substrate_name: S-Adenosyl-L-homocysteine

column_label: Table II (Kinetic constants of wild-type and mutant AdoHcy hydrolases), block 'Substrate: AdoHcy', enzyme row 'C113D'; column 'Km (uM)' = 10.5; column 'kcat (s^-1)' = 2.8; column 'kcat/Km (uM^-1 s^-1)' = 0.27; column 'DDG (Kcal/mol)' = 0.34.

normalized_value_unit_evidence: Km: printed Table II cell 10.5 uM; 10.5 / 1000 = 0.0105 mM. kcat: printed Table II cell 2.8 s^-1; the cell is already in s^-1, so no unit conversion applies. kcat/Km: printed Table II cell 0.27 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.27 * 1000 = 270.0 s^-1 mM^-1.

raw_value_unit_evidence: Table II, block Substrate: AdoHcy, enzyme row C113D: Km = 10.5 uM; kcat = 2.8 s^-1; printed kcat/Km = 0.27 uM^-1 s^-1.

substrate: S-Adenosyl-L-homocysteine


enzyme_display_name: Transferred entry: 3.13.2.1

organism: Homo sapiens

source_db: oed

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C113S to reconstruct the assayed variant sequence.

mutation_type: substitution

data_origin: experimental

enzyme: Transferred entry: 3.13.2.1

status: unverified

source: oed


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23526 and applied mutation signature C195D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; 310.15 K; buffer 50 mM potassium phosphate

column_label: Table II (Kinetic constants of wild-type and mutant AdoHcy hydrolases), block 'Substrate: AdoHcy', enzyme row 'C195D'; column 'Km (uM)' = 4.1; column 'kcat (s^-1)' = 0.27; column 'kcat/Km (uM^-1 s^-1)' = 0.07; column 'DDG (Kcal/mol)' = 1.22.

normalized_value_unit_evidence: Km: printed Table II cell 4.1 uM; 4.1 / 1000 = 0.0041 mM. kcat: printed Table II cell 0.27 s^-1; the cell is already in s^-1, so no unit conversion applies. kcat/Km: printed Table II cell 0.07 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.07 * 1000 = 70.0 s^-1 mM^-1.

raw_value_unit_evidence: Table II, block Substrate: AdoHcy, enzyme row C195D: Km = 4.1 uM; kcat = 0.27 s^-1; printed kcat/Km = 0.07 uM^-1 s^-1.

table_label: Table II: Kinetic constants of wild-type and mutant AdoHcy hydrolases (J. Biol. Chem. 1996, 271(45):28009-28016)

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23526 and applied mutation signature C195S to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of wild-type and mutant AdoHcy hydrolases), block 'Substrate: AdoHcy', enzyme row 'C195S'; column 'Km (uM)' = 2.7; column 'kcat (s^-1)' = 0.44; column 'kcat/Km (uM^-1 s^-1)' = 0.16; column 'DDG (Kcal/mol)' = 0.67.

normalized_value_unit_evidence: Km: printed Table II cell 2.7 uM; 2.7 / 1000 = 0.0027 mM. kcat: printed Table II cell 0.44 s^-1; the cell is already in s^-1, so no unit conversion applies. kcat/Km: printed Table II cell 0.16 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.16 * 1000 = 160.0 s^-1 mM^-1.

raw_value_unit_evidence: Table II, block Substrate: AdoHcy, enzyme row C195S: Km = 2.7 uM; kcat = 0.44 s^-1; printed kcat/Km = 0.16 uM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23526 and applied mutation signature C421D to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of wild-type and mutant AdoHcy hydrolases), block 'Substrate: AdoHcy', enzyme row 'C421D'; column 'Km (uM)' = 11.8; column 'kcat (s^-1)' = 3.1; column 'kcat/Km (uM^-1 s^-1)' = 0.26; column 'DDG (Kcal/mol)' = 0.37.

normalized_value_unit_evidence: Km: printed Table II cell 11.8 uM; 11.8 / 1000 = 0.0118 mM. kcat: printed Table II cell 3.1 s^-1; the cell is already in s^-1, so no unit conversion applies. kcat/Km: printed Table II cell 0.26 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.26 * 1000 = 260.0 s^-1 mM^-1.

raw_value_unit_evidence: Table II, block Substrate: AdoHcy, enzyme row C421D: Km = 11.8 uM; kcat = 3.1 s^-1; printed kcat/Km = 0.26 uM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P23526 and applied mutation signature C421S to reconstruct the assayed variant sequence.

column_label: Table II (Kinetic constants of wild-type and mutant AdoHcy hydrolases), block 'Substrate: AdoHcy', enzyme row 'C421S'; column 'Km (uM)' = 10.6; column 'kcat (s^-1)' = 3.8; column 'kcat/Km (uM^-1 s^-1)' = 0.36; column 'DDG (Kcal/mol)' = 0.18.

normalized_value_unit_evidence: Km: printed Table II cell 10.6 uM; 10.6 / 1000 = 0.0106 mM. kcat: printed Table II cell 3.8 s^-1; the cell is already in s^-1, so no unit conversion applies. kcat/Km: printed Table II cell 0.36 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.36 * 1000 = 360.0 s^-1 mM^-1.

raw_value_unit_evidence: Table II, block Substrate: AdoHcy, enzyme row C421S: Km = 10.6 uM; kcat = 3.8 s^-1; printed kcat/Km = 0.36 uM^-1 s^-1.


mutation_signature: Unknown

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

column_label: Table II. Kinetic constants of wild-type and mutant AdoHcy hydrolases; substrate block AdoHcy; row Wild-type / AdoHcy; columns Km (uM), kcat (s^-1), kcat/Km (uM^-1 s^-1); cells Km 7.9, kcat 3.8, kcat/Km 0.48.

normalized_value_unit_evidence: Km normalized_value=0.0079 normalized_unit=mM; kcat normalized_value=3.8 normalized_unit=s^-1; kcat/Km normalized_value=480 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table II substrate AdoHcy row Wild-type / AdoHcy: Km 7.9 uM; kcat 3.8 s^-1; kcat/Km 0.48 uM^-1 s^-1.

row_label: Wild-type / AdoHcy


enzyme_display_name: maltose-6'-phosphate glucosidase

organism: Bacillus subtilis

verification_status: verified

assay_conditions_summary: pH 7.5; 310.15 K; buffer HEPES; cofactor NAD+

column_label: Table 5 columns aryl 6-phospho-beta-D-glucoside, kcat (s^-1), KM (uM), and kcat/KM (s^-1/mM); row matched by 4NPbetaG6P at pH 7.5.

raw_value_unit_evidence: Table 5 row 4NPbetaG6P: kcat 0.52 s^-1; KM 54 uM; kcat/KM 9.6 s^-1/mM.

row_label: 4NPbetaG6P; beta-D-glucoside; HEPES pH 7.5

table_label: Table 5, aryl 6-phospho-beta-D-glucosides by GlvA at 37 C in HEPES buffer pH 7.5

enzyme: maltose-6'-phosphate glucosidase

status: verified


assay_conditions_summary: pH 8.4; 310.15 K; buffer Tris-HCl; cofactor NAD+

column_label: Table 6 columns aryl 6-phospho-beta-D-glucoside, kcat (s^-1), KM (uM), and kcat/KM (s^-1/mM); row matched by 4NPbetaG6P at pH 8.4.

raw_value_unit_evidence: Table 6 row 4NPbetaG6P: kcat 0.34 s^-1; KM 24 uM; kcat/KM 14 s^-1/mM.

row_label: 4NPbetaG6P; beta-D-glucoside; Tris-HCl pH 8.4

table_label: Table 6, aryl 6-phospho-beta-D-glucosides by GlvA at 37 C in Tris-HCl buffer pH 8.4


substrate_name: Methyl 6-phospho-alpha-D-glucoside

assay_conditions_summary: pH 7.5; 310.15 K; buffer Tris-HCl; cofactor NADP+

column_label: Table 4 columns 6-phospho-alpha-D-glucoside, kcat (s^-1), KM (uM), and kcat/KM (s^-1/mM); row matched by MeRG6P at pH 8.4.

raw_value_unit_evidence: Table 4 row MeRG6P: kcat 1.1 s^-1; KM 5.0 x 10^2 uM; kcat/KM 2.2 s^-1/mM.

row_label: MeRG6P; alpha-D-glucoside; Tris-HCl pH 8.4

table_label: Table 4, aryl 6-phospho-alpha-D-glucosides by GlvA at 37 C in Tris-HCl buffer pH 8.4

substrate: Methyl 6-phospho-alpha-D-glucoside


substrate_name: Phenyl 6-phospho-alpha-D-glucoside

column_label: Table 3 columns 6-phospho-alpha-D-glucoside, kcat (s^-1), KM (uM), and kcat/KM (s^-1/mM); row matched by PRG6P at pH 7.5.

raw_value_unit_evidence: Table 3 row PRG6P: kcat 0.90 s^-1; KM 69 uM; kcat/KM 13 s^-1/mM.

row_label: PRG6P; alpha-D-glucoside; HEPES pH 7.5

table_label: Table 3, aryl 6-phospho-alpha-D-glucosides by GlvA at 37 C in HEPES buffer pH 7.5

substrate: Phenyl 6-phospho-alpha-D-glucoside


column_label: Table 4 columns 6-phospho-alpha-D-glucoside, kcat (s^-1), KM (uM), and kcat/KM (s^-1/mM); row matched by PRG6P at pH 8.4.

raw_value_unit_evidence: Table 4 row PRG6P: kcat 0.26 s^-1; KM 38 uM; kcat/KM 6.9 s^-1/mM.

row_label: PRG6P; alpha-D-glucoside; Tris-HCl pH 8.4


substrate_name: maltose 6'-phosphate

column_label: Table 4 columns 6-phospho-alpha-D-glucoside, kcat (s^-1), KM (uM), and kcat/KM (s^-1/mM); row matched by M6'P at pH 8.4.

normalized_value_unit_evidence: kcat 1.3 s^-1; Km 0.36 mM; printed kcat/Km 3.6 s^-1 mM^-1; source quotient 3.611111111111111 is table-rounding compatible.

raw_value_unit_evidence: Table 4 row M6'P: kcat 1.3 s^-1; KM 3.6 x 10^2 uM; kcat/KM 3.6 s^-1/mM.

row_label: M6'P; alpha-D-glucoside; Tris-HCl pH 8.4

substrate: maltose 6'-phosphate


enzyme_display_name: alpha,alpha-phosphotrehalase

organism: Bacillus licheniformis

substrate_name: 4-nitrophenyl alpha-D-glucopyranoside

sequence_variant_note: Resolved canonical sequence from uniprotkb:Q65MI2;refseq:WP_003179746.1;rcsb:5BRQ,5BRP and applied mutation signature H281A to reconstruct the assayed variant sequence.

column_label: Table 2; row H281A; pPNG Km, kcat, and kcat/Km columns; table footnote says purified enzymes were assayed using either pPNG or trehalose 6-phosphate as substrate.

normalized_value_unit_evidence: normalized Table 2 values: Km=12.2 mM; kcat=12.4 s^-1; printed kcat/Km=1.0 s^-1 mM^-1; exported kcat/Km=1.0163934426229508 s^-1 mM^-1.

row_label: H281A / pPNG

table_label: Table 2

enzyme: alpha,alpha-phosphotrehalase

substrate: 4-nitrophenyl alpha-D-glucopyranoside


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q65MI2;refseq:WP_003179746.1;rcsb:5BRQ,5BRP and applied mutation signature H282A to reconstruct the assayed variant sequence.

column_label: Table 2; row H282A; pPNG Km, kcat, and kcat/Km columns; table footnote says purified enzymes were assayed using either pPNG or trehalose 6-phosphate as substrate.

normalized_value_unit_evidence: normalized Table 2 values: Km=11.4 mM; kcat=22.6 s^-1; printed kcat/Km=2.0 s^-1 mM^-1; exported kcat/Km=1.9824561403508774 s^-1 mM^-1.

row_label: H282A / pPNG


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q65MI2;refseq:WP_003179746.1;rcsb:5BRQ,5BRP and applied mutation signature K284A to reconstruct the assayed variant sequence.

column_label: Table 2; row K284A; pPNG Km, kcat, and kcat/Km columns; table footnote says purified enzymes were assayed using either pPNG or trehalose 6-phosphate as substrate.

normalized_value_unit_evidence: normalized Table 2 values: Km=7.4 mM; kcat=25.6 s^-1; printed kcat/Km=3.5 s^-1 mM^-1; exported kcat/Km=3.4594594594594597 s^-1 mM^-1.

row_label: K284A / pPNG


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q65MI2;refseq:WP_003179746.1;rcsb:5BRQ,5BRP and applied mutation signature K292A to reconstruct the assayed variant sequence.

column_label: Table 2; row K292A; pPNG Km, kcat, and kcat/Km columns; table footnote says purified enzymes were assayed using either pPNG or trehalose 6-phosphate as substrate.

normalized_value_unit_evidence: normalized Table 2 values: Km=13.6 mM; kcat=0.3 s^-1; printed kcat/Km=0.02 s^-1 mM^-1; exported kcat/Km=0.022058823529411766 s^-1 mM^-1.

row_label: K292A / pPNG


column_label: Table 2; row Wild type; pPNG Km, kcat, and kcat/Km columns; table footnote says purified enzymes were assayed using either pPNG or trehalose 6-phosphate as substrate.

normalized_value_unit_evidence: normalized Table 2 values: Km=5.8 mM; kcat=30.3 s^-1; printed kcat/Km=5.3 s^-1 mM^-1; exported kcat/Km=5.224137931034483 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Wild type; pPNG columns: Km=5.8 +/- 0.3 mM; kcat=30.3 +/- 0.6 s^-1; kcat/Km=5.3 s^-1 mM^-1.

row_label: Wild type / pPNG


substrate_name: alpha,alpha-trehalose 6-phosphate

column_label: Table 2; row H281A; T6P Km, kcat, and kcat/Km columns; table footnote says purified enzymes were assayed using either pPNG or trehalose 6-phosphate as substrate.

normalized_value_unit_evidence: normalized Table 2 values: Km=5.3 mM; kcat=19.1 s^-1; printed kcat/Km=3.6 s^-1 mM^-1; exported kcat/Km=3.6037735849056607 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row H281A; trehalose 6-phosphate columns: Km=5.3 +/- 0.6 mM; kcat=19.1 +/- 1.3 s^-1; kcat/Km=3.6 s^-1 mM^-1.

row_label: H281A / trehalose 6-phosphate

substrate: alpha,alpha-trehalose 6-phosphate


column_label: Table 2; row H282A; T6P Km, kcat, and kcat/Km columns; table footnote says purified enzymes were assayed using either pPNG or trehalose 6-phosphate as substrate.

normalized_value_unit_evidence: normalized Table 2 values: Km=4.9 mM; kcat=34.8 s^-1; printed kcat/Km=7.2 s^-1 mM^-1; exported kcat/Km=7.10204081632653 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row H282A; trehalose 6-phosphate columns: Km=4.9 +/- 0.9 mM; kcat=34.8 +/- 2.3 s^-1; kcat/Km=7.2 s^-1 mM^-1.

row_label: H282A / trehalose 6-phosphate


column_label: Table 2; row K284A; T6P Km, kcat, and kcat/Km columns; table footnote says purified enzymes were assayed using either pPNG or trehalose 6-phosphate as substrate.

normalized_value_unit_evidence: normalized Table 2 values: Km=3.2 mM; kcat=39.5 s^-1; printed kcat/Km=12.2 s^-1 mM^-1; exported kcat/Km=12.34375 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row K284A; trehalose 6-phosphate columns: Km=3.2 +/- 0.1 mM; kcat=39.5 +/- 2.7 s^-1; kcat/Km=12.2 s^-1 mM^-1.

row_label: K284A / trehalose 6-phosphate


column_label: Table 2; row K292A; T6P Km, kcat, and kcat/Km columns; table footnote says purified enzymes were assayed using either pPNG or trehalose 6-phosphate as substrate.

normalized_value_unit_evidence: normalized Table 2 values: Km=5.9 mM; kcat=0.4 s^-1; printed kcat/Km=0.1 s^-1 mM^-1; exported kcat/Km=0.06779661016949153 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row K292A; trehalose 6-phosphate columns: Km=5.9 +/- 0.3 mM; kcat=0.4 +/- 0.1 s^-1; kcat/Km=0.1 s^-1 mM^-1.

row_label: K292A / trehalose 6-phosphate


column_label: Table 2; row Wild type; T6P Km, kcat, and kcat/Km columns; table footnote says purified enzymes were assayed using either pPNG or trehalose 6-phosphate as substrate.

normalized_value_unit_evidence: normalized Table 2 values: Km=2.5 mM; kcat=46.7 s^-1; printed kcat/Km=18.9 s^-1 mM^-1; exported kcat/Km=18.68 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row Wild type; trehalose 6-phosphate columns: Km=2.5 +/- 0.3 mM; kcat=46.7 +/- 1.2 s^-1; kcat/Km=18.9 s^-1 mM^-1.

row_label: Wild type / trehalose 6-phosphate


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

substrate_name: Arabinotetraose

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +9, so it is treated as a source-provided variant sequence.

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

substrate: Arabinotetraose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F94A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H13A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W152A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


organism: Streptococcus pneumoniae

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N322A to reconstruct the assayed variant sequence.


substrate_name: Fmoc-Asn(GlcNAc)-OH

substrate: Fmoc-Asn(GlcNAc)-OH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N322Q to reconstruct the assayed variant sequence.


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.


enzyme_display_name: aminodeoxyfutalosine nucleosidase

organism: Campylobacter jejuni subsp. jejuni serotype O:2

source_db: brenda

column_label: Table 1. Substrate Specificity and Kinetic Parameters for CjMTAN; row 6-amino-6-deoxyfutalosine; columns kcat, Km, kcat/Km; kcat raw_value=0.27 +/- 0.01 raw_unit=s^-1; Km raw_value=3.5 +/- 0.4 raw_unit=uM; kcat/Km raw_value=7.8 (+/-0.9) x 10^4 raw_unit=M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.27 normalized_unit=s^-1; Km normalized_value=0.0035 normalized_unit=mM; kcat/Km normalized_value=78.0 normalized_unit=s^-1*mM^-1

enzyme: aminodeoxyfutalosine nucleosidase

source: brenda


substrate_name: adenosine

column_label: Table 1. Substrate Specificity and Kinetic Parameters for CjMTAN; row adenosine; columns kcat, Km, kcat/Km; kcat raw_value=0.30 +/- 0.01 raw_unit=s^-1; Km raw_value=7.5 +/- 0.6 raw_unit=uM; kcat/Km raw_value=4.0 (+/-0.3) x 10^4 raw_unit=M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.3 normalized_unit=s^-1; Km normalized_value=0.0075 normalized_unit=mM; kcat/Km normalized_value=40.0 normalized_unit=s^-1*mM^-1

row_label: adenosine

substrate: adenosine


column_label: Table 1. Substrate Specificity and Kinetic Parameters for CjMTAN; row 5'-deoxyadenosine; columns kcat, Km, kcat/Km; kcat raw_value=0.92 +/- 0.02 raw_unit=s^-1; Km raw_value=21.4 +/- 1.3 raw_unit=uM; kcat/Km raw_value=4.3 (+/-0.3) x 10^4 raw_unit=M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.92 normalized_unit=s^-1; Km normalized_value=0.0214 normalized_unit=mM; kcat/Km normalized_value=43.0 normalized_unit=s^-1*mM^-1


raw_value_unit_evidence: kcat raw_value=0.92 +/- 0.02 raw_unit=s^-1; Km raw_value=21.4 +/- 1.3 raw_unit=uM; kcat/Km raw_value=4.3 (+/-0.3) x 10^4 raw_unit=M^-1 s^-1

table_label: Table 1. Substrate Specificity and Kinetic Parameters for CjMTAN


column_label: Table 1. Substrate Specificity and Kinetic Parameters for CjMTAN; row 5'-methylthioadenosine; columns kcat, Km, kcat/Km; kcat raw_value=0.80 +/- 0.02 raw_unit=s^-1; Km raw_value=7.1 +/- 0.7 raw_unit=uM; kcat/Km raw_value=11.3 (+/-1.1) x 10^4 raw_unit=M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.8 normalized_unit=s^-1; Km normalized_value=0.0071 normalized_unit=mM; kcat/Km normalized_value=113.0 normalized_unit=s^-1*mM^-1


raw_value_unit_evidence: kcat raw_value=0.27 +/- 0.01 raw_unit=s^-1; Km raw_value=3.5 +/- 0.4 raw_unit=uM; kcat/Km raw_value=7.8 (+/-0.9) x 10^4 raw_unit=M^-1 s^-1


raw_value_unit_evidence: kcat raw_value=0.30 +/- 0.01 raw_unit=s^-1; Km raw_value=7.5 +/- 0.6 raw_unit=uM; kcat/Km raw_value=4.0 (+/-0.3) x 10^4 raw_unit=M^-1 s^-1


column_label: Table 1. Substrate Specificity and Kinetic Parameters for CjMTAN; row S-5'-Adenosyl-L-homocysteine; columns kcat, Km, kcat/Km; kcat raw_value=0.55 +/- 0.03 raw_unit=s^-1; Km raw_value=12.2 +/- 1.5 raw_unit=uM; kcat/Km raw_value=4.6 (+/-0.6) x 10^4 raw_unit=M^-1 s^-1

normalized_value_unit_evidence: kcat normalized_value=0.55 normalized_unit=s^-1; Km normalized_value=0.0122 normalized_unit=mM; kcat/Km normalized_value=46.0 normalized_unit=s^-1*mM^-1


enzyme_display_name: beta-apiosyl-beta-glucosidase

organism: Dalbergia nigrescens

assay_conditions_summary: pH 5

column_label: Table 5 row pNP-b-D-glucoside under columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 14.7, 10.4, 876.

row_label: pNP-b-D-glucoside

table_label: Table 5

enzyme: beta-apiosyl-beta-glucosidase


substrate_name: daidzin

sequence_source: multiple

source_databases_merged: brenda uniprot

substrate: daidzin


substrate_name: genistin

substrate: genistin


column_label: Table 5 row Compound 2 glycoside under columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 0.7, 334, 4.4 x 10^5. Abstract identifies compound 2 as dalnigrein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside.

row_label: Compound 2 glycoside


column_label: Table 5 row Compound 1 glycoside under columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 0.5, 465, 9.9 x 10^5. Abstract identifies compound 1 as dalpatein 7-O-beta-D-apiofuranosyl-(1->6)-beta-D-glucopyranoside.

row_label: Compound 1 glycoside


substrate_name: Genistein 7-O-beta-D-glucoside

substrate: Genistein 7-O-beta-D-glucoside


substrate_name: p-Nitrophenyl-beta-D-fucoside

column_label: Table 5 row pNP-b-D-fucoside under columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1): 1.8, 7.0, 4020.

row_label: pNP-b-D-fucoside

substrate: p-Nitrophenyl-beta-D-fucoside


substrate_name: p-Nitrophenyl-beta-D-glucoside

substrate: p-Nitrophenyl-beta-D-glucoside


column_label: Table 5 columns aryl 6-phospho-beta-D-glucoside, kcat (s^-1), KM (uM), and kcat/KM (s^-1/mM); row matched by 24DNPbetaG6P at pH 7.5.

raw_value_unit_evidence: Table 5 row 24DNPbetaG6P: kcat 0.27 s^-1; KM 35 uM; kcat/KM 7.5 s^-1/mM.

row_label: 24DNPbetaG6P; beta-D-glucoside; HEPES pH 7.5


column_label: Table 6 columns aryl 6-phospho-beta-D-glucoside, kcat (s^-1), KM (uM), and kcat/KM (s^-1/mM); row matched by 24DNPbetaG6P at pH 8.4.

raw_value_unit_evidence: Table 6 row 24DNPbetaG6P: kcat 0.63 s^-1; KM 41 uM; kcat/KM 16 s^-1/mM.

row_label: 24DNPbetaG6P; beta-D-glucoside; Tris-HCl pH 8.4


assay_conditions_summary: pH 7.5; 310.15 K; buffer the assay; cofactor NAD+

column_label: Table 5: Michaelis-Menten Kinetic Parameters for the Hydrolysis of a Series of Aryl 6-Phospho-beta-D-glucosides by GlvA at 37 C in HEPES Buffer (pH 7.5). Row '25DNPbetaG6P' (2,5-Dinitrophenyl 6-phospho-beta-D-glucoside); column 'kcat (s^-1)' = 0.25; column 'KM (uM)' = 1.3 x 10^2; column 'kcat/KM (s^-1/mM)' = 2.0; column 'phenol pKa' = 5.15.

normalized_value_unit_evidence: kcat: printed Table 5 cell 0.25 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 0.46 s^(-1). KM: printed Table 5 cell 1.3 x 10^2 uM = 130.0 uM; 130.0 / 1000 = 0.13 mM; the exported value is 0.073 mM. kcat/KM: printed Table 5 cell 2.0 s^-1/mM; the printed column head is already s^-1 per mM, so the cell is 2 s^(-1)*mM^(-1) with no scaling; the exported value is 6.301369863013699 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 5 (journal page 9848), aryl 6-phospho-beta-D-glucoside row '25DNPbetaG6P': kcat = 0.25 s^-1; KM = 1.3 x 10^2 uM; kcat/KM = 2.0 s^-1/mM.

row_label: Table 5 (HEPES pH 7.5), aryl 6-phospho-beta-D-glucoside row '25DNPbetaG6P' (2,5-Dinitrophenyl 6-phospho-beta-D-glucoside)


column_label: Table 5: Michaelis-Menten Kinetic Parameters for the Hydrolysis of a Series of Aryl 6-Phospho-beta-D-glucosides by GlvA at 37 C in HEPES Buffer (pH 7.5). Row '2NPbetaG6P' (2-Nitrophenyl 6-phospho-beta-D-glucoside); column 'kcat (s^-1)' = 0.29; column 'KM (uM)' = 2.9 x 10^2; column 'kcat/KM (s^-1/mM)' = 1.0; column 'phenol pKa' = 7.22.

normalized_value_unit_evidence: kcat: printed Table 5 cell 0.29 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 0.4 s^(-1). KM: printed Table 5 cell 2.9 x 10^2 uM = 290.0 uM; 290.0 / 1000 = 0.29 mM; the exported value is 0.29 mM. kcat/KM: printed Table 5 cell 1.0 s^-1/mM; the printed column head is already s^-1 per mM, so the cell is 1 s^(-1)*mM^(-1) with no scaling; the exported value is 1.3793103448275863 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 5 (journal page 9848), aryl 6-phospho-beta-D-glucoside row '2NPbetaG6P': kcat = 0.29 s^-1; KM = 2.9 x 10^2 uM; kcat/KM = 1.0 s^-1/mM.

row_label: Table 5 (HEPES pH 7.5), aryl 6-phospho-beta-D-glucoside row '2NPbetaG6P' (2-Nitrophenyl 6-phospho-beta-D-glucoside)


assay_conditions_summary: pH 7.5; 310.15 K; buffer Tris-HCl; cofactor NAD+

column_label: Table 4 columns 6-phospho-alpha-D-glucoside, kcat (s^-1), KM (uM), and kcat/KM (s^-1/mM); row matched by 34DNPRG6P at pH 8.4.

normalized_value_unit_evidence: kcat 0.81 s^-1; Km 0.004 mM; printed kcat/Km 200 s^-1 mM^-1; source quotient 202.5 is table-rounding compatible.

raw_value_unit_evidence: Table 4 row 34DNPRG6P: kcat 0.81 s^-1; KM 4.0 uM; kcat/KM 2.0 x 10^2 s^-1/mM.

row_label: 34DNPRG6P; alpha-D-glucoside; Tris-HCl pH 8.4


column_label: Table 5: Michaelis-Menten Kinetic Parameters for the Hydrolysis of a Series of Aryl 6-Phospho-beta-D-glucosides by GlvA at 37 C in HEPES Buffer (pH 7.5). Row '34DNPbetaG6P' (3,4-Dinitrophenyl 6-phospho-beta-D-glucoside); column 'kcat (s^-1)' = 0.42; column 'KM (uM)' = 2.9; column 'kcat/KM (s^-1/mM)' = 1.5 x 10^2; column 'phenol pKa' = 5.36.

normalized_value_unit_evidence: kcat: printed Table 5 cell 0.42 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 0.42 s^(-1). KM: printed Table 5 cell 2.9 uM = 2.9 uM; 2.9 / 1000 = 0.0029 mM; the exported value is 0.002 mM. kcat/KM: printed Table 5 cell 1.5 x 10^2 s^-1/mM; the printed column head is already s^-1 per mM, so the cell is 150 s^(-1)*mM^(-1) with no scaling; the exported value is 210.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 5 (journal page 9848), aryl 6-phospho-beta-D-glucoside row '34DNPbetaG6P': kcat = 0.42 s^-1; KM = 2.9 uM; kcat/KM = 1.5 x 10^2 s^-1/mM.

row_label: Table 5 (HEPES pH 7.5), aryl 6-phospho-beta-D-glucoside row '34DNPbetaG6P' (3,4-Dinitrophenyl 6-phospho-beta-D-glucoside)


column_label: Table 5 columns aryl 6-phospho-beta-D-glucoside, kcat (s^-1), KM (uM), and kcat/KM (s^-1/mM); row matched by 35DCPbetaG6P at pH 7.5.

raw_value_unit_evidence: Table 5 row 35DCPbetaG6P: kcat 0.66 s^-1; KM 27 uM; kcat/KM 24 s^-1/mM.

row_label: 35DCPbetaG6P; beta-D-glucoside; HEPES pH 7.5


column_label: Table 6 columns aryl 6-phospho-beta-D-glucoside, kcat (s^-1), KM (uM), and kcat/KM (s^-1/mM); row matched by 35DCPbetaG6P at pH 8.4.

normalized_value_unit_evidence: kcat 0.47 s^-1; Km 0.0038 mM; kcat/Km 120 s^-1 mM^-1; current Km 0.004 mM is rounded above the printed table cell.

raw_value_unit_evidence: Table 6 row 35DCPbetaG6P: kcat 0.47 s^-1; KM 3.8 uM; kcat/KM 1.2 x 10^2 s^-1/mM.

row_label: 35DCPbetaG6P; beta-D-glucoside; Tris-HCl pH 8.4


column_label: Table 5: Michaelis-Menten Kinetic Parameters for the Hydrolysis of a Series of Aryl 6-Phospho-beta-D-glucosides by GlvA at 37 C in HEPES Buffer (pH 7.5). Row '3NPbetaG6P' (3-Nitrophenyl 6-phospho-beta-D-glucoside); column 'kcat (s^-1)' = 0.54; column 'KM (uM)' = 34; column 'kcat/KM (s^-1/mM)' = 16; column 'phenol pKa' = 8.39.

normalized_value_unit_evidence: kcat: printed Table 5 cell 0.54 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 0.97 s^(-1). KM: printed Table 5 cell 34 uM = 34.0 uM; 34.0 / 1000 = 0.034 mM; the exported value is 0.009 mM. kcat/KM: printed Table 5 cell 16 s^-1/mM; the printed column head is already s^-1 per mM, so the cell is 16 s^(-1)*mM^(-1) with no scaling; the exported value is 107.77777777777779 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 5 (journal page 9848), aryl 6-phospho-beta-D-glucoside row '3NPbetaG6P': kcat = 0.54 s^-1; KM = 34 uM; kcat/KM = 16 s^-1/mM.

row_label: Table 5 (HEPES pH 7.5), aryl 6-phospho-beta-D-glucoside row '3NPbetaG6P' (3-Nitrophenyl 6-phospho-beta-D-glucoside)


column_label: Table 5: Michaelis-Menten Kinetic Parameters for the Hydrolysis of a Series of Aryl 6-Phospho-beta-D-glucosides by GlvA at 37 C in HEPES Buffer (pH 7.5). Row '4Cl2NPbetaG6P' (4-Chloro-2-Nitrophenyl 6-phospho-beta-D-glucoside); column 'kcat (s^-1)' = 0.18; column 'KM (uM)' = 67; column 'kcat/KM (s^-1/mM)' = 2.7; column 'phenol pKa' = 6.45.

normalized_value_unit_evidence: kcat: printed Table 5 cell 0.18 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 0.52 s^(-1). KM: printed Table 5 cell 67 uM = 67.0 uM; 67.0 / 1000 = 0.067 mM; the exported value is 0.067 mM. kcat/KM: printed Table 5 cell 2.7 s^-1/mM; the printed column head is already s^-1 per mM, so the cell is 2.7 s^(-1)*mM^(-1) with no scaling; the exported value is 7.7611940298507465 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 5 (journal page 9848), aryl 6-phospho-beta-D-glucoside row '4Cl2NPbetaG6P': kcat = 0.18 s^-1; KM = 67 uM; kcat/KM = 2.7 s^-1/mM.

row_label: Table 5 (HEPES pH 7.5), aryl 6-phospho-beta-D-glucoside row '4Cl2NPbetaG6P' (4-Chloro-2-Nitrophenyl 6-phospho-beta-D-glucoside)


column_label: Table 5: Michaelis-Menten Kinetic Parameters for the Hydrolysis of a Series of Aryl 6-Phospho-beta-D-glucosides by GlvA at 37 C in HEPES Buffer (pH 7.5). Row '4CNPbetaG6P' (4-Cyanophenyl 6-phospho-beta-D-glucoside); column 'kcat (s^-1)' = 0.64; column 'KM (uM)' = 1.2 x 10^2; column 'kcat/KM (s^-1/mM)' = 5.5; column 'phenol pKa' = 8.49.

normalized_value_unit_evidence: kcat: printed Table 5 cell 0.64 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 0.64 s^(-1). KM: printed Table 5 cell 1.2 x 10^2 uM = 120.0 uM; 120.0 / 1000 = 0.12 mM; the exported value is 0.028 mM. kcat/KM: printed Table 5 cell 5.5 s^-1/mM; the printed column head is already s^-1 per mM, so the cell is 5.5 s^(-1)*mM^(-1) with no scaling; the exported value is 22.857142857142858 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 5 (journal page 9848), aryl 6-phospho-beta-D-glucoside row '4CNPbetaG6P': kcat = 0.64 s^-1; KM = 1.2 x 10^2 uM; kcat/KM = 5.5 s^-1/mM.

row_label: Table 5 (HEPES pH 7.5), aryl 6-phospho-beta-D-glucoside row '4CNPbetaG6P' (4-Cyanophenyl 6-phospho-beta-D-glucoside)


column_label: Table 4 columns 6-phospho-alpha-D-glucoside, kcat (s^-1), KM (uM), and kcat/KM (s^-1/mM); row matched by 4NPRG6P at pH 8.4.

normalized_value_unit_evidence: kcat 0.85 s^-1; Km 0.014 mM; printed kcat/Km 60 s^-1 mM^-1; source quotient 60.71428571428571 is table-rounding compatible.

raw_value_unit_evidence: Table 4 row 4NPRG6P: kcat 0.85 s^-1; KM 14 uM; kcat/KM 60 s^-1/mM.

row_label: 4NPRG6P; alpha-D-glucoside; Tris-HCl pH 8.4


enzyme_display_name: glucan 1,6-alpha-isomaltosidase

organism: Arthrobacter globiformis

substrate_name: 4-nitrophenyl alpha-isomaltoside

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

enzyme: glucan 1,6-alpha-isomaltosidase

substrate: 4-nitrophenyl alpha-isomaltoside


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D207A/N209A with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M243A with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt P53582

substrate_name: L-methionine 4-nitroanilide

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P53582

substrate: L-methionine 4-nitroanilide

source: skid


enzyme_display_name: isochorismatase

organism: Escherichia coli

assay_conditions_summary: pH 7.01; 310.15 K; cofactor NADH

column_label: Table III, Biochemistry 29 (1990), page 1431, compound 8 row and the Km/kcat/kcat/Km columns.

raw_value_unit_evidence: Compound 8 | Km 86 uM | kcat 1300 min^-1 | kcat/Km 15 uM^-1 min^-1.

row_label: Compound 8: 3-((1-Carboxyethenyl)oxy)-1-cyclohexene-1-carboxylic acid

table_label: Table III: substrate analogues utilized by isochorismatase

enzyme: isochorismatase


column_label: Table III, Biochemistry 29 (1990), page 1431, compound 6 row and the Km/kcat/kcat/Km columns.

raw_value_unit_evidence: Compound 6 | Km 120 uM | kcat 540 min^-1 | kcat/Km 4.5 uM^-1 min^-1.


column_label: Table III, Biochemistry 29 (1990), page 1431, compound 7 row and the Km/kcat/kcat/Km columns.

raw_value_unit_evidence: Compound 7 | Km 280 uM | kcat 980 min^-1 | kcat/Km 3.5 uM^-1 min^-1.

row_label: Compound 7: cis-3-((1-Carboxyethenyl)oxy)-4-cyclohexene-1-carboxylic acid


substrate_name: Isochorismate

substrate: Isochorismate


enzyme_display_name: Epoxide hydrolase 1

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

column_label: TABLE 1 row 8,9-EET; mEH column; Km [uM] metric row.

normalized_value_unit_evidence: Km=0.0008 mM after converting uM to mM.

raw_value_unit_evidence: TABLE 1 row 8,9-EET, mEH column reports Km 0.8 +/- 0.25 uM.

row_label: 8,9-EET, mEH column

table_label: TABLE 1. Catalytic properties of EH3 compared with sEH and mEH

enzyme: Epoxide hydrolase 1

source: uniprot


column_label: TABLE 1 row 11,12-EET; mEH column; Km [uM] metric row.

normalized_value_unit_evidence: Km=0.0004 mM after converting uM to mM.

raw_value_unit_evidence: TABLE 1 row 11,12-EET, mEH column reports Km 0.4 +/- 0.08 uM.

row_label: 11,12-EET, mEH column


column_label: TABLE 1 row 14,15-EET; mEH column; Km [uM] metric row.

normalized_value_unit_evidence: Km=0.0009000000000000001 mM after converting uM to mM.

raw_value_unit_evidence: TABLE 1 row 14,15-EET, mEH column reports Km 0.9 +/- 0.1 uM.

row_label: 14,15-EET, mEH column


substrate_name: leukotoxin

column_label: TABLE 1 row Leukotoxin; mEH column; Km [uM] metric row.

normalized_value_unit_evidence: Km=0.0058 mM after converting uM to mM.

raw_value_unit_evidence: TABLE 1 row Leukotoxin, mEH column reports Km 5.8 +/- 0.2 uM.

row_label: Leukotoxin, mEH column

substrate: leukotoxin


enzyme_display_name: steryl-beta-glucosidase

organism: Cryptococcus neoformans

substrate_name: 4-methylumbelliferyl beta-D-glucoside

proof_lines:
EGCrP2
Cryptococcus neoformans
beta-glucoside hydrolysis

enzyme: steryl-beta-glucosidase

substrate: 4-methylumbelliferyl beta-D-glucoside


substrate_name: 4-nitrophenyl beta-D-glucoside

column_label: Table 2; row pNP-beta-Glc; enzyme EGCrP2; columns Km, kcat, and kcat/Km.

row_label: pNP-beta-Glc / EGCrP2

substrate: 4-nitrophenyl beta-D-glucoside


substrate_name: resorufin 3-O-beta-D-glucoside

substrate: resorufin 3-O-beta-D-glucoside


enzyme_display_name: UniProt P80561

organism: Streptomyces griseus

enzyme: UniProt P80561


substrate_name: bis(p-nitrophenyl)phosphate

substrate: bis(p-nitrophenyl)phosphate


organism: Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)

substrate_name: cellotetraose

substrate: cellotetraose


enzyme_display_name: Clostridial aminopeptidase

organism: Hathewaya histolytica

substrate_name: Val-Gly-Gly

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

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

enzyme: Clostridial aminopeptidase

substrate: Val-Gly-Gly


substrate_name: Pro-Gly-Pro-Pro

substrate: Pro-Gly-Pro-Pro


substrate_name: Pro-Gly-Pro

substrate: Pro-Gly-Pro


substrate_name: Phe-Gly-Gly

substrate: Phe-Gly-Gly


substrate_name: Leu-Gly-Gly

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

substrate: Leu-Gly-Gly


substrate_name: Pro-Gly-Gly

substrate: Pro-Gly-Gly


substrate_name: Ala-Gly-Gly

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

substrate: Ala-Gly-Gly


enzyme_display_name: Xaa-Trp aminopeptidase

organism: Sus scrofa

substrate_name: Pro-Trp

enzyme: Xaa-Trp aminopeptidase

substrate: Pro-Trp


substrate_name: Ala-Trp

substrate: Ala-Trp


substrate_name: Leu-Trp

substrate: Leu-Trp


substrate_name: Glu-Trp

substrate: Glu-Trp


substrate_name: Gly-Trp

substrate: Gly-Trp


enzyme_display_name: coniferin beta-glucosidase

organism: Pinus contorta

substrate_name: coniferin

enzyme: coniferin beta-glucosidase

substrate: coniferin


substrate_name: syringin

substrate: syringin


substrate_name: 4-nitrophenyl beta-D-glucoside

proof_lines:
coniferin
syringin
synthetic coniferin analog

substrate: 4-nitrophenyl beta-D-glucoside


substrate_name: 4-methylumbelliferyl beta-D-glucoside

substrate: 4-methylumbelliferyl beta-D-glucoside


enzyme_display_name: leukotriene-A4 hydrolase

organism: Xenopus laevis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F375Y to reconstruct the assayed variant sequence.

enzyme: leukotriene-A4 hydrolase


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


substrate_name: leukotriene A4

substrate: leukotriene A4


enzyme_display_name: aminopeptidase S

organism: Streptomyces septatus

substrate_name: L-Phe-O-methyl ester

proof_lines: pH 8.0, 37°C, recombinant wild-type enzyme

enzyme: aminopeptidase S

substrate: L-Phe-O-methyl ester


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


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


enzyme_display_name: archaeal arginyl aminopeptidase

organism: Pyrococcus horikoshii

enzyme: archaeal arginyl aminopeptidase


enzyme_display_name: aminopeptidase I

organism: Vibrio proteolyticus

substrate_name: L-leucine 4-nitroanilide

proof_lines: pH 8.0, 25°C, enzyme with Cd2+ and Zn2+ bound

proof_lines: pH 8.0, 25°C, enzyme with Zn2+ and Cd2+ bound

enzyme: aminopeptidase I

substrate: L-leucine 4-nitroanilide


substrate_name: L-leucine-anilide

substrate: L-leucine-anilide


enzyme_display_name: methionyl aminopeptidase

organism: Mycobacterium tuberculosis

substrate_name: L-Met 4-nitroanilide

enzyme: methionyl aminopeptidase

substrate: L-Met 4-nitroanilide


organism: Plasmodium falciparum

substrate_name: Met-Gly-Met-Met

substrate: Met-Gly-Met-Met


organism: Streptococcus pneumoniae


enzyme_display_name: UniProt B2IQ22

substrate_name: L-methionine 4-nitroanilide

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

enzyme: UniProt B2IQ22

substrate: L-methionine 4-nitroanilide


organism: Synechocystis sp.

substrate_name: Met-Gly-Gly

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

proof_lines: recombinant isozyme c2MetAP-Ia, pH 7.2, 37°C

proof_lines: recombinant isozyme c1MetAP-Ia, pH 7.2, 37°C

proof_lines: recombinant isozyme c3MetAP-Ib, pH 7.2, 37°C

substrate: Met-Gly-Gly


substrate_name: Met-Ala-Ala

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

substrate: Met-Ala-Ala


substrate_name: alpha-Asp-Phe

substrate: alpha-Asp-Phe


substrate_name: Aspartame

substrate: Aspartame


enzyme_display_name: aminopeptidase Ey

substrate_name: His-Ala

enzyme: aminopeptidase Ey

substrate: His-Ala


substrate_name: Leu-Gly-Leu

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

substrate: Leu-Gly-Leu


substrate_name: Leu-Gly

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

substrate: Leu-Gly


substrate_name: Leu-Ala

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

substrate: Leu-Ala


substrate_name: Arg-Ala

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

substrate: Arg-Ala


substrate_name: Leu-Gly-Pro

substrate: Leu-Gly-Pro


substrate_name: Leu-Gly-Gly

substrate: Leu-Gly-Gly


substrate_name: Lys-Ala

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

substrate: Lys-Ala


enzyme_display_name: membrane dipeptidase

organism: Streptomyces coelicolor

substrate_name: L-Arg-L-Asp

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

enzyme: membrane dipeptidase

substrate: L-Arg-L-Asp


substrate_name: L-Leu-D-Leu

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

substrate: L-Leu-D-Leu


substrate_name: L-Tyr-D-Leu

substrate: L-Tyr-D-Leu


substrate_name: L-Ala-L-Gln

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

substrate: L-Ala-L-Gln


substrate_name: L-Leu-L-Asp

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

substrate: L-Leu-L-Asp


substrate_name: L-Ala-L-Glu

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

substrate: L-Ala-L-Glu


substrate_name: L-Met-L-Leu

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

substrate: L-Met-L-Leu


substrate_name: L-Ala-L-Asp

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

substrate: L-Ala-L-Asp


substrate_name: L-Ala-L-Lys

km_display: Not reported

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

substrate: L-Ala-L-Lys


substrate_name: D-Ala-D-Ala / L-Ala-L-Ala

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

substrate: D-Ala-D-Ala / L-Ala-L-Ala


substrate_name: L-Ala-L-His

substrate: L-Ala-L-His


substrate_name: L-Arg-Gly

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

substrate: L-Arg-Gly


enzyme_display_name: Met-Xaa dipeptidase

substrate_name: Met-Val

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

enzyme: Met-Xaa dipeptidase

substrate: Met-Val


substrate_name: Met-Ala

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

substrate: Met-Ala


substrate_name: Met-Ile

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

substrate: Met-Ile


substrate_name: Met-Leu

substrate: Met-Leu


substrate_name: Met-Thr

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

substrate: Met-Thr


substrate_name: Met-Ser

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

substrate: Met-Ser


enzyme_display_name: non-stereospecific dipeptidase

organism: Loligo vulgaris

substrate_name: L-Ala-D-Ala

enzyme: non-stereospecific dipeptidase

substrate: L-Ala-D-Ala


substrate_name: L-Ala-L-Ala

substrate: L-Ala-L-Ala


substrate_name: Gly-D-Ala

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

substrate: Gly-D-Ala


substrate_name: D-Leu-D-Leu

substrate: D-Leu-D-Leu


substrate_name: Met-Gly-Met-Met

proof_lines: calculated with 29.5 kDa as molecular mass, pH 7.5, 30°C

substrate: Met-Gly-Met-Met


substrate_name: Met-Ala-Ser

proof_lines: pH 7.5, 37°C, isozyme MetAP1a, with Co2+

proof_lines: pH 7.5, 37°C, isozyme MetAP1c, with Co2+

substrate: Met-Ala-Ser


substrate_name: Leu-Leu

proof_lines:
recombinant protein, pH 5.0, 37°C
recombinant protein, pH 5.5, 37°C
recombinant protein, pH 7.5, 37°C

substrate: Leu-Leu


substrate_name: Met-Phe

proof_lines:
recombinant protein, pH 7.5, 37°C
recombinant protein, pH 5.0, 37°C
recombinant protein, pH 5.5, 37°C

substrate: Met-Phe


enzyme_display_name: cytosol nonspecific dipeptidase

organism: Platyrrhini

substrate_name: Ala-Leu

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

assay_conditions_summary: buffer and Tris buffer

proof_lines:
phosphate buffer
Tris buffer

enzyme: cytosol nonspecific dipeptidase

substrate: Ala-Leu


substrate_name: Gly-Val

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

substrate: Gly-Val


substrate_name: Gly-Phe

substrate: Gly-Phe


substrate_name: Gly-Ile

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

substrate: Gly-Ile


substrate_name: Gly-Leu

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

substrate: Gly-Leu


organism: Neurospora crassa

substrate_name: Met-Ala

substrate: Met-Ala


substrate_name: Met-Ile

substrate: Met-Ile


organism: Novosphingobium capsulatum

substrate_name: Ala-beta-naphthylamide

proof_lines:
pH 7.5, 21°C, native enzyme
pH 7.5, 21°C

substrate: Ala-beta-naphthylamide


organism: Aspergillus oryzae


organism: Mycolicibacterium phlei

substrate_name: Leu-Gly

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

substrate: Leu-Gly


substrate_name: Ala-Gly

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

substrate: Ala-Gly


enzyme_display_name: aminopeptidase Y

organism: Yarrowia lipolytica

enzyme: aminopeptidase Y


column_label: Table 1 row rPfA-M1 / Arg-betaNA / pH 7.5 gives Km 170 +/- 10 microM, kcat 21 +/- 2 s^-1, and kcat/Km (1.2 +/- 0.1) x 10^5 M^-1*s^-1.

normalized_value_unit_evidence: Km normalized_value=0.17 normalized_unit=mM; kcat normalized_value=21 normalized_unit=s^-1; kcat/Km normalized_value=120 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=170 +/- 10 raw_unit=microM; kcat raw_value=21 +/- 2 raw_unit=s^-1; kcat/Km raw_value=(1.2 +/- 0.1) x 10^5 raw_unit=M^-1*s^-1

row_label: rPfA-M1 / Arg-betaNA / pH 7.5

table_label: Table 1. Kinetic parameters for native and recombinant PfA-M1


substrate_name: L-Lys 4-nitroanilide

substrate: L-Lys 4-nitroanilide


substrate_name: L-Arg 4-nitroanilide

substrate: L-Arg 4-nitroanilide


enzyme_display_name: tryptophanyl aminopeptidase

organism: Cutaneotrichosporon cutaneum

substrate_name: Trp-amide

enzyme: tryptophanyl aminopeptidase

substrate: Trp-amide


organism: Ixodes persulcatus


organism: Hathewaya histolytica

substrate_name: L-leucine 4-nitroanilide

substrate: L-leucine 4-nitroanilide


enzyme_display_name: beta-peptidyl aminopeptidase

organism: Pseudomonas aeruginosa

substrate_name: beta-homoGly 4-nitroanilide

proof_lines:
wild-type, pH 9.0, 25°C
wild-type, pH 6.0, 25°C

enzyme: beta-peptidyl aminopeptidase

substrate: beta-homoGly 4-nitroanilide


sequence_variant_note: Mutation signature S237C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


proof_lines: recombinant isozyme MetAP1a in presence of Fe2+

proof_lines: recombinant isozyme MetAP1a in presence of Ni2+

proof_lines: recombinant isozyme MetAP1a in presence of Mn2+


organism: Eimeria tenella


enzyme_display_name: D-stereospecific aminopeptidase

substrate_name: L-Ala 4-nitroanilide

enzyme: D-stereospecific aminopeptidase

substrate: L-Ala 4-nitroanilide


proof_lines:
pH 7.2, 37°C
recombinant protein, pH 7.5, 37°C
p120, pH 7.5, 37°C


enzyme_display_name: aspartyl aminopeptidase

organism: Lactobacillus delbrueckii subsp. lactis

enzyme: aspartyl aminopeptidase


organism: Lactococcus lactis ssp. lactis


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: Asp-Xaa

substrate: Asp-Xaa


organism: Cryptomeria japonica

substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Plasmodium falciparum

substrate_name: Leu-Leu

normalized_value_unit_evidence: Km normalized_value=0.13 normalized_unit=mM; kcat normalized_value=12 normalized_unit=s^-1; kcat/Km normalized_value=97 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=130 +/- 10 raw_unit=microM; kcat raw_value=12 +/- 1 raw_unit=s^-1; kcat/Km raw_value=(9.7 +/- 1.2) x 10^4 raw_unit=M^-1*s^-1

row_label: rPfA-M1 / Leu-Leu / pH 7.5

substrate: Leu-Leu


column_label: Table 1 row rPfA-M1 / Ala-betaNA / pH 5.5 gives Km 4400 +/- 400 microM, kcat 16 +/- 1 s^-1, and kcat/Km (3.7 +/- 0.1) x 10^3 M^-1*s^-1.

normalized_value_unit_evidence: Km normalized_value=4.4 normalized_unit=mM; kcat normalized_value=16 normalized_unit=s^-1; kcat/Km normalized_value=3.7 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=4400 +/- 400 raw_unit=microM; kcat raw_value=16 +/- 1 raw_unit=s^-1; kcat/Km raw_value=(3.7 +/- 0.1) x 10^3 raw_unit=M^-1*s^-1

row_label: rPfA-M1 / Ala-betaNA / pH 5.5


substrate_name: Met-Phe

normalized_value_unit_evidence: Km normalized_value=0.38 normalized_unit=mM; kcat normalized_value=7.4 normalized_unit=s^-1; kcat/Km normalized_value=19 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=380 +/- 40 raw_unit=microM; kcat raw_value=7.4 +/- 0.6 raw_unit=s^-1; kcat/Km raw_value=(1.9 +/- 0.3) x 10^4 raw_unit=M^-1*s^-1

row_label: rPfA-M1 / Met-Phe / pH 5.0

substrate: Met-Phe


normalized_value_unit_evidence: Km normalized_value=0.065 normalized_unit=mM; kcat normalized_value=7.5 normalized_unit=s^-1; kcat/Km normalized_value=120 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=65 +/- 7 raw_unit=microM; kcat raw_value=7.5 +/- 0.4 raw_unit=s^-1; kcat/Km raw_value=(1.2 +/- 0.1) x 10^5 raw_unit=M^-1*s^-1

row_label: rPfA-M1 / Met-Phe / pH 5.5


normalized_value_unit_evidence: Km normalized_value=0.022 normalized_unit=mM; kcat normalized_value=5.9 normalized_unit=s^-1; kcat/Km normalized_value=270 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=22 +/- 4 raw_unit=microM; kcat raw_value=5.9 +/- 0.5 raw_unit=s^-1; kcat/Km raw_value=(2.7 +/- 0.6) x 10^5 raw_unit=M^-1*s^-1

row_label: rPfA-M1 / Met-Phe / pH 7.5


organism: Homo sapiens

substrate_name: WRVYEKCALK

substrate: WRVYEKCALK


organism: Parietaria judaica

substrate_name: L-Ala-p-nitroanilide

substrate: L-Ala-p-nitroanilide


organism: Sus scrofa

substrate_name: AYWANATRSGA

substrate: AYWANATRSGA


organism: Colwellia psychrerythraea


enzyme_display_name: dipeptidyl-peptidase III

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G313A to reconstruct the assayed variant sequence.

enzyme: dipeptidyl-peptidase III


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R510K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R510Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R510W to reconstruct the assayed variant sequence.


organism: Grifola frondosa

substrate_name: L-Val-4-nitroanilide / L-Phe-4-nitroanilide / L-Leu-4-nitroanilide


organism: Tenebrio molitor

proof_lines: pH 7.8, 37°C, in presence of 1,10-phenanthroline


organism: Raphanus sativus

substrate_name: L-cysteinylglycine

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

substrate: L-cysteinylglycine


organism: Saccharomyces cerevisiae


enzyme_display_name: intermediate cleaving peptidase 55

substrate_name: Tyr-Ala-Ala

column_label: Table 2: Enzyme kinetics (FEBS Letters 593 (2019) 443-454); printed column heads Substrate | Vmax (umol min^-1 mg^-1) | Km (mM) | Ki (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) (x 10^3). Table 2, substrate row YAA; column Vmax (umol min^-1 mg^-1) = 1.5; column Km (mM) = 0.72; column Ki (mM) = 5 mM; column kcat (s^-1) = 1.4; column kcat/Km (M^-1 s^-1) (x 10^3) = 1.94. captured primary segment: YAA | Vmax 1.5 umol min^-1 mg^-1 | Km 0.72 mM | Ki 5 mM | kcat 1.4 s^-1 | kcat/Km 1.94 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 0.72 mM; the printed unit is already mM, so no unit conversion applies and the exported value is 0.72 mM. kcat: printed Table 2 kcat cell 1.4 s^-1; the printed unit is already s^-1, so no unit conversion applies and the exported value is 1.4 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 1.94 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1940.0 x 0.001 = 1.94 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.4 / 0.72 = 1.9444444444444444 s^-1 mM^-1, against the printed catalytic-efficiency cell 1.94 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate row YAA: Km = 0.72 mM; kcat = 1.4 s^-1; printed kcat/Km = 1.94 x 10^3 M^-1 s^-1.

row_label: Table 2, substrate row YAA

enzyme: intermediate cleaving peptidase 55

substrate: Tyr-Ala-Ala


substrate_name: Tyr-Pro-Ala

column_label: Table 2: Enzyme kinetics (FEBS Letters 593 (2019) 443-454); printed column heads Substrate | Vmax (umol min^-1 mg^-1) | Km (mM) | Ki (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) (x 10^3). Table 2, substrate row YPA; column Vmax (umol min^-1 mg^-1) = 14.0; column Km (mM) = 1.8; column Ki (mM) = NA; column kcat (s^-1) = 14.0; column kcat/Km (M^-1 s^-1) (x 10^3) = 7.78. captured primary segment: YPA | Vmax 14.0 umol min^-1 mg^-1 | Km 1.8 mM | Ki NA | kcat 14.0 s^-1 | kcat/Km 7.78 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 1.8 mM; the printed unit is already mM, so no unit conversion applies and the exported value is 1.8 mM. kcat: printed Table 2 kcat cell 14.0 s^-1; the printed unit is already s^-1, so no unit conversion applies and the exported value is 14.0 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 7.78 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7780.0 x 0.001 = 7.78 s^(-1)*mM^(-1). Quotient disclosure for this row: 14.0 / 1.8 = 7.777777777777778 s^-1 mM^-1, against the printed catalytic-efficiency cell 7.78 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, substrate row YPA: Km = 1.8 mM; kcat = 14.0 s^-1; printed kcat/Km = 7.78 x 10^3 M^-1 s^-1.

row_label: Table 2, substrate row YPA

substrate: Tyr-Pro-Ala


substrate_name: Met-Pro-Ala

proof_lines:
pH 7.5, 40°C
pH 7.5, 40°C, recombinant enzyme

substrate: Met-Pro-Ala


enzyme_display_name: Xaa-Pro dipeptidyl-peptidase

organism: Lactobacillus helveticus

enzyme: Xaa-Pro dipeptidyl-peptidase


substrate_name: Ala-Pro-Arg

substrate: Ala-Pro-Arg


substrate_name: Arg-Pro-Ala

substrate: Arg-Pro-Ala


substrate_name: L-Ala-L-Pro-L-Ser

substrate: L-Ala-L-Pro-L-Ser


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

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


substrate_name: L-Asp-L-Pro-L-Ala

substrate: L-Asp-L-Pro-L-Ala


substrate_name: L-Ser-L-Pro-L-Ala

substrate: L-Ser-L-Pro-L-Ala


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

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


organism: Brucella anthropi

substrate_name: nitrocefin

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N275R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

proof_lines: mutant lacking residues 476-486 plus mutation N275R, pH 8.0, 30°C

proof_lines: mutant lacking residues 476-486 plus mutation N275R, pH 7.0, 30°C

substrate: nitrocefin


enzyme_display_name: aminopeptidase S

organism: Streptomyces septatus

proof_lines: pH 8.0, 37°C, recombinant enzyme, in absence of Ca2+

proof_lines: pH 8.0, 37°C, recombinant enzyme, in presence of Ca2+

enzyme: aminopeptidase S


enzyme_display_name: dipeptidyl-peptidase IV

organism: Lactococcus lactis

enzyme: dipeptidyl-peptidase IV


substrate_name: Leu-Ala-Pro

substrate: Leu-Ala-Pro


substrate_name: His-Pro-Leu

substrate: His-Pro-Leu


substrate_name: His-Pro-Tyr

substrate: His-Pro-Tyr


substrate_name: Gly-Pro-Ala

substrate: Gly-Pro-Ala


enzyme_display_name: Puromycin-sensitive aminopeptidase

organism: Caenorhabditis elegans

substrate_name: L-Arg-AMC

enzyme: Puromycin-sensitive aminopeptidase

substrate: L-Arg-AMC


enzyme_display_name: cytosol alanyl aminopeptidase

organism: Danio rerio

enzyme: cytosol alanyl aminopeptidase


substrate_name: H2O; Ala-4-methylcoumaryl-7-amide

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

substrate: H2O; Ala-4-methylcoumaryl-7-amide


enzyme_display_name: Cyclic dipeptide prenyltransferase

organism: Aspergillus fumigatus

substrate_name: H-L-Trp-L-Gly-OH (for aminopeptidase activity)

enzyme: Cyclic dipeptide prenyltransferase


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

substrate: H-L-Trp-L-Gly-OH (for aminopeptidase activity)


enzyme_display_name: Fumigaclavine A dimethylallyltransferase easL


enzyme_display_name: Xaa-Xaa-Pro tripeptidyl-peptidase

organism: Prevotella nigrescens

substrate_name: Ala-Ala-Pro-p-nitroanilide

enzyme: Xaa-Xaa-Pro tripeptidyl-peptidase

substrate: Ala-Ala-Pro-p-nitroanilide


enzyme_display_name: 7-dimethylallyltryptophan synthase

enzyme: 7-dimethylallyltryptophan synthase


enzyme_display_name: Tryprostatin B synthase ftmPT1

enzyme: Tryprostatin B synthase ftmPT1


enzyme_display_name: methionyl aminopeptidase

organism: Encephalitozoon cuniculi

substrate_name: Met-Ala-Ser; H2O

enzyme: methionyl aminopeptidase

substrate: Met-Ala-Ser; H2O


organism: Escherichia coli

substrate_name: Met-Gly-Met-Met; H2O

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

substrate: Met-Gly-Met-Met; H2O


organism: Homo sapiens

substrate_name: Met-Pro-p-nitroanilide; H2O

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

substrate: Met-Pro-p-nitroanilide; H2O


substrate_name: H2O; Met-Pro-p-nitroanilide

substrate: H2O; Met-Pro-p-nitroanilide


enzyme_display_name: tripeptidyl-peptidase II

organism: Kitasatospora herbaricolor

enzyme: tripeptidyl-peptidase II


organism: Hordeum vulgare


organism: Crocodylus acutus


organism: Aspergillus oryzae

substrate_name: Gly-Pro 4-nitroanilide

substrate: Gly-Pro 4-nitroanilide


organism: Streptomyces mobaraensis

substrate_name: Gly-L-Ala-Gly-L-Pro-beta-naphthylamide

substrate: Gly-L-Ala-Gly-L-Pro-beta-naphthylamide


organism: Streptococcus anginosus


organism: Saccharomyces cerevisiae

proof_lines: heat resistant enzyme form from protoplast lysate


organism: Streptococcus mitis


organism: Lactococcus lactis subsp. cremoris

substrate_name: His-Pro-Leu; H2O

substrate: His-Pro-Leu; H2O


organism: Streptococcus thermophilus

substrate_name: Gly-Pro-p-nitroanilide

substrate: Gly-Pro-p-nitroanilide


organism: Streptococcus suis


enzyme_display_name: tripeptidyl-peptidase I

organism: Aspergillus fumigatus

enzyme: tripeptidyl-peptidase I


organism: Porphyromonas gingivalis

proof_lines:
recombinant enzyme, pH 7.5, 25°C
native enzyme, pH 7.5, 25°C


enzyme_display_name: aminopeptidase Y

organism: Pyrococcus furiosus

substrate_name: Lys-Gly-Gly

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

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

proof_lines: pH 8.0, 100°C, enzyme from Pyrococcus furiosus

source_databases_merged: brenda skid uniprot

enzyme: aminopeptidase Y

substrate: Lys-Gly-Gly


substrate_name: Met-Ala-Ser

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D219N to reconstruct the assayed variant sequence.

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

substrate: Met-Ala-Ser


substrate_name: Met-Gly-Met-Met

substrate: Met-Gly-Met-Met


organism: Streptococcus salivarius

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: Prolyl endopeptidase FAP

organism: Bos taurus

substrate_name: Gly-Pro-Phe-His (Prolyl endopeptidase activity)

enzyme: Prolyl endopeptidase FAP


organism: Homo sapiens

substrate_name: Ac-Gly-Pro (Prolyl endopeptidase activity)


organism: Pseudoxanthomonas mexicana


enzyme_display_name: Aminopeptidase RNPEPL1

substrate_name: Citrulline-AMC

enzyme: Aminopeptidase RNPEPL1

substrate: Citrulline-AMC


organism: Mycobacterium tuberculosis

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

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

row_label: MtMetAP1c / Met-Ala-Ser

table_label: Kinetic parameters prose in Results


substrate_name: H2O; Met-Gly-Met-Met

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

row_label: MtMetAP1c / Met-Gly-Met-Met

substrate: H2O; Met-Gly-Met-Met


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

row_label: MtMetAP1a / Met-Ala-Ser


substrate_name: L-Met-p-nitroanilide

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

column_label: PMID 16844071 Table 1, PfMetAP-II row, L-Met-p-NA column group: Km = 0.59 +/- 0.07 mM and kcat = 0.057 s^-1.

raw_value_unit_evidence: Table 1 reports PfMetAP-II Km = 0.59 +/- 0.07 mM and kcat = 0.057 s^-1 for L-Met-p-NA.

row_label: PfMetAP-II / L-Met-p-NA

table_label: Table 1. Kinetic constants for Co(II)-loaded EcMetAP-I and PfMetAP-II

substrate: L-Met-p-nitroanilide


enzyme_display_name: D-stereospecific aminopeptidase

organism: Bacillus sp.

substrate_name: D-Alanine-p-nitroanilide; H2O

enzyme: D-stereospecific aminopeptidase

substrate: D-Alanine-p-nitroanilide; H2O


organism: Ochrobactrum anthropi

substrate_name: H2O; D-Alaninamide

substrate: H2O; D-Alaninamide


enzyme_display_name: aspartyl aminopeptidase

organism: Aspergillus oryzae

substrate_name: H2O; Aspartic acid-p-nitroanilide

enzyme: aspartyl aminopeptidase

substrate: H2O; Aspartic acid-p-nitroanilide


enzyme_display_name: Aspartyl aminopeptidase

organism: Caenorhabditis elegans

substrate_name: H-Asp-NHMec (at pH 7.5)

enzyme: Aspartyl aminopeptidase

substrate: H-Asp-NHMec (at pH 7.5)


enzyme_display_name: aminopeptidase I

organism: Saccharomyces cerevisiae

substrate_name: Cystinyl 4-nitroanilide

enzyme: aminopeptidase I

substrate: Cystinyl 4-nitroanilide


enzyme_display_name: PepB aminopeptidase

organism: Escherichia coli

substrate_name: L-Leucinyl-p-nitroanilide; H2O

enzyme: PepB aminopeptidase

substrate: L-Leucinyl-p-nitroanilide; H2O


enzyme_display_name: beta-peptidyl aminopeptidase

organism: Sphingosinicella microcystinivorans

substrate_name: beta-Ala-p-nitroanilide

enzyme: beta-peptidyl aminopeptidase

substrate: beta-Ala-p-nitroanilide


organism: Staphylococcus aureus

proof_lines:
pH 7.5, in presence of Mn2+
pH 7.5, in presence of Zn2+
pH 7.5, in presence of Co2+


enzyme_display_name: Methionine aminopeptidase

organism: Thermococcus onnurineus (strain NA1)

proof_lines: kcat is 168 min(-1) with L-Met-p-nitroanilide as substrate.

enzyme: Methionine aminopeptidase


organism: Brucella anthropi

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

proof_lines: mutant lacking residues 476-486 plus mutation N275R, pH 8.0, 37°C

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


enzyme_display_name: aminopeptidase Ey

organism: Gallus gallus

substrate_name: Leu-Pro-Leu-Arg-PheNH2; H2O

proof_lines:
plasma enzyme
granule enzyme

source_databases_merged: sabio_rk brenda uniprot

enzyme: aminopeptidase Ey

substrate: Leu-Pro-Leu-Arg-PheNH2; H2O


organism: Oryctolagus cuniculus

substrate_name: Asp-Xaa-Xaa-Xaa

substrate: Asp-Xaa-Xaa-Xaa


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: Asn-ACC (at pH 7.5, 37 degrees Celsius and in the presence of Co(2+))

proof_lines: kcat is 0.028 sec(-1) with for Asn-ACC as substrate (at pH 7.5, 37 degrees Celsius and in the presence of Co(2+)) (PubMed:22709581). kcat is 0.203 sec(-1) with for Asp-ACC as substrate (at pH 7.5, 37 degrees Celsius and in the presence of C


organism: Sphingosinicella xenopeptidilytica

proof_lines:
pH 8.0, 25°C
Raw SKiD Env: Temp=25°C, pH=8


enzyme_display_name: cytosol nonspecific dipeptidase

organism: Homo sapiens

substrate_name: H2O; L-Seryl-L-Glutamine

enzyme: cytosol nonspecific dipeptidase

substrate: H2O; L-Seryl-L-Glutamine


organism: Rattus norvegicus

substrate_name: H2O; beta-Alanyl-L-arginine

substrate: H2O; beta-Alanyl-L-arginine


enzyme_display_name: membrane dipeptidase

substrate_name: H2O; L-Alanylglycine

enzyme: membrane dipeptidase

substrate: H2O; L-Alanylglycine


enzyme_display_name: Xaa-Pro dipeptidyl-peptidase

organism: Streptococcus gordonii

substrate_name: 4-Nitroaniline; Gly-Pro

enzyme: Xaa-Pro dipeptidyl-peptidase

substrate: 4-Nitroaniline; Gly-Pro


enzyme_display_name: Probable dipeptidyl peptidase 4

organism: Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10)

substrate_name: Gly-Pro pNA and Ala-Pro pNA

enzyme: Probable dipeptidyl peptidase 4

substrate: Gly-Pro pNA and Ala-Pro pNA


organism: Pyrococcus furiosus

substrate_name: H2O; L-Lysyl-p-nitroanilide

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

source_databases_merged: sabio_rk brenda skid uniprot

substrate: H2O; L-Lysyl-p-nitroanilide


enzyme_display_name: Methionine aminopeptidase 1b

substrate_name: methionine containing-oligopeptide

proof_lines: kcat is 13.9 min(-1) with methionine containing-oligopeptide as substrate (PubMed:16983082). kcat is 552.49 min(-1) in presence of 1 uM Zn(2+), 442.48 min(-1) in presence of 10 uM Zn(2+) and 364.30 min(-1) in presence of 100 uM Zn(2+), with

enzyme: Methionine aminopeptidase 1b

substrate: methionine containing-oligopeptide


enzyme_display_name: methionyl aminopeptidase

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature N53C with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, mutant enzyme N53C, substrate: L-Leu-7-amido-4-methylcoumarin

proof_lines: pH 7.5, 37°C, mutant enzyme N53C, substrate: L-Met-7-amido-4-methylcoumarin

enzyme: methionyl aminopeptidase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature N53G with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, mutant enzyme N53G, substrate: L-Met-7-amido-4-methylcoumarin

proof_lines: pH 7.5, 37°C, mutant enzyme N53G, substrate: L-Leu-7-amido-4-methylcoumarin


assay_conditions_summary: pH 7.5; 310.15 K; buffer 25 mM HEPES

proof_lines: Co2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C

proof_lines: pH 7.5, 37°C, wild-type enzyme, substrate: L-Leu-7-amido-4-methylcoumarin


enzyme_display_name: Methionine aminopeptidase 1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: a Met-Ala-Ser peptide

proof_lines: kcat is 1173, 1416 and 507 min(-1) with a Met-Ala-Ser, a Met-Gly-Met-Met and a Met-Ala-Ser-Trp peptide substrate, respectively.

enzyme: Methionine aminopeptidase 1

substrate: a Met-Ala-Ser peptide


enzyme_display_name: dipeptidyl-peptidase IV

substrate_name: Gly-Pro-4-Nitroanilide; H2O

enzyme: dipeptidyl-peptidase IV

substrate: Gly-Pro-4-Nitroanilide; H2O


proof_lines: kcat is 121 sec(-1) with Gly-Pro-AMC substrate (PubMed:29382749). kcat is 52.6 sec(-1) with Lys-Pro-AMC substrate (PubMed:29382749). kcat is 54 sec(-1) with Asp-Pro-AMC substrate (PubMed:29382749). kcat is 40.3 sec(-1) with Trp-Pro-AMC subs


enzyme_display_name: tripeptidyl-peptidase I

organism: Dictyostelium discoideum

substrate_name: Ala-Phe-Pro-p-nitroanilide

enzyme: tripeptidyl-peptidase I

substrate: Ala-Phe-Pro-p-nitroanilide


organism: Saccharomyces cerevisiae

substrate_name: Ala-Thr-Ala

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

substrate: Ala-Thr-Ala


enzyme_display_name: aminopeptidase S

organism: Streptomyces griseus

substrate_name: H2O; L-Leucinyl-p-nitroanilide

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
kcat is 390 sec(-1) with Leu-pNA.

source_databases_merged: sabio_rk skid uniprot

enzyme: aminopeptidase S

substrate: H2O; L-Leucinyl-p-nitroanilide


enzyme_display_name: Dipeptidase 1

substrate_name: Unknown

enzyme: Dipeptidase 1

substrate: Unknown


enzyme_display_name: tripeptidyl-peptidase II

organism: Drosophila melanogaster

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D387G to reconstruct the assayed variant sequence.

proof_lines:
pH 7.6, 37°C, mutant D387G
mutant D387G, pH 8.3, 37°C
pH 7.3, 37°C, mutant D387G

enzyme: tripeptidyl-peptidase II


substrate_name: H2O; Ala-Pro-7-amido-4-methylcoumarin

substrate: H2O; Ala-Pro-7-amido-4-methylcoumarin


enzyme_display_name: Dipeptidyl peptidase 9

substrate_name: Gly-Pro-AMC

enzyme: Dipeptidyl peptidase 9

substrate: Gly-Pro-AMC


substrate_name: Lys-Pro-AMC

substrate: Lys-Pro-AMC


enzyme_display_name: Aminopeptidase RNPEPL1

substrate_name: Met-AMC

enzyme: Aminopeptidase RNPEPL1

substrate: Met-AMC


substrate_name: Ala-AMC

substrate: Ala-AMC


substrate_name: Arg-AMC

substrate: Arg-AMC


substrate_name: Gln-AMC

substrate: Gln-AMC


substrate_name: Leu-AMC

substrate: Leu-AMC


substrate_name: Lys-AMC

substrate: Lys-AMC


substrate_name: Phe-AMC

substrate: Phe-AMC


enzyme_display_name: cytosol alanyl aminopeptidase

assay_conditions_summary: pH 7.5; 310.15 K; buffer Tris-HCl

column_label: PMID 10978616 ScienceDirect article HTML, Results and discussion prose sentence listing metric labels Km, Kcat, and Kcat/Km for each MCA substrate; no table element was present in the rendered HTML. Row/segment Ala-MCA: Km=182 uM; Kcat=4.9 s^-1; Kcat/Km=26.9 s^-1*mM^-1.

row_label: Ala-MCA kinetic-prose entry

table_label: Results and discussion prose (ScienceDirect HTML)

enzyme: cytosol alanyl aminopeptidase


column_label: PMID 10978616 ScienceDirect article HTML, Results and discussion prose sentence listing metric labels Km, Kcat, and Kcat/Km for each MCA substrate; no table element was present in the rendered HTML. Row/segment Leu-MCA: Km=91 uM; Kcat=5.6 s^-1; Kcat/Km=61.7 s^-1*mM^-1.

raw_value_unit_evidence: Km=91 uM; Kcat=5.6 s^-1; Kcat/Km=61.7 s^-1*mM^-1 for Leu-MCA.

row_label: Leu-MCA kinetic-prose entry


column_label: PMID 10978616 ScienceDirect article HTML, Results and discussion prose sentence listing metric labels Km, Kcat, and Kcat/Km for each MCA substrate; no table element was present in the rendered HTML. Row/segment Lys-MCA: Km=220 uM; Kcat=13.2 s^-1; Kcat/Km=60 s^-1*mM^-1.

raw_value_unit_evidence: Km=220 uM; Kcat=13.2 s^-1; Kcat/Km=60 s^-1*mM^-1 for Lys-MCA.

row_label: Lys-MCA kinetic-prose entry


column_label: PMID 10978616 ScienceDirect article HTML, Results and discussion prose sentence listing metric labels Km, Kcat, and Kcat/Km for each MCA substrate; no table element was present in the rendered HTML. Row/segment Met-MCA: Km=189 uM; Kcat=12.7 s^-1; Kcat/Km=67.2 s^-1*mM^-1.

row_label: Met-MCA kinetic-prose entry


column_label: PMID 10978616 ScienceDirect article HTML, Results and discussion prose sentence listing metric labels Km, Kcat, and Kcat/Km for each MCA substrate; no table element was present in the rendered HTML. Row/segment Phe-MCA: Km=167 uM; Kcat=9.3 s^-1; Kcat/Km=55.6 s^-1*mM^-1.

row_label: Phe-MCA kinetic-prose entry


enzyme_display_name: Puromycin-sensitive aminopeptidase

substrate_name: Ala-MCA

assay_conditions_summary: pH 7.5; buffer Tris-HCl

column_label: PMID 10978616 ScienceDirect article HTML, Results and discussion prose sentence listing metric labels Km, Kcat, and Kcat/Km for each MCA substrate; no table element was present in the rendered HTML. Row/segment Ala-MCA: Km=182 uM.

normalized_value_unit_evidence: Km=0.182 mM for Ala-MCA.

raw_value_unit_evidence: Km=182 uM for Ala-MCA.

enzyme: Puromycin-sensitive aminopeptidase

substrate: Ala-MCA


substrate_name: Met-MCA

column_label: PMID 10978616 ScienceDirect article HTML, Results and discussion prose sentence listing metric labels Km, Kcat, and Kcat/Km for each MCA substrate; no table element was present in the rendered HTML. Row/segment Met-MCA: Km=189 uM.

normalized_value_unit_evidence: Km=0.189 mM for Met-MCA.

raw_value_unit_evidence: Km=189 uM for Met-MCA.

substrate: Met-MCA


substrate_name: Lys-MCA

column_label: PMID 10978616 ScienceDirect article HTML, Results and discussion prose sentence listing metric labels Km, Kcat, and Kcat/Km for each MCA substrate; no table element was present in the rendered HTML. Row/segment Lys-MCA: Km=220 uM.

normalized_value_unit_evidence: Km=0.22 mM for Lys-MCA.

raw_value_unit_evidence: Km=220 uM for Lys-MCA.

substrate: Lys-MCA


substrate_name: Leu-MCA

column_label: PMID 10978616 ScienceDirect article HTML, Results and discussion prose sentence listing metric labels Km, Kcat, and Kcat/Km for each MCA substrate; no table element was present in the rendered HTML. Row/segment Leu-MCA: Km=91 uM.

normalized_value_unit_evidence: Km=0.091 mM for Leu-MCA.

raw_value_unit_evidence: Km=91 uM for Leu-MCA.

substrate: Leu-MCA


substrate_name: Phe-MCA

column_label: PMID 10978616 ScienceDirect article HTML, Results and discussion prose sentence listing metric labels Km, Kcat, and Kcat/Km for each MCA substrate; no table element was present in the rendered HTML. Row/segment Phe-MCA: Km=167 uM.

normalized_value_unit_evidence: Km=0.167 mM for Phe-MCA.

raw_value_unit_evidence: Km=167 uM for Phe-MCA.

substrate: Phe-MCA


enzyme_display_name: aminopeptidase Ey

organism: Eimeria tenella

column_label: Table 1 (Enzymatic specificity of EtAPN1r), substrate row 'Ala-ACC'; column 'Km (uM)' = 59.8; column 'kcat (s^-1)' = 0.456; column 'kcat/Km (mM^-1 s^-1)' = 7.6. 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 59.8 uM; 59.8 / 1000 = 0.0598 mM; the exported value is 0.0598 mM. kcat: printed Table 1 cell 0.456 s^-1; the printed unit is already the canonical kcat unit, so no unit conversion applies; the exported value is 0.456 s^(-1). kcat/Km: printed Table 1 cell 7.6 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 7.6 s^(-1)*mM^(-1); the exported 7.625418060200669 s^(-1)*mM^(-1) is the full-precision quotient 0.456 / 0.0598 of the same Table 1 row, which this table prints rounded to its own one-decimal precision as 7.6.

raw_value_unit_evidence: Table 1: Enzymatic specificity of EtAPN1r (Eukaryotic Cell, July 2014, volume 13, number 7, page 891), substrate row 'Ala-ACC': printed Km cell 59.8 uM; printed kcat cell 0.456 s^-1; printed kcat/Km cell 7.6 mM^-1 s^-1.

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

enzyme: aminopeptidase Ey


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'


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'


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'


organism: Mycobacterium tuberculosis

substrate_name: L-Met 4-nitroanilide

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

substrate: L-Met 4-nitroanilide


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.


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


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

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)

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

enzyme: Methionine aminopeptidase 2


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

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


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.

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)


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

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

enzyme: Dipeptidase 2


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

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

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

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


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

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

substrate: 4-nitrophenyl beta-D-xylopyranoside


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


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


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

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


organism: Homo sapiens

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.


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_databases_merged: skid uniprot

enzyme: UniProt Q9AGA6

substrate: trehalose 6-phosphate


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

organism: Saccharomyces cerevisiae

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

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

substrate: Unknown


organism: Rattus norvegicus

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

substrate: hippuryl-L-Arg


organism: Bacillus subtilis

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

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

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.

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

source_databases_merged: sabio_rk brenda skid