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


enzyme_display_name: propionyl-CoA carboxylase

organism: Streptomyces coelicolor

substrate_name: propionyl-CoA

source_db: brenda

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: pH 7.6; 303.15 K; cofactor CoA

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

data_origin: experimental

enzyme: propionyl-CoA carboxylase

substrate: propionyl-CoA

source: brenda


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.

mutation_type: substitution

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


substrate_name: butyryl-CoA


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

source_db: uniprot

assay_conditions_summary: cofactor ATP

substrate: ATP

source: uniprot


substrate_name: hydrogencarbonate

substrate: hydrogencarbonate


enzyme_display_name: acetone carboxylase

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

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

smiles: CC(=O)C

enzyme: acetone carboxylase

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


smiles: [Co]


enzyme_display_name: methylcrotonoyl-CoA carboxylase

organism: Xanthomonas citri pv. citri

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

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

enzyme: methylcrotonoyl-CoA carboxylase


organism: Myxococcus xanthus

verification_status: verified

sequence: PKIRKVLVANRGEIAIRVMRTXKELGIATV

sequence_source: multiple

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

source_databases_merged: brenda uniprot

status: verified


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


enzyme_display_name: acetophenone carboxylase

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

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

enzyme: acetophenone carboxylase


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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


enzyme_display_name: acetyl-CoA carboxylase

source_db: skid

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

assay_conditions_summary: 310.15 K; cofactor CoA

source_databases_merged: skid uniprot

enzyme: acetyl-CoA carboxylase

source: skid


enzyme_display_name: GMP synthase (glutamine-hydrolyzing)

organism: Plasmodium falciparum

enzyme: GMP synthase (glutamine-hydrolyzing)


smiles: N


assay_conditions_summary: cofactor CoA


enzyme_display_name: lipid II isoglutaminyl synthase (glutamine-hydrolyzing)

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

substrate_name: L-glutamine

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

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


substrate_name: glutamine

verification_status: unverified

substrate: glutamine

status: unverified


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


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

organism: Pseudomonas denitrificans (nom. rej.)

substrate_name: adenosyl-cobyrinic acid a,c-diamide

substrate: adenosyl-cobyrinic acid a,c-diamide


organism: Saccharomyces cerevisiae

source_db: oed

kcat_over_km_origin: calculated

source: oed


organism: Sus scrofa

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


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

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

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

km_display: Not reported

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


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

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


substrate_name: ATP

substrate: 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


proof_lines: pH 7.6, 25°C, HCO3(-)-dependent ATPase, mutant D207A

proof_lines: pH 7.6, 25°C, Gln-dependent ATPase, mutant D207A


proof_lines: pH 7.6, 25°C, HCO3(-)-dependent ATPase, mutant A144Q/D207A

proof_lines: pH 7.6, 25°C, Gln-dependent ATPase, mutant A144Q/D207A


proof_lines: pH 7.6, 25°C, HCO3(-)-dependent ATPase, mutant D753N

proof_lines: pH 7.6, 25°C, Gln-dependent ATPase, mutant D753N


proof_lines: pH 7.6, 25°C, HCO3(-)-dependent ATPase, mutant D753A

proof_lines: pH 7.6, 25°C, Gln-dependent ATPase, mutant D753A


proof_lines: pH 7.6, 25°C, HCO3(-)-dependent ATPase, mutant I211S

proof_lines: pH 7.6, 25°C, Gln-dependent ATPase, mutant I211S


proof_lines: pH 7.6, 25°C, HCO3(-)-dependent ATPase, mutant S209A

proof_lines: pH 7.6, 25°C, Gln-dependent ATPase, mutant S209A


organism: Geobacillus thermodenitrificans

assay_conditions_summary: pH 8


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

organism: Mycobacterium tuberculosis

proof_lines: mutant D656A, ammonia-dependent reaction

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


proof_lines: mutant D656A, glutamine-dependent reaction


substrate_name: deamido-NAD+

assay_conditions_summary: cofactor NAD+

proof_lines:
wild-type, glutamine-dependent reaction
wild-type, ammonia-dependent reaction
wild-type enzyme

substrate: deamido-NAD+


assay_conditions_summary: cofactor ATP


proof_lines: mutant C176A, ammonia-dependent reaction


substrate_name: L-Glu

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

substrate: L-Glu


proof_lines:
wild-type, ammonia-dependent reaction
wild-type, glutamine-dependent reaction


substrate_name: L-glutamic acid gamma-monohydroxamate

smiles: C(CC(=O)NO)C(C(=O)O)N

substrate: L-glutamic acid gamma-monohydroxamate


proof_lines: ATP, wild-type enzyme, Gln-dependent activity


proof_lines:
wild-type
wild-type enzyme


substrate_name: hydroxylamine

smiles: NO

substrate: hydroxylamine


proof_lines:
N74A mutant
mutant N74A


organism: Bacillus amyloliquefaciens

proof_lines: wild type enzyme, in 50 mM HEPES (pH 7.5), at 37°C


proof_lines: mutant enzyme T970A, in 50 mM HEPES (pH 7.5), at 37°C


proof_lines: mutant enzyme T941F, in 50 mM HEPES (pH 7.5), at 37°C


proof_lines: mutant enzyme K986I, in 50 mM HEPES (pH 7.5), at 37°C


proof_lines: mutant enzyme T941F/K986I, in 50 mM HEPES (pH 7.5), at 37°C


proof_lines: mutant enzyme T941F/T970A/K986I, in 50 mM HEPE (pH 7.5), at 37°C


assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM HEPES; cofactor ATP

proof_lines: mutant enzyme W437T, at 25°C in 50 mM HEPES buffer, pH 7.5


proof_lines: mutant enzyme W213T, at 25°C in 50 mM HEPES buffer, pH 7.5


proof_lines: mutant enzyme W71T, at 25°C in 50 mM HEPES buffer, pH 7.5


proof_lines: mutant enzyme W461T, at 25°C in 50 mM HEPES buffer, pH 7.5


proof_lines: mutant enzyme W170T, at 25°C in 50 mM HEPES buffer, pH 7.5


proof_lines: mutant enzyme W175T, at 25°C in 50 mM HEPES buffer, pH 7.5


proof_lines: mutant enzyme E25Q/E383Q/E604Q, NH4Cl-dependent ATP hydrolysis


proof_lines: mutant enzyme E306A, Gln-dependent ATP hydrolysis


proof_lines: mutant enzyme E577Q, NH4Cl-dependent ATP hydrolysis


proof_lines: mutant enzyme E25Q/E383Q/E604Q, Gln-dependent ATP hydrolysis


proof_lines: mutant enzyme E577Q, Gln-dependent ATP hydrolysis


proof_lines: mutant enzyme E25Q/E383Q, Gln-dependent ATP hydrolysis


proof_lines: mutant enzyme E25Q/E383Q, NH4Cl-dependent ATP hydrolysis


proof_lines: mutant enzyme R848A, Gln-dependent ATP hydrolysis


proof_lines: mutant enzyme E604Q, NH4Cl-depebndent ATP hydrolysis


proof_lines: mutant enzyme E916Q, NH4Cl-dependent ATP hydrolysis


proof_lines: mutant enzyme E604Q, Gln-dependent ATP hydrolysis


proof_lines: mutant enzyme E383Q, NH4Cl-dependent ATP hydrolysis


proof_lines: mutant enzyme E383Q,Gln-dependent ATP hydrolysis


proof_lines: mutant enzyme E383QE916Q, Gln-dependent ATP hydrolysis

proof_lines: mutant enzyme E383QE916Q, Gln-dependent ASTP hydrolysis


proof_lines: mutant enzyme E916Q, Gln-dependent ATP hydrolysis


organism: Rhizobium etli

assay_conditions_summary: pH 7.8; 303.15 K; cofactor ATP


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


substrate_name: Carbamoyl phosphate

assay_conditions_summary: pH 7.8; 303.15 K; cofactor CoA

proof_lines: pH 7.8, 30°C, C249A mutant, with acetyl-CoA and K+

proof_lines: pH 7.8, 30°C, C249A mutant, without acetyl-CoA and K+

substrate: Carbamoyl phosphate


proof_lines: pH 7.8, 30°C, wild-type Pyc1, with acetyl-CoA and K+

proof_lines: pH 7.8, 30°C, wild-type Pyc1, without acetyl-CoA and K+


organism: Bos taurus

assay_conditions_summary: cofactor CoA


substrate_name: (E)-crotonoyl-CoA

substrate: (E)-crotonoyl-CoA


proof_lines: mutant D471A, pH 7.8, 30°C, presence of acetyl-CoA


proof_lines: wild-type, pH 7.8, 30°C, Hill coefficient 2.7

proof_lines: hybrid tetramers between wild-type and mutant K1119Q, pH 7.8, 30°C


proof_lines: mutant R469K, pH 7.8, 30°C, Hill coefficient 0.9, presence of acetyl-CoA


proof_lines: mutant E1027R, pH 7.8, 30°C, Hill coefficient 2.3, presence of acetyl-CoA


proof_lines: mutant R469S, pH 7.8, 30°C, Hill coefficient 2.3, presence of acetyl-CoA


proof_lines: mutant D1018A, pH 7.8, 30°C, Hill coefficient 2.1, presence of acetyl-CoA


proof_lines: mutant E1027A, pH 7.8, 30°C, Hill coefficient 3.0, presence of acetyl-CoA


organism: Lupinus albus


substrate_name: L-Asp

substrate: L-Asp


substrate_name: L-glutamine

proof_lines: pH 7.6, 25°C, mutant Q351A, L-glutamine hydrolysis

substrate: L-glutamine


proof_lines: pH 7.6, 25°C, mutant N311A, L-glutamine hydrolysis


proof_lines: pH 7.6, 25°C, mutant D334A, L-glutamine hydrolysis


proof_lines: pH 7.6, 25°C, mutant Q310A, L-glutamine hydrolysis


substrate_name: acetyl-CoA

proof_lines:
mutant enzyme
MgATP2-, mutant enzyme

substrate: acetyl-CoA


proof_lines:
40°C, pH 8.0, His-ATPP/DD
40°C, pH 8.0, NF-ATPP/DD


assay_conditions_summary: pH 8; 313.15 K; cofactor ATP


proof_lines:
40°C, pH 8.0, NF-ATPP/DD
40°C, pH 8.0, His-ATPP/DD


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: pH 7.5, 25°C, mutant K119Q, no biotin, pyruvate carboxylation

proof_lines: pH 7.5, 25°C, mutant K119Q, 10 mM biotin, pyruvate carboxylation


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ADP

proof_lines: pH 7.5, 25°C, wild-type, reverse reaction

proof_lines: wild-type, MgADP phosphorylation, pH 7.8, 30°C


proof_lines: pH 7.5, 25°C, wild-type, no biotin, pyruvate carboxylation

proof_lines: pH 7.5, 25°C, wild-type, 10 mM biotin, pyruvate carboxylation

proof_lines: pH 7.5, 25°C, wild-type, pyruvate carboxylation


proof_lines: pH 7.5, 25°C, mutant T882A, no biotin, pyruvate carboxylation

proof_lines: pH 7.5, 25°C, mutant T882A, 10 mM biotin, pyruvate carboxylation


proof_lines: mutant E348D, ammonia-dependent activity, pH 8.0, 37°C

proof_lines: mutant E348D, synthetase activity, ammonia-dependent activity, 100 mM NH4Cl, pH 8.0, 37°C

proof_lines: mutant E348D, glutamine-dependent activity, pH 8.0, 37°C


proof_lines: mutant E348Q, glutaminase activity, pH 8.0, 37°C, ATP absent

proof_lines: mutant E348Q, glutaminase activity, pH 8.0, 37°C, 5 mM ATP present


proof_lines: mutant E348D, glutaminase activity, pH 8.0, 37°C, ATP absent

proof_lines: mutant E348D, glutaminase activity, pH 8.0, 37°C, 5 mM ATP present


proof_lines: mutant E348A, glutaminase activity, pH 8.0, 37°C, 5 mM ATP present

proof_lines: mutant E348A, glutaminase activity, pH 8.0, 37°C, ATP absent


substrate_name: propanoyl-CoA

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

substrate: propanoyl-CoA


assay_conditions_summary: 310.15 K; cofactor NAD+


assay_conditions_summary: 310.15 K; cofactor ATP


proof_lines: pH 7.6, mutant alphaP360A/alphaH361A/betaR265A

proof_lines: pH 7.6, mutant betaQ262A/betaR265A/betaN266A


proof_lines: pH 7.6, 25°C, wild-type enzyme, L-glutamine hydrolysis

proof_lines: wild-type, glutaminase activity pH 7.6, temperature not specified in the publication


assay_conditions_summary: pH 7.6; cofactor ATP

proof_lines: wild-type enzyme, NH4Cl-dependent ATP hydrolysis


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


substrate_name: L-aspartic acid

proof_lines: pH 8, reaction with glutamine, C-terminally tagged recombinant enzyme

proof_lines: pH 8, reaction with NH3, C-terminally tagged recombinant enzyme

substrate: L-aspartic acid


assay_conditions_summary: pH 8; cofactor ATP


substrate_name: glutamine

proof_lines: pH 8, C-terminally tagged recombinant enzyme

substrate: glutamine


organism: Mus musculus


substrate_name: L-Gln

substrate: L-Gln


substrate_name: pyruvate

proof_lines: co-substrate: HCO3-, mutant H216N, pyruvate carboxylation, pH 7.8, 30°C

substrate: pyruvate


substrate_name: oxaloacetate

assay_conditions_summary: pH 7.8; 303.15 K; cofactor ADP

proof_lines: co-substrate: ADP + phosphate, mutant H216N, oxaloacetate decarboxylation, pH 7.8, 30°C

substrate: oxaloacetate


substrate_name: ADP

proof_lines: mutant H216N, MgADP phosphorylation, pH 7.8, 30°C

substrate: ADP


substrate_name: ATP

proof_lines: mutant H216N, MgATP cleavage, pH 7.8, 30°C

substrate: ATP


organism: Rattus norvegicus

substrate_name: XMP

substrate: XMP


substrate_name: GMP

substrate: GMP


substrate_name: Gln

substrate: Gln


proof_lines: mutant D420A, pH 7.8, 30°C, presence of acetyl-CoA


proof_lines: mutant R424S, pH 7.8, 30°C, presence of acetyl-CoA


proof_lines: mutant R429S, pH 7.8, 30°C, presence of acetyl-CoA


proof_lines: mutant R429K, pH 7.8, 30°C, presence of acetyl-CoA


mutation_signature: N-terminal deletion mutant

mutation_type: deletion

proof_lines: N-terminal deletion mutant, pH 7.5, 37°C


substrate_name: L-glutamyl-tRNAGln

substrate: L-glutamyl-tRNAGln


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

organism: Salmonella enterica subsp. enterica serovar Typhimurium

assay_conditions_summary: pH 7.7; 303.15 K; cofactor ATP


substrate_name: cobyrinate

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

substrate: cobyrinate


substrate_name: ammonia

substrate: ammonia


substrate_name: deamido-NAD+

assay_conditions_summary: pH 7.6; cofactor NAD+

substrate: deamido-NAD+


organism: Sinorhizobium meliloti

assay_conditions_summary: pH 8


substrate_name: Unknown

substrate: Unknown


organism: Alopecurus myosuroides

substrate_name: acetyl-CoA

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines: cytosolic enzyme from strain Rothamsted, pH 8.0, 30°C

proof_lines: cytosolic enzyme from strain Notts A1, pH 8.0, 30°C

proof_lines: plastidic enzyme from strain Rothamsted, pH 8.0, 30°C

substrate: acetyl-CoA


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: plastidic enzyme from strain Notts A1, pH 8.0, 30°C


proof_lines: mutant H186E/E383H, overall reaction, pH 8.5, 37°C

proof_lines: mutant H186E/E383H, release of NH3, pH 8.5, 37°C


proof_lines: mutant H186A/E383A, overall reaction, pH 8.5, 37°C

proof_lines: mutant H186A/E383A, release of NH3, pH 8.5, 37°C


proof_lines: mutant E383A, overall reaction, pH 8.5, 37°C

proof_lines: mutant E383A, release of NH3, pH 8.5, 37°C


substrate_name: L-glutamine

substrate: L-glutamine


proof_lines: wild-type, overall reaction, pH 8.5, 37°C


proof_lines: mutant H186A, overall reaction, pH 8.5, 37°C

proof_lines: mutant H186A, release of NH3, pH 8.5, 37°C


organism: Bacillus subtilis

assay_conditions_summary: cofactor ATP

proof_lines: formylglycinamide ribonucleotide amidotransferase complex


substrate_name: formylglycinamide ribonucleotide

substrate: formylglycinamide ribonucleotide


substrate_name: Asp

substrate: Asp


organism: Vibrio cholerae serotype O1

substrate_name: glutamine

substrate: glutamine


substrate_name: L-asparagine

substrate: L-asparagine


proof_lines:
Kis, versus ATP
Kis, versus Gln
Kii, versus Asp


organism: Aromatoleum aromaticum

substrate_name: acetophenone

substrate: acetophenone


assay_conditions_summary: pH 6.5; 303.15 K; cofactor ATP


organism: Achromobacter sp.

assay_conditions_summary: cofactor CoA


proof_lines: chimeric enzyme, in comparison to effect of phosphorylation and presence of effectors


assay_conditions_summary: pH 7.6; 310.15 K; cofactor ADP

proof_lines: chimeric enzyme, in presence of ornithine and absence of UMP

proof_lines: Escherichia coli enzyme, in presence of ornithine and absence of UMP


organism: Emiliania huxleyi


substrate_name: pyruvate

substrate: pyruvate


organism: Brassica napus

substrate_name: ATP

substrate: ATP


organism: Escherichia coli


substrate_name: L-Gln

substrate: L-Gln


proof_lines: wild-type, glutamine-dependent activity, pH 8.0, 37°C

proof_lines: wild-type, synthetase activity, glutamine-dependent activity, 20 mM L-Gln, pH 8.0, 37°C


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: wild-type, glutaminase activity, pH 8.0, 37°C, ATP absent


organism: Festuca rubra

proof_lines:
cytosolic enzyme, pH 8.0, 30°C
plastidic enzyme, pH 8.0, 30°C


proof_lines:
plastidic enzyme, pH 8.0, 30°C
cytosolic enzyme, pH 8.0, 30°C


organism: Glycine max

assay_conditions_summary: pH 7.6; 295.15 K; cofactor ATP


substrate_name: L-Asp

substrate: L-Asp


proof_lines: glutaminase activity in the absence of ATP

proof_lines: glutamine dependent asparagine synthetase activity

proof_lines: glutaminase activity in the presence of ATP


substrate_name: L-aspartate

substrate: L-aspartate


organism: Geobacillus stearothermophilus


organism: Homo sapiens

substrate_name: XMP

proof_lines:
native enzyme
recombinant enzyme

substrate: XMP


substrate_name: Gln

substrate: Gln


proof_lines:
9686 enzyme
Wayne enzyme


proof_lines:
Wayne enzyme
9686 enzyme


organism: Ligilactobacillus salivarius


organism: Mycobacterium tuberculosis


assay_conditions_summary: pH 7.5; 313.15 K; cofactor ATP


assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

proof_lines:
37°C, pH 8.0, recombinant NadE-679
37°C, pH 8.5, recombinant NadE-738


proof_lines: pH and temperature not specified in the publication


organism: Helicobacter pylori

substrate_name: L-aspartyl-tRNAAsn

proof_lines: in the absence of GluRS2, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 12 mM MgCl2, at 37°C

proof_lines: in the presence of 440fold excess of GluRS2, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 12 mM MgCl2, at 37°C

substrate: L-aspartyl-tRNAAsn


assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

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


organism: Lupinus luteus


organism: Pseudomonas fluorescens


organism: Rattus norvegicus

assay_conditions_summary: pH 7

proof_lines:
in 30% dimethyl sulfoxide
in 10% glycerol, pH 7
in absence of cryoprotectants


assay_conditions_summary: pH 7; cofactor ATP


assay_conditions_summary: 310.15 K; cofactor ATP

proof_lines:
hindlimb muscle
second value 0.227 mM
adipose tissue


substrate_name: malonyl-CoA

substrate: malonyl-CoA


substrate_name: acetodethio-CoA

substrate: acetodethio-CoA


organism: Nicotiana tabacum

substrate_name: deamido-NAD+

assay_conditions_summary: cofactor NAD+

substrate: deamido-NAD+


organism: Rhizobium etli

proof_lines: mutant enzyme R548K, in 100 mM Tris-HCl pH 7.8, 30°C


substrate_name: oxamate

proof_lines: mutant enzyme Q552N, in 100 mM Tris-HCl pH 7.8, 30°C

substrate: oxamate


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 7.8; 303.15 K; cofactor ATP

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

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


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

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


substrate_name: L-glutamine

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

substrate: L-glutamine


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

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


organism: Ricinus communis

substrate_name: acetyl-CoA

substrate: acetyl-CoA


enzyme_display_name: DNA ligase (ATP)

organism: Tequatrovirus T4

substrate_name: geranyl diphosphate

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

enzyme: DNA ligase (ATP)

substrate: geranyl diphosphate


substrate_name: farnesyl diphosphate

substrate: farnesyl diphosphate


substrate_name: isopentenyl diphosphate

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

substrate: isopentenyl diphosphate


substrate_name: (2E,6E)-farnesyl triphosphate

substrate: (2E,6E)-farnesyl triphosphate


substrate_name: dimethylallyl diphosphate

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

substrate: dimethylallyl diphosphate


substrate_name: farnesyl triphosphate

substrate: farnesyl triphosphate


enzyme_display_name: RNA ligase (ATP)

enzyme: RNA ligase (ATP)


substrate_name: (2E,6E)-farnesyl diphosphate

substrate: (2E,6E)-farnesyl diphosphate


substrate_name: GTP

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

substrate: GTP


substrate_name: ATP

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines: pH 7.4, 30°C, ATP as acceptor of AMP, Ap4A synthesis

substrate: ATP


enzyme_display_name: DNA ligase (NAD(+))

organism: Melanoplus sanguinipes

substrate_name: DNA

proof_lines: pH 7.6, 21°C, C/G matched nick DNA substrate

enzyme: DNA ligase (NAD(+))

substrate: DNA


substrate_name: NAD+

assay_conditions_summary: pH 7.6; 294.15 K; cofactor NAD+

substrate: NAD+


substrate_name: methylenebisphosphonate

proof_lines: in 50 mM HEPES/KOH (pH 7.2), 1 mM dithiothreitol, 5 mM MgCl2, at 30°C

proof_lines: internal phosphomonoesters in nicked natural DNA

proof_lines: for either the joining of oligo(dT)10 on poly(dA) or the joining of DNA fragments with a two base-pair overhang generated by a restriction enzyme

substrate: methylenebisphosphonate


substrate_name: clodronate

substrate: clodronate


substrate_name: etidronate

substrate: etidronate


organism: Triticum aestivum

substrate_name: 5'-phosphate termini of RNA

assay_conditions_summary: cofactor ATP

substrate: 5'-phosphate termini of RNA


organism: Chlorella virus

substrate_name: (single-stranded DNA splinted by RNA)m

proof_lines:
pH 7.4, 25°C
value below, pH 7.4, 25°C

substrate: (single-stranded DNA splinted by RNA)m


organism: Hemicentrotus pulcherrimus

substrate_name: dATP

substrate: dATP


organism: Paramecium bursaria chlorella virus

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP


organism: Thermococcus kodakarensis

substrate_name: nicked DNA

substrate: nicked DNA


organism: Betaentomopoxvirus amoorei


organism: Psychromonas sp. SP041

verification_status: corrected

source_license: CC BY-NC-ND 4.0

assay_conditions_summary: 303.15 K; cofactor ATP

status: corrected


organism: synthetic construct

substrate_name: (RNA)n

smiles: N#N

proof_lines: pH 6.0, 22°C, multiple-turnover derivatives 210t and 207t, engineered by changing the arrangement of the base pairs in the P2 stem

proof_lines: pH 8.0, 22°C, multiple-turnover derivative 207t, engineered by changing the arrangement of the base pairs in the P2 stem

proof_lines: pH 9.0, 22°C, multiple-turnover derivative 207t, engineered by changing the arrangement of the base pairs in the P2 stem

substrate: (RNA)n


organism: Phage TS2126

proof_lines:
activity with RNA
activity with DNA


substrate_name: diguanosine tetraphosphate

substrate: diguanosine tetraphosphate


organism: Mammalia

proof_lines:
DNA ligase I
DNA ligase II


organism: Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)


substrate_name: 2,3 diphosphoglycerate

substrate: 2,3 diphosphoglycerate


substrate_name: (ribonucleotide)n+m

substrate: (ribonucleotide)n+m


substrate_name: Unknown

substrate: Unknown


organism: Escherichia phage T7

proof_lines:
ATP-diphosphate exchange reaction
dATP
joinig reaction


enzyme_display_name: didemethylasterriquinone D synthase

organism: Aspergillus nidulans

proof_lines:
at pH 6.5 and 42°C
at pH 8.0 and 25°C

enzyme: didemethylasterriquinone D synthase


enzyme_display_name: 3-aminoavenalumate diazotase

organism: Streptomyces sp. RI-77

substrate_name: nitrite

proof_lines: with 3-aminoavenalumic acid as cosubstrate, at pH 7.0, temperature not specified in the publication

enzyme: 3-aminoavenalumate diazotase

substrate: nitrite


substrate_name: 3-Amino-4-hydroxybenzoic acid

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

proof_lines: at pH 7.0, temperature not specified in the publication

proof_lines: kcat is 0.30 min(-1) with 3-AAA as substrate. kcat is 0.13 min(-1) with 3,4-AHBA as substrate. kcat is 0.10 min(-1) with ATP as substrate (in the presence of 3-AAA). kcat is 0.25 min(-1) with ATP as substrate (in the presence of 3,4-AHBA).

substrate: 3-Amino-4-hydroxybenzoic acid


substrate_name: ATP

proof_lines: with 3-amino-4-hydroxybenzoic acid as cosubstrate, at pH 7.0, temperature not specified in the publication

substrate: ATP


enzyme_display_name: cyclic 2,3-diphosphoglycerate synthase

organism: Methanothermus fervidus

substrate_name: ADP

assay_conditions_summary: pH 7; cofactor ADP

proof_lines:
recombinant enzyme, at pH 7.0 and 83°C
native enzyme, at pH 7.0 and 83°C

enzyme: cyclic 2,3-diphosphoglycerate synthase

substrate: ADP


substrate_name: cyclic 2,3-bisphosphoglycerate

proof_lines:
native enzyme, at pH 7.0 and 83°C
recombinant enzyme, at pH 7.0 and 83°C

substrate: cyclic 2,3-bisphosphoglycerate


assay_conditions_summary: pH 7; 348.15 K; cofactor ATP

proof_lines:
at pH 7.0 and 75°C
native enzyme, at pH 7.0 and 83°C
recombinant enzyme, at pH 7.0 and 83°C


organism: Entamoeba histolytica

assay_conditions_summary: pH 7.5; 294.15 K; cofactor ATP

proof_lines: in 50 mM Tris pH 7.5, 100 mM NaCl, 10 mM dithiothreitol, at 21°C


organism: Homo sapiens

substrate_name: ATP (at 37 degrees Celsius)

proof_lines: kcat is 0.0000281 sec(-1) for ATP (at 37 degrees Celsius). kcat is 0.0000314 sec(-1) for GTP (at 37 degrees Celsius).

substrate: ATP (at 37 degrees Celsius)


substrate_name: GTP (at 37 degrees Celsius)

substrate: GTP (at 37 degrees Celsius)


organism: Enterobacteria phage T3


organism: Ferroplasma acidiphilum

substrate_name: (deoxyribonucleotide)n

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D162E to reconstruct the assayed variant sequence.

substrate: (deoxyribonucleotide)n


organism: Saccharolobus shibatae

assay_conditions_summary: pH 6.5; 338.15 K; cofactor ATP

proof_lines: 65°C, pH 6.5, recombinant DNA-ligase, in the presence of 1mM ATP and 5 mM Mn2+


organism: Pyrococcus furiosus

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: pH 7.5, 70°C, synthesis of P1-(5'-adenosyl),P4-(5'-guanosyl)tetraphosphate


substrate_name: GTP

source_databases_merged: brenda skid

substrate: GTP


enzyme_display_name: magnesium chelatase

organism: Synechocystis sp.

substrate_name: H2O; ATP; Protoporphyrin; Mg2+

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

enzyme: magnesium chelatase

substrate: H2O; ATP; Protoporphyrin; Mg2+


substrate_name: Mg2+; H2O; ATP; Protoporphyrin

substrate: Mg2+; H2O; ATP; Protoporphyrin


substrate_name: deuteroporphyrin

proof_lines:
pH 7.7, 37°C, 100 nM ChlH subunit
pH 7.7, 37°C, 200 nM ChlH subunit

substrate: deuteroporphyrin


enzyme_display_name: RNA 3'-terminal-phosphate cyclase (ATP)

organism: Escherichia coli (strain K12)

column_label: Abstract reports ATP is the best cofactor (Km = 20 microM), whereas GTP (Km = 100 microM) and other NTPs act less efficiently.

raw_value_unit_evidence: Km raw_value=20 microM raw_unit=microM

row_label: Escherichia coli RNA 3'-terminal phosphate cyclase / ATP

table_label: PubMed XML abstract PMID 9738023

enzyme: RNA 3'-terminal-phosphate cyclase (ATP)


raw_value_unit_evidence: Km raw_value=100 microM raw_unit=microM

row_label: Escherichia coli RNA 3'-terminal phosphate cyclase / GTP


organism: Mycobacterium tuberculosis

substrate_name: ATP; n+m m n DNA; n+m m n DNA

substrate: ATP; n+m m n DNA; n+m m n DNA


organism: Plasmodium falciparum

substrate_name: nicked DNA

substrate: nicked DNA


organism: Aquifex aeolicus


organism: Deinococcus radiodurans


substrate_name: n+m m n n+m n m DNA; n+m m n n+m n m DNA; NAD+


organism: Arabidopsis thaliana

substrate_name: ATP; H2O

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

substrate: ATP; H2O


enzyme_display_name: DNA ligase (ATP or NAD(+))

organism: Thermococcus fumicolans

substrate_name: NAD+

assay_conditions_summary: pH 6.5; cofactor NAD+

enzyme: DNA ligase (ATP or NAD(+))

substrate: NAD+


assay_conditions_summary: pH 6.5; cofactor ATP


organism: Escherichia phage T7

substrate_name: dATP

substrate: dATP


organism: Crithidia fasciculata

substrate_name: Unknown

substrate: Unknown


organism: Bacteriophage TS2126

substrate_name: ATP on the RNA substrate

proof_lines: Optimum activity is reached at 0.025-2.5 mM ATP.

substrate: ATP on the RNA substrate


organism: Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)


organism: Thermosynechococcus vestitus

proof_lines: pH 7.7, 45°C. At high ChlH concentrations, substrate inhibition is very noticeable


organism: Streptomyces sp. RI-77

substrate_name: 3-aminoavenalumic acid

assay_conditions_summary: pH 7; cofactor ATP

substrate: 3-aminoavenalumic acid


organism: Rattus norvegicus

substrate_name: NADP+; NADH

assay_conditions_summary: cofactor NADP+

substrate: NADP+; NADH


enzyme_display_name: polyporic acid synthase

organism: Streptomyces sp. LZ35

enzyme: polyporic acid synthase


substrate_name: ATP

substrate: ATP


organism: Saccharolobus shibatae (strain ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12)


enzyme_display_name: cobaltochelatase

organism: Pseudomonas denitrificans (nom. rej.)

substrate_name: hydrogenobyrinic acid a,c-diamide

enzyme: cobaltochelatase

substrate: hydrogenobyrinic acid a,c-diamide


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP


organism: Homo sapiens

assay_conditions_summary: pH 8; cofactor NAD+


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: NAD(+)

substrate: NAD(+)


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+


organism: Entamoeba histolytica

column_label: PubMed abstract reports that EhDNAligI uses ATP as nucleotide cofactor and follows Michaelis-Menten steady-state kinetics with K(m) ATP of 64 nM and k(cat) of 2.4 min^-1.

normalized_value_unit_evidence: Km normalized_value=0.000064 normalized_unit=mM from 64 nM; kcat normalized_value=0.04 normalized_unit=s^-1 from 2.4 min^-1 divided by 60; kcat_over_km normalized_value=625 normalized_unit=s^-1 mM^-1 from 0.04/0.000064

raw_value_unit_evidence: K(m) ATP raw_value=64 raw_unit=nM; k(cat) raw_value=2.4 raw_unit=min^-1

row_label: EhDNAligI ATP steady-state kinetics sentence

table_label: PubMed XML abstract PMID 20603158


organism: Escherichia coli

substrate_name: reduced acetylpyridine adenine dinucleotide

proof_lines: reverse reaction of wild-type domain III/R. rubrum domain I mixture

proof_lines: cyclic reaction of wild-type domain III/R. rubrum domain I mixture


proof_lines: reverse reaction of A432C mutant domain III/R. rubrum domain I mixture

proof_lines: cyclic reaction of A432C mutant domain III/R. rubrum domain I mixture

substrate: reduced acetylpyridine adenine dinucleotide


proof_lines: reverse reaction of D393C mutant domain III/R. rubrum domain I mixture

proof_lines: cyclic reaction of D393C mutant domain III/R. rubrum domain I mixture


proof_lines: reverse reaction of H345C mutant domain III/R. rubrum domain I mixture

proof_lines: cyclic reaction of H345C mutant domain III/R. rubrum domain I mixture


proof_lines: reverse reaction of R350C mutant domain III/R. rubrum domain I mixture

proof_lines: cyclic reaction of R350C mutant domain III/R. rubrum domain I mixture


proof_lines: reverse reaction of K424C mutant domain III/R. rubrum domain I mixture

proof_lines: cyclic reaction of K424C mutant domain III/R. rubrum domain I mixture


proof_lines: reverse reaction of R425C mutant domain III/R. rubrum domain I mixture

proof_lines: cyclic reaction of R425C mutant domain III/R. rubrum domain I mixture


proof_lines: reverse reaction of A348C mutant domain III/R. rubrum domain I mixture

proof_lines: cyclic reaction of A348C mutant domain III/R. rubrum domain I mixture


proof_lines: reverse reaction of G430C mutant domain III/R. rubrum domain I mixture

proof_lines: cyclic reaction of G430C mutant domain III/R. rubrum domain I mixture


proof_lines: reverse reaction of D392C mutant domain III/R. rubrum domain I mixture

proof_lines: cyclic reaction of D392C mutant domain III/R. rubrum domain I mixture


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


proof_lines: A348C mutation introduced into cysteine-free mutant enzyme


proof_lines: A390C mutation introduced into cysteine-free mutant enzyme


proof_lines: K424C mutation introduced into cysteine-free mutant enzyme


proof_lines: R425C mutation introduced into cysteine-free mutant enzyme


organism: Synechocystis sp.

assay_conditions_summary: pH 7.7; 307.15 K; cofactor ATP


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


proof_lines: enzyme co-reconstituted with bacteriorhodopsin, in the light

proof_lines: enzyme co-reconstituted with bacteriorhodopsin, in the dark


proof_lines: vs. oxidized acetylpyridine adenine dinucleotide


organism: Rhodospirillum rubrum


substrate_name: oxidized 3-acetylpyridine adenine dinucleotide


substrate: oxidized 3-acetylpyridine adenine dinucleotide


organism: Streptococcus pneumoniae

substrate_name: deoxyribonucleotide

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

proof_lines: co-substrate: NAD+, wild-type, 25°C, pH 7.5

substrate: deoxyribonucleotide


proof_lines: co-substrate: NAD+, mutant L75F, 25°C, pH 7.5


organism: Bos taurus

substrate_name: NADP+

proof_lines:
cosubstrate NADH
energy-linked reaction
nonenergy-linked reaction

substrate: NADP+


proof_lines:
cosubstrate NAD+
nonenergy-linked reaction
energy-linked reaction


substrate_name: acetylpyridine adenine dinucleotide

substrate: acetylpyridine adenine dinucleotide


organism: Mycolicibacterium smegmatis

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: 37°C and 45°C, pH 8, Mg2+ concentration higher than ATP concentration

proof_lines: 37°C, pH 8, Mg2+ concentration equal to that of ATP

proof_lines: 45°C, pH 8, Mg2+ concentration equal to that of ATP


substrate_name: pyruvate

proof_lines:
37°C, pH 8
45°C, pH 8

substrate: pyruvate


organism: Arabidopsis thaliana

assay_conditions_summary: cofactor ATP


organism: Saccharomyces cerevisiae

substrate_name: L-glutamine

assay_conditions_summary: 310.15 K; cofactor NAD+

substrate: L-glutamine


organism: Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)

substrate_name: cyclic 2,3-diphosphoglycerate (at pH 7.0 and 83 degrees Celsius)


organism: Rhizobium etli

substrate_name: oxaloacetate

proof_lines: mutant DELTA BC T882A, presence of oxamate, pH 7.5, 25°C

proof_lines: 1:1 hybrids of mutants DELTA BC T882A and DELTA BC DELTA BCCP, pH 7.5, 25°C

substrate: oxaloacetate


proof_lines: mutant DELTA BC DELTA BCCP, presence of oxamate, pH 7.5, 25°C

proof_lines: mutant DELTA BC DELTA BCCP, pH 7.5, 25°C

proof_lines: mutant lacking the N-terminal biotin carboxylase domain, pH 7.5, 25°C


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ADP

proof_lines: co-substrate: ADP + phosphate, wild-type, oxaloacetate decarboxylation, pH 7.8, 30°C

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R289A to reconstruct the assayed variant sequence.


substrate_name: deuteroporphyrin

substrate: deuteroporphyrin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R208A to reconstruct the assayed variant sequence.


enzyme: lipid II isoglutaminyl synthase (glutamine-hydrolyzing)


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


organism: Staphylococcus aureus


assay_conditions_summary: pH 7.5; cofactor CoA

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


organism: Streptococcus pyogenes

substrate_name: L-Glutamine; H2O

substrate: L-Glutamine; H2O


substrate_name: Gln

substrate: Gln


substrate_name: ATP


enzyme_display_name: acetone carboxylase

organism: Xanthobacter autotrophicus

substrate_name: acetone

enzyme: acetone carboxylase

substrate: acetone


substrate: ATP


organism: Thermus thermophilus

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


substrate_name: 5'-phosphoryl termini of poly(dA-dT)

substrate: 5'-phosphoryl termini of poly(dA-dT)


enzyme_display_name: methylcrotonoyl-CoA carboxylase

organism: Zea mays

enzyme: methylcrotonoyl-CoA carboxylase


substrate_name: crotonoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: crotonoyl-CoA


enzyme_display_name: acetyl-CoA carboxylase

organism: Yarrowia lipolytica

enzyme: acetyl-CoA carboxylase


substrate_name: acetyl-CoA

substrate: acetyl-CoA


enzyme_display_name: pyruvate carboxylase

organism: Apis mellifera

enzyme: pyruvate carboxylase


organism: Bacillus subtilis

substrate_name: 5'-phosphate terminus of deoxyribonucleotides


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

organism: Acinetobacter baumannii

substrate_name: deamido-NMN

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

substrate: deamido-NMN


substrate_name: deamido-NAD+

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

substrate: deamido-NAD+


organism: Azospirillum brasilense

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NAD+


organism: Escherichia coli


organism: Sulfolobus acidocaldarius


substrate_name: caldariellaquinol

substrate: caldariellaquinol


enzyme_display_name: propionyl-CoA carboxylase

organism: Bos taurus

substrate_name: propanoyl-CoA

enzyme: propionyl-CoA carboxylase

substrate: propanoyl-CoA


substrate_name: Unknown

substrate: Unknown


substrate_name: decylubiquinone

substrate: decylubiquinone


column_label: Figure 5C reports WT Kcat 0.4 +/- 0.03 s^-1, Km 745 +/- 45 uM, Kcat/Km 0.53 mM^-1 s^-1; kcat and Km match, but kcat/Km differs from the current export

normalized_value_unit_evidence: Km normalized_value=0.745 normalized_unit=mM; kcat normalized_value=0.4 normalized_unit=s^-1; kcat_over_km normalized_value=0.53 normalized_unit=s^-1*mM^-1; current_export_kcat_over_km=0.5369127516778524 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=745 +/- 45 raw_unit=uM; kcat raw_value=0.4 +/- 0.03 raw_unit=s^-1; kcat_over_km raw_value=0.53 raw_unit=mM^-1*s^-1 for WT PccBBs

row_label: Figure 5C WT column; Kcat, Km, and Kcat/Km rows

table_label: PMID 32860966 ScienceDirect Figure 5C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N220I/I391T to reconstruct the assayed variant sequence.


organism: Neomoorella thermoacetica


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: oxidized 2,6-dichlorophenolindophenol

substrate: oxidized 2,6-dichlorophenolindophenol


substrate_name: NADH

substrate: NADH


assay_conditions_summary: pH 6; 303.15 K; cofactor NADH


substrate_name: NADPH

assay_conditions_summary: pH 6; 303.15 K; cofactor NADPH

substrate: NADPH


organism: Plasmodium falciparum


substrate_name: oxidized dichlorophenolindophenol

substrate: oxidized dichlorophenolindophenol


substrate_name: menadione

substrate: menadione


organism: Corynebacterium glutamicum

assay_conditions_summary: pH 7


assay_conditions_summary: pH 7; cofactor NADH


organism: Mycobacterium tuberculosis

substrate_name: menaquinone

proof_lines: pH 7.0, temperature not specified in the publication

substrate: menaquinone


proof_lines: cosubstrate ubiquinone-2, pH 7.0, temperature not specified in the publication

proof_lines: cosubstrate ubiquinone-0, pH 7.0, temperature not specified in the publication

proof_lines: cosubstrate menaquinone, pH 7.0, temperature not specified in the publication


organism: Paracoccus denitrificans

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

proof_lines: uncoupled oxidase reaction, pH 8.0, 25°C


substrate_name: coenzyme Q1

substrate: coenzyme Q1


substrate_name: NAD+

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines: pH 8.0, 25°C, succinate supported NAD+ reduction

substrate: NAD+


proof_lines:
pH 8.0, 25°C, NADH oxidase reaction
pH 8.0, 25°C, NAD+ reduction
pH 8.0, 25°C


organism: Aeropyrum pernix

substrate_name: ferrocytochrome c

substrate: ferrocytochrome c


smiles: O=O


organism: Rhodobacter capsulatus


organism: Aquifex aeolicus

assay_conditions_summary: cofactor NADH


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH

proof_lines: enzyme activated before assay, electron acceptor: ferricyanide

proof_lines: enzyme activated before assay, electron acceptor: ubiquinone-1


assay_conditions_summary: cofactor NADPH


substrate_name: naphthoquinone

substrate: naphthoquinone


substrate_name: benzoquinone

substrate: benzoquinone


organism: Methylococcus capsulatus


substrate_name: coenzyme Q10

substrate: coenzyme Q10


substrate_name: duroquinone

substrate: duroquinone


proof_lines: pH 6.5, 40°C, enzyme in detergent micelle (dodecyl-beta-D-maltoside)

proof_lines: pH 6.5, 40°C, enzyme in liposomes (tetraether lipids)


substrate_name: caldariellaquinol

proof_lines: pH 6.5, 50°C, enzyme in liposomes (tetraether lipids)

proof_lines: pH 6.5, 50°C, enzyme in detergent micelle (dodecyl-beta-D-maltoside)

substrate: caldariellaquinol


enzyme_display_name: menaquinol oxidase (H(+)-transporting)

substrate_name: dimethylnitrosamine

smiles: CN(C)N=O

enzyme: menaquinol oxidase (H(+)-transporting)

substrate: dimethylnitrosamine


substrate_name: hexaammineruthenium-III-chloride

substrate: hexaammineruthenium-III-chloride


organism: Thermoplasma acidophilum


substrate_name: Unknown

substrate: Unknown


proof_lines:
using decylubiquinone as substrate
using ubiquinone-1 as substrate


organism: Mycolicibacterium smegmatis


organism: Saccharomyces cerevisiae

substrate_name: oxidized 2,6-dichlorophenolindophenol

substrate: oxidized 2,6-dichlorophenolindophenol


substrate_name: menadiol

substrate: menadiol


substrate_name: NADH

proof_lines: with ubiquinone-6 as acceptor, Triton assay medium

proof_lines: with ubiquinone-6 as acceptor, mitochondria

substrate: NADH


organism: Bacillus subtilis

substrate_name: O2; 2,3-Dimethylnaphthalene-1,4-diol

substrate: O2; 2,3-Dimethylnaphthalene-1,4-diol


assay_conditions_summary: pH 7; 298.15 K; buffer phosphate

proof_lines: in phosphate buffer, pH 6.5, containing 0.5 mg/ml lauryl maltoside, temperature not specified in the publication


organism: Acidianus ambivalens


enzyme_display_name: quinol--cytochrome-c reductase

organism: Helianthus tuberosus

enzyme: quinol--cytochrome-c reductase


organism: Trichormus variabilis

substrate_name: 2 ferricytochrome c1

substrate: 2 ferricytochrome c1


substrate_name: Gln

substrate: Gln


substrate_name: Asn

substrate: Asn


organism: Rhodospirillum rubrum


enzyme_display_name: ubiquinol oxidase (electrogenic, proton-motive force generating)

organism: Escherichia coli (strain K12)


enzyme: ubiquinol oxidase (electrogenic, proton-motive force generating)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I269M to reconstruct the assayed variant sequence.


enzyme_display_name: cytochrome-c oxidase

organism: Cereibacter sphaeroides

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E157Q/E254A to reconstruct the assayed variant sequence.

proof_lines: Rhodobacter sphaeroides cytochrome c, E157Q and E254A mutant enzyme

enzyme: cytochrome-c oxidase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E157Q to reconstruct the assayed variant sequence.

proof_lines: horse cytochrome c, E157Q and E254Amutant enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E148Q to reconstruct the assayed variant sequence.

proof_lines: Rhodobacter sphaeroides cytochrome c, E148Q mutant enzyme


organism: Homo sapiens

substrate_name: decylubiquinone

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

substrate: decylubiquinone


column_label: Preserved note reports Table 3 KM for CoQ1 and decylubiquinone (DQ), Healthy control 1 = 55 uM.

raw_value_unit_evidence: Km raw_value=55 raw_unit=uM

row_label: Healthy control 1 complex I / CoQ1 (ubiquinone-1)

table_label: Preserved full-text Table 3 evidence from current verified_catlog note


substrate_name: ferrocytochrome c

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature R54M to reconstruct the assayed variant sequence.

substrate: ferrocytochrome c


organism: Paramagnetospirillum magnetotacticum

substrate_name: ferrocytochrome c550

proof_lines: Magnetospirillum magnetotacticum cytochrome c550

substrate: ferrocytochrome c550


organism: Yarrowia lipolytica

substrate_name: n-decylubiquinone

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature S416P to reconstruct the assayed variant sequence.

substrate: n-decylubiquinone


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature S416A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature R211W with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.


enzyme_display_name: ubiquinol oxidase (H(+)-transporting)

enzyme: ubiquinol oxidase (H(+)-transporting)


enzyme_display_name: plastoquinol--plastocyanin reductase

organism: Chlamydomonas reinhardtii

substrate_name: cytochrome f

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

enzyme: plastoquinol--plastocyanin reductase

substrate: cytochrome f


organism: Spinacia oleracea


enzyme_display_name: DNA ligase (ATP)

organism: Ferroplasma acidiphilum

substrate_name: (deoxyribonucleotide)n

sequence_source: uniprot

sequence_variant_note: Resolved canonical sequence from uniprot and applied mutation signature E143L with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

enzyme: DNA ligase (ATP)

substrate: (deoxyribonucleotide)n


sequence_variant_note: Resolved canonical sequence from uniprot and applied mutation signature T491S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot and applied mutation signature N255G to reconstruct the assayed variant sequence.


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


substrate_name: decylubiquinol

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S183A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

substrate: decylubiquinol


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S183T with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


organism: Thermus thermophilus

assay_conditions_summary: pH 7.5; cofactor NADH


substrate_name: menadione

substrate: menadione


organism: Escherichia coli

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


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

proof_lines:
wild type enzyme, at pH 7.0 and 25°C
wild type enzyme, at 37°C, pH 7.0


organism: Geobacillus thermodenitrificans

substrate_name: reduced cytochrome c551

proof_lines: mutant enzyme E116Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8

substrate: reduced cytochrome c551


proof_lines: mutant enzyme D99N, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8


proof_lines: mutant enzyme E66Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8


proof_lines: mutant enzyme D49N, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8


proof_lines: mutant enzyme E68Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8


proof_lines: wild type enzyme, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8


proof_lines: mutant enzyme E139Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8


proof_lines: mutant enzyme E64Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8


proof_lines: mutant enzyme E84Q, at 40°C, 200 mM KCl, 1 mM MgSO4, 1 mM sodium phosphate buffer, pH 6.8


organism: Saccharomyces cerevisiae


proof_lines: pH 7.0, 23°C, wild-type enzyme and mutant F278I


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D36V with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


proof_lines: Rhodobacter sphaeroides cytochrome c, W143A mutant enzyme


proof_lines: Rhodobacter sphaeroides cytochrome c, W143F mutant enzyme


proof_lines: Rhodobacter sphaeroides cytochrome c, D229N mutant enzyme


proof_lines: Rhodobacter sphaeroides cytochrome c, D195Q mutant enzyme


proof_lines: Rhodobacter sphaeroides cytochrome c, D214N mutant enzyme


proof_lines: Rhodobacter sphaeroides cytochrome c, D151N/E152Q mutant enzyme

proof_lines: horse cytochrome c, D151N/E152Q mutant enzyme


proof_lines: Rhodobacter sphaeroides cytochrome c, D188N/E189Q mutant enzyme

proof_lines: horse cytochrome c, D188N/E189Q mutant enzyme


proof_lines: Rhodobacter sphaeroides cytochrome c, wild-type enzyme

proof_lines: wild-type enzyme, horse cytochrome c, 155 mM ionic strength

proof_lines: wild-type enzyme, horse cytochrome c, 5 mM ionic strength


proof_lines: horse cytochrome c, D214N and D229N mutant enzyme


organism: Bos taurus

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+

proof_lines:
pH 7.0, 25°C
pH 8.0, 26°C
pH 8.0, 25°C, NADH oxidase reaction


substrate_name: coenzyme Q0

substrate: coenzyme Q0


substrate_name: coenzyme Q1

substrate: coenzyme Q1


organism: Beta vulgaris


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: Unknown

substrate: Unknown


organism: Micrococcus luteus


substrate_name: diaminodurene

substrate: diaminodurene


substrate_name: phenazine methosulfate

proof_lines: ascorbate/phenazine methosulfate assay system

substrate: phenazine methosulfate


proof_lines: wild type enzyme, when Triton X-100 is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C

proof_lines: wild type enzyme, when 0.02% (v/v) n-dodecyl beta-D-maltoside is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C


proof_lines: mutant enzyme Q101N, when Triton X-100 is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C

proof_lines: mutant enzyme Q101N, when 0.02% (v/v) n-dodecyl beta-D-maltoside is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C


proof_lines: mutant enzyme H98N, when 0.02% (v/v) n-dodecyl beta-D-maltoside is used as detergent in the isolation of the enzyme, in 50 mM Tris-HCl, pH 7.4, at 25°C


organism: Rhodopseudomonas palustris

substrate_name: horse heart cytochrome c

substrate: horse heart cytochrome c


substrate_name: cytochrome c2

proof_lines:
MgCl2 20 mM
MgCl2 5 mM

substrate: cytochrome c2


substrate_name: ubiquinol

substrate: ubiquinol


substrate_name: 2 ferricytochrome c

substrate: 2 ferricytochrome c


enzyme_display_name: H(+)-transporting two-sector ATPase

organism: Bacillus PS3

substrate_name: ATP; H2O

assay_conditions_summary: cofactor ATP

enzyme: H(+)-transporting two-sector ATPase

substrate: ATP; H2O


organism: Bacillus subtilis


organism: Streptococcus mutans


enzyme_display_name: P-type H(+)-exporting transporter

substrate_name: H+; ATP; H2O

enzyme: P-type H(+)-exporting transporter

substrate: H+; ATP; H2O


substrate_name: ATP

substrate: ATP


enzyme_display_name: H(+)-exporting diphosphatase

organism: Kalanchoe daigremontiana

substrate_name: H+[side 1]

enzyme: H(+)-exporting diphosphatase

substrate: H+[side 1]


substrate_name: diphosphate

substrate: diphosphate


organism: Avena sativa


substrate_name: K+

substrate: K+


organism: Streptococcus sanguis


organism: Thermosynechococcus vestitus

substrate_name: reduced ferredoxin [iron-sulfur] cluster

proof_lines: pH and temperature not specified in the publication, surface plasmon resonance measurement


organism: Amaranthus hybridus

assay_conditions_summary: pH 7.6; 294.15 K; cofactor NADH

proof_lines: NADH/ferredoxin:plastoquinone reductase activity, pH 7.6, 21°C


organism: Cereibacter sphaeroides

substrate_name: ferrocytochrome c

proof_lines: reconstituted recombinant D407C mutant enzyme

substrate: ferrocytochrome c


proof_lines: reconstituted recombinant D407A mutant enzyme


proof_lines: reconstituted recombinant D407N mutant enzyme


organism: Vibrio cholerae serotype O1

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D397S to reconstruct the assayed variant sequence.

proof_lines: mutant D397S, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+

proof_lines: mutant D397S, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D397K to reconstruct the assayed variant sequence.

proof_lines: mutant D397K, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+

proof_lines: mutant D397K, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D397N to reconstruct the assayed variant sequence.

proof_lines: mutant D397N, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+

proof_lines: mutant D397N, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D397C to reconstruct the assayed variant sequence.

proof_lines: mutant D397C, presence of 2-mercaptoethanol, pH 8.0, temperature not specified in the publication

proof_lines: mutant D397C, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D397E to reconstruct the assayed variant sequence.

proof_lines: mutant D397E, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+

proof_lines: mutant D397E, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D397A to reconstruct the assayed variant sequence.

proof_lines: mutant D397A, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+

proof_lines: mutant D397A, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+


substrate_name: NADH

assay_conditions_summary: pH 8; cofactor NADH

proof_lines: mutant D397K, pH 8.0, temperature not specified in the publication

substrate: NADH


proof_lines: mutant D397C, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+


proof_lines: mutant D397S, pH 8.0, temperature not specified in the publication


proof_lines: mutant D397E, pH 8.0, temperature not specified in the publication


proof_lines: mutant D397N, pH 8.0, temperature not specified in the publication


proof_lines: mutant D397A, pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S716A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 5.7; 303.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D720C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N715A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D720A to reconstruct the assayed variant sequence.

proof_lines:
mutant D720A, 30°C, pH 5.7
mutant D720A, pH 5.7, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D720E to reconstruct the assayed variant sequence.

proof_lines:
mutant D720E, 30°C, pH 5.7
mutant D720E, pH 5.7, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D714N to reconstruct the assayed variant sequence.

proof_lines:
mutant D714N, 30°C, pH 5.7
mutant D714N, pH 5.7, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D720N to reconstruct the assayed variant sequence.

proof_lines:
mutant D720N, 30°C, pH 5.7
mutant D720N, pH 5.7, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S716C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I719A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D718A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I719C to reconstruct the assayed variant sequence.


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

proof_lines:
wild-type, 30°C, pH 5.7
wild-type, pH 5.7, 30°C
wild type enzyme, at pH 5.7 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N715C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D718C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature G141L to reconstruct the assayed variant sequence.

proof_lines: NqrB, mutant G141L, pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature G141A to reconstruct the assayed variant sequence.

proof_lines: NqrB, mutant G141A, pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature G141V to reconstruct the assayed variant sequence.

proof_lines: NqrB, mutant G141V, pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D720V to reconstruct the assayed variant sequence.


organism: Vibrio harveyi

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C377A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


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

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines: enzyme in vesicles from pH 7.0-grown cells, pH and temperature not specified in the publication

proof_lines: enzyme in vesicles from pH 5.0-grown cells, pH and temperature not specified in the publication


organism: Ascaris suum


organism: Saccharomyces cerevisiae


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N715A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D720A to reconstruct the assayed variant sequence.

proof_lines:
mutant D720A, pH 5.7, 30°C
mutant D720A, 30°C, pH 5.7


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D720C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D714N to reconstruct the assayed variant sequence.


proof_lines:
wild-type, 30°C, pH 5.7
wild-type, pH 5.7, 30°C


substrate_name: ubiquinone

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature G140A to reconstruct the assayed variant sequence.

proof_lines: above, mutant NqrB-G140A, pH 8.0, temperature not specified in the publication

substrate: ubiquinone


substrate_name: n Li+/in

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D397E to reconstruct the assayed variant sequence.

substrate: n Li+/in


substrate_name: n Na+/in

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D397S to reconstruct the assayed variant sequence.

proof_lines: mutant D397S, pH 8.0, temperature not specified in the publication

substrate: n Na+/in


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D397N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D397C to reconstruct the assayed variant sequence.

proof_lines: mutant D397C, presence of 2-mercaptoethanol, pH 8.0, temperature not specified in the publication

proof_lines: mutant D397C, pH 8.0, temperature not specified in the publication


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D718A to reconstruct the assayed variant sequence.

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S716A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S716C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature G141A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature G141L to reconstruct the assayed variant sequence.


organism: Leishmania amazonensis

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


substrate_name: Triphosphate

substrate: Triphosphate


organism: Arabidopsis thaliana

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

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


organism: Bacillus sp. PS3

sequence_variant_note: Mutation signature P104A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature P100A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P146A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature P14A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature P116A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature P43A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature P59A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


organism: Pneumocystis carinii

assay_conditions_summary: pH 6.5; cofactor ATP

proof_lines: wild-type lacking C-terminal 40 amino acids, pH 6.5


substrate_name: H2O; ATP

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

substrate: H2O; ATP


organism: Candida albicans (strain SC5314 / ATCC MYA-2876)

substrate_name: Mg(2+)-ATP at pH 6.5

substrate: Mg(2+)-ATP at pH 6.5


organism: Mus musculus

substrate_name: ATP; H2O; H+

substrate: ATP; H2O; H+


substrate_name: H2O; ATP; H+

substrate: H2O; ATP; H+


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

substrate_name: Mg-ATP

assay_conditions_summary: pH 6; cofactor ATP

column_label: Prose section 'Catalytic properties of the purified A1AO ATPase', PDF page 6 / article page 254; metric label KM; substrate Mg-ATP; raw value 1.2 +/- 0.2 mM.

raw_value_unit_evidence: Prose states: The KM value for Mg-ATP was determined to be 1.2 +/- 0.2 mM.

row_label: Purified A1AO ATPase from Methanococcus jannaschii; Mg-ATP substrate

table_label: Prose section: Catalytic properties of the purified A1AO ATPase

substrate: Mg-ATP


substrate_name: ATP

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

substrate: ATP


organism: Neurospora crassa


organism: Kluyveromyces lactis

assay_conditions_summary: pH 6.8; cofactor ATP


substrate_name: vanadate

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

substrate: vanadate


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


organism: Escherichia coli

substrate_name: ADP

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: recombinant wild-type F1Fo, pH 7.5-8.8, temperature not specified in the publication

substrate: ADP


substrate_name: phosphate

substrate: phosphate


proof_lines: recombinant subunit epsilon mutant EF1Fo, pH 7.5-8.8, temperature not specified in the publication


organism: Avena sativa


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M795A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 5.7; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L797A to reconstruct the assayed variant sequence.

proof_lines:
mutant L797A, pH 5.7, 30°C
mutant enzyme L797A, at pH 5.7 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E803A to reconstruct the assayed variant sequence.

proof_lines:
mutant E803A, pH 5.7, 30°C
mutant enzyme E803A, at pH 5.7 and 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F808A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G793E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W805A with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R811A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N792A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G793A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T802A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T810A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N792H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q798E with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N792Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M791A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N792D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S800A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I809A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N804A with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L806A to reconstruct the assayed variant sequence.


organism: Bos taurus

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


proof_lines: wild-type, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+

proof_lines: wild-type, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+


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

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


organism: Trichormus variabilis


proof_lines: wild type enzyme and histidine-tagged enzyme


assay_conditions_summary: pH 7; 296.15 K; cofactor ATP


organism: Aphanothece halophytica

assay_conditions_summary: pH 7.6; cofactor ATP

proof_lines: apparent value, recombinant enzyme, in 20 mM Tris-HCl, pH 7.6, 5mM MgCl2, 10 mM NaCl, temperature not specified in the publication


substrate_name: Na+/in

substrate: Na+/in


organism: Beta vulgaris

substrate_name: diphosphate

substrate: diphosphate


organism: Bacillus sp. (in: firmicutes)

assay_conditions_summary: 303.15 K; cofactor ATP

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


substrate_name: decylubiquinone

substrate: decylubiquinone


substrate_name: NADH

assay_conditions_summary: cofactor NADH

proof_lines:
nonenergy-linked reaction
cosubstrate NADP+
energy-linked reaction

substrate: NADH


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

proof_lines:
nonenergy-linked reaction
energy-linked reaction
cosubstrate NADPH

substrate: NAD+


substrate_name: DNA

proof_lines:
nicked DNA, enzyme DNA ligase II
nicked DNA 5'-phosphoryl ends
nicked DNA, enzyme DNA ligase I

substrate: DNA


proof_lines:
ATP
ATP, ATP-diphosphate exchange reaction
DNA ligase I


organism: Coprinopsis cinerea


substrate_name: ferricyanide

substrate: ferricyanide


assay_conditions_summary: pH 8; cofactor ATP

proof_lines:
pH 8, membrane-bound enzyme
pH 8, soluble enzyme


organism: Daucus carota

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


substrate_name: malonyl-CoA

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: pH 8.0, recombinant subunits AccA and AccD

substrate: malonyl-CoA


substrate_name: biocytin

assay_conditions_summary: pH 8

substrate: biocytin


substrate_name: biotin

proof_lines:
isolated biotin carboxylase domain
isolated carboxyltransferase domain

substrate: biotin


substrate_name: Unknown

assay_conditions_summary: pH 7.8; cofactor CoA

proof_lines: pH 7.8, temperature not specified in the publication

substrate: Unknown


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

assay_conditions_summary: 298.15 K; cofactor ATP

proof_lines: mutant enzyme E190Q, at 25°C, pH not specified in the publication


proof_lines: mutant enzyme K164A, at 25°C, pH not specified in the publication


proof_lines: mutant enzyme E190A, at 25°C, pH not specified in the publication


proof_lines: mutant enzyme R364A, at 25°C, pH not specified in the publication


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


enzyme_display_name: GMP synthase (glutamine-hydrolyzing)

substrate_name: XMP

assay_conditions_summary: pH 8; 313.15 K; cofactor ATP

proof_lines:
40°C, pH 8.0, NF-ATPP/DD
40°C, pH 8.0, His-ATPP/DD

enzyme: GMP synthase (glutamine-hydrolyzing)

substrate: XMP


assay_conditions_summary: cofactor ATP


substrate_name: H2O2[side 2]

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication

substrate: H2O2[side 2]


substrate_name: decylubiquinol

substrate: decylubiquinol


substrate_name: acetylpyridine adenine dinucleotide

substrate: acetylpyridine adenine dinucleotide


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


organism: Glycine max


substrate_name: ATP

substrate: ATP


organism: Helicobacter pylori

substrate_name: ferrocytochrome c553

substrate: ferrocytochrome c553


organism: Geobacillus stearothermophilus

substrate_name: L-Gln

proof_lines: arginine specific carbamoyl-phosphate synthase

proof_lines: carbamoyl-phosphate synthase belonging to the arginine pathway

substrate: L-Gln


proof_lines: carbamoyl-phosphate synthase belonging to the pyrimidine pathway


organism: Herbaspirillum seropedicae

substrate_name: deamido-NAD+

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NAD+

proof_lines: pH 8.5, 30°C, recombinant His-tagged enzyme

substrate: deamido-NAD+


assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP


organism: Vibrio cholerae serotype O1

substrate_name: ubiquinone

sequence_source: UniProtKB A5F5X0

sequence_variant_note: Resolved canonical sequence from UniProtKB A5F5X0 and applied mutation signature G140A to reconstruct the assayed variant sequence.

proof_lines: above, mutant G140A, pH 8.0, temperature not specified in the publication

substrate: ubiquinone


proof_lines: mutant G140A, pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB A5F5X0 and applied mutation signature G140L to reconstruct the assayed variant sequence.

proof_lines: mutant G140L, pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB A5F5X0 and applied mutation signature G141V to reconstruct the assayed variant sequence.

proof_lines: mutant G141V, pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB A5F5X0 and applied mutation signature G141A to reconstruct the assayed variant sequence.

proof_lines: mutant G141A, pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB A5F5X0 and applied mutation signature G141L to reconstruct the assayed variant sequence.

proof_lines: mutant G141L, pH 8.0, temperature not specified in the publication


organism: Homo sapiens


substrate_name: L-glutamine

substrate: L-glutamine


organism: Klebsiella pneumoniae

substrate_name: acetyl-CoA

assay_conditions_summary: pH 8; 293.15 K; cofactor CoA

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

substrate: acetyl-CoA


assay_conditions_summary: pH 8; 293.15 K; cofactor ATP


enzyme_display_name: 2-oxoglutarate carboxylase

organism: Hydrogenobacter thermophilus

enzyme: 2-oxoglutarate carboxylase


assay_conditions_summary: pH 8.5; 293.15 K; cofactor ATP


enzyme_display_name: methylcrotonoyl-CoA carboxylase

organism: Hordeum vulgare

proof_lines:
pH 8.0, 37°C
experimental conditions not available

enzyme: methylcrotonoyl-CoA carboxylase


organism: Methylobacillus flagellatus KT

substrate_name: ferrocytochrome c

substrate: ferrocytochrome c


organism: Medicago sativa

substrate_name: Gln

substrate: Gln


enzyme_display_name: acetyl-CoA carboxylase

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

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: in 50 mM HEPES (pH 7.5), 2.0 mM MgCl2, 2.0 mM ATP, 2.0 mM potassium citrate, 12.5 mM sodium bicarbonate, 1 mg/ml bovine serum albumin, and 0.005 mM acetyl-CoA, at 25°C

enzyme: acetyl-CoA carboxylase


assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA


organism: Mus musculus

substrate_name: DNA

substrate: DNA


organism: Lathyrus oleraceus


assay_conditions_summary: cofactor CoA


organism: Mycolicibacterium smegmatis

substrate_name: propanoyl-CoA

substrate: propanoyl-CoA


organism: Methanothermobacter thermautotrophicus


substrate_name: dATP

substrate: dATP


organism: Pseudomonas aeruginosa


enzyme_display_name: pyruvate carboxylase

organism: Phycomyces blakesleeanus

substrate_name: pyruvate

enzyme: pyruvate carboxylase

substrate: pyruvate


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

organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: pH and temperature not specified in the publication

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


substrate_name: Unknown

substrate: Unknown


organism: Rattus norvegicus


enzyme_display_name: propionyl-CoA carboxylase

organism: Rhizobium etli

enzyme: propionyl-CoA carboxylase


substrate_name: butyryl-CoA

substrate: butyryl-CoA


enzyme_display_name: magnesium chelatase

organism: Rhodobacter capsulatus

assay_conditions_summary: 303.15 K; cofactor ATP

enzyme: magnesium chelatase


organism: Psychromonas sp. SP041

substrate_name: (nicked double-stranded DNA)n

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

substrate: (nicked double-stranded DNA)n


substrate_name: thio-NADP+

assay_conditions_summary: pH 6.3; cofactor NADP+

proof_lines:
pH 6.3, in the light
pH 7.6, in the light
pH 7.6, in the dark

substrate: thio-NADP+


substrate_name: NADH

assay_conditions_summary: pH 6.3; cofactor NADH

proof_lines:
pH 6.3, in the light
pH 6.3, in the dark
pH 7.6, in the light

substrate: NADH


organism: Neisseria meningitidis

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


substrate_name: ATP

substrate: ATP


organism: Saccharomyces cerevisiae


substrate_name: malonyl-CoA

assay_conditions_summary: pH 8; cofactor CoA

substrate: malonyl-CoA


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


enzyme_display_name: quinol--cytochrome-c reductase

enzyme: quinol--cytochrome-c reductase


enzyme_display_name: DNA ligase (NAD(+))

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: 5'-phosphate terminus of deoxyribonucleotides

enzyme: DNA ligase (NAD(+))


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R656E to reconstruct the assayed variant sequence.

proof_lines: mutant R656E, pH 7.5, temperature not specified in the publication


proof_lines: wild-type, pH 7.5, temperature not specified in the publication


organism: Staphylococcus aureus

proof_lines: pH 8.0, recombinant subunits AccA and AccD


substrate_name: biocytin

assay_conditions_summary: pH 8

substrate: biocytin


substrate_name: acridinium-ester labelled DNA

substrate: acridinium-ester labelled DNA


assay_conditions_summary: pH 7.4; 294.15 K; cofactor NAD+


organism: Solanum tuberosum

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA


organism: Streptococcus pneumoniae

assay_conditions_summary: pH 8; 294.15 K; cofactor NAD+


organism: Sus scrofa


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


organism: Synechocystis sp.

substrate_name: deuteroporphyrin IX

substrate: deuteroporphyrin IX


assay_conditions_summary: cofactor ATP


organism: Thermosynechococcus vestitus

assay_conditions_summary: pH 7.7; 318.15 K; cofactor ATP


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: pH 8.0, 30°C, recombinant mutant epsilonDELTAC, ATP hydrolysis


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


organism: Trypanosoma brucei

substrate_name: Polyphosphate

proof_lines: hydrolysis of diphosphate, pH 7.5, 25°C, no inhibition of tripolyphosphate and polyphosphate hydrolysis

substrate: Polyphosphate


substrate_name: diphosphate

proof_lines:
in the presence of Zn2+, pH 7.5, 25°C
in the presence of Mg2+, pH 7.5, 25°C

substrate: diphosphate


organism: Vibrio cholerae serotype O1

substrate_name: ubiquinone

substrate: ubiquinone


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


organism: Vigna radiata


organism: Zea mays

proof_lines:
non-mesophyll chloroplast isoform
plastidic enzyme, pH 8.0, 30°C
cytosolic enzyme, pH 8.0, 30°C


substrate_name: acetyl-CoA

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines:
mesophyll chloroplast isoform
non-mesophyll chloroplast isoform
cytosolic enzyme, pH 8.0, 30°C

substrate: acetyl-CoA


organism: Acetabularia acetabulum


organism: Acidithiobacillus ferrooxidans

assay_conditions_summary: pH 8.5; 313.15 K; cofactor ATP


enzyme_display_name: cytochrome-c oxidase

substrate_name: ferrocytochrome c552

enzyme: cytochrome-c oxidase

substrate: ferrocytochrome c552


organism: Wolbachia endosymbiont of Brugia malayi

substrate_name: deoxyribonucleotide

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

column_label: Results prose reports a Km of 0.193 uM for wBm-LigA using the nicked substrate.

raw_value_unit_evidence: Km raw_value=0.193 uM raw_unit=uM

row_label: Nicked DNA substrate Km

table_label: PMC3397958 Results prose / Figure 5

substrate: deoxyribonucleotide


assay_conditions_summary: pH 8; cofactor NAD+

column_label: Results prose reports a Km of 4.8 uM for NAD+ obtained for wBm-LigA.

raw_value_unit_evidence: Km raw_value=4.8 uM raw_unit=uM

row_label: NAD+ cofactor Km


organism: Aedes aegypti

substrate_name: ferrocytochrome c

assay_conditions_summary: 301.15 K; cofactor ADP

proof_lines: 28°C, pH not specified in the publication

proof_lines: 28°C, presence of 3 mM ADP, pH not specified in the publication

substrate: ferrocytochrome c


organism: Alkalithermobacter thermoalcaliphilus

assay_conditions_summary: pH 7; cofactor ATP

proof_lines: purified enzyme stimulated with Na+ at pH 7.0 and 9.0

proof_lines: purified enzyme, Mg2+/ATP ratio maintained at 2:1


organism: Agrobacterium tumefaciens

assay_conditions_summary: cofactor NADPH


organism: Arabidopsis thaliana


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


organism: Ancylobacter novellus

proof_lines: Thiobacillus novellus cytochrome c, 12.5 mM phosphate at pH 5.5 and 20°C

proof_lines: Candida krusei cytochrome c, 30 mM phosphate at pH 5.5 and 20°C


organism: Bacillus sp. (in: firmicutes)


organism: Bacillus subtilis

proof_lines: Saccharomyces cerevisiae cytochrome c, in the presence of 0.05% laurylmaltoside

proof_lines: Saccharomyces cerevisiae cytochrome c, in the presence of asolectin

proof_lines: in the presence of 0.1% dodecyl-beta-D-maltoside


organism: Paracoccus denitrificans

substrate_name: 2 ferricytochrome c

mutation_signature: with truncated cytochrome c1

mutation_type: truncation

proof_lines: mutant with truncated cytochrome c1, membrane fraction

proof_lines: mutant with truncated cytochrome c1, purified bc1 complex

substrate: 2 ferricytochrome c


proof_lines:
wild type, membrane fraction
wild type, purified bc1 complex
wild-type protein


organism: Bos taurus

substrate_name: deamino-NADH

assay_conditions_summary: pH 8; 299.15 K; cofactor NADH

substrate: deamino-NADH


organism: Bacteria

proof_lines: soluble enzyme, higher values for particulate enzyme

proof_lines: from Thermus thermophilus, bacterial enzyme

proof_lines: from thermophilic bacterium PS3, bacterial enzyme


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines: pH 8.0, 25°C, succinate supported NAD+ reduction