organism: Enterococcus faecalis

sequence_source: UniProtKB reviewed FASTA Q837U7 (PTC_ENTFA), Enterococcus faecalis strain V583; UniProt recommended EC 2.1.3.6.

proof_lines: recombinant wild-type enzyme, pH 8.5, 37°C


enzyme_display_name: ornithine carbamoyltransferase

substrate_name: L-ornithine

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA Q837U7 (PTC_ENTFA), Enterococcus faecalis strain V583; UniProt recommended EC 2.1.3.6. and applied mutation signature Y230V/G231S/L232M/Y233G to reconstruct the assayed variant sequence.

proof_lines: recombinant enzyme mutant Y230V/G231S/L232M/Y233G, pH 8.5, 37°C

enzyme: ornithine carbamoyltransferase

substrate: L-ornithine

source: brenda


organism: Escherichia coli

substrate_name: L-ornithine, Carbamoyl phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA P04391 (OTC1_ECOLI), Escherichia coli K-12 ornithine carbamoyltransferase subunit I; UniProt recommended EC 2.1.3.3. and applied mutation signature Y229S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

mutation_type: substitution

substrate: L-ornithine, Carbamoyl phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA P04391 (OTC1_ECOLI), Escherichia coli K-12 ornithine carbamoyltransferase subunit I; UniProt recommended EC 2.1.3.3. and applied mutation signature Y229F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: Carbamoyl phosphate, L-ornithine

sequence_source: UniProtKB reviewed FASTA P04391 (OTC1_ECOLI), Escherichia coli K-12 ornithine carbamoyltransferase subunit I; UniProt recommended EC 2.1.3.3.

sequence_variant_note: Mutation signature E299D could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: Carbamoyl phosphate, L-ornithine


mutation_signature: Unknown

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 UniProtKB reviewed FASTA P04391 (OTC1_ECOLI), Escherichia coli K-12 ornithine carbamoyltransferase subunit I; UniProt recommended EC 2.1.3.3. and applied mutation signature Y160S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature D231A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA P04391 (OTC1_ECOLI), Escherichia coli K-12 ornithine carbamoyltransferase subunit I; UniProt recommended EC 2.1.3.3. and applied mutation signature R57A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA P04391 (OTC1_ECOLI), Escherichia coli K-12 ornithine carbamoyltransferase subunit I; UniProt recommended EC 2.1.3.3. and applied mutation signature S61A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA P04391 (OTC1_ECOLI), Escherichia coli K-12 ornithine carbamoyltransferase subunit I; UniProt recommended EC 2.1.3.3. and applied mutation signature H272N with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA P04391 (OTC1_ECOLI), Escherichia coli K-12 ornithine carbamoyltransferase subunit I; UniProt recommended EC 2.1.3.3. and applied mutation signature Y160F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA P04391 (OTC1_ECOLI), Escherichia coli K-12 ornithine carbamoyltransferase subunit I; UniProt recommended EC 2.1.3.3. and applied mutation signature D140N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA P04391 (OTC1_ECOLI), Escherichia coli K-12 ornithine carbamoyltransferase subunit I; UniProt recommended EC 2.1.3.3. and applied mutation signature C273A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA P04391 (OTC1_ECOLI), Escherichia coli K-12 ornithine carbamoyltransferase subunit I; UniProt recommended EC 2.1.3.3. and applied mutation signature E299Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA P04391 (OTC1_ECOLI), Escherichia coli K-12 ornithine carbamoyltransferase subunit I; UniProt recommended EC 2.1.3.3. and applied mutation signature Q104L with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


organism: Lathyrus oleraceus

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

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

substrate: Unknown


organism: Moritella abyssi

sequence_source: NCBI Protein/UniProt Q9K4Y9 linked from PMID:12644485


organism: Mycobacterium tuberculosis variant bovis

substrate_name: Carbamoyl phosphate

sequence_source: NCBI Protein CAA45530.1 linked from PMID:1406593

proof_lines: determined in the presence of 0.5 mM ornithine and 0.5 mM carbamoylphosphate

substrate: Carbamoyl phosphate


organism: Ovis aries

sequence_source: NCBI Protein/UniProt P84010 linked from PMID:14527149; PDB 1FB5 is also linked as the structural chain


organism: Piaractus mesopotamicus

assay_conditions_summary: pH 7

proof_lines: liver enzyme, presence of putrescine, pH 7.0


organism: Pseudomonas aeruginosa

substrate_name: ornithine

sequence_source: NCBI Protein/UniProt P08308 linked from PMID:2118516

substrate: ornithine


proof_lines:
mutant arcB6254, pH 7.25
mutant arcB6240, pH 7.25


organism: Pseudomonas savastanoi

substrate_name: Diaminobutane

substrate: Diaminobutane


organism: Pyrococcus furiosus

sequence_source: Reconstructed from UniProt Q51742 linked from PMID:11208811

sequence_variant_note: Mutation signature A240D/E277G matches the mutant residue at offset +1 and the reference residue at offset -35; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines:
A240D/E277G double mutant, at 55°C
A240D/E277G double mutant, at 30°C


sequence_source: NCBI Protein/UniProt Q51742 linked from PMID:11208811

proof_lines:
at 55°C
at 30°C


sequence_variant_note: Mutation signature Y227C/E277G matches the mutant residue at offset +1 and the reference residue at offset -37; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines:
Y227C/E277G double mutant, at 55°C
Y227C/E277G double mutant, at 30°C


organism: Rattus norvegicus

proof_lines: at 30°C and pH 7.4, competitive vs. carbamoyl phosphate, noncompetitive vs. ornithine


enzyme_display_name: Ornithine carbamoyltransferase

enzyme_name_source: UniProtKB:P05150 targeted protein-name/EC/organism lookup

organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from UniProtKB:P05150 targeted OTCase EC 2.1.3.3 lookup; variant reconstructed by coordinate substitution and applied mutation signature K265A to reconstruct the assayed variant sequence.

enzyme: Ornithine carbamoyltransferase


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05150 targeted OTCase EC 2.1.3.3 lookup; variant reconstructed by coordinate substitution and applied mutation signature D182N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P05150 targeted OTCase EC 2.1.3.3 lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05150 targeted OTCase EC 2.1.3.3 lookup; variant reconstructed by coordinate substitution and applied mutation signature K260R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05150 targeted OTCase EC 2.1.3.3 lookup; variant reconstructed by coordinate substitution and applied mutation signature E256Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05150 targeted OTCase EC 2.1.3.3 lookup; variant reconstructed by coordinate substitution and applied mutation signature K263A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05150 targeted OTCase EC 2.1.3.3 lookup; variant reconstructed by coordinate substitution and applied mutation signature E256A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05150 targeted OTCase EC 2.1.3.3 lookup; variant reconstructed by coordinate substitution and applied mutation signature C191M/C194N/F197V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05150 targeted OTCase EC 2.1.3.3 lookup; variant reconstructed by coordinate substitution and applied mutation signature E123S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05150 targeted OTCase EC 2.1.3.3 lookup; variant reconstructed by coordinate substitution and applied mutation signature K260A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05150 targeted OTCase EC 2.1.3.3 lookup; variant reconstructed by coordinate substitution and applied mutation signature K268R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05150 targeted OTCase EC 2.1.3.3 lookup; variant reconstructed by coordinate substitution and applied mutation signature L290Q to reconstruct the assayed variant sequence.


sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from UniProtKB P00480 FASTA direct lookup; reconstructed by applying K307A to the canonical sequence and applied mutation signature K307A to reconstruct the assayed variant sequence.

proof_lines: mutant K307A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P00480 FASTA direct lookup; reconstructed by applying E98Q to the canonical sequence and applied mutation signature E98Q to reconstruct the assayed variant sequence.

proof_lines: mutant E98Q, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P00480 FASTA direct lookup; reconstructed by applying A152V to the canonical sequence and applied mutation signature A152V to reconstruct the assayed variant sequence.

proof_lines: mutant A152V, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P00480 FASTA direct lookup; reconstructed by applying H107N to the canonical sequence and applied mutation signature H107N to reconstruct the assayed variant sequence.

proof_lines: mutant H107N, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P00480 FASTA direct lookup; reconstructed by applying K307E to the canonical sequence and applied mutation signature K307E to reconstruct the assayed variant sequence.

proof_lines: mutant K307E, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P00480 FASTA direct lookup; reconstructed by applying E310Q to the canonical sequence and applied mutation signature E310Q to reconstruct the assayed variant sequence.

proof_lines: mutant E310Q, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P00480 FASTA direct lookup; reconstructed by applying C303A to the canonical sequence and applied mutation signature C303A to reconstruct the assayed variant sequence.

proof_lines: mutant C303A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P00480 FASTA direct lookup; reconstructed by applying Q171A to the canonical sequence and applied mutation signature Q171A to reconstruct the assayed variant sequence.

proof_lines: mutant Q171A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P00480 FASTA direct lookup; reconstructed by applying D263N to the canonical sequence and applied mutation signature D263N to reconstruct the assayed variant sequence.

proof_lines: mutant D263N, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P00480 FASTA direct lookup; reconstructed by applying H302L to the canonical sequence and applied mutation signature H302L to reconstruct the assayed variant sequence.

proof_lines: mutant H302L, pH and temperature not specified in the publication


sequence_source: UniProtKB P00480 FASTA direct lookup

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

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


organism: Pyrococcus abyssi

sequence_source: UniProtKB O93656 FASTA direct lookup


organism: Thermus thermophilus

sequence_source: UniProtKB/Swiss-Prot:P96134; NCBI Protein:3183103; GenBank:Y10266


organism: Alnus glutinosa

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

proof_lines:
at 2 mM carbamoyl phosphate
at 10 mM carbamoyl phosphate


organism: Bacillus subtilis


organism: Chlorella vulgaris var. autotrophica


organism: Escherichia coli

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


proof_lines: mixed or competitive vs. carbamoyl phosphate


organism: Giardia duodenalis

substrate_name: L-citrulline

sequence_source: UniProt O76458 via RCSB 3GRF entity 1 and PMID 19507245

substrate: L-citrulline


enzyme_display_name: carbonic anhydrase

assay_conditions_summary: pH 8.98; buffer conditions

proof_lines: pH 8.98, TAPS buffer, carbonic anhydrase I mutant V62N and carbonic anhydrase I mutant H67N

proof_lines: pH 8.88, TAPS buffer, carbonic anhydrase I mutant V62N,H67N

proof_lines: pH 8.72, 1,2-dimethyimidazole buffer, carbonic anhydrase I mutant V62N,H67N

enzyme: carbonic anhydrase


organism: Methanosarcina thermophila

assay_conditions_summary: pH 7.5; 298.15 K; buffer conditions

proof_lines: pH 7.5, 25°C, variant E84A, 50 mM MOPS-Ac buffer

proof_lines: pH 7.5, 25°C, variant E84A, 50 mM MOPS buffer

proof_lines: pH 7.5, 25°C, variant E84A, 50 mM IMID buffer


sequence_source: UniProtKB:P40881 identity checked; row-specific variant sequence not accepted without exact kinetic evidence

smiles: O=C=O

assay_conditions_summary: pH 7.5; 298.15 K; buffer condition for CO2

proof_lines: pH 7.5, 25°C, variant E84Q, 50 mM MOPS buffer


assay_conditions_summary: pH 7.5; 298.15 K; buffer pH 7.5 MOPS

proof_lines: pH 7.5, 25°C, variant E84D, 50 mM MOPS buffer


enzyme_display_name: cholinesterase

substrate_name: Benzoylcholine

enzyme: cholinesterase

substrate: Benzoylcholine


substrate_name: butyrylthiocholine

substrate: butyrylthiocholine


substrate_name: succinylthiocholine

substrate: succinylthiocholine


proof_lines:
W82A mutant, pH 7, 25°C
pH 8, 25°C, W82A mutant


proof_lines:
A328Y mutant, pH 7, 25°C
pH 8, 25°C, A328Y mutant


enzyme_display_name: GDP-fucose protein O-fucosyltransferase 1

enzyme_name_source: UniProtKB P83337

organism: Cricetulus griseus

substrate_name: factor VII EGF

sequence_source: UniProtKB P83337 via NCBI pubmed_protein link from PMID 9525914

substrate: factor VII EGF


organism: Amblyomma americanum

substrate_name: butanoylthiocholine

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

substrate: butanoylthiocholine


organism: Berryteuthis magister

substrate_name: propionylthiocholine

substrate: propionylthiocholine


organism: Chelidonichthys lucerna

proof_lines: enzyme isolated from muscle, 25°C, pH not specified in the publication

proof_lines: enzyme isolated from brain, 25°C, pH not specified in the publication


organism: Diopatra neapolitana


organism: Eisenia andrei

substrate_name: propionylthiocholine iodide

substrate: propionylthiocholine iodide


organism: Equus caballus


organism: Gallotia galloti

substrate_name: butyrylthiocholine iodide

substrate: butyrylthiocholine iodide


organism: Gambusia yucatana

proof_lines: enzyme from muscle, pH 7.4, temperature not specified in the publication

proof_lines: enzyme from head, pH 7.4, temperature not specified in the publication


organism: Homo sapiens


proof_lines: A539T mutant, E497V/A539T mutant and E497V mutant, pH 7, 25°C


organism: Bos taurus

sequence_source: UniProtKB accession P32749 direct lookup on 2026-06-26


sequence_source: UniProtKB accession Q9N1N9 direct lookup on 2026-06-26


sequence_source: UniProtKB accession P81908 direct lookup on 2026-06-26


substrate_name: Butyrylthiocholine

source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

sequence_source: UniProtKB accession P06276 direct lookup on 2026-06-26

smiles: CCCC(=O)SCC[N+](C)(C)C

data_origin: experimental

substrate: Butyrylthiocholine

status: unverified

source: oed


substrate_name: (-)-cocaine

sequence_variant_note: Mutation signature A328W could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: (-)-cocaine


proof_lines: wild-type, adapted method using probe IV, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB accession P06276 direct lookup on 2026-06-26 and applied mutation signature A328W/Y332A with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature Y332A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: benzoylthiocholine

proof_lines: reconmbinant enzyme produced in rice, pH not specified in the publication, temperature not specified in the publication

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

substrate: benzoylthiocholine


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

proof_lines:
recombinant enzyme, pH 8.0, 22°C
recombinant enzyme, pH 7.4, 37°C
pH 7.4, 25°C

source_databases_merged: brenda skid


substrate_name: acetylthiocholine

smiles: CC(=O)SCC[N+](C)(C)C

substrate: acetylthiocholine


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from UniProt:P06276 reviewed CHLE_HUMAN canonical precursor; selected BChE mutation numbering matches mature chain with +28 signal-peptide offset and applied mutation signature A277W with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from UniProt:P06276 reviewed CHLE_HUMAN canonical precursor; selected BChE mutation numbering matches mature chain with +28 signal-peptide offset and applied mutation signature V288F with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P06276 reviewed CHLE_HUMAN canonical precursor; selected BChE mutation numbering matches mature chain with +28 signal-peptide offset and applied mutation signature Q119Y with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P06276 reviewed CHLE_HUMAN canonical precursor; selected BChE mutation numbering matches mature chain with +28 signal-peptide offset and applied mutation signature Q119Y/V288F/A328Y with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P06276 reviewed CHLE_HUMAN canonical precursor; selected BChE mutation numbering matches mature chain with +28 signal-peptide offset and applied mutation signature D70G with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.

proof_lines:
mutant D70G, pH 7.4, 25°C
pH 7.4, 25°C, D70G mutant
pH 7, 25°C, D70G mutant


sequence_variant_note: Resolved canonical sequence from UniProt:P06276 reviewed CHLE_HUMAN canonical precursor; selected BChE mutation numbering matches mature chain with +28 signal-peptide offset and applied mutation signature G333C with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P06276 reviewed CHLE_HUMAN canonical precursor; selected BChE mutation numbering matches mature chain with +28 signal-peptide offset and applied mutation signature R470W with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P06276 reviewed CHLE_HUMAN canonical precursor; selected BChE mutation numbering matches mature chain with +28 signal-peptide offset and applied mutation signature K12R with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P06276 reviewed CHLE_HUMAN canonical precursor; selected BChE mutation numbering matches mature chain with +28 signal-peptide offset and applied mutation signature V294M with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.


substrate_name: cocaine

sequence_variant_note: Resolved canonical sequence from UniProt:P06276 reviewed CHLE_HUMAN canonical precursor; selected BChE mutation numbering matches mature chain with +28 signal-peptide offset and applied mutation signature A328W/Y332A with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.

substrate: cocaine


substrate_name: Acetylcholine

sequence_variant_note: Resolved canonical sequence from UniProt:P06276 reviewed CHLE_HUMAN canonical precursor; selected BChE mutation numbering matches mature chain with +28 signal-peptide offset and applied mutation signature A199S/F227A/S287G/A328W/Y332G/E441D with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A199S/F227A/S287G/A328W/Y332G/E441D, pH not specified in the publication, at 25°C

substrate: Acetylcholine


sequence_variant_note: Resolved canonical sequence from UniProt:P06276 reviewed CHLE_HUMAN canonical precursor; selected BChE mutation numbering matches mature chain with +28 signal-peptide offset and applied mutation signature A199S/F227A/S287G/A328W/E441D with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A199S/F227A/S287G/A328W/E441D, pH not specified in the publication, at 25°C


substrate_name: butyryl thiocholine iodide

proof_lines: pH 7, mutant with only 5 N-glycosylation sites

substrate: butyryl thiocholine iodide


substrate_name: N-methylindoxyl acetate

substrate: N-methylindoxyl acetate


assay_conditions_summary: pH 5

proof_lines: pH 5, A328W and E197Q mutant, absence of excess substrate


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

proof_lines: pH 5, wild-type enzyme, absence of excess substrate


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

proof_lines: pH 5, A328G mutant, absence of excess substrate


proof_lines: pH 5, L286W mutant, absence of excess substrate

proof_lines: pH 5, L286W mutant, presence of excess substrate


proof_lines: pH 5, A328F mutant, absence of excess substrate

proof_lines: pH 5, A328F mutant, presence of excess substrate


proof_lines: pH 5, Y332A mutant, presence of excess substrate

proof_lines: pH 5, Y332A mutant, absence of excess substrate


proof_lines: pH 5, V288W mutant, absence of excess substrate

proof_lines: pH 5, V288W mutant, presence of excess substrate


proof_lines: pH 5, A328I mutant, presence of excess substrate

proof_lines: pH 5, A328I mutant, absence of excess substrate


proof_lines: mutant enzyme A199S/S287G/A328W/Y332G, pH not specified in the publication, at 25°C

proof_lines: mutant enzyme A199S/S287G/A328W/Y332G, at 25°C, in 0.1 M potassium phosphate, pH 7.5


substrate_name: Benzoylcholine

proof_lines:
usual and atypical enzyme
pH 7.4, 37°C
pH 7.0, 30°C

substrate: Benzoylcholine


organism: Lumbriculus variegatus

substrate_name: butyrylthiocholine

assay_conditions_summary: pH 7.5; 303.15 K; buffer assay condition

proof_lines: in 0.1 M phosphate buffer, pH 7.5, at 30°C

substrate: butyrylthiocholine


organism: Mus musculus


organism: Oncorhynchus gorbuscha


organism: Oncorhynchus keta


organism: Oncorhynchus kisutch


organism: Oncorhynchus nerka


organism: Oreochromis niloticus

proof_lines: with methanolic extract of Enteromorpha intestinalis (1.4 - 7 mg/ml), Vmax: 192.8 nmole/min/mg protein

proof_lines: with methanolic extract of Dictyota dichotoma (1.3 - 6.5 mg/ml), Vmax: 232.8 nmole/min/mg protein


organism: Oryctolagus cuniculus

proof_lines:
mBuChE II
ChE I and ChE II
mBuChE I


organism: Oryza sativa


organism: Potamopyrgus antipodarum


sequence_source: UniProtKB reviewed accession P06276; direct UniProt REST check on 2026-06-26

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


substrate_name: heroin

verification_status: corrected

assay_conditions_summary: pH 7.4; 310.15 K; buffer 0.1 M phosphate

column_label: Table 1. Kinetic parameters of BChE, AChE, and CocHl against heroin Table 1, heroin row, enzyme column BChE; column 'K_M (uM)' = 120; column 'kcat (min^-1)' = 1840; column 'k_cat/K_M (min^-1 M^-1)' = 1.53 x 10^7.

normalized_value_unit_evidence: Km: printed cell 120 uM converts to 0.12 mM; the exported value is 0.12 mM. kcat: printed cell 1840 min^-1 converts to 30.666666666666668 s^(-1); the exported value is 30.67 s^(-1). kcat/Km: printed cell 1.53 x 10^7 min^-1 M^-1 converts to 255.0 s^(-1)*mM^(-1); the exported value is 255.58333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1. Kinetic parameters of BChE, AChE, and CocHl against heroin Table 1, heroin row, enzyme column BChE: Km = 120 uM; kcat = 1840 min^-1; printed kcat/Km = 1.53 x 10^7 min^-1 M^-1.

row_label: Table 1, heroin row, enzyme column BChE

substrate: heroin

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P06276; direct UniProt REST check on 2026-06-26 and applied mutation signature E197Q with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: mutant E197Q, adapted method using probe IV, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant E197Q, classical Ellmans method, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P06276; direct UniProt REST check on 2026-06-26 and applied mutation signature E197G with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: mutant E197G, adapted method using probe IV, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant E197G, classical Ellmans method, pH not specified in the publication, temperature not specified in the publication


substrate_name: Acetylthiocholine

sequence_source: UniProtKB reviewed accession Q03311; direct UniProt REST check on 2026-06-26

substrate: Acetylthiocholine


organism: Sus scrofa

sequence_source: UniProtKB reviewed accession P32752; direct UniProt REST check on 2026-06-26

proof_lines:
recombinant enzyme, pH 8.0, 22°C
pH 8.0, 22°C


enzyme_display_name: peptide-O-fucosyltransferase

organism: Arabidopsis thaliana

substrate_name: GDP-beta-L-fucose

source_db: uniprot

enzyme: peptide-O-fucosyltransferase

substrate: GDP-beta-L-fucose

source: uniprot


organism: Cricetulus griseus


substrate_name: F7 EGF domain

substrate: F7 EGF domain


substrate_name: GDP-fucose

substrate: GDP-fucose


substrate_name: Thr-216 of MMRN1 protein

substrate: Thr-216 of MMRN1 protein


substrate_name: butyrylthiocholine (at 25 degrees Celsius)


organism: Pseudomonas aeruginosa

substrate_name: propionylthiocholine

substrate: propionylthiocholine


organism: Pseudopleuronectes yokohamae

proof_lines: pH 7.6, mean value of different animal muscle samples, overview


organism: Rattus norvegicus


proof_lines: pH 8, 37°C, liver, soluble form, component I


organism: Salmo salar


organism: Sardina pilchardus

substrate_name: butanoylthiocholine

proof_lines: enzyme isolated from brain, 25°C, pH not specified in the publication

proof_lines: enzyme isolated from muscle, 25°C, pH not specified in the publication

substrate: butanoylthiocholine


organism: Scomber scombrus


organism: Sparus aurata

proof_lines: pH 7.4, 25°C, enzyme from yolk-sac of seabream larvae stage


organism: Trichinella spiralis

substrate_name: acetylcholine iodide

proof_lines:
fraction 5.3S
fraction 13S

substrate: acetylcholine iodide


organism: Valvata piscinalis


organism: Vigna radiata var. radiata


substrate_name: factor VII EGF

substrate: factor VII EGF


organism: Homo sapiens

sequence_source: UniProtKB reviewed exact accession Q9H488 (OFUT1_HUMAN), checked 2026-06-26

enzyme: GDP-fucose protein O-fucosyltransferase 1


enzyme_display_name: GDP-fucose protein O-fucosyltransferase 3

substrate_name: GDP-L-fucose

sequence_source: UniProtKB reviewed exact accession Q6P4F1 (OFUT3_HUMAN), checked 2026-06-26

substrate: GDP-L-fucose


enzyme_display_name: GDP-fucose protein O-fucosyltransferase 2

sequence_source: UniProtKB reviewed exact accession Q9Y2G5 (OFUT2_HUMAN), checked 2026-06-26

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: GDP-fucose protein O-fucosyltransferase 4

sequence_source: UniProtKB reviewed exact accession Q495W5 (OFUT4_HUMAN), checked 2026-06-26

proof_lines:
pH 7.0, 37Â°C, T216 O-fucosylation site
pH 7.0, 37Â°C, T265 O-fucosylation site


enzyme_display_name: sucrose alpha-glucosidase

organism: Bacillus subtilis

substrate_name: p-nitrophenyl-alpha-D-glucoside

enzyme: sucrose alpha-glucosidase

substrate: p-nitrophenyl-alpha-D-glucoside


organism: Gallus gallus

substrate_name: sucrose

substrate: sucrose


substrate_name: maltose

assay_conditions_summary: pH 6

proof_lines: mutant enzyme V638A, pH 6.0, temperature not specified in the publication

substrate: maltose


proof_lines: mutant enzyme Q265N, pH 6.0, temperature not specified in the publication


proof_lines: wild-type enzyme, pH 6.0, temperature not specified in the publication


proof_lines: mutant enzyme Q265A, pH 6.0, temperature not specified in the publication


proof_lines: mutant enzyme V638L, pH 6.0, temperature not specified in the publication


proof_lines: mutant enzyme L266V, pH 6.0, temperature not specified in the publication


proof_lines: mutant enzyme L266A, pH 6.0, temperature not specified in the publication


organism: Mus musculus

proof_lines: inbred strains of mice with genetic and posttranslational variations in SI complex structure, incubation at 37°C


organism: Oryctolagus cuniculus

proof_lines: value remains constant at Li+ concentration from 20-120 mM


sequence_source: UniProt P14410 direct lookup


proof_lines: recombinant wild-type enzyme, pH 6.2, 37°C, in presence of 0.7 mM glucose


sequence_variant_note: Resolved canonical sequence from UniProt P14410 direct lookup plus reviewer-applied substitution from selected mutation_signature and applied mutation signature D1500Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt P14410 direct lookup plus reviewer-applied substitution from selected mutation_signature and applied mutation signature D604Y to reconstruct the assayed variant sequence.


organism: Pyrococcus furiosus

substrate_name: panose

proof_lines: 90°C, pH not specified in the publication

substrate: panose


organism: Xanthomonas axonopodis


organism: Perna viridis


organism: Platyrrhini


organism: Rattus rattus

proof_lines: the existence of 2 Km values supports the notion of substrate hydrolysis at 2 active sites on the sucrase-isomaltase complex


organism: Saccharomyces cerevisiae

proof_lines: pH 7.0, temperature not specified in the publication


organism: Streptococcus salivarius


organism: Sus scrofa

substrate_name: Unknown

substrate: Unknown


organism: Xanthomonas campestris pv. campestris

sequence_source: RCSB 2WPG chain A SIFTS mapping to UniProt Q8P5I2; UniProt Q8P5I2 FASTA


enzyme_display_name: undecaprenyl-diphosphate phosphatase

organism: Escherichia coli (strain K12)

substrate_name: undecaprenyl pyrophosphate

enzyme: undecaprenyl-diphosphate phosphatase

substrate: undecaprenyl pyrophosphate


organism: Escherichia coli

substrate_name: undecaprenyl diphosphate

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

substrate: undecaprenyl diphosphate


organism: Micrococcus luteus


substrate_name: farnesyl diphosphate

sequence_source: UniProtKB:P60932 direct lookup on 2026-06-26

substrate: farnesyl diphosphate


organism: Vibrio vulnificus


enzyme_display_name: beta-lactamase

substrate_name: cefalotin

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

enzyme: beta-lactamase

substrate: cefalotin


substrate_name: ceftazidime

substrate: ceftazidime


organism: Klebsiella pneumoniae

substrate_name: ticarcillin

substrate: ticarcillin


organism: Pseudomonas aeruginosa

substrate_name: cefepime

sequence_source: UniProtKB Q3SAW3 direct REST lookup on 2026-06-26

substrate: cefepime


substrate_name: Imipenem

sequence_source: UniProtKB Q9XAY4 direct REST lookup on 2026-06-26

substrate: Imipenem


substrate_name: meropenem

sequence_source: UniProtKB Q2HY42 direct REST lookup on 2026-06-26

substrate: meropenem


organism: Pseudomonas putida

sequence_source: UniProtKB Q8GCU7 direct REST lookup on 2026-06-26

proof_lines: enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin

proof_lines: inhibitor binding constant (Ki) using 10 microM nitrocefin as indicator substrate


organism: Bacteroides fragilis

proof_lines: pH and temperature not specified in the publication


organism: Enterobacter cloacae

assay_conditions_summary: pH 7; 303.15 K; buffer 50mM sodium phosphate

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

proof_lines: at 30°C in 50mM sodium phosphate buffer (pH 7.0)


substrate_name: aztreonam

substrate: aztreonam


organism: Serratia marcescens

substrate_name: nitrocefin

sequence_source: UniProtKB direct accession lookup for P52699 on 2026-06-26

proof_lines:
pH 7.5, 25°C
at 30°C

substrate: nitrocefin


organism: Shewanella algae

substrate_name: Cloxacillin

sequence_source: UniProtKB direct accession lookup for Q6VCW0 on 2026-06-26

substrate: Cloxacillin


organism: Shewanella frigidimarina

substrate_name: cefaloridine

sequence_source: UniProtKB direct accession lookup for Q53BU0 on 2026-06-26

substrate: cefaloridine


organism: Shewanella livingstonensis

substrate_name: piperacillin

sequence_source: UniProtKB direct accession lookup for Q53BU1 on 2026-06-26

substrate: piperacillin


organism: Psychrobacter immobilis

substrate_name: benzylpenicillin

sequence_source: UniProtKB reviewed O05465 / AMPC_PSYIM; primary paper PMID 9063463; GenBank X83586

substrate: benzylpenicillin


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


substrate_name: cefoxitin

sequence_source: UniProtKB:C7C422 direct lookup 2026-06-26

substrate: cefoxitin


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB:P9WKD3 direct lookup 2026-06-26


organism: Burkholderia pseudomallei


organism: Citrobacter freundii

substrate_name: cefazolin

substrate: cefazolin


organism: Elizabethkingia meningoseptica

substrate_name: cefotaxime

substrate: cefotaxime


organism: Escherichia coli

substrate_name: ampicillin

assay_conditions_summary: pH 7; 303.15 K; buffer 50 mM phosphate

proof_lines: 30°C, pH 7.0, plasmid-encoded, pBC2e, beta-lactamase MIR-1

proof_lines: 30°C, pH 7.0, plasmid-encoded, pBC3e, beta-lactamase CMY-1

proof_lines: 30°C, pH 7.0, plasmid-encoded, pBC4e, beta-lactamase CMY-2

substrate: ampicillin


substrate_name: penicillin G

proof_lines: mutant R61H/E64H/43H, 25°C, pH not specified in the publication

substrate: penicillin G


proof_lines: mutant M182T/T195S/A224V, 25°C, pH not specified in the publication


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


organism: Fluoribacter gormanii

substrate_name: Unknown

substrate: Unknown


organism: plasmid pBG66

proof_lines: pH and temperature not specified in the publication, mutant enzyme N166A/N170G


substrate_name: cephalexin

proof_lines: pH and temperature not specified in the publication, mutant enzyme N170G

substrate: cephalexin


proof_lines: pH and temperature not specified in the publication, mutant enzyme N170A


organism: plasmid pGEM-T-easy

proof_lines: mutant enzyme W154A, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate

proof_lines: mutant enzyme W154A, 25°C, pH 7, in presence of 50 mM sodium bicarbonate


proof_lines: mutant enzyme W154G, 25°C, pH 7, in presence of 50 mM sodium bicarbonate

proof_lines: mutant enzyme W154G, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate


substrate_name: cephalothin

proof_lines: mutant enzyme W154H, 25°C, pH 7, in presence of 50 mM sodium bicarbonate

proof_lines: mutant enzyme W154H, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate

substrate: cephalothin


proof_lines: wild-type, 25°C, pH 7, in presence of 50 mM sodium bicarbonate

proof_lines: wild-type, 25°C, pH 7, in presence of 1.1 mM sodium bicarbonate


proof_lines: mutant enzyme W154F, 25°C, pH 7, in presence of 50 mM sodium bicarbonate


organism: plasmid pQE32Chl17


organism: plasmid RGN238

substrate_name: cephaloridine

proof_lines: pH and temperature not specified in the publication, OXA-1 beta-lactamase

substrate: cephaloridine


organism: Proteus penneri


organism: [Haemophilus] ducreyi


organism: Janthinobacterium lividum


organism: Klebsiella aerogenes


organism: Klebsiella pneumoniae

assay_conditions_summary: pH 6.8; 313.15 K; buffer 50 mM HEPES

proof_lines: pH 7.0, temperature not specified in the publication


organism: Kluyvera ascorbata

assay_conditions_summary: pH 7; 298.15 K; buffer 0.01 M phosphate

proof_lines: Km above 1.0 mM, in 0.01 M phosphate buffer (pH 7.0), at 25°C


organism: Moraxella catarrhalis

substrate_name: Loracarbef

proof_lines:
enzyme 1, BRO-1
enzyme 2, BRO-2

substrate: Loracarbef


organism: Morganella morganii


organism: Mycobacterium tuberculosis

proof_lines:
at 30°C
in 100 mM MES (pH 6.4)


organism: plasmid pBC


substrate_name: Imipenem

substrate: Imipenem


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


organism: Streptomyces cacaoi


organism: Streptomyces sp.


organism: synthetic construct


organism: Yersinia enterocolitica

substrate_name: cefalotin

substrate: cefalotin


organism: Providencia stuartii


organism: Pseudomonas aeruginosa

proof_lines: pH and temperature not specified in the publication, OXA-10 beta-lactamase


organism: Psychrobacter immobilis

proof_lines: at 30°C in 50mM sodium phosphate buffer (pH 7.0)


organism: Serratia fonticola

substrate_name: ceftazidime

assay_conditions_summary: pH 7; 298.15 K; buffer assay condition only

proof_lines: at 25°C in 50 mM sodium phosphate (pH 7.0)

substrate: ceftazidime


organism: Serratia marcescens

proof_lines: wild-type inhibitor protein, pH 7.5, 25°C


assay_conditions_summary: pH 7; 303.15 K; buffer 50 mM sodium phosphate

proof_lines: at 30°C in 50 mM sodium phosphate buffer (pH 7.0)


organism: Staphylococcus aureus

substrate_name: cefamandole

proof_lines:
beta-lactamase C
beta-lactamase A
beta-lactamase D

substrate: cefamandole


organism: Stenotrophomonas maltophilia

substrate_name: cefprozil

proof_lines:
30°C, pH 8.0
30°C, pH 8.0, uncompetitive
30°C, pH 8.0, competitive

substrate: cefprozil


organism: Streptomyces albus

substrate_name: carbenicillin

substrate: carbenicillin


organism: Acinetobacter sp.

proof_lines: pH and temperature not specified in the publication


organism: Aeromonas sobria


organism: Aeromonas veronii


organism: Bacillus anthracis


organism: Bacillus cereus

substrate_name: cephalosporin C

proof_lines:
beta-lactamase III
beta-lactamse II
pH 7, 20°C

substrate: cephalosporin C


organism: Bacillus licheniformis

substrate_name: nitrocefin

proof_lines:
strain 749/C
both strains
strain 6346/C

substrate: nitrocefin


substrate_name: phenoxymethylpenicillin

substrate: phenoxymethylpenicillin


organism: Bacillus sp. (in: firmicutes)

proof_lines:
penicillinase I
penicillinase II


organism: Bacteroides fragilis


organism: Burkholderia pseudomallei


organism: Bos taurus

substrate_name: COS

proof_lines: 0.5°C, pH 7.1, high activity carbonic anhydrase

proof_lines: pH 7.4, 20°C, outer peripheral isoenzyme

substrate: COS


organism: Elephas trogontherii

substrate_name: p-nitrophenyl acetate

proof_lines:
cytosolic isoenzyme
integral isoenzyme
outer peripheral isoenzyme

substrate: p-nitrophenyl acetate


organism: Homo sapiens

proof_lines: pH 8.7, 1,2-dimethylimidazole buffer, carbonic anhydrase II


organism: Mus musculus

proof_lines: isoform carbonic anhydrase XIII, at pH 7.4 and 25°C


organism: Solanum tuberosum

proof_lines:
chloroplastic isoenzyme
cytosolic isoenzyme


organism: Stylophora pistillata

assay_conditions_summary: pH 7.5; 298.15 K; buffer 10 mM HEPES

proof_lines: in the presence of 0.01 mM L-Trp, at 25°C and pH 7.5

proof_lines: in the absence of L-Trp and D-Trp, at 25°C and pH 7.5

proof_lines: in the presence of 0.01 mM D-Trp, at 25°C and pH 7.5


organism: Unknown


organism: Pseudoalteromonas haloplanktis ANT/505

proof_lines: pH 8.3, 20°C, inhibition of CO2 hydration activity


organism: Sordaria macrospora

sequence_source: UniProtKB:C1L336 direct lookup

proof_lines:
20°C, pH 8.3
value above, 20°C, pH 8.3


sequence_source: UniProtKB:B5SU02 direct lookup

assay_conditions_summary: pH 7.5; 293.15 K; buffer 10 mM HEPES

proof_lines: at 20°C and pH 7.5 in 10 mM HEPES buffer


organism: Sulfurihydrogenibium azorense

sequence_source: UniProtKB:C1DTU5 direct lookup

proof_lines: pH 7.5, 20°C, recombinant His-tagged enzyme


organism: Sulfurihydrogenibium sp. YO3AOP1


organism: Synechocystis sp. PCC 6803 / Kazusa

sequence_source: UniProtKB:Q54735 direct lookup

proof_lines: recombinant full-length CcaA274 enzyme, pH 7.5, 25°C, CO2 hydration reaction

proof_lines: recombinant full-length CcaA274 enzyme, pH 9.5, 25°C, CO2 hydration reaction


mutation_signature: recombinant truncated CcaA220 enzyme / CO2 hydration reaction recombinant truncated CcaA220 enzyme

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

mutation_type: truncation

proof_lines: recombinant truncated CcaA220 enzyme, pH 9.5, 25°C, CO2 hydration reaction


organism: Thermovibrio ammonificans

sequence_source: UniProtKB:E8T502 direct lookup


organism: Trichomonas vaginalis

sequence_source: UniProtKB:A2ENQ8 direct lookup


sequence_source: UniProtKB:A2DLG4 direct lookup

proof_lines:
at pH 7.5 and 20°C
Ki above 0.01 mM, at pH 7.5 and 20°C


sequence_source: UniProtKB reviewed accession P23280; direct REST check

proof_lines: saliva isoform CA VI, at pH 7.5, temperature not specified in the publication

proof_lines: milk isoform CA VI, at pH 7.5, temperature not specified in the publication

proof_lines: 20°C, pH 7.5, full-length recombinant hCA VI


organism: Mesorhizobium loti

substrate_name: CO2, H2CO3

assay_conditions_summary: pH 7.5; 277.15 K; buffer a MES/KOH pH 6.3

proof_lines: recombinant enzyme, at 4°C in a HEPES/NaOH, pH 7.5

proof_lines: recombinant enzyme, at 4°C in a MES/KOH pH 6.3 buffer

substrate: CO2, H2CO3


organism: Methanosarcina thermophila

sequence_source: UniProtKB reviewed accession P40881; direct REST check

proof_lines: pH 7.5, 37°C, wild-type, 100 mM guanidine hydrochloride

proof_lines: pH 7.5, 37°C, wild-type, without guanidine hydrochloride


sequence_source: UniProtKB P40881 canonical sequence with R59Q reconstructed by mature-chain offset +34

sequence_variant_note: Mutation signature R59Q matches the mutant residue at offset +12 and the reference residue at offset -13; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: pH 7.5, 37°C, variant R59Q, without guanidine hydrochloride

proof_lines: pH 7.5, 37°C, variant R59Q, 100 mM guanidine hydrochloride


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

proof_lines: pH 7.5, 37°C, 100 mM guanidine hydrochloride

proof_lines: 20°C, pH not specified in the publication, Co2+-substituted enzyme

proof_lines: 20°C, pH not specified in the publication, Zn2+-substituted enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB P40881 canonical sequence with R59K reconstructed by mature-chain offset +34 and applied mutation signature R59K with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, variant R59K, 100 mM guanidine hydrochloride

proof_lines: pH 7.5, 37°C, variant R59K, without guanidine hydrochloride


proof_lines: pH 7.5, 37°C, variant R59C, 100 mM methylguanidine, variant R59Q, 100 mM guanidine hydrochloride


proof_lines: pH 7.5, 37°C, variant R59A, 100 mM 1.3-diaminoguanidine, variant R59H plus 100 mM guanidine hydrochloride


sequence_variant_note: Resolved canonical sequence from UniProtKB P40881 canonical sequence with R59M reconstructed by mature-chain offset +34 and applied mutation signature R59M with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, variant R59M, without guanidine hydrochloride

proof_lines: pH 7.5, 37°C, variant R59M, 100 mM guanidine hydrochloride


sequence_source: UniProtKB P40881 canonical sequence with R59A reconstructed by mature-chain offset +34

sequence_variant_note: Mutation signature R59A matches the mutant residue at offset +0 and the reference residue at offset -13; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: pH 7.5, 37°C, variant R59A, 100 mM imidazole


sequence_variant_note: Resolved canonical sequence from UniProtKB P40881 canonical sequence with R59E reconstructed by mature-chain offset +34 and applied mutation signature R59E with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, variant R59E, without guanidine hydrochloride

proof_lines: pH 7.5, 37°C, variant R59E, 100 mM guanidine hydrochloride


sequence_variant_note: Resolved canonical sequence from UniProtKB P40881 canonical sequence with R59C reconstructed by mature-chain offset +34 and applied mutation signature R59C with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, variant R59C, 100 mM ethylguanidine

proof_lines: pH 7.5, 37°C, variant R59C, 100 mM methylguanidine


sequence_variant_note: Resolved canonical sequence from UniProtKB P40881 canonical sequence with R59H reconstructed by mature-chain offset +34 and applied mutation signature R59H with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, variant R59H, without guanidine hydrochloride

proof_lines: pH 7.5, 37°C, variant R59H, 100 mM guanidine hydrochloride


sequence_source: UniProtKB unreviewed accession C3W4Q7; direct REST check

proof_lines: pH 7.5, 25°C, enzyme cultured with supplemental iron

proof_lines: pH 7.5, 25°C, enzyme cultured with supplemental zinc


sequence_variant_note: Resolved canonical sequence from UniProtKB P40881 canonical sequence with Y200F reconstructed by mature-chain offset +34 and applied mutation signature Y200F to reconstruct the assayed variant sequence.

proof_lines:
25°C, pH 7.5, mutant enzyme Y200F
25°C, pH 8.8, mutant enzyme Y200F


sequence_source: UniProtKB P40881 canonical sequence with W19N reconstructed by mature-chain offset +34

sequence_variant_note: Mutation signature W19N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
25°C, pH 7.5, mutant enzyme W19N
25°C, pH 8.8, mutant enzyme W19N


sequence_variant_note: Resolved canonical sequence from UniProtKB:P40881 exact accession lookup; variant reconstructed from selected BRENDA mutation note; retrieved 2026-06-26 and applied mutation signature W19F with inferred residue-numbering offset +34 to reconstruct the assayed variant sequence.

proof_lines:
25°C, pH 7.5, mutant enzyme W19F
25°C, pH 8.8, mutant enzyme W19F


sequence_variant_note: Resolved canonical sequence from UniProtKB:P40881 exact accession lookup; variant reconstructed from selected BRENDA mutation note; retrieved 2026-06-26 and applied mutation signature W19A with inferred residue-numbering offset +34 to reconstruct the assayed variant sequence.

proof_lines:
25°C, pH 7.5, mutant enzyme W19A
25°C, pH 8.8, mutant enzyme W19A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P40881 exact accession lookup; variant reconstructed from selected BRENDA mutation note; retrieved 2026-06-26 and applied mutation signature Y200A to reconstruct the assayed variant sequence.

proof_lines:
25°C, pH 7.5, mutant enzyme Y200A
25°C, pH 8.8, mutant enzyme Y200A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P40881 exact accession lookup; variant reconstructed from selected BRENDA mutation note; retrieved 2026-06-26 and applied mutation signature Y200S to reconstruct the assayed variant sequence.

proof_lines:
25°C, pH 7.5, mutant enzyme Y200S
25°C, pH 8.8, mutant enzyme Y200S


organism: Methanothermobacter thermautotrophicus

sequence_source: UniProtKB:D9PU79 exact accession lookup; canonical sequence context only; retrieved 2026-06-26

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


substrate_name: Unknown

sequence_source: UniProtKB:Q9D6N1 exact accession lookup; retrieved 2026-06-26

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

proof_lines:
pH 7.5, 25°C, mCA XIII
isoenzyme mCA XIII
pH 7.5, 25°C, mCA V

substrate: Unknown


sequence_source: UniProtKB:Q99N23 exact accession lookup; retrieved 2026-06-26


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB:P96878 exact accession lookup; retrieved 2026-06-26


organism: Mytilus galloprovincialis

sequence_source: UniProtKB:A0A0N9FGL8 exact accession lookup; retrieved 2026-06-26

proof_lines: CO2 hydration, pH 8.3, 22°C, recombinant enzyme

proof_lines: CO2 hydration, pH 8.3, 22°C, native enzyme


organism: Oncorhynchus mykiss

sequence_source: UniProtKB:Q6R4A2 exact accession lookup; retrieved 2026-06-26


sequence_source: UniProtKB:Q7T2K6 exact accession lookup; retrieved 2026-06-26


organism: Persephonella marina

substrate_name: CO2; H2CO3

sequence_source: UniProtKB:C0QRB5 exact accession lookup; retrieved 2026-06-26

proof_lines:
pH 7.8, 25°C, recombinant enzyme
pH 7.5, 20°C

substrate: CO2; H2CO3


organism: Plasmodium falciparum

mutation_signature: truncated form PfCA1 / truncated form PfCA1

sequence_source: UniProtKB:Q8IHW5 exact accession lookup; canonical sequence context only; retrieved 2026-06-26

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

proof_lines: pH 7.5, 22°C, truncated form PfCA1, CO2 hydration reaction


proof_lines: pH 7.5, 22°C, long enzyme form PfCAdom, CO2 hydration reaction

proof_lines: pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA22


mutation_signature: truncated mutant PfCA1


organism: Porphyromonas gingivalis

sequence_source: UniProtKB:B2RL07 exact accession lookup; retrieved 2026-06-26

proof_lines: pH 8.3, 22°C, recombinant His-tagged enzyme


organism: Acipenser gueldenstaedtii

proof_lines: pH 9.0, 30°C, inhibition of esterase activity with 4-nitrophenyl acetate

proof_lines: pH 7.4, 30°C, inhibition of CO2 hydration activity


organism: Aedes aegypti


organism: Anguilla anguilla


organism: Arabidopsis thaliana


organism: Astrosclera willeyana


organism: Bacillus subtilis

substrate_name: 4-nitrophenyl acetate

assay_conditions_summary: pH 8.3; 310.15 K; buffer 0.1 M Tris-HCl

proof_lines: in 0.1 M Tris-HCl buffer, pH 8.3, and 37°C

substrate: 4-nitrophenyl acetate


organism: Caenorhabditis elegans

proof_lines: purified recombinant CAH-4a, pH 7.5, 4°C


organism: Candida albicans

assay_conditions_summary: pH 8.3; 293.15 K; buffer and 20 mM NaClO4

proof_lines: at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4

proof_lines: CaNce103, at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4, in the presence of 0.01 mM histamine


organism: Cavia porcellus

proof_lines: 0°C, pH 7.2, low activity carbonic anhydrase

proof_lines: 0°C, pH 7.2, high activity carbonic anhydrase


organism: Chionodraco hamatus


organism: Clostridium perfringens

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


organism: Coccomyxa sp.


organism: Columba livia


organism: Conticribra weissflogii

proof_lines: pH 7.9, temperature not specified in the publication, the activities depended on culture conditions, ranging between 20/sec and 150/sec


organism: Corynebacterium flavescens


organism: Cryptococcus neoformans

assay_conditions_summary: pH 8.3; 293.15 K; buffer 20 mM Tris

proof_lines: Can2, at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4, in the presence of 0.01 mM histamine


organism: Cyprinus carpio


organism: Drosophila melanogaster

proof_lines:
pH 8.3, 20°C
above, pH 8.3, 20°C


organism: Dunaliella salina

proof_lines:
without NaCl
0.1 M NaCl
0.25 M NaCl


organism: Entamoeba histolytica


organism: Felis catus

proof_lines:
pH 6-8
above pH 8


organism: Flaveria bidentis


organism: Gyrodactylus salaris


organism: Halomonas sp.

proof_lines: pH 7.5, 20°C, inhibition of CO2 hydration reaction


organism: Halothiobacillus neapolitanus

assay_conditions_summary: pH 7

proof_lines:
pH 7.0, rCsoSCA
rCsoSCA


organism: Helicobacter pylori


organism: Homo sapiens

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


proof_lines: pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant N62V


assay_conditions_summary: pH 6.28; buffer contexts

proof_lines: pH 6.28, MES buffer, carbonic anhydrase I mutant V62N

proof_lines: pH 8.95, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant V62N

proof_lines: pH 8.98, TAPS buffer, carbonic anhydrase I mutant V62N


proof_lines: pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant T200H


proof_lines: pH 6.28, MES buffer, carbonic anhydrase I mutant V62N,H67N,H200T

proof_lines: pH 8.98, TAPS buffer, carbonic anhydrase I mutant V62N,H67N,H200T

proof_lines: pH 7.23, 1-methylimidazolebuffer, carbonic anhydrase I mutant V62N,H67N,H200T


proof_lines: pH 8.98, TAPS buffer, carbonic anhydrase I mutant V62N and carbonic anhydrase I mutant H67N

proof_lines: pH 8.88, TAPS buffer, carbonic anhydrase I mutant V62N,H67N

proof_lines: pH 8.72, 1,2-dimethyimidazole buffer, carbonic anhydrase I mutant V62N,H67N


proof_lines: pH 6.3, MES buffer, wild-type carbonic anhydrase I

proof_lines: pH 8.8, TAPS buffer, wild-type carbonic anhydrase I

proof_lines: pH 8.77, 1,2-dimethylimidazole buffer, wild-type carbonic anhydrase I


proof_lines: pH 8.72, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant V62B, H67B

proof_lines: pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant N67HV

proof_lines: pH 8.98, TAPS buffer, carbonic anhydrase I mutant H67B


proof_lines: pH 8.94, 1,2-dimethylimidazole buffer, carbonic anhydrase II mutant N67H


proof_lines: pH 6.28, MES buffer, carbonic anhydrase I mutant H67N

proof_lines: pH 7.23, 1-methylimidazole buffer, carbonic anhydrase I mutant H67N

proof_lines: pH 8.75, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant H67N


proof_lines: pH 8.88, TAPS buffer, carbonic anhydrase I mutant H200T

proof_lines: pH 7.21, 1-methylimidazole buffer, carbonic anhydrase I mutant H200T

proof_lines: pH 8.95, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant H200T


organism: Lacticaseibacillus rhamnosus


organism: Lathyrus oleraceus

proof_lines:
pH 6.2, 25°C, mutant H208A
pH 8.8, 25°C, mutant H208A
pH 7.3, 25°C, mutant H208A


proof_lines: pH 6.2, 25°C, wild-type, term extrapolated from the highest substrate concentrations, due to curved Eadie–Hofstee plots


organism: Leishmania chagasi


organism: Macropus eugenii desmarest


organism: Malassezia globosa


organism: Malassezia pachydermatis

proof_lines: at pH 8.3, temperature not specified in the publication


organism: Malassezia restricta


organism: Methanosarcina thermophila

proof_lines: pH 7.5, 25°C, recombinant enzyme expressed from Escherichia coli and aerobically purified


assay_conditions_summary: pH 7.5; 298.15 K; buffer variants

proof_lines: pH 7.5, 25°C, variant E84A, 50 mM MOPS-Ac buffer

proof_lines: pH 7.5, 25°C, variant E84A, 50 mM MOPS buffer

proof_lines: pH 7.5, 25°C, variant E84A, 50 mM IMID buffer


proof_lines: pH 7.5, 25°C, variant E62D, 50 mM MOPS buffer


proof_lines:
pH 7.5, 25°C, wild-type, D2O
pH 5.7-9.5, 25°C, wild-type
pH 6.5, 25°C, wild-type, D2O


proof_lines: pH 7.5, 25°C, variant E84C, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62A/E84A, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84C and E62A, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62Y, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84H, 50 mM MOPS buffer


organism: Brucella suis

sequence_source: UniProtKB A0A0H3GB68 canonical sequence

assay_conditions_summary: pH 8.3; 293.15 K; buffer 20 mM Tris-HCl

proof_lines: at 20°C, pH 8.3 in 20 mM Tris-HCl buffer and 20 mM NaCl

proof_lines: isozyme bsCAI, pH 8.3, temperature not specified in the publication


organism: Colwellia psychrerythraea

sequence_source: UniProtKB Q47YG3 canonical sequence

proof_lines: pH 8.3, 22°C, inhibition of CO2 hydration activity


organism: Conticribra weissflogii

sequence_source: UniProtKB Q5U9J1 canonical sequence

proof_lines: measured with hydration of CO2 activity assay, pH 7.5-8.3, 0°C


organism: Danio rerio

sequence_source: UniProtKB A0A8M3ANQ1 canonical sequence

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


organism: Dunaliella salina

sequence_source: UniProtKB P54212 canonical sequence

proof_lines:
pH 6.8, in absence of NaCl
pH 6.8, 0.1 M NaCl
pH 6.8, 0.5 M NaCl


organism: Enterobacter sp. B13

sequence_source: UniProtKB A0A0S1NK17 canonical sequence

proof_lines: pH 8.3, 20°C, recombinant His-tagged enzyme


organism: Escherichia coli


organism: Helicobacter pylori

proof_lines:
isoenzyme hpbetaCA
isoenzyme hpbetaCA, i.e. daranide


sequence_source: UniProtKB O24855 canonical sequence

proof_lines:
isoenzyme hpalphaCA
isoenzyme hpalphaCA, i.e. daranide


organism: Homo sapiens

sequence_source: UniProtKB O43570 canonical sequence

proof_lines: pH 7.5, catalytic domain of cloned isoenzyme


sequence_source: UniProtKB P07451 canonical sequence only; row-specific variant not reconstructed


sequence_source: UniProtKB P35218 canonical sequence

proof_lines:
isoenzyme hCA VA
isoenzyme hCA VA catalytic domain
isoenzyme hCA VA, i.e. daranide


sequence_source: UniProtKB P00915 canonical sequence

proof_lines:
isoenzyme hCA I
pH 8.3, 22°C
inhibition of isozyme, pH 9.0, 40°C


sequence_source: UniProtKB P22748 canonical sequence

proof_lines: inhibition of isozyme hCA IV, pH 9.0, 40°C


sequence_source: UniProtKB P43166 canonical sequence

assay_conditions_summary: pH 8

proof_lines: at pH 8.0, temperature not specified in the publication


assay_conditions_summary: pH 7.5; 298.15 K; buffer context

proof_lines: pH 7.5, 25°C, variant E84Q, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84D, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62H, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E89A, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84Y, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84S, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84S and E84Y, 50 mM MOPS buffer


assay_conditions_summary: pH 7.5; 298.15 K; buffer contexts

proof_lines: pH 7.5, 25°C, variant E62A, 50 mM IMID buffer

proof_lines: pH 7.5, 25°C, variant E62A, 50 mM MOPS-Ac buffer

proof_lines: pH 7.5, 25°C, variant E62A, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62T, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E88A, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62Q, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84A and E84K, 50 mM MOPS buffer


organism: Nostoc commune

proof_lines: pH 7.5, 20°C, inhibition of CO2 hydration activity


organism: Nostoc sp.


organism: Oncorhynchus mykiss

assay_conditions_summary: pH 9; 298.15 K; buffer 0.05 M Tris-SO4

proof_lines: in 0.05 M Tris-SO4 buffer, at pH 9.0 and 25°C


organism: Oryctolagus cuniculus

proof_lines: enzyme from red muscle sarcolemmal membranes

proof_lines: enzyme from white muscle sarcoplasmic reticulum

proof_lines: enzyme from red muscle sarcoplasmic reticulum


organism: Oryza sativa


organism: Ovis aries

proof_lines:
Vmax: 0.168 micromol/min, pH 8.5, 35°C
pH 7.4, 25°C, purified enzyme
pH 8.5, 35°C


organism: Petromyzon marinus


organism: Petroselinum crispum

proof_lines: 25°C, pH 7.07, high activity carbonic anhydrase


organism: Plasmodium falciparum


organism: Populus tremula

assay_conditions_summary: pH 6.6; buffer pH 6

proof_lines:
pH 6.6, MES buffer
pH 8.8, TAPS buffer


organism: Porphyromonas gingivalis


organism: Python bivittatus

proof_lines: pH not specified in the publication, 4°C, assay using the delta pH method


organism: Rattus norvegicus

proof_lines: 25°C, pH 7.0, low activity carbonic anhydrase

proof_lines: 0°C, pH 7.0, high activity carbonic anhydrase


organism: Rhodospirillum rubrum


organism: Saccharomyces cerevisiae

proof_lines: at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-

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


organism: Salmo labrax

proof_lines: pH 7.4, 25°C, inhibition of 4-nitrophenyl acetate hydrolysis activity


organism: Salmo trutta Labrax Coruhensis


organism: Sander vitreus


organism: Struthio camelus


organism: Sulfurihydrogenibium azorense

proof_lines:
pH 7.5, 20°C
pH 7.5, 25°C, 10 microM L-Phe
pH 7.5, 25°C, 10 microM D-Phe


organism: Sulfurihydrogenibium yellowstonense


organism: Sus scrofa


organism: Tectona grandis


organism: Thalassiosira pseudonana

proof_lines: pH 7.9, temperature not specified in the publication, the activities depended on culture conditions, ranging between 80/sec and 200/sec


organism: Methanosarcina thermophila

proof_lines: pH 7.5, 25°C, variant E84K, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62C, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62D/E84D, 50 mM MOPS buffer


organism: Methanothermobacter thermautotrophicus

proof_lines: 20°C, pH not specified in the publication


assay_conditions_summary: pH 8.5; 298.15 K; buffer imidazole or MOPS

proof_lines: pH 8.5, 25°C, wild-type, imidazole buffer


assay_conditions_summary: pH 8.5; 298.15 K; buffer contexts

proof_lines: pH 8.5, 25°C, mutant D34A, imidazole buffer


proof_lines: pH 8.5, 25°C, mutant D34A/R36A, imidazole buffer

proof_lines: pH 8.5, 25°C, mutant D34A/R36A, MOPS buffer


proof_lines: pH 8.5, 25°C, mutant R36A, imidazole buffer


organism: Micropterus salmoides


organism: Mus musculus


organism: Trachurus trachurus

proof_lines: pH and temperature not specified in the publication


organism: Trematomus bernacchii


organism: Trypanosoma cruzi


organism: Vibrio cholerae serotype O1


proof_lines:
pH 9.0, 25°C, mutant R94H/E92Q
pH 7.0, 10°C, double mutant R94H/E92Q


mutation_signature: truncated form of carbonic anhydrase VII lacking the amino-terminal 23 residues of recombinant enzyme truncated form of carbonic anhydrase VII lacking the amino


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 8.3; 293.15 K; buffer and 20 mM NaCl

proof_lines: at 20°C, pH 8.3, in 20 mM Tris-HCl and 20 mM NaCl

proof_lines: isoform CA 3, at 20°C and pH 8.3, in 20 mM Tris-HCl buffer and 20 mM NaCl


organism: Nakaseomyces glabratus

substrate_name: histamine

assay_conditions_summary: pH 8.3; 298.15 K; buffer and 20 mM NaClO4

proof_lines: at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4, in the presence of 0.01 mM histamine

substrate: histamine


organism: Neisseria gonorrhoeae


proof_lines:
pH 6.7, 25°C
purified recombinant enzyme


organism: Homo sapiens

proof_lines:
isoenzyme hCA XII catalytic domain
isoenzyme hCA XII


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

proof_lines:
isoenzyme hCA VB
isoenzyme hCA VB catalytic domain
isoenzyme hCA VB, i.e. daranide


proof_lines:
at 20°C and pH 7.5
isoenzyme hCA III
20°C, pH 7.5


proof_lines: recombinant CA IX catalytic domain expressed in Sf9 cells, in the presence of 0.05 mM Mg2+

proof_lines: recombinant CA IX catalytic domain expressed in Escherichia coli

proof_lines: recombinant CA IX catalytic domain expressed in Sf9 cells, in the absence of Zn2+


sequence_variant_note: Resolved canonical sequence from uniprot_accession_variant_reconstruction and applied mutation signature Y7F to reconstruct the assayed variant sequence.


proof_lines: pH 7.6, temperature not specified in the publication, mutant A23C/L203C/C206S


proof_lines: isozyme CA XII, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4

proof_lines: isozyme CA XIV, in 10 mM HEPES (pH 7.5) and 0.1 M Na2SO4


proof_lines:
pH 7.5, 25°C, recombinant enzyme
isoenzyme hCA XIV, i.e. daranide
pH 7.5, full-length recombinant enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_accession_variant_reconstruction and applied mutation signature A65T/N67Q/F130Y/V134Q/L203T to reconstruct the assayed variant sequence.

proof_lines: isoform CA II mutant A65T/N67Q/F130Y/V134Q/L203T, at pH 7.5 and 23Â°C


proof_lines: wild type isoform CA IV, at pH 7.5 and 23°C


proof_lines: wild type isoform CA II, at pH 7.5 and 23Â°C


organism: Cryptococcus neoformans

proof_lines: at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4

proof_lines: Can2, at 25°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4, in the presence of 0.01 mM histamine


proof_lines: pH 6.28, MES buffer, carbonic anhydrase I mutant V62N

proof_lines: pH 8.95, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant V62N

proof_lines: pH 8.98, TAPS buffer, carbonic anhydrase I mutant V62N


assay_conditions_summary: pH 6.28; buffer conditions

proof_lines: pH 6.28, MES buffer, carbonic anhydrase I mutant V62N,H67N,H200T

proof_lines: pH 8.98, TAPS buffer, carbonic anhydrase I mutant V62N,H67N,H200T

proof_lines: pH 7.23, 1-methylimidazolebuffer, carbonic anhydrase I mutant V62N,H67N,H200T


proof_lines: pH 7.5, 25°C, variant E84A, 50 mM MOPS-Ac buffer

proof_lines: pH 7.5, 25°C, variant E84A, 50 mM MOPS buffer

proof_lines: pH 7.5, 25°C, variant E84A, 50 mM IMID buffer


assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM MOPS

proof_lines: pH 7.5, 25°C, variant E84Q, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84D, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62H, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E89A, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84Y, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84S, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62A, 50 mM IMID buffer

proof_lines: pH 7.5, 25°C, variant E62A, 50 mM MOPS-Ac buffer

proof_lines: pH 7.5, 25°C, variant E62A, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62T, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E88A, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62Q, 50 mM MOPS buffer


sequence_source: NCBI Protein/RCSB PDB 1G5C chain sequence linked from the PMID 11096105 Cab structure paper cited by PMID 12107142

proof_lines: pH 8.5, 25°C, wild-type, imidazole buffer


sequence_variant_note: Resolved canonical sequence from D34A reconstructed from NCBI Protein/RCSB PDB 1G5C chain sequence linked from PMID 11096105 and cited by PMID 12107142 and applied mutation signature D34A to reconstruct the assayed variant sequence.

proof_lines: pH 8.5, 25°C, mutant D34A, imidazole buffer


sequence_variant_note: Resolved canonical sequence from D34A/R36A reconstructed from NCBI Protein/RCSB PDB 1G5C chain sequence linked from PMID 11096105 and cited by PMID 12107142 and applied mutation signature D34A/R36A to reconstruct the assayed variant sequence.

proof_lines: pH 8.5, 25°C, mutant D34A/R36A, imidazole buffer

proof_lines: pH 8.5, 25°C, mutant D34A/R36A, MOPS buffer


sequence_variant_note: Resolved canonical sequence from R36A reconstructed from NCBI Protein/RCSB PDB 1G5C chain sequence linked from PMID 11096105 and cited by PMID 12107142 and applied mutation signature R36A to reconstruct the assayed variant sequence.

proof_lines: pH 8.5, 25°C, mutant R36A, imidazole buffer


organism: Saccharomyces cerevisiae

sequence_source: NCBI Protein records linked directly from PMID 18993072: Swiss-Prot P53615.1 / RefSeq NP_014362.3

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

assay_conditions_summary: pH 8.3; 293.15 K; buffer and 20 mM NaClO4

proof_lines: at 20°C, pH 8.3 in 20 mM Tris buffer and 20 mM NaClO4-

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


organism: Brucella suis

sequence_source: UniProtKB REST direct accession lookup for A0A0H3GB68 on 2026-06-26; TrEMBL entry A0A0H3GB68_BRUSU, carbonic anhydrase, EC 4.2.1.1, Brucella suis biovar 1 strain 1330.

proof_lines: at 20°C, pH 8.3 in 20 mM Tris-HCl buffer and 20 mM NaCl

proof_lines: isozyme bsCAI, pH 8.3, temperature not specified in the publication


organism: Mesorhizobium loti

assay_conditions_summary: pH 7.5; 277.15 K; buffer a MES/KOH pH 6.3

proof_lines: recombinant enzyme, at 4°C in a HEPES/NaOH, pH 7.5

proof_lines: recombinant enzyme, at 4°C in a MES/KOH pH 6.3 buffer


organism: Persephonella marina

sequence_source: UniProtKB REST direct accession lookup for C0QRB5 on 2026-06-26; TrEMBL entry C0QRB5_PERMH, carbonic anhydrase, EC 4.2.1.1, Persephonella marina strain DSM 14350 / EX-H1.

proof_lines:
pH 7.8, 25°C, recombinant enzyme
pH 7.5, 20°C


organism: Plasmodium falciparum

sequence_source: UniProtKB REST direct accession lookup for Q8IHW5 on 2026-06-26; TrEMBL entry Q8IHW5_PLAF7, carbonic anhydrase, EC 4.2.1.1, Plasmodium falciparum isolate 3D7.

proof_lines: pH 7.5, 22°C, long enzyme form PfCAdom, CO2 hydration reaction

proof_lines: pH 7.5, 22°C, inhibition of CO2 hydration activity of PfCA22


enzyme_display_name: tyrosinase

organism: Priestia megaterium

substrate_name: L-Dopa

sequence_variant_note: Resolved canonical sequence from UniProtKB B2ZB02 FASTA plus direct V218F substitution check; RCSB 4HD4/4HD6 confirm PMID 23305929 V218F structure context. and applied mutation signature V218F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V218F, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C

enzyme: tyrosinase

substrate: L-Dopa


substrate_name: L-tyrosine

sequence_variant_note: Resolved canonical sequence from UniProtKB B2ZB02 FASTA plus direct V218G substitution check; RCSB 4HD7 confirms PMID 23305929 V218G structure context. and applied mutation signature V218G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V218G, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C

substrate: L-tyrosine


sequence_source: UniProtKB B2ZB02 FASTA; UniProt references PMID 23305929 for the same tyrosinase paper context.

proof_lines: wild type enzyme, in 50 mM Tris HCl buffer pH 7.5, 0.01 mM CuSO4, at 28°C


organism: Charybdis japonica

assay_conditions_summary: pH 7.1; buffer 20 mM Tris-HCl


organism: Solanum tuberosum

assay_conditions_summary: pH 6.8; 298.15 K; buffer notes

proof_lines: with catechol as a substrate, at pH 6.8 and 25°C

proof_lines: with 4-methylcatechol as a substrate, at pH 6.8 and 25°C


enzyme_display_name: versatile peroxidase

organism: Pleurotus eryngii

substrate_name: syringol

proof_lines:
pH 3.0, isoenzyme PS1
pH 3.0, isoenzyme PS3
pH 5.0, isoenzyme PS1

enzyme: versatile peroxidase

substrate: syringol


organism: Pleurotus ostreatus


substrate_name: Reactive Black 5

proof_lines:
at pH 3.5 and 25°C
at pH 5.0 and 25°C
at pH 3.0 and 25°C

substrate: Reactive Black 5


organism: Pseudomonas putida

substrate_name: Acid Blue 62

substrate: Acid Blue 62


organism: Stereum ostrea

substrate_name: Phenol red

substrate: Phenol red


proof_lines: mutant E140G, high efficiency site, pH 3.5, 25°C

proof_lines: mutant E140G, low efficiency site, pH 3.5, 25°C


proof_lines: mutant E140G/P141G, low efficiency site, pH 3.5, 25°C

proof_lines: mutant E140G/P141G, high efficiency site, pH 3.5, 25°C


proof_lines: mutant E140G/P141G/K176G, high efficiency site, pH 3.5, 25°C

proof_lines: mutant E140G/P141G/K176G, low efficiency site, pH 3.5, 25°C


proof_lines: mutant E140G/W164S/K176G, low efficiency site, pH 3.5, 25°C


proof_lines: mutant K215G, high efficiency site, pH 3.5, 25°C

proof_lines: mutant K215G, low efficiency site, pH 3.5, 25°C


proof_lines: mutant P76G, high efficiency site, pH 3.5, 25°C

proof_lines: mutant P76G, low efficiency site, pH 3.5, 25°C


organism: Pleurotus sapidus

substrate_name: beta-carotene

substrate: beta-carotene


organism: Rhodococcus jostii


proof_lines: pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2

proof_lines: pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 50 mM 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and 2 mM Mn2+

proof_lines: pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2


sequence_source: UniProtKB:O94753 canonical sequence with mature-chain mutation reconstruction

sequence_variant_note: Mutation signature M247L could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
pH 3.5, 25°C, mutant M247L
pH 3.0, 25°C, mutant M247L


sequence_source: UniProtKB:O94753 canonical sequence

proof_lines: wild-type, high efficiency site, pH 3.5, 25°C

proof_lines: wild-type, pH 3.5, temperature not specified in the publication


sequence_variant_note: Mutation signature R257K matches the mutant residue at offset -12 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines:
pH 3.5, 25°C, mutant R257K
pH 3.0, 25°C, mutant R257K


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 canonical sequence with mature-chain mutation reconstruction and applied mutation signature W164Y/R257A/A260F with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature W164S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant W164S, low efficiency site, pH 3.5, 25°C


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +2, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 canonical sequence with mature-chain mutation reconstruction and applied mutation signature R257A/A260F with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme R257A/A260F
pH 3.0, 25°C, mutant R257A/A260F
pH 3.5, 25°C, mutant R257A/A260F


sequence_variant_note: Mutation signature W164Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 canonical sequence with mature-chain mutation reconstruction and applied mutation signature E37K/V160A/T184M/Q202L with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines: mutant E37K/V160A/T184M/Q202L, pH 3.5, temperature not specified in the publication


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

proof_lines:
pH 3.5, 25°C
native recombinant enzyme
pH 5.0, 25°C


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

proof_lines: mutant K176D, high efficiency site, pH 3.5, 25°C

proof_lines: mutant K176D, low efficiency site, pH 3.5, 25°C


sequence_variant_note: Mutation signature K176G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant K176G, high efficiency site, pH 3.5, 25°C

proof_lines: mutant K176G, low efficiency site, pH 3.5, 25°C


substrate_name: catechol

sequence_variant_note: Mutation signature K215Q matches the mutant residue at offset +11 and the reference residue at offset -9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: mutant K215Q, high efficiency site, pH 3.5, 25°C

proof_lines: mutant K215Q, low efficiency site, pH 3.5, 25°C

substrate: catechol


sequence_variant_note: Mutation signature F142G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant F142G, high efficiency site, pH 3.5, 25°C

proof_lines: mutant F142G, low efficiency site, pH 3.5, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 canonical sequence with mature-chain mutation reconstruction and applied mutation signature E140G/K176G with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines: mutant E140G/K176G, low efficiency site, pH 3.5, 25°C

proof_lines: mutant E140G/K176G, high efficiency site, pH 3.5, 25°C


sequence_variant_note: Mutation signature P141G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant P141G, high efficiency site, pH 3.5, 25°C

proof_lines: mutant P141G, low efficiency site, pH 3.5, 25°C


organism: Bjerkandera adusta

substrate_name: veratryl alcohol

sequence_source: UniProtKB:A5JTV4 direct accession lookup

substrate: veratryl alcohol


sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

proof_lines: 25°C, pH 5, mutant E36A/E40A/D175A/P327ter


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 plus reconstructed mutation signature using +30 residue-numbering offset and applied mutation signature E36D with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 plus reconstructed mutation signature using +30 residue-numbering offset and applied mutation signature E36A/E40A with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 plus reconstructed mutation signature using +30 residue-numbering offset and applied mutation signature E40D with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 plus reconstructed mutation signature using +30 residue-numbering offset and applied mutation signature D175A with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 plus reconstructed mutation signature using +30 residue-numbering offset and applied mutation signature E36A with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


proof_lines:
pH 3.5, 25°C, mutant S158D
pH 3.0, 25°C, mutant S158D


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 plus reconstructed mutation signature using +30 residue-numbering offset and applied mutation signature A260F with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines:
pH 3.5, 25°C, mutant A260F
pH 3.0, 25°C, mutant A260F


proof_lines:
pH 3.0, 25°C, mutant R257L
pH 3.5, 25°C, mutant R257L


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 plus reconstructed mutation signature using +30 residue-numbering offset and applied mutation signature K264A with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines:
pH 3.5, 25°C, mutant K264A
pH 3.0, 25°C, mutant K264A


proof_lines:
pH 3.5, 25°C, mutant M247F
pH 3.0, 25°C, mutant M247F


proof_lines:
pH 3.5, 25°C, mutant S158E
pH 3.0, 25°C, mutant S158E


substrate_name: Reactive Violet 5

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

proof_lines: Hill coefficient 2.8, presence of Mn2+, pH 3.5, 25°C

proof_lines: Hill coefficient 3.6, absence of Mn2+, pH 3.5, 25°C

substrate: Reactive Violet 5


organism: Bjerkandera fumosa

proof_lines: absence of Mn2+, pH 4.5, temperature not specified in the publication

proof_lines: presence of Mn2+, pH not specified in the publication, temperature not specified in the publication

proof_lines: presence of Mn2+, pH 7.0, temperature not specified in the publication


organism: Bjerkandera sp.


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

assay_conditions_summary: pH 5


assay_conditions_summary: pH 3

proof_lines:
wild-type, pH 3.0
wild-type, pH 3.5
wild-type, pH 5.0


proof_lines:
mutant P76H, pH 3.5
mutant P76H, pH 3.0
mutant P76H, pH 5.0


proof_lines:
mutant H232F, pH 3.0
mutant H232F, pH 3.5
mutant H232F, pH 5.0


enzyme_display_name: coagulation factor Xa

organism: Unknown

enzyme: coagulation factor Xa


organism: Rattus norvegicus


organism: Bos taurus

proof_lines: enzyme from which the residues 1-44 of the light chain have been removed by chymotryptic proteolysis


organism: Camelus bactrianus


organism: Canis lupus familiaris


organism: Homo sapiens


substrate_name: prothrombin

substrate: prothrombin


proof_lines: pH 7.4, 25°C, wild-type enzyme, activated by factor Va


proof_lines: pH 7.4, 25°C, mutant enzyme E36K/E37K/E39K, activated by factor Va


proof_lines: pH 7.4, 25°C, mutant enzyme E74K/E76K/E77K, activated by factor Va


proof_lines: pH 7.4, 25°C, mutant enzyme E36Q/E37Q/E39Q, activated by factor Va


proof_lines: pH 7.4, 25°C, mutant enzyme E74Q, E76Q/E77Q, activated by factor Va


proof_lines: mutant E217A, pH 7.5, presence of 0.5 M NaCl


proof_lines: mutant E217Q, pH 7.5, presence of 0.5 M NaCl


proof_lines: prothrombinase assembled with mutant V17A, pH 7.5


proof_lines: prothrombinase assembled with mutant I16L, pH 7.5


proof_lines: pH 7.4, 22°C, in presence of 20 mM factor Va


organism: Mammalia


organism: Mus musculus

proof_lines: pH 7.4, 37°C, wild-type enzyme in presence of factor Va


organism: Oryctolagus cuniculus


sequence_source: UniProtKB reviewed accession P00742, direct UniProt REST lookup

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

proof_lines: pH 8.0, temperature not specified in the publication


enzyme_display_name: phosphatidylserine decarboxylase

substrate_name: phosphatidylserine

enzyme: phosphatidylserine decarboxylase

substrate: phosphatidylserine


substrate_name: phosphatidyl-L-serine

assay_conditions_summary: pH 6.8; buffer note: 100 mM potassium phosphate

proof_lines: in 100 mM potassium phosphate, pH 6.8, 10 mM EDTA, and 0.05% Triton X-100

substrate: phosphatidyl-L-serine


organism: Tetrahymena pyriformis

proof_lines: natural saturated


organism: Toxoplasma gondii

assay_conditions_summary: pH 6.8; 310.15 K; buffer phosphate

proof_lines: in 60 mM potassium phosphate (pH 6.8), 0.17 M sucrose, 0.35 mM phenylmethylsulfonyl fluoride, 2 mM EDTA, 0.5 mM 2-mercaptoethanol, at 37°C


organism: Plasmodium falciparum

substrate_name: dioleoyl phosphatidylserine

substrate: dioleoyl phosphatidylserine


organism: Toxoplasma gondii (strain ATCC 50853 / GT1)


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A8K1 canonical sequence with Y137F reconstructed during review and applied mutation signature Y137F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0A8K1 canonical sequence from direct review lookup


sequence_source: UniProtKB:Q9GPP8 canonical sequence from direct review lookup


substrate_name: Phosphatidylserine

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

sequence_source: UniProtKB:Q58DH2 REST direct lookup (reviewed Swiss-Prot PISD_BOVIN; EC 4.1.1.65)

substrate: Phosphatidylserine


substrate_name: Dipalmitoyl phosphatidylserine

sequence_source: UniProtKB:P0A8K1 REST direct lookup (reviewed Swiss-Prot PSD_ECOLI; EC 4.1.1.65)

substrate: Dipalmitoyl phosphatidylserine


substrate_name: Dioleoyl phosphatidylserine

sequence_source: UniProtKB:F6N7K6 REST direct lookup (reviewed Swiss-Prot PSD2_TOXGG; EC 4.1.1.65)

substrate: Dioleoyl phosphatidylserine


verification_status: verified

sequence_source: PMID 22563079; GenBank JN003619; NCBI Protein AEG64709.1; UniProtKB F6N7K6

status: verified


organism: Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)

substrate_name: Unknown

substrate: Unknown


organism: Thermus brockianus

substrate_name: maltotriose

sequence_variant_note: Resolved canonical sequence from UniProtKB Q2VJA0 direct lookup plus selected BRENDA source note; W258G reconstructed from canonical accession sequence. and applied mutation signature W258G to reconstruct the assayed variant sequence.

substrate: maltotriose


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB Q2VJA0 direct lookup from selected SKiD accession.

source: skid


organism: Thermus thermophilus

sequence_source: UniProtKB O87172 direct lookup from selected BRENDA/SKiD accession.

proof_lines:
pH 5.5, 70°C, competitive inhibition
pH 5.5, 70°C, uncompetitive inhibition
Raw SKiD Env: Temp=70°C, pH=5.5


sequence_source: UniProtKB O87172 direct lookup from selected BRENDA wild-type source rows.


substrate_name: maltotetraose

sequence_variant_note: Resolved canonical sequence from UniProtKB O87172 direct lookup plus selected BRENDA source note; D249S reconstructed from canonical accession sequence. and applied mutation signature D249S to reconstruct the assayed variant sequence.

substrate: maltotetraose


substrate_name: maltopentaose

sequence_variant_note: Resolved canonical sequence from UniProtKB O87172 direct lookup plus selected BRENDA source note; F366L reconstructed from canonical accession sequence. and applied mutation signature F366L to reconstruct the assayed variant sequence.

substrate: maltopentaose


organism: Aquifex aeolicus


organism: Corynebacterium glutamicum


proof_lines:
wild type enzyme, at pH 6.0 and 30°C
wild-type, pH 6.0, 30°C


organism: Ipomoea batatas


organism: Lathyrus oleraceus


organism: Manihot esculenta


organism: Paenibacillus macerans

substrate_name: dodecyl-beta-maltoside

substrate: dodecyl-beta-maltoside


organism: Pyrobaculum aerophilum


organism: Saccharolobus solfataricus

substrate_name: maltosyl-beta-cyclodextrin

proof_lines: pH 5.5, 75°C, recombinant His-tagged enzyme

substrate: maltosyl-beta-cyclodextrin


organism: Saccharomyces cerevisiae

substrate_name: phi-dextrin

proof_lines:
native enzyme
recombinant enzyme

substrate: phi-dextrin


organism: Stutzerimonas stutzeri


organism: Arabidopsis thaliana

sequence_source: UniProtKB:Q9LV91 direct REST/FASTA lookup

proof_lines:
at pH 7.0 and 37 °C
Raw SKiD Env: Temp=°C, pH=7


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8NNA7 direct REST/FASTA lookup; variant reconstructed from the canonical accession sequence and applied mutation signature H461S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8NNA7 direct REST/FASTA lookup; variant reconstructed from the canonical accession sequence and applied mutation signature H461D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8NNA7 direct REST/FASTA lookup; variant reconstructed from the canonical accession sequence and applied mutation signature H461R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8NNA7 direct REST/FASTA lookup; variant reconstructed from the canonical accession sequence and applied mutation signature H461W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8NNA7 direct REST/FASTA lookup; variant reconstructed from the canonical accession sequence and applied mutation signature H461A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q8NNA7 direct REST/FASTA lookup; variant reconstructed from the canonical accession sequence


sequence_source: UniProtKB:Q8NNA7 direct REST/FASTA lookup


substrate_name: starch

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8NNA7 direct REST/FASTA lookup; variant reconstructed from the canonical accession sequence and applied mutation signature Y23A to reconstruct the assayed variant sequence.

proof_lines: pH 6.0, 30°C, cyclization activity, recombinant mutant Y23A

proof_lines: pH 6.0, 30°C, disproportionation activity, recombinant mutant Y23A

proof_lines: pH 6.0, 30°C, starch transglycosylation, recombinant mutant Y23A

substrate: starch


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8NNA7 direct REST/FASTA lookup; variant reconstructed from the canonical accession sequence and applied mutation signature G417F to reconstruct the assayed variant sequence.

proof_lines: pH 6.0, 30°C, starch transglycosylation, recombinant mutant G417F

proof_lines: pH 6.0, 30°C, disproportionation activity, recombinant mutant G417F

proof_lines: pH 6.0, 30°C, cyclization activity, recombinant mutant G417F


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8NNA7 direct REST/FASTA lookup; variant reconstructed from the canonical accession sequence and applied mutation signature E231Y to reconstruct the assayed variant sequence.

proof_lines: pH 6.0, 30°C, starch transglycosylation, recombinant mutant E231Y

proof_lines: pH 6.0, 30°C, cyclization activity, recombinant mutant E231Y

proof_lines: pH 6.0, 30°C, disproportionation activity, recombinant mutant E231Y


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8NNA7 direct REST/FASTA lookup; variant reconstructed from the canonical accession sequence and applied mutation signature P228Y to reconstruct the assayed variant sequence.

proof_lines: pH 6.0, 30°C, starch transglycosylation, recombinant mutant P228Y

proof_lines: pH 6.0, 30°C, disproportionation activity, recombinant mutant P228Y

proof_lines: pH 6.0, 30°C, cyclization activity, recombinant mutant P228Y


substrate_name: starch; maltotriose

proof_lines: pH 6.0, 30°C, disproportionation activity, recombinant wild-type enzyme

proof_lines: pH 6.0, 30°C, starch transglycosylation, recombinant wild-type enzyme

substrate: starch; maltotriose


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


substrate_name: maltoheptaose

column_label: Table 2 (Kinetics of glucose release by PyAMase for G3 to G7), substrate row 'G7'; column 'Km (mM)' = 1.5 (printed with its plus-minus term 0.5); column 'kcat (s^-1)' = 8.7 (printed with its plus-minus term 0.6); column 'kcat/Km (mM^-1 s^-1)' = 5.8 (printed without a plus-minus term).

normalized_value_unit_evidence: Km: printed Table 2 cell 1.5 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 1.5 mM; the exported value is 1.5 mM. kcat: printed Table 2 cell 8.7 under the column head kcat (s^-1); the column is already per second, so no unit conversion applies and the paper value is 8.7 s^(-1); the exported value is 8.7 s^(-1). kcat/Km: printed Table 2 cell 5.8 under the column head kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell is 5.8 s^(-1)*mM^(-1); the exported value is 5.8 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate row 'G7' (maltoheptaose): Km = 1.5 mM; kcat = 8.7 s^-1; printed kcat/Km = 5.8 mM^-1 s^-1.

table_label: Table 2: Kinetics of glucose release by PyAMase for G3 to G7 (Applied and Environmental Microbiology 2005, 71(9):5098-5106)

substrate: maltoheptaose


substrate_name: Maltotriose

column_label: Table 2 (Kinetics of glucose release by PyAMase for G3 to G7), substrate row 'G3'; column 'Km (mM)' = 3.7 (printed with its plus-minus term 0.5); column 'kcat (s^-1)' = 115 (printed with its plus-minus term 5); column 'kcat/Km (mM^-1 s^-1)' = 31 (printed without a plus-minus term).

normalized_value_unit_evidence: Km: printed Table 2 cell 3.7 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 3.7 mM; the exported value is 3.7 mM. kcat: printed Table 2 cell 115 under the column head kcat (s^-1); the column is already per second, so no unit conversion applies and the paper value is 115.0 s^(-1); the exported value is 115.0 s^(-1). kcat/Km: printed Table 2 cell 31 under the column head kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell is 31.0 s^(-1)*mM^(-1); the exported value 31.08108108108108 s^(-1)*mM^(-1) is the full-precision quotient of the two printed component cells, 115 / 3.7, and that quotient written to the significant figures of the printed column is 31, the printed cell.

raw_value_unit_evidence: Table 2, substrate row 'G3' (maltotriose): Km = 3.7 mM; kcat = 115 s^-1; printed kcat/Km = 31 mM^-1 s^-1.

substrate: Maltotriose


substrate_name: Maltohexaose

column_label: Table 2 (Kinetics of glucose release by PyAMase for G3 to G7), substrate row 'G6'; column 'Km (mM)' = 3.2 (printed with its plus-minus term 1.0); column 'kcat (s^-1)' = 8.9 (printed with its plus-minus term 0.6); column 'kcat/Km (mM^-1 s^-1)' = 2.8 (printed without a plus-minus term).

normalized_value_unit_evidence: Km: printed Table 2 cell 3.2 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 3.2 mM; the exported value is 3.2 mM. kcat: printed Table 2 cell 8.9 under the column head kcat (s^-1); the column is already per second, so no unit conversion applies and the paper value is 8.9 s^(-1); the exported value is 8.9 s^(-1). kcat/Km: printed Table 2 cell 2.8 under the column head kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell is 2.8 s^(-1)*mM^(-1); the exported value 2.78125 s^(-1)*mM^(-1) is the full-precision quotient of the two printed component cells, 8.9 / 3.2, and that quotient written to the significant figures of the printed column is 2.8, the printed cell.

raw_value_unit_evidence: Table 2, substrate row 'G6' (maltohexaose): Km = 3.2 mM; kcat = 8.9 s^-1; printed kcat/Km = 2.8 mM^-1 s^-1.

substrate: Maltohexaose


column_label: Table 2 (Kinetics of glucose release by PyAMase for G3 to G7), substrate row 'G5'; column 'Km (mM)' = 6.9 (printed with its plus-minus term 1.7); column 'kcat (s^-1)' = 24.8 (printed with its plus-minus term 2.1); column 'kcat/Km (mM^-1 s^-1)' = 3.6 (printed without a plus-minus term).

normalized_value_unit_evidence: Km: printed Table 2 cell 6.9 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 6.9 mM; the exported value is 6.9 mM. kcat: printed Table 2 cell 24.8 under the column head kcat (s^-1); the column is already per second, so no unit conversion applies and the paper value is 24.8 s^(-1); the exported value is 24.8 s^(-1). kcat/Km: printed Table 2 cell 3.6 under the column head kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell is 3.6 s^(-1)*mM^(-1); the exported value 3.5942028985507246 s^(-1)*mM^(-1) is the full-precision quotient of the two printed component cells, 24.8 / 6.9, and that quotient written to the significant figures of the printed column is 3.6, the printed cell.

raw_value_unit_evidence: Table 2, substrate row 'G5' (maltopentaose): Km = 6.9 mM; kcat = 24.8 s^-1; printed kcat/Km = 3.6 mM^-1 s^-1.