column_label: Table 1 (Enzymatic specificity of EtAPN1r), substrate row 'hArg-ACC'; column 'Km (uM)' = 27.7; column 'kcat (s^-1)' = 0.575; column 'kcat/Km (mM^-1 s^-1)' = 20.8. The kcat/Km column head is printed on two physical lines, 'kcat/Km' above '(mM^-1 . s^-1)'.

normalized_value_unit_evidence: Km: printed Table 1 cell 27.7 uM; 27.7 / 1000 = 0.0277 mM; the exported value is 0.0277 mM. kcat: printed Table 1 cell 0.575 s^-1; the printed unit is already the canonical kcat unit, so no unit conversion applies; the exported value is 0.575 s^(-1). kcat/Km: printed Table 1 cell 20.8 mM^-1 s^-1; mM^-1 s^-1 is the canonical kcat/Km unit, so no unit conversion applies and the printed cell normalizes to 20.8 s^(-1)*mM^(-1); the exported 20.75812274368231 s^(-1)*mM^(-1) is the full-precision quotient 0.575 / 0.0277 of the same Table 1 row, which this table prints rounded to its own one-decimal precision as 20.8.

raw_value_unit_evidence: Table 1: Enzymatic specificity of EtAPN1r (Eukaryotic Cell, July 2014, volume 13, number 7, page 891), substrate row 'hArg-ACC': printed Km cell 27.7 uM; printed kcat cell 0.575 s^-1; printed kcat/Km cell 20.8 mM^-1 s^-1.

row_label: Table 1, substrate row 'hArg-ACC'


enzyme_display_name: aminopeptidase Ey

organism: Eimeria tenella

source_db: oed

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

column_label: Table 1 (Enzymatic specificity of EtAPN1r), substrate row 'hPhe-ACC'; column 'Km (uM)' = 26.2; column 'kcat (s^-1)' = 0.836; column 'kcat/Km (mM^-1 s^-1)' = 31.9. The kcat/Km column head is printed on two physical lines, 'kcat/Km' above '(mM^-1 . s^-1)'.

normalized_value_unit_evidence: Km: printed Table 1 cell 26.2 uM; 26.2 / 1000 = 0.0262 mM; the exported value is 0.0262 mM. kcat: printed Table 1 cell 0.836 s^-1; the printed unit is already the canonical kcat unit, so no unit conversion applies; the exported value is 0.836 s^(-1). kcat/Km: printed Table 1 cell 31.9 mM^-1 s^-1; mM^-1 s^-1 is the canonical kcat/Km unit, so no unit conversion applies and the printed cell normalizes to 31.9 s^(-1)*mM^(-1); the exported 31.90839694656488 s^(-1)*mM^(-1) is the full-precision quotient 0.836 / 0.0262 of the same Table 1 row, which this table prints rounded to its own one-decimal precision as 31.9.

raw_value_unit_evidence: Table 1: Enzymatic specificity of EtAPN1r (Eukaryotic Cell, July 2014, volume 13, number 7, page 891), substrate row 'hPhe-ACC': printed Km cell 26.2 uM; printed kcat cell 0.836 s^-1; printed kcat/Km cell 31.9 mM^-1 s^-1.

row_label: Table 1, substrate row 'hPhe-ACC'

data_origin: experimental

enzyme: aminopeptidase Ey

status: verified

source: oed


column_label: Table 1 (Enzymatic specificity of EtAPN1r), substrate row 'Met-ACC'; column 'Km (uM)' = 31.4; column 'kcat (s^-1)' = 0.704; column 'kcat/Km (mM^-1 s^-1)' = 22.4. The kcat/Km column head is printed on two physical lines, 'kcat/Km' above '(mM^-1 . s^-1)'.

normalized_value_unit_evidence: Km: printed Table 1 cell 31.4 uM; 31.4 / 1000 = 0.0314 mM; the exported value is 0.0314 mM. kcat: printed Table 1 cell 0.704 s^-1; the printed unit is already the canonical kcat unit, so no unit conversion applies; the exported value is 0.704 s^(-1). kcat/Km: printed Table 1 cell 22.4 mM^-1 s^-1; mM^-1 s^-1 is the canonical kcat/Km unit, so no unit conversion applies and the printed cell normalizes to 22.4 s^(-1)*mM^(-1); the exported 22.420382165605098 s^(-1)*mM^(-1) is the full-precision quotient 0.704 / 0.0314 of the same Table 1 row, which this table prints rounded to its own one-decimal precision as 22.4.

raw_value_unit_evidence: Table 1: Enzymatic specificity of EtAPN1r (Eukaryotic Cell, July 2014, volume 13, number 7, page 891), substrate row 'Met-ACC': printed Km cell 31.4 uM; printed kcat cell 0.704 s^-1; printed kcat/Km cell 22.4 mM^-1 s^-1.

row_label: Table 1, substrate row 'Met-ACC'


column_label: Table 1 (Enzymatic specificity of EtAPN1r), substrate row 'Nle-ACC'; column 'Km (uM)' = 16.5; column 'kcat (s^-1)' = 0.710; column 'kcat/Km (mM^-1 s^-1)' = 43.0. The kcat/Km column head is printed on two physical lines, 'kcat/Km' above '(mM^-1 . s^-1)'.

normalized_value_unit_evidence: Km: printed Table 1 cell 16.5 uM; 16.5 / 1000 = 0.0165 mM; the exported value is 0.0165 mM. kcat: printed Table 1 cell 0.710 s^-1; the printed unit is already the canonical kcat unit, so no unit conversion applies; the exported value is 0.71 s^(-1). kcat/Km: printed Table 1 cell 43.0 mM^-1 s^-1; mM^-1 s^-1 is the canonical kcat/Km unit, so no unit conversion applies and the printed cell normalizes to 43.0 s^(-1)*mM^(-1); the exported 43.030303030303024 s^(-1)*mM^(-1) is the full-precision quotient 0.71 / 0.0165 of the same Table 1 row, which this table prints rounded to its own one-decimal precision as 43.0.

raw_value_unit_evidence: Table 1: Enzymatic specificity of EtAPN1r (Eukaryotic Cell, July 2014, volume 13, number 7, page 891), substrate row 'Nle-ACC': printed Km cell 16.5 uM; printed kcat cell 0.710 s^-1; printed kcat/Km cell 43.0 mM^-1 s^-1.

row_label: Table 1, substrate row 'Nle-ACC'


column_label: Table 1 (Enzymatic specificity of EtAPN1r), substrate row 'Nva-ACC'; column 'Km (uM)' = 35.4; column 'kcat (s^-1)' = 0.658; column 'kcat/Km (mM^-1 s^-1)' = 18.6. The kcat/Km column head is printed on two physical lines, 'kcat/Km' above '(mM^-1 . s^-1)'.

normalized_value_unit_evidence: Km: printed Table 1 cell 35.4 uM; 35.4 / 1000 = 0.0354 mM; the exported value is 0.0354 mM. kcat: printed Table 1 cell 0.658 s^-1; the printed unit is already the canonical kcat unit, so no unit conversion applies; the exported value is 0.658 s^(-1). kcat/Km: printed Table 1 cell 18.6 mM^-1 s^-1; mM^-1 s^-1 is the canonical kcat/Km unit, so no unit conversion applies and the printed cell normalizes to 18.6 s^(-1)*mM^(-1); the exported 18.587570621468927 s^(-1)*mM^(-1) is the full-precision quotient 0.658 / 0.0354 of the same Table 1 row, which this table prints rounded to its own one-decimal precision as 18.6.

raw_value_unit_evidence: Table 1: Enzymatic specificity of EtAPN1r (Eukaryotic Cell, July 2014, volume 13, number 7, page 891), substrate row 'Nva-ACC': printed Km cell 35.4 uM; printed kcat cell 0.658 s^-1; printed kcat/Km cell 18.6 mM^-1 s^-1.

row_label: Table 1, substrate row 'Nva-ACC'


column_label: Table 1 (Enzymatic specificity of EtAPN1r), substrate row 'Styryl-Ala-ACC'; column 'Km (uM)' = 30.2; column 'kcat (s^-1)' = 0.577; column 'kcat/Km (mM^-1 s^-1)' = 19.1. The kcat/Km column head is printed on two physical lines, 'kcat/Km' above '(mM^-1 . s^-1)'.

normalized_value_unit_evidence: Km: printed Table 1 cell 30.2 uM; 30.2 / 1000 = 0.0302 mM; the exported value is 0.0302 mM. kcat: printed Table 1 cell 0.577 s^-1; the printed unit is already the canonical kcat unit, so no unit conversion applies; the exported value is 0.577 s^(-1). kcat/Km: printed Table 1 cell 19.1 mM^-1 s^-1; mM^-1 s^-1 is the canonical kcat/Km unit, so no unit conversion applies and the printed cell normalizes to 19.1 s^(-1)*mM^(-1); the exported 19.10596026490066 s^(-1)*mM^(-1) is the full-precision quotient 0.577 / 0.0302 of the same Table 1 row, which this table prints rounded to its own one-decimal precision as 19.1.

raw_value_unit_evidence: Table 1: Enzymatic specificity of EtAPN1r (Eukaryotic Cell, July 2014, volume 13, number 7, page 891), substrate row 'Styryl-Ala-ACC': printed Km cell 30.2 uM; printed kcat cell 0.577 s^-1; printed kcat/Km cell 19.1 mM^-1 s^-1.

row_label: Table 1, substrate row 'Styryl-Ala-ACC'


enzyme_display_name: methionyl aminopeptidase

organism: Mycobacterium tuberculosis

substrate_name: L-Met 4-nitroanilide

verification_status: unverified

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C105S to reconstruct the assayed variant sequence.

mutation_type: substitution

enzyme: methionyl aminopeptidase

substrate: L-Met 4-nitroanilide

status: unverified


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C105T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C105V to reconstruct the assayed variant sequence.


enzyme_display_name: tripeptidyl-peptidase II

organism: Mus musculus

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

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

proof_lines:
Mycobacterium tuberculosis
MetAP proteins
catalytic efficiency

enzyme: tripeptidyl-peptidase II

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H267A to reconstruct the assayed variant sequence.


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

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


enzyme_display_name: Methionine aminopeptidase 2

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: Met-Gly-Met-Met (at pH 7.5 and at 37 degrees Celsius)

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

column_label: Article prose states MtMetAP1c Km for Met-Gly-Met-Met.

row_label: MtMetAP1c / Met-Gly-Met-Met

table_label: Kinetic parameters prose in Results

enzyme: Methionine aminopeptidase 2

source: uniprot


substrate_name: Met-Ala-Ser (at pH 7.5 and at 37 degrees Celsius)

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

column_label: Article prose states MtMetAP1c Km for Met-Ala-Ser.

row_label: MtMetAP1c / Met-Ala-Ser


enzyme_display_name: Methionine aminopeptidase 1

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

column_label: Article prose states MtMetAP1a Km for Met-Ala-Ser.

row_label: MtMetAP1a / Met-Ala-Ser

enzyme: Methionine aminopeptidase 1

substrate: Met-Ala-Ser (at pH 7.5 and at 37 degrees Celsius)


column_label: Article prose states MtMetAP1a Km for Met-Gly-Met-Met.

row_label: MtMetAP1a / Met-Gly-Met-Met

substrate: Met-Gly-Met-Met (at pH 7.5 and at 37 degrees Celsius)


organism: Drosophila melanogaster

sequence_variant_note: Mutation signature D387G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: Dipeptidyl peptidase 8

organism: Homo sapiens

substrate_name: H-Ala-Pro-pNa

proof_lines: DPP8 Ala-X-pNA X-Pro-pNA

enzyme: Dipeptidyl peptidase 8

substrate: H-Ala-Pro-pNa


substrate_name: H-Ala-Ala-pNa

proof_lines: DPP8 Ala-Ala-pNA Ala-X-pNA

substrate: H-Ala-Ala-pNa


substrate_name: H-Arg-Pro-pNa

proof_lines: DPP8 X-Pro-pNA Arg-Pro-pNA

substrate: H-Arg-Pro-pNa


substrate_name: H-Asp-Pro-pNa

proof_lines: DPP8 X-Pro-pNA Asp-Pro-pNA

substrate: H-Asp-Pro-pNa


enzyme_display_name: Dipeptidase 2

column_label: Table 2, Properties of MBDs; row=MBD-2; column=LTD4 Km1; footnote Km1 uM.

raw_value_unit_evidence: Table 2 row MBD-2: LTD4 Km1 = 5 uM; cys-bis-gly = ND; beta-lactam = ND.

row_label: MBD-2; substrate LTD4 Km1

table_label: Table 2

enzyme: Dipeptidase 2


enzyme_display_name: Dipeptidase 1

substrate_name: leukotriene D4

column_label: Table 2, Properties of MBDs; row=MBD-1; column=LTD4 Km1; footnote Km1 uM.

raw_value_unit_evidence: Table 2 row MBD-1: LTD4 Km1 = 10 uM; cys-bis-gly Km2 = 0.45 mM; beta-lactam Km3 = 111 uM.

row_label: MBD-1; substrate LTD4 Km1

enzyme: Dipeptidase 1

substrate: leukotriene D4


substrate_name: cystinyl-bis-glycine

column_label: Table 2, Properties of MBDs; row=MBD-1; column=cys-bis-gly Km2; footnote Km2 mM.

row_label: MBD-1; substrate cys-bis-gly Km2

substrate: cystinyl-bis-glycine


substrate_name: beta-lactam

substrate: beta-lactam


enzyme_display_name: aminopeptidase Y

organism: Pyrococcus furiosus

substrate_name: L-arginine 4-nitroanilide

column_label: Table 5 columns Km (mM), Vmax (umol/min/mg), kcat (s^-1), and kcat/Km (mM^-1 s^-1); row r-KAP / Arg-pNA.

raw_value_unit_evidence: Table 5 row r-KAP / Arg-pNA reports Km 1.4 mM, Vmax 1200 umol/min/mg, kcat 769 s^-1, and rounded kcat/Km 550 mM^-1 s^-1.

row_label: r-KAP / Arg-pNA

table_label: Table 5. Kinetic parameters for substrates of P. furiosus lysine aminopeptidase

enzyme: aminopeptidase Y

substrate: L-arginine 4-nitroanilide


substrate_name: L-lysine 4-nitroanilide

verification_status: corrected

column_label: Table 5, r-KAP / Lys-pNA row, Km, kcat, and kcat/Km columns.

raw_value_unit_evidence: r-KAP Lys-pNA: Km 4.0 mM; kcat 1840 s^-1; kcat/Km 460 mM^-1 s^-1.

row_label: r-KAP / Lys-pNA

substrate: L-lysine 4-nitroanilide

status: corrected


substrate_name: Lys-Gly-Gly

column_label: Table 5 columns Km (mM), Vmax (umol/min/mg), kcat (s^-1), and kcat/Km (mM^-1 s^-1); row r-KAP / Lys-Gly-Gly.

raw_value_unit_evidence: Table 5 row r-KAP / Lys-Gly-Gly reports Km 2.7 mM, Vmax 2300 umol/min/mg, kcat 1460 s^-1, and rounded kcat/Km 540 mM^-1 s^-1.

row_label: r-KAP / Lys-Gly-Gly

substrate: Lys-Gly-Gly


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

organism: Talaromyces purpureogenus

substrate_name: 4-nitrophenyl beta-D-xylopyranoside

source_db: brenda

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

substrate: 4-nitrophenyl beta-D-xylopyranoside

source: brenda


substrate_name: 4-nitrophenyl beta-D-glucopyranoside

substrate: 4-nitrophenyl beta-D-glucopyranoside


substrate_name: 4-nitrophenyl alpha-L-arabinofuranoside

proof_lines:
ABN1
p-nitrophenyl arabinofuranoside
pNPAra

substrate: 4-nitrophenyl alpha-L-arabinofuranoside


enzyme_display_name: dipeptidyl-peptidase IV

column_label: PDF page 4 Table 2, row H-Ala-Ala-pNA, columns Km, kcat, kcat/Km.

raw_value_unit_evidence: Table 2 row H-Ala-Ala-pNA: Km 1420 uM; kcat 0.7 s^-1; kcat/Km 0.0005 s^-1 uM^-1.

row_label: H-Ala-Ala-pNA

enzyme: dipeptidyl-peptidase IV


column_label: PDF page 4 Table 2, row H-Ala-Pro-pNA, columns Km, kcat, kcat/Km.

raw_value_unit_evidence: Table 2 row H-Ala-Pro-pNA: Km 120 uM; kcat 40 s^-1; kcat/Km 0.33 s^-1 uM^-1.

row_label: H-Ala-Pro-pNA


column_label: PDF page 4 Table 2, row H-Arg-Pro-pNA, columns Km, kcat, kcat/Km.

raw_value_unit_evidence: Table 2 row H-Arg-Pro-pNA: Km 310 uM; kcat 12.8 s^-1; kcat/Km 0.04 s^-1 uM^-1.

row_label: H-Arg-Pro-pNA


column_label: PDF page 4 Table 2, row H-Asp-Pro-pNA, columns Km, kcat, kcat/Km.

raw_value_unit_evidence: Table 2 row H-Asp-Pro-pNA: Km 2050 uM; kcat 1.6 s^-1; kcat/Km 0.0008 s^-1 uM^-1.

row_label: H-Asp-Pro-pNA


column_label: PDF page 4 Table 2, row H-Gly-Pro-pNA, columns Km, kcat, kcat/Km.

raw_value_unit_evidence: Table 2 row H-Gly-Pro-pNA: Km 480 uM; kcat 62 s^-1; kcat/Km 0.13 s^-1 uM^-1.

row_label: H-Gly-Pro-pNA


enzyme_display_name: beta-peptidyl aminopeptidase

organism: Sphingosinicella microcystinivorans

substrate_name: beta-Ala-p-nitroanilide

enzyme: beta-peptidyl aminopeptidase

substrate: beta-Ala-p-nitroanilide


substrate_name: beta-homoAla-beta-homoLeu

column_label: table Table 3; row H-βhAla-βhLeu-OH; columns kcat, Km, kcat/Km; Table 3 row H-βhAla-βhLeu-OH under Y2 BapA columns; CSV kcat_over_km is quotient precision 60/41.

raw_value_unit_evidence: kcat 60 ± 13 s−1; Km 41 ± 16 mm; kcat/Km 1500 ± 600 m−1·s−1

table_label: Table 3

substrate: beta-homoAla-beta-homoLeu


substrate_name: beta-homoVal-beta-homoAla-beta-homoLeu

column_label: table Table 3; row H-βhVal-βhAla-βhLeu-OH; columns kcat, Km, kcat/Km; Table 3 row H-βhVal-βhAla-βhLeu-OH under Y2 BapA columns.

raw_value_unit_evidence: kcat 4.3 ± 1.1 s−1; Km 39 ± 15 mm; kcat/Km 110 ± 50 m−1·s−1

substrate: beta-homoVal-beta-homoAla-beta-homoLeu


enzyme_display_name: intermediate cleaving peptidase 55

organism: Saccharomyces cerevisiae

substrate_name: Met-Pro-Ala

column_label: Table 2 columns Km (mM), kcat (s^-1), kcat/Km (10^3 M^-1 s^-1); row MPA.

normalized_value_unit_evidence: Km 2.0 mM; kcat 25.7 s^-1; explicit kcat/Km 12.8 s^-1 mM^-1.

row_label: Icp55t1 / MPA (Met-Pro-Ala)

table_label: Table 2: Enzyme kinetics

enzyme: intermediate cleaving peptidase 55

substrate: Met-Pro-Ala


substrate_name: Tyr-Ala-Ala

column_label: Table 2 columns Km (mM), kcat (s^-1), kcat/Km (10^3 M^-1 s^-1); row YAA.

normalized_value_unit_evidence: Km 0.72 mM; kcat 1.4 s^-1; explicit kcat/Km 1.94 s^-1 mM^-1.

row_label: Icp55t1 / YAA (Tyr-Ala-Ala)

substrate: Tyr-Ala-Ala


substrate_name: Tyr-Pro-Ala

column_label: Table 2 columns Km (mM), kcat (s^-1), kcat/Km (10^3 M^-1 s^-1); row YPA.

normalized_value_unit_evidence: Km 1.8 mM; kcat 14.0 s^-1; explicit kcat/Km 7.78 s^-1 mM^-1.

row_label: Icp55t1 / YPA (Tyr-Pro-Ala)

substrate: Tyr-Pro-Ala


organism: Sphingosinicella xenopeptidilytica


column_label: table Table 3; row H-βhAla-βhLeu-OH; columns kcat, Km, kcat/Km; Table 3 row H-βhAla-βhLeu-OH under 3-2W4 BapA columns; CSV kcat_over_km is quotient precision 12/20.

raw_value_unit_evidence: kcat 12 ± 2 s−1; Km 20 ± 7 mm; kcat/Km 590 ± 240 m−1·s−1


column_label: table Table 3; row H-βhVal-βhAla-βhLeu-OH; columns kcat, Km, kcat/Km; Table 3 row H-βhVal-βhAla-βhLeu-OH under 3-2W4 BapA columns; CSV kcat_over_km is quotient precision 6/9.

normalized_value_unit_evidence: kcat 6 s^-1; Km 9 mM; kcat/Km 0.67 s^-1 mM^-1

raw_value_unit_evidence: kcat 6.0 ± 0.2 s−1; Km 9.0 ± 0.8 mm; kcat/Km 670 ± 70 m−1·s−1


enzyme_display_name: tripeptidyl-peptidase I

column_label: Paper Table 1 columns Peptide | kcat (s)^-1 | KM (uM) | kcat/KM (mM s)^-1; row NH2-KWF[cleavage]FIQ-EDDnp has 2.0 +/- 0.1 | 0.70 +/- 0.04 | 2857.

table_label: Table 1. Hydrolysis of synthetic peptides exploring amino and endopeptidase activities.

enzyme: tripeptidyl-peptidase I


column_label: Paper Table 1 columns Peptide | kcat (s)^-1 | KM (uM) | kcat/KM (mM s)^-1; row NH2-RWF[cleavage]FIQ-EDDnp has 5.04 +/- 0.04 | 0.70 +/- 0.07 | 7200.


column_label: Paper Table 1 columns Peptide | kcat (s)^-1 | KM (uM) | kcat/KM (mM s)^-1; row NH2-RWF[cleavage]VIQ-EDDnp has 1.5 +/- 0.2 | 0.55 +/- 0.04 | 2727.


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

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D341N to reconstruct the assayed variant sequence.

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


enzyme_display_name: UniProt Q9AGA6

organism: Klebsiella pneumoniae

substrate_name: trehalose 6-phosphate

source_db: skid

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

source_databases_merged: skid uniprot

enzyme: UniProt Q9AGA6

substrate: trehalose 6-phosphate

source: skid


substrate_name: maltose 6'-phosphate

substrate: maltose 6'-phosphate


enzyme_display_name: Prolyl endopeptidase FAP

substrate_name: Ala-Pro (Dipeptidyl peptidase activity)

column_label: Results prose reports Ala-Pro-AFC (Km = 0.46 +/- 0.04 mM), not the exported 0.24 mM value.

raw_value_unit_evidence: Km raw_value=0.46 raw_unit=mM

row_label: FAPmCD8 substrate preference; Ala-Pro-AFC

table_label: Results prose, FAP Is a Dipeptidyl Peptidase

enzyme: Prolyl endopeptidase FAP

substrate: Ala-Pro (Dipeptidyl peptidase activity)


substrate_name: Lys-Pro (Dipeptidyl peptidase activity)

column_label: Results prose reports Lys-Pro-AFC (Km = 0.9 +/- 0.24 mM) in the same substrate comparison as Ala-Pro-AFC and Gly-Pro-AFC.

raw_value_unit_evidence: Km raw_value=0.9 raw_unit=mM

row_label: FAPmCD8 substrate preference; Lys-Pro-AFC

substrate: Lys-Pro (Dipeptidyl peptidase activity)


substrate_name: Gly-Pro (Dipeptidyl peptidase activity)

substrate: Gly-Pro (Dipeptidyl peptidase activity)


enzyme_display_name: leukotriene-A4 hydrolase

substrate_name: Leukotriene A4

proof_lines:
PMID 9287304
Mus musculus
leukotriene A4 hydrolase

enzyme: leukotriene-A4 hydrolase

substrate: Leukotriene A4


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

proof_lines:
PMID 9287304
Mus musculus
Y383Q


enzyme_display_name: Transferred entry: 3.13.2.1

organism: Thermotoga maritima

substrate_name: S-Adenosyl-L-homocysteine

enzyme: Transferred entry: 3.13.2.1

substrate: S-Adenosyl-L-homocysteine


substrate_name: S-Inosyl-L-homocysteine

substrate: S-Inosyl-L-homocysteine


enzyme_display_name: peptidyl-dipeptidase A

organism: Struthio camelus australis

enzyme: peptidyl-dipeptidase A


enzyme_display_name: endoglycosylceramidase

organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)

substrate_name: D-erythro-sphingosine

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

enzyme: endoglycosylceramidase

substrate: D-erythro-sphingosine


substrate_name: D-erythro-dihydrosphingosine

smiles: CCCCCCCCCCCCCCCC(C(CO)N)O

substrate: D-erythro-dihydrosphingosine


enzyme_display_name: 7-dimethylallyltryptophan synthase

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

substrate_name: dimethylallyl diphosphate

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

enzyme: 7-dimethylallyltryptophan synthase

substrate: dimethylallyl diphosphate


substrate_name: L-tryptophan

substrate: L-tryptophan


enzyme_display_name: Epoxide hydrolase 1

organism: Rattus norvegicus

substrate_name: styrene 7,8-oxide

enzyme: Epoxide hydrolase 1

substrate: styrene 7,8-oxide


substrate_name: 9,10-epoxystearic acid

substrate: 9,10-epoxystearic acid


enzyme_display_name: Tryprostatin B synthase ftmPT1

substrate_name: brevianamide F

enzyme: Tryprostatin B synthase ftmPT1

substrate: brevianamide F


column_label: Table 3 columns: FtmPT1 Km [mM], kcat [s^-1], kcat/Km [mM^-1 s^-1], ratio kcat/Km; row: l-tryptophan.

normalized_value_unit_evidence: Km 0.82 mM matches expected export Km 0.82 mM.

raw_value_unit_evidence: Table 3 l-tryptophan row under FtmPT1 reports Km 0.82 mM, kcat 0.12 s^-1, and kcat/Km 0.15 mM^-1 s^-1.

row_label: FtmPT1 / l-tryptophan

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


enzyme_display_name: Cyclic dipeptide prenyltransferase

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

enzyme: Cyclic dipeptide prenyltransferase


enzyme_display_name: Fumigaclavine A dimethylallyltransferase easL

substrate_name: fumigaclavine A

column_label: Abstract reports Km(app) values for fumigaclavine A and dimethylallyl diphosphate were 6 and 13 microM, respectively.

raw_value_unit_evidence: Km raw_value=6 microM raw_unit=microM

row_label: FgaPT1 / fumigaclavine A

table_label: PubMed XML abstract PMID 16397874

substrate: fumigaclavine A


enzyme: Fumigaclavine A dimethylallyltransferase easL


enzyme_display_name: D-stereospecific aminopeptidase

organism: Aspergillus oryzae

substrate_name: D-Ala 4-nitroanilide

proof_lines:
GdaA
Aspergillus oryzae
D-stereospecific aminopeptidase

enzyme: D-stereospecific aminopeptidase

substrate: D-Ala 4-nitroanilide


substrate_name: Gly 4-nitroanilide

substrate: Gly 4-nitroanilide


enzyme_display_name: methionyl aminopeptidase

organism: Escherichia coli

substrate_name: Met-Gly-Met-Met

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H178A to reconstruct the assayed variant sequence.

proof_lines:
H178A EcMetAP-I
WT EcMetAP-I
MGMM

enzyme: methionyl aminopeptidase

substrate: Met-Gly-Met-Met


proof_lines:
WT EcMetAP-I
H178A EcMetAP-I
MGMM


enzyme_display_name: aminopeptidase I

substrate_name: Ala-Gly-Gly

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

proof_lines:
aminopeptidase I
EC 3.4.11.1

enzyme: aminopeptidase I

substrate: Ala-Gly-Gly


substrate_name: Ala-Gly

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

substrate: Ala-Gly


organism: Bacillus sp.

substrate_name: D-Alanine-p-nitroanilide

substrate: D-Alanine-p-nitroanilide


substrate_name: Glycine-p-nitroanilide

substrate: Glycine-p-nitroanilide


enzyme_display_name: aminopeptidase Ey

organism: Gallus gallus

proof_lines:
Aminopeptidase Ey
Gallus gallus domesticus
Leu-Pro-Leu-Arg-PheNH2

enzyme: aminopeptidase Ey


enzyme_display_name: Aminopeptidase Ey

substrate_name: fMet-Leu-Phe

enzyme: Aminopeptidase Ey

substrate: fMet-Leu-Phe


enzyme_display_name: PepB aminopeptidase

substrate_name: L-Cysteinylglycine

enzyme: PepB aminopeptidase

substrate: L-Cysteinylglycine


substrate_name: L-Leucylglycine

substrate: L-Leucylglycine


enzyme_display_name: lysosomal Pro-Xaa carboxypeptidase

organism: Stenotrophomonas maltophilia

substrate_name: N-benzyloxycarbonyl-L-Pro-Leu

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

enzyme: lysosomal Pro-Xaa carboxypeptidase

substrate: N-benzyloxycarbonyl-L-Pro-Leu


substrate_name: angiotensin II

substrate: angiotensin II


enzyme_display_name: carboxypeptidase B

organism: Struthio camelus

substrate_name: hippuryl-Lys

proof_lines:
ostrich carboxypeptidase B
hipp-lys

enzyme: carboxypeptidase B

substrate: hippuryl-Lys


substrate_name: furylacryloylalanyllysine

proof_lines:
ostrich carboxypeptidase B
FAAL

substrate: furylacryloylalanyllysine


substrate_name: hippuryl-L-Arg

proof_lines:
ostrich carboxypeptidase B
hipp-arg

substrate: hippuryl-L-Arg


substrate_name: furylacryloylalanylarginine

proof_lines:
ostrich carboxypeptidase B
FAAA

substrate: furylacryloylalanylarginine


substrate_name: hippuryl-Arg

substrate: hippuryl-Arg


organism: Penicillium janthinellum

substrate_name: myoglobin

proof_lines: Michaelis-Menten kinetics in the bulk solution

substrate: myoglobin


enzyme_display_name: carboxypeptidase C

organism: Citrus sp.

substrate_name: benzyloxycarbonyl-Leu-Phe

enzyme: carboxypeptidase C

substrate: benzyloxycarbonyl-Leu-Phe


enzyme_display_name: beta-peptidyl aminopeptidase

organism: Sphingosinicella microcystinivorans

substrate_name: beta-homoAla-p-nitroanilide

proof_lines:
Sphingosinicella microcystinivorans
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: carboxypeptidase D

organism: Drosophila melanogaster

substrate_name: dansyl-Phe-Ala-Arg

proof_lines:
pH 5.7, 37°C, domain 2
pH 7.4, 37°C, domain 1B

enzyme: carboxypeptidase D

substrate: dansyl-Phe-Ala-Arg


organism: Monascus pilosus

substrate_name: benzyloxycarbonyl-Tyr-Glu

proof_lines:
pH 4.0, 37°C, isoenzyme MpiCP-1
pH 3.5, 37°C, isoenzyme MpiCP-2

substrate: benzyloxycarbonyl-Tyr-Glu


enzyme_display_name: carboxypeptidase A

organism: Aspergillus niger

substrate_name: ochratoxin A

enzyme: carboxypeptidase A

substrate: ochratoxin A


organism: Homo sapiens

substrate_name: dansyl-L-Ala-L-Arg

substrate: dansyl-L-Ala-L-Arg


organism: Mammalia

substrate_name: Ac-Phe-ThiaPhe

substrate: Ac-Phe-ThiaPhe


organism: Penaeus setiferus


substrate_name: hippuryl-L-Phe

substrate: hippuryl-L-Phe


organism: Patella vulgata

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Rattus norvegicus

sequence_source: multiple

column_label: Table 1 row Km (uM); column Nb2 CPD-N; substrate dansyl-L-alanyl-L-arginine.

raw_value_unit_evidence: Table 1 row Km (uM), column Nb2 CPD-N: 132.0 +/- 30.0 uM.

row_label: Km (uM)

table_label: Table 1. CPD/CPD-N kinetics with dansyl-L-alanyl-L-arginine as substrate


organism: Squalus acanthias

substrate_name: carbobenzoxy-Gly-L-Phe

substrate: carbobenzoxy-Gly-L-Phe


organism: Sus scrofa

substrate_name: carbobenzoxy-Gly-L-Leu

substrate: carbobenzoxy-Gly-L-Leu


organism: Trypanosoma cruzi

proof_lines:
in the absence of Co2+
in the presence of Co2+


organism: Salaria basilisca


organism: Asterias amurensis

substrate_name: benzoyl-Gly-Arg

substrate: benzoyl-Gly-Arg


organism: Anopheles stephensi

substrate_name: hippuryl-L-Arg

assay_conditions_summary: pH 8

substrate: hippuryl-L-Arg


organism: Bacillus subtilis

substrate_name: H2O; Nalpha-Acetyl-L-Lys-D-Ala-D-Ala

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

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

substrate: H2O; Nalpha-Acetyl-L-Lys-D-Ala-D-Ala


organism: Enterococcus hirae

substrate_name: (Ac)2-L-Lys-D-Ala-D-Ala; H2O

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

substrate: (Ac)2-L-Lys-D-Ala-D-Ala; H2O


organism: Escherichia coli


substrate_name: H2O; Phenyl-lactyl benzoylaminoacetate

substrate: H2O; Phenyl-lactyl benzoylaminoacetate


organism: Geobacillus stearothermophilus


organism: Ochrobactrum anthropi


organism: Mus musculus

proof_lines: in 100% mouse plasma, pH not specified in the publication, temperature not specified in the publication


organism: Actinomadura sp.

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

source_databases_merged: sabio_rk brenda skid


enzyme_display_name: Penicillin-binding protein 2a

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

substrate_name: dansylated lipid II

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

enzyme: Penicillin-binding protein 2a

substrate: dansylated lipid II


organism: Streptomyces sp.

substrate_name: benzoyl-Gly-thioglycolate

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

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

substrate: benzoyl-Gly-thioglycolate


substrate_name: benzoyl-Gly-thiolactate

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

substrate: benzoyl-Gly-thiolactate


enzyme_display_name: Carboxypeptidase Y

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: furylacryloyl-Phe-Leu-OH

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

enzyme: Carboxypeptidase Y

substrate: furylacryloyl-Phe-Leu-OH


organism: Rattus norvegicus

substrate_name: H2O; Carbobenzoxy-Gly-Gly-Phe

substrate: H2O; Carbobenzoxy-Gly-Gly-Phe


organism: Protopterus aethiopicus

substrate_name: benzoyl-Gly-L-Arg

sequence: EPTPRSFNGDKVFRV

wild_type_sequence: EPTPRSFNGDKVFRV

substrate: benzoyl-Gly-L-Arg


organism: Helicoverpa armigera

substrate_name: Carbobenzoxy-Gly-Gly-Leu

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

substrate: Carbobenzoxy-Gly-Gly-Leu


substrate_name: Carbobenzoxy-Gly-Gly-Phe

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

substrate: Carbobenzoxy-Gly-Gly-Phe


substrate_name: Carbobenzoxy-Gly-Gly-Val

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

substrate: Carbobenzoxy-Gly-Gly-Val


substrate_name: Carbobenzoxy-Gly-Phe

proof_lines:
Helicoverpa armigera
carboxypeptidase A
Carbobenzoxy-Gly-Phe

substrate: Carbobenzoxy-Gly-Phe


substrate_name: Carboxymethylbenzoylaminothioacetate

column_label: Table 6, enzyme block 'TEM-1', row 'WT', thiolester-substrate column group (paper label given in the captured segment): kcat column = 20 + 2; Km column = 3800 + 500 (uM); kcat/Km column = 5.2 + 0.8 (mM-1 s-1).

normalized_value_unit_evidence: kcat: printed Table 6 cell 20 (S2a, TEM-1 WT); no unit conversion, value already s-1; exported value 20.0 s-1. Km: printed Table 6 cell 3800 uM; 3800 / 1000 = 3.8 mM; exported value 3.8 mM. kcat/Km: derived as the exact quotient of the paper's own kcat and Km cells, 20 / 3.8 = 5.263157894736842 s-1 mM-1, matching the exported kcat_over_km; the paper's own printed cell rounds to 5.2 at its own one-decimal precision, consistent with this quotient.

raw_value_unit_evidence: Table 6, TEM-1 block, WT row, S2a (thiolester): kcat = 20 + 2; Km = 3800 + 500 (uM); printed kcat/Km = 5.2 + 0.8 (mM-1 s-1).

row_label: Table 6, TEM-1 block, WT row, thiolester-substrate columns

table_label: Table 6: Kinetic parameters for the acyclic depsipeptides with the WT and mutant enzymes (Biochem. J. 1994, 301:485-494)

substrate: Carboxymethylbenzoylaminothioacetate


substrate_name: Phenyl-lactyl benzoylaminoacetate

column_label: Table 6, enzyme block 'AmpC', row 'WT', substrate column group 'Sle (ester)': kcat column = 30 + 1; Km column = 1320 + 100 (uM); kcat/Km column = 22.7 + 0.3 (mM-1 s-1).

normalized_value_unit_evidence: kcat: printed Table 6 cell 30 (Sle, AmpC WT); no unit conversion, value already s-1; exported value 30.0 s-1. Km: printed Table 6 cell 1320 uM; 1320 / 1000 = 1.32 mM; exported value 1.32 mM. kcat/Km: derived as the exact quotient of the paper's own kcat and Km cells, 30 / 1.32 = 22.727272727272727 s-1 mM-1, matching the exported kcat_over_km; the paper's own printed cell rounds to 22.7 at its own one-decimal precision, consistent with this quotient.

raw_value_unit_evidence: Table 6, AmpC block, WT row, Sle (ester): kcat = 30 + 1; Km = 1320 + 100 (uM); printed kcat/Km = 22.7 + 0.3 (mM-1 s-1).

row_label: Table 6, AmpC block, WT row, Sle (ester) columns

substrate: Phenyl-lactyl benzoylaminoacetate


column_label: Table 6, enzyme block 'TEM-1', row 'WT', substrate column group 'Sle (ester)': kcat column = 0.10 + 0.01; Km column = 1920 + 250 (uM); kcat/Km column = 0.052 + 0.008 (mM-1 s-1).

normalized_value_unit_evidence: kcat: printed Table 6 cell 0.10 (Sle, TEM-1 WT); no unit conversion, value already s-1; exported value 0.1 s-1. Km: printed Table 6 cell 1920 uM; 1920 / 1000 = 1.92 mM; exported value 1.92 mM. kcat/Km: derived as the exact quotient of the paper's own kcat and Km cells, 0.10 / 1.92 = 0.052083333333333336 s-1 mM-1, matching the exported kcat_over_km; the paper's own printed cell rounds to 0.052 at its own three-decimal precision, consistent with this quotient.

row_label: Table 6, TEM-1 block, WT row, Sle (ester) columns


enzyme_display_name: Maltose-6'-phosphate glucosidase

organism: Bacillus subtilis (strain 168)

assay_conditions_summary: pH 8.4; cofactor NAD+

enzyme: Maltose-6'-phosphate glucosidase


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

assay_conditions_summary: pH 7

proof_lines:
AbnA
Bacillus subtilis strain 168
endo-arabinanase


enzyme_display_name: leukotriene-A4 hydrolase

substrate_name: leukotriene A4

source_databases_merged: brenda uniprot

enzyme: leukotriene-A4 hydrolase

substrate: leukotriene A4


enzyme_display_name: Tripeptidyl-peptidase sed2

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

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

enzyme: Tripeptidyl-peptidase sed2

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


enzyme_display_name: UniProt Q04609

organism: Homo sapiens

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

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt Q04609

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


enzyme_display_name: UniProt P39377

substrate_name: beta-Asp-Phe

enzyme: UniProt P39377

substrate: beta-Asp-Phe


substrate_name: beta-Asp-His

substrate: beta-Asp-His


substrate_name: beta-Asp-Gly

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

substrate: beta-Asp-Gly


substrate_name: alpha-Asp-Leu

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

substrate: alpha-Asp-Leu


enzyme_display_name: UniProt Q484B6

organism: Colwellia psychrerythraea

enzyme: UniProt Q484B6


substrate_name: beta-Asp-Leu

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

substrate: beta-Asp-Leu


substrate_name: beta-Ala-Ala

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

substrate: beta-Ala-Ala


enzyme_display_name: UniProt O25743

organism: Helicobacter pylori

substrate_name: L-glutamine

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

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

enzyme: UniProt O25743

substrate: L-glutamine


substrate_name: glutathione

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

substrate: glutathione


enzyme_display_name: UniProt P00766

organism: Bos taurus

enzyme: UniProt P00766


substrate_name: 4-nitrophenyl benzoate

substrate: 4-nitrophenyl benzoate


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

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


substrate_name: N-benzoyl-L-tyrosine ethyl ester

substrate: N-benzoyl-L-tyrosine ethyl ester


enzyme_display_name: chymotrypsin

substrate_name: 4-nitrophenyl acetate

enzyme: chymotrypsin

substrate: 4-nitrophenyl acetate


enzyme_display_name: UniProt P00775

organism: Streptomyces griseus

enzyme: UniProt P00775


enzyme_display_name: UniProt P00734

substrate_name: Fibrinopeptide A

enzyme: UniProt P00734

substrate: Fibrinopeptide A


enzyme_display_name: UniProt P98073

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

enzyme: UniProt P98073


substrate_name: Z-Lys-SBzl

substrate: Z-Lys-SBzl


enzyme_display_name: cucumisin

organism: Cucumis melo

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

enzyme: cucumisin

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


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

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


enzyme_display_name: UniProt Q9X6R4

organism: Aeromonas caviae

enzyme: UniProt Q9X6R4


enzyme_display_name: leukocyte elastase

enzyme: leukocyte elastase


enzyme_display_name: subtilisin

organism: Bacillus lentus

substrate_name: Peptidyl-p-nitroanilide

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

enzyme: subtilisin

substrate: Peptidyl-p-nitroanilide


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


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


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


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


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


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


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


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


enzyme_display_name: peptidase K

organism: Parengyodontium album

substrate_name: benzoyl-L-Arg ethyl ester

enzyme: peptidase K

substrate: benzoyl-L-Arg ethyl ester


enzyme_display_name: UniProt P04070

substrate_name: spectrozyme PCa

enzyme: UniProt P04070

substrate: spectrozyme PCa


enzyme_display_name: Thermomycolin

organism: Malbranchea pulchella

substrate_name: Acetyl-Ala-Ala-Ala methyl ester

enzyme: Thermomycolin

substrate: Acetyl-Ala-Ala-Ala methyl ester


enzyme_display_name: Pancreatic endopeptidase E

organism: Sus scrofa

substrate_name: Benzoyl-L-alanine methyl ester

enzyme: Pancreatic endopeptidase E

substrate: Benzoyl-L-alanine methyl ester


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

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


enzyme_display_name: Endopeptidase So

organism: Escherichia coli

substrate_name: casein

enzyme: Endopeptidase So

substrate: casein


substrate_name: Unknown

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

substrate: Unknown


enzyme_display_name: Thermitase

organism: Coprothermobacter proteolyticus

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

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

enzyme: Thermitase


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

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

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


enzyme_display_name: protein C (activated)

enzyme: protein C (activated)


enzyme_display_name: IgA-specific serine endopeptidase

organism: Streptococcus sanguinis

substrate_name: IgA

enzyme: IgA-specific serine endopeptidase

substrate: IgA


enzyme_display_name: t-Plasminogen activator

organism: synthetic construct

proof_lines: recombinant tPA bound to polyacrylic acid-coated magnetite

enzyme: t-Plasminogen activator


organism: Prevotella melaninogenica


substrate_name: Acetyl-tri-L-alanine methyl ester

substrate: Acetyl-tri-L-alanine methyl ester


substrate_name: Lys-plasminogen

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

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

substrate: Lys-plasminogen


organism: Mus musculus


enzyme_display_name: activated protein C (thrombin-activated peptidase)

organism: Homo sapiens

substrate_name: SpPCa

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

substrate: SpPCa


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

enzyme: activated protein C (thrombin-activated peptidase)


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


enzyme_display_name: thermitase

enzyme: thermitase


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

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

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


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

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


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

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


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

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


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


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


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

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


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

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


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

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


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


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


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

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


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


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


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

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


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

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


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

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


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

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


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

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

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

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


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


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


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


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


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


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


substrate_name: spectrozyme tPA

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

substrate: spectrozyme tPA


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


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


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


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


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


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


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


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


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


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

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


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


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


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

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


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


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


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


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


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


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


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


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


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


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


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


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


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


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


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


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


substrate_name: plasminogen

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

substrate: plasminogen


enzyme_display_name: myeloblastin

enzyme: myeloblastin


enzyme_display_name: Pancreatic elastase II

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

enzyme: Pancreatic elastase II

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


organism: Haemophilus influenzae


enzyme_display_name: oligopeptidase B

organism: Unknown

source_db: unknown

source_license: see source

enzyme: oligopeptidase B

source: unknown


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


enzyme_display_name: signal peptidase I

enzyme: signal peptidase I


enzyme_display_name: cytosol alanyl aminopeptidase

enzyme: cytosol alanyl aminopeptidase


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


substrate_name: Factor VaR506Q

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

substrate: Factor VaR506Q


enzyme_display_name: thymine-DNA glycosylase

substrate_name: thymine-mismatched double-stranded DNA

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

enzyme: thymine-DNA glycosylase

substrate: thymine-mismatched double-stranded DNA


enzyme_display_name: aspartyl aminopeptidase

substrate_name: Asp-Ala-Pro-sulfamethoxazole

enzyme: aspartyl aminopeptidase

substrate: Asp-Ala-Pro-sulfamethoxazole


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

proof_lines: extracted from human glioblastoma cells LNZ308


enzyme_display_name: membrane dipeptidase

substrate_name: glycyldehydrophenylalanine

enzyme: membrane dipeptidase

substrate: glycyldehydrophenylalanine


enzyme_display_name: methionyl aminopeptidase

organism: Klebsiella pneumoniae

enzyme: methionyl aminopeptidase


enzyme_display_name: Xaa-Pro dipeptidyl-peptidase

organism: Lactococcus lactis

substrate_name: Gly-Pro-Gly-Gly

enzyme: Xaa-Pro dipeptidyl-peptidase

substrate: Gly-Pro-Gly-Gly


organism: Lactobacillus helveticus

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

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


enzyme_display_name: microsomal epoxide hydrolase

organism: Manduca sexta

substrate_name: juvenile hormone III

enzyme: microsomal epoxide hydrolase

substrate: juvenile hormone III


enzyme_display_name: tripeptidyl-peptidase II

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

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

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

enzyme: tripeptidyl-peptidase II

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


organism: Neisseria gonorrhoeae


enzyme_display_name: dipeptidyl-peptidase IV

enzyme: dipeptidyl-peptidase IV


organism: Oryctolagus cuniculus

substrate_name: glycoprotein IV from ovalbumin

assay_conditions_summary: pH 6

substrate: glycoprotein IV from ovalbumin


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

organism: Phanerodontia chrysosporium

substrate_name: p-nitrophenyl-beta-D-cellobioside

substrate: p-nitrophenyl-beta-D-cellobioside


organism: Plasmodium falciparum

substrate_name: Met-peptide

substrate: Met-peptide


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


enzyme_display_name: Genome polyprotein

organism: Hepatitis GB virus B

substrate_name: ATP for NS3 NTPase

enzyme: Genome polyprotein

substrate: ATP for NS3 NTPase


substrate_name: CTP for NS3 NTPase

substrate: CTP for NS3 NTPase


substrate_name: UTP for NS3 NTPase

substrate: UTP for NS3 NTPase


substrate_name: dATP for NS3 NTPase

substrate: dATP for NS3 NTPase


substrate_name: dCTP for NS3 NTPase

substrate: dCTP for NS3 NTPase


substrate_name: dTTP for NS3 NTPase

substrate: dTTP for NS3 NTPase


substrate_name: Met-Gly-Met-Met

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

substrate: Met-Gly-Met-Met


enzyme_display_name: prunasin beta-glucosidase

organism: Prunus serotina

substrate_name: Unknown

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

enzyme: prunasin beta-glucosidase

substrate: Unknown


organism: Rattus norvegicus


enzyme_display_name: amygdalin beta-glucosidase

substrate_name: (R)-amygdalin

proof_lines:
AH II'
AH II
AH I

enzyme: amygdalin beta-glucosidase

substrate: (R)-amygdalin


substrate_name: cis-stilbene oxide

substrate: cis-stilbene oxide


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

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

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


substrate_name: styrene oxide

substrate: styrene oxide


enzyme_display_name: tripeptidyl-peptidase I

assay_conditions_summary: pH 4

enzyme: tripeptidyl-peptidase I


organism: Saccharomyces cerevisiae

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

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

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


substrate_name: angiotensin I

substrate: angiotensin I


enzyme_display_name: lysoplasmalogenase

substrate_name: lysoplasmenylcholine

assay_conditions_summary: pH 7.1; cofactor NADH

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

enzyme: lysoplasmalogenase

substrate: lysoplasmenylcholine


organism: Streptococcus pneumoniae

substrate_name: L-Met 4-nitroanilide

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

substrate: L-Met 4-nitroanilide


enzyme_display_name: carboxypeptidase C

substrate_name: endothelin

enzyme: carboxypeptidase C

substrate: endothelin


enzyme_display_name: endo-alpha-N-acetylgalactosaminidase

enzyme: endo-alpha-N-acetylgalactosaminidase


organism: Streptomyces sp.

substrate_name: benzoyl-Gly-thiolactate

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

substrate: benzoyl-Gly-thiolactate


substrate_name: L-methionine 4-nitroanilide

substrate: L-methionine 4-nitroanilide


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


organism: Sus scrofa

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


organism: Streptococcus thermophilus


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

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


substrate_name: Gly-Pro-Met 2-naphthylamide

substrate: Gly-Pro-Met 2-naphthylamide


enzyme_display_name: lysosomal Pro-Xaa carboxypeptidase

substrate_name: N-benzyloxycarbonyl-Pro-Phe

enzyme: lysosomal Pro-Xaa carboxypeptidase

substrate: N-benzyloxycarbonyl-Pro-Phe


substrate_name: Glu 2-naphthylamide

substrate: Glu 2-naphthylamide


substrate_name: glycyldehydrophenylalanine

substrate: glycyldehydrophenylalanine


substrate_name: Gly-D-Phe

substrate: Gly-D-Phe


enzyme_display_name: cytosol nonspecific dipeptidase

substrate_name: carnosine

enzyme: cytosol nonspecific dipeptidase

substrate: carnosine


organism: Thermoascus aurantiacus

substrate_name: 4-nitrophenyl beta-D-cellobioside

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

substrate: 4-nitrophenyl beta-D-cellobioside


enzyme_display_name: aspartyl aminopeptidase

organism: Toxoplasma gondii

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

enzyme: aspartyl aminopeptidase


organism: Vibrio cholerae

proof_lines: pH and temperature not specified in the publication


organism: Streptococcus pyogenes


organism: Bacillus subtilis


organism: Enterococcus hirae


enzyme_display_name: UniProt O15393

organism: Homo sapiens

enzyme: UniProt O15393


enzyme_display_name: papain

organism: Carica papaya

substrate_name: N-benzoylglycinamide

enzyme: papain

substrate: N-benzoylglycinamide


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

organism: Beta vulgaris

substrate_name: sucrose

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

substrate: sucrose


enzyme_display_name: methionyl aminopeptidase

organism: Vibrio coralliilyticus

enzyme: methionyl aminopeptidase


enzyme_display_name: kumamolysin

organism: Bacillus novosp.

enzyme: kumamolysin


organism: Alicyclobacillus sendaiensis

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


enzyme_display_name: cathepsin B

organism: Artemia sp.

enzyme: cathepsin B


organism: Capra aegagrus

proof_lines:
free enzyme
encapsulated enzyme


organism: Heyndrickxia coagulans


organism: Dorytheuthis bleekeri

substrate_name: benzoyl-DL-Arg-beta-naphthylamide

substrate: benzoyl-DL-Arg-beta-naphthylamide


substrate_name: IQF peptide

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

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

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

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

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

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

substrate: IQF peptide


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


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

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

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

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

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


organism: Heliocidaris crassispina


organism: Fasciola hepatica


organism: Hemicentrotus pulcherrimus


organism: Meretrix meretrix


organism: Fasciola gigantica


organism: Nicotiana benthamiana

substrate_name: Abz-GIVRAK-Dnp

substrate: Abz-GIVRAK-Dnp


organism: Schistosoma mansoni


organism: Sus scrofa

proof_lines:
isoenzyme II
isoenzyme I
isoenzyme I and isoenzyme II


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

proof_lines:
isoenzyme I
isoenzyme II

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


organism: Bubalus bubalis

substrate_name: hemoglobin

substrate: hemoglobin


enzyme_display_name: ficain

organism: Ficus insipida

enzyme: ficain


organism: Alphacoronavirus

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

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


organism: Ficus johannis

substrate_name: casein

substrate: casein


organism: Tetrahymena pyriformis


organism: Ficus pumila var. awkeotsang

substrate_name: azocasein

substrate: azocasein


enzyme_display_name: Papain

organism: Carica papaya

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

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

enzyme: Papain

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


organism: Naegleria fowleri


organism: Rattus norvegicus

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

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

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


enzyme_display_name: Kumamolisin

organism: Bacillus sp. (strain MN-32)

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

enzyme: Kumamolisin


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


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


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


substrate_name: Boc-L-His

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

substrate: Boc-L-His


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

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

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

source_databases_merged: sabio_rk brenda skid uniprot


organism: Trichinella spiralis

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

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


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

row_label: NbCathB; Abz-FRF(NO2)A

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


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

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

row_label: NbCathB; Abz-GIVRAK(Dnp)


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

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

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

row_label: NbCathB; Z-Arg-Arg-MCA


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

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

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

row_label: NbCathB; Z-Phe-Arg-MCA


organism: Homo sapiens


substrate_name: Z-Arg-Arg-p-nitroanilide

substrate: Z-Arg-Arg-p-nitroanilide


organism: Meretrix meretrix


organism: Oryctolagus cuniculus


substrate_name: gelatin

substrate: gelatin


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

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

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


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


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


substrate_name: Z-Arg-Arg-AMC

proof_lines: pH 4.6, temperature not specified in the publication

proof_lines: pH 7.2, temperature not specified in the publication

substrate: Z-Arg-Arg-AMC


substrate_name: Z-Nle-Lys-Arg-AMC

substrate: Z-Nle-Lys-Arg-AMC


substrate_name: Z-Phe-Arg-AMC

substrate: Z-Phe-Arg-AMC


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


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


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


organism: Bos taurus


organism: Ficus carica

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

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

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


organism: Cyprinus carpio


organism: Ficus sp.

substrate_name: p-nitrophenyl N-acetylglycinate

proof_lines:
ficin II
ficin III

substrate: p-nitrophenyl N-acetylglycinate


substrate_name: benzoyl-DL-Arg-p-nitroanilide

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

substrate: benzoyl-DL-Arg-p-nitroanilide


enzyme_display_name: cathepsin S

enzyme: cathepsin S


enzyme_display_name: picornain 3C

organism: Hepatovirus A

proof_lines: pH and temperature not specified in the publication

enzyme: picornain 3C


enzyme_display_name: cancer procoagulant

enzyme: cancer procoagulant


organism: Rhinovirus B14

substrate_name: MBP-LEVLFQ-C

substrate: MBP-LEVLFQ-C


substrate_name: MBP-LEVLFQ-Q

substrate: MBP-LEVLFQ-Q


organism: Platyrrhini

substrate_name: Unknown

assay_conditions_summary: pH 5

substrate: Unknown


organism: Avihepatovirus A


enzyme_display_name: Stem bromelain

organism: Ananas comosus

substrate_name: Tosyl-L-Lys methyl ester

enzyme: Stem bromelain

substrate: Tosyl-L-Lys methyl ester


substrate_name: benzoyl-L-Arg methyl ester

substrate: benzoyl-L-Arg methyl ester


substrate_name: tosyl-L-Lys ethyl ester

substrate: tosyl-L-Lys ethyl ester


organism: Enterovirus A71


organism: Norwalk virus


organism: Coxsackievirus B3

substrate_name: Dabcyl-KEALFQGPPQFE-Edans; H2O

substrate: Dabcyl-KEALFQGPPQFE-Edans; H2O


organism: SARS coronavirus

substrate_name: Dabcyl-KTSAVLQSGFRKME-Edans; H2O

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

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

row_label: TG-0204998 against SARS-CoV 3CLpro

table_label: Results text and Table 2

substrate: Dabcyl-KTSAVLQSGFRKME-Edans; H2O


organism: Gallus gallus


organism: Southampton virus

proof_lines: pH 8.5, temperature not specified in the publication


organism: tobacco etch virus

substrate_name: TENLYFQSGTRR

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

substrate: TENLYFQSGTRR


organism: Sapelovirus A

substrate_name: Ac-RHSVGATLEALFQGPPVYREIKIS-NH2; H2O

substrate: Ac-RHSVGATLEALFQGPPVYREIKIS-NH2; H2O


enzyme_display_name: picornain 2A

enzyme: picornain 2A


organism: Human rhinovirus 2

substrate_name: TRPIITTA-p-nitroanilide; H2O

substrate: TRPIITTA-p-nitroanilide; H2O


organism: Bos taurus

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


organism: Canis lupus familiaris

proof_lines:
pH 5.0, room temperature
pH 5.0


organism: Rattus norvegicus


organism: Saimiri boliviensis


substrate_name: Dabcyl-ASFMNQSKVRRFE-Edans; H2O

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

substrate: Dabcyl-ASFMNQSKVRRFE-Edans; H2O


substrate_name: H2O; Dabcyl-KTSAVLQSGFRKME-Edans

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

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

table_label: Fig. 1B caption/body

substrate: H2O; Dabcyl-KTSAVLQSGFRKME-Edans


enzyme_display_name: Genome polyprotein

organism: Poliovirus type 1 (strain Mahoney)

substrate_name: ATP

assay_conditions_summary: cofactor ATP

enzyme: Genome polyprotein

substrate: ATP


enzyme_display_name: glycyl endopeptidase

organism: Carica papaya

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

source_databases_merged: sabio_rk brenda uniprot

enzyme: glycyl endopeptidase


organism: Homo sapiens

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


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


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

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


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

mutation_type: deletion


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


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


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

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


organism: Mus musculus

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

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


organism: Aichivirus A


organism: Coxsackievirus

substrate_name: Dabcyl-KTLEALFQGPPVYE-Edans; H2O

substrate: Dabcyl-KTLEALFQGPPVYE-Edans; H2O


organism: Enterovirus A71


organism: coxsackievirus


organism: Coxsackievirus B3

substrate_name: Dabcyl-KTSAVLQSGFRKME-Edans

substrate: Dabcyl-KTSAVLQSGFRKME-Edans


organism: enterovirus


organism: Enterovirus B


organism: Enterovirus D

substrate_name: H2O; Ac-RHSVGATLEALFQGPPVYREIKIS-NH2

substrate: H2O; Ac-RHSVGATLEALFQGPPVYREIKIS-NH2


organism: Erbovirus A

substrate_name: Ac-AKDGGIFAQSRDRHYLVGTV-NH2; H2O

substrate: Ac-AKDGGIFAQSRDRHYLVGTV-NH2; H2O


organism: Hepatitis A virus

substrate_name: Dabcyl-GLRTQSND(Edans)G; H2O

substrate: Dabcyl-GLRTQSND(Edans)G; H2O


organism: Human rhinovirus


organism: Enterovirus C

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

proof_lines: in D2O, in the absence of sodium citrate

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


enzyme_display_name: transmembrane protease serine 2

enzyme: transmembrane protease serine 2


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

column_label: Table 2: Cleavage efficiencies of fluorogenic peptide substrates (Antimicrobial Agents and Chemotherapy 2015, 59(4):1827-1836); peptide row 'P07', column 'Sequence' = NMA-DEAMEQGVSDYIK-DNP; column 'Km (uM)' = 73.5; column 'kcat (min^-1)' = 0.03; column 'kcat/Km (mM^-1 min^-1)' = 0.4.

normalized_value_unit_evidence: Km: printed Table 2 cell 73.5 uM; 73.5 / 1000 = 0.0735 mM; the exported value is 0.0735 mM. kcat: printed Table 2 cell 0.03 min^-1; 0.03 / 60 = 0.0005 s^(-1); the exported value is 0.0005 s^(-1). kcat/Km: printed Table 2 cell 0.4 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 0.4 / 60 = 0.006666666666666667 s^-1 mM^-1, which is the printed cell at the table's own precision; the exported value 0.006802721088435375 s^(-1)*mM^(-1) is the full-precision quotient 0.0005 / 0.0735 of the two printed component cells of the same row, and the printed cell rounds to that quotient at the precision Table 2 uses.

raw_value_unit_evidence: Table 2, peptide substrate row 'P07': Km = 73.5 uM; kcat = 0.03 min^-1; printed kcat/Km = 0.4 mM^-1 min^-1.

row_label: Table 2, peptide substrate row 'P07', sequence NMA-DEAMEQGVSDYIK-DNP (columns Km, kcat and kcat/Km of that row)


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

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

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


column_label: Table 2: Cleavage efficiencies of fluorogenic peptide substrates (Antimicrobial Agents and Chemotherapy 2015, 59(4):1827-1836); peptide row 'P13', column 'Sequence' = NMA-IEAAFQGPPK(DNP)FR; column 'Km (uM)' = 66.7; column 'kcat (min^-1)' = 0.3; column 'kcat/Km (mM^-1 min^-1)' = 4.5.

normalized_value_unit_evidence: Km: printed Table 2 cell 66.7 uM; 66.7 / 1000 = 0.0667 mM; the exported value is 0.0667 mM. kcat: printed Table 2 cell 0.3 min^-1; 0.3 / 60 = 0.005 s^(-1); the exported value is 0.005 s^(-1). kcat/Km: printed Table 2 cell 4.5 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 4.5 / 60 = 0.075 s^-1 mM^-1, which is the printed cell at the table's own precision; the exported value 0.07496251874062969 s^(-1)*mM^(-1) is the full-precision quotient 0.005 / 0.0667 of the two printed component cells of the same row, and the printed cell rounds to that quotient at the precision Table 2 uses.

raw_value_unit_evidence: Table 2, peptide substrate row 'P13': Km = 66.7 uM; kcat = 0.3 min^-1; printed kcat/Km = 4.5 mM^-1 min^-1.

row_label: Table 2, peptide substrate row 'P13', sequence NMA-IEAAFQGPPK(DNP)FR (columns Km, kcat and kcat/Km of that row)


column_label: Table 2: Cleavage efficiencies of fluorogenic peptide substrates (Antimicrobial Agents and Chemotherapy 2015, 59(4):1827-1836); peptide row 'P12', column 'Sequence' = NMA-IELLFQGPPK(DNP)FR; column 'Km (uM)' = 48.2; column 'kcat (min^-1)' = 0.24; column 'kcat/Km (mM^-1 min^-1)' = 5.

normalized_value_unit_evidence: Km: printed Table 2 cell 48.2 uM; 48.2 / 1000 = 0.0482 mM; the exported value is 0.0482 mM. kcat: printed Table 2 cell 0.24 min^-1; 0.24 / 60 = 0.004 s^(-1); the exported value is 0.004 s^(-1). kcat/Km: printed Table 2 cell 5 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 5 / 60 = 0.08333333333333333 s^-1 mM^-1, which is the printed cell at the table's own precision; the exported value 0.08298755186721991 s^(-1)*mM^(-1) is the full-precision quotient 0.004 / 0.0482 of the two printed component cells of the same row, and the printed cell rounds to that quotient at the precision Table 2 uses.

raw_value_unit_evidence: Table 2, peptide substrate row 'P12': Km = 48.2 uM; kcat = 0.24 min^-1; printed kcat/Km = 5 mM^-1 min^-1.

row_label: Table 2, peptide substrate row 'P12', sequence NMA-IELLFQGPPK(DNP)FR (columns Km, kcat and kcat/Km of that row)


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

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

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


column_label: Table 2: Cleavage efficiencies of fluorogenic peptide substrates (Antimicrobial Agents and Chemotherapy 2015, 59(4):1827-1836); peptide row 'P03', column 'Sequence' = NMA-RTATVQGPSLDFK(DNP); column 'Km (uM)' = 58.2; column 'kcat (min^-1)' = 0.21; column 'kcat/Km (mM^-1 min^-1)' = 3.6.

normalized_value_unit_evidence: Km: printed Table 2 cell 58.2 uM; 58.2 / 1000 = 0.0582 mM; the exported value is 0.0582 mM. kcat: printed Table 2 cell 0.21 min^-1; 0.21 / 60 = 0.0035 s^(-1); the exported value is 0.0035 s^(-1). kcat/Km: printed Table 2 cell 3.6 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 3.6 / 60 = 0.06 s^-1 mM^-1, which is the printed cell at the table's own precision; the exported value 0.06013745704467354 s^(-1)*mM^(-1) is the full-precision quotient 0.0035 / 0.0582 of the two printed component cells of the same row, and the printed cell rounds to that quotient at the precision Table 2 uses.

raw_value_unit_evidence: Table 2, peptide substrate row 'P03': Km = 58.2 uM; kcat = 0.21 min^-1; printed kcat/Km = 3.6 mM^-1 min^-1.

row_label: Table 2, peptide substrate row 'P03', sequence NMA-RTATVQGPSLDFK(DNP) (columns Km, kcat and kcat/Km of that row)


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

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

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


substrate_name: Dabcyl-IEALFQGPPKFRE-Edans

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

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

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

substrate: Dabcyl-IEALFQGPPKFRE-Edans


substrate_name: Dabcyl-RTATVQGPSLDFKE-Edans

column_label: Table 2: Cleavage efficiencies of fluorogenic peptide substrates (Antimicrobial Agents and Chemotherapy 2015, 59(4):1827-1836); peptide row 'P01', column 'Sequence' = Dabcyl-RTATVQGPSLDFKE-Edans; column 'Km (uM)' = 82.5; column 'kcat (min^-1)' = 0.12; column 'kcat/Km (mM^-1 min^-1)' = 1.45.

normalized_value_unit_evidence: Km: printed Table 2 cell 82.5 uM; 82.5 / 1000 = 0.0825 mM; the exported value is 0.0825 mM. kcat: printed Table 2 cell 0.12 min^-1; 0.12 / 60 = 0.002 s^(-1); the exported value is 0.002 s^(-1). kcat/Km: printed Table 2 cell 1.45 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 1.45 / 60 = 0.024166666666666666 s^-1 mM^-1, which is the printed cell at the table's own precision; the exported value 0.024242424242424242 s^(-1)*mM^(-1) is the full-precision quotient 0.002 / 0.0825 of the two printed component cells of the same row, and the printed cell rounds to that quotient at the precision Table 2 uses.

raw_value_unit_evidence: Table 2, peptide substrate row 'P01': Km = 82.5 uM; kcat = 0.12 min^-1; printed kcat/Km = 1.45 mM^-1 min^-1.

row_label: Table 2, peptide substrate row 'P01', sequence Dabcyl-RTATVQGPSLDFKE-Edans (columns Km, kcat and kcat/Km of that row)

substrate: Dabcyl-RTATVQGPSLDFKE-Edans


organism: Human rhinovirus sp.

substrate_name: TRPIITTA-p-nitroanilide

proof_lines:
human rhinovirus
human rhinovirus type 2

substrate: TRPIITTA-p-nitroanilide


substrate_name: SLEVLFQGPVRR

substrate: SLEVLFQGPVRR


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


organism: Rattus norvegicus


organism: Enterovirus D68

substrate_name: Unknown

substrate: Unknown


organism: Homo sapiens


enzyme_display_name: cruzipain

organism: Unknown

enzyme: cruzipain


organism: Oryctolagus cuniculus


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


enzyme_display_name: staphopain

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

enzyme: staphopain


enzyme_display_name: separase

enzyme: separase


enzyme_display_name: V-cath endopeptidase

enzyme: V-cath endopeptidase


organism: ancestral Carnivora reconstruction


enzyme_display_name: SARS coronavirus main proteinase

organism: SARS coronavirus

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

enzyme: SARS coronavirus main proteinase

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


substrate_name: SITSAVLQSGFRKMA

substrate: SITSAVLQSGFRKMA


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


enzyme_display_name: calicivirin

organism: Norwalk virus

enzyme: calicivirin


organism: Middle East respiratory syndrome-related coronavirus


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

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


organism: Tylonycteris bat coronavirus HKU4


organism: Pipistrellus bat coronavirus HKU5


organism: Southampton virus


organism: Feline infectious peritonitis virus


substrate_name: H2O; Dabcyl-KTSAVLQSGFRKM-Edans

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

substrate: H2O; Dabcyl-KTSAVLQSGFRKM-Edans


enzyme_display_name: Replicase polyprotein 1ab

organism: Severe acute respiratory syndrome coronavirus

substrate_name: peptide TSAVLQSGFRK-NH(2)

enzyme: Replicase polyprotein 1ab

substrate: peptide TSAVLQSGFRK-NH(2)


substrate_name: Dabcyl-KTSAVLQSGFRKM-Edans; H2O

substrate: Dabcyl-KTSAVLQSGFRKM-Edans; H2O


substrate_name: H-TSAVLQSGFRK-NH2; H2O

substrate: H-TSAVLQSGFRK-NH2; H2O


substrate_name: SAVLQMGFRK

substrate: SAVLQMGFRK


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


substrate_name: Caspase-9 cleaved; Caspase-3

substrate: Caspase-9 cleaved; Caspase-3


substrate_name: Caspase-3; Caspase-9

substrate: Caspase-3; Caspase-9


organism: Avian infectious bronchitis virus


organism: Human coronavirus 229E

substrate_name: VSYGSTLQAGLRKMA; H2O

substrate: VSYGSTLQAGLRKMA; H2O


organism: Human coronavirus HKU1


organism: Human coronavirus NL63


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

assay_conditions_summary: pH 7.6; 303.15 K; buffer phosphate


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


organism: Severe acute respiratory syndrome-related coronavirus

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

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

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


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


organism: Homo sapiens


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


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


proof_lines:
mutant enzyme R298L
R298L mutant protein


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


substrate_name: Dabcyl-KTSAVLQSGFRKME-EDANS

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

substrate: Dabcyl-KTSAVLQSGFRKME-EDANS


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


proof_lines:
pH 7.5
pH 6.5
caspase-9 holoenzyme


enzyme_display_name: peptidase 1 (mite)

organism: Dermatophagoides pteronyssinus

proof_lines: Der p 1 purified from Dermatophagoides pteronyssinus

enzyme: peptidase 1 (mite)


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

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


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

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

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

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


enzyme_display_name: UniProt P03367

organism: Human immunodeficiency virus 1

substrate_name: KARVLAEAMS

enzyme: UniProt P03367

substrate: KARVLAEAMS


enzyme_display_name: renin

organism: Sus scrofa

enzyme: renin


enzyme_display_name: rhizopuspepsin

organism: Rhizomucor miehei

substrate_name: Abz-LSFMAIQ-EDDnp

enzyme: rhizopuspepsin

substrate: Abz-LSFMAIQ-EDDnp


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

substrate_name: Z-His-Phe-Phe-OEt

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

substrate: Z-His-Phe-Phe-OEt


enzyme_display_name: HIV-1 retropepsin

organism: Human immunodeficiency virus

unit: Mswedgeone

enzyme: HIV-1 retropepsin


enzyme_display_name: aspergillopepsin I

organism: Aspergillus fumigatus

substrate_name: hemoglobin

enzyme: aspergillopepsin I

substrate: hemoglobin


enzyme_display_name: penicillopepsin

organism: Penicillium janthinellum

substrate_name: Trypsinogen; H2O

enzyme: penicillopepsin

substrate: Trypsinogen; H2O


organism: Rattus norvegicus

substrate_name: angiotensinogen

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

substrate: angiotensinogen


enzyme_display_name: candidapepsin

organism: Candida albicans

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

proof_lines:
pH 3.25, isoenzyme Sap2p
isoenzyme Sap2p

enzyme: candidapepsin

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


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

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


substrate_name: Unknown

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

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

substrate: Unknown


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


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


substrate_name: PARVLAEAMR

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

substrate: PARVLAEAMR


organism: Aspergillus pseudoglaucus

substrate_name: equine myoglobin

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

substrate: equine myoglobin


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


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

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


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


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


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


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

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


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

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


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

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


enzyme_display_name: endothiapepsin

organism: Cryphonectria parasitica

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

assay_conditions_summary: pH 4.6; buffer 0.1 M acetate

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

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

enzyme: endothiapepsin


enzyme_display_name: mucorpepsin

proof_lines:
pH 6.5, 45°C
Mucor miehei

enzyme: mucorpepsin


enzyme_display_name: saccharopepsin

organism: Saccharomyces cerevisiae

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

enzyme: saccharopepsin


enzyme_display_name: Pro-opiomelanocortin converting enzyme

organism: Bos taurus

substrate_name: beta-Lipotropin

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

proof_lines: human substrate, cleavage at Lys37-Lys38

proof_lines: human substrate, cleavage at Lys57-Arg58

enzyme: Pro-opiomelanocortin converting enzyme

substrate: beta-Lipotropin


substrate_name: VSQNYPIVQ

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

substrate: VSQNYPIVQ


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


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

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

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


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

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


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


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


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


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


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


substrate_name: VVQNYPIVQ

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

substrate: VVQNYPIVQ


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

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

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

table_label: Table I Kinetic Parameters Obtained for Oligopeptide Substrates


enzyme_display_name: UniProt P00797

enzyme: UniProt P00797


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


substrate_name: IPFAAAQQRK

substrate: IPFAAAQQRK


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

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

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


substrate_name: KARLMAEALK

substrate: KARLMAEALK


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

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

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


substrate_name: VLQNYPIVQ

substrate: VLQNYPIVQ


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

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

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


substrate_name: VSQLYPIVQ

substrate: VSQLYPIVQ


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

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

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


substrate_name: VSQVYPIVQ

substrate: VSQVYPIVQ


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

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

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


proof_lines:
HIV-1 protease precursor
autoprocessing reaction
mature PR


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

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

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

row_label: p1-p6; RPGNF*LQSRP

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


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

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


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