organism: Glycine max


enzyme_display_name: chalcone isomerase

source_db: brenda

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

proof_lines:
pH 8, 20°C
methanethiolated enzyme
native enzyme

enzyme: chalcone isomerase

source: brenda


enzyme_display_name: muconate cycloisomerase

organism: Pseudomonas sp.

substrate_name: cis,cis-muconate

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

mutation_type: substitution

enzyme: muconate cycloisomerase

substrate: cis,cis-muconate


km_display: Not reported


kcat_display: Not reported


organism: Adiantum capillus-veneris

substrate_name: isoliquiritigenin

substrate: isoliquiritigenin


substrate_name: naringenin chalcone

substrate: naringenin chalcone


organism: Agrobacterium tumefaciens


enzyme_display_name: inositol-3-phosphate synthase

organism: Homo sapiens

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

enzyme: inositol-3-phosphate synthase

substrate: NAD+


substrate_name: glucose 6-phosphate

substrate: glucose 6-phosphate


organism: Pseudomonas putida

verification_status: unverified

status: unverified


proof_lines: pH 7.5, 25°C, mutant enzyme A271S or I54V/F329


substrate_name: D-glucose 6-phosphate

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

proof_lines: presence of 0.6 mM valnoctamide, pH 7.6, 37°C

substrate: D-glucose 6-phosphate


substrate_name: Unknown

ki_unit: mM

proof_lines:
pH 7.6, 37°C
brain, post mortem

substrate: Unknown


organism: Medicago sativa


organism: Oryza sativa

proof_lines:
chloroplastic enzyme
cytosolic enzyme


proof_lines:
cytosolic enzyme
chloroplastic enzyme


organism: Oryza coarctata


organism: Oryza sativa Japonica Group

proof_lines: at pH 7.5, temperature not specified in the publication


substrate_name: muconolactone

substrate: muconolactone


organism: Archaeoglobus fulgidus

protein_accession_database: UniProt

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

data_origin: experimental


assay_conditions_summary: pH 7.5; cofactor NAD+


proof_lines: mutant bearing amino acids 174-210 of Porteresia coarctata enzyme, 37°C


organism: Pseudomonas reinekei


enzyme_display_name: dichloromuconate cycloisomerase

organism: Cupriavidus necator

assay_conditions_summary: pH 8

enzyme: dichloromuconate cycloisomerase


smiles: C(=C(C=C(C(=O)O)Cl)Cl)C(=O)O


enzyme_display_name: (+)-bornyl diphosphate synthase

organism: Tanacetum vulgare

substrate_name: geranyl diphosphate

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

enzyme: (+)-bornyl diphosphate synthase

substrate: geranyl diphosphate


substrate_name: (+)-(3S)-linalyl diphosphate

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

substrate: (+)-(3S)-linalyl diphosphate


enzyme_display_name: cycloeucalenol cycloisomerase

organism: Zea mays

substrate_name: cycloeucalenol

enzyme: cycloeucalenol cycloisomerase

substrate: cycloeucalenol


enzyme_display_name: ent-copalyl diphosphate synthase

organism: Cucurbita maxima

substrate_name: geranylgeranyl diphosphate

enzyme: ent-copalyl diphosphate synthase

substrate: geranylgeranyl diphosphate


enzyme_display_name: alpha-pinene-oxide decyclase

organism: Nocardia sp.

substrate_name: alpha-Pinene oxide

enzyme: alpha-pinene-oxide decyclase

substrate: alpha-Pinene oxide


enzyme_display_name: copalyl diphosphate synthase

organism: Abies grandis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T769G to reconstruct the assayed variant sequence.

enzyme: copalyl diphosphate synthase


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


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

proof_lines:
wild-type
wild-type, D405A, Y520A


sequence_variant_note: Resolved canonical sequence from brenda_getSequence_unique_ec_organism and applied mutation signature D405N/Y520A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from brenda_getSequence_unique_ec_organism and applied mutation signature D402N/R365A/R454A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from brenda_getSequence_unique_ec_organism and applied mutation signature R411A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from brenda_getSequence_unique_ec_organism and applied mutation signature W358A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from brenda_getSequence_unique_ec_organism and applied mutation signature D405N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from brenda_getSequence_unique_ec_organism and applied mutation signature D361A to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation context was captured, but conflicting substitutions targeted the same residue position.


sequence_variant_note: Resolved canonical sequence from brenda_getSequence_unique_ec_organism and applied mutation signature E499A/R411A/R365A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from brenda_getSequence_unique_ec_organism and applied mutation signature D404A to reconstruct the assayed variant sequence.


substrate_name: CPP (in presence of magnesium)

source_db: uniprot

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

substrate: CPP (in presence of magnesium)

source: uniprot


enzyme_display_name: terpentedienyl-diphosphate synthase

organism: Kitasatospora griseola

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

enzyme: terpentedienyl-diphosphate synthase


organism: Salvia officinalis


organism: Arabidopsis thaliana

substrate_name: (E,E,E)-geranylgeranyl diphosphate

source_db: oed

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D503A to reconstruct the assayed variant sequence.

substrate: (E,E,E)-geranylgeranyl diphosphate

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E211A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N425A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N425H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R340A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T421A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T421S to reconstruct the assayed variant sequence.


verification_status: verified

assay_conditions_summary: pH 7.8; 295.15 K; buffer of 50 mM HEPES pH 7

column_label: Table 2 (Steady-State Kinetic Parameters for CPS Mutants), enzyme-form row 'Wild-type'; column 'kcat (s^-1)' = 0.9; column 'KM (uM)' = 3; column 'kcat/KM (M^-1 s^-1)' = 3 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.9 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.9 s^(-1). Km: printed Table 2 cell 3 uM; 3 / 1000 = 0.003 mM; the exported value is 0.003 mM. kcat/Km: printed Table 2 cell 3 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 300000 / 1000 = 300.0 s^-1 mM^-1; the exported value is 300.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row Wild-type: kcat = 0.9 s^-1; KM = 3 uM; printed kcat/KM = 3 x 10^5 M^-1 s^-1.

row_label: Table 2, row Wild-type

table_label: Table 2: Steady-State Kinetic Parameters for CPS Mutants (Biochim Biophys Acta 2014, 1840(1))

status: verified


organism: Phaeosphaeria sp.

substrate_name: copalyl diphosphate

substrate: copalyl diphosphate


organism: Talaromyces verruculosus

substrate_name: DMAPP (for prenyltransferase activity)

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

substrate: DMAPP (for prenyltransferase activity)


substrate_name: IPP (for prenyltransferase activity)

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

substrate: IPP (for prenyltransferase activity)


source_db: skid

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

sequence_source: multiple

source_databases_merged: skid uniprot

source: skid


substrate_name: farnesyl diphosphate

substrate: farnesyl diphosphate


source_databases_merged: brenda uniprot


substrate_name: Geranyl diphosphate

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

substrate: Geranyl diphosphate


organism: Agrobacterium tumefaciens

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


proof_lines: pH 7.5, 30°C, periodate assay method, in absence of 1 mM Mg2+

proof_lines: pH 7.5, 30°C, periodate assay method, in presence of 1 mM Mg2+

proof_lines: pH 7.5, 30°C, IMP-coupled assay method, in presence of 1 mM Mg2+


enzyme_display_name: prosolanapyrone-III cycloisomerase

organism: Saccharopolyspora spinosa

proof_lines: pH and temperature not specified in the publication

enzyme: prosolanapyrone-III cycloisomerase


enzyme_display_name: (-)-bornyl diphosphate synthase

organism: Blumea balsamifera

enzyme: (-)-bornyl diphosphate synthase


enzyme_display_name: UniProt P34808

organism: Caenorhabditis elegans

substrate_name: ATP

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P34808

substrate: ATP


enzyme_display_name: aklanonic acid methyl ester cyclase

organism: Streptomyces galilaeus

substrate_name: nogalonic acid methyl ester

proof_lines: kcat is 1 sec(-1) for cyclization with nogalonic acid methyl ester.

enzyme: aklanonic acid methyl ester cyclase

substrate: nogalonic acid methyl ester


substrate_name: (-)-(3R)-linalyl diphosphate

column_label: Table I row (+)-BPP cyclase (sage) / (3R)-LPP, Km column: 0.7 uM.

raw_value_unit_evidence: Table I reports (3R)-LPP Km 0.7 uM for (+)-BPP cyclase from sage.

row_label: (3R)-LPP for (+)-BPP cyclase from sage

table_label: Table I

substrate: (-)-(3R)-linalyl diphosphate


organism: Alternaria solani

substrate_name: Prosolanapyrone II; O2

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

substrate: Prosolanapyrone II; O2


enzyme_display_name: halimadienyl-diphosphate synthase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: Unknown

enzyme: halimadienyl-diphosphate synthase

substrate: Unknown


organism: Streptomyces peucetius


enzyme_display_name: lycopene beta-cyclase

organism: Paracoccus haeundaensis

substrate_name: lycopene

assay_conditions_summary: pH 6.5; cofactor NADPH

enzyme: lycopene beta-cyclase

substrate: lycopene


assay_conditions_summary: pH 7.8; 303.15 K; buffer of 50 mM HEPES pH 7


enzyme_display_name: microtubule-severing ATPase

assay_conditions_summary: pH 8; 301.15 K; cofactor ATP

proof_lines: pH 8.0, 28°C, MEI-1 WT/MEI-2 wild-type enzyme

enzyme: microtubule-severing ATPase


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

proof_lines: pH 8.0, 28°C, mutant enzyme MEI-1 K293Q/MEI-2


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature K239A with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 28°C, mutant enzyme MEI-1 K239A/MEI-2


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E29D with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: mutant E29D, 30°C, pH not specified in the publication, Vmax: 0.24 nmol/h/mg


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D260H with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: mutant D260H, 30°C, pH not specified in the publication, Vmax: 0.35 nmol/h/mg


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E29H with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: mutant E29H, 30°C, pH not specified in the publication, Vmax: 0.33 nmol/h/mg


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W112L with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

proof_lines: mutant W112L, 30°C, pH not specified in the publication, Vmax: 14.7 nmol/h/mg


proof_lines: wild-type, 30°C, pH not specified in the publication, Vmax: 22 nmol/h/mg


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

proof_lines: mutant F111L, 30°C, pH not specified in the publication, Vmax: 4.7 nmol/h/mg


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D260E with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: mutant D260E, 30°C, pH not specified in the publication, Vmax: 44 nmol/h/mg


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T113S with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

proof_lines: mutant T113S, 30°C, pH not specified in the publication, Vmax: 26 nmol/h/mg


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

proof_lines: mutant F117L, 30°C, pH not specified in the publication, Vmax: 5.3 nmol/h/mg


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +6, so it is treated as a source-provided variant sequence.

proof_lines: mutant G108A, 30°C, pH not specified in the publication, Vmax: 11.4 nmol/h/mg


proof_lines: mutant T113A, 30°C, pH not specified in the publication, Vmax: 4.9 nmol/h/mg


organism: Tanacetum vulgare

substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


substrate_name: (+)-(3S)-linalyl diphosphate

substrate: (+)-(3S)-linalyl diphosphate


organism: Streptomyces sp.

substrate_name: geranylgeranyl diphosphate

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

substrate: geranylgeranyl diphosphate


organism: Homo sapiens

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

mutation_type: truncation

assay_conditions_summary: cofactor ATP

proof_lines: Kinetic parameters shown are for full-length enzyme. N-terminally truncated spastin (residues 228-616), which has been shown to exhibit full severing activity, shows a basal ATP turnover rate of 0.78 sec(-1) in the absence of microtubules,


enzyme_display_name: (+)-cis,trans-nepetalactol synthase

organism: Nepeta racemosa

substrate_name: cis-trans-nepetalactol (in the presence of NAD(+) at pH 8.0 and 25 degrees Celsius)

proof_lines: kcat is 0.148 sec(-1) with cis-trans-nepetalactol as substrate (in the presence of NAD(+) at pH 8.0 and 25 degrees Celsius). kcat is 0.32 sec(-1) with cis-cis-nepetalactol as substrate (in the presence of NAD(+) at pH 8.0 and 25 degrees Cel

enzyme: (+)-cis,trans-nepetalactol synthase


substrate_name: NAD(+) (in the presence of cis-trans-nepetalactol at pH 8.0 and 25 degrees Celsius)


substrate_name: H2O; ATP

substrate: H2O; ATP


organism: Mus musculus

substrate_name: ATP; H2O

substrate: ATP; H2O


organism: Citrullus lanatus

substrate_name: Lycopene

substrate: Lycopene


organism: Capsicum annuum

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: Prosolanapyrone II

substrate: Prosolanapyrone II


assay_conditions_summary: pH 6.8; 295.15 K; cofactor ATP


enzyme_display_name: (S)-beta-macrocarpene synthase

organism: Zea mays

substrate_name: farnesyl diphosphate

assay_conditions_summary: pH 7; buffer 100 uL assay

column_label: Table 1; row label: TPS6-B73; column label: FPP / Km column; raw value 2.1 uM; normalized value 0.0021 mM.

normalized_value_unit_evidence: Km=0.0021 mM after converting 2.1 uM from Table 1.

raw_value_unit_evidence: Table 1; TPS6-B73; FPP / Km column = 2.1 uM (footnote a).

row_label: TPS6-B73 table row / FPP / Km column

table_label: Table 1. Kinetic constants for TPS6-B73 heterologously expressed in E. coli

enzyme: (S)-beta-macrocarpene synthase


column_label: Table 1; row label: TPS6-B73; column label: GPP / Km column; raw value 1.1 uM; normalized value 0.0011 mM.

normalized_value_unit_evidence: Km=0.0011 mM after converting 1.1 uM from Table 1.

raw_value_unit_evidence: Table 1; TPS6-B73; GPP / Km column = 1.1 uM (footnote a).

row_label: TPS6-B73 table row / GPP / Km column


substrate_name: magnesium (in the presence of 10 uM farnesyl diphosphate)

smiles: [Mg]

assay_conditions_summary: pH 7; buffer assay

column_label: Table 1; row label: TPS6-B73; column label: Mg2+ / Km column; raw value 130.7 uM; normalized value 0.1307 mM.

normalized_value_unit_evidence: Km=0.1307 mM after converting 130.7 uM from Table 1.

raw_value_unit_evidence: Table 1; TPS6-B73; Mg2+ / Km column = 130.7 uM (footnote b).

row_label: TPS6-B73 table row / Mg2+ / Km column


substrate_name: manganese (in the presence of 10 uM farnesyl diphosphate)

smiles: [Mn]

column_label: Table 1; row label: TPS6-B73; column label: Mn2+ / Km column; raw value 23.4 uM; normalized value 0.0234 mM.

normalized_value_unit_evidence: Km=0.0234 mM after converting 23.4 uM from Table 1.

raw_value_unit_evidence: Table 1; TPS6-B73; Mn2+ / Km column = 23.4 uM (footnote b).

row_label: TPS6-B73 table row / Mn2+ / Km column


organism: Drosophila melanogaster

substrate_name: ATP

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


organism: Mycobacterium tuberculosis

substrate_name: (E,E,E)-geranylgeranyl diphosphate

substrate: (E,E,E)-geranylgeranyl diphosphate


proof_lines:
microtubule-free KSP
microtubule-free KSP + 50 microM KSPA-1
KSP + microtubules + 30 microM KSPA-1


substrate_name: Unknown

proof_lines: inhibition of the microtubule-stimulated ATP activity of the ispinesib resistant mutant KHC-L5


assay_conditions_summary: pH 6.8; cofactor ATP

proof_lines: inhibition of the microtubule-stimulated ATP activity

proof_lines: pH 6.8, temperature not specified in the publication


proof_lines: pH 8.0, 28°C, mutant enzyme MEI-1 K293A/MEI-2


enzyme_display_name: phosphoribosylanthranilate isomerase

organism: Escherichia coli

proof_lines:
pH 7.5
25°C, bifunctional IGPS:PRAI
25°C, monomeric domain PRAI[ML256-452]

enzyme: phosphoribosylanthranilate isomerase


organism: Cinnamomum burmanni


enzyme_display_name: glutamine synthetase

substrate_name: Gln

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

enzyme: glutamine synthetase

substrate: Gln


substrate_name: methyl aklanonate

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

assay_conditions_summary: pH 7

substrate: methyl aklanonate


mutation_signature: Kinetic parameters shown are for full-length enzyme. N-terminally truncated spastin (residues 228-616)

substrate: ATP


enzyme_display_name: ADP-glyceromanno-heptose 6-epimerase

substrate_name: ADP-D-glycero-D-manno-heptose

assay_conditions_summary: cofactor ADP

enzyme: ADP-glyceromanno-heptose 6-epimerase

substrate: ADP-D-glycero-D-manno-heptose


substrate_name: formate

substrate: formate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R169T to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP


substrate_name: holo-[aryl-carrier protein EntB]

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

proof_lines: product analog inhibitor, competitive inhibitor, result indicates that the catecholic 2-OH group is critical for tight binding

substrate: holo-[aryl-carrier protein EntB]


enzyme_display_name: isochorismate synthase

substrate_name: chorismate

proof_lines:
in absence of 2-mercaptoethanol
in presence of 2-mercaptoethanol

enzyme: isochorismate synthase

substrate: chorismate


enzyme_display_name: tRNA pseudouridine(38-40) synthase

substrate_name: tRNAHis guanidine36 uridine38 cytidine39

enzyme: tRNA pseudouridine(38-40) synthase


enzyme_display_name: chorismate mutase

assay_conditions_summary: pH 7.8; 310.15 K; cofactor NAD+

proof_lines: genetically engineered enzyme containg the amino acid residues 1-300

proof_lines: genetically engineered enzyme containg the amino acid residues 1-285

enzyme: chorismate mutase


enzyme_display_name: D-alanine--D-alanine ligase

substrate_name: D-serine

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

enzyme: D-alanine--D-alanine ligase

substrate: D-serine


enzyme_display_name: peptidylprolyl isomerase

enzyme: peptidylprolyl isomerase

substrate: Unknown


enzyme_display_name: L-rhamnose isomerase

substrate_name: L-rhamnulose

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

enzyme: L-rhamnose isomerase

substrate: L-rhamnulose


enzyme_display_name: cellobiose epimerase

organism: [Eubacterium] cellulosolvens

substrate_name: lactose

proof_lines: pH and temperature not specified in the publication

enzyme: cellobiose epimerase

substrate: lactose


enzyme_display_name: adenylate cyclase

organism: Euglena gracilis

assay_conditions_summary: 298.15 K; cofactor ATP

proof_lines: 25°C, plasma membrane isolated from glutamate/malate grown cells

proof_lines: 25°C, plasma membrane isolated from lactic acid grown cells

enzyme: adenylate cyclase


organism: Flavobacterium johnsoniae


enzyme_display_name: bisphosphoglycerate mutase

organism: Gallus gallus

proof_lines: presence of activator 2-phosphoglycolate

enzyme: bisphosphoglycerate mutase


enzyme_display_name: aldose 1-epimerase

substrate_name: alpha-D-glucose

enzyme: aldose 1-epimerase

substrate: alpha-D-glucose


organism: Ganoderma lucidum

substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


enzyme_display_name: methionine gamma-lyase

organism: Fusobacterium nucleatum subsp. nucleatum

substrate_name: L-cysteine

sequence_source: UniProtKB/Swiss-Prot Q8RDT4 FASTA

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

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

enzyme: methionine gamma-lyase

substrate: L-cysteine


enzyme_display_name: isopentenyl-diphosphate Delta-isomerase

substrate_name: isopentenyl diphosphate

proof_lines:
isomerase II and III
isomerase I
isomerase IV

enzyme: isopentenyl-diphosphate Delta-isomerase

substrate: isopentenyl diphosphate


enzyme_display_name: myosin ATPase

organism: Oryctolagus cuniculus

substrate_name: CTP

enzyme: myosin ATPase

substrate: CTP


substrate_name: UTP

substrate: UTP


substrate_name: TTP

substrate: TTP


substrate_name: GTP

substrate: GTP


substrate_name: ITP

substrate: ITP


enzyme_display_name: proteasome ATPase

organism: Methanocaldococcus jannaschii

enzyme: proteasome ATPase


substrate_name: ATP

mutation_signature: Δ1

mutation_type: deletion

substrate: ATP


enzyme_display_name: dynein ATPase

organism: Saccharomyces cerevisiae

proof_lines:
mutant E2488Q, basal activity
mutant E2488Q, microtubule-stimulated

enzyme: dynein ATPase


proof_lines:
mutant E2819Q, basal activity
mutant E2819Q, microtubule-stimulated


proof_lines:
basal activity
microtubule-stimulated


substrate_name: a dynein associated with a microtubule at position n


substrate: a dynein associated with a microtubule at position n


enzyme_display_name: plus-end-directed kinesin ATPase

organism: Dictyostelium discoideum

mutation_signature: truncated Kif3-342

proof_lines: truncated protein Kif3-342, 22°C, pH 6.8

enzyme: plus-end-directed kinesin ATPase


mutation_signature: truncated Kif3-592

proof_lines: truncated protein Kif3-592, 22°C, pH 6.8


organism: Schizosaccharomyces pombe

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


mutation_signature: C-terminally truncated enzyme

proof_lines: C-terminally truncated enzyme, at pH 7.5 and 37°C


organism: Neurospora crassa

substrate_name: phosphate

proof_lines: in presence of microtubule the ATP hydrolysis is activated 3fold to 4fold compared to kcat, 125 vs. 34 s-1, while phosphate release is approximately equally fast: 29 s-1, pH and temperature not specified in the publication

substrate: phosphate


substrate_name: ADP

substrate: ADP


organism: Heliocidaris crassispina

proof_lines: 12S sucrose gradient fraction of inner arm dynein

proof_lines: 21S sucrose gradient fraction of outer arm dynein


organism: Bos taurus

proof_lines:
19S sucrose gradient dynein particle
12S sucrose gradient dynein particle


organism: Lytechinus pictus

proof_lines: latent dynein ATPase 1, in the presence of 0.02 mM P1,P5-di(adenosine-5')-pentaphosphate


proof_lines:
in the presence of microtubules
in the absence of microtubules


organism: Tetrahymena pyriformis

proof_lines: 30S dynein, in the absence of tubulin, 1 mM KCl

proof_lines: 30S dynein, in the presence of tubulin, 1 mM KCl


organism: Tetrahymena thermophila

assay_conditions_summary: pH 7; 301.15 K; cofactor ATP

proof_lines: 22S sucrose gradient fraction, per site at pH 7 and 28°C


substrate_name: Formycin triphosphate

substrate: Formycin triphosphate


organism: Hemicentrotus pulcherrimus


organism: Tripneustes gratilla

proof_lines:
21S dynein 1
12S dynein 2


organism: Plasmodium berghei

assay_conditions_summary: pH 7; 299.15 K; cofactor ATP


proof_lines: in 12.5 mM ACES-KOH, 25 mM potassium acetate, 5 mM MgCl2, 0.5 M EGTA, pH 6.8, at 22°C


enzyme_display_name: minus-end-directed kinesin ATPase

organism: Eremothecium gossypii

assay_conditions_summary: pH 6.9; 295.15 K; cofactor ATP

proof_lines: motor domain, 25 mM potassium acetate, Vmax/2 at 0.0007 mM microtubles, pH 6.9, 22°C

proof_lines: motor domain, 0 mM potassium acetate, Vmax/2 at 0.00008 mM microtubles, pH 6.9, 22°C

proof_lines: motor domain, 0 mM potassium acetate, pH 6.9, 22°C

enzyme: minus-end-directed kinesin ATPase


organism: Plasmodium falciparum


organism: Bifidobacterium longum subsp. infantis

assay_conditions_summary: pH 5; 310.15 K; cofactor ATP


organism: Rattus norvegicus

proof_lines:
rSUG1 + 0.001 mg poly(U)
rSUG1 + 0.0005 mg poly(U)
rSUG1 + 0.00025 mg poly(U)


enzyme_display_name: chaperonin ATPase

organism: Pyrococcus furiosus

assay_conditions_summary: pH 7.5; 358.15 K; cofactor ATP

enzyme: chaperonin ATPase


organism: Lathyrus oleraceus

assay_conditions_summary: cofactor ATP


organism: Saccharomyces cerevisiae


organism: Escherichia coli


substrate_name: K48-GREEN-TAIL polypeptide

proof_lines:
at pH 7.6 and 30°C
at pH and ?C

substrate: K48-GREEN-TAIL polypeptide


organism: Dictyostelium sp.

proof_lines: chimeric myosin, Dictyostelium myosin loop 2 replaced by chicken smooth muscle myosin loop 2, actin activated


organism: Caenorhabditis elegans


enzyme_display_name: inositol-3-phosphate synthase

organism: Bos taurus

substrate_name: D-glucose 6-phosphate

proof_lines: with addition of 5% ethanol plus 50 mM KCl

enzyme: inositol-3-phosphate synthase

substrate: D-glucose 6-phosphate


organism: Gallus gallus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: actin-activated, unphosphorylated myosin, pH 7.5, 25°C


organism: Lethocerus griseus

proof_lines: activation with 0.02 mM actin from rabbit skeletal muscle

proof_lines: activation with 0.06 mM actin from rabbit skeletal muscle


organism: Mammalia

proof_lines:
Myo1b1IQ-GAGEGA, pCa 8.9
Myo1b1IQ-WT, pCa 4.6
Myo1b1IQ-WT, pCa 8.9


organism: Oryctolagus cuniculus

substrate_name: ATP; H2O

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

proof_lines:
pH 7.6, 25°C, cosubstrate GTP
pH 7.6, 25°C, cosubstrate ITP
pH 7.6, 25°C, presence of Sr2+ at 2 mM

substrate: ATP; H2O


proof_lines:
Mg-ATPase, 0.6 M KCl
Ca-ATPase, 2.0 mM Ca2+
K+EDTA-ATPase, 1 mM EDTA


assay_conditions_summary: pH 7; 296.15 K; cofactor ATP

proof_lines: enzyme in complex with the calmodulin-like domain of its light chain MLC-B, at pH 7.0 and 23°C


organism: Lethocerus indicus


organism: Sus scrofa

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines: in the presence of 5 mM Zn2+, at pH 7.2 and 37°C

proof_lines: in the absence of Zn2+, at pH 7.2 and 37°C


organism: Homo sapiens

proof_lines: beta-cardiac myosin isoform, at pH 7.0 and 20°C

proof_lines: embryonic myosin isoform, at pH 7.0 and 20°C


organism: Mus musculus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A247C to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.7; 298.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G272C with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A252C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S275C to reconstruct the assayed variant sequence.


substrate_name: Unknown

substrate: Unknown


proof_lines: various isoenzymes of subfragment 1 and heavy-meromyosin, absence of actin


organism: Drosophila melanogaster

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E585D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: mutant NcN-E585D, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C


sequence_variant_note: Mutation context was captured, but conflicting substitutions targeted the same residue position.

proof_lines: E585D/E585E, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C


proof_lines: mutant E585A/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C

proof_lines: mutant E552A/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C

proof_lines: mutant E552A plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C


organism: Thermoplasma acidophilum

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D94A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 328.15 K; cofactor ATP

proof_lines: mutant enzyme D94A, with rhamnose dehydrogenase as protein substrate, at pH 7.5 and 55°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D93K with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D93K, with rhamnose dehydrogenase as protein substrate, at pH 7.5 and 55°C


proof_lines: Ncd700SG (residue 250-700, residue 671-679 replaced by sequence GGSGGSGGS), microtuble stimulated, Vmax/2 at 0.00014 mM microtubles, pH 7.2, 25°C

proof_lines: Ncd670 (residue 250-670), microtuble stimulated, Vmax/2 at 0.00014 mM microtubles, pH 7.2, 25°C

proof_lines: NcdWT (residue 250-700), microtuble stimulated, Vmax/2 at 0.00022 mM microtubles, pH 7.2, 25°C


proof_lines: mutant Ncd700SG, pH 7.2, 25°C, microtubule-stimulated ATPase activity

proof_lines: mutant Ncd670, pH 7.2, 25°C, microtubule-stimulated ATPase activity

proof_lines: mutant NcN, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M672N to reconstruct the assayed variant sequence.

proof_lines: NcdM672N (residue 250-679, M672N mutation), microtuble stimulated, Vmax/2 at 0.00061 mM microtubles, pH 7.2, 25°C


proof_lines:
asthenozoospermic samples
normozoospermic samples


assay_conditions_summary: pH 7.2; 298.15 K; cofactor ATP

proof_lines: in presence of microtubles, pH 7.2, 25°C

proof_lines: in presence of microtubles, Vmax/2 at 0.0004 mM microtubles, pH 7.2, 25°C


organism: Acetivibrio thermocellus


organism: Schizosaccharomyces pombe

assay_conditions_summary: pH 6.8; cofactor ATP

proof_lines: green fluorescent protein-tagged Pkl1H, in 12 mM PIPES-KOH, 2 mM MgCl2, 1 mM EGTA, pH 6.8, containing 1 mM dithiothreitol, 0.7 mg/ml casein, and 1% (v/v) Tween 20 at 25°C


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: MgATP

proof_lines: kcat is 0.49 sec(-1) with MgATP as substrate (PubMed:17382884). kcat is 2.8 sec(-1) with MgATP as substrate in complex with CIK1 (PubMed:17382884). kcat is 3.7 sec(-1) with MgATP as substrate in complex with VIK1 (PubMed:17382884).

substrate: MgATP


organism: Escherichia coli


organism: Allochromatium vinosum


substrate_name: MgATP in complex with CIK1

substrate: MgATP in complex with CIK1


enzyme_display_name: channel-conductance-controlling ATPase

enzyme: channel-conductance-controlling ATPase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat for ATPase activity is 0.16 min(-1).


proof_lines: kcat for ATPase activity is 0.28 min(-1) (PubMed:15327959). kcat for ATPase activity is 0.18 min(-1) (PubMed:21802426).


organism: Dictyostelium discoideum

proof_lines: ATPase activity of the actomyosin complex


enzyme_display_name: microtubule-severing ATPase

organism: Caenorhabditis elegans

substrate_name: ATP (at 37 degrees Celsius and pH 8.8)

enzyme: microtubule-severing ATPase

substrate: ATP (at 37 degrees Celsius and pH 8.8)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y485W to reconstruct the assayed variant sequence.


substrate_name: glutathione (in the presence of MgAMP-PNP)

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

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

column_label: Figure 1C caption and adjacent results prose report CFTR-mediated GSH flux in the presence of MgAMP-PNP with K_m 0.47 mM.

raw_value_unit_evidence: Km raw_value=0.47 raw_unit=mM

row_label: wild-type CFTR-dependent GSH flux in the presence of MgAMP-PNP

table_label: PMC Fig. 1C caption and results prose PMID 12727866


organism: Danio rerio

column_label: Cell full text reports: Phosphorylated zebrafish CFTR has a KM of 0.22 mM for ATP, comparable to the 0.30 mM value reported for human CFTR.

raw_value_unit_evidence: Km raw_value=0.22 raw_unit=mM

row_label: phosphorylated zebrafish CFTR / ATPase activity

table_label: Results and Discussion / Figure 1 Biochemical Properties of Zebrafish CFTR


organism: Methanococcus maripaludis

column_label: Prose section 'ATPase activity and stability of Mm-cpn as a function of temperature', PDF page 3 / journal page 671; metric label ATPase activity/rate; substrate ATP; raw value 59.4 +/- 2.1 ATP min^-1 at 37 C.

normalized_value_unit_evidence: kcat normalized_value=0.99 normalized_unit=s^-1 from 59.4 ATP min^-1 / 60

raw_value_unit_evidence: Prose states that the Mm-cpn oligomer hydrolyses ATP at a rate of 59.4 +/- 2.1 ATP min^-1 at 37 C.

row_label: Mm-cpn oligomer, ATPase rate at 37 C

table_label: Prose section: ATPase activity and stability of Mm-cpn as a function of temperature


assay_conditions_summary: pH 6.8; 298.15 K; cofactor ATP

proof_lines: in presence of mutant microtubles alpha-E415A, pH 6.8, 25°C


proof_lines: in presence of mutant microtubles alpha-E416A, pH 6.8, 25°C


proof_lines: in presence of mutant microtubles alpha-E418A, pH 6.8, 25°C


proof_lines: in presence of mutant microtubles alpha-E421A, pH 6.8, 25°C


proof_lines: in presence of mutant microtubles beta-E410A, pH 6.8, 25°C


proof_lines:
basal MgATPase activity
Vmax of actin-activated ATPase activity
basal CaATPase activity


substrate_name: actin

substrate: actin


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


organism: Acanthamoeba castellanii

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S639D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; cofactor ATP

proof_lines: mutant S639D, pH 7.0, 30°C, in presence of F-actin


proof_lines: wild-type S1 fragment, pH 7.0, 30°C, in presence of F-actin

proof_lines: wild-type S1 fragment, pH 7.0, 30°C, hyperbolic fit


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D417A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

proof_lines: in presence of mutant microtubles beta-D417A, pH 6.8, 25°C


proof_lines:
wild-type
wild-type, pH 6.8


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


enzyme_display_name: UniProt P11388

enzyme: UniProt P11388


enzyme_display_name: UniProt P38935

enzyme: UniProt P38935


substrate_name: methylanthraniloyl-ATP

assay_conditions_summary: pH 6.9; 298.15 K; cofactor ATP

proof_lines: basal activity, in absence of tubulin or microtubles, pH 6.9, 25°C

proof_lines: +/-0.022 mM, Vmax: 247 nmol/s, pH and temperature not specified in the publication. The fluorescent ATP analog can fuel kinesin-1'S processsive motion and is a suitable substrate analog, but it alters the motor's kinetic parameters

substrate: methylanthraniloyl-ATP


proof_lines: in presence of unpolymerized tubulin, pH 6.9, 25°C


assay_conditions_summary: 293.15 K; cofactor ATP

proof_lines: Mn2+ concentration variable, ATP concentration fixed, Mn-ATP complexes at 1 mM ATP and 0.8 mM Mn2+

proof_lines: ATP concentration variable, Mn2+ concentration fixed, Mn-ATP complexes at 1 mM ATP and 0.8 mM Mn2+


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 KIF4 enzyme, pH and temperature not specified in the publication

proof_lines: recombinant wild-type K888, pH and temperature not specified in the publication


organism: Saccharomyces cerevisiae

proof_lines: both wild-type and GST-fusion protein, pH 7.2, 25°C


enzyme_display_name: RNA 3'-5' helicase

organism: West Nile virus

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

enzyme: RNA 3'-5' helicase


substrate_name: GTP


proof_lines: pH 7.5, 37°C, wild-type enzyme, inhibition of the ATPase reaction


substrate_name: ITP


substrate_name: ribavirin triphosphate

substrate: ribavirin triphosphate


enzyme_display_name: DNA 5'-3' helicase

organism: Severe acute respiratory syndrome-related coronavirus

enzyme: DNA 5'-3' helicase

substrate: GTP


substrate_name: dGTP

substrate: dGTP


substrate_name: UTP

substrate: UTP


substrate_name: CTP

substrate: CTP


substrate_name: dCTP

substrate: dCTP


substrate_name: dATP

substrate: dATP


substrate_name: dUTP

substrate: dUTP


substrate_name: ATP

assay_conditions_summary: pH 6.6; 298.15 K; cofactor ATP

substrate: ATP


enzyme_display_name: DEAD-box RNA helicase

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q169E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor ATP

table_label: Table I. Kinetic parameters for RNA-dependent ATPase activity

enzyme: DEAD-box RNA helicase

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F162A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q169A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T166S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F162L to reconstruct the assayed variant sequence.

column_label: Table I; row F162L; columns Km, kcat, and kcat/Km; exact printed cells 0.78 +/- 0.11 mM, 120 +/- 10 min^-1, and 150000 +/- 20000 M^-1 min^-1; central values normalize to 0.78 mM, 2.0 s^-1, and 2.5 s^-1*mM^-1.

normalized_value_unit_evidence: Paper Km=0.78 mM; paper kcat=2.0 s^-1; paper printed kcat/Km=2.5 s^-1*mM^-1. Current tuple is Km=0.78 mM, kcat=2.0 s^-1, kcat/Km=2.564102564102564 s^-1*mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T166A to reconstruct the assayed variant sequence.

column_label: Table I; row T166A; columns Km, kcat, and kcat/Km; exact printed cells 0.51 +/- 0.04 mM, 120 +/- 10 min^-1, and 230000 +/- 20000 M^-1 min^-1; central values normalize to 0.51 mM, 2.0 s^-1, and 3.8333333333333335 s^-1*mM^-1.


assay_conditions_summary: pH 7.5; buffer used 50 mM potassium acetate; cofactor ATP

column_label: Table I; row WT; columns Km, kcat, and kcat/Km; raw cells 0.34 +/- 0.05 mM, 210 +/- 20 min^-1, and 620000 +/- 90000 M^-1 min^-1; kcat/Km is explicitly printed, while the package ratio is also derivable from rounded package kcat/Km.

normalized_value_unit_evidence: paper Km=0.34 mM; paper kcat=3.5 s^-1; paper printed kcat/Km=10.3333 s^-1*mM^-1; package kcat/Km=10.294117647058822 s^-1*mM^-1 is derived from the package rounded kcat/Km pair

row_label: WT


column_label: Table I; row T166S; column Ki(d) (mM); raw value 0.34 +/- 0.07 mM; normalized Ki=0.34 mM; footnote d identifies competitive inhibition by ADP; ATP is the ATPase substrate.

normalized_value_unit_evidence: Current Ki=0.34 mM; paper Ki=0.34 mM; inhibitor/modifier is ADP competitive inhibition and ATP is the substrate.

raw_value_unit_evidence: Table I row T166S, Ki(d) column: 0.34 +/- 0.07 mM.


column_label: Table I; row WT; column Ki(d) (mM); raw value 0.36 +/- 0.07 mM; normalized Ki=0.36 mM; footnote d identifies competitive inhibition by ADP; ATP is the ATPase substrate.

normalized_value_unit_evidence: Current Ki=0.36 mM; paper Ki=0.36 mM; inhibitor/modifier is ADP competitive inhibition and ATP is the substrate.

raw_value_unit_evidence: Table I row WT, Ki(d) column: 0.36 +/- 0.07 mM.


column_label: Table I; row T166A; column Ki(d) (mM); raw value 0.36 +/- 0.08 mM; normalized Ki=0.36 mM; footnote d identifies competitive inhibition by ADP; ATP is the ATPase substrate.

raw_value_unit_evidence: Table I row T166A, Ki(d) column: 0.36 +/- 0.08 mM.


column_label: Table I; row F162L; column Ki(d) (mM); raw value 3.0 +/- 0.1 mM; normalized Ki=3.0 mM; footnote d identifies competitive inhibition by ADP; ATP is the ATPase substrate.

normalized_value_unit_evidence: Current Ki=3.0 mM; paper Ki=3.0 mM; inhibitor/modifier is ADP competitive inhibition and ATP is the substrate.

raw_value_unit_evidence: Table I row F162L, Ki(d) column: 3.0 +/- 0.1 mM.


organism: Bacillus subtilis

substrate_name: RNA

proof_lines: pH 7.5, 37°C, recombinant YxiN mutant S108C/S229C

substrate: RNA


proof_lines: pH 7.5, 37°C, recombinant YxiN mutant S108C/E224C


proof_lines: pH 7.5, 37°C, recombinant wild-type YxiN


proof_lines: pH 7.5, 37°C, recombinant YxiN mutantA115C/S229C


proof_lines: pH 7.5, 37°C, recombinant YxiN mutantA115C/E224C


proof_lines: pH 7.5, 37°C, recombinant YxiN mutantA115C/D262C


organism: Hepacivirus hominis

assay_conditions_summary: pH 6.5; 310.15 K; cofactor ATP

proof_lines: pH 6.5, 37°C, RNA-stimulated ATPase activity of mutant NS3-4A


proof_lines: pH 6.5, 37°C, RNA-stimulated ATPase activity of mutant S1369R/M1708A

proof_lines: RNA-stimulated ATPase activity, recombinant protein, NS3-4A S1369R/M1708A mutant


proof_lines: pH 6.5, 37°C, RNA-stimulated ATPase activity of wild-type NS3


proof_lines: pH 6.5, 37°C, RNA-stimulated ATPase activity of mutant Y1702A

proof_lines: RNA-stimulated ATPase activity, recombinant protein, NS3-4A Y1702A mutant


proof_lines: pH 6.5, 37°C, RNA-stimulated ATPase activity of mutant M1708A

proof_lines: RNA-stimulated ATPase activity, recombinant protein, NS3-4A M1708A mutant


assay_conditions_summary: cofactor ATP

proof_lines: RNA-stimulated ATPase activity, recombinant protein, NS3-4A S1369R mutant


proof_lines: RNA-stimulated ATPase activity, recombinant protein, NS3-4A S1369R/Y1702A mutant


substrate_name: dTTP

proof_lines: inhibition of NTPase activity of NS3 protein by NTP derivatives

substrate: dTTP


enzyme_display_name: DNA topoisomerase (ATP-hydrolyzing)

organism: Mycobacterium tuberculosis

sequence_source: UniProt P9WG47 canonical sequence.

enzyme: DNA topoisomerase (ATP-hydrolyzing)


sequence_source: UniProt P9WG45 canonical sequence with GyrBA_mC-loop substitutions E221K/D225K/E228K/R236E/H244A.


sequence_source: UniProt P9WG47 canonical sequence with GyrBAKKKK substitution D211K/E212K/E213K/E214K.


sequence_source: UniProt P9WG45 canonical sequence with A57D substitution.


assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP

proof_lines: pH 7.5, 22°C, recombinant engineered enzyme


proof_lines: pH 7.5, 22°C, recombinant wild-type enzyme


enzyme_display_name: DNA 3'-5' helicase

substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

proof_lines: i.e. ppopT, dTTP analogue, inhibition of NTPase activity of NS3 protein by NTP derivatives

enzyme: DNA 3'-5' helicase

substrate: Unknown


assay_conditions_summary: pH 6.5; 295.15 K; cofactor ATP

proof_lines: addition of polyuridylate lowers Km for the ATP substrate

proof_lines: pH 6.5, 22°C, recombinant enzyme, calculated by BRENDA


organism: Dengue virus

proof_lines: full-length enzyme in presence of cofactor CF40-Gly4-Ser-Gly4-NS3FL


proof_lines: RNA-stimulated ATPase activity, recombinant protein, NS3-4A construct

proof_lines: RNA-stimulated ATPase activity, NS3, recombinant protein


enzyme_display_name: RNA 5'-3' helicase

organism: Homo sapiens

enzyme: RNA 5'-3' helicase


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


organism: Thermochaetoides thermophila

proof_lines: recombinant enzyme mutant ctPrp43-IDSB, pH and temperature not specified in the publication


organism: Saccharolobus solfataricus

sequence_variant_note: Mutation signature K323A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH and temperature not specified in the publication, mutant enzyme K323A


sequence_variant_note: Mutation signature R329A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH and temperature not specified in the publication, mutant enzyme R329A


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +23, so it is treated as a source-provided variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme E326A/D327A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D327A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme D327A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V324A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme V324A


sequence_variant_note: Mutation signature E326A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH and temperature not specified in the publication, mutant enzyme E326A


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +25, so it is treated as a source-provided variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme V324A/L325A


proof_lines: pH and temperature not specified in the publication, mutant enzyme L325A


proof_lines: pH 7.5, 37°C, native WNV NS3 protein purified from infected cells

proof_lines: recombinant protein including C-terminal portion the ATPase/helicase domain encompassing residues 181-619, ATP concentration 1mM ATP, ATPase but not RNA helicase activity

proof_lines: pH 7.5, 37°C, recombinant C-terminal portion of the NS3


organism: Pseudomonas phage EL

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

assay_conditions_summary: 298.15 K; cofactor ATP

proof_lines:
at 100 mM KCl, at pH and 25°C
at 10 mM KCl, at pH and 25°C


sequence_variant_note: Mutation signature E326A/D327A/R329A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH and temperature not specified in the publication, mutant enzyme E326A/D327A/R329A


sequence_variant_note: Mutation signature E202G/E203G/V204G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: + Y-DNA, pH and temperature not specified in the publication, mutant enzyme E202G/E203G/V204G


sequence_variant_note: Mutation signature I555D/L556S/I557D could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: + Y-DNA, pH and temperature not specified in the publication, mutant enzyme I555D/L556S/I557D


proof_lines: + Y-DNA, pH and temperature not specified in the publication, wild-type enzyme


sequence_variant_note: Mutation signature T550G/P551G/D552G/S553G/P554G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: + Y-DNA, pH and temperature not specified in the publication, mutant enzyme T550G/P551G/D552G/S553G/P554G


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L189D/D191R with inferred residue-numbering offset -32 to reconstruct the assayed variant sequence.

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


organism: Thermoanaerobacter brockii

assay_conditions_summary: 343.15 K; cofactor ATP


organism: Enterobacteria phage T4


enzyme_display_name: myosin ATPase

proof_lines: myosin IA, 100-kDa fragment resulting from digestion of myosin heavy chain with alpha-chymotrypsin shows similar activity

enzyme: myosin ATPase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: ATP with dsDNA

proof_lines: kcat is 3180 min(-1) with dsDNA (PubMed:22628485). kcat is 61 min(-1) with mobile HJ, kcat is 46 min(-1) with immobile HJ (PubMed:23438087).

substrate: ATP with dsDNA


organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)


organism: Drosophila melanogaster

substrate_name: ATP; negatively supercoiled circular DNA


substrate_name: ATP in helicase activity

substrate: ATP in helicase activity


organism: Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216)

substrate_name: 21-mer ssDNA substrate

substrate: 21-mer ssDNA substrate


organism: Dictyostelium discoideum

proof_lines:
HFG380, basal activity
HFG380, microtubule-activated activity
HFG380, microtubule-activated


proof_lines: kcat is 0.0095 sec(-1) for ATP. kcat is 0.0075 sec(-1) for GTP.


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: dNTPs

proof_lines: kcat is 22 sec(-1) for polymerase activity (PubMed:27487482). kcat is 10 min(-1) for polymerase activity (PubMed:39490679). kcat is 1.69 min(-1) for polymerase activity on dA template with dTTP (PubMed:35220686, PubMed:32636411). kcat is 1.

substrate: dNTPs


proof_lines: kcat is 10 sec(-1) on a ssDNA 21-mer and about 50 sec(-1) on ssDNA 5kb template.


substrate_name: ssDNA

substrate: ssDNA


organism: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)

substrate_name: ATP in presence of forked DNA with 40 bp lagging strand arm

proof_lines: kcat is 9 sec(-1) for ATPase, in the presence of 100 nM monomeric PriB kcat is 14 sec(-1) for ATPase.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: ATP hydrolysis by TFIIH in the absence of RAD3/XPD ATPase activity

proof_lines: kcat for ssDNA-dependent ATPase activity is 140 min(-1) of purified protein.


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

proof_lines: pH 6.8, 25°C, tubulin-vinblastine-stimulated recombinant Kif2C functional domain mutant L2

proof_lines: pH 6.8, 25°C, tubuline-stimulated recombinant Kif2C functional domain mutant DSK

proof_lines: pH 6.8, 25°C, tubuline-stimulated recombinant Kif2C functional domain mutant DVK


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

proof_lines: pH 6.8, 25°C, tubulin-stimulated recombinant Kif2C functional domain wild-type

proof_lines: pH 6.8, 25°C, tubulin-vinblastine-stimulated recombinant Kif2C functional domain wild-type

proof_lines: in presence of wild type microtubles, pH 6.8, 25°C


organism: Geobacillus stearothermophilus

substrate_name: ATP (for hydrolysis activity)

proof_lines: kcat is 19 sec(-1) with ATP as substrate, and varies from 3-40 sec(-1) depending on the (d)NTP. In the absence of single-stranded (ss)DNA, kcat decreases 400-fold with ATP as substrate.

substrate: ATP (for hydrolysis activity)


substrate_name: dATP (for hydrolysis activity)

substrate: dATP (for hydrolysis activity)


substrate_name: CTP (for hydrolysis activity)

substrate: CTP (for hydrolysis activity)


substrate_name: GTP (for hydrolysis activity)

substrate: GTP (for hydrolysis activity)


substrate_name: dGTP (for hydrolysis activity)

substrate: dGTP (for hydrolysis activity)


substrate_name: dTTP (for hydrolysis activity)

substrate: dTTP (for hydrolysis activity)


substrate_name: 1,N6-ethenoadenosine 5'-triphosphate (for hydrolysis activity)


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R334Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R354P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R357P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R374Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S369P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S369Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T457I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W315L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W474C to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A318T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A359T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A475P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F485L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I367T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K319E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K319T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L381P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P335L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R303W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y508C with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E44Q with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


organism: Bacillus subtilis (strain 168)

proof_lines: kcat for ATP hydrolysis by AddAB is 88 sec(-1), ATPase is strongly stimulated by ssDNA.


substrate_name: ATP (at 30 degrees Celsius)

substrate: ATP (at 30 degrees Celsius)


substrate_name: dATP (at 30 degrees Celsius)

substrate: dATP (at 30 degrees Celsius)


substrate_name: ATP with dsDNA

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


organism: Escherichia coli (strain K12)

assay_conditions_summary: 308.15 K; cofactor ATP

column_label: Abstract reports ATP is the preferred substrate (Km 0.27 mM) and dephosphorylated at the gamma-position at a maximal rate near 10(4) molecules per enzyme monomer per min at 35 degrees C.

raw_value_unit_evidence: Km raw_value=0.27 mM raw_unit=mM

row_label: Escherichia coli DNA-dependent ATPase / ATP

table_label: PubMed XML abstract PMID 133022

substrate: ATP


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y564A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: mutant (RECQ1(T1))Y564A, a construct encompassing amino acids 49?616 (of 649) of RECQ1, followed by a C-terminal tag of 22 aa


substrate_name: dATP

substrate: dATP


organism: Helicobacter pylori (strain ATCC 700392 / 26695)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A475P with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

proof_lines: mutant A475P, pH 7.5, 37°C, in the presence of calf thymus DNA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K319T to reconstruct the assayed variant sequence.

proof_lines: mutant K319T, pH 7.5, 37°C, in the presence of calf thymus DNA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F485L to reconstruct the assayed variant sequence.

proof_lines: mutant F485L, pH 7.5, 37°C, in the presence of calf thymus DNA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K319E to reconstruct the assayed variant sequence.

proof_lines: mutant K319E, pH 7.5, 37°C, in the presence of calf thymus DNA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L381P to reconstruct the assayed variant sequence.

proof_lines: mutant L381P, pH 7.5, 37°C, in the presence of calf thymus DNA


sequence_variant_note: Mutation signature K897del could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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

proof_lines: kcat is 0.0095 sec(-1) for ATP. kcat is 0.0075 sec(-1) for GTP.


substrate_name: UTP (using ssM13mp18 as DNA substrate)

substrate: UTP (using ssM13mp18 as DNA substrate)


organism: Leishmania major

assay_conditions_summary: pH 8.3; 310.15 K; cofactor ATP


column_label: Results text states EcoLhr has a Km of 0.17 +/- 0.076 mM ATP from a nonlinear Michaelis-Menten fit of ATP hydrolysis velocity versus ATP concentration.

raw_value_unit_evidence: Km raw_value=0.17 +/- 0.076 raw_unit=mM ATP

row_label: full-length Escherichia coli Lhr (EcoLhr-FL) / ATP hydrolysis

table_label: Results text and Figure 5C, Characterization of the EcoLhr ATPase


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


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

proof_lines: mutant W474C, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant T457I, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant R334Q, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant A359T, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant P335L, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant W315L, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant R354P, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant A318T, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant R357P, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant S369Y pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant Y508C, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant S369P, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant R374Q , pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant R303W, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines: mutant I367T, pH 7.5, 37°C, in the presence of calf thymus DNA


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP


column_label: The paper reports apparent Km values derived from ATPase activity versus ATP concentration and gives 0.05 mM for wild-type UvrD.

raw_value_unit_evidence: Km raw_value=0.05 raw_unit=mM

row_label: wild-type UvrD DNA helicase II ATPase activity

table_label: Results prose and Fig. 6, ATPase activity as a function of ATP concentration


substrate_name: DNA

substrate: DNA


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

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


organism: Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / KCTC 9307 / NBRC 14880 / R51)


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


proof_lines: enzyme dimeric mutant GyrBA5, pH 7.5, 30°C

proof_lines: enzyme dimeric mutant GyrBA57DELTAC-loop, pH 7.5, 30°C

proof_lines: enzyme mutant GyrBADELTAC-loop, pH 7.5, 30°C


proof_lines: enzyme mutant GyrBAmC-loop (E221K/D225K/E228K/R236E/H244A), pH 7.5, 30°C


proof_lines: enzyme mutant GyrBAKKK (D211K/E212K/E213K/E214K), pH 7.5, 30°C


assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines: mutant DELTA Q25, pH 7.4, 30°C, in the absence of DNA

proof_lines: mutant DELTA Q25, pH 7.4, 30°C, in the presence of M13 ssDNA


proof_lines: mutant K52R, pH 7.4, 30°C, in the presence of M13 ssDNA


proof_lines: mutant Q25A, pH 7.4, 30°C, in the absence of DNA

proof_lines: mutant Q25A, pH 7.4, 30°C, in the presence of M13 ssDNA


proof_lines: wild-type, pH 7.4, 30°C, in the absence of DNA

proof_lines: wild-type wit His-tag, pH 7.5, 37°C, in the presence of calf thymus DNA

proof_lines: wild-type without His-tag, pH 7.5, 37°C, in the presence of calf thymus DNA


proof_lines:
pH 8.0, 30°C, without ssDNA
pH 8.0, 30°C, in presence of ssDNA


assay_conditions_summary: pH 7.5; 293.15 K; cofactor ATP

proof_lines:
pH 7.5, 20°C, without DNA
pH 7.5, 20°C, in presence of DNA


organism: Bos taurus

proof_lines:
relaxation reaction
ATPase reaction
in presence of supercoiled plasmid DNA


organism: Leishmania donovani

proof_lines: pH 7.5, 30°C, recombinant N-terminal domain, ATPase activity


substrate_name: Unknown

proof_lines: pH 7.5, 30°C, recombinant N-terminal domain, inhibition of ATPase activity

substrate: Unknown


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 7.7; 303.15 K; cofactor ATP

proof_lines: pH 7.7, 30°C, recombinant Y50F mutant enzyme, in absence of DNA

proof_lines: pH 7.7, 30°C, recombinant Y50F mutant enzyme, in presence of DNA


proof_lines: pH 7.7, 30°C, recombinant Y28F mutant enzyme


assay_conditions_summary: pH 7.9; 303.15 K; cofactor ATP

proof_lines: recombinant mutant enzyme K168A from Saccharomyces cerevisiae cells, at pH 7.9 and 30°C


proof_lines: recombinant enzyme from Saccharomyces cerevisiae cells, at pH 7.9 and 30°C

proof_lines: recombinant enzyme from BHK-21 cells, at pH 7.9 and 30°C


organism: Saccharolobus solfataricus

assay_conditions_summary: 353.15 K; cofactor ATP

proof_lines: 80°C, pH not specified in the publication, wild-type enzyme


proof_lines: 80°C, pH not specified in the publication, mutant enzyme Y965F


proof_lines: pH 7.7, 30°C, recombinant wild-type or Y50F mutant enzyme, in absence of DNA

proof_lines: pH 7.7, 30°C, recombinant wild-type enzyme, in presence of DNA


proof_lines: pH 7.7, 30°C, recombinant Y50F mutant enzyme


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K230A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: below, recombinant mutant K230A, pH 8.0, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K335A with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K333A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K328A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K334A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K330A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K329A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


column_label: Figure 2A; row WT; kmax and KDNA cells; kcat/Km derived from those same cells.

raw_value_unit_evidence: Figure 2A row WT: kmax 130 +/- 5 min^-1; KDNA 100 +/- 20 nM.

table_label: Figure 2A PriA DNA-dependent ATPase kmax and KDNA labels


organism: Bacillus anthracis

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: pH 7.5, 37°C, addition of 60-mer oligonucleotide


proof_lines: pH 7.7, 30°C, recombinant wild-type enzyme, in absence of DNA


assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: mutant Y782F, presence of 68 bp DNA duplex, pH 7.5


organism: Drosophila melanogaster

assay_conditions_summary: pH 7.2; 298.15 K; cofactor ATP

proof_lines: 22-25°C, pH 7.2, kinesin-microtubules complex

proof_lines: pH and temperature not specified in the publication


organism: Cereibacter sphaeroides

assay_conditions_summary: cofactor ATP


proof_lines: in the absence of target protein, without cofactor A


organism: Bacillus subtilis


enzyme_display_name: isobutyryl-CoA mutase

organism: Geobacillus kaustophilus

substrate_name: isobutyryl-CoA

assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM sodium phosphate; cofactor CoA

proof_lines: recombinant enzyme, in the presence of GTP, in 50 mM sodium phosphate buffer, pH 7.5, 250 mM NaCl at 37°C

proof_lines: recombinant enzyme, in the presence of GDP, in 50 mM sodium phosphate buffer, pH 7.5, 250 mM NaCl at 37°C

proof_lines: recombinant enzyme, in 50 mM sodium phosphate buffer, pH 7.5, 250 mM NaCl at 37°C

enzyme: isobutyryl-CoA mutase

substrate: isobutyryl-CoA


organism: Aeropyrum pernix

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

assay_conditions_summary: pH 5; 363.15 K; cofactor ATP

column_label: PMID 17092293 Figure 4/prose, ApcpnA ATP hydrolysis, Km = 10.04 mM and kcat = 2.21 min^-1.

raw_value_unit_evidence: Figure 4/prose reports Km = 10.04 mM and kcat = 2.21 min^-1 for ATP hydrolysis by ApcpnA.

row_label: ApcpnA ATP hydrolysis

table_label: Figure 4/prose


enzyme_display_name: DNA topoisomerase

substrate_name: negatively supercoiled plasmid pXXZ06 DNA

enzyme: DNA topoisomerase


organism: Geobacillus stearothermophilus


enzyme_display_name: L-arabinose isomerase

substrate_name: L-arabinose

enzyme: L-arabinose isomerase

substrate: L-arabinose


substrate_name: D-galactose

proof_lines: recombinant mutant H18T/Y234C, pH 6.0, 60°C

proof_lines: recombinant mutant H18T/Y234C, pH 7.5, 60°C

substrate: D-galactose


enzyme_display_name: alanine racemase

enzyme: alanine racemase


enzyme_display_name: triose-phosphate isomerase

organism: Giardia duodenalis

substrate_name: D-glyceraldehyde 3-phosphate

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

proof_lines: presence of 2-carboxyethyl methanethiosulfonate

enzyme: triose-phosphate isomerase

substrate: D-glyceraldehyde 3-phosphate


enzyme_display_name: glucose-6-phosphate isomerase

substrate_name: fructose 6-phosphate

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

enzyme: glucose-6-phosphate isomerase

substrate: fructose 6-phosphate


substrate_name: L-Ala

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

substrate: L-Ala


enzyme_display_name: chalcone isomerase

organism: Glycine max

substrate_name: liquiritigenin

enzyme: chalcone isomerase

substrate: liquiritigenin


enzyme_display_name: peptidylprolyl isomerase

organism: Halobacterium salinarum

enzyme: peptidylprolyl isomerase


organism: Helicobacter pylori

substrate_name: D-alanine

proof_lines:
Vmax 37.9 micromol/min/mg
Vmax 909 micromol/min/mg

substrate: D-alanine


enzyme_display_name: D-sedoheptulose-7-phosphate isomerase

substrate_name: D-sedoheptulose 7-phosphate

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

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

enzyme: D-sedoheptulose-7-phosphate isomerase

substrate: D-sedoheptulose 7-phosphate


organism: Heyndrickxia coagulans

proof_lines:
at pH 7.0 and 70°C
pH 7.0, 70°C, recombinant enzyme
pH 7.5, 60°C


enzyme_display_name: D-alanine--D-alanine ligase

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ATP

proof_lines:
pH 7.4, 25°C, versus ATP
pH 7.4, 25°C, versus D-Ala

enzyme: D-alanine--D-alanine ligase


enzyme_display_name: microtubule-severing ATPase

organism: Caenorhabditis elegans

substrate_name: ATP

sequence_source: UniProtKB/Swiss-Prot Q8MNV0

assay_conditions_summary: pH 8.8; 310.15 K; cofactor ATP

enzyme: microtubule-severing ATPase


enzyme_display_name: protein disulfide-isomerase

organism: Homo sapiens

substrate_name: RNase

enzyme: protein disulfide-isomerase

substrate: RNase


enzyme_display_name: glutamate--cysteine ligase

substrate_name: L-alpha-aminobutyrate

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

enzyme: glutamate--cysteine ligase

substrate: L-alpha-aminobutyrate


enzyme_display_name: channel-conductance-controlling ATPase

assay_conditions_summary: pH 7.5; 306.15 K; cofactor ATP

proof_lines: pH 7.5, 33°C, mutant enzyme R347D, in presence of protein kinase A

proof_lines: pH 7.5, 33°C, mutant enzyme R347D, in absence of protein kinase A

enzyme: channel-conductance-controlling ATPase


enzyme_display_name: phosphoacetylglucosamine mutase

substrate_name: N-acetyl-alpha-D-glucosamine

enzyme: phosphoacetylglucosamine mutase

substrate: N-acetyl-alpha-D-glucosamine


enzyme_display_name: glutamine synthetase

substrate_name: L-Glutamine; ADP; Phosphate

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ADP

enzyme: glutamine synthetase

substrate: L-Glutamine; ADP; Phosphate


enzyme_display_name: thromboxane-A synthase

proof_lines:
recombinant TXAS
23°C, pH 7.5
native TXAS

enzyme: thromboxane-A synthase


enzyme_display_name: steroid Delta-isomerase

proof_lines: 22°C, pH 7.4, truncated cytosolic enzyme DEALTA283-310

enzyme: steroid Delta-isomerase


enzyme_display_name: UDP-N-acetylglucosamine 4-epimerase

enzyme: UDP-N-acetylglucosamine 4-epimerase


enzyme_display_name: adenylate cyclase

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

enzyme: adenylate cyclase

substrate: ATP


enzyme_display_name: leukotriene-C4 synthase

substrate_name: leukotriene A4

proof_lines:
human recombinant enzyme
pH 7.4, 25°C
pH 6.5, 30°C

enzyme: leukotriene-C4 synthase

substrate: leukotriene A4


enzyme_display_name: aldose 1-epimerase

substrate_name: alpha-D-glucose

proof_lines:
pH 8.0, 20°C
kidney
alpha-D-glucose, liver

enzyme: aldose 1-epimerase

substrate: alpha-D-glucose


substrate_name: leukotriene A4 methyl ester

substrate: leukotriene A4 methyl ester


enzyme_display_name: prostaglandin-E synthase

proof_lines: in the presence of 0.3 mM dodecylmaltoside

enzyme: prostaglandin-E synthase


enzyme_display_name: lactoylglutathione lyase

substrate_name: (R)-S-lactoylglutathione

enzyme: lactoylglutathione lyase

substrate: (R)-S-lactoylglutathione


proof_lines: recombinant catalytic subunit, pH 8.0, 37°C


substrate_name: prostaglandin G2

substrate: prostaglandin G2


enzyme_display_name: pancreatic ribonuclease

substrate_name: poly(C)

enzyme: pancreatic ribonuclease

substrate: poly(C)


enzyme_display_name: prostaglandin-I synthase

substrate_name: prostaglandin H2

enzyme: prostaglandin-I synthase

substrate: prostaglandin H2


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: phosphomannomutase

proof_lines:
isoform alpha-PMM2, pH 6.5, 25°C
isoform PMM2, at pH 7.5 and 32°C

enzyme: phosphomannomutase


enzyme_display_name: UniProt P0AGJ9

enzyme: UniProt P0AGJ9


enzyme_display_name: UniProt P0A8M3

substrate_name: hydroxynorvaline

smiles: CCCC(C(=O)O)NO

enzyme: UniProt P0A8M3

substrate: hydroxynorvaline


substrate_name: L-serine

substrate: L-serine


substrate_name: L-threonine

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

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=37°C, pH=7.2

substrate: L-threonine


enzyme_display_name: UniProt Q58597

organism: Methanocaldococcus jannaschii

enzyme: UniProt Q58597


proof_lines:
Raw SKiD Env: Temp=60°C, pH=7.2
Raw SKiD Env: Temp=65°C, pH=7.5


enzyme_display_name: UniProt P07813

substrate_name: L-leucine

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

enzyme: UniProt P07813

substrate: L-leucine


enzyme_display_name: UniProt Q9P2J5

enzyme: UniProt Q9P2J5


substrate_name: L-isoleucine

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

substrate: L-isoleucine


enzyme_display_name: UniProt P09436

organism: Saccharomyces cerevisiae

substrate_name: AMP

enzyme: UniProt P09436

substrate: AMP


enzyme_display_name: Isoleucine--tRNA ligase 2

organism: Pseudomonas fluorescens

substrate_name: isoleucine

enzyme: Isoleucine--tRNA ligase 2

substrate: isoleucine


substrate_name: ATP


substrate_name: cyclic 2',3'-cytidine monophosphate

proof_lines: mutant R4A/K6A/Q9E/D16G/S17N, 25°C, pH 5.0

substrate: cyclic 2',3'-cytidine monophosphate


enzyme_display_name: peptidylprolyl isomerase

enzyme: peptidylprolyl isomerase


enzyme_display_name: isopentenyl-diphosphate Delta-isomerase

substrate_name: isopentenyl diphosphate

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

assay_conditions_summary: pH 8

enzyme: isopentenyl-diphosphate Delta-isomerase

substrate: isopentenyl diphosphate


enzyme_display_name: bisphosphoglycerate mutase

proof_lines:
pH 7.5, low salt concentration
pH 7.8
pH 7.2, 0.1 M KCl

enzyme: bisphosphoglycerate mutase


enzyme_display_name: DNA topoisomerase

proof_lines: with 0.63 microM camptothecin or more numerous shifted htopoI bands detected

enzyme: DNA topoisomerase


enzyme_display_name: threonine--tRNA ligase

organism: Escherichia coli

substrate_name: tRNA(Thr); L-Threonine; ATP

enzyme: threonine--tRNA ligase

substrate: tRNA(Thr); L-Threonine; ATP


substrate_name: ATP; tRNA(Thr); L-Threonine

substrate: ATP; tRNA(Thr); L-Threonine


substrate_name: tRNA(Thr); ATP; L-Threonine

substrate: tRNA(Thr); ATP; L-Threonine


enzyme_display_name: leucine--tRNA ligase

organism: Methanothermobacter thermautotrophicus

substrate_name: L-Leucine; tRNA(Leu); ATP

enzyme: leucine--tRNA ligase

substrate: L-Leucine; tRNA(Leu); ATP


organism: Euglena gracilis

substrate_name: tRNALeu

substrate: tRNALeu


substrate_name: L-Leu

substrate: L-Leu


substrate: ATP


enzyme_display_name: isoleucine--tRNA ligase

proof_lines:
pH 7.5, recombinant isozyme IleRS-R1
pH 7.5, recombinant isozyme IleRS-R2
pH 7.5, native isozyme IleRS-R2

enzyme: isoleucine--tRNA ligase


proof_lines:
pH 7.5, recombinant isozyme IleRS-R1
pH 7.5, native isozyme IleRS-R2
pH 7.5, recombinant isozyme IleRS-R2


substrate_name: Unknown

proof_lines: pH 7.5, recombinant isozyme IleRS-R1, versus L-isoleucine

proof_lines: pH 7.5, recombinant isozyme IleRS-R1, versus ATP

substrate: Unknown


proof_lines: 37°C, pH 7.6, tRNALeu from calf liver, leucylation, full-length enzyme

proof_lines: recombinant mitochondrial isozyme, pH 7.6, 37°C


assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines: 37°C, pH 7.6, leucylation, full-length enzyme

proof_lines: 37°C, pH 7.6, ATP-diphosphate exchange, full-length enzyme


proof_lines: recombinant mitochondrial isozyme mutant, 37°C


assay_conditions_summary: 310.15 K; cofactor ATP


organism: Brevundimonas vesicularis


organism: Pyrococcus horikoshii

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E113A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R106A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 338.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R97A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I104A to reconstruct the assayed variant sequence.


column_label: Table 3 (Steady-state leucine activation kinetics of Ph LeuRS and its single-point mutants), Leucine column group, enzyme row 'Ph LeuRS'; column 'K m (uM)' = 5.92; column 'k cat (s-1)' = 6.0; column 'k cat /K m (s-1 . mM-1)' = 1013. The ATP column group of the same enzyme row prints 'K m (uM)' = 578, 'k cat (s-1)' = 6.8 and 'k cat /K m (s-1 . mM-1)' = 11.8 for the separate ATP-substrate export row.

normalized_value_unit_evidence: Km: printed Table 3 Leucine-group cell 5.92 under the column head K m (uM); 1 uM is 1/1000 mM, so 5.92 / 1000 = 0.00592 mM. kcat: printed Table 3 Leucine-group cell 6.0 under the column head k cat (s-1); the printed turnover column is already per second, so no unit conversion applies and the paper value is 6.0 s^(-1). kcat/Km: printed Table 3 Leucine-group cell 1013 under the column head k cat /K m (s-1 . mM-1); that column is already in s^-1 mM^-1, so no unit conversion applies and the paper value is 1013.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, Leucine column group, enzyme row Ph LeuRS: K m = 5.92 uM; k cat = 6.0 s^-1; printed k cat /K m = 1013 s^-1 . mM^-1.

table_label: Table 3: Steady-state leucine activation kinetics of Ph LeuRS and its single-point mutants (Biochem. J. 2010, 429(3):505-513)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D121A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y105A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W103A with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T118A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I115A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K100A/Y105A with inferred residue-numbering offset -33 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E114A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D98A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F119A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T101A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K100A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V108A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N96A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K100A/Y109A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R106A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y109A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D121A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R97A to reconstruct the assayed variant sequence.


organism: Pseudomonas putida

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

proof_lines: kcat is 47 sec(-1) for HCCA, 19 sec(-1) for THBPA and 39 sec(-1) for glutathion.


substrate_name: glutathione (at pH 7 and 25 degrees Celsius)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D173A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E167A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8.2; 318.15 K; cofactor ATP


enzyme_display_name: lactoylglutathione lyase

substrate_name: glutathione-methylglyoxal

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

enzyme: lactoylglutathione lyase

substrate: glutathione-methylglyoxal


enzyme_display_name: tyrosine--tRNA ligase

substrate_name: L-tyrosine

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

proof_lines:
mutant TyrRS, RMSSS
mutant TyrRS, AMSSS
mutant TyrRS, KMGCA

enzyme: tyrosine--tRNA ligase

substrate: L-tyrosine


substrate_name: L-leucine

proof_lines: mutant lacking residues Q281 to D294, 45°C

proof_lines: mutant lacking residues S295 to L304, 45°C


assay_conditions_summary: 318.15 K; cofactor ATP


organism: Saccharolobus solfataricus

substrate_name: L-serine

proof_lines: pH 7.2, 60°C, recombinant wild-type enzyme

substrate: L-serine


substrate_name: L-threonine

substrate: L-threonine


proof_lines: kcat is 5.8 sec(-1) for the activation reaction of L-threonine. kcat is 1.1 sec(-1) for the activation reaction of L-serine. kcat is 0.061 sec(-1) for the aminoacylation of tRNA(Thr) with L-threonine.


organism: Escherichia coli (strain K12)

substrate_name: azatyrosine

proof_lines: kcat is 0.74 sec(-1) with L-tyrosine as substrate. kcat is 0.11 sec(-1) with azatyrosine as substrate.

substrate: azatyrosine


enzyme_display_name: diaminopimelate epimerase

organism: Haemophilus influenzae

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

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

enzyme: diaminopimelate epimerase


organism: Acidithiobacillus ferrooxidans

substrate_name: ATP


substrate_name: tyrosine

substrate: tyrosine


organism: Bacillus subtilis

substrate_name: L-Isoleucine; tRNA(Ile); ATP

substrate: L-Isoleucine; tRNA(Ile); ATP


substrate_name: ATP; Isoleucine

substrate: ATP; Isoleucine


substrate_name: ATP; L-Isoleucine; tRNA(Ile)

substrate: ATP; L-Isoleucine; tRNA(Ile)


substrate_name: tRNA(Ile); L-Isoleucine; ATP

substrate: tRNA(Ile); L-Isoleucine; ATP


organism: Staphylococcus aureus

substrate_name: L-Isoleucine; ATP; tRNA(Ile)

substrate: L-Isoleucine; ATP; tRNA(Ile)


organism: Aeropyrum pernix

substrate_name: tRNATyr

proof_lines: wild type enzyme, at 55°C, in 100 mM HEPES-NaOH (pH 8.0), 10 mM MgCl2, 10 mM KCl

substrate: tRNATyr


substrate_name: ATP; tRNA(Tyr); L-Tyrosine

substrate: ATP; tRNA(Tyr); L-Tyrosine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D268R with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: tRNA(Tyr)

proof_lines: The catalytic activity is reduced by substitutions of residues forming the specificity determinant on the target tRNA(Tyr).

substrate: tRNA(Tyr)


substrate_name: Unknown

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


enzyme_display_name: tryptophan--tRNA ligase

substrate_name: tRNA(Trp); ATP; L-Tryptophan

enzyme: tryptophan--tRNA ligase

substrate: tRNA(Trp); ATP; L-Tryptophan


organism: Mus musculus

substrate_name: tRNA(Thr)

substrate: tRNA(Thr)


substrate_name: tRNA(Leu); L-Leucine; ATP

substrate: tRNA(Leu); L-Leucine; ATP


organism: Homo sapiens

substrate_name: L-Leucine; ATP; tRNA(Leu)

substrate: L-Leucine; ATP; tRNA(Leu)


substrate_name: tRNA

substrate: tRNA


organism: Thiobacillus ferrooxidans

substrate_name: tRNA(Tyr); L-Tyrosine; ATP

substrate: tRNA(Tyr); L-Tyrosine; ATP


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

substrate_name: L-threonine activation

substrate: L-threonine activation


organism: Burkholderia thailandensis

proof_lines: Ki above 0.05 mM, with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication

substrate: Unknown


proof_lines: kcat is 36, 22 and 26 sec(-1) for L-threonine, beta-hydroxynorvaline and L-serine respectively.


organism: Methanocaldococcus jannaschii


organism: Giardia duodenalis

substrate_name: L-leucine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q154A to reconstruct the assayed variant sequence.

substrate: L-leucine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K152A to reconstruct the assayed variant sequence.


substrate_name: ATP

substrate: ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K170A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K148A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K166A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K144A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E165A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W155A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K139A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S153A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K141A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K142A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D173A to reconstruct the assayed variant sequence.


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

substrate_name: L-serine activation

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

proof_lines: kcat is 12.3 sec(-1) for L-serine, 13.5 for L-threonine at 60 degrees Celsius (PubMed:15240874). kcat is 1.2 sec(-1) (PubMed:15507440).

substrate: L-serine activation


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

proof_lines: kcat is 1.3 sec(-1) for L-serine, 1.9 for L-threonine at 60 degrees Celsius (PubMed:15240874).


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D423A with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D423A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R439A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R439A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R434A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R434A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N400A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N400A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S409E with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S409E, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K408A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K408A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E405A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E405A, in 100 mM Na-HEPES pH 7.2, 30 mM KCl, 10 mM MgCl2C, temperature not specified in the publication


organism: Yersinia pestis

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

proof_lines: Ki above 0.05 mM with L-serine as substrate, in 60 mM Tris, pH 7.6, 10 mM MgCl2, 20 mM KCl, temperature not specified in the publication


organism: Aquifex aeolicus

substrate_name: tRNALeu

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q269ter with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

substrate: tRNALeu


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -6, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -3, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -11, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -13, so it is treated as a source-provided variant sequence.


proof_lines:
wild-type, pH 8.2, 45°C
wild-type, 45°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V286ter to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K238A to reconstruct the assayed variant sequence.


substrate_name: L-isoleucyl-tRNALeu

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y520A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

substrate: L-isoleucyl-tRNALeu


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

proof_lines:
wild-type, pH 7.5, 37°C
wild-type, 45°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y520H with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


organism: Pseudomonas putida


organism: Acanthamoeba polyphaga mimivirus


organism: Geobacillus stearothermophilus

substrate_name: L-Tyrosine; ATP

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

unit: molwedgeoneswedgeone

substrate: L-Tyrosine; ATP


substrate_name: L-Tyrosine; ATP; tRNA(Tyr)

substrate: L-Tyrosine; ATP; tRNA(Tyr)