enzyme_display_name: Penicillin-binding protein 2a

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

substrate_name: dansylated lipid II

proof_lines: kcat is greater than 0.0005 sec(-1) with dansylated lipid II as substrate (PubMed:22487093). kcat/KM is 0.001 M(-1)sec(-1) with dansylated lipid II as substrate (PubMed:12867450).

enzyme: Penicillin-binding protein 2a

substrate: dansylated lipid II


organism: Streptomyces sp.

substrate_name: benzoyl-Gly-thioglycolate

source_db: brenda

verification_status: unverified

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 uniprot_ec_organism_mutation_ranked_match and applied mutation signature C98A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines:
pH 7.2, 37°C, mutant enzyme C98A
above, pH 7.2, 37°C, mutant enzyme C98A

substrate: benzoyl-Gly-thioglycolate

status: unverified

source: brenda


substrate_name: benzoyl-Gly-thiolactate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K38H with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

substrate: benzoyl-Gly-thiolactate


enzyme_display_name: Carboxypeptidase Y

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: furylacryloyl-Phe-Leu-OH

source_db: uniprot

kcat_display: Not reported

mutation_signature: Unknown

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

proof_lines: kcat is 4900 min(-1) with furylacryloyl-Phe-Leu-OH as substrate.

enzyme: Carboxypeptidase Y

substrate: furylacryloyl-Phe-Leu-OH

source: uniprot


enzyme_display_name: carboxypeptidase A

organism: Rattus norvegicus

substrate_name: H2O; Carbobenzoxy-Gly-Gly-Phe

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

enzyme: carboxypeptidase A

substrate: H2O; Carbobenzoxy-Gly-Gly-Phe


enzyme_display_name: carboxypeptidase B

organism: Protopterus aethiopicus

substrate_name: benzoyl-Gly-L-Arg

sequence: EPTPRSFNGDKVFRV

wild_type_sequence: EPTPRSFNGDKVFRV

enzyme: carboxypeptidase B

substrate: benzoyl-Gly-L-Arg


organism: Helicoverpa armigera

substrate_name: Carbobenzoxy-Gly-Gly-Leu

source_db: oed

proof_lines:
Helicoverpa armigera
carboxypeptidase A
Carbobenzoxy-Gly-Gly-Leu

data_origin: experimental

substrate: Carbobenzoxy-Gly-Gly-Leu

source: oed


substrate_name: Carbobenzoxy-Gly-Gly-Phe

proof_lines:
Helicoverpa armigera
carboxypeptidase A
Carbobenzoxy-Gly-Gly-Phe

substrate: Carbobenzoxy-Gly-Gly-Phe


substrate_name: Carbobenzoxy-Gly-Gly-Val

kcat_over_km_origin: calculated

proof_lines:
Helicoverpa armigera
carboxypeptidase A
Carbobenzoxy-Gly-Gly-Val

substrate: Carbobenzoxy-Gly-Gly-Val


substrate_name: Carbobenzoxy-Gly-Phe

proof_lines:
Helicoverpa armigera
carboxypeptidase A
Carbobenzoxy-Gly-Phe

substrate: Carbobenzoxy-Gly-Phe


organism: Escherichia coli

substrate_name: Carboxymethylbenzoylaminothioacetate

proof_lines:
class A beta-lactamase
class C beta-lactamase
DD-peptidase

substrate: Carboxymethylbenzoylaminothioacetate


substrate_name: Phenyl-lactyl benzoylaminoacetate

substrate: Phenyl-lactyl benzoylaminoacetate


enzyme_display_name: Maltose-6'-phosphate glucosidase

organism: Bacillus subtilis (strain 168)

assay_conditions_summary: pH 8.4; cofactor NAD+

enzyme: Maltose-6'-phosphate glucosidase


substrate_name: arabinotetraose (at 27 degrees Celsius and pH 7)

assay_conditions_summary: pH 7

proof_lines:
AbnA
Bacillus subtilis strain 168
endo-arabinanase


enzyme_display_name: leukotriene-A4 hydrolase

organism: Mus musculus

substrate_name: leukotriene A4

sequence_source: multiple

assay_conditions_summary: pH 8

source_databases_merged: brenda uniprot

enzyme: leukotriene-A4 hydrolase

substrate: leukotriene A4


enzyme_display_name: Tripeptidyl-peptidase sed2

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

substrate_name: Phe-Pro-Ala-pNA (at 20 degrees Celsius)

enzyme: Tripeptidyl-peptidase sed2

substrate: Phe-Pro-Ala-pNA (at 20 degrees Celsius)


enzyme_display_name: UniProt Q04609

organism: Homo sapiens

substrate_name: N-acetyl-L-aspartyl-L-glutamate

source_db: skid

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=37°C, pH=7.4

enzyme: UniProt Q04609

substrate: N-acetyl-L-aspartyl-L-glutamate

source: skid


enzyme_display_name: UniProt P39377

substrate_name: beta-Asp-Phe

enzyme: UniProt P39377

substrate: beta-Asp-Phe


substrate_name: beta-Asp-His

substrate: beta-Asp-His


substrate_name: beta-Asp-Gly

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

substrate: beta-Asp-Gly


substrate_name: alpha-Asp-Leu

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

substrate: alpha-Asp-Leu


enzyme_display_name: UniProt Q484B6

organism: Colwellia psychrerythraea

enzyme: UniProt Q484B6


substrate_name: beta-Asp-Leu

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

substrate: beta-Asp-Leu


substrate_name: beta-Ala-Ala

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

substrate: beta-Ala-Ala


enzyme_display_name: UniProt O25743

organism: Helicobacter pylori

substrate_name: L-glutamine

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

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7
Raw SKiD Env: Temp=37°C, pH=9
Raw SKiD Env: Temp=37°C, pH=8

enzyme: UniProt O25743

substrate: L-glutamine


substrate_name: glutathione

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

substrate: glutathione


enzyme_display_name: UniProt P00766

organism: Bos taurus

enzyme: UniProt P00766


substrate_name: 4-nitrophenyl benzoate

substrate: 4-nitrophenyl benzoate


substrate_name: N-benzoyl-L-tyrosine 4-nitroanilide

substrate: N-benzoyl-L-tyrosine 4-nitroanilide


substrate_name: N-benzoyl-L-tyrosine ethyl ester

substrate: N-benzoyl-L-tyrosine ethyl ester


enzyme_display_name: chymotrypsin

substrate_name: 4-nitrophenyl acetate

enzyme: chymotrypsin

substrate: 4-nitrophenyl acetate


enzyme_display_name: UniProt P00775

organism: Streptomyces griseus

km_display: Not reported

enzyme: UniProt P00775


enzyme_display_name: UniProt P00734

substrate_name: Fibrinopeptide A

enzyme: UniProt P00734

substrate: Fibrinopeptide A


enzyme_display_name: UniProt P98073

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8.4
Raw SKiD Env: Temp=37°C, pH=-----

enzyme: UniProt P98073


substrate_name: Z-Lys-SBzl

substrate: Z-Lys-SBzl


enzyme_display_name: cucumisin

organism: Cucumis melo

substrate_name: Ala-Ala-Pro-Phe-p-nitroanilide

enzyme: cucumisin

substrate: Ala-Ala-Pro-Phe-p-nitroanilide


substrate_name: Ala-Ala-Pro-Leu-p-nitroanilide

substrate: Ala-Ala-Pro-Leu-p-nitroanilide


enzyme_display_name: UniProt Q9X6R4

organism: Aeromonas caviae

enzyme: UniProt Q9X6R4


enzyme_display_name: leukocyte elastase

enzyme: leukocyte elastase


enzyme_display_name: subtilisin

organism: Bacillus lentus

substrate_name: Peptidyl-p-nitroanilide

sequence_variant_note: Mutation signature L217C could not be applied safely because the resolved sequence does not match the expected reference residue(s).

enzyme: subtilisin

substrate: Peptidyl-p-nitroanilide


sequence_variant_note: Mutation signature L217C/H2C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M222C with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature N62C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature N62C/H2C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature S166C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature S166C/H2C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: peptidase K

organism: Parengyodontium album

substrate_name: benzoyl-L-Arg ethyl ester

enzyme: peptidase K

substrate: benzoyl-L-Arg ethyl ester


enzyme_display_name: UniProt P04070

substrate_name: spectrozyme PCa

enzyme: UniProt P04070

substrate: spectrozyme PCa


enzyme_display_name: Thermomycolin

organism: Malbranchea pulchella

substrate_name: Acetyl-Ala-Ala-Ala methyl ester

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

enzyme: Thermomycolin

substrate: Acetyl-Ala-Ala-Ala methyl ester


enzyme_display_name: Pancreatic endopeptidase E

organism: Sus scrofa

substrate_name: Benzoyl-L-alanine methyl ester

enzyme: Pancreatic endopeptidase E

substrate: Benzoyl-L-alanine methyl ester


substrate_name: Succinyl-tri-L-alanine 4-nitroanilide

substrate: Succinyl-tri-L-alanine 4-nitroanilide


enzyme_display_name: Endopeptidase So

substrate_name: casein

enzyme: Endopeptidase So

substrate: casein


substrate_name: Unknown

ki_unit: mM

proof_lines: substrate Abz-DIYISRRLL-GTFT-Tyx-A, 37°C, pH 7.4

substrate: Unknown


enzyme_display_name: Thermitase

organism: Coprothermobacter proteolyticus

proof_lines: pH 7.5, 40°C, recombinant wild-type enzyme, in presence of DTT

proof_lines: pH 7.5, 70°C, recombinant wild-type enzyme

enzyme: Thermitase


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

proof_lines: pH 7.5, 40°C, recombinant mutant C182A/C201A, in presence of DTT

proof_lines: pH 7.5, 70°C, recombinant mutant C182A/C201A


enzyme_display_name: protein C (activated)

enzyme: protein C (activated)


enzyme_display_name: IgA-specific serine endopeptidase

organism: Streptococcus sanguinis

substrate_name: IgA

enzyme: IgA-specific serine endopeptidase

substrate: IgA


enzyme_display_name: t-Plasminogen activator

organism: synthetic construct

proof_lines: recombinant tPA bound to polyacrylic acid-coated magnetite

enzyme: t-Plasminogen activator


organism: Prevotella melaninogenica


substrate_name: Acetyl-tri-L-alanine methyl ester

substrate: Acetyl-tri-L-alanine methyl ester


substrate_name: Lys-plasminogen

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature L420E/P422E with inferred residue-numbering offset -39 to reconstruct the assayed variant sequence.

proof_lines: pH 7.2, 37°C, mutant L420E and P422E, two-chain form, absence of soluble fibrin

substrate: Lys-plasminogen


organism: Mus musculus


enzyme_display_name: activated protein C (thrombin-activated peptidase)

substrate_name: SpPCa

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature E167A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: SpPCa


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature E170A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

enzyme: activated protein C (thrombin-activated peptidase)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R75A to reconstruct the assayed variant sequence.


enzyme_display_name: thermitase

enzyme: thermitase


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

proof_lines: pH 7.2, 37°C, mutant P422E/R275E, single-chain form, absence of soluble fibrin

proof_lines: pH 7.2, 37°C, mutant P422E/R275E, single-chain form, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant P422G/R275E, single-chain form, absence of soluble fibrin

proof_lines: pH 7.2, 37°C, mutant P422G/R275E, single-chain form, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant S421G/R275E, single-chain form, absence of soluble fibrin

proof_lines: pH 7.2, 37°C, mutant S421G/R275E, single-chain form, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant P422E, two-chain form, absence of soluble fibrin

proof_lines: pH 7.2, 37°C, mutant P422E, two-chain form, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant L420E/R275E and S421E/R275E, single-chain form, absence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant P422G, two-chain form, absence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant F423E/R275E, single-chain form, absence of soluble fibrin

proof_lines: pH 7.2, 37°C, mutant F423E/R275E, single-chain form, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant F423A/R275E, single-chain form, absence of soluble fibrin

proof_lines: pH 7.2, 37°C, mutant F423A/R275E, single-chain form, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant L420E, two-chain form, absence of soluble fibrin

proof_lines: pH 7.2, 37°C, mutant L420E, two-chain form, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant P422A/R275E, single-chain form, absence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant L420A/R275E, single-chain form, absence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant L420A, two-chain form, absence of soluble fibrin

proof_lines: pH 7.2, 37°C, mutant L420A, two-chain form, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant S421E, two-chain form, absence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant F423E, two-chain form, absence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant S421G, two-chain form, absence of soluble fibrin

proof_lines: pH 7.2, 37°C, mutant S421G, two-chain form, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant F423A, two-chain form, absence of soluble fibrin

proof_lines: pH 7.2, 37°C, two-chain form of mutant F423A, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant R275E, single-chain form, absence of soluble fibrin

proof_lines: pH 7.2, 37°C, mutant R275E, single-chain form, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant P422A, two-chain form, absence of soluble fibrin

proof_lines: pH 7.2, 37°C, mutant P422A, two-chain form, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, wild-type, two-chain form, absence of soluble fibrin

proof_lines: pH 7.2, 37°C, wild-type, two-chain form, presence of soluble fibrin

proof_lines: pH 7.2, 37°C, two-chain form of wild-type and mutant F423E, single-chain form of mutant P422E/R275E, absence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant S421G and P422A, two-chain form, presence of soluble fibrin


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


proof_lines: pH 7.2, 37°C, two-chain form of mutant S421E, P422E and P422G, single chain form of mutant L420E/R275E, P422A/R275E and F423E/R275E, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, two-chain form of mutant L420E and L420A, single chain form of mutant P422E/R275E, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, two-chain form of mutant F423E, single-chain form of mutant L420A/R275E, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant P422G/R275E and S421E/R275E, single-chain form, presence of soluble fibrin


substrate_name: spectrozyme tPA

proof_lines: pH 7.2, 37°C, mutant F423E/R275E, single chain form

substrate: spectrozyme tPA


proof_lines: pH 7.2, 37°C, mutant S421G, two-chain form


proof_lines: pH 7.2, 37°C, mutant P422G/R275E, single chain form


proof_lines: pH 7.2, 37°C, mutant S421G/R275E, single chain form


proof_lines: pH 7.2, 37°C, mutant S421E/R275E, single chain form


proof_lines: pH 7.2, 37°C, mutant F423A/R275E, single chain form


proof_lines: pH 7.2, 37°C, mutant L420E/R275E, single chain form


proof_lines: pH 7.2, 37°C, mutant P422E/R275E, single chain form


proof_lines: pH 7.2, 37°C, mutant P422A/R275E, single chain form


proof_lines: pH 7.2, 37°C, mutant R275E, single chain form


proof_lines: pH 7.2, 37°C, mutant L420A/R275E, single chain form

proof_lines: pH 7.2, 37°C, mutant L420A/R275E, two-chain form


proof_lines: pH 7.2, 37°C, mutant L420A, L420E, two-chain form


proof_lines: pH 7.2, 37°C, mutant S421E, two-chain form


proof_lines: pH 7.2, 37°C, wild-type t-PA, mutant P422A, two-chain form

proof_lines: pH 7.2, 37°C, wild-type t-PA, mutant L420A, L420E, S421G, S421E, P422A, P422E, two-chain form


proof_lines: pH 7.2, 37°C, mutant F423E, two-chain form


proof_lines: pH 7.2, 37°C, mutant P422E, F423A, two-chain form


proof_lines: pH 7.2, 37°C, mutant R275E and P422A/R275E, single-chain form, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, two-chain form of mutant F423A, single-chain form of mutant L420A/R275E, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, two-chain form of mutant S421E, single-chain form of mutant L420E/R275E, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, two-chain form of mutant F423E, single-chain form of mutant S421E/R275E, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, two-chain form of mutant P422G, single-chain form of mutant S421G/R275E, presence of soluble fibrin


proof_lines: pH 7.2, 37°C, two-chain form of mutant S421G, F423A and P422A, single chain form of mutant S421G/R275E and P422G/R275E, absence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant L420E/R275E, single-chain form, absence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant S421E/R275E, single-chain form, absence of soluble fibrin


proof_lines: pH 7.2, 37°C, mutant F423A, F422E, two-chain form


proof_lines: pH 7.2, 37°C, mutant L420E/R275E, F423E/R275E, single chain form


proof_lines: pH 7.2, 37°C, mutant R275E, F423A/R275E, single-chain form


proof_lines:
with Na+ or Cs+ as activating cation
with Cs+ as activating cation
with Na+ as activating cation


proof_lines: pH 7.4, 37°C, wildtype enzyme, recombinant expressed and mutant R74A


proof_lines: pH 7.4, 37°C, mutant K78A and mutant R75A


substrate_name: plasminogen

proof_lines:
pH 7.4, 37°C, absence of fibrinogen
pH 7.4, 37°C

substrate: plasminogen


enzyme_display_name: myeloblastin

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

enzyme: myeloblastin


enzyme_display_name: Pancreatic elastase II

substrate_name: Gly-Ile-Asp-Val-Gln-Ile-Tyr

enzyme: Pancreatic elastase II

substrate: Gly-Ile-Asp-Val-Gln-Ile-Tyr


organism: Haemophilus influenzae


enzyme_display_name: oligopeptidase B

organism: Unknown

source_db: unknown

source_license: see source

enzyme: oligopeptidase B

source: unknown


organism: Homo sapiens

proof_lines: pH 7.4, 37°C, recombinant wild-type enzyme


enzyme_display_name: signal peptidase I

enzyme: signal peptidase I


enzyme_display_name: cytosol alanyl aminopeptidase

enzyme: cytosol alanyl aminopeptidase


proof_lines:
pH 7.4, 37°C
pH 7.4, 25°C, sc-tPA
pH 7.4, 25°C, tc-tPA


substrate_name: Factor VaR506Q

proof_lines: pH 7.2, 37°C, cleavage at Arg336 in A1 subunit

substrate: Factor VaR506Q


enzyme_display_name: thymine-DNA glycosylase

substrate_name: thymine-mismatched double-stranded DNA

proof_lines: excision of 3,N4-ethenocytosine from 3,N4-ethenocytidine/G mismatches

enzyme: thymine-DNA glycosylase

substrate: thymine-mismatched double-stranded DNA


enzyme_display_name: aspartyl aminopeptidase

substrate_name: Asp-Ala-Pro-sulfamethoxazole

enzyme: aspartyl aminopeptidase

substrate: Asp-Ala-Pro-sulfamethoxazole


proof_lines: reaction volume containing 4-methylumbelliferyl alpha-D-mannopyranoside, sodium acetate pH 5.6 and ZnCl at 37°C

proof_lines: extracted from human glioblastoma cells LNZ308


enzyme_display_name: membrane dipeptidase

substrate_name: glycyldehydrophenylalanine

enzyme: membrane dipeptidase

substrate: glycyldehydrophenylalanine


enzyme_display_name: methionyl aminopeptidase

organism: Klebsiella pneumoniae

enzyme: methionyl aminopeptidase


enzyme_display_name: Xaa-Pro dipeptidyl-peptidase

organism: Lactococcus lactis

substrate_name: Gly-Pro-Gly-Gly

enzyme: Xaa-Pro dipeptidyl-peptidase

substrate: Gly-Pro-Gly-Gly


organism: Lactobacillus helveticus

substrate_name: L-Ala-L-Pro-L-Tyr

substrate: L-Ala-L-Pro-L-Tyr


enzyme_display_name: microsomal epoxide hydrolase

organism: Manduca sexta

substrate_name: juvenile hormone III

enzyme: microsomal epoxide hydrolase

substrate: juvenile hormone III


enzyme_display_name: tripeptidyl-peptidase II

substrate_name: L-Ala-L-Ala-L-Phe-p-nitroanilide

assay_conditions_summary: pH 7.5; 310.15 K; buffer 100 mM potassium phosphate

proof_lines: mutant enzyme E331K, Km above 1.0 mM, in 100 mM potassium phosphate buffer, pH 7.5, containing 2 mM dithiothreitol, and 15% glycerol, at 37°C

enzyme: tripeptidyl-peptidase II

substrate: L-Ala-L-Ala-L-Phe-p-nitroanilide


organism: Neisseria gonorrhoeae


enzyme_display_name: dipeptidyl-peptidase IV

enzyme: dipeptidyl-peptidase IV


organism: Oryctolagus cuniculus

substrate_name: glycoprotein IV from ovalbumin

assay_conditions_summary: pH 6

substrate: glycoprotein IV from ovalbumin


enzyme_display_name: cellulose 1,4-beta-cellobiosidase (non-reducing end)

organism: Phanerodontia chrysosporium

substrate_name: p-nitrophenyl-beta-D-cellobioside

substrate: p-nitrophenyl-beta-D-cellobioside


organism: Plasmodium falciparum

substrate_name: Met-peptide

substrate: Met-peptide


proof_lines:
at pH 7.5, in the absesence of Co2+
at pH 7.5, in the absence of Co2+
at pH 7.5, in the presence of 1 mM Co2+


enzyme_display_name: Genome polyprotein

organism: Hepatitis GB virus B

substrate_name: ATP for NS3 NTPase

enzyme: Genome polyprotein

substrate: ATP for NS3 NTPase


substrate_name: CTP for NS3 NTPase

substrate: CTP for NS3 NTPase


substrate_name: UTP for NS3 NTPase

substrate: UTP for NS3 NTPase


substrate_name: dATP for NS3 NTPase

substrate: dATP for NS3 NTPase


substrate_name: dCTP for NS3 NTPase

substrate: dCTP for NS3 NTPase


substrate_name: dTTP for NS3 NTPase

substrate: dTTP for NS3 NTPase


substrate_name: Met-Gly-Met-Met

proof_lines:
presence of 0.1 mM Zn2+, pH 7.5, 37°C
presence of 0.1 mM Co2+, pH 7.5, 37°C

substrate: Met-Gly-Met-Met


enzyme_display_name: prunasin beta-glucosidase

organism: Prunus serotina

substrate_name: Unknown

proof_lines:
PH IIb, pH 5, 30°C
PH I, pH 5, 30°C

enzyme: prunasin beta-glucosidase

substrate: Unknown


organism: Rattus norvegicus

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


enzyme_display_name: amygdalin beta-glucosidase

substrate_name: (R)-amygdalin

proof_lines:
AH II'
AH II
AH I

enzyme: amygdalin beta-glucosidase

substrate: (R)-amygdalin


substrate_name: cis-stilbene oxide

substrate: cis-stilbene oxide


assay_conditions_summary: pH 9; 310.15 K; buffer Tris/HCl

proof_lines: in Tris/HCl buffer (0.1 M, pH 9.0), at 30°C

proof_lines: pH 7.4, 37°C, competitive inhibition type


substrate_name: styrene oxide

substrate: styrene oxide


enzyme_display_name: tripeptidyl-peptidase I

assay_conditions_summary: pH 4

enzyme: tripeptidyl-peptidase I


organism: Saccharomyces cerevisiae

substrate_name: L-Met-PSI[C(O)S]Gly-L-Phe

proof_lines:
Co(II)-form of enzyme, 22°C, pH 7.0
pH 7.25, 30°C
Zn(II)-form of enzyme, 22°C, pH 7.0

substrate: L-Met-PSI[C(O)S]Gly-L-Phe


substrate_name: angiotensin I

substrate: angiotensin I


enzyme_display_name: lysoplasmalogenase

substrate_name: lysoplasmenylcholine

assay_conditions_summary: pH 7.1; cofactor NADH

proof_lines: pH 7.1, temperature not specified in the publication. Coupled enzyme assay, the aldehyde that is produced by hydrolysis of lysoplasmalogen is reduced to an alcohol in a second enzymic reaction. In the second reaction, NADH is oxidized in a

enzyme: lysoplasmalogenase

substrate: lysoplasmenylcholine


organism: Streptococcus pneumoniae

substrate_name: L-Met 4-nitroanilide

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

substrate: L-Met 4-nitroanilide


enzyme_display_name: carboxypeptidase C

substrate_name: endothelin

enzyme: carboxypeptidase C

substrate: endothelin


enzyme_display_name: endo-alpha-N-acetylgalactosaminidase

enzyme: endo-alpha-N-acetylgalactosaminidase


organism: Streptomyces sp.

substrate_name: benzoyl-Gly-thiolactate

proof_lines:
pH 7.2, 37°C, wild-type enzyme
above, pH 7.2, 37°C, wild-type enzyme

substrate: benzoyl-Gly-thiolactate


substrate_name: L-methionine 4-nitroanilide

substrate: L-methionine 4-nitroanilide


proof_lines:
pH 7.5, 25°C
Streptomyces sp. R39
Streptomyces sp. R61


organism: Sus scrofa

proof_lines:
pH 7.2, 30°C
at pH 8.0 and 37°C
microsomal enzyme, at pH 8.0 and 37°C


organism: Streptococcus thermophilus


substrate_name: Met-Val-His-Thr-Leu-Pro-Glu-Glu-Leu

substrate: Met-Val-His-Thr-Leu-Pro-Glu-Glu-Leu


substrate_name: Gly-Pro-Met 2-naphthylamide

substrate: Gly-Pro-Met 2-naphthylamide


enzyme_display_name: lysosomal Pro-Xaa carboxypeptidase

substrate_name: N-benzyloxycarbonyl-Pro-Phe

enzyme: lysosomal Pro-Xaa carboxypeptidase

substrate: N-benzyloxycarbonyl-Pro-Phe


substrate_name: Glu 2-naphthylamide

substrate: Glu 2-naphthylamide


substrate_name: glycyldehydrophenylalanine

substrate: glycyldehydrophenylalanine


substrate_name: Gly-D-Phe

substrate: Gly-D-Phe


enzyme_display_name: cytosol nonspecific dipeptidase

substrate_name: carnosine

enzyme: cytosol nonspecific dipeptidase

substrate: carnosine


organism: Thermoascus aurantiacus

substrate_name: 4-nitrophenyl beta-D-cellobioside

enzyme: cellulose 1,4-beta-cellobiosidase (non-reducing end)

substrate: 4-nitrophenyl beta-D-cellobioside


enzyme_display_name: aspartyl aminopeptidase

organism: Toxoplasma gondii

proof_lines: pH 7.5, 37°C, recombinant enzyme, with Co2+

enzyme: aspartyl aminopeptidase


organism: Vibrio cholerae

proof_lines: pH and temperature not specified in the publication


organism: Streptococcus pyogenes


organism: Bacillus subtilis


organism: Enterococcus hirae


enzyme_display_name: UniProt O15393

organism: Homo sapiens

enzyme: UniProt O15393


enzyme_display_name: papain

organism: Carica papaya

substrate_name: N-benzoylglycinamide

enzyme: papain

substrate: N-benzoylglycinamide


enzyme_display_name: fructan beta-(2,6)-fructosidase

organism: Beta vulgaris

substrate_name: sucrose

enzyme: fructan beta-(2,6)-fructosidase

substrate: sucrose


enzyme_display_name: methionyl aminopeptidase

organism: Vibrio coralliilyticus

enzyme: methionyl aminopeptidase


enzyme_display_name: kumamolysin

organism: Bacillus novosp.

enzyme: kumamolysin


organism: Alicyclobacillus sendaiensis

proof_lines:
mutant enzyme E78H
pH 4.0, 40°C, recombinant mutant E78H


enzyme_display_name: cathepsin B

organism: Artemia sp.

enzyme: cathepsin B


organism: Capra aegagrus

proof_lines:
free enzyme
encapsulated enzyme


organism: Heyndrickxia coagulans


organism: Dorytheuthis bleekeri

substrate_name: benzoyl-DL-Arg-beta-naphthylamide

substrate: benzoyl-DL-Arg-beta-naphthylamide


substrate_name: IQF peptide

verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q8GB88 and applied mutation signature E78H/D164N with inferred residue-numbering offset +189 to reconstruct the assayed variant sequence.

column_label: Official Wiley Table 1; row E78H/D164N; kcat column raw cell 0.00045 +/- 0.00005 s^-1; Km and kcat/Km cells nd under footnote b; assay pH 4.0 and 40 C.

normalized_value_unit_evidence: Paper kcat 0.00045 s^-1 exactly matches export 0.00045 s^-1. No Km normalization is required because Km is not populated for this row.

raw_value_unit_evidence: Table 1 E78H/D164N row reports kcat = 0.00045 +/- 0.00005 s^-1. Km is nd under footnote b and is not populated in the export row.

row_label: E78H/D164N mature kumamolisin-As / IQF NMA-MGPH*FFPK-(DNP)dRdR

table_label: 2006 Wiley Table 1: Kinetic parameters of kumamolisin-As mutants

substrate: IQF peptide

status: verified


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D164N to reconstruct the assayed variant sequence.


column_label: Official 2004 JBC full-text kinetic prose; wild-type kumamolisin-As / IQF substrate; explicit kcat 395 +/- 7 s^-1 and Km 1.0 +/- 0.2 uM. The 2006 Wiley Table 1 wild-type row explicitly points back to this source in footnote a.

normalized_value_unit_evidence: Paper kcat 395 s^-1 exactly matches export 395.0 s^-1. Paper Km 1.0 uM converts to 0.0010 mM and exactly matches export 0.001 mM.

raw_value_unit_evidence: The 2004 JBC primary paper reports kcat = 395 +/- 7 s^-1 and Km = 1.0 +/- 0.2 uM for wild-type kumamolisin-As with the IQF substrate at pH 4.0 and 40 C.

row_label: Wild-type mature kumamolisin-As / IQF NMA-MGPH*FFPK-(DNP)dRdR

table_label: 2004 JBC primary full-text, Specificity Analysis of Kumamolisin-As kinetic prose; values are also carried in 2006 Wiley Table 1 with footnote a


organism: Heliocidaris crassispina


organism: Fasciola hepatica


organism: Hemicentrotus pulcherrimus


organism: Meretrix meretrix


organism: Fasciola gigantica


organism: Nicotiana benthamiana

substrate_name: Abz-GIVRAK-Dnp

substrate: Abz-GIVRAK-Dnp


organism: Schistosoma mansoni


organism: Sus scrofa

proof_lines:
isoenzyme II
isoenzyme I
isoenzyme I and isoenzyme II


substrate_name: benzoyl-Pro-Phe-Arg-p-nitroanilide

proof_lines:
isoenzyme I
isoenzyme II

substrate: benzoyl-Pro-Phe-Arg-p-nitroanilide


organism: Bubalus bubalis

substrate_name: hemoglobin

substrate: hemoglobin


enzyme_display_name: ficain

organism: Ficus insipida

enzyme: ficain


organism: Alphacoronavirus

proof_lines: pH not specified in the publication, 30°C, PLpro(1541-1858, DNA fragment)

proof_lines: pH not specified in the publication, 30°C, PLpro(1600-1858, DNA fragment)


organism: Ficus johannis

substrate_name: casein

substrate: casein


organism: Tetrahymena pyriformis


organism: Ficus pumila var. awkeotsang

substrate_name: azocasein

substrate: azocasein


enzyme_display_name: Papain

organism: Carica papaya

substrate_name: N-benzoyl-DL-arginine p-nitroanilide

proof_lines: kcat is 1.021 sec(-1) with L-pyroglutamyl-L-phenylalanyl-L-leucyl-p-nitroanilide as substrate (PubMed:23151624). kcat is 0.73 sec(-1) with N-benzoyl-DL-arginine p-nitroanilide as substrate (PubMed:23151624). kcat is 1.6 sec(-1) with Boc-Ala

enzyme: Papain

substrate: N-benzoyl-DL-arginine p-nitroanilide


organism: Naegleria fowleri


organism: Rattus norvegicus

substrate_name: H2O; Z-Arg-Arg-p-nitroanilide

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

substrate: H2O; Z-Arg-Arg-p-nitroanilide


enzyme_display_name: Kumamolisin

organism: Bacillus sp. (strain MN-32)

proof_lines: kcat is 176 sec(-1) with Lys-Pro-Ile-Pro-Phe-p-nitrophenylalanine-Arg-Leu as substrate (PubMed:10965051). kcat is 6.02 sec(-1) with Lys-Pro-Ile-Ala-Phe-p-nitrophenylalanine-Arg-Leu as substrate (at 60 degrees Celsius and pH 3.5) (PubMed:152

enzyme: Kumamolisin


sequence_variant_note: Mutation signature V133A/S205E could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature V133A/V157G/S205E could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


substrate_name: Boc-L-His

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

substrate: Boc-L-His


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

assay_conditions_summary: pH 7.5; 318.15 K; buffer + 12% ethanol, pH 3

proof_lines: papain immobilized on sepharose 6B, pH 7.5, 22°C

proof_lines: papain immobilized on sepharose 6B in presence of 200 mM cysteine, pH 7.5, 22°C

source_databases_merged: sabio_rk brenda skid uniprot


organism: Trichinella spiralis

substrate_name: Z-L-Phe-L-Arg 7-amido-4-methylcoumarin

substrate: Z-L-Phe-L-Arg 7-amido-4-methylcoumarin


verification_status: corrected

normalized_value_unit_evidence: kcat normalized_value=2.9 normalized_unit=s^-1; Km normalized_value=0.0014 normalized_unit=mM; kcat_over_km normalized_value=2037 normalized_unit=s^-1*mM^-1.

row_label: NbCathB; Abz-FRF(NO2)A

table_label: Table 1. Kinetic parameters of recombinant N. benthamiana PLCPs

status: corrected


column_label: PMID 26166069 Table 1, NbCathB row Abz-GIVRAK(Dnp); columns Km [uM], kcat [s^-1], and kcat/Km [mM^-1 s^-1]: 0.8 +/- 0.3 uM, 0.10 +/- 0.01 s^-1, and 116 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=0.1 normalized_unit=s^-1; Km normalized_value=0.0008 normalized_unit=mM; kcat_over_km normalized_value=116 normalized_unit=s^-1*mM^-1.

row_label: NbCathB; Abz-GIVRAK(Dnp)


column_label: PMID 26166069 Table 1, NbCathB row Z-Arg-Arg-MCA; columns Km [uM], kcat [s^-1], and kcat/Km [mM^-1 s^-1]: 99 +/- 7 uM, 11 +/- 1 s^-1, and 111 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=11 normalized_unit=s^-1; Km normalized_value=0.099 normalized_unit=mM; kcat_over_km normalized_value=111 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1, NbCathB, Z-Arg-Arg-MCA: Km 99 +/- 7 uM; kcat 11 +/- 1 s^-1; kcat/Km 111 mM^-1 s^-1.

row_label: NbCathB; Z-Arg-Arg-MCA


column_label: PMID 26166069 Table 1, NbCathB row Z-Phe-Arg-MCA; columns Km [uM], kcat [s^-1], and kcat/Km [mM^-1 s^-1]: 48 +/- 4 uM, 4.7 +/- 2.3 s^-1, and 98 mM^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=4.7 normalized_unit=s^-1; Km normalized_value=0.048 normalized_unit=mM; kcat_over_km normalized_value=98 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1, NbCathB, Z-Phe-Arg-MCA: Km 48 +/- 4 uM; kcat 4.7 +/- 2.3 s^-1; kcat/Km 98 mM^-1 s^-1.

row_label: NbCathB; Z-Phe-Arg-MCA


organism: Homo sapiens


substrate_name: Z-Arg-Arg-p-nitroanilide

substrate: Z-Arg-Arg-p-nitroanilide


organism: Meretrix meretrix


organism: Oryctolagus cuniculus


substrate_name: gelatin

substrate: gelatin


assay_conditions_summary: pH 6; 298.15 K; buffer 0.4 M sodium potassium phosphate

proof_lines: pH 6.0, 25°C, wild-type enzyme in presence of heparin

proof_lines: wild type enzyme, in 0.4 M sodium potassium phosphate buffer (pH 6.0) containing 8 mM dithiothreitol and 4 mM EDTA, at 37°C


proof_lines: pH 6.0, 25°C, mutant H110A in presence of heparin


proof_lines: pH 6.0, 25°C, mutant H111A in presence of heparin


substrate_name: Z-Arg-Arg-AMC

proof_lines: pH 4.6, temperature not specified in the publication

proof_lines: pH 7.2, temperature not specified in the publication

substrate: Z-Arg-Arg-AMC


substrate_name: Z-Nle-Lys-Arg-AMC

substrate: Z-Nle-Lys-Arg-AMC


substrate_name: Z-Phe-Arg-AMC

substrate: Z-Phe-Arg-AMC


sequence_variant_note: Mutation signature S115A/Q255T could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature S115A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Bos taurus

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


organism: Ficus carica

proof_lines: enzyme immobilized on carboxymethyl chitosan 200, pH 7.5, 37°C

proof_lines: enzyme immobilized on carboxymethyl chitosan 350, pH 7.5, 37°C

proof_lines: enzyme immobilized on carboxymethyl chitosan 600, pH 7.5, 37°C


organism: Cyprinus carpio


organism: Ficus sp.

substrate_name: p-nitrophenyl N-acetylglycinate

proof_lines:
ficin II
ficin III

substrate: p-nitrophenyl N-acetylglycinate


substrate_name: benzoyl-DL-Arg-p-nitroanilide

proof_lines:
ficin II
pH 6.36, 23.2% v/v CH3CN, ficin II
pH 3.91

substrate: benzoyl-DL-Arg-p-nitroanilide


enzyme_display_name: cathepsin S

enzyme: cathepsin S


enzyme_display_name: picornain 3C

organism: Hepatovirus A

proof_lines: pH and temperature not specified in the publication

enzyme: picornain 3C


enzyme_display_name: cancer procoagulant

enzyme: cancer procoagulant


organism: Rhinovirus B14

substrate_name: MBP-LEVLFQ-C

substrate: MBP-LEVLFQ-C


substrate_name: MBP-LEVLFQ-Q

substrate: MBP-LEVLFQ-Q


organism: Platyrrhini

substrate_name: Unknown

assay_conditions_summary: pH 5

substrate: Unknown


organism: Avihepatovirus A


enzyme_display_name: Stem bromelain

organism: Ananas comosus

substrate_name: Tosyl-L-Lys methyl ester

enzyme: Stem bromelain

substrate: Tosyl-L-Lys methyl ester


substrate_name: benzoyl-L-Arg methyl ester

substrate: benzoyl-L-Arg methyl ester


substrate_name: tosyl-L-Lys ethyl ester

substrate: tosyl-L-Lys ethyl ester


organism: Enterovirus A71


organism: Norwalk virus


organism: Coxsackievirus B3

substrate_name: Dabcyl-KEALFQGPPQFE-Edans; H2O

substrate: Dabcyl-KEALFQGPPQFE-Edans; H2O


organism: SARS coronavirus

substrate_name: Dabcyl-KTSAVLQSGFRKME-Edans; H2O

column_label: Results text immediately below Table 2; TG-0204998 row/series and SARS-CoV 3CLpro Ki column

raw_value_unit_evidence: Results text: Ki values of TG-0203770, TG-0204998, TG-0205221, and TG-0205486 against SARS-CoV 3CLpro were 0.058, 0.038, 0.054, and 0.099 uM, respectively

row_label: TG-0204998 against SARS-CoV 3CLpro

table_label: Results text and Table 2

substrate: Dabcyl-KTSAVLQSGFRKME-Edans; H2O


organism: Gallus gallus


organism: Southampton virus

proof_lines: pH 8.5, temperature not specified in the publication


organism: tobacco etch virus

substrate_name: TENLYFQSGTRR

proof_lines:
at pH 8.0 and 4°C
at pH 8.0 and 30°C

substrate: TENLYFQSGTRR


organism: Sapelovirus A

substrate_name: Ac-RHSVGATLEALFQGPPVYREIKIS-NH2; H2O

substrate: Ac-RHSVGATLEALFQGPPVYREIKIS-NH2; H2O


enzyme_display_name: picornain 2A

enzyme: picornain 2A


organism: Human rhinovirus 2

substrate_name: TRPIITTA-p-nitroanilide; H2O

substrate: TRPIITTA-p-nitroanilide; H2O


organism: Bos taurus

proof_lines:
pH 6.5, 25°C
pH 5.5, 30°C
pH 5.0, room temperature


organism: Canis lupus familiaris

proof_lines:
pH 5.0, room temperature
pH 5.0


organism: Rattus norvegicus


organism: Saimiri boliviensis


substrate_name: Dabcyl-ASFMNQSKVRRFE-Edans; H2O

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

substrate: Dabcyl-ASFMNQSKVRRFE-Edans; H2O


substrate_name: H2O; Dabcyl-KTSAVLQSGFRKME-Edans

column_label: Fig. 1B caption/body; metric labels kcat and Km for the Dabcyl-KTSAVLQSGFRKME-Edans substrate

row_label: CVB3 3Cpro with fluorogenic substrate Dabcyl-KTSAVLQSGFRKME-Edans

table_label: Fig. 1B caption/body

substrate: H2O; Dabcyl-KTSAVLQSGFRKME-Edans


enzyme_display_name: Genome polyprotein

organism: Poliovirus type 1 (strain Mahoney)

substrate_name: ATP

assay_conditions_summary: cofactor ATP

enzyme: Genome polyprotein

substrate: ATP


enzyme_display_name: glycyl endopeptidase

organism: Carica papaya

proof_lines: kcat is 22 sec(-1) with Boc-Ala-Ala-Gly-NHPhNO(2) as substrate (PubMed:2404797). kcat is 5 sec(-1) with Boc-Ala-Ala-Gly-NHMec as substrate (PubMed:2404797). kcat is 0.08 sec(-1) with Boc-Ala-Ala-Ala-NHMec as substrate (PubMed:2404797).

source_databases_merged: sabio_rk brenda uniprot

enzyme: glycyl endopeptidase


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature R48A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature E44A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 6.5; 310.15 K; buffer 0.1 M citrate

proof_lines: in 0.1 M citrate buffer, pH 5.5 containing 4 mM dithiothreitol, at 37°C


sequence_variant_note: Mutation signature ΔG119 could not be applied safely because the resolved sequence does not match the expected reference residue(s).

mutation_type: deletion


proof_lines: mutant with replaced residues 94-177 and introduction of residues 174-180 of cathepsin L,, pH 5.5, 25°C


proof_lines:
wild-type, pH 5.5, 25°C
wild-type enzyme


sequence_variant_note: Mutation signature Y118A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant with replaced residues 94-177 and introduction of residues 174-180 of cathepsin L plus mutation Y118A, pH 5.5, 25°C


organism: Mus musculus

proof_lines: excellent selectivity and activity for cathepsin S over the other cathepsin family members L, K and B

proof_lines: CatS activity in RAW264.7 cells or peritoneal macrophages from C57Bl/6 or LDLr-/-mice is completely repressed


organism: Aichivirus A


organism: Coxsackievirus

substrate_name: Dabcyl-KTLEALFQGPPVYE-Edans; H2O

substrate: Dabcyl-KTLEALFQGPPVYE-Edans; H2O


organism: Enterovirus A71


organism: coxsackievirus


organism: Coxsackievirus B3

substrate_name: Dabcyl-KTSAVLQSGFRKME-Edans

substrate: Dabcyl-KTSAVLQSGFRKME-Edans


organism: enterovirus


organism: Enterovirus B


organism: Enterovirus D

substrate_name: H2O; Ac-RHSVGATLEALFQGPPVYREIKIS-NH2

substrate: H2O; Ac-RHSVGATLEALFQGPPVYREIKIS-NH2


organism: Erbovirus A

substrate_name: Ac-AKDGGIFAQSRDRHYLVGTV-NH2; H2O

substrate: Ac-AKDGGIFAQSRDRHYLVGTV-NH2; H2O


organism: Hepatitis A virus

substrate_name: Dabcyl-GLRTQSND(Edans)G; H2O

substrate: Dabcyl-GLRTQSND(Edans)G; H2O


organism: Human rhinovirus


organism: Enterovirus C

proof_lines: in 50 mM Tris-HCl, at pH 8.0, in the absence of sodium citrate

proof_lines: in D2O, in the absence of sodium citrate

proof_lines: in 50 mM Tris-HCl, at pH 8.0, in the presence of 1 M sodium citrate


enzyme_display_name: transmembrane protease serine 2

enzyme: transmembrane protease serine 2


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

column_label: Table 2: Cleavage efficiencies of fluorogenic peptide substrates Table 2, peptide row 'P11' (NMA-IAALFQGPPK(DNP)FR); column 'K_m (uM)' = 75; column 'k_cat (min^-1)' = 0.16; column 'k_cat/K_m (mM^-1 min^-1)' = 2.13.

normalized_value_unit_evidence: kcat: printed cell 0.16 min^-1 converts to 0.0026666666666666666 s^-1, and the exported value is 0.0027; km: printed cell 75 uM converts to 0.075 mM, and the exported value is 0.075; kcat_over_km: printed cell 2.13 mM^-1 min^-1 converts to 0.0355 s^-1 mM^-1, and the exported value is 0.036000000000000004.

raw_value_unit_evidence: Table 2, peptide row 'P11' (NMA-IAALFQGPPK(DNP)FR): K_m (uM) = 75; k_cat (min^-1) = 0.16; k_cat/K_m (mM^-1 min^-1) = 2.13.


column_label: Table 2: Cleavage efficiencies of fluorogenic peptide substrates Table 2, peptide row 'P05' (NMA-RQAVTQGFPTELK-DNP); column 'K_m (uM)' = 92.4; column 'k_cat (min^-1)' = 0.2; column 'k_cat/K_m (mM^-1 min^-1)' = 2.2.

normalized_value_unit_evidence: kcat: printed cell 0.2 min^-1 converts to 0.0033333333333333335 s^-1, and the exported value is 0.003; km: printed cell 92.4 uM converts to 0.09240000000000001 mM, and the exported value is 0.0924; kcat_over_km: printed cell 2.2 mM^-1 min^-1 converts to 0.03666666666666667 s^-1 mM^-1, and the exported value is 0.03246753246753247.

raw_value_unit_evidence: Table 2, peptide row 'P05' (NMA-RQAVTQGFPTELK-DNP): K_m (uM) = 92.4; k_cat (min^-1) = 0.2; k_cat/K_m (mM^-1 min^-1) = 2.2.


column_label: Table 2: Cleavage efficiencies of fluorogenic peptide substrates Table 2, peptide row 'P04' (NMA-TSAVLQSGFRK(DNP)M); column 'K_m (uM)' = 75; column 'k_cat (min^-1)' = 0.02; column 'k_cat/K_m (mM^-1 min^-1)' = 0.27.

normalized_value_unit_evidence: kcat: printed cell 0.02 min^-1 converts to 0.0003333333333333333 s^-1, and the exported value is 0.0003; km: printed cell 75 uM converts to 0.075 mM, and the exported value is 0.075; kcat_over_km: printed cell 0.27 mM^-1 min^-1 converts to 0.0045000000000000005 s^-1 mM^-1, and the exported value is 0.004. The publisher serves this kcat cell as the literal string '0. 02' with a stray space inside the numeral The paper's own two other P04 cells settle the numeral: 0.02 min^-1 over 75 uM is 0.267 mM^-1 min^-1, which reproduces the printed P04 efficiency cell 0.27 at the two significant figures that column carries.

raw_value_unit_evidence: Table 2, peptide row 'P04' (NMA-TSAVLQSGFRK(DNP)M): K_m (uM) = 75; k_cat (min^-1) = 0.02; k_cat/K_m (mM^-1 min^-1) = 0.27.


substrate_name: Dabcyl-IEALFQGPPKFRE-Edans

column_label: Table 2: Cleavage efficiencies of fluorogenic peptide substrates Table 2, peptide row 'P10' (Dabcyl-IEALFQGPPKFRE-Edans); column 'K_m (uM)' = 63.2; column 'k_cat (min^-1)' = 0.17; column 'k_cat/K_m (mM^-1 min^-1)' = 2.69.

normalized_value_unit_evidence: kcat: printed cell 0.17 min^-1 converts to 0.0028333333333333335 s^-1, and the exported value is 0.0028; km: printed cell 63.2 uM converts to 0.0632 mM, and the exported value is 0.0632; kcat_over_km: printed cell 2.69 mM^-1 min^-1 converts to 0.04483333333333333 s^-1 mM^-1, and the exported value is 0.044303797468354424.

raw_value_unit_evidence: Table 2, peptide row 'P10' (Dabcyl-IEALFQGPPKFRE-Edans): K_m (uM) = 63.2; k_cat (min^-1) = 0.17; k_cat/K_m (mM^-1 min^-1) = 2.69.

substrate: Dabcyl-IEALFQGPPKFRE-Edans


substrate_name: Dabcyl-RTATVQGPSLDFKE-Edans

substrate: Dabcyl-RTATVQGPSLDFKE-Edans


organism: Human rhinovirus sp.

substrate_name: TRPIITTA-p-nitroanilide

proof_lines:
human rhinovirus
human rhinovirus type 2

substrate: TRPIITTA-p-nitroanilide


substrate_name: SLEVLFQGPVRR

substrate: SLEVLFQGPVRR


proof_lines:
24°C, pH 8.0
at pH 8.0 and 37°C
pH 8.0, 23°C


organism: Rattus norvegicus


organism: Enterovirus D68

substrate_name: Unknown

substrate: Unknown


organism: Homo sapiens


enzyme_display_name: cruzipain

organism: Unknown

enzyme: cruzipain


organism: Oryctolagus cuniculus


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


enzyme_display_name: staphopain

enzyme: staphopain


enzyme_display_name: separase

enzyme: separase


enzyme_display_name: V-cath endopeptidase

enzyme: V-cath endopeptidase


organism: ancestral Carnivora reconstruction


enzyme_display_name: SARS coronavirus main proteinase

organism: SARS coronavirus

substrate_name: MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2; H2O

enzyme: SARS coronavirus main proteinase

substrate: MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2; H2O


substrate_name: SITSAVLQSGFRKMA

substrate: SITSAVLQSGFRKMA


proof_lines:
at pH 7.0 and pH 7.5
pH 7.5
pH 7.5, 25°C


enzyme_display_name: calicivirin

organism: Norwalk virus

enzyme: calicivirin


organism: Middle East respiratory syndrome-related coronavirus


substrate_name: H2O; MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2

substrate: H2O; MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2


organism: Tylonycteris bat coronavirus HKU4


organism: Pipistrellus bat coronavirus HKU5


organism: Southampton virus


organism: Feline infectious peritonitis virus


substrate_name: H2O; Dabcyl-KTSAVLQSGFRKM-Edans

proof_lines: The kinetic parameters are studied for the 3C-like proteinase domain.

substrate: H2O; Dabcyl-KTSAVLQSGFRKM-Edans


enzyme_display_name: Replicase polyprotein 1ab

organism: Severe acute respiratory syndrome coronavirus

substrate_name: peptide TSAVLQSGFRK-NH(2)

enzyme: Replicase polyprotein 1ab

substrate: peptide TSAVLQSGFRK-NH(2)


substrate_name: Dabcyl-KTSAVLQSGFRKM-Edans; H2O

substrate: Dabcyl-KTSAVLQSGFRKM-Edans; H2O


substrate_name: H-TSAVLQSGFRK-NH2; H2O

substrate: H-TSAVLQSGFRK-NH2; H2O


substrate_name: SAVLQMGFRK

substrate: SAVLQMGFRK


substrate_name: Apaf-1-Caspase-9 cleaved complex; Caspase-3


substrate_name: Caspase-9 cleaved; Caspase-3

substrate: Caspase-9 cleaved; Caspase-3


substrate_name: Caspase-3; Caspase-9

substrate: Caspase-3; Caspase-9


organism: Avian infectious bronchitis virus


organism: Human coronavirus 229E

substrate_name: VSYGSTLQAGLRKMA; H2O

substrate: VSYGSTLQAGLRKMA; H2O


organism: Human coronavirus HKU1


organism: Human coronavirus NL63


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

assay_conditions_summary: pH 7.6; 303.15 K; buffer phosphate


sequence_variant_note: Mutation signature T126S/M298R could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Severe acute respiratory syndrome-related coronavirus

substrate_name: Ser-Ala-Val-Leu-Gln-Met-Gly-Phe-Arg-Lys

proof_lines:
wild-type protein
wild-type enzyme
wild-type, pH 7.3, 37°C

substrate: Ser-Ala-Val-Leu-Gln-Met-Gly-Phe-Arg-Lys


proof_lines:
T25G mutant protein
mutant enzyme T25G, at 37°C


organism: Homo sapiens


proof_lines:
mutant enzyme DELTA(297-306)
mutant enzyme DELTA(298-306)
mutant enzyme DELTA(299-306)


proof_lines:
mutant enzyme R298A
mutant enzyme S123a/R298A
R298A mutant protein


proof_lines:
mutant enzyme R298L
R298L mutant protein


proof_lines: enzyme mutant R188I, pH and temperature not specified in the publication


substrate_name: Dabcyl-KTSAVLQSGFRKME-EDANS

proof_lines: wild type enzyme, in 10 mM sodium phosphate, 10 mM sodium chloride, 1 mM EDTA, 1 mM TCEP, pH 7.4, at 25°C

substrate: Dabcyl-KTSAVLQSGFRKME-EDANS


proof_lines: mutant enzyme N28A, in 10 mM sodium phosphate, 10 mM sodium chloride, 1 mM EDTA, 1 mM TCEP, pH 7.4, at 25°C


proof_lines:
pH 7.5
pH 6.5
caspase-9 holoenzyme


enzyme_display_name: peptidase 1 (mite)

organism: Dermatophagoides pteronyssinus

proof_lines: Der p 1 purified from Dermatophagoides pteronyssinus

enzyme: peptidase 1 (mite)


substrate_name: Thr-Ser-Ala-Val-Leu-Gln-p-nitroanilide

substrate: Thr-Ser-Ala-Val-Leu-Gln-p-nitroanilide


assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM Tris-HCl

proof_lines: in the absence of sodium sulfate, pH 7.5 in 50 mM Tris-HCl buffer with 1 mM dithiothreitol, at 25°C

proof_lines: rate of hydrolysis measured by change in absorbance at 496 nm

proof_lines: in the presence of 1 M sodium sulfate, pH 7.5 in 50 mM Tris-HCl buffer with 1 mM dithiothreitol, at 25°C


enzyme_display_name: UniProt P03367

organism: Human immunodeficiency virus 1

substrate_name: KARVLAEAMS

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

enzyme: UniProt P03367

substrate: KARVLAEAMS


enzyme_display_name: renin

organism: Sus scrofa

enzyme: renin


enzyme_display_name: rhizopuspepsin

organism: Rhizomucor miehei

substrate_name: Abz-LSFMAIQ-EDDnp

enzyme: rhizopuspepsin

substrate: Abz-LSFMAIQ-EDDnp


organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40)

substrate_name: Z-His-Phe-Phe-OEt

proof_lines: kcat is 1.65 sec(-1) with Z-His-Phe-Phe-OEt as substrate, 0.35 sec(-1) with Z-Ala-Ala-Phe-Phe-OPy4Pr as substrate, 13 sec(-1) with bovine trypsinogen as substrate and 1.14 sec(-1) with bovine chymotrysinogen A as substrate.

substrate: Z-His-Phe-Phe-OEt


enzyme_display_name: HIV-1 retropepsin

organism: Human immunodeficiency virus

unit: Mswedgeone

enzyme: HIV-1 retropepsin


enzyme_display_name: aspergillopepsin I

organism: Aspergillus fumigatus

substrate_name: hemoglobin

enzyme: aspergillopepsin I

substrate: hemoglobin


enzyme_display_name: penicillopepsin

organism: Penicillium janthinellum

substrate_name: Trypsinogen; H2O

enzyme: penicillopepsin

substrate: Trypsinogen; H2O


organism: Rattus norvegicus

substrate_name: angiotensinogen

proof_lines:
isoenzyme R-III
isoenzyme R-II
isoenzyme R-I

substrate: angiotensinogen


enzyme_display_name: candidapepsin

organism: Candida albicans

substrate_name: Lys-Pro-Ala-Arg-Phe-Nph-Arg-Leu

proof_lines:
pH 3.25, isoenzyme Sap2p
isoenzyme Sap2p

enzyme: candidapepsin

substrate: Lys-Pro-Ala-Arg-Phe-Nph-Arg-Leu


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature V82A to reconstruct the assayed variant sequence.

proof_lines:
pH 5.0, mutant V82A
mutant V82A
mutant enzyme V82A


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature M46I with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: pH 4.7, 37°C, recombinant V6 mutant M46I

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature G73S with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature A71V with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


substrate_name: PARVLAEAMR

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature V82T to reconstruct the assayed variant sequence.

substrate: PARVLAEAMR


organism: Aspergillus pseudoglaucus

substrate_name: equine myoglobin

proof_lines: kcat is 0.05 min(-1) with equine myoglobin as substrate and 0.0646 min(-1) with bovine hemoglobin as substrate.

substrate: equine myoglobin


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature T291V with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature T219G with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines:
pH 5.0, 25°C, mutant T219G
pH 5.0, 37°C, mutant T219G


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature T291S with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature T291G with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature T291A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature T219V with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines:
pH 5.0, 25°C, mutant T219V
pH 5.0, 25°C, and mutant T219V
pH 5.0, 37°C, mutant T219V


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature T219A with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines:
pH 5.0, 25°C, mutant T219A
pH 5.0, 37°C, mutant T219A


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature T219S with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines:
pH 5.0, 25°C, mutant T219S
pH 5.0, 25°C, and mutant T219S
pH 5.0, 37°C, mutant T219S


enzyme_display_name: endothiapepsin

organism: Cryphonectria parasitica

assay_conditions_summary: pH 4.6; buffer 0.1 M acetate

proof_lines: in 0.1 M acetate buffer, pH 4.6, containing 0.01% (v/v) Tween 20, temperature not specified in the publication

proof_lines: at pH 4.6, temperature not specified in the publication

enzyme: endothiapepsin


enzyme_display_name: mucorpepsin

proof_lines:
pH 6.5, 45°C
Mucor miehei

enzyme: mucorpepsin


enzyme_display_name: saccharopepsin

organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K31M to reconstruct the assayed variant sequence.

enzyme: saccharopepsin


enzyme_display_name: Pro-opiomelanocortin converting enzyme

organism: Bos taurus

substrate_name: beta-Lipotropin

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

proof_lines: human substrate, cleavage at Lys37-Lys38

proof_lines: human substrate, cleavage at Lys57-Arg58

enzyme: Pro-opiomelanocortin converting enzyme

substrate: beta-Lipotropin


substrate_name: VSQNYPIVQ

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V82E to reconstruct the assayed variant sequence.

substrate: VSQNYPIVQ


sequence_variant_note: Mutation signature V82A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature D22L with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: pH 4.7, 37°C, D22L inhibitor and synthetic peptide form 24 inhibitor

proof_lines: pH 3.1, 37°C, chimera inhibitor, D22L inhibitor, synthetic peptide form 5 inhibitor, and synthetic peptide 10-NH2 inhibitor, pH 4.7, 37°C, synthetic peptide form 15 inhibitor


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

proof_lines: pH 3.1, 37°C, K7mutant inhibitor and synthetic peptide form 2 inhibitor, pH 4.7, synthetic peptide form 9 inhibitor and synthetic peptide 10-NH2 inhibitor


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature T222A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


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

proof_lines:
wild type enzyme, pH 4.7
pH 3.1, 37°C, wild-type inhibitor


sequence_variant_note: Mutation signature T287A/P288G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature A213I with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


proof_lines: pH 4.7, 37°C, synthetic peptide form 4 inhibitor and synthetic peptide form 9-NH2 inhibitor


substrate_name: VVQNYPIVQ

sequence_variant_note: Mutation signature V32I/I47V/V82I could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: VVQNYPIVQ


column_label: PMID 22238126 Table I, row (5) HIV-1 MA/CA VVQNY-PIVQ, protease column PR1, metric columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1)

raw_value_unit_evidence: Table I row (5) HIV-1 MA/CA VVQNY-PIVQ, protease PR1: Km 0.19 mM; kcat 0.16 s^-1; kcat/Km printed 0.8 mM^-1 s^-1

row_label: (5) HIV-1 MA/CA VVQNY-PIVQ

table_label: Table I Kinetic Parameters Obtained for Oligopeptide Substrates


enzyme_display_name: UniProt P00797

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

source_databases_merged: skid uniprot

enzyme: UniProt P00797


substrate_name: angiotensinogen (in presence of membrane-bound ATP6AP2)


substrate_name: IPFAAAQQRK

substrate: IPFAAAQQRK


column_label: PMID 22238126 Table I, row (2) HIV-2 p2/NC IPFAA-AQQRK, protease column PR1 footnote a, metric columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1); table footnote a states data taken from Reference 35

raw_value_unit_evidence: Table I row (2) HIV-2 p2/NC IPFAA-AQQRK, protease PR1 footnote a: Km 0.28 mM; kcat 0.3 s^-1; kcat/Km printed 1.1 mM^-1 s^-1

row_label: (2) HIV-2 p2/NC IPFAA-AQQRK


substrate_name: KARLMAEALK

substrate: KARLMAEALK


column_label: PMID 22238126 Table I, row (1) HIV-2 CA/p2 KARLM-AEALK, protease column PR1 footnote a, metric columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1); table footnote a states data taken from Reference 35

raw_value_unit_evidence: Table I row (1) HIV-2 CA/p2 KARLM-AEALK, protease PR1 footnote a: Km 0.13 mM; kcat 0.3 s^-1; kcat/Km printed 2.3 mM^-1 s^-1

row_label: (1) HIV-2 CA/p2 KARLM-AEALK


substrate_name: VLQNYPIVQ

substrate: VLQNYPIVQ


column_label: PMID 22238126 Table I, row (6) HIV-1 MA/CA VLQNY-PIVQ, protease column PR1 footnote c, metric columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1); table footnote c states data taken from Reference 48

raw_value_unit_evidence: Table I row (6) HIV-1 MA/CA VLQNY-PIVQ, protease PR1 footnote c: Km 0.40 mM; kcat 0.06 s^-1; kcat/Km printed 0.2 mM^-1 s^-1

row_label: (6) HIV-1 MA/CA VLQNY-PIVQ


substrate_name: VSQLYPIVQ

substrate: VSQLYPIVQ


column_label: PMID 22238126 Table I, row (4) HIV-1 MA/CA VSQLY-PIVQ, protease column PR1 footnote b, metric columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1); table footnote b states data taken from Reference 13

raw_value_unit_evidence: Table I row (4) HIV-1 MA/CA VSQLY-PIVQ, protease PR1 footnote b: Km 0.12 mM; kcat 0.4 s^-1; kcat/Km printed 3.3 mM^-1 s^-1

row_label: (4) HIV-1 MA/CA VSQLY-PIVQ


substrate_name: VSQVYPIVQ

substrate: VSQVYPIVQ


column_label: PMID 22238126 Table I, row (3) HIV-1 MA/CA VSQVY-PIVQ, protease column PR1, metric columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1)

raw_value_unit_evidence: Table I row (3) HIV-1 MA/CA VSQVY-PIVQ, protease PR1: Km 0.24 mM; kcat 2.6 s^-1; kcat/Km printed 10.8 mM^-1 s^-1

row_label: (3) HIV-1 MA/CA VSQVY-PIVQ


proof_lines:
HIV-1 protease precursor
autoprocessing reaction
mature PR


substrate_name: Arg-Pro-Gly-Asn-Phe-Leu-Gln-Ser-Arg-Pro

column_label: Table 3. HIV-1 protease-catalyzed hydrolysis of oligopeptides representing r-preNC cleavage sites; row/segment p1-p6; RPGNF*LQSRP; column/metric Km (mM), kcat (s-1), and kcat/Km (mM-1 s-1)

raw_value_unit_evidence: Table 3 reports Km 1.20 mM, kcat 0.98 s-1, and kcat/Km 0.80 mM-1 s-1 for p1-p6 peptide RPGNF*LQSRP.

row_label: p1-p6; RPGNF*LQSRP

substrate: Arg-Pro-Gly-Asn-Phe-Leu-Gln-Ser-Arg-Pro


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

proof_lines:
mutant I50V, pH 5.6, 26°C
pH 5.0, 25°C, mutant I50V
I50V, pH 5.5


proof_lines: pH 4.7, 37°C, recombinant V6 mutant I54V


proof_lines:
mutant G48V, pH 5.6, 26°C
pH 5.0, 37°C, mutant enzyme G48V


proof_lines: 37°C, pH 4.7, HIV-1 subtype B protease D30N/N88D

proof_lines: 37°C, pH 4.7, HIV-1 subtype B protease mutant D30N/N88D


proof_lines: 37°C, pH 4.7, HIV-1 subtype B protease mutant D30M/L90M

proof_lines: 37°C, pH 4.7, HIV-1 subtype B protease mutant 0.03 D30M/L90M


proof_lines: 37°C, pH 4.7, HIV-1 subtype B protease D30N/L90M


proof_lines: 37°C, pH 4.7, HIV-1 subtype B protease mutant N88D


proof_lines: 37°C, pH 4.7, HIV-1 subtype B protease mutant L90M


proof_lines: 37°C, pH 4.7, HIV-1 subtype B protease mutant D30N

proof_lines: 37°C, pH 4.7, HIV-1 subtype C protease mutant D30N


proof_lines: 37°C, pH 4.7, HIV-1 subtype B protease N88D/L90M


substrate_name: REYDQILIKVS

assay_conditions_summary: pH 5.5; 303.15 K; buffer 0.5 M potassium phosphate

proof_lines: wild type enzyme, in 0.5 M potassium phosphate buffer, pH 5.6, containing 10% (v/v) glycerol, 2 mM EDTA, 10 mM dithiothreitol, 4 M NaCl, at 37°C

substrate: REYDQILIKVS


proof_lines: pH 5.5, 30°C, mutant enzyme Q7K/L33I/L63I


substrate_name: DTVLEEMS

substrate: DTVLEEMS


substrate_name: TATIMMQRGN

substrate: TATIMMQRGN


substrate_name: PAFVLAEAMR

proof_lines:
mutant enzyme G48V/L90M
pH 5.0, 37°C, mutant enzyme G48V/L90M

substrate: PAFVLAEAMR


proof_lines:
mutant enzyme I84V
pH 5.0, mutant I84V
I84V, pH 5.5


substrate_name: Unknown


proof_lines: mutant enzyme L10I/L63P/A71V/G73S/I84V/L90M, in 0.1 M sodium acetate, 1 M sodium chloride, 1 mM EDTA, 1 mM dithiothreitol, 2% (v/v) DMSO, and 1 mg/ml bovine serum albumin, at pH 4.7 and 22°C


organism: Aspergillus oryzae

substrate_name: chymotrypsinogen

substrate: chymotrypsinogen


substrate_name: Trypsinogen

substrate: Trypsinogen


proof_lines: pH 4.7, 37°C, recombinant V6 mutant M46I/I84V

substrate: Unknown


proof_lines: pH 4.7, 37°C, recombinant V6 mutant M46I/I54V/I84V


proof_lines: pH 4.7, 37°C, recombinant V6 mutant I54V/I84V


proof_lines: 37°C, pH 4.7, mutant enzyme D30N/L63PA71V/L90M


proof_lines: pH 5.0, 25°C, wild-type pencillopepsin JT-2 and mutant T219A

proof_lines: pH 5.0, 25°C, wild-type Pencillopepsin JT-2


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


organism: Aspergillus niger

substrate_name: Benzyloxycarbonyl-Lys-Ala-Ala-Ala

proof_lines:
pH 3.2, Aspergillus niger
pH 4.5, Aspergillus niger
Aspergillus niger

substrate: Benzyloxycarbonyl-Lys-Ala-Ala-Ala


organism: Rhizopus sp.

substrate_name: KPILF p-nitrophenylalanine-RL

proof_lines:
pH 3.0, 37°C
pH 3.0, 37°C, chimeric enzyme
pH 7.4, 37°C

substrate: KPILF p-nitrophenylalanine-RL


substrate_name: KPLEF p-nitrophenylalanine-RL

proof_lines: pH 3.0, 37°C, wild-type and chimeric enzyme

substrate: KPLEF p-nitrophenylalanine-RL


substrate_name: AETFYVDGAA

proof_lines: pH 5.6, 37°C, autolysis reistant and truncated enzyme form PR-(5-99) with mutation Q7K/L33I/L63I/C67A/C95A

proof_lines: pH 5.6, 37°C, autolysis resistant enzyme form PR with the mutations Q7K/L33I/L63I/C67A/C95A

proof_lines: pH 5.0, 25°C, truncated version PR-(5-99) from mutant enzyme Q7K/L33I/L63I/C67A/C95A

substrate: AETFYVDGAA


substrate_name: KARVLAEAMS

substrate: KARVLAEAMS


enzyme_display_name: aspergillopepsin II

organism: Aspergillus niger var. macrosporus

enzyme: aspergillopepsin II


substrate_name: RGFFHTPRA

substrate: RGFFHTPRA


organism: Human immunodeficiency virus 1

proof_lines: pH 5.0, 25°C, mutant enzyme C67A/C95A and mutant enzyme C95A


organism: Candida parapsilosis

assay_conditions_summary: pH 3.75; 310.15 K; buffer 150 mM sodium citrate

proof_lines: isoform Sapp2p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C

proof_lines: isoform Sapp1p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C

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


substrate_name: angiotensinogen

substrate: angiotensinogen


proof_lines: pH 5.0, 25°C, mutant enzyme Q7K/R8Q/L33I/L63I/C67A/C95A


proof_lines: mutant enzyme PRV82A, at pH 5.6 and 37°C


proof_lines: mutant I50V/A71V, pH not specified in the publication, temperature not specified in the publication


substrate_name: VVQNYPIVQ

assay_conditions_summary: pH 5.6; 310.15 K; buffer 0.5 M potassium phosphate

proof_lines: mutant enzyme V32I/I47V/V82I, in 0.5 M potassium phosphate buffer, pH 5.6, containing 10% (v/v) glycerol, 2 mM EDTA, 10 mM dithiothreitol, 4 M NaCl, at 37°C

proof_lines: mutant enzyme V32I/I47V/V82I, at pH 4.0 and 28°C

proof_lines: mutant enzyme V32I/I47V/V82I, at pH 5.8 and 28°C

substrate: VVQNYPIVQ


proof_lines:
pH 5.2, 2.0 M NaCl
pH 4.5, 0.1 M NaCl
37°C, pH 4.7, HIV-1 subtype C protease


organism: Penicillium sp.


organism: Rhizopus microsporus

substrate_name: Abz-KLRQSKQ-EDDnp

substrate: Abz-KLRQSKQ-EDDnp


organism: Rhizopus microsporus var. chinensis


organism: Human immunodeficiency virus


enzyme_display_name: interstitial collagenase

substrate_name: bovine type I collagen

enzyme: interstitial collagenase

substrate: bovine type I collagen


enzyme_display_name: microbial collagenase

organism: Bacillus cereus

substrate_name: gelatin

enzyme: microbial collagenase

substrate: gelatin


enzyme_display_name: Collagenase ColH

organism: Hathewaya histolytica

proof_lines: kcat is 0.11 sec(-1) on Pz peptide with whole enzyme (PubMed:10217773). kcat is 15.9 sec(-1) on FALGPA with a catalytic fragment (residues 41-717) (PubMed:18937627).

enzyme: Collagenase ColH


organism: Homo sapiens


proof_lines:
30°C, MMP-1(DELTA243-450)
mutant enzyme DELTA243-450


substrate_name: [alpha1(II)769-783] fluorogenic triple-helical peptide-4

proof_lines:
wild-type enzyme
pH 7.5, 25°C, wild-type substrate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E200A with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


substrate_name: human type II collagen

assay_conditions_summary: pH 7.5; 310.15 K; buffer pH not specified in the publication

proof_lines: pH not specified in the publication, 37°C, MMP-1: 2-protonated

proof_lines: pH not specified in the publication, 37°C, MMP-1: 1-protonated

substrate: human type II collagen


organism: Rattus norvegicus


substrate_name: GPLGIAGQ

substrate: GPLGIAGQ


enzyme_display_name: Collagenase ColQ1

organism: Bacillus cereus (strain Q1)

proof_lines: kcat is 7.7 sec(-1) with gelatin as substrate (PubMed:33603127). kcat is 2.1 sec(-1) with native collagen from rat tail as substrate (PubMed:33603127).

enzyme: Collagenase ColQ1


organism: Clostridium histolyticum

substrate_name: Peptide; H2O

proof_lines: isoform ColH with N-terminal His6-tag, pH 7.5, 25°C

substrate: Peptide; H2O


enzyme_display_name: Collagenase ColT

organism: Clostridium tetani (strain Massachusetts / E88)

substrate_name: furylacryloyl-Leu-Gly-Pro-Ala (FALGPA)

proof_lines: kcat is 7.24/sec, using a catalytic fragment (residues 53-727) on an artificial substrate.

enzyme: Collagenase ColT

substrate: furylacryloyl-Leu-Gly-Pro-Ala (FALGPA)


substrate_name: furylacryloyl-Leu-Gly-Pro-Ala

substrate: furylacryloyl-Leu-Gly-Pro-Ala


proof_lines: isoform ColG with N-terminal His6-tag, pH 7.5, 25°C

proof_lines: kcat is 0.11/sec, using a catalytic fragment (119-790) on an artificial substrate.


enzyme_display_name: UniProt P08473

substrate_name: Substance P

enzyme: UniProt P08473

substrate: Substance P


substrate_name: Arg-vasopressin

substrate: Arg-vasopressin


substrate_name: bradykinin

substrate: bradykinin


substrate_name: Neurokinin A

substrate: Neurokinin A


substrate_name: neurokinin B

substrate: neurokinin B


substrate_name: gamma-endorphin

substrate: gamma-endorphin


substrate_name: alpha-endorphin

substrate: alpha-endorphin


substrate_name: neurotensin

substrate: neurotensin


substrate_name: glucagon

substrate: glucagon


substrate_name: nociceptin

substrate: nociceptin


substrate_name: somatostatin 14

substrate: somatostatin 14


substrate_name: somatostatin 28

substrate: somatostatin 28


organism: Vibrio parahaemolyticus


enzyme_display_name: stromelysin 1

organism: Escherichia coli

assay_conditions_summary: pH 6

proof_lines: pH 6.0, 25°C, catalytic domain (residues 83-247)

enzyme: stromelysin 1


enzyme_display_name: UniProt P14756

organism: Pseudomonas aeruginosa

substrate_name: tetraalanine

enzyme: UniProt P14756

substrate: tetraalanine


enzyme_display_name: procollagen C-endopeptidase

organism: Gallus gallus

substrate_name: Procollagen type I

enzyme: procollagen C-endopeptidase

substrate: Procollagen type I


enzyme_display_name: astacin

organism: Mus musculus

enzyme: astacin


enzyme_display_name: thimet oligopeptidase

organism: Geobacillus sp.

proof_lines: pH and temperature not specified in the publication

enzyme: thimet oligopeptidase


enzyme_display_name: pseudolysin

organism: Vibrio cholerae serotype O1

enzyme: pseudolysin


enzyme_display_name: matrilysin

organism: Mammalia

substrate_name: entactin

enzyme: matrilysin

substrate: entactin


enzyme_display_name: IgA-specific metalloendopeptidase

organism: Unknown

substrate_name: Unknown

enzyme: IgA-specific metalloendopeptidase

substrate: Unknown


organism: Steinernema carpocapsae

substrate_name: azocasein

proof_lines:
pH 7.5, 37°C
pH 7.5, 37°C, Vmax: 0.281 microM/min

substrate: azocasein


proof_lines: pH and temperature not specified in the publication, recombinant enzyme, in presence of PCPE-1 NTR domain

proof_lines: pH and temperature not specified in the publication, recombinant enzyme, in presence of PCPE-1 CUB1/CUB2 domains


enzyme_display_name: peptidyl-Lys metalloendopeptidase

organism: Armillaria mellea

substrate_name: SAQKRVS

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

enzyme: peptidyl-Lys metalloendopeptidase

substrate: SAQKRVS


organism: Astacus fluviatilis

substrate_name: Dansyl-Pro-Lys-Arg-Ala-Pro-Trp-Val; H2O

proof_lines: analyzed by tryptophan fluorescence changes between enzyme-substrate complex and enzyme plus product

substrate: Dansyl-Pro-Lys-Arg-Ala-Pro-Trp-Val; H2O


enzyme_display_name: stromelysin 2

organism: Homo sapiens

proof_lines:
pH 7.5, 30°C
catalytic enzyme domain, pH 7.0, 37°C

enzyme: stromelysin 2


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +8, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature Y219S with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.


enzyme_display_name: neprilysin

organism: Lactococcus lactis

substrate_name: Met-enkephalin amide

enzyme: neprilysin

substrate: Met-enkephalin amide


substrate_name: adrenocorticotropic hormone

substrate: adrenocorticotropic hormone


substrate_name: Vasoactive intestinal peptide

substrate: Vasoactive intestinal peptide


substrate_name: bradykinin

substrate: bradykinin


substrate_name: Met-enkephalin

substrate: Met-enkephalin


substrate_name: Leu-enkephalinamide

substrate: Leu-enkephalinamide


substrate_name: Leu-enkephalin

substrate: Leu-enkephalin


substrate_name: beta-endorphin

substrate: beta-endorphin


substrate_name: Substance P

substrate: Substance P


substrate_name: alpha-neoendorphin

substrate: alpha-neoendorphin


substrate_name: angiotensin I

substrate: angiotensin I


enzyme_display_name: saccharolysin

organism: Saccharomyces cerevisiae

substrate_name: Pz-Pro-Leu-Gly-Pro-D-Arg

enzyme: saccharolysin

substrate: Pz-Pro-Leu-Gly-Pro-D-Arg


substrate_name: Dnp-Pro-Leu-Gly-Pro-Trp-D-Lys

substrate: Dnp-Pro-Leu-Gly-Pro-Trp-D-Lys


organism: Grifola frondosa


enzyme_display_name: vibriolysin

organism: Vibrio proteolyticus

enzyme: vibriolysin


substrate_name: dialanine-phenylalanylalaninamide

substrate: dialanine-phenylalanylalaninamide


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y219A with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y219C with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.


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


substrate_name: dansyl-PLALWAR

proof_lines:
pH 7.5, 25°C, wild-type
pH 7.5, 25°C, wild-type enzyme

substrate: dansyl-PLALWAR


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E198C with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E198Q with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.


enzyme_display_name: gelatinase A

proof_lines: pH 7.5, 37°C, GaCDfn, with fibronectin-like insert

proof_lines: pH 7.5, 37°C, GaCD, without fibronectin-like insert

enzyme: gelatinase A


proof_lines:
pH 7.5, 25°C, with 0.05 mM heparin
pH 7.5, 25°C
pH 7.5, 25°C, without heparin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E198D with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E198A with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.


substrate_name: peptide B74

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E412D with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

substrate: peptide B74


substrate_name: vitronectin of MW 65000 and 75000

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

substrate: vitronectin of MW 65000 and 75000


substrate_name: Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln

substrate: Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln


enzyme_display_name: UniProt P14735

substrate_name: Insulin

enzyme: UniProt P14735

substrate: Insulin


substrate_name: Dansyl-Pro-Lys-Arg-Ala-Pro-Trp-Val

sequence_variant_note: Mutation signature E103A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: astacin E103A pro-astacin

substrate: Dansyl-Pro-Lys-Arg-Ala-Pro-Trp-Val


sequence_variant_note: Mutation signature E103Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: astacin E103Q pro-astacin


proof_lines:
astacin
pro-astacin
autoproteolytic activation


enzyme_display_name: serralysin

substrate_name: Unknown

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

enzyme: serralysin

substrate: Unknown


organism: Astacus astacus


substrate_name: tetraalanine

substrate: tetraalanine


substrate_name: azocasein

substrate: azocasein


substrate_name: furylacryloyl-Gly-Leu-Gly

proof_lines: pH 7.2, temperature not specified in the publication

substrate: furylacryloyl-Gly-Leu-Gly


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: benzoyl-Phe-Ala-Arg

column_label: The abstract reports benzoyl-Phe-Ala-Arg with Km = 284 microM.

raw_value_unit_evidence: Km raw_value=284 microM raw_unit=microM

row_label: Prose segment: benzoyl-Phe-Ala-Arg Km

table_label: PubMed PMID 8416959 abstract

substrate: benzoyl-Phe-Ala-Arg


substrate_name: furylacryloyl-Ala-Arg

column_label: The abstract reports fa-Ala-Arg with Km = 516 microM.

raw_value_unit_evidence: Km raw_value=516 microM raw_unit=microM

row_label: Prose segment: fa-Ala-Arg Km

substrate: furylacryloyl-Ala-Arg


substrate_name: furylacryloyl-Ala-Lys

column_label: The abstract reports fa-Ala-Lys with Km = 962 microM.

raw_value_unit_evidence: Km raw_value=962 microM raw_unit=microM

row_label: Prose segment: fa-Ala-Lys Km

substrate: furylacryloyl-Ala-Lys


enzyme_display_name: dactylysin

enzyme: dactylysin


enzyme_display_name: mitochondrial processing peptidase

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

enzyme: mitochondrial processing peptidase


enzyme_display_name: Carboxypeptidase A1

substrate_name: 3-(2-furyl)acryloyl-Phe-Phe (at 25 degrees Celsius)

proof_lines: kcat is 76.6 sec(-1) with 3-(2-furyl)acryloyl-Phe-Phe as substrate (at 25 degrees Celsius) (PubMed:20385563). kcat is 81.3 sec(-1) with 3-(2-furyl)acryloyl-Phe-Trp as substrate (at 25 degrees Celsius) (PubMed:20385563). kcat is 34 sec(-1) w

enzyme: Carboxypeptidase A1


enzyme_display_name: carboxypeptidase B

organism: Helicoverpa zea

proof_lines: kcat is 45.7 sec(-1) for benzoyl-glycyl-lysine (Bz-Gly-Lys). kcat is 15.3 sec(-1) for N-(4-furylacryloyl)-Ala-Lys (FAAK).

enzyme: carboxypeptidase B


enzyme_display_name: choriolysin H

organism: Paralichthys olivaceus

substrate_name: casein

enzyme: choriolysin H

substrate: casein


enzyme_display_name: insulysin

organism: Triticum aestivum

enzyme: insulysin


enzyme_display_name: fibrolase

organism: Bacillus cereus

enzyme: fibrolase


organism: Patiria pectinifera


enzyme_display_name: UniProt P39042

organism: Streptomyces sp.

substrate_name: benzoyl-Gly-thiolactate

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

enzyme: UniProt P39042

substrate: benzoyl-Gly-thiolactate


enzyme_display_name: UniProt P15555

enzyme: UniProt P15555


enzyme_display_name: carboxypeptidase C

enzyme: carboxypeptidase C


organism: Monascus purpureus

substrate_name: benzyloxycarbonyl-Tyr-Glu

substrate: benzyloxycarbonyl-Tyr-Glu


enzyme_display_name: carboxypeptidase A

organism: Bos taurus

substrate_name: H2O; Carbobenzoxy-Gly-Gly-Val

enzyme: carboxypeptidase A

substrate: H2O; Carbobenzoxy-Gly-Gly-Val


organism: Helicoverpa armigera

substrate_name: Carbobenzoxy-Gly-Gly-Phe; H2O

substrate: Carbobenzoxy-Gly-Gly-Phe; H2O


organism: Xylaria curta


organism: Homo sapiens

substrate_name: ochratoxin A

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R124K with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

substrate: ochratoxin A


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


enzyme_display_name: bontoxilysin

organism: Clostridium botulinum

substrate_name: VAMP1; H2O

sequence_source: UniProt accession lookup (P10844)

column_label: Table 3 columns V (uM/min), Km (uM), and Apparent rate (min^-1); row LC/B.

raw_value_unit_evidence: Table 3 row LC/B reports V = 0.22 (0.01) uM/min, Km = 8.2 (0.8) uM, apparent rate = 46 min^-1.

row_label: LC/B

table_label: Table 3. Lambert-Omega Function parameters (see Fig. 6C)

enzyme: bontoxilysin

substrate: VAMP1; H2O


sequence_source: UniProt accession lookup (P0DPK1)

column_label: Table 3 columns V (uM/min), Km (uM), and Apparent rate (min^-1); row LC/X.

raw_value_unit_evidence: Table 3 row LC/X reports V = 0.65 (0.03) uM/min, Km = 4.3 (0.3) uM, apparent rate = 271 min^-1.

row_label: LC/X


enzyme_display_name: endothelin-converting enzyme 1

substrate_name: Peptide E

sequence_source: UniProt accession lookup (P0DPD6)

enzyme: endothelin-converting enzyme 1

substrate: Peptide E


substrate_name: Big endothelin-1

substrate: Big endothelin-1


substrate_name: Bradykinin

column_label: Table III row Bradykinin, ECE-2 columns for Km, kcat, and kcat/Km provide the primary metric evidence.

normalized_value_unit_evidence: Paper Km is 0.0274 mM and explicit kcat/Km normalizes to 210 s^-1*mM^-1; targets are Km 0.027 mM and kcat_over_km 214.8148148148148 s^-1*mM^-1.

raw_value_unit_evidence: Table III row Bradykinin: ECE-2 Km 0.0274 mM-normalized from uM column; kcat 5.8 s^-1; kcat/Km 2.1 x 10^5 M^-1 s^-1.

row_label: Bradykinin

table_label: Table III. Steady-state kinetic constants for hydrolysis of bioactive peptides by ECE-2

substrate: Bradykinin


substrate_name: Dynorphin B (1-13)

column_label: Table III row Dynorphin B, ECE-2 columns for Km, kcat, and kcat/Km provide the primary metric evidence.

normalized_value_unit_evidence: Paper Km is 0.0484 mM and explicit kcat/Km normalizes to 180 s^-1*mM^-1; targets are Km 0.048 mM and kcat_over_km 183.33333333333334 s^-1*mM^-1.

raw_value_unit_evidence: Table III row Dynorphin B: ECE-2 Km 0.0484 mM-normalized from uM column; kcat 8.8 s^-1; kcat/Km 1.8 x 10^5 M^-1 s^-1.

row_label: Dynorphin B

substrate: Dynorphin B (1-13)


enzyme_display_name: Botulinum neurotoxin type A

substrate_name: purified SNAP25 with isolated botulinum neurotoxin A light chain

enzyme: Botulinum neurotoxin type A


enzyme_display_name: Botulinum neurotoxin type E

substrate_name: purified SNAP25 with botulinum neurotoxin E light chain

proof_lines: kcat is 257 min(-1) with botulinum neurotoxin E light chain.

enzyme: Botulinum neurotoxin type E


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E262Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E262D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L175A/R177A to reconstruct the assayed variant sequence.

proof_lines: pH 7.6, 37°C, recombinant mutant L175A/R177A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E257A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W319A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E315A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I52A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y322A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


enzyme_display_name: Botulinum neurotoxin type B

substrate_name: over-expressed human VAMP1

proof_lines: kcat is 3.96, 4.68 and 3.50 sec(-1) for over-expressed human VAMP1, VAMP2 and VAMP3 respectively.

enzyme: Botulinum neurotoxin type B

substrate: over-expressed human VAMP1


substrate_name: vesicle-associated membrane protein-2

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H132Q with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H132Q, in 10 mM Tris-HCl (pH 7.6) and 20 mM NaCl, at 37°C

substrate: vesicle-associated membrane protein-2


enzyme_display_name: tentoxilysin

organism: Clostridium tetani

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

enzyme: tentoxilysin


substrate_name: Big endothelin-1; H2O

substrate: Big endothelin-1; H2O


substrate_name: H2O; Big endothelin-1

substrate: H2O; Big endothelin-1


organism: Sus scrofa


organism: Agkistrodon contortrix

substrate_name: low molecular weight kininogen

substrate: low molecular weight kininogen


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature H269A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature I115A/C134A to reconstruct the assayed variant sequence.

proof_lines: pH 7.6, 37°C, recombinant mutants I115A and C134A


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature E257K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature F194A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature R177A/E257A to reconstruct the assayed variant sequence.

proof_lines: pH 7.6, 37°C, recombinant mutants R177A and E257A


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature C134A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W315D with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W315D, in 10 mM Tris-HCl (pH 7.6) and 20 mM NaCl, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F50D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F50D, in 10 mM Tris-HCl (pH 7.6) and 20 mM NaCl, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W315A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W315A, in 10 mM Tris-HCl (pH 7.6) and 20 mM NaCl, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I191D with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I191D, in 10 mM Tris-HCl (pH 7.6) and 20 mM NaCl, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y168D/L200D with inferred residue-numbering offset +33 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y168D/L200D, in 10 mM Tris-HCl (pH 7.6) and 20 mM NaCl, at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I151D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I151D, in 10 mM Tris-HCl (pH 7.6) and 20 mM NaCl, at 37°C


enzyme_display_name: Endothelin-converting enzyme 2

substrate_name: big ET-1

column_label: Table III row Big ET-1, ECE-2 Km column, reports 0.4 +/- 0.03 uM.

row_label: Big ET-1

table_label: Table III. Steady-state kinetic constants for hydrolysis of bioactive peptides by ECE-2, PMID 12560336

enzyme: Endothelin-converting enzyme 2

substrate: big ET-1


substrate_name: peptide E

column_label: Table III row Peptide E, ECE-2 Km column, reports 1.4 +/- 0.17 uM.

raw_value_unit_evidence: Peptide E ECE-2 Km 1.4 +/- 0.17 uM

row_label: Peptide E

substrate: peptide E


substrate_name: bradykinin

column_label: Table III row Bradykinin, ECE-2 Km column, reports 27.4 +/- 3.0 uM.

normalized_value_unit_evidence: Km 27.4 uM = 0.0274 mM, matching target 0.0274 mM.

raw_value_unit_evidence: Table III row Bradykinin, ECE-2 Km column, raw value 27.4 +/- 3.0 uM.

substrate: bradykinin


substrate_name: dynorphin B

column_label: Table III row Dynorphin B, ECE-2 Km column, reports 48.4 +/- 4.1 uM.

raw_value_unit_evidence: Dynorphin B ECE-2 Km 48.4 +/- 4.1 uM

substrate: dynorphin B


substrate_name: Carbobenzoxy-Gly-Gly-Leu

column_label: Official JBC PDF Table II row Cbz-Gly-Gly-Leu under Bovine CPA columns kcat, Km, and (kcat/Km) x 10^5.

normalized_value_unit_evidence: kcat normalized_value=63.4 s^-1; Km normalized_value=1.18 mM; kcat/Km table-normalized=54 s^-1*mM^-1; sheet-normalized=53.728813559322035 s^-1*mM^-1 from same row kcat/Km cells

raw_value_unit_evidence: kcat raw_value=63.4 s^-1; Km raw_value=1180 plus/minus 93 uM; kcat/Km raw_value=0.54 x 10^5 M^-1 s^-1

row_label: Cbz-Gly-Gly-Leu / Bovine CPA

table_label: Table II, Kinetic constants for substrate hydrolysis by rat CPA1, rat CPA2, and bovine CPA

substrate: Carbobenzoxy-Gly-Gly-Leu


substrate_name: Carbobenzoxy-Gly-Gly-Phe

column_label: Official JBC PDF Table II row Cbz-Gly-Gly-Phe under Bovine CPA columns kcat, Km, and (kcat/Km) x 10^5.

normalized_value_unit_evidence: kcat normalized_value=131 s^-1; Km normalized_value=0.172 mM; kcat/Km table-normalized=762 s^-1*mM^-1; sheet-normalized=761.6279069767443 s^-1*mM^-1 from same row kcat/Km cells

raw_value_unit_evidence: kcat raw_value=131 s^-1; Km raw_value=172 plus/minus 12 uM; kcat/Km raw_value=7.62 x 10^5 M^-1 s^-1

row_label: Cbz-Gly-Gly-Phe / Bovine CPA

substrate: Carbobenzoxy-Gly-Gly-Phe


substrate_name: Carbobenzoxy-Gly-Phe

column_label: Official JBC PDF Table II row Cbz-Gly-Phe under Bovine CPA columns kcat, Km, and (kcat/Km) x 10^5.

normalized_value_unit_evidence: kcat normalized_value=41.7 s^-1; Km normalized_value=1.093 mM; kcat/Km table-normalized=38 s^-1*mM^-1; sheet-normalized=38.15187557182068 s^-1*mM^-1 from same row kcat/Km cells

raw_value_unit_evidence: kcat raw_value=41.7 s^-1; Km raw_value=1093 plus/minus 154 uM; kcat/Km raw_value=0.38 x 10^5 M^-1 s^-1

row_label: Cbz-Gly-Phe / Bovine CPA

substrate: Carbobenzoxy-Gly-Phe


enzyme_display_name: Botulinum neurotoxin type X

substrate_name: a human VAMP1 fragment (residues 34-87) construct

enzyme: Botulinum neurotoxin type X


enzyme_display_name: Botulinum neurotoxin type C

organism: Clostridium botulinum C phage

substrate_name: purified SNAP25 with isolated botulinum neurotoxin C light chain

proof_lines: kcat is 0.391 min(-1), for isolated botulinum neurotoxin C light chain.

enzyme: Botulinum neurotoxin type C


enzyme_display_name: Botulinum neurotoxin type D

organism: Clostridium botulinum D phage

proof_lines: kcat is 0.59, 146.60 and 113.41 sec(-1) for over-expressed human VAMP1, VAMP2 and VAMP3 respectively.

enzyme: Botulinum neurotoxin type D


enzyme_display_name: Botulinum neurotoxin type A2

organism: Clostridium botulinum (strain Kyoto / Type A2)

substrate_name: SNAP25 fragment (146-206) with isolated botulinum neurotoxin A2 light chain

proof_lines: kcat is 0.13 sec(-1), for botulinum neurotoxin A2 light chain.

enzyme: Botulinum neurotoxin type A2


enzyme_display_name: Botulinum neurotoxin type F

organism: Clostridium botulinum (strain Langeland / NCTC 10281 / Type F)

proof_lines: kcat is 16.12, 34.37 and 28.57 sec(-1) for over-expressed human VAMP1, VAMP2 and VAMP3 respectively.

enzyme: Botulinum neurotoxin type F


enzyme_display_name: jararhagin

organism: Bothrops jararaca

substrate_name: Abz-LVEALYQ-EDDnp

proof_lines:
catalytic domain of jararhagin
native jararhagin
deglycosylated jararhagin

enzyme: jararhagin

substrate: Abz-LVEALYQ-EDDnp


organism: Rattus norvegicus

column_label: Official JBC PDF Table II row Cbz-Gly-Gly-Leu under Rat CPA1 columns kcat, Km, and (kcat/Km) x 10^5.

normalized_value_unit_evidence: kcat normalized_value=199 s^-1; Km normalized_value=0.740 mM; kcat/Km table-normalized=270 s^-1*mM^-1; sheet-normalized=268.9189189189189 s^-1*mM^-1 from same row kcat/Km cells

raw_value_unit_evidence: kcat raw_value=199 s^-1; Km raw_value=740 plus/minus 43 uM; kcat/Km raw_value=2.7 x 10^5 M^-1 s^-1

row_label: Cbz-Gly-Gly-Leu / Rat CPA1


column_label: Official JBC PDF Table II row Cbz-Gly-Gly-Phe under Rat CPA1 columns kcat, Km, and (kcat/Km) x 10^5.

normalized_value_unit_evidence: kcat normalized_value=57.4 s^-1; Km normalized_value=0.0346 mM; kcat/Km table-normalized=1600 s^-1*mM^-1; sheet-normalized=1639.9999999999998 s^-1*mM^-1 from same row kcat/Km cells

raw_value_unit_evidence: kcat raw_value=57.4 s^-1; Km raw_value=34.6 plus/minus 5.6 uM; kcat/Km raw_value=16 x 10^5 M^-1 s^-1

row_label: Cbz-Gly-Gly-Phe / Rat CPA1


column_label: Official JBC PDF Table II row Cbz-Gly-Phe under Rat CPA1 columns kcat, Km, and (kcat/Km) x 10^5.

normalized_value_unit_evidence: kcat normalized_value=22.4 s^-1; Km normalized_value=0.0449 mM; kcat/Km table-normalized=500 s^-1*mM^-1; sheet-normalized=497.77777777777777 s^-1*mM^-1 from same row kcat/Km cells

raw_value_unit_evidence: kcat raw_value=22.4 s^-1; Km raw_value=44.9 plus/minus 2.6 uM; kcat/Km raw_value=5 x 10^5 M^-1 s^-1

row_label: Cbz-Gly-Phe / Rat CPA1


enzyme_display_name: beta-peptidyl aminopeptidase

organism: Sphingosinicella xenopeptidilytica

substrate_name: beta-homoAla-p-nitroanilide

proof_lines:
Sphingosinicella xenopeptidilytica
beta-peptidyl aminopeptidase
beta-peptides

enzyme: beta-peptidyl aminopeptidase

substrate: beta-homoAla-p-nitroanilide


substrate_name: beta-homoPhe-p-nitroanilide

substrate: beta-homoPhe-p-nitroanilide


enzyme_display_name: cytosol non-specific dipeptidase

substrate_name: L-Cysteinylglycine

enzyme: cytosol non-specific dipeptidase

substrate: L-Cysteinylglycine


enzyme_display_name: Cytosolic non-specific dipeptidase

substrate_name: L-cysteinylglycine (at pH 8.0 and in the presence of 50 uM manganese ions)

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

enzyme: Cytosolic non-specific dipeptidase


enzyme_display_name: Prolyl endopeptidase FAP

substrate_name: Ile-Pro (Dipeptidyl peptidase activity)

enzyme: Prolyl endopeptidase FAP

substrate: Ile-Pro (Dipeptidyl peptidase activity)


substrate_name: Phe-Pro (Dipeptidyl peptidase activity)

substrate: Phe-Pro (Dipeptidyl peptidase activity)


organism: Bacillus subtilis

substrate_name: Benzoyl-D-Ala-thioglycolate

substrate: Benzoyl-D-Ala-thioglycolate


substrate_name: Benzoyl-Gly-thioglycolate

substrate: Benzoyl-Gly-thioglycolate


organism: Actinomadura sp.


column_label: Table 1 columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1); row R39, substrate 4 (X = OMe), d(R).

row_label: R39; substrate 4 (X = OMe); d(R) enantiomer

table_label: Table 1: Steady state kinetics parameters for enzyme-catalyzed hydrolysis of 5 and of 1 and 4 (X = OMe) for comparison


organism: Nonomuraea sp.

substrate_name: acetyl-L-Lys-D-Ala-D-Ala

column_label: Primary article PDF page 4 / printed page 3206, Table 1; row Acetyl-L-Lys-D-Ala-D-Ala

normalized_value_unit_evidence: Per-metric normalized values and units are preserved in paper_metric_evidence.

raw_value_unit_evidence: Per-metric raw values and units are preserved in paper_metric_evidence; captured_primary_segment preserves the exact source transcription.

row_label: Acetyl-L-Lys-D-Ala-D-Ala

substrate: acetyl-L-Lys-D-Ala-D-Ala


substrate_name: D-Ala-D-Ala

column_label: Table 1, row D-Ala-D-Ala, columns kcat=8.3 s^-1, Km=20 mM, kcat/Km=0.415 mM^-1 s^-1; specific activity=19 U mg^-1 protein.

normalized_value_unit_evidence: kcat=8.3 s^-1; Km=20 mM; kcat/Km=0.415 s^-1 mM^-1. Expected 0.41500000000000004 is a serialization tail and numerically matches.

raw_value_unit_evidence: kcat raw_value=8.3 s^-1; Km raw_value=20 mM; kcat/Km raw_value=0.415 mM^-1 s^-1.

row_label: D-Ala-D-Ala

table_label: Primary article PDF page 4 / printed page 3206, Table 1

substrate: D-Ala-D-Ala


organism: Streptomyces sp.

column_label: Table 1 columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1); row R61, substrate 5, d(R).

normalized_value_unit_evidence: kcat 6.9 s^-1; Km 0.36 mM; kcat/Km 1.9 x 10^4 s^-1 M^-1 = 19 s^-1 mM^-1. Sheet ratio 19.1667 is kcat/Km from rounded kcat and Km.

row_label: R61; substrate 5; d(R) enantiomer


column_label: Table 1 columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 M^-1); row R61, substrate 4 (X = OMe), d(R).

normalized_value_unit_evidence: Actual source-table values are kcat 44 s^-1, Km 0.45 mM, and kcat/Km 98 s^-1 mM^-1; sheet has kcat 4.0 and kcat/Km 8.8889.

row_label: R61; substrate 4 (X = OMe); d(R) enantiomer


organism: Ochrobactrum anthropi

sequence_variant_note: Mutation signature N275R could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
Ochrobactrum anthropi
D-aminopeptidase
D,D-carboxypeptidase