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


enzyme_display_name: HIV-1 retropepsin

organism: Human immunodeficiency virus 1

source_db: brenda

verification_status: unverified

ki_display: Not reported

kcat_over_km_display: Not reported

source_license: CC BY 4.0

km_unit: mM

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

mutation_type: substitution

enzyme: HIV-1 retropepsin

status: unverified

source: brenda


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

mutation_signature: Unknown

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

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: VSQNYPIVQ

substrate: VSQNYPIVQ


substrate_name: PARVLAEAMR

substrate: PARVLAEAMR


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


km_display: Not reported


substrate_name: Unknown

kcat_display: Not reported

ki_unit: mM

substrate: 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


enzyme_display_name: aspergillopepsin I

organism: Aspergillus oryzae

substrate_name: chymotrypsinogen

enzyme: aspergillopepsin I

substrate: chymotrypsinogen


substrate_name: Trypsinogen

substrate: Trypsinogen


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


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


enzyme_display_name: penicillopepsin

organism: Penicillium janthinellum

protein_accession_database: UniProt

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

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

enzyme: penicillopepsin


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


enzyme_display_name: rhizopuspepsin

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

enzyme: rhizopuspepsin

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


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


enzyme_display_name: candidapepsin

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

enzyme: candidapepsin


enzyme_display_name: renin

organism: Bos taurus

substrate_name: angiotensinogen

enzyme: renin

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

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


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

source_db: uniprot

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).

data_origin: experimental

enzyme: Collagenase ColH

source: uniprot


organism: Homo sapiens


mutation_type: deletion

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

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

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

source_databases_merged: sabio_rk brenda uniprot

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.

source_databases_merged: brenda uniprot


enzyme_display_name: UniProt P08473

substrate_name: Substance P

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P08473

substrate: Substance P

source: skid


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

source_db: unknown

source_license: see source

enzyme: IgA-specific metalloendopeptidase

substrate: Unknown

source: 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

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


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


sequence_source: multiple

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

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

source_db: oed

kcat_over_km_origin: calculated

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

source: oed


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

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


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

verification_status: verified

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

status: verified


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

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

verification_status: corrected

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

status: corrected


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

enzyme: tentoxilysin


substrate_name: Big endothelin-1; H2O

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

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

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

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

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

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


substrate_name: Nalpha-Acetyl-L-Lys-D-Ala-D-Ala

substrate: Nalpha-Acetyl-L-Lys-D-Ala-D-Ala


enzyme_display_name: maltose-6'-phosphate glucosidase

organism: Clostridium acetobutylicum

substrate_name: maltose 6'-phosphate

assay_conditions_summary: pH 7; cofactor NAD+

column_label: PMID 14570887 Table III, Maltose-6'P row, MalH Km column = 1.95 mM.

raw_value_unit_evidence: Table III lists Maltose-6'P for MalH with Km = 1.95 and Vmax = 0.49; PagL is NDH.

row_label: Maltose-6'P / MalH

table_label: Table III. Substrate specificity and kinetic parameters of purified phospho-alpha-glucosidase(s): MalH and PagL

enzyme: maltose-6'-phosphate glucosidase

substrate: maltose 6'-phosphate


organism: Fusobacterium mortiferum

assay_conditions_summary: pH 7


enzyme_display_name: carboxypeptidase C

organism: Homo sapiens

enzyme: carboxypeptidase C


substrate_name: N-Benzoyl-L-tyrosine ethyl ester

substrate: N-Benzoyl-L-tyrosine ethyl ester


organism: Bacteroides fragilis

substrate_name: 4-nitrophenyl alpha-L-fucopyranoside

substrate: 4-nitrophenyl alpha-L-fucopyranoside


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

organism: Beta vulgaris

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


enzyme_display_name: oligosaccharide reducing-end xylanase

organism: Halalkalibacterium halodurans

substrate_name: D-xylose

proof_lines:
Rex glycosynthase
xylose
alpha-xylobiosyl fluoride

enzyme: oligosaccharide reducing-end xylanase

substrate: D-xylose


organism: Trichoderma reesei

substrate_name: beta-Glucan

substrate: beta-Glucan


organism: Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)

substrate_name: cellotetraose

substrate: cellotetraose


enzyme_display_name: beta-apiosyl-beta-glucosidase

organism: Viburnum furcatum

substrate_name: furcatin

column_label: Abstract reports the recombinant FH exhibited highest activity toward furcatin with Km value of 2.2 mm.

raw_value_unit_evidence: Km raw_value=2.2 mm raw_unit=mM

row_label: Recombinant furcatin hydrolase / furcatin

table_label: PubMed XML abstract PMID 14976214

enzyme: beta-apiosyl-beta-glucosidase

substrate: furcatin


enzyme_display_name: Trehalose-6-phosphate hydrolase

organism: Escherichia coli (strain K12)

column_label: Abstract states the enzyme hydrolyzes trehalose-6-phosphate with a Km of 6 mM.

raw_value_unit_evidence: Km raw_value=6 raw_unit=mM

row_label: Escherichia coli TreC trehalose-6-phosphate hydrolase with trehalose-6-phosphate

table_label: PubMed abstract PMID 8083158

enzyme: Trehalose-6-phosphate hydrolase


enzyme_display_name: Maltose-6'-phosphate glucosidase

organism: Bacillus subtilis (strain 168)

substrate_name: maltose-6'-phosphate (at pH 7.5 and 37 degrees Celsius)

enzyme: Maltose-6'-phosphate glucosidase


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

organism: Talaromyces purpureogenus

substrate_name: 4-nitrophenyl beta-D-cellobioside

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

assay_conditions_summary: pH 5

substrate: 4-nitrophenyl beta-D-cellobioside


organism: Rhizomucor pusillus

substrate_name: sialylglycopeptide

substrate: sialylglycopeptide


organism: Talaromyces funiculosus


enzyme_display_name: Lysoplasmalogenase

organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)

substrate_name: lysoplasmenylcholine

enzyme: Lysoplasmalogenase

substrate: lysoplasmenylcholine


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


enzyme_display_name: leukotriene-A4 hydrolase

organism: Mus musculus

assay_conditions_summary: pH 8

enzyme: leukotriene-A4 hydrolase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


enzyme_display_name: Leukotriene A-4 hydrolase

substrate_name: Pro-Gly-Pro

proof_lines:
proline-glycine-proline
leukotriene A-4 hydrolase
Homo sapiens

enzyme: Leukotriene A-4 hydrolase

substrate: Pro-Gly-Pro


substrate_name: leukotriene A4

proof_lines:
leukotriene A4 hydrolase
LTA4
L-alanine-p-nitroanilide

substrate: leukotriene A4


organism: Xenopus laevis

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

proof_lines:
pH 8.0, 22°C
Raw SKiD Env: Temp=22°C, pH=7.8

source_databases_merged: brenda skid


enzyme_display_name: microsomal epoxide hydrolase

organism: Heliothis virescens

substrate_name: juvenile hormone III

enzyme: microsomal epoxide hydrolase

substrate: juvenile hormone III


organism: Cavia porcellus

substrate_name: styrene oxide

proof_lines:
guinea pigs
styrenes
epoxide hydrase

substrate: styrene oxide


enzyme_display_name: Puromycin-sensitive aminopeptidase

organism: Caenorhabditis elegans

substrate_name: L-Leu-AMC

proof_lines:
PAM-1
puromycin-sensitive aminopeptidase
small neutral amino acids

enzyme: Puromycin-sensitive aminopeptidase

substrate: L-Leu-AMC


organism: Homo sapiens

substrate_name: Leukotriene A4

substrate: Leukotriene A4


enzyme_display_name: Cyclic dipeptide prenyltransferase

organism: Aspergillus fumigatus

substrate_name: L-tryptophan

column_label: Table 3 columns: CdpNPT Km [mM], kcat [s^-1], kcat/Km [mM^-1 s^-1], ratio kcat/Km; row: l-tryptophan.

normalized_value_unit_evidence: Km 0.83 mM; expected export Km is 0.38 mM, so the populated Km metric does not match.

raw_value_unit_evidence: Table 3 l-tryptophan row under CdpNPT reports Km 0.83 mM, kcat 0.005 s^-1, and kcat/Km 0.006 mM^-1 s^-1.

row_label: CdpNPT / l-tryptophan

table_label: ACS article Table 3: Km Values and Turnover Numbers of CdpNPT and FtmPT1

enzyme: Cyclic dipeptide prenyltransferase

substrate: L-tryptophan


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

substrate_name: dimethylallyl diphosphate (DMAPP)

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

substrate: dimethylallyl diphosphate (DMAPP)


enzyme_display_name: D-aminopeptidase

organism: Brucella anthropi

substrate_name: D-alanine amide (at 30 degrees Celsius)

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

enzyme: D-aminopeptidase

substrate: D-alanine amide (at 30 degrees Celsius)


enzyme_display_name: methionyl aminopeptidase

organism: Pyrococcus furiosus

substrate_name: Met-Gly-Met-Met

assay_conditions_summary: pH 7.5; buffer 25 mM HEPES

proof_lines: Pyrococcus furiosus methionine aminopeptidase assay

enzyme: methionyl aminopeptidase

substrate: Met-Gly-Met-Met


organism: Leishmania donovani


enzyme_display_name: Aspartyl aminopeptidase

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

substrate_name: angiotensin II

enzyme: Aspartyl aminopeptidase

substrate: angiotensin II


enzyme_display_name: D-stereospecific aminopeptidase

organism: Ochrobactrum anthropi

substrate_name: D-Alanine-p-nitroanilide

enzyme: D-stereospecific aminopeptidase

substrate: D-Alanine-p-nitroanilide


enzyme_display_name: aspartyl aminopeptidase

organism: Oryctolagus cuniculus

enzyme: aspartyl aminopeptidase


enzyme_display_name: Aspartyl aminopeptidase 4

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: angiotensin I

enzyme: Aspartyl aminopeptidase 4

substrate: angiotensin I


enzyme_display_name: cytosol nonspecific dipeptidase

organism: Lactobacillus helveticus

substrate_name: Pro-Leu

enzyme: cytosol nonspecific dipeptidase

substrate: Pro-Leu


enzyme_display_name: aminopeptidase S

organism: Streptomyces griseus

substrate_name: L-Valine-p-nitroanilide

enzyme: aminopeptidase S

substrate: L-Valine-p-nitroanilide


enzyme_display_name: Cytosolic non-specific dipeptidase

substrate_name: carnosine (at pH 9.5 and in the presence of 0.1 mM manganese ions)

enzyme: Cytosolic non-specific dipeptidase


enzyme_display_name: Tripeptidyl-peptidase sed2

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: Dipeptidase 1

substrate_name: imipenem

column_label: Kinetic analysis paragraph / Figure 4 label for imipenem, Km: 10.9 +/- 1.7 mM.

raw_value_unit_evidence: Text reports imipenem Vmax 44.5 +/- 5.9 umol/min/mg, Km 10.9 +/- 1.7 mM, and Ki 0.73 +/- 0.02 uM.

row_label: Imipenem hydrolysis by purified human renal dipeptidase

table_label: Kinetic analysis text / Figure 4

enzyme: Dipeptidase 1

substrate: imipenem


enzyme_display_name: tripeptidyl-peptidase II

organism: Mus musculus

substrate_name: L-Ala-L-Ala-L-Phe 4-nitroanilide

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E331Q to reconstruct the assayed variant sequence.

enzyme: tripeptidyl-peptidase II

substrate: L-Ala-L-Ala-L-Phe 4-nitroanilide


enzyme_display_name: dipeptidyl-peptidase IV

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y547F with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.

enzyme: dipeptidyl-peptidase IV


organism: Pseudoxanthomonas mexicana


enzyme_display_name: carboxypeptidase A

organism: Bos taurus

substrate_name: Carbobenzoxy-Gly-Gly-Val

enzyme: carboxypeptidase A

substrate: Carbobenzoxy-Gly-Gly-Val


enzyme_display_name: carboxypeptidase B

organism: Protopterus aethiopicus

substrate_name: hippuryl-L-Arg

sequence: EPTPRSFNGDKVFRV

wild_type_sequence: EPTPRSFNGDKVFRV

enzyme: carboxypeptidase B

substrate: hippuryl-L-Arg


enzyme_display_name: Prolyl endopeptidase FAP

substrate_name: Gly-Pro (Prolyl endopeptidase activity)

enzyme: Prolyl endopeptidase FAP

substrate: Gly-Pro (Prolyl endopeptidase activity)


enzyme_display_name: fibrolase

organism: Agkistrodon contortrix

substrate_name: Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg

enzyme: fibrolase

substrate: Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg


enzyme_display_name: Dipeptidyl aminopeptidase 4

substrate_name: Gly-Pro-pNA (at pH 8.0 and 37 degrees Celsius)

enzyme: Dipeptidyl aminopeptidase 4


organism: Homo sapiens

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

proof_lines: pH 7.4, mutant N229A and N281A, expressed in Hi5 cells


proof_lines: pH 7.4, mutant N219A, expressed in Hi5 cells

proof_lines: pH 7.4, mutant N219A, expressed in Sf9 cells


proof_lines: pH 7.4, mutant N229A and N685A, expressed in Hi5 cells


proof_lines: pH 7.4, mutant N85A and N219A, expressed in Sf9 cells


proof_lines: pH 7.4, mutant N92A, N150A, and N520A, expressed in Hi5 cells


proof_lines: pH 7.4, mutant N520A, expressed in Hi5 cells

proof_lines: pH 7.4, mutant N520A, expressed in Sf9 cells


proof_lines: pH 7.4, mutant N321A, expressed in Sf9 cells

proof_lines: pH 7.4, mutant N321A, expressed in Hi5 cells


proof_lines: pH 7.4, mutant enzyme N321A expressed in Sf9 cells


proof_lines: pH 7.4, mutant N229A, expressed in Sf9 cells

proof_lines: pH 7.4, mutant N229A, expressed in Hi5 cells


proof_lines: pH 7.4, mutant enzyme N229A expressed in Sf9 cells


proof_lines: pH 7.4, mutant enzyme N520A expressed in Sf9 cells


proof_lines: pH 7.4, mutant N281A, expressed in Sf9 cells

proof_lines: pH 7.4, mutant N281A, expressed in Hi5 cells


proof_lines: pH 7.4, mutant enzyme N281A expressed in Sf9 cells


proof_lines: pH 7.4, mutant N85A, expressed in Sf9 cells

proof_lines: pH 7.4, mutant N85A, expressed in Hi5 cells


proof_lines: pH 7.4, mutant enzyme N85A expressed in Sf9 cells


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

proof_lines: pH 7.4, wild-type enzyme expressed in Sf9 cells


proof_lines: pH 7.4, mutant enzyme N92A expressed in Sf9 cells


proof_lines: pH 7.4, mutant enzyme N150A expressed in Sf9 cells


proof_lines: pH 7.4, mutant enzyme N219A expressed in Sf9 cells


proof_lines: pH 7.4, mutant N685A, expressed in Sf9 cells

proof_lines: pH 7.4, mutant N685A, expressed in Hi5 cells


proof_lines: pH 7.4, mutant N92A, N150A, and N219A, expressed in Sf9 cells


proof_lines: pH 7.4, mutant enzyme N685A expressed in Sf9 cells


proof_lines: pH 7.4, mutant N92A, expressed in Hi5 cells

proof_lines: pH 7.4, mutant N92A, expressed in Sf9 cells


proof_lines: pH 7.4, mutant N321A and N520A, expressed in Hi5 cells


proof_lines: pH 7.4, mutant N150A, expressed in Hi5 cells

proof_lines: pH 7.4, mutant N150A, expressed in Sf9 cells


enzyme_display_name: bontoxilysin

organism: Clostridium botulinum

enzyme: bontoxilysin


substrate_name: D-Ala-Gly-Gly

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

substrate: D-Ala-Gly-Gly


substrate_name: D-alanine amide

substrate: D-alanine amide


substrate_name: D-Ala-Gly

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

substrate: D-Ala-Gly


substrate_name: D-Ala-D-Ala

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

substrate: D-Ala-D-Ala


substrate_name: D-2-Aminobutyric acid amide

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

substrate: D-2-Aminobutyric acid amide


substrate_name: glycine amide

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

substrate: glycine amide


substrate_name: D-Serine amide

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

substrate: D-Serine amide


substrate_name: D-threonine amide

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

substrate: D-threonine amide


substrate_name: vesicle-associated membrane protein-2

proof_lines: mutant enzyme F50D/I191D, in 10 mM Tris-HCl (pH 7.6) and 20 mM NaCl, at 37°C

substrate: vesicle-associated membrane protein-2


proof_lines: mutant enzyme R63E, in 10 mM Tris-HCl (pH 7.6) and 20 mM NaCl, at 37°C


proof_lines: mutant enzyme R372A, in 10 mM Tris-HCl (pH 7.6) and 20 mM NaCl, at 37°C


proof_lines: mutant enzyme F50A/I191A, in 10 mM Tris-HCl (pH 7.6) and 20 mM NaCl, at 37°C


proof_lines: mutant enzyme R63A, in 10 mM Tris-HCl (pH 7.6) and 20 mM NaCl, at 37°C


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


proof_lines: mutant enzyme R23D/H132A, in 10 mM Tris-HCl (pH 7.6) and 20 mM NaCl, at 37°C


proof_lines: mutant enzyme W44A/I152A/P154A, in 10 mM Tris-HCl (pH 7.6) and 20 mM NaCl, at 37°C


proof_lines: mutant enzyme P154D, in 10 mM Tris-HCl (pH 7.6) and 20 mM NaCl, at 37°C


proof_lines: pH 7.6, 37°C, recombinant mutant F194A/T220A


proof_lines: pH 7.6, 37°C, recombinant mutants K41A and V129A


organism: Escherichia coli K-12


proof_lines:
wild type enzyme
mutant wild type enzyme


substrate_name: Gly-Pro-p-nitroanilide

substrate: Gly-Pro-p-nitroanilide


enzyme_display_name: membrane dipeptidase

substrate_name: L-Val-Gly

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

enzyme: membrane dipeptidase

substrate: L-Val-Gly


substrate_name: L-Trp-Gly

substrate: L-Trp-Gly


substrate_name: L-Leu-Gly

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

substrate: L-Leu-Gly


substrate_name: L-Phe-Gly

substrate: L-Phe-Gly


substrate_name: Gly-L-Phe

substrate: Gly-L-Phe


substrate_name: Gly-L-Trp

substrate: Gly-L-Trp


substrate_name: Gly-L-Val

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

substrate: Gly-L-Val


substrate_name: Ser-Pro-p-nitroanilide

substrate: Ser-Pro-p-nitroanilide


substrate_name: Ala-Pro-p-nitroanilide

substrate: Ala-Pro-p-nitroanilide


substrate_name: Asp-Pro-p-nitroanilide

substrate: Asp-Pro-p-nitroanilide


substrate_name: Arg-Pro-p-nitroanilide

substrate: Arg-Pro-p-nitroanilide


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

organism: Trichoderma reesei

substrate_name: 4-nitrophenyl lactoside

substrate: 4-nitrophenyl lactoside


proof_lines: pH 5.0, 37°C, recombinant wild-type enzyme

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


substrate_name: cellotetraose

substrate: cellotetraose


proof_lines: pH 5, 27°C, Y247F mutant and D241C/D249C mutant


enzyme_display_name: tripeptidyl-peptidase I

enzyme: tripeptidyl-peptidase I


enzyme_display_name: carboxypeptidase C

organism: Saccharomyces cerevisiae

substrate_name: Benzyloxycarbonyl-Gly-Phe

enzyme: carboxypeptidase C

substrate: Benzyloxycarbonyl-Gly-Phe


proof_lines:
pH 6.5, 25°C, wild-type enzyme
wild-type enzyme
wild-type


substrate_name: Benzyloxycarbonyl-Phe-Leu

substrate: Benzyloxycarbonyl-Phe-Leu


substrate_name: Benzyloxycarbonyl-Gly-Leu

substrate: Benzyloxycarbonyl-Gly-Leu


enzyme_display_name: endo-alpha-N-acetylgalactosaminidase

organism: Streptococcus pneumoniae R6

enzyme: endo-alpha-N-acetylgalactosaminidase


mutation_signature: Δ1


proof_lines: pH 6.5, 37°C, DELTA1-39,DELTA1568-1767 deletion mutant


substrate_name: cellotriose

substrate: cellotriose


substrate_name: cellohexaose

substrate: cellohexaose


substrate_name: cellopentaose

substrate: cellopentaose


enzyme_display_name: D-stereospecific aminopeptidase

organism: Brucella anthropi

substrate_name: nitrocefin

proof_lines: mutant lacking residues 476-486, pH 8.0, 30°C

proof_lines: mutant lacking residues 476-486, pH 7.0, 30°C

enzyme: D-stereospecific aminopeptidase

substrate: nitrocefin


proof_lines: mutant lacking residues 476-486 plus domains DAP-BC, pH 8.0, 30°C


proof_lines: complex of domain DAP-A plus domains DAP-BC, pH 8.0, 30°C


substrate_name: synaptosome-associated protein SNAP-25

substrate: synaptosome-associated protein SNAP-25


proof_lines: 37°C, pH 7.4, mutant enzyme E158A/T159A/N160A


enzyme_display_name: methionyl aminopeptidase

substrate_name: Met-Ser

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

enzyme: methionyl aminopeptidase

substrate: Met-Ser


substrate_name: Met-Thr

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

substrate: Met-Thr


substrate_name: Met-Val

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

substrate: Met-Val


substrate_name: Met-Pro

substrate: Met-Pro


substrate_name: Met-Gly-Met-Met

substrate: Met-Gly-Met-Met


enzyme_display_name: Xaa-Pro dipeptidyl-peptidase

organism: Lactococcus lactis

enzyme: Xaa-Pro dipeptidyl-peptidase


substrate_name: Leu-Ala-Pro

substrate: Leu-Ala-Pro


substrate_name: His-Pro-Leu

substrate: His-Pro-Leu


substrate_name: His-Pro-Tyr

substrate: His-Pro-Tyr


substrate_name: Gly-Pro-Ala

substrate: Gly-Pro-Ala


organism: Rattus norvegicus

substrate_name: L-Leu-L-Leu-Gly

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

substrate: L-Leu-L-Leu-Gly


substrate_name: L-Leu-L-Leu-L-Leu

substrate: L-Leu-L-Leu-L-Leu


proof_lines:
pH 8.0, 37°C, microsomes
pH 8.0, 37°C


substrate_name: L-Ala-L-Ala-L-Ala

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

substrate: L-Ala-L-Ala-L-Ala


substrate_name: L-Ala-L-Pro-Gly

substrate: L-Ala-L-Pro-Gly


enzyme_display_name: asparaginase

organism: Pseudomonas chlororaphis subsp. aurantiaca

substrate_name: L-Gln

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

enzyme: asparaginase

substrate: L-Gln


substrate_name: L-Asn

substrate: L-Asn


organism: Brevibacillus borstelensis

substrate_name: L-asparagine

substrate: L-asparagine


enzyme_display_name: UniProt H0W0T5

organism: Cavia porcellus

enzyme: UniProt H0W0T5


enzyme_display_name: UniProt P00805

organism: Escherichia coli

substrate_name: L-glutamine

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

enzyme: UniProt P00805

substrate: L-glutamine


source_databases_merged: skid uniprot


enzyme_display_name: UniProt P50286

organism: Wolinella succinogenes

enzyme: UniProt P50286


organism: Thermococcus gammatolerans

substrate_name: L-Asparagine

substrate: L-Asparagine


substrate_name: D-Asparagine

substrate: D-Asparagine


substrate_name: D-Glutamine

substrate: D-Glutamine


enzyme_display_name: L-asparaginase 1

organism: Escherichia coli (strain K12)

enzyme: L-asparaginase 1


enzyme_display_name: UniProt Q7DKE4

organism: Rhodococcus sp. N-771

substrate_name: Propionamide

smiles: CCC(=O)N

enzyme: UniProt Q7DKE4

substrate: Propionamide


substrate_name: Acrylamide

smiles: C=CC(=O)N

substrate: Acrylamide


substrate_name: acetamide

smiles: CC(=O)N

substrate: acetamide


substrate_name: Benzamide

substrate: Benzamide


enzyme_display_name: dipeptidyl-peptidase IV

enzyme: dipeptidyl-peptidase IV


substrate_name: Tyr-Pro-Phe-Val-Glu-Pro-Ile

substrate: Tyr-Pro-Phe-Val-Glu-Pro-Ile


substrate_name: Tyr-Pro-Phe

substrate: Tyr-Pro-Phe


substrate_name: Tyr-Pro-Phe-Pro

substrate: Tyr-Pro-Phe-Pro


substrate_name: Tyr-Pro-Phe-Pro-Gly

substrate: Tyr-Pro-Phe-Pro-Gly


organism: Thermochaetoides thermophila

substrate_name: Beta-D-glucan

substrate: Beta-D-glucan


substrate_name: Met-Ala-Ser

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

substrate: Met-Ala-Ser


substrate_name: Met-Gly-Met-Met

substrate: Met-Gly-Met-Met


mutation_signature: Δ2


mutation_signature: truncated enzyme truncated enzyme

mutation_type: truncation


enzyme_display_name: carboxypeptidase A

organism: Homo sapiens

substrate_name: neurotensin

column_label: Table 2: Kinetic constants for the hydrolysis of biological peptides by CPA4; row Neurotensin; columns kcat, Km, and kcat/Km; Neurotensin: kcat = 0.240 s^-1; Km = 0.329 uM; kcat/Km = 43.8 uM^-1 min^-1.

row_label: Neurotensin; kcat/Km/Km columns

enzyme: carboxypeptidase A

substrate: neurotensin


substrate_name: Met-enkephalin-L-Arg-L-Phe

proof_lines: in 50 mM Tris-HCl, 100 mM NaCl, pH 7.5, at 37°C

substrate: Met-enkephalin-L-Arg-L-Phe


substrate_name: Leu-enkephalin

column_label: Table 2: Kinetic constants for the hydrolysis of biological peptides by CPA4; row Leu-enkephalin; columns kcat, Km, and kcat/Km; Leu-enkephalin: kcat = 2.33 s^-1; Km = 165 uM; kcat/Km = 0.85 uM^-1 min^-1.

normalized_value_unit_evidence: Km 165 uM = 0.165 mM; kcat/Km normalized from components = 14.121212121212121 s^-1 mM^-1.

row_label: Leu-enkephalin; kcat/Km/Km columns

substrate: Leu-enkephalin


substrate_name: Met-enkephalin

column_label: Table 2: Kinetic constants for the hydrolysis of biological peptides by CPA4; row Met-enkephalin; columns kcat, Km, and kcat/Km; Met-enkephalin: kcat = 3.43 s^-1; Km = 550 uM; kcat/Km = 0.374 uM^-1 min^-1.

normalized_value_unit_evidence: Km 550 uM = 0.55 mM; kcat/Km normalized from components = 6.236363636363636 s^-1 mM^-1.

row_label: Met-enkephalin; kcat/Km/Km columns

substrate: Met-enkephalin


substrate_name: angiotensin I

column_label: Table 2: Kinetic constants for the hydrolysis of biological peptides by CPA4; row Angiotensin I; columns kcat, Km, and kcat/Km; Angiotensin I: kcat = 8.23 s^-1; Km = 227 uM; kcat/Km = 2.18 uM^-1 min^-1.

normalized_value_unit_evidence: Km 227 uM = 0.227 mM; kcat/Km normalized from components = 36.25550660792952 s^-1 mM^-1.

row_label: Angiotensin I; kcat/Km/Km columns

substrate: angiotensin I


enzyme_display_name: cytosol nonspecific dipeptidase

substrate_name: Leu-Leu

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

enzyme: cytosol nonspecific dipeptidase

substrate: Leu-Leu


substrate_name: L-Leu-L-Phe

substrate: L-Leu-L-Phe


substrate_name: Met-Leu

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

substrate: Met-Leu


substrate_name: Gly-L-Lys

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

substrate: Gly-L-Lys


enzyme_display_name: arylformamidase

organism: Gallus gallus

enzyme: arylformamidase


enzyme_display_name: UniProt Q04066

substrate_name: N-formyl-L-kynurenine

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7.4

enzyme: UniProt Q04066

substrate: N-formyl-L-kynurenine


enzyme_display_name: UniProt P07941

organism: Kluyvera cryocrescens

substrate_name: penicillin G

enzyme: UniProt P07941

substrate: penicillin G


enzyme_display_name: UniProt Q03154

substrate_name: N-acetyl-L-histidine

enzyme: UniProt Q03154

substrate: N-acetyl-L-histidine


substrate_name: N-acetyl-L-phenylalanine

substrate: N-acetyl-L-phenylalanine


substrate_name: N-acetyl-L-valine

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

substrate: N-acetyl-L-valine


substrate_name: N-butanoyl-L-methionine

smiles: CCCC(=O)NC(CCSC)C(=O)O

substrate: N-butanoyl-L-methionine


substrate_name: N-acetyl-L-leucine

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

substrate: N-acetyl-L-leucine


substrate_name: N-formyl-L-methionine

smiles: CSCCC(C(=O)O)NC=O

substrate: N-formyl-L-methionine


substrate_name: N-propionyl-L-methionine

smiles: CCC(=O)NC(CCSC)C(=O)O

substrate: N-propionyl-L-methionine


substrate_name: N-acetyl-L-norleucine

smiles: CCCCC(C(=O)O)NC(=O)C

substrate: N-acetyl-L-norleucine


substrate_name: N-acetyl-L-threonine

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

substrate: N-acetyl-L-threonine


substrate_name: N-acetyl-L-glutamine

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

substrate: N-acetyl-L-glutamine


substrate_name: N-benzoyl-L-methionine

substrate: N-benzoyl-L-methionine


substrate_name: N-acetyl-glycine

smiles: CC(=O)NCC(=O)O

substrate: N-acetyl-glycine


substrate_name: N-acetyl-L-cysteine

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

substrate: N-acetyl-L-cysteine


substrate_name: N-benzoyl-L-glutamate

substrate: N-benzoyl-L-glutamate


substrate_name: N-acetyl-L-methionine

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

proof_lines:
Raw SKiD Env: Temp=25°C, pH=-----
Raw SKiD Env: Temp=-----, pH=-----

substrate: N-acetyl-L-methionine


substrate_name: N-acetyl-L-glutamate

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

substrate: N-acetyl-L-glutamate


substrate_name: N-acetyl-L-alanine

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

substrate: N-acetyl-L-alanine


substrate_name: N-acetyl-L-asparagine

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

substrate: N-acetyl-L-asparagine


enzyme_display_name: glucan 1,4-alpha-maltohexaosidase

organism: Klebsiella pneumoniae

substrate_name: short-chain amylose

enzyme: glucan 1,4-alpha-maltohexaosidase

substrate: short-chain amylose


substrate_name: maltohexaose

substrate: maltohexaose


substrate_name: maltopentaose

substrate: maltopentaose


substrate_name: maltotetraose

substrate: maltotetraose


organism: Lactobacillus helveticus

substrate_name: Ala-Pro-Arg

substrate: Ala-Pro-Arg


substrate_name: Arg-Pro-Ala

substrate: Arg-Pro-Ala


substrate_name: Tyr-Pro-Ala

substrate: Tyr-Pro-Ala


substrate_name: Ser-Pro-Ala

substrate: Ser-Pro-Ala


enzyme_display_name: tripeptidyl-peptidase II

organism: Mus musculus

proof_lines:
pH 6.2, 37°C, mutant H267A
mutant H267A, pH 6.4, 37°C
pH 7.6, 37°C, mutant H267A

enzyme: tripeptidyl-peptidase II


substrate_name: L-Ala-L-Ala-L-Phe 4-nitroanilide

assay_conditions_summary: pH 7.9; 310.15 K; buffer 100 mM potassium phosphate

proof_lines:
mutant E331Q, pH 7.9, 37°C
mutant E331Q, pH 8.3, 37°C
mutant E331Q, pH 6.4, 37°C

substrate: L-Ala-L-Ala-L-Phe 4-nitroanilide


substrate_name: L-Ala-L-Ala-L-Ala 4-nitroanilide

assay_conditions_summary: pH 6.4; 310.15 K; buffer 100 mM potassium phosphate

proof_lines:
wild-type, pH 6.4, 37°C
wild-type, pH 6.8, 37°C
wild-type, pH 7.6, 37°C

substrate: L-Ala-L-Ala-L-Ala 4-nitroanilide


enzyme_display_name: leukotriene-A4 hydrolase

assay_conditions_summary: pH 7.5; buffer 250 mM Tris

proof_lines: in 250 mM Tris buffer, pH 7.5, containing 500 mM KCl and 0.1% (w/v) of bovine serum albumin, at 37°C

enzyme: leukotriene-A4 hydrolase


assay_conditions_summary: pH 7.5; 310.15 K; buffer 250 mM Tris

proof_lines: in 250 mM Tris buffer, pH 7.5, containing 500 mM KCl and 0.1% of bovine serum albumin, at 37°C


enzyme_display_name: UniProt Q9KQ52

organism: Vibrio cholerae

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

enzyme: UniProt Q9KQ52


enzyme_display_name: UniProt P53184

organism: Saccharomyces cerevisiae

enzyme: UniProt P53184


substrate_name: Benzamide

substrate: Benzamide


enzyme_display_name: UniProt Q86V24

enzyme: UniProt Q86V24


organism: Streptococcus pneumoniae

proof_lines: mutant enzyme N322A, with Fmoc-Asn(Fucalpha1,6GlcNAc)-OH as acceptor, at pH 7.5 and 30°C


substrate_name: Fmoc-Asn(GlcNAc)-OH

substrate: Fmoc-Asn(GlcNAc)-OH


proof_lines: mutant enzyme N322Q, with Fmoc-Asn(Fucalpha1,6GlcNAc)-OH as acceptor, at pH 7.5 and 30°C


organism: Bos taurus


organism: Drosophila melanogaster

substrate_name: 5-fluoro-beta-L-gulosyl fluoride

substrate: 5-fluoro-beta-L-gulosyl fluoride


substrate_name: 2,4-dinitrophenyl alpha-D-mannoside

substrate: 2,4-dinitrophenyl alpha-D-mannoside


enzyme_display_name: methionyl aminopeptidase

organism: Escherichia coli

substrate_name: Met-Gly-Met-Met

enzyme: methionyl aminopeptidase

substrate: Met-Gly-Met-Met


proof_lines:
wild-type enzyme
wild-type enzyme, Fe(II) loaded, pH 7.5
wild-type enzyme, Co(II) loaded, pH 7.5


enzyme_display_name: UniProt J7H3P9

organism: Ligilactobacillus salivarius

substrate_name: glycochenodeoxycholic acid

enzyme: UniProt J7H3P9

substrate: glycochenodeoxycholic acid


substrate_name: taurochenodeoxycholic acid

substrate: taurochenodeoxycholic acid


substrate_name: taurocholic acid

substrate: taurocholic acid


substrate_name: glycocholic acid

substrate: glycocholic acid


substrate_name: glycodeoxycholic acid

substrate: glycodeoxycholic acid


substrate_name: taurodeoxycholic acid

substrate: taurodeoxycholic acid


enzyme_display_name: UniProt P0AF18

substrate_name: N-acetyl-D-glucosamine 6-sulfate

enzyme: UniProt P0AF18

substrate: N-acetyl-D-glucosamine 6-sulfate


substrate_name: Met-Pro-p-nitroanilide

proof_lines: mutant enzyme H178A, Co(II) loaded, pH 7.5

proof_lines: mutant enzyme H178A, Fe(II) loaded, pH 7.5

substrate: Met-Pro-p-nitroanilide


assay_conditions_summary: pH 7.5; 303.15 K; buffer 25 mM HEPES

proof_lines: wild type enzyme, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Mn2+


enzyme_display_name: isochorismatase

proof_lines: pH and temperature not specified in the publication

enzyme: isochorismatase


substrate_name: isochorismate

substrate: isochorismate


substrate_name: chorismate

substrate: chorismate


substrate_name: L-Met-Gly-L-Met-L-Met

proof_lines: mutant enzyme D97N, Co2+-loaded, in 25 mM HEPES buffer, at 30°C and pH 7.5

substrate: L-Met-Gly-L-Met-L-Met


proof_lines: mutant enzyme D97E, Co2+-loaded, in 25 mM HEPES buffer, at 30°C and pH 7.5


proof_lines: mutant enzyme D97A, Co2+-loaded, in 25 mM HEPES buffer, at 30°C and pH 7.5


substrate_name: Pro-Val

assay_conditions_summary: pH 7.8; 310.15 K; buffer 50 mM Tris-HCl

proof_lines: pH 7.8, 37°C, erythrocyte lysate from patients with prolidase (EC 3.4.13.9) deficiency, activated by 20 mM Gly

proof_lines: pH 7.8, 37°C, erythrocyte lysate from patients with prolidase (EC 3.4.13.9) deficiency, activated by 0.1 mM MnCl2 and 20 mM Gly

proof_lines: pH 7.8, 37°C, erythrocyte lysate from patients with prolidase (EC 3.4.13.9) deficiency, without activating compound

substrate: Pro-Val


substrate_name: Pro-Met

substrate: Pro-Met


substrate_name: Pro-Gly

proof_lines: pH 7.8, 37?, erythrocyte lysate from healthy patients, activated by 0.1 mM MnCl2 and 20 mM Gly

proof_lines: pH 7.8, 37?, erythrocyte lysate from patients with prolidase (EC 3.4.13.9) deficiency, activated by 0.1 mM MnCl2 and 20 mM Gly

substrate: Pro-Gly


substrate_name: Pro-Ala

substrate: Pro-Ala


substrate_name: Gly-Leu

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

substrate: Gly-Leu


enzyme_display_name: membrane dipeptidase

enzyme: membrane dipeptidase


enzyme_display_name: maltose-6'-phosphate glucosidase

enzyme: maltose-6'-phosphate glucosidase


substrate_name: trehalose 6-phosphate

substrate: trehalose 6-phosphate


substrate_name: maltose 6'-phosphate

substrate: maltose 6'-phosphate


enzyme_display_name: UniProt F1QCV2

organism: Danio rerio

smiles: CC(=O)NCCCCCCCCN

enzyme: UniProt F1QCV2


substrate_name: N-butylacetamide

smiles: CCCCNC(=O)C

substrate: N-butylacetamide


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


enzyme_display_name: formamidase

organism: Methylophilus methylotrophus

substrate_name: Formamide

smiles: C(=O)N

enzyme: formamidase

substrate: Formamide


enzyme_display_name: N-carbamoylputrescine amidase

organism: Zea mays

substrate_name: N-Carbamoylputrescine

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

enzyme: N-carbamoylputrescine amidase

substrate: N-Carbamoylputrescine


enzyme_display_name: UniProt Q0BRB0

organism: Granulibacter bethesdensis

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.3
Raw SKiD Env: Temp=25°C, pH=7.4

enzyme: UniProt Q0BRB0


enzyme_display_name: UniProt Q936X2

organism: Pseudomonas sp.

substrate_name: malonamic acid

enzyme: UniProt Q936X2

substrate: malonamic acid


substrate_name: leukotriene D4

proof_lines:
membrane-bound dipeptidase-2
membrane-bound dipeptidase-1

substrate: leukotriene D4


substrate_name: beta-lactam

substrate: beta-lactam


substrate_name: L-cystinyl-bis-Gly

proof_lines:
membrane-bound dipeptidase-1
membrane-bound dipeptidase-3

substrate: L-cystinyl-bis-Gly


organism: Mycobacterium tuberculosis

substrate_name: L-Met 4-nitroanilide

substrate: L-Met 4-nitroanilide


enzyme_display_name: arabinan endo-1,5-alpha-L-arabinanase

organism: Paenibacillus polymyxa

substrate_name: linear 1,5-alpha-L-arabinan

enzyme: arabinan endo-1,5-alpha-L-arabinanase

substrate: linear 1,5-alpha-L-arabinan


organism: Arthrobacter sp.

proof_lines: compound B, 2-(N-morpholino)ethane-sulfonic acid, pH 6.0


proof_lines:
compound A, 25°C, pH 7.0
competitive, most effective inhibitor
competitive


enzyme_display_name: N-feruloylglycine deacylase

organism: Hordeum vulgare

substrate_name: N-feruloylglycine

proof_lines:
Eadie-Hofstee plot
Lineweaver-Burk plot

enzyme: N-feruloylglycine deacylase

substrate: N-feruloylglycine


substrate_name: N-Sinapoylglycine

substrate: N-Sinapoylglycine


substrate_name: N-Feruloyl-L-alanine

substrate: N-Feruloyl-L-alanine


substrate_name: N-p-Coumaroylglycine

proof_lines: 5 mM: potent reversible inhibitor, kinetics of inhibition.

substrate: N-p-Coumaroylglycine


substrate_name: N-cinnamoylglycine

substrate: N-cinnamoylglycine


substrate_name: N-Dihydroferuloylglycine

substrate: N-Dihydroferuloylglycine


substrate_name: N-Feruloyl-D,L-aspartic acid

substrate: N-Feruloyl-D,L-aspartic acid


substrate_name: N-benzoylglycine

substrate: N-benzoylglycine


organism: Arachis hypogaea

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


substrate_name: L-glutamine

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

substrate: L-glutamine


enzyme_display_name: theanine hydrolase

organism: Pseudomonas aeruginosa

substrate_name: L-Theanine

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

enzyme: theanine hydrolase

substrate: L-Theanine


proof_lines: competitive non-competitive


enzyme_display_name: aculeacin-A deacylase

organism: Actinoplanes utahensis

substrate_name: aculeacin A

proof_lines: recombinant immobilized enzyme, Vmax: 35.2 micromol of hydrolzed aculeacin A min-1/g wet biocatalyst, pH 7, 60°C

enzyme: aculeacin-A deacylase

substrate: aculeacin A


enzyme_display_name: N-formylglutamate deformylase

organism: Rattus norvegicus

substrate_name: beta-Citryl-L-glutamate

enzyme: N-formylglutamate deformylase

substrate: beta-Citryl-L-glutamate


enzyme_display_name: snapalysin

organism: Streptomyces septatus

enzyme: snapalysin


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: N-formyl-L-glutamate

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

substrate: N-formyl-L-glutamate


substrate_name: penicillin F

proof_lines: recombinant immobilized enzyme, Vmax: 0.54 micromol of produced 6-aminopenicillanic acid min-1/g wet biocatalyst, pH 8, 45°C

substrate: penicillin F


substrate_name: penicillin G

assay_conditions_summary: pH 8; buffer 100 mM potassium phosphate

column_label: PMC article HTML Table 3, row Penicillin G: Km column 155.8 mM; kcat column 2.2 s^-1; kcat/Km column 0.01 mM^-1 s^-1. Local HTML line refs: PMC1950969_pmc_article.html lines 1586-1628.

normalized_value_unit_evidence: Km 155.8 mM and kcat 2.2 s^-1 match the export; paper kcat/Km is 0.01 mM^-1 s^-1, while the export carries 0.014120667522464698 s^-1*mM^-1.

raw_value_unit_evidence: Table 3 row Penicillin G reports Km 155.8 mM, kcat 2.2 s^-1, and kcat/Km 0.01 mM^-1 s^-1.

row_label: Penicillin G

table_label: Table 3. Kinetic parameters of recombinant AuAAC assayed with different natural penicillins

substrate: penicillin G


substrate_name: penicillin dihydroF

proof_lines: recombinant immobilized enzyme, Vmax: 1.45 micromol of produced 6-aminopenicillanic acid min-1/g wet biocatalyst, pH 8, 45°C

substrate: penicillin dihydroF


substrate_name: penicillin K

proof_lines: recombinant immobilized enzyme, Vmax: 7.6 micromol of produced 6-aminopenicillanic acid min-1/g wet biocatalyst, pH 8, 45°C

substrate: penicillin K


substrate_name: Penicillin V

proof_lines: recombinant immobilized enzyme, Vmax: 35.2 micromol of produced 6-aminopenicillanic acid min-1/g wet biocatalyst, pH 8, 45°C

substrate: Penicillin V


organism: Pseudomonas putida

column_label: Abstract/full text reports FGase exhibited a Km of 14 mM for FG in the presence of 5 mM substrate and 0.8 mM CoCl2 at 30 C.

raw_value_unit_evidence: Km raw_value=14 mM raw_unit=mM

row_label: formylglutamate amidohydrolase / N-formyl-L-glutamate (FG)

table_label: PubMed XML abstract and PMC full text PMID 3308850


organism: Macaca fascicularis

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: Disintegrin and metalloproteinase domain-containing protein 10

organism: Homo sapiens

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: ADAMTS-4 endopeptidase

proof_lines:
pH 7.5, 37°C, isoenzyme ADAMTS4-3
pH 7.5, 37°C, isoenzyme ADAMTS4-1
pH 7.5, 37°C, isoenzyme ADAMTS4-2

enzyme: ADAMTS-4 endopeptidase


enzyme_display_name: carboxypeptidase D

organism: Saccharomyces cerevisiae

substrate_name: Benzoyl-Phe-Ala-Arg

enzyme: carboxypeptidase D

substrate: Benzoyl-Phe-Ala-Arg


substrate_name: furylacryloyl-Ala-Arg

substrate: furylacryloyl-Ala-Arg


substrate_name: furylacryloyl-Ala-Lys

substrate: furylacryloyl-Ala-Lys


enzyme_display_name: dipeptidyl-peptidase IV

enzyme: dipeptidyl-peptidase IV


enzyme_display_name: ADAM10 endopeptidase

enzyme: ADAM10 endopeptidase


enzyme_display_name: UniProt P9WIJ3

substrate_name: N-formyl-Met-Ala

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

enzyme: UniProt P9WIJ3

substrate: N-formyl-Met-Ala


enzyme_display_name: UniProt Q93LE9

organism: Leptospira interrogans

substrate_name: N-formyl-Met-Ala-Ser

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

enzyme: UniProt Q93LE9

substrate: N-formyl-Met-Ala-Ser


enzyme_display_name: membrane dipeptidase

organism: Sus scrofa

substrate_name: Gly-D-Phe

enzyme: membrane dipeptidase

substrate: Gly-D-Phe


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

organism: Acetivibrio thermocellus


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


enzyme_display_name: tripeptidyl-peptidase II

organism: Arabidopsis sp.

enzyme: tripeptidyl-peptidase II


enzyme_display_name: carboxypeptidase B

organism: Bos taurus

substrate_name: benzoyl-Gly-Gly-Phe

proof_lines:
crystallized enzyme
soluble enzyme
carboxypeptidase B II

enzyme: carboxypeptidase B

substrate: benzoyl-Gly-Gly-Phe


substrate_name: Carbobenzoxy-Gly-Phe

proof_lines:
soluble enzyme
crystallized enzyme

substrate: Carbobenzoxy-Gly-Phe


enzyme_display_name: methionyl aminopeptidase

organism: Escherichia coli

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

enzyme: methionyl aminopeptidase

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


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

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


enzyme_display_name: maltose-6'-phosphate glucosidase

organism: Bacillus subtilis

assay_conditions_summary: pH 8.4; 310.15 K; buffer Tris-HCl

proof_lines:
at 37°C in Tris-HCl buffer, pH 8.4
at 37°C in HEPES buffer, pH 7.5

enzyme: maltose-6'-phosphate glucosidase


substrate_name: maltose 6'-phosphate

assay_conditions_summary: pH 7.5; 310.15 K; buffer HEPES

proof_lines:
at 37°C in HEPES buffer, pH 7.5
at 37°C in Tris-HCl buffer, pH 8.4

substrate: maltose 6'-phosphate


enzyme_display_name: UniProt P9WJN3

organism: Mycobacterium tuberculosis

substrate_name: N-acetyl-D-glucosamine

enzyme: UniProt P9WJN3

substrate: N-acetyl-D-glucosamine


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

mutation_signature: N-terminally truncated mutant

proof_lines: N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C

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


proof_lines: N-terminally truncated mutant lacking 135 amino acids, pH 7.0, 22°C


enzyme_display_name: cytosol nonspecific dipeptidase

substrate_name: Ala-Ala-p-nitroanilide

enzyme: cytosol nonspecific dipeptidase

substrate: Ala-Ala-p-nitroanilide


substrate_name: Ala-Pro-p-nitroanilide

substrate: Ala-Pro-p-nitroanilide


enzyme_display_name: tripeptidyl-peptidase I

substrate_name: Ala-Arg-Phe-p-nitrophenylalanyl-Arg-Leu

assay_conditions_summary: pH 4

proof_lines:
pH 4.0, 378°C, mutant enzyme E77A
pH 4.0, 37°C, mutant enzyme E77A

enzyme: tripeptidyl-peptidase I

substrate: Ala-Arg-Phe-p-nitrophenylalanyl-Arg-Leu


substrate_name: Arg-Ala-Phe-p-nitrophenylalanyl-Arg-Leu

substrate: Arg-Ala-Phe-p-nitrophenylalanyl-Arg-Leu


enzyme_display_name: cytosol alanyl aminopeptidase

substrate_name: Leu-Leu

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

enzyme: cytosol alanyl aminopeptidase

substrate: Leu-Leu


substrate_name: Ala-Ala

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

substrate: Ala-Ala


proof_lines:
wild-type, pH 7.5, 22°C
wild-type, pH 7.0, 22°C


proof_lines: truncated mutant lacking N-terminal 89 amino acids, pH 7.5, 22°C


enzyme_display_name: lysosomal Pro-Xaa carboxypeptidase

enzyme: lysosomal Pro-Xaa carboxypeptidase


substrate_name: 4-nitrophenyl alpha-D-mannopyranoside

substrate: 4-nitrophenyl alpha-D-mannopyranoside


enzyme_display_name: UniProt Q91XE4

organism: Mus musculus

smiles: CC(=O)NC(CSC(=CCl)Cl)C(=O)O

enzyme: UniProt Q91XE4


substrate_name: L-methionine 4-nitroanilide

proof_lines: mutant F309M, pH not specified in the publication, temperature not specified in the publication

substrate: L-methionine 4-nitroanilide


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


proof_lines: pH not specified in the publication, 37°C, recombinant wild-type membrane-bound enzyme

proof_lines: partial blockade of autolysis of both wild type and CHO-4 mutant MT1-MMP

proof_lines: complete blockade of autolysis of both wild type and CHO-4 mutant MT1-MMP


proof_lines: pH not specified in the publication, 37°C, recombinant enzyme mutant lacking the HPX domain

proof_lines: pH not specified in the publication, 37°C, recombinant enzyme mutant lacking the C-terminal domain


substrate_name: L-Lys-L-Pro-p-nitroanilide

substrate: L-Lys-L-Pro-p-nitroanilide


proof_lines: pH 7.4, wild-type soluble enzyme, mutant N150A, N219A, and N92A, expressed in Sf9 cells

proof_lines: pH 7.4, wild-type soluble enzyme, expressed in Sf9 cells


substrate_name: angiotensin II

substrate: angiotensin II


substrate_name: angiotensin III

substrate: angiotensin III


enzyme_display_name: Protein/nucleic acid deglycase 1

organism: Escherichia coli (strain K12)

substrate_name: methylglyoxal

smiles: CC(=O)C=O

proof_lines: kcat is 156.9 min(-1) for glyoxalase activity with methylglyoxal as substrate (PubMed:21696459). kcat is 0.43 min(-1) for aminopeptidase activity with Lys-AMC as substrate. kcat is 0.51 min(-1) for aminopeptidase activity with Arg-AMC as su

enzyme: Protein/nucleic acid deglycase 1

substrate: methylglyoxal


enzyme_display_name: IAA-amino acid hydrolase ILR1-like 4

organism: Arabidopsis thaliana

substrate_name: IAA-Ala

proof_lines: kcat is 0.024 sec(-1) with IAA-Ala as substrate.

enzyme: IAA-amino acid hydrolase ILR1-like 4

substrate: IAA-Ala


substrate_name: Lys-AMC (at 37 degrees Celsius and pH 8.5)


substrate_name: Arg-AMC (at 37 degrees Celsius and pH 8.5)


substrate_name: Ala-AMC (at 37 degrees Celsius and pH 8.5)


enzyme_display_name: Protein N-terminal asparagine amidohydrolase

substrate_name: NHGSGAWL peptide

proof_lines: kcat is 554 sec(-1) with NHGSGAWL as substrate. kcat is 457 sec(-1) with NAGVELEG as substrate. kcat is 470 sec(-1) with NHGVELEG as substrate. kcat is 598 sec(-1) with NRVYVHPFL as substrate. kcat is 398 sec(-1) with NV as substrate. kcat

substrate: NHGSGAWL peptide


enzyme_display_name: protein deglycase

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

proof_lines: kcat is 0.27 sec(-1) for the deglycation of glycated N-acetylarginine. kcat is 0.28 sec(-1) for the deglycation of glycated N-acetyllysine. kcat is 0.42 sec(-1) for the deglycation of glycated N-acetylcysteine. kcat is 0.02 sec(-1) for glyo

source_databases_merged: sabio_rk skid uniprot

enzyme: protein deglycase


enzyme_display_name: Oxamate amidohydrolase proenzyme

organism: Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)

substrate_name: Unknown

proof_lines: kcat is 5.5 sec(-1) with oxamate as substrate.

enzyme: Oxamate amidohydrolase proenzyme

substrate: Unknown


enzyme_display_name: chitin disaccharide deacetylase

organism: Pyrococcus horikoshii

substrate_name: N,N'-diacetylchitobiose

enzyme: chitin disaccharide deacetylase

substrate: N,N'-diacetylchitobiose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R157H with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R157W with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


enzyme_display_name: Protein/nucleic acid deglycase 2

substrate_name: glyoxal (at pH 7.4 and 37 degrees Celsius)

smiles: C(=O)C=O

proof_lines: kcat is 118.44 min(-1) and 20.80 min(-1) for glyoxalase activity with glyoxal (GO) and methylglyoxal (MGO) as substrate, respectively (at pH 7.4 and 37 degrees Celsius) (PubMed:26678554). The apparent kcat of MGO and GO degradation is 0.29

enzyme: Protein/nucleic acid deglycase 2


substrate_name: methylglyoxal (at pH 7.4 and 37 degrees Celsius)


enzyme_display_name: Protein/nucleic acid deglycase 3

proof_lines: kcat is 70.32 min(-1) for glyoxalase activity with glyoxal as substrate (at pH 7.4 and 37 degrees Celsius) (PubMed:26678554). The apparent kcat of methylglyoxal and glyoxal degradation is 0.08 sec(-1), and 0.15 sec(-1), respectively (at 22

enzyme: Protein/nucleic acid deglycase 3

substrate: glyoxal (at pH 7.4 and 37 degrees Celsius)


enzyme_display_name: dihydropyrimidinase

organism: Geobacillus stearothermophilus

substrate_name: DL-p-hydroxyphenylhydantoin

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M63H/F159N to reconstruct the assayed variant sequence.

enzyme: dihydropyrimidinase

substrate: DL-p-hydroxyphenylhydantoin


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M63I/F159S to reconstruct the assayed variant sequence.


substrate_name: hydantoin

substrate: hydantoin


enzyme_display_name: UniProt O66990

organism: Aquifex aeolicus

substrate_name: N-carbamoyl-L-aspartate

enzyme: UniProt O66990

substrate: N-carbamoyl-L-aspartate


enzyme_display_name: UniProt Q81WF0

organism: Bacillus anthracis

enzyme: UniProt Q81WF0


enzyme_display_name: allantoinase

organism: Vigna unguiculata subsp. cylindrica

substrate_name: allantoin

proof_lines:
pH 7.5
pH 4

enzyme: allantoinase

substrate: allantoin


organism: Ricinus communis


enzyme_display_name: oxamate amidohydrolase

organism: Klebsiella pneumoniae subsp. pneumoniae

substrate_name: oxamate

enzyme: oxamate amidohydrolase

substrate: oxamate


organism: Vibrio cholerae


organism: Nonomuraea sp.

substrate_name: D-Ala-D-Ala

substrate: D-Ala-D-Ala


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

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


organism: Homo sapiens


enzyme_display_name: methionyl aminopeptidase

enzyme: methionyl aminopeptidase


proof_lines:
pH 7.5, 37°C, wild-type enzyme
wild-type, pH 7.5, 30°C


enzyme_display_name: membrane dipeptidase

organism: Rattus norvegicus

substrate_name: L-cystinyl-bis-Gly

enzyme: membrane dipeptidase

substrate: L-cystinyl-bis-Gly


substrate_name: L-Ala-Gly

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

substrate: L-Ala-Gly


enzyme_display_name: microsomal epoxide hydrolase

substrate_name: phenanthrene 9,10-oxide

enzyme: microsomal epoxide hydrolase

substrate: phenanthrene 9,10-oxide


substrate_name: 1,10-phenanthroline 5,6-oxide

substrate: 1,10-phenanthroline 5,6-oxide


organism: Mycolicibacterium smegmatis

proof_lines: wild type enzyme, at pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme D169A, at pH 7.4, temperature not specified in the publication


enzyme_display_name: endothelin-converting enzyme 1

substrate_name: Big endothelin-1

enzyme: endothelin-converting enzyme 1

substrate: Big endothelin-1


substrate_name: big endothelin-3

substrate: big endothelin-3


enzyme_display_name: N-formylglutamate deformylase

organism: Pseudomonas putida

substrate_name: N-formyl-L-glutamate

enzyme: N-formylglutamate deformylase

substrate: N-formyl-L-glutamate


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: aminopeptidase S

organism: Streptomyces sp.

substrate_name: 4-nitrophenyl phenylphosphonate

proof_lines:
pH 8.0, 50°C, Ni2+-enzyme
pH 8.0, 50°C, Mn2+-enzyme
pH 8.0, 50°C, Zn2+-enzyme

enzyme: aminopeptidase S

substrate: 4-nitrophenyl phenylphosphonate


substrate_name: bis(4-nitrophenyl) phosphate

proof_lines:
pH 8.0, 30°C, Ni2+-enzyme
pH 8.0, 30°C, Cd2+-enzyme
pH 8.0, 30°C, Mn2+-enzyme

substrate: bis(4-nitrophenyl) phosphate


organism: Streptomyces sp. R61


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

organism: Trichoderma reesei

substrate_name: alpha-cellobiosyl fluoride

substrate: alpha-cellobiosyl fluoride


substrate_name: beta-cellobiosyl fluoride

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

substrate: beta-cellobiosyl fluoride


enzyme_display_name: carboxypeptidase C

organism: Saccharomyces cerevisiae

substrate_name: Benzyloxycarbonyl-Gly-Glu

enzyme: carboxypeptidase C

substrate: Benzyloxycarbonyl-Gly-Glu


substrate_name: Benzyloxycarbonyl-Glu-Tyr

substrate: Benzyloxycarbonyl-Glu-Tyr


organism: Acinetobacter baumannii

proof_lines: after removal of divalent metal ions activated with 0.020 mM Mn2+, pH not specified in the publication, temperature not specified in the publication

proof_lines: after removal of divalent metal ions activated with 0.020 mM Co2+, pH not specified in the publication, temperature not specified in the publication

proof_lines: after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: arabinan endo-1,5-alpha-L-arabinanase

organism: Aspergillus niger

proof_lines: apple juice ultrafiltration retentate, UFR, arabinan, linearised

enzyme: arabinan endo-1,5-alpha-L-arabinanase


enzyme_display_name: aspartyl aminopeptidase

organism: Aspergillus oryzae

proof_lines:
pH 7.0, 37°C
pH 7.0, 37°C, with 3 M NaCl

enzyme: aspartyl aminopeptidase


organism: Bacillus subtilis

substrate_name: linear 1,5-alpha-L-arabinan

substrate: linear 1,5-alpha-L-arabinan


organism: Babesia bovis

substrate_name: L-methionine 4-methylcoumaryl-7-amide

proof_lines: pH 7.5, temperature not specified in the publication

substrate: L-methionine 4-methylcoumaryl-7-amide


proof_lines: wild type isoform Arb43B, pH and temperature not specified in the publication


enzyme_display_name: dipeptidyl-peptidase IV

organism: Bos taurus

substrate_name: amyloid beta42

enzyme: dipeptidyl-peptidase IV

substrate: amyloid beta42


enzyme_display_name: carboxypeptidase A

substrate_name: hippuryl-L-phenylalanine

proof_lines: in the absence of spermidine, at pH 7.5 and 37°C

proof_lines: in the absence of spermine, at pH 7.5 and 37°C

proof_lines: in the presence of 0.1 mM spermine, at pH 7.5 and 37°C

enzyme: carboxypeptidase A

substrate: hippuryl-L-phenylalanine


mutation_signature: truncated recombinant mature enzyme

proof_lines: truncated recombinant mature enzyme, at pH 8.0 and 40°C


organism: Bifidobacterium longum subsp. infantis

substrate_name: ribonuclease B

substrate: ribonuclease B


assay_conditions_summary: pH 7.5; 298.15 K; buffer 0.05 M Tris/0.5 M NaCl

proof_lines:
pH 7.5
soluble enzyme
immobilized enzyme


enzyme_display_name: D-stereospecific aminopeptidase

organism: Brucella sp. F23/97

enzyme: D-stereospecific aminopeptidase


substrate_name: Gly-L-Tyr

substrate: Gly-L-Tyr


organism: Canis lupus familiaris


organism: Capra hircus

proof_lines:
soluble enzyme
enzyme immobilized on Ca alginate beads


organism: Cellulomonas sp.

substrate_name: arabinogalactan

substrate: arabinogalactan


enzyme_display_name: bontoxilysin

organism: Clostridium botulinum

proof_lines: pH 7.4, 37°C, recombinant wild-type enzyme in absence of exogenous ZnCl2

proof_lines: pH 7.4, 37°C, recombinant wild-type enzyme in presence of exogenous ZnCl2

enzyme: bontoxilysin


organism: Clostridium baratii

substrate_name: vesicle-associated membrane protein-2

proof_lines: enzyme subtype BoNT/F7, at pH 6.8 and 37°C

substrate: vesicle-associated membrane protein-2


proof_lines: pH 7.4, 23°C, mutant light chain + translocation domain


substrate_name: SNAPtide 521

proof_lines: recombinant light chain-translocation domain, at pH 7.4 and 37°C

proof_lines: botulinum neurotoxin type A, at pH 7.4 and 37°C

substrate: SNAPtide 521


organism: Drosophila melanogaster

proof_lines: pH 6.0, temperature not specified in the publication


enzyme_display_name: tripeptidyl-peptidase II

organism: Drosophila sp. (in: flies)

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

enzyme: tripeptidyl-peptidase II


substrate_name: big endothelin-3

substrate: big endothelin-3


organism: Enterococcus faecalis


substrate_name: L-methionine 4-nitroanilide

substrate: L-methionine 4-nitroanilide


enzyme_display_name: adenine glycosylase

organism: Escherichia coli

substrate_name: DNA containing a 5-hydroxyuracil/adenine mismatch

enzyme: adenine glycosylase


substrate_name: L-Met-Gly-L-Met-L-Met

proof_lines: mutant enzyme H79A, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Co2+

substrate: L-Met-Gly-L-Met-L-Met


proof_lines: recombinant PBP 6, in 50 mM Tris-HCl, pH 8.5, at 37°C

proof_lines: recombinant PBP 5, in 50 mM Tris-HCl, pH 8.5, at 37°C


enzyme_display_name: oligopeptidase A

substrate_name: Abz-GESPFRQ-EDDnp

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

enzyme: oligopeptidase A

substrate: Abz-GESPFRQ-EDDnp


enzyme_display_name: PepB aminopeptidase

substrate_name: O-methyl-DL-serinamide

enzyme: PepB aminopeptidase

substrate: O-methyl-DL-serinamide


enzyme_display_name: UniProt C7C422

organism: Klebsiella pneumoniae

substrate_name: doripenem

enzyme: UniProt C7C422

substrate: doripenem


enzyme_display_name: UniProt H6WZS9

substrate_name: nitrocefin

enzyme: UniProt H6WZS9

substrate: nitrocefin


enzyme_display_name: UniProt M1VE66

substrate_name: ceftazidime

enzyme: UniProt M1VE66

substrate: ceftazidime


enzyme_display_name: UniProt P00808

organism: Bacillus licheniformis

substrate_name: penicillin G

enzyme: UniProt P00808

substrate: penicillin G


enzyme_display_name: UniProt P00811

enzyme: UniProt P00811


substrate_name: cefoxitin

substrate: cefoxitin


enzyme_display_name: UniProt P05364

organism: Enterobacter cloacae

substrate_name: benzylpenicillin

enzyme: UniProt P05364

substrate: benzylpenicillin


substrate_name: ampicillin

substrate: ampicillin


substrate_name: carbenicillin

substrate: carbenicillin


substrate_name: Cloxacillin

substrate: Cloxacillin


substrate_name: cephalexin

substrate: cephalexin


substrate_name: Oxacillin

substrate: Oxacillin


substrate_name: cefazolin

substrate: cefazolin


enzyme_display_name: UniProt P52700

organism: Stenotrophomonas maltophilia

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7

enzyme: UniProt P52700


enzyme_display_name: UniProt P85302

organism: Pseudomonas fluorescens

enzyme: UniProt P85302


enzyme_display_name: UniProt Q09HD0

substrate_name: piperacillin

enzyme: UniProt Q09HD0

substrate: piperacillin


substrate_name: cephaloridine

substrate: cephaloridine


enzyme_display_name: UniProt Q3SAW3

organism: Pseudomonas aeruginosa

substrate_name: ticarcillin

enzyme: UniProt Q3SAW3

substrate: ticarcillin


substrate_name: cefuroxime

substrate: cefuroxime


substrate_name: aztreonam

substrate: aztreonam


substrate_name: amoxicillin

substrate: amoxicillin


substrate_name: ceftriaxone

substrate: ceftriaxone


substrate_name: cefsulodine

substrate: cefsulodine


substrate_name: cefotaxime

substrate: cefotaxime


substrate_name: cephalothin

substrate: cephalothin


enzyme_display_name: UniProt Q76DI4

substrate_name: cefpirome

enzyme: UniProt Q76DI4

substrate: cefpirome


substrate_name: ampicillin

substrate: ampicillin


substrate_name: cefoxitin

substrate: cefoxitin


substrate_name: ceftazidime

substrate: ceftazidime


enzyme_display_name: UniProt Q9RMI1

organism: Serratia fonticola

substrate_name: moxalactam

enzyme: UniProt Q9RMI1

substrate: moxalactam


substrate_name: cefepime

substrate: cefepime


substrate_name: nitrocefin

substrate: nitrocefin


substrate_name: Imipenem

substrate: Imipenem


substrate_name: meropenem

substrate: meropenem


substrate_name: carbenicillin

substrate: carbenicillin


enzyme_display_name: UniProt P26918

organism: Aeromonas hydrophila

substrate_name: cephaloridine

enzyme: UniProt P26918

substrate: cephaloridine


substrate_name: biapenem

substrate: biapenem


substrate_name: cefaclor

substrate: cefaclor


substrate_name: penicillin G

substrate: penicillin G


substrate_name: doripenem

substrate: doripenem


substrate_name: cefalotin

substrate: cefalotin


enzyme_display_name: UniProt I3VKD5

enzyme: UniProt I3VKD5


substrate_name: cefuroxime

substrate: cefuroxime


enzyme_display_name: UniProt P16897

enzyme: UniProt P16897


enzyme_display_name: UniProt P62593

enzyme: UniProt P62593


substrate_name: cephalothin

substrate: cephalothin


enzyme_display_name: UniProt Q59401

substrate_name: 7-aminocephalosporanic acid

enzyme: UniProt Q59401

substrate: 7-aminocephalosporanic acid


enzyme_display_name: UniProt Q5QT35

organism: Acinetobacter baumannii

enzyme: UniProt Q5QT35


substrate_name: Cloxacillin

substrate: Cloxacillin


substrate_name: Oxacillin

substrate: Oxacillin


substrate_name: ceftazidime

substrate: ceftazidime


substrate_name: ampicillin

substrate: ampicillin


enzyme_display_name: UniProt P14488

organism: Bacillus cereus

substrate_name: benzylpenicillin

enzyme: UniProt P14488

substrate: benzylpenicillin


enzyme_display_name: methionyl aminopeptidase

assay_conditions_summary: pH 7; 303.15 K; buffer 25 mM HEPES

proof_lines: in 25 mM HEPES buffer at 30°C (pH 7.5) with 150 mM KCl

enzyme: methionyl aminopeptidase


substrate_name: L-Met-L-Ala-L-Ser

proof_lines: mutant enzyme H63A, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C

substrate: L-Met-L-Ala-L-Ser


substrate_name: Met-Gly-Met-Met

substrate: Met-Gly-Met-Met


organism: Geobacillus stearothermophilus


enzyme_display_name: aspartyl aminopeptidase

organism: Gallus gallus

enzyme: aspartyl aminopeptidase


organism: Helicobacter pylori


enzyme_display_name: UniProt A0P0F0

organism: Roseibium aggregatum

substrate_name: isatin

enzyme: UniProt A0P0F0

substrate: isatin


enzyme_display_name: arginase

organism: Phaseolus vulgaris

substrate_name: L-Arg

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

enzyme: arginase

substrate: L-Arg


enzyme_display_name: UniProt P05089

organism: Homo sapiens

substrate_name: L-arginine

proof_lines:
Raw SKiD Env: Temp=37°C, pH=9.4
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=9.5

enzyme: UniProt P05089

substrate: L-arginine


enzyme_display_name: UniProt P39138

organism: Bacillus subtilis

enzyme: UniProt P39138


enzyme_display_name: microsomal epoxide hydrolase

organism: Heliothis virescens

substrate_name: juvenile hormone III

proof_lines: in 100 mM sodium phosphate, pH 8.0, at 30°C

enzyme: microsomal epoxide hydrolase

substrate: juvenile hormone III


organism: Hevea brasiliensis


organism: Haemophilus influenzae

substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


enzyme_display_name: UniProt P38488

organism: Pseudomonas putida

substrate_name: Creatine

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

enzyme: UniProt P38488

substrate: Creatine


enzyme_display_name: UniProt Q7SIB5

organism: Actinobacillus sp.

enzyme: UniProt Q7SIB5


enzyme_display_name: allantoicase

organism: Streptomyces viridiviolaceus

substrate_name: Allantoate

enzyme: allantoicase

substrate: Allantoate