: 430 nmol/mg/min, pH and temperature not specified in the publication


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP


enzyme_display_name: atromentin synthase

organism: Tapinella panuoides

enzyme: atromentin synthase


substrate_name: Propanoyl-CoA; Hydrogencarbonate; ATP

substrate: Propanoyl-CoA; Hydrogencarbonate; ATP


substrate_name: Hydrogencarbonate; Propanoyl-CoA; ATP

substrate: Hydrogencarbonate; Propanoyl-CoA; ATP


organism: Pseudomonas citronellolis


substrate_name: (E)-crotonoyl-CoA

substrate: (E)-crotonoyl-CoA


organism: Escherichia coli

substrate: ATP


organism: Amycolatopsis mediterranei


enzyme_display_name: geranoyl-CoA carboxylase

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

enzyme: geranoyl-CoA carboxylase


assay_conditions_summary: pH 8.5; 310.15 K; cofactor CoA


organism: Zea mays


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R410W to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA


organism: Acidianus brierleyi

assay_conditions_summary: pH 7.5; 343.15 K; cofactor CoA


organism: Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: acetophenone carboxylase

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

substrate_name: acetophone

proof_lines: Kinetic parameters have been established using the heteromeric complex including recombinant Apc5.

enzyme: acetophenone carboxylase

substrate: acetophone


substrate_name: geranoyl-CoA

substrate: geranoyl-CoA


organism: Pisum sativum


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: glutamine

substrate: glutamine


substrate_name: hydrogencarbonate

column_label: PubMed abstract says the Km values for glutamine and bicarbonate are 5 X 10(-4) M and 3 X 10(-3) M, respectively; bicarbonate maps to 3 X 10(-3) M.

raw_value_unit_evidence: Km raw_value=3 X 10(-3) raw_unit=M

row_label: CPSase activity; substrate bicarbonate

table_label: PMID 182284 PubMed abstract

substrate: hydrogencarbonate


organism: Streptomyces coelicolor

substrate_name: butyryl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D422C with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 303.15 K; cofactor CoA

proof_lines: mutant enzyme D422C, in 100 mM potassium phosphate, pH 7.6, at 30°C


substrate_name: propionyl-CoA

substrate: propionyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D422A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D422A, in 100 mM potassium phosphate, pH 7.6, at 30°C

substrate: butyryl-CoA


proof_lines: wild type enzyme, in 100 mM potassium phosphate, pH 7.6, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D422V with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D422V, in 100 mM potassium phosphate, pH 7.6, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D422N with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D422N, in 100 mM potassium phosphate, pH 7.6, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D422L with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D422L, in 100 mM potassium phosphate, pH 7.6, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D422I with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D422I, in 100 mM potassium phosphate, pH 7.6, at 30°C


substrate_name: acetyl-CoA

substrate: acetyl-CoA


organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)

substrate_name: ATP


substrate_name: acetone (in the presence of CO(2))

substrate: acetone (in the presence of CO(2))


smiles: [Co]


organism: Xanthomonas citri pv. citri

assay_conditions_summary: pH 7.6; cofactor CoA

proof_lines: pH 7.6, temperature not specified in the publication

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


organism: Myxococcus xanthus

sequence: PKIRKVLVANRGEIAIRVMRTXKELGIATV

assay_conditions_summary: pH 7.2; cofactor CoA

column_label: The abstract reports apparent Km values for acetyl-CoA, butyryl-CoA, propionyl-CoA, and succinyl-CoA of 0.2, 0.2, 0.03, and 1.0 mM, respectively.

raw_value_unit_evidence: Km raw_value=0.03 mM raw_unit=mM

row_label: Prose segment: propionyl-CoA Km

table_label: PubMed PMID 9683657 abstract


assay_conditions_summary: pH 7.2; cofactor ATP


raw_value_unit_evidence: Km raw_value=0.2 mM raw_unit=mM

row_label: Prose segment: butyryl-CoA Km


row_label: Prose segment: acetyl-CoA Km


substrate_name: succinyl-CoA

substrate: succinyl-CoA


substrate_name: aspartate

substrate: aspartate


substrate_name: carbamoyl phosphate

substrate: carbamoyl phosphate


organism: Homo sapiens

column_label: Abstract reports apparent Km values for ATP, propionyl-CoA, and bicarbonate as 0.08 mM, 0.29 mM, and 3.0 mM, respectively.

raw_value_unit_evidence: Km raw_value=0.08 mM raw_unit=mM

row_label: Human propionyl-CoA carboxylase / ATP

table_label: PubMed XML abstract PMID 6765947


substrate_name: propanoyl-CoA

raw_value_unit_evidence: Km raw_value=0.29 mM raw_unit=mM

row_label: Human propionyl-CoA carboxylase / propionyl-CoA

substrate: propanoyl-CoA


assay_conditions_summary: 310.15 K; cofactor CoA


organism: Plasmodium falciparum


organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

substrate_name: L-glutamine

assay_conditions_summary: pH 7.5; cofactor ATP

column_label: Table 1 reports MurT/GatD enzymatic parameters with L-Gln apparent KM 78+/-8 uM.

raw_value_unit_evidence: Km raw_value=78+/-8 uM raw_unit=uM

row_label: MurT/GatD enzymatic parameters / L-Gln

table_label: PMC full text Table 1 PMID 30093673

substrate: L-glutamine


column_label: The abstract reports the enzyme had unusually high affinity for ATP (Km = 0.2 mM).

row_label: Prose segment: ATP Km

table_label: PubMed PMID 206652 abstract


organism: Pseudomonas denitrificans (nom. rej.)

substrate_name: adenosyl-cobyrinic acid a,c-diamide

substrate: adenosyl-cobyrinic acid a,c-diamide


organism: Saccharomyces cerevisiae


organism: Sus scrofa

assay_conditions_summary: cofactor CoA

column_label: Table III row Propionyl-CoA reports apparent Km 0.2 x 10^-3 M. Propionyl-CoA is the common-name synonym for propanoyl-CoA.

normalized_value_unit_evidence: apparent Km normalized_value=0.2 normalized_unit=mM

raw_value_unit_evidence: apparent Km raw_value=0.2 x 10^-3 raw_unit=M

row_label: Propionyl-CoA

table_label: Table III - Substrate specificity and kinetic constants of crystalline pig heart propionyl carboxylase


substrate_name: butanoyl-CoA

column_label: Table III row Butyryl-CoA reports apparent Km 1.5 x 10^-3 M. Butyryl-CoA is the common-name synonym for butanoyl-CoA.

normalized_value_unit_evidence: apparent Km normalized_value=1.5 normalized_unit=mM

raw_value_unit_evidence: apparent Km raw_value=1.5 x 10^-3 raw_unit=M

row_label: Butyryl-CoA

substrate: butanoyl-CoA


substrate_name: NaHCO3 (isoform 3)

column_label: Table 1 row hACC2.v2 / NaHCO3 reports Km 6500 ± 556 μM. UniProt O00763 is human ACC2/ACACB, matching the ACC2.v2 row rather than ACC1.

raw_value_unit_evidence: Km raw_value=6500 ± 556 raw_unit=μM

row_label: hACC2.v2 / NaHCO3

table_label: PMC2629817 Table 1

substrate: NaHCO3 (isoform 3)


organism: Lathyrus oleraceus

assay_conditions_summary: pH 8; cofactor ATP

proof_lines:
pH 8.0, 37°C
ATP


substrate: ATP


organism: Gallus gallus

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


enzyme_display_name: pyruvate carboxylase

organism: Bacillus subtilis (strain 168)

substrate_name: pyruvate

column_label: Results state: We determined a Km for pyruvate of 0.23 mM (Fig. 3A), and substrate affinity was not altered in the presence of DarB (0.23 mM).

raw_value_unit_evidence: Km raw_value=0.23 raw_unit=mM

row_label: Bacillus subtilis pyruvate carboxylase assayed with pyruvate

table_label: PMC full-text PMID 35130724 / Results paragraph and Fig. 3A caption

enzyme: pyruvate carboxylase

substrate: pyruvate


organism: Escherichia coli

assay_conditions_summary: pH 7.6; cofactor ATP

proof_lines: mutant I18W/A23F/C24F, Gln-dependent ATPase activity, pH 7.6, temperature not specified in the publication

proof_lines: mutant I18W/A23F/C24F, value below 0.01, CP-synthesis (co-substrate: L-Gln, HCO3-), pH 7.6, temperature not specified in the publication

proof_lines: mutant I18W/A23F/C24F, HCO3-dependent ATPase activity, pH 7.6, temperature not specified in the publication


substrate_name: ADP

proof_lines: mutant M911E, value below 0.01, ATP-synthesis, pH 7.6, temperature not specified in the publication

substrate: ADP


proof_lines: mutant M174E/M378E, value below 0.01, CP-synthesis (co-substrate: L-Gln, HCO3-), pH 7.6, temperature not specified in the publication

proof_lines: mutant M174E/M378E, HCO3-dependent ATPase activity, pH 7.6, temperature not specified in the publication

proof_lines: mutant M174E/M378E, Gln-dependent ATPase activity, pH 7.6, temperature not specified in the publication


proof_lines: mutant L648E,value below 0.01, CP-synthesis (co-substrate: L-Gln, HCO3-), pH 7.6, temperature not specified in the publication

proof_lines: mutant L648E, HCO3-dependent ATPase activity, pH 7.6, temperature not specified in the publication

proof_lines: mutant L648E, Gln-dependent ATPase activity, pH 7.6, temperature not specified in the publication


proof_lines: mutant L720E, value below 0.01, CP-synthesis (co-substrate: L-Gln, HCO3-), pH 7.6, temperature not specified in the publication

proof_lines: mutant L720E, HCO3-dependent ATPase activity, pH 7.6, temperature not specified in the publication

proof_lines: mutant L720E, Gln-dependent ATPase activity, pH 7.6, temperature not specified in the publication


proof_lines: mutant M378E, CP-synthesis (co-substrate: L-Gln, HCO3-), pH 7.6, temperature not specified in the publication

proof_lines: mutant M378E, HCO3-dependent ATPase activity, pH 7.6, temperature not specified in the publication

proof_lines: mutant M378E, Gln-dependent ATPase activity, pH 7.6, temperature not specified in the publication


proof_lines: mutant M911E, value below 0.01, CP-synthesis (co-substrate: L-Gln, HCO3-), pH 7.6, temperature not specified in the publication

proof_lines: mutant M911E, HCO3-dependent ATPase activity, pH 7.6, temperature not specified in the publication

proof_lines: mutant M911E, Gln-dependent ATPase activity, pH 7.6, temperature not specified in the publication


proof_lines: mutant L648E, ATP-synthesis, pH 7.6, temperature not specified in the publication


proof_lines: mutant L720E, ATP-synthesis, pH 7.6, temperature not specified in the publication


proof_lines: mutant A23F, CP-synthesis (co-substrate: L-Gln, HCO3-), pH 7.6, temperature not specified in the publication

proof_lines: mutant A23F, HCO3-dependent ATPase activity, pH 7.6, temperature not specified in the publication

proof_lines: mutant A23F, Gln-dependent ATPase activity, pH 7.6, temperature not specified in the publication


proof_lines: mutant M174E, HCO3-dependent ATPase activity, pH 7.6, temperature not specified in the publication

proof_lines: mutant M174E, Gln-dependent ATPase activity, pH 7.6, temperature not specified in the publication

proof_lines: mutant M174E, CP-synthesis (co-substrate: L-Gln, HCO3-), pH 7.6, temperature not specified in the publication


proof_lines: mutant G575F, ATP-synthesis, pH 7.6, temperature not specified in the publication


proof_lines: mutant G575F, CP-synthesis (co-substrate: L-Gln, HCO3-), pH 7.6, temperature not specified in the publication

proof_lines: mutant G575F, HCO3-dependent ATPase activity, pH 7.6, temperature not specified in the publication

proof_lines: mutant G575F, Gln-dependent ATPase activity, pH 7.6, temperature not specified in the publication


proof_lines: mutant I18W/A23F/C24F, ATP-synthesis, pH 7.6, temperature not specified in the publication


substrate_name: L-Gln

proof_lines: mutant M174E/M378E, glutaminase activity pH 7.6, temperature not specified in the publication

substrate: L-Gln


proof_lines: mutant M174E, ATP-synthesis, pH 7.6, temperature not specified in the publication


proof_lines: mutant I18W/A23F/C24F, glutaminase activity pH 7.6, temperature not specified in the publication


proof_lines: mutant M378E, glutaminase activity pH 7.6, temperature not specified in the publication


proof_lines: wild-type, ATP-synthesis, pH 7.6, temperature not specified in the publication


proof_lines: mutant M911E, glutaminase activity pH 7.6, temperature not specified in the publication


substrate_name: Asp

substrate: Asp


proof_lines: mutant M174E, glutaminase activity pH 7.6, temperature not specified in the publication


assay_conditions_summary: pH 7.6; cofactor ADP

proof_lines: mutant G575K, ATP-synthesis, pH 7.6, temperature not specified in the publication


proof_lines: mutant A23K, CP-synthesis (co-substrate: L-Gln, HCO3-), pH 7.6, temperature not specified in the publication

proof_lines: mutant A23K, HCO3-dependent ATPase activity, pH 7.6, temperature not specified in the publication

proof_lines: mutant A23K, Gln-dependent ATPase activity, pH 7.6, temperature not specified in the publication


proof_lines: mutant G575K, HCO3-dependent ATPase activity, pH 7.6, temperature not specified in the publication

proof_lines: mutant G575K, CP-synthesis (co-substrate: L-Gln, HCO3-), pH 7.6, temperature not specified in the publication

proof_lines: mutant G575K, Gln-dependent ATPase activity, pH 7.6, temperature not specified in the publication


proof_lines: mutant M378E, ATP-synthesis, pH 7.6, temperature not specified in the publication


proof_lines: mutant A23K, glutaminase activity pH 7.6, temperature not specified in the publication


proof_lines: mutant M174E/M378E, ATP-synthesis, pH 7.6, temperature not specified in the publication


proof_lines: mutant A23F, ATP-synthesis, pH 7.6, temperature not specified in the publication


proof_lines: mutant A23K, ATP-synthesis, pH 7.6, temperature not specified in the publication


proof_lines: mutant L720E, glutaminase activity pH 7.6, temperature not specified in the publication


proof_lines: mutant A23F, glutaminase activity pH 7.6, temperature not specified in the publication


proof_lines: mutant L648E, glutaminase activity pH 7.6, temperature not specified in the publication


proof_lines: mutant G575F, glutaminase activity pH 7.6, temperature not specified in the publication


proof_lines: mutant G575K, glutaminase activity pH 7.6, temperature not specified in the publication


substrate_name: Gln

substrate: Gln


assay_conditions_summary: cofactor ATP


proof_lines:
C386 mutant
C436 mutant
C168 mutant


proof_lines:
C386A mutant
ATP, C386A mutant


proof_lines:
C99A mutant
mutant C99A


substrate_name: malonyl-CoA

assay_conditions_summary: pH 8; cofactor CoA

substrate: malonyl-CoA


assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

proof_lines: pH 7.6, 25°C, HCO3(-)-dependent ATPase, mutant D207N

proof_lines: pH 7.6, 25°C, Gln-dependent ATPase, mutant D207N


proof_lines: pH 7.6, 25°C, HCO3(-)-dependent ATPase, mutant F755A

proof_lines: pH 7.6, 25°C, Gln-dependent ATPase, mutant F755A


assay_conditions_summary: pH 7.6; 298.15 K; buffer 50 mM HEPES; cofactor ATP

proof_lines: pH 7.6, 25°C, HCO3(-)-dependent ATPase, wild-type enzyme

proof_lines: wild-type, HCO3-dependent ATPase activity, pH 7.6, temperature not specified in the publication

proof_lines: wild-type, CP-synthesis (co-substrate: L-Gln, HCO3-), pH 7.6, temperature not specified in the publication


proof_lines: pH 7.6, 25°C, HCO3(-)-dependent ATPase, mutant P690Q

proof_lines: pH 7.6, 25°C, Gln-dependent ATPase, mutant P690Q


proof_lines: pH 7.6, 25°C, HCO3(-)-dependent ATPase, mutant A144Q

proof_lines: pH 7.6, 25°C, Gln-dependent ATPase, mutant A144Q