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

proof_lines: DELTA357-513 (truncated mutant lacking C-terminal 150 amino acids), pH not specified, 37°C


enzyme_display_name: Protein ARG5,6, mitochondrial

organism: Saccharomyces cerevisiae

substrate_name: ATP

source_db: skid

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY-NC-ND 4.0

km_unit: mM

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) Q01217 direct REST lookup on 2026-06-17

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

assay_conditions_summary: 310.15 K; cofactor ATP

enzyme: Protein ARG5,6, mitochondrial

substrate: ATP

source: skid


enzyme_display_name: Acetylglutamate kinase

organism: Xanthomonas campestris

substrate_name: AcCoA

source_db: brenda

kcat_display: Not reported

source_license: CC BY 4.0

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) Q8P8J6 direct REST lookup on 2026-06-17

proof_lines: only for N-acetylglutamate synthase activity

enzyme: Acetylglutamate kinase

substrate: AcCoA

source: brenda


enzyme_display_name: glucan 1,6-alpha-glucosidase

organism: Streptococcus mutans

substrate_name: H2O; Isomaltose

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

sequence_source: UniProtKB Q99040 direct lookup

unit: lgwedgeoneswedgeone

enzyme: glucan 1,6-alpha-glucosidase

substrate: H2O; Isomaltose


substrate_name: isomaltotriose

source_db: oed

verification_status: verified

kcat_over_km_origin: calculated

assay_conditions_summary: pH 6; 310.15 K; buffer pH 6

column_label: Table 3 (Kinetic parameters of wild type and mutated SMDGs), enzyme-form column group 'Wild type', substrate row 'IG3' (isomaltotriose (IG3)); column 'kcat (s-1)' = 541; column 'Km (mM)' = 3.17; column 'kcat/Km (s-1 mM-1)' = 171; column 'Relative(a)' = 331.

normalized_value_unit_evidence: kcat: printed Table 3 cell 541 s^-1; the turnover column is already per second, so no unit conversion applies and the paper value is 541.0 s^(-1). Km: printed Table 3 cell 3.17 mM; the column is already millimolar, so the paper value is 3.17 mM. kcat/Km: printed Table 3 cell 171 s^-1 mM^-1; the column is already in s^-1 mM^-1, so the paper value is 171.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (Kinetic parameters of wild type and mutated SMDGs), enzyme-form column 'Wild type', substrate row 'IG3': kcat = 541 s^-1; Km = 3.17 mM; printed kcat/Km = 171 s^-1 mM^-1.

table_label: Table 3: Kinetic parameters of wild type and mutated SMDGs (Biochimica et Biophysica Acta 1764 (2006) 688-698)

data_origin: experimental

substrate: isomaltotriose

status: verified

source: oed


substrate_name: Panose

sequence_variant_note: Resolved canonical sequence from UniProtKB Q99040 direct lookup plus row-specific mutation reconstruction and applied mutation signature W238A to reconstruct the assayed variant sequence.

mutation_type: substitution

substrate: Panose


sequence_variant_note: Resolved canonical sequence from UniProtKB Q99040 direct lookup plus row-specific mutation reconstruction and applied mutation signature W238P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q99040 direct lookup plus row-specific mutation reconstruction and applied mutation signature W238N to reconstruct the assayed variant sequence.


substrate_name: isomaltohexaose

sequence_source: UniProtKB Q99040 direct lookup plus row-specific mutation reconstruction

substrate: isomaltohexaose


substrate_name: p-Nitrophenyl-alpha-D-glucoside

substrate: p-Nitrophenyl-alpha-D-glucoside


sequence_source: UniProtKB Q99040 canonical context only; chimeric DOD201-210 sequence not reconstructed

proof_lines: SABIO-RK modifier species: glucan 1,6-alpha-glucosidase(Enzyme) mutant chimeric DOD201-210


substrate_name: isomaltotetraose

substrate: isomaltotetraose


substrate_name: isomaltoheptaose

substrate: isomaltoheptaose


substrate_name: isomaltopentaose

substrate: isomaltopentaose


sequence_source: UniProtKB TrEMBL Q2HWU5 direct lookup (fragment; live accession)


column_label: Table 3 (Kinetic parameters of wild type and mutated SMDGs), enzyme-form column group 'Wild type', substrate row 'IG6' (isomaltohexaose (IG6)); column 'kcat (s-1)' = 401; column 'Km (mM)' = 7.88; column 'kcat/Km (s-1 mM-1)' = 50.9; column 'Relative(a)' = 98.5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 401 s^-1; the turnover column is already per second, so no unit conversion applies and the paper value is 401.0 s^(-1). Km: printed Table 3 cell 7.88 mM; the column is already millimolar, so the paper value is 7.88 mM. kcat/Km: printed Table 3 cell 50.9 s^-1 mM^-1; the column is already in s^-1 mM^-1, so the paper value is 50.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (Kinetic parameters of wild type and mutated SMDGs), enzyme-form column 'Wild type', substrate row 'IG6': kcat = 401 s^-1; Km = 7.88 mM; printed kcat/Km = 50.9 s^-1 mM^-1.


enzyme_display_name: DNA (cytosine-5-)-methyltransferase

organism: Mus musculus

substrate_name: poly(dI*dC-dI*dC) of chain length 5000

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

proof_lines: isoenzyme Dnmt3b2, reaction with poly(dI-dC)-poly(dI-dC)

enzyme: DNA (cytosine-5-)-methyltransferase

substrate: poly(dI*dC-dI*dC) of chain length 5000


organism: Unknown

substrate_name: S-adenosyl-L-methionine

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

substrate: S-adenosyl-L-methionine


enzyme_display_name: ornithine decarboxylase

organism: Trypanosoma brucei

substrate_name: L-Ornithine

proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant D361A N-terminal His6-tagged

enzyme: ornithine decarboxylase

substrate: L-Ornithine


verification_status: unverified

sequence_variant_note: Resolved canonical sequence from UniProtKB P07805 canonical sequence with row-specific substitution reconstructed from PMID 7744828 residue numbering mapped to P07805 by minus-two offset and applied mutation signature E274A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

status: unverified


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant D361E N-terminal His6-tagged


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant E274A N-terminal His6-tagged


sequence_source: UniProtKB P07805 canonical sequence with row-specific substitution reconstructed from PMID 7744828 residue numbering mapped to P07805 by minus-two offset

sequence_variant_note: Mutation signature D233A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: L-Lysine

sequence_source: UniProtKB REST P07805 canonical sequence

substrate: L-Lysine


proof_lines: SABIO-RK modifier species: ornithine decarboxylase(Enzyme) mutant D233A N-terminal His6-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB P07805 canonical sequence with row-specific substitution reconstructed from PMID 7744828 residue numbering mapped to P07805 by minus-two offset and applied mutation signature E94A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


organism: Haemophilus aegyptius

sequence_source: UniProtKB:P20589 direct REST lookup on 2026-06-17


organism: Haemophilus parahaemolyticus

substrate_name: Cytosine (in DNA); S-Adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P05102 direct REST lookup on 2026-06-17 and applied mutation signature Q237S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA (cytosine-5-)-methyltransferase(Enzyme) mutant Q237S


substrate_name: S-Adenosyl-L-methionine; Cytosine (in DNA)

sequence_variant_note: Resolved canonical sequence from UniProtKB:P05102 direct REST lookup on 2026-06-17 and applied mutation signature Q237A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA (cytosine-5-)-methyltransferase(Enzyme) mutant Q237A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05102 direct REST lookup on 2026-06-17 and applied mutation signature Q237L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA (cytosine-5-)-methyltransferase(Enzyme) mutant Q237L

substrate: Cytosine (in DNA); S-Adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05102 direct REST lookup on 2026-06-17 and applied mutation signature Q237E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA (cytosine-5-)-methyltransferase(Enzyme) mutant Q237E


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05102 direct REST lookup on 2026-06-17 and applied mutation signature Q237H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: DNA (cytosine-5-)-methyltransferase(Enzyme) mutant Q237H


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

sequence_source: UniProtKB:P05102 direct REST lookup on 2026-06-17


organism: Homo sapiens

substrate_name: linear pRW 3602 DNA containing cytosine

sequence_source: UniProtKB:P26358 direct REST lookup on 2026-06-17

proof_lines:
reaction with poly(dI-dC)*poly(dI-dC)
reaction with (CGG*CCG)73
reaction with pRW3602, supercoiled

substrate: linear pRW 3602 DNA containing cytosine


substrate_name: mononucleosomal DNA containing cytosine

sequence_source: UniProtKB:Q9Y6K1 direct REST lookup on 2026-06-17

substrate: mononucleosomal DNA containing cytosine


substrate_name: dGdC

sequence_source: UniProtKB:O88509 direct REST lookup on 2026-06-17

substrate: dGdC


sequence_source: UniProtKB:O88508 direct REST lookup on 2026-06-17

proof_lines:
enzyme Dnmt3A, in absence of Dnmt3L
enzyme Dnmt3A, in presence of Dnmt3L
pH 7.4, 37°C, Dnmt3b


organism: Oryza sativa

sequence_source: UniProtKB:Q7Y1I7 direct REST lookup on 2026-06-17


organism: Helicobacter pylori

substrate_name: GDP-beta-L-fucose

sequence_variant_note: Resolved canonical sequence from UniProtKB:O25142 direct REST lookup on 2026-06-17 and applied mutation signature A128N/H129E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A128N/H129E, at pH 7.6 and 37°C

substrate: GDP-beta-L-fucose


substrate_name: D-lactose

sequence_variant_note: Resolved canonical sequence from UniProtKB:O25142 direct REST lookup on 2026-06-17 and applied mutation signature A128N/H129E/Y132I/S46F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A128N/H129E/Y132I/S46F, at pH 7.6 and 37°C

substrate: D-lactose


sequence_variant_note: Resolved canonical sequence from UniProtKB:O25142 direct REST lookup on 2026-06-17 and applied mutation signature A128N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O25142 direct REST lookup on 2026-06-17 and applied mutation signature A128N/H129E/S46F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A128N/H129E/S46F, at pH 7.6 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession O25142 checked 2026-06-17 and applied mutation signature A128N/H129E/Y132I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A128N/H129E/Y132I, at pH 7.6 and 37°C


sequence_source: UniProtKB REST accession O25142 checked 2026-06-17

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


substrate_name: lactose

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

sequence_source: UniProtKB REST accession O30511 checked 2026-06-17

proof_lines: cosubstrate N-acetyllactosamine, pH 7.5, 37°C

source_databases_merged: brenda skid

substrate: lactose


substrate_name: N-acetyllactosamine

substrate: N-acetyllactosamine


substrate_name: GDP-beta-fucose

substrate: GDP-beta-fucose


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q99040 checked 2026-06-17 and applied mutation signature W238A to reconstruct the assayed variant sequence.


substrate_name: p-Nitrophenyl-alpha-D-glucoside

sequence_source: UniProtKB REST accession Q99040 checked 2026-06-17

column_label: Table 3 (Kinetic parameters of wild type and mutated SMDGs), enzyme-form column group 'Wild type', substrate row 'pNPG' (pNPG, p-nitrophenyl alpha-D-glucoside); column 'kcat (s-1)' = 235; column 'Km (mM)' = 0.549; column 'kcat/Km (s-1 mM-1)' = 428; column 'Relative(a)' = 828.

normalized_value_unit_evidence: kcat: printed Table 3 cell 235 s^-1; the turnover column is already per second, so no unit conversion applies and the paper value is 235.0 s^(-1). Km: printed Table 3 cell 0.549 mM; the column is already millimolar, so the paper value is 0.549 mM. kcat/Km: printed Table 3 cell 428 s^-1 mM^-1; the column is already in s^-1 mM^-1, so the paper value is 428.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (Kinetic parameters of wild type and mutated SMDGs), enzyme-form column 'Wild type', substrate row 'pNPG': kcat = 235 s^-1; Km = 0.549 mM; printed kcat/Km = 428 s^-1 mM^-1.

substrate: p-Nitrophenyl-alpha-D-glucoside


substrate_name: isomaltotriose

substrate: isomaltotriose


substrate_name: Isomaltose

column_label: Table 3 (Kinetic parameters of wild type and mutated SMDGs), enzyme-form column group 'Wild type', substrate row 'IG2' (isomaltose (IG2)); column 'kcat (s-1)' = 483; column 'Km (mM)' = 9.35; column 'kcat/Km (s-1 mM-1)' = 51.7; column 'Relative(a)' = 100.

normalized_value_unit_evidence: kcat: printed Table 3 cell 483 s^-1; the turnover column is already per second, so no unit conversion applies and the paper value is 483.0 s^(-1). Km: printed Table 3 cell 9.35 mM; the column is already millimolar, so the paper value is 9.35 mM. kcat/Km: printed Table 3 cell 51.7 s^-1 mM^-1; the column is already in s^-1 mM^-1, so the paper value is 51.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (Kinetic parameters of wild type and mutated SMDGs), enzyme-form column 'Wild type', substrate row 'IG2': kcat = 483 s^-1; Km = 9.35 mM; printed kcat/Km = 51.7 s^-1 mM^-1.

substrate: Isomaltose


substrate_name: Panose

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q99040 checked 2026-06-17 and applied mutation signature W238P to reconstruct the assayed variant sequence.

substrate: Panose


substrate_name: isomaltopentaose

column_label: Table 3 (Kinetic parameters of wild type and mutated SMDGs), enzyme-form column group 'Wild type', substrate row 'IG5' (isomaltopentaose (IG5)); column 'kcat (s-1)' = 419; column 'Km (mM)' = 5.10; column 'kcat/Km (s-1 mM-1)' = 82.2; column 'Relative(a)' = 159.

normalized_value_unit_evidence: kcat: printed Table 3 cell 419 s^-1; the turnover column is already per second, so no unit conversion applies and the paper value is 419.0 s^(-1). Km: printed Table 3 cell 5.10 mM; the column is already millimolar, so the paper value is 5.1 mM. kcat/Km: printed Table 3 cell 82.2 s^-1 mM^-1; the column is already in s^-1 mM^-1, so the paper value is 82.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (Kinetic parameters of wild type and mutated SMDGs), enzyme-form column 'Wild type', substrate row 'IG5': kcat = 419 s^-1; Km = 5.10 mM; printed kcat/Km = 82.2 s^-1 mM^-1.

substrate: isomaltopentaose


substrate_name: isomaltohexaose

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q2HWU5 checked 2026-06-17 and applied mutation signature W238A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

substrate: isomaltohexaose


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q99040 checked 2026-06-17 and applied mutation signature W238N to reconstruct the assayed variant sequence.


enzyme_display_name: phospholipase A2

organism: Macrovipera lebetinus

substrate_name: Unknown

source_db: uniprot

km_display: Not reported

enzyme: phospholipase A2

substrate: Unknown

source: uniprot


substrate_name: oleoyl-CoA

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

assay_conditions_summary: cofactor CoA

substrate: oleoyl-CoA


organism: Naja haje haje


organism: Naja kaouthia


organism: Oxyuranus scutellatus

sequence: NLAQFGFMIRCANGGSRSAL

wild_type_sequence: NLAQFGFMIRCANGGSRSAL


organism: Oxyuranus scutellatus scutellatus


organism: Rattus norvegicus

substrate_name: dipalmitoyl phosphatidylcholine

substrate: dipalmitoyl phosphatidylcholine


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: phosphatidylethanolamine (PE)

substrate: phosphatidylethanolamine (PE)


organism: Scolopendra dehaani


sequence: SLANFLSMTLTAAKRKPKEYDGYGNYCG

wild_type_sequence: SLANFLSMTLTAAKRKPKEYDGYGNYCG


organism: Vipera renardi


organism: Walterinnesia aegyptia

sequence: NLYQFKNMVQCVGTQLCVAYVKYGCYCGPG

wild_type_sequence: NLYQFKNMVQCVGTQLCVAYVKYGCYCGPG


enzyme_display_name: acetylspermidine deacetylase

organism: Danio rerio

substrate_name: acetylcadaverine

enzyme: acetylspermidine deacetylase

substrate: acetylcadaverine


organism: Mycoplana ramosa

substrate_name: N-acetylcadaverine

substrate: N-acetylcadaverine


organism: Selenomonas ruminantium

substrate_name: L-lysine

substrate: L-lysine


enzyme_display_name: acetylglutamate kinase

organism: Escherichia coli (strain K12)

substrate_name: N-acetyl-L-glutamate

assay_conditions_summary: cofactor ATP

enzyme: acetylglutamate kinase

substrate: N-acetyl-L-glutamate


organism: Bothrops jararacussu

substrate_name: 4-nitro-3-(octanoyloxy)benzoic acid

sequence: DLWSWGQMIQETGLLPSYTTY

wild_type_sequence: DLWSWGQMIQETGLLPSYTTY

substrate: 4-nitro-3-(octanoyloxy)benzoic acid


organism: Carcinus aestuarii

substrate_name: phosphatidylcholine (in the presence of 8 mM NaDC and 10 mM CaCl(2), at 50 degrees Celsius and pH 8)

sequence: XIGAGATSKLVY

assay_conditions_summary: pH 8


organism: Crotalus durissus cumanensis

sequence: SLVQFEKMIKEVAGKNGVPWY

wild_type_sequence: SLVQFEKMIKEVAGKNGVPWY


organism: Crotalus durissus ruruima

substrate_name: NOBA

substrate: NOBA


organism: Crotalus durissus terrificus


substrate_name: 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (monomer CBb)


substrate_name: 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (monomer CBd)


substrate_name: 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (monomer CBa2)


organism: Crotalus lutosus

substrate_name: 4-nitro-3-octanoyl benzioc acid (NOBA)

substrate: 4-nitro-3-octanoyl benzioc acid (NOBA)


organism: Crotalus tzabcan

substrate_name: 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (monomer CBc)


organism: Daboia russelii

substrate_name: diheptanoyl thio-phosphatidylcholine

substrate: diheptanoyl thio-phosphatidylcholine


organism: Echis carinatus

substrate_name: phospholipids

substrate: phospholipids


organism: Homo sapiens

substrate_name: Unknown


substrate_name: dipalmitoyl-PC

substrate: dipalmitoyl-PC


substrate_name: triacylglycerol

substrate: triacylglycerol


substrate_name: palmitoyl-CoA (lysophosphatidylcholine acyltransferase activity at pH 4.0)

assay_conditions_summary: pH 4; cofactor CoA


organism: Lachesis muta rhombeata

substrate_name: 4-nitro-3-(octanoyloxy) benzoic acid

substrate: 4-nitro-3-(octanoyloxy) benzoic acid


organism: Macrovipera lebetinus


organism: Escherichia coli

substrate_name: H+; NADPH; L-2,3-Dihydrodipicolinate

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

ki_unit: mM

assay_conditions_summary: cofactor NADPH

proof_lines: histidine-tagged enzyme, pH and temperature not specified in the publication

source_databases_merged: sabio_rk brenda skid

substrate: H+; NADPH; L-2,3-Dihydrodipicolinate


substrate_name: NADH; L-2,3-Dihydrodipicolinate; H+

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature H159Q to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NADH

proof_lines: SABIO-RK modifier species: 4-hydroxy-tetrahydrodipicolinate reductase(Enzyme) mutant H159Q

substrate: NADH; L-2,3-Dihydrodipicolinate; H+


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature K163Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-tetrahydrodipicolinate reductase(Enzyme) mutant K163Q


substrate_name: L-2,3-Dihydrodipicolinate; NADH; H+

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature K163C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-tetrahydrodipicolinate reductase(Enzyme) mutant K163C

substrate: L-2,3-Dihydrodipicolinate; NADH; H+


substrate_name: H+; L-2,3-Dihydrodipicolinate; NADH

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature H159A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-tetrahydrodipicolinate reductase(Enzyme) mutant H159A

substrate: H+; L-2,3-Dihydrodipicolinate; NADH


substrate_name: L-2,3-Dihydrodipicolinate; H+; NADH

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature K163A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-tetrahydrodipicolinate reductase(Enzyme) mutant K163A

substrate: L-2,3-Dihydrodipicolinate; H+; NADH


organism: Mycobacterium tuberculosis

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature K9A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-tetrahydrodipicolinate reductase(Enzyme) mutant K9A


substrate_name: NADH

substrate: NADH


substrate_name: NADH; H+; L-2,3-Dihydrodipicolinate

proof_lines: pH and temperature not specified in the publication

substrate: NADH; H+; L-2,3-Dihydrodipicolinate


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature K11A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-tetrahydrodipicolinate reductase(Enzyme) mutant K11A


organism: Neisseria meningitidis

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines:
pH 8.0, 25°C, cofactor: NADPH
pH 8.0, 25°C, cofactor: NADH
pH 8.0, 25°C


organism: Selaginella moellendorffii


organism: Staphylococcus aureus

substrate_name: NADPH

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

substrate: NADPH


organism: Thermotoga maritima

proof_lines:
apparent value, at 30°C
apparent value, at 45°C
at 30°C


organism: Trichormus variabilis

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

assay_conditions_summary: 303.15 K; cofactor NADH

proof_lines: 30°C, pH not specified in the publication


organism: Vitis vinifera


organism: Streptococcus mutans

substrate_name: isomaltotetraose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W238N with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

substrate: isomaltotetraose


substrate_name: Isomaltose; H2O

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W238P to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucan 1,6-alpha-glucosidase(Enzyme) mutant W238P

substrate: Isomaltose; H2O


substrate_name: H2O; Isomaltose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W238A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucan 1,6-alpha-glucosidase(Enzyme) mutant W238A

substrate: H2O; Isomaltose


substrate_name: isomaltopentaose

substrate: isomaltopentaose


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

column_label: Table 3 (Kinetic parameters of wild type and mutated SMDGs), enzyme-form column group 'Wild type', substrate row 'IG4' (isomaltotetraose (IG4)); column 'kcat (s-1)' = 499; column 'Km (mM)' = 5.58; column 'kcat/Km (s-1 mM-1)' = 89.4; column 'Relative(a)' = 173.

normalized_value_unit_evidence: kcat: printed Table 3 cell 499 s^-1; the turnover column is already per second, so no unit conversion applies and the paper value is 499.0 s^(-1). Km: printed Table 3 cell 5.58 mM; the column is already millimolar, so the paper value is 5.58 mM. kcat/Km: printed Table 3 cell 89.4 s^-1 mM^-1; the column is already in s^-1 mM^-1, so the paper value is 89.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (Kinetic parameters of wild type and mutated SMDGs), enzyme-form column 'Wild type', substrate row 'IG4': kcat = 499 s^-1; Km = 5.58 mM; printed kcat/Km = 89.4 s^-1 mM^-1.


substrate_name: Isomaltose

substrate: Isomaltose


organism: Unknown


enzyme_display_name: stratum corneum chymotryptic enzyme

sequence_source: UniProtKB reviewed P49862 direct REST lookup, 2026-06-17

enzyme: stratum corneum chymotryptic enzyme


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

proof_lines: mutant S195A, pH 8.0, temperature not specified in the publication


proof_lines: wild-type, pH 8.0, temperature not specified in the publication


organism: Mus musculus

substrate_name: Unknown

sequence_source: UniProtKB reviewed Q91VE3 direct REST lookup, 2026-06-17

proof_lines: pH 8.0, temperature not specified in the publication

substrate: Unknown


sequence_source: UniProtKB REST/FASTA direct check for reviewed accession P49862 (KLK7_HUMAN, Homo sapiens, EC 3.4.21.117)


enzyme_display_name: 4-hydroxybenzoate 3-monooxygenase

organism: Pseudomonas fluorescens

substrate_name: p-OHB

assay_conditions_summary: pH 6; cofactor NADPH

proof_lines: kcat is 55 sec(-1) for hydroxylase activity (PubMed:9578477, PubMed:9694855). kcat is 55 sec(-1) for hydroxylase activity (at 25 degrees Celsius) (PubMed:1459126). kcat is 55 sec(-1) for hydroxylase activity (at pH 8) (PubMed:10025942, PubM

enzyme: 4-hydroxybenzoate 3-monooxygenase

substrate: p-OHB


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


substrate_name: GDP-fucose

proof_lines: kcat is 1.70 min(-1) for the alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc (PubMed:9737989). kcat is 9.3 min(-1) for the beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine (PubMed:9737988).

substrate: GDP-fucose


substrate_name: N-acetyllactosamine

proof_lines: kcat is 0.59 sec(-1) for LNnT. kcat is 0.43 sec(-1) for H-type 2 LacNAc. kcat is 0.41 sec(-1) for type 2 LacNAc. kcat is 0.58 sec(-1) for sialyl-type 2 LacNAc. kcat is 0.49 sec(-1) for GDP-fucose.

substrate: N-acetyllactosamine


enzyme_display_name: uridine phosphorylase

organism: Schistosoma mansoni

substrate_name: uridine

proof_lines: kcat is 35.9 sec(-1) for uridine. kcat is 0.41 sec(-1) for thymidine.

enzyme: uridine phosphorylase

substrate: uridine


enzyme_display_name: choline-phosphate cytidylyltransferase

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

substrate_name: phosphocholine

proof_lines: kcat is 17.5 sec(-1) with phosphocholine as substrate (PubMed:11786295). kcat is 1.06 sec(-1) with phosphocholine as substrate. kcat is 0.72 sec(-1) with 2-aminoethylphosphonate as substrate (PubMed:31420548).

enzyme: choline-phosphate cytidylyltransferase

substrate: phosphocholine


organism: Bothriechis schlegelii


organism: Cerrophidion godmani


organism: Crotalus durissus terrificus

sequence: HLLQFNKMIKFETGKNAIPFYAF

wild_type_sequence: HLLQFNKMIKFETGKNAIPFYAF


organism: Crotalus horridus


organism: Crotalus lepidus lepidus


organism: Crotalus mitchellii mitchellii

sequence: SLLQFNKMIKFETRKNAIPFYAF

wild_type_sequence: SLLQFNKMIKFETRKNAIPFYAF


organism: Bacillus subtilis (strain 168)


organism: Haemophilus parahaemolyticus

substrate_name: DNA

substrate: DNA


organism: Helicobacter pylori


organism: Homo sapiens


enzyme_display_name: amidophosphoribosyltransferase

organism: Arabidopsis thaliana

substrate_name: glutamine

enzyme: amidophosphoribosyltransferase

substrate: glutamine


organism: Escherichia coli (strain K12)

substrate_name: phosphoribosylpyrophosphate

substrate: phosphoribosylpyrophosphate


substrate_name: N-acetyl glutamate (NAG)

substrate: N-acetyl glutamate (NAG)


organism: Drosophila melanogaster

substrate_name: CTP

sequence_source: UniProtKB Q7K4C7 direct accession lookup, release 2026_02 (10-June-2026)

substrate: CTP


substrate_name: choline phosphate

sequence_source: UniProtKB Q9W0D9 direct accession lookup, release 2026_02 (10-June-2026)

substrate: choline phosphate


organism: Pisum sativum

substrate_name: Choline phosphate; CTP

sequence_source: UniProtKB P93470 direct accession lookup, release 2026_02 (10-June-2026)

substrate: Choline phosphate; CTP


organism: Plasmodium falciparum

sequence_source: UniProtKB Q8IEE9 direct accession lookup, release 2026_02 (10-June-2026)

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

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


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8IEE9 direct accession lookup, release 2026_02 (10-June-2026) and applied mutation signature H630N to reconstruct the assayed variant sequence.

proof_lines: H630N mutant, pH and temperature not specified in the publication

proof_lines: pH and temperature not specified in the publication, H630N mutant


organism: Rattus norvegicus

sequence_source: UniProtKB P19836 direct accession lookup, release 2026_02 (10-June-2026)

sequence_variant_note: Mutation signature Y173A matches the mutant residue at offset +0 and the reference residue at offset +9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: Y173A mutant deletion construct 1-236, 8.8 mM CTP

proof_lines: Y173A mutant deletion construct 1-236, 1.5 mM choline phosphate


proof_lines: wild-type deletion construct 1-236, 8.8 mM CTP

proof_lines: wild-type deletion construct 1-236, 1.5 mM choline phosphate


sequence_variant_note: Mutation signature H168A matches the mutant residue at offset +0 and the reference residue at offset -7; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: H168A mutant deletion construct 1-236, 8.8 mM CTP

proof_lines: H168A mutant deletion construct 1-236, 1.5 mM choline phosphate


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

proof_lines: H168A/Y173A mutant deletion construct 1-236, 1.5 mM choline phosphate

proof_lines: H168A/Y173A mutant deletion construct 1-236, 8.8 mM CTP


organism: Streptococcus pneumoniae


sequence_source: UniProtKB P49862 direct accession lookup, release 2026_02 (10-June-2026)


enzyme_display_name: phenylpyruvate decarboxylase

organism: Saccharomyces cerevisiae

substrate_name: 2-oxohexanoic acid

sequence_source: UniProtKB Q06408 canonical FASTA direct lookup

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

enzyme: phenylpyruvate decarboxylase

substrate: 2-oxohexanoic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB Q06408 canonical FASTA direct lookup; variant reconstructed from the selected mutation signature and applied mutation signature I335Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; buffer 100 mM KPO4

proof_lines: mutant enzyme I335Y, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C


substrate_name: 4-methylthio-2-oxobutanoic acid

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

substrate: 4-methylthio-2-oxobutanoic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB Q06408 canonical FASTA direct lookup; variant reconstructed from the selected mutation signature and applied mutation signature I335Y/M624W to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I335Y/M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C


substrate_name: 2-oxopentanoic acid

sequence_source: UniProtKB Q06408 canonical FASTA direct lookup; variant reconstructed from the selected mutation signature

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

substrate: 2-oxopentanoic acid


substrate_name: phenylpyruvate

assay_conditions_summary: pH 7; 303.15 K; buffer 100 mM KPO4; cofactor NADH

column_label: Table 1: ScPPDC substrate profile (FEBS Journal 2011, 278(11):1842-1853); printed column heads Substrate | Amino acid | Km (mM) | kcat (s^-1) | kcat/Km (mM^-1 s^-1) | % of the kcat/Km for PPA. Table 1, body row 'Phenylpyruvic acid' (amino acid Phe); column 'Km (mM)' = 0.10; column 'kcat (s^-1)' = 20; column 'kcat/Km (mM^-1 s^-1)' = 200. captured primary segment: ScPPDC-His | Phenylpyruvic acid | Phe | Km 0.10 ± 0.01 mM | kcat 20 ± 2.1 s^-1 | kcat/Km 200 mM^-1 s^-1 | 100 %

normalized_value_unit_evidence: Km: printed Table 1 cell 0.10 mM; the printed concentration column is already in mM, so no unit conversion applies and the value is 0.1 mM. kcat: printed Table 1 cell 20 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 20.0 s^(-1). kcat/Km: printed Table 1 cell 200 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the value is 200.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 20 / 0.10 = 200.0 s^-1 mM^-1, the same number as the printed efficiency cell.

raw_value_unit_evidence: Table 1, body row 'Phenylpyruvic acid': Km = 0.10 mM; kcat = 20 s^-1; printed kcat/Km = 200 mM^-1 s^-1.

substrate: phenylpyruvate


substrate_name: Pyruvic acid

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

substrate: Pyruvic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB Q06408 canonical FASTA direct lookup; variant reconstructed from the selected mutation signature and applied mutation signature E545L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E545L, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q06408 canonical FASTA direct lookup; variant reconstructed from the selected mutation signature and applied mutation signature Q448W to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q448W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q06408 canonical FASTA direct lookup; variant reconstructed from the selected mutation signature and applied mutation signature M624W to reconstruct the assayed variant sequence.


substrate_name: 2-oxobutanoic acid

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

substrate: 2-oxobutanoic acid


substrate_name: 3-methyl-2-oxopentanoic acid

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

substrate: 3-methyl-2-oxopentanoic acid


enzyme_display_name: signal peptidase I

organism: Escherichia coli

substrate_name: m n n+m n m n+m n m n+m n m n+m n m n+m m n n+m m n n+m n m n+m n m n+m m n n+m m n n+m n m n+m m n n+m n m n+m n m n...

sequence_variant_note: Resolved canonical sequence from UniProtKB:P00803 canonical sequence with PMID 15195997/source mutation label; paper numbering maps to UniProt position +1. and applied mutation signature R77A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R77A

enzyme: signal peptidase I


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00803 canonical sequence with PMID 15195997/source mutation label; paper numbering maps to UniProt position +1. and applied mutation signature R295A with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R295A

substrate: m n n+m n m n+m n m n+m n m n+m n m n+m m n n+m m n n+m n m n+m n m n+m m n n+m m n n+m n m n+m m n n+m n m n+m n m n...


substrate_name: Peptide

sequence_source: UniProtKB:P00803 canonical sequence with PMID 15195997/source mutation label; paper numbering maps to UniProt position +1.

sequence_variant_note: Mutation signature R236A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: Peptide


substrate_name: H2O; m n n+m n m n+m n m n+m n m n+m n m n+m m n n+m m n n+m n m n+m n m n+m m n n+m m n n+m n m n+m m n n+m n m n+m ...

sequence_variant_note: Resolved canonical sequence from UniProtKB:P00803 canonical sequence with PMID 15195997/source mutation label; paper numbering maps to UniProt position +1. and applied mutation signature R226A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R226A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00803 canonical sequence with PMID 15195997/source mutation label; paper numbering maps to UniProt position +1. and applied mutation signature R222A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature R315A matches the mutant residue at offset +1 and the reference residue at offset +4; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R315A

substrate: H2O; m n n+m n m n+m n m n+m n m n+m n m n+m m n n+m m n n+m n m n+m n m n+m m n n+m m n n+m n m n+m m n n+m n m n+m ...


organism: Thermococcus kodakaraensis

sequence_source: UniProtKB:Q5JE91 checked as context only; sequence not accepted for EC 3.4.21.89 because the accession/protein family conflicts with the selected EC.

proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant S184A


proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant D277A


proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant H191A


proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant K150A


proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant E226A


proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant S131A


proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant R221A


proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant Y165A


proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant R250A


enzyme_display_name: lysine decarboxylase

organism: Selenomonas ruminantium

substrate_name: L-Lys

verification_status: corrected

sequence_source: UniProt O50657 direct accession lookup; variant sequence reconstructed from selected BRENDA mutation_signature when present

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

assay_conditions_summary: pH 6; 303.15 K; buffer containing 50 uM PLP and 0

column_label: Table 2: Kinetic parameters for the decarboxylation of lysine and ornithine by wild-type and mutant LDCs and mouse ODC (J. Bacteriol. 2000, 182(23):6732-6741); printed column heads Line no. | Mutant no. | Enzyme | Km (mM) Lysine | Km (mM) Ornithine | kcat (s^-1) Lysine | kcat (s^-1) Ornithine | kcat/Km ratio Lysine | kcat/Km ratio Ornithine | Substrate specificity. Table 2, line no. 2, Enzyme column 'Wild-type rLDC', Lysine sub-columns; column Km (mM) Lysine = 1.5; column kcat (s^-1) Lysine = 16; column kcat/Km ratio Lysine = 11,000. captured primary segment: L-lysine | Wild-type rLDC | Table 2, line no. 2 | Km 1.5 mM | kcat 16 s^-1 | kcat/Km ratio 11,000 (printed kcat/Km ratio cell; the ratio column head carries no printed unit, and the cell is in M^-1 s^-1 on this row's own printed Km (mM) and kcat (s^-1) columns)

normalized_value_unit_evidence: Km: printed Table 2 Lysine Km cell 1.5 mM; the printed Km column is already in mM, so no unit conversion applies and the value is 1.5 mM. kcat: printed Table 2 Lysine kcat cell 16 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 16.0 s^(-1). kcat/Km: printed Table 2 Lysine ratio cell 11,000 in M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 11,000 / 1000 = 11.0 s^-1 mM^-1. Quotient disclosure for this measurement: 16.0 / 1.5 = 10.666666666666666 s^-1 mM^-1, against the printed ratio cell 11.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, line no. 2, Enzyme column 'Wild-type rLDC', Lysine sub-columns: Km = 1.5 mM; kcat = 16 s^-1; printed kcat/Km ratio cell = 11,000, in a column whose head carries no printed unit and whose basis is M^-1 s^-1 on this line's own printed Km (mM) and kcat (s^-1) columns.

enzyme: lysine decarboxylase

substrate: L-Lys

status: corrected


substrate_name: L-Orn

sequence_variant_note: Resolved canonical sequence from UniProt O50657 direct accession lookup; variant sequence reconstructed from selected BRENDA mutation_signature when present and applied mutation signature A44V/G45T/V46P/P54D/S322T/I326L to reconstruct the assayed variant sequence.

proof_lines: pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322T/I326L

substrate: L-Orn


sequence_variant_note: Resolved canonical sequence from UniProt O50657 direct accession lookup; variant sequence reconstructed from selected BRENDA mutation_signature when present and applied mutation signature S322A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O50657 and applied mutation signature P54D to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters for the decarboxylation of lysine and ornithine by wild-type and mutant LDCs and mouse ODC (J. Bacteriol. 2000, 182(23):6732-6741); printed column heads Line no. | Mutant no. | Enzyme | Km (mM) Lysine | Km (mM) Ornithine | kcat (s^-1) Lysine | kcat (s^-1) Ornithine | kcat/Km ratio Lysine | kcat/Km ratio Ornithine | Substrate specificity. Table 2, line no. 5, Enzyme column 'P54D' (Mutant no. 6), Lysine sub-columns; column Km (mM) Lysine = 5.7; column kcat (s^-1) Lysine = 16; column kcat/Km ratio Lysine = 2,900. captured primary segment: L-lysine | mutant 6 P54D | Table 2, line no. 5 | Km 5.7 mM | kcat 16 s^-1 | kcat/Km ratio 2,900 (printed kcat/Km ratio cell; the ratio column head carries no printed unit, and the cell is in M^-1 s^-1 on this row's own printed Km (mM) and kcat (s^-1) columns)

normalized_value_unit_evidence: Km: printed Table 2 Lysine Km cell 5.7 mM; the printed Km column is already in mM, so no unit conversion applies and the value is 5.7 mM. kcat: printed Table 2 Lysine kcat cell 16 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 16.0 s^(-1). kcat/Km: printed Table 2 Lysine ratio cell 2,900 in M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2,900 / 1000 = 2.9 s^-1 mM^-1. Quotient disclosure for this measurement: 16.0 / 5.7 = 2.807017543859649 s^-1 mM^-1, against the printed ratio cell 2.9 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, line no. 5, Enzyme column 'P54D' (Mutant no. 6), Lysine sub-columns: Km = 5.7 mM; kcat = 16 s^-1; printed kcat/Km ratio cell = 2,900, in a column whose head carries no printed unit and whose basis is M^-1 s^-1 on this line's own printed Km (mM) and kcat (s^-1) columns.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O50657 and applied mutation signature M50V/A52C/P54D/T55S to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters for the decarboxylation of lysine and ornithine by wild-type and mutant LDCs and mouse ODC (J. Bacteriol. 2000, 182(23):6732-6741); printed column heads Line no. | Mutant no. | Enzyme | Km (mM) Lysine | Km (mM) Ornithine | kcat (s^-1) Lysine | kcat (s^-1) Ornithine | kcat/Km ratio Lysine | kcat/Km ratio Ornithine | Substrate specificity. Table 2, line no. 7, Enzyme column 'M50V/A52C/P54D/T55S' (Mutant no. 13), Lysine sub-columns; column Km (mM) Lysine = 3.6; column kcat (s^-1) Lysine = 2.6; column kcat/Km ratio Lysine = 700. captured primary segment: L-lysine | mutant 13 M50V/A52C/P54D/T55S | Table 2, line no. 7 | Km 3.6 mM | kcat 2.6 s^-1 | kcat/Km ratio 700 (printed kcat/Km ratio cell; the ratio column head carries no printed unit, and the cell is in M^-1 s^-1 on this row's own printed Km (mM) and kcat (s^-1) columns)

normalized_value_unit_evidence: Km: printed Table 2 Lysine Km cell 3.6 mM; the printed Km column is already in mM, so no unit conversion applies and the value is 3.6 mM. kcat: printed Table 2 Lysine kcat cell 2.6 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 2.6 s^(-1). kcat/Km: printed Table 2 Lysine ratio cell 700 in M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 700 / 1000 = 0.7 s^-1 mM^-1. Quotient disclosure for this measurement: 2.6 / 3.6 = 0.7222222222222222 s^-1 mM^-1, against the printed ratio cell 0.7 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, line no. 7, Enzyme column 'M50V/A52C/P54D/T55S' (Mutant no. 13), Lysine sub-columns: Km = 3.6 mM; kcat = 2.6 s^-1; printed kcat/Km ratio cell = 700, in a column whose head carries no printed unit and whose basis is M^-1 s^-1 on this line's own printed Km (mM) and kcat (s^-1) columns.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O50657 and applied mutation signature A52C to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters for the decarboxylation of lysine and ornithine by wild-type and mutant LDCs and mouse ODC (J. Bacteriol. 2000, 182(23):6732-6741); printed column heads Line no. | Mutant no. | Enzyme | Km (mM) Lysine | Km (mM) Ornithine | kcat (s^-1) Lysine | kcat (s^-1) Ornithine | kcat/Km ratio Lysine | kcat/Km ratio Ornithine | Substrate specificity. Table 2, line no. 4, Enzyme column 'A52C' (Mutant no. 5), Ornithine sub-columns; column Km (mM) Ornithine = 1.3; column kcat (s^-1) Ornithine = 7.0; column kcat/Km ratio Ornithine = 5,500. captured primary segment: L-ornithine | mutant 5 A52C | Table 2, line no. 4 | Km 1.3 mM | kcat 7.0 s^-1 | kcat/Km ratio 5,500 (printed kcat/Km ratio cell; the ratio column head carries no printed unit, and the cell is in M^-1 s^-1 on this row's own printed Km (mM) and kcat (s^-1) columns)

normalized_value_unit_evidence: Km: printed Table 2 Ornithine Km cell 1.3 mM; the printed Km column is already in mM, so no unit conversion applies and the value is 1.3 mM. kcat: printed Table 2 Ornithine kcat cell 7.0 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 7.0 s^(-1). kcat/Km: printed Table 2 Ornithine ratio cell 5,500 in M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5,500 / 1000 = 5.5 s^-1 mM^-1. Quotient disclosure for this measurement: 7.0 / 1.3 = 5.384615384615384 s^-1 mM^-1, against the printed ratio cell 5.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, line no. 4, Enzyme column 'A52C' (Mutant no. 5), Ornithine sub-columns: Km = 1.3 mM; kcat = 7.0 s^-1; printed kcat/Km ratio cell = 5,500, in a column whose head carries no printed unit and whose basis is M^-1 s^-1 on this line's own printed Km (mM) and kcat (s^-1) columns.


sequence_variant_note: Resolved canonical sequence from UniProt O50657 direct accession lookup; variant sequence reconstructed from selected BRENDA mutation_signature when present and applied mutation signature A52C/P54D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O50657 and applied mutation signature A44V/G45T/V46P to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters for the decarboxylation of lysine and ornithine by wild-type and mutant LDCs and mouse ODC (J. Bacteriol. 2000, 182(23):6732-6741); printed column heads Line no. | Mutant no. | Enzyme | Km (mM) Lysine | Km (mM) Ornithine | kcat (s^-1) Lysine | kcat (s^-1) Ornithine | kcat/Km ratio Lysine | kcat/Km ratio Ornithine | Substrate specificity. Table 2, line no. 3, Enzyme column 'A44V/G45T/V46P' (Mutant no. 2), Lysine sub-columns; column Km (mM) Lysine = 3.0; column kcat (s^-1) Lysine = 13; column kcat/Km ratio Lysine = 4,300. captured primary segment: L-lysine | mutant 2 A44V/G45T/V46P | Table 2, line no. 3 | Km 3.0 mM | kcat 13 s^-1 | kcat/Km ratio 4,300 (printed kcat/Km ratio cell; the ratio column head carries no printed unit, and the cell is in M^-1 s^-1 on this row's own printed Km (mM) and kcat (s^-1) columns)

normalized_value_unit_evidence: Km: printed Table 2 Lysine Km cell 3.0 mM; the printed Km column is already in mM, so no unit conversion applies and the value is 3.0 mM. kcat: printed Table 2 Lysine kcat cell 13 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 13.0 s^(-1). kcat/Km: printed Table 2 Lysine ratio cell 4,300 in M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4,300 / 1000 = 4.3 s^-1 mM^-1. Quotient disclosure for this measurement: 13.0 / 3.0 = 4.333333333333333 s^-1 mM^-1, against the printed ratio cell 4.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, line no. 3, Enzyme column 'A44V/G45T/V46P' (Mutant no. 2), Lysine sub-columns: Km = 3.0 mM; kcat = 13 s^-1; printed kcat/Km ratio cell = 4,300, in a column whose head carries no printed unit and whose basis is M^-1 s^-1 on this line's own printed Km (mM) and kcat (s^-1) columns.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O50657 and applied mutation signature A44V/G45T/V46P/P54D/S322A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters for the decarboxylation of lysine and ornithine by wild-type and mutant LDCs and mouse ODC (J. Bacteriol. 2000, 182(23):6732-6741); printed column heads Line no. | Mutant no. | Enzyme | Km (mM) Lysine | Km (mM) Ornithine | kcat (s^-1) Lysine | kcat (s^-1) Ornithine | kcat/Km ratio Lysine | kcat/Km ratio Ornithine | Substrate specificity. Table 2, line no. 13, Enzyme column 'A44V/G45T/V46P/P54D/S322A' (Mutant no. 29), Lysine sub-columns; column Km (mM) Lysine = 270; column kcat (s^-1) Lysine = 5.5; column kcat/Km ratio Lysine = 21. captured primary segment: L-lysine | mutant 29 A44V/G45T/V46P/P54D/S322A | Table 2, line no. 13 | Km 270 mM | kcat 5.5 s^-1 | kcat/Km ratio 21 (printed kcat/Km ratio cell; the ratio column head carries no printed unit, and the cell is in M^-1 s^-1 on this row's own printed Km (mM) and kcat (s^-1) columns)

normalized_value_unit_evidence: Km: printed Table 2 Lysine Km cell 270 mM; the printed Km column is already in mM, so no unit conversion applies and the value is 270.0 mM. kcat: printed Table 2 Lysine kcat cell 5.5 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 5.5 s^(-1). kcat/Km: printed Table 2 Lysine ratio cell 21 in M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 21 / 1000 = 0.021 s^-1 mM^-1. Quotient disclosure for this measurement: 5.5 / 270.0 = 0.020370370370370372 s^-1 mM^-1, against the printed ratio cell 0.021 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, line no. 13, Enzyme column 'A44V/G45T/V46P/P54D/S322A' (Mutant no. 29), Lysine sub-columns: Km = 270 mM; kcat = 5.5 s^-1; printed kcat/Km ratio cell = 21, in a column whose head carries no printed unit and whose basis is M^-1 s^-1 on this line's own printed Km (mM) and kcat (s^-1) columns.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O50657 and applied mutation signature S322T/I326L to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters for the decarboxylation of lysine and ornithine by wild-type and mutant LDCs and mouse ODC (J. Bacteriol. 2000, 182(23):6732-6741); printed column heads Line no. | Mutant no. | Enzyme | Km (mM) Lysine | Km (mM) Ornithine | kcat (s^-1) Lysine | kcat (s^-1) Ornithine | kcat/Km ratio Lysine | kcat/Km ratio Ornithine | Substrate specificity. Table 2, line no. 10, Enzyme column 'S322T/I326L' (Mutant no. 23), Lysine sub-columns; column Km (mM) Lysine = 17; column kcat (s^-1) Lysine = 21; column kcat/Km ratio Lysine = 1,200. captured primary segment: L-lysine | mutant 23 S322T/I326L | Table 2, line no. 10 | Km 17 mM | kcat 21 s^-1 | kcat/Km ratio 1,200 (printed kcat/Km ratio cell; the ratio column head carries no printed unit, and the cell is in M^-1 s^-1 on this row's own printed Km (mM) and kcat (s^-1) columns)

normalized_value_unit_evidence: Km: printed Table 2 Lysine Km cell 17 mM; the printed Km column is already in mM, so no unit conversion applies and the value is 17.0 mM. kcat: printed Table 2 Lysine kcat cell 21 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 21.0 s^(-1). kcat/Km: printed Table 2 Lysine ratio cell 1,200 in M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1,200 / 1000 = 1.2 s^-1 mM^-1. Quotient disclosure for this measurement: 21.0 / 17.0 = 1.2352941176470589 s^-1 mM^-1, against the printed ratio cell 1.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, line no. 10, Enzyme column 'S322T/I326L' (Mutant no. 23), Lysine sub-columns: Km = 17 mM; kcat = 21 s^-1; printed kcat/Km ratio cell = 1,200, in a column whose head carries no printed unit and whose basis is M^-1 s^-1 on this line's own printed Km (mM) and kcat (s^-1) columns.


sequence_variant_note: Resolved canonical sequence from UniProt O50657 direct accession lookup; variant sequence reconstructed from selected BRENDA mutation_signature when present and applied mutation signature G319W to reconstruct the assayed variant sequence.


organism: Streptomyces coelicolor

sequence_source: UniProt Q9L072 direct accession lookup


organism: Thermotoga maritima

substrate_name: L-Lysine

sequence_source: UniProt Q9X2I6 direct accession lookup

substrate: L-Lysine


organism: Vibrio vulnificus

sequence_source: UniProt A0A3Q0KZG4 direct accession lookup plus RCSB 2PLJ sequence containment check


sequence_variant_note: Resolved canonical sequence from UniProtKB P00803 FASTA fetched 2026-06-17; row-specific variant reconstructed from PMID 15195997 mutation signature with +1 paper-to-UniProt coordinate offset. and applied mutation signature R77A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: m n n+m n m n+m n m n+m n m n+m n m n+m m n n+m m n n+m n m n+m n m n+m m n n+m m n n+m n m n+m m n n+m n m n+m n m n+m n m n+m n m n+m m n n+m Peptide; H2O

sequence_source: UniProtKB P00803 FASTA fetched 2026-06-17; row-specific variant reconstructed from PMID 15195997 mutation signature with +1 paper-to-UniProt coordinate offset.

proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R236A


sequence_variant_note: Mutation signature R318A matches the mutant residue at offset +1 and the reference residue at offset -2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


substrate_name: H2O; m n n+m n m n+m n m n+m n m n+m n m n+m m n n+m m n n+m n m n+m n m n+m m n n+m m n n+m n m n+m m n n+m n m n+m n m n+m n m n+m n m n+m m n n+m Peptide

sequence_variant_note: Mutation signature R282A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R282A


sequence_variant_note: Resolved canonical sequence from UniProtKB P00803 FASTA fetched 2026-06-17; row-specific variant reconstructed from PMID 15195997 mutation signature with +1 paper-to-UniProt coordinate offset. and applied mutation signature R199A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R199A

substrate: H2O; m n n+m n m n+m n m n+m n m n+m n m n+m m n n+m m n n+m n m n+m n m n+m m n n+m m n n+m n m n+m m n n+m n m n+m n m n+m n m n+m n m n+m m n n+m Peptide


sequence_variant_note: Resolved canonical sequence from UniProtKB P00803 FASTA fetched 2026-06-17; row-specific variant reconstructed from PMID 15195997 mutation signature with +1 paper-to-UniProt coordinate offset. and applied mutation signature R315K with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R315K


sequence_variant_note: Resolved canonical sequence from UniProtKB P00803 FASTA fetched 2026-06-17; row-specific variant reconstructed from PMID 15195997 mutation signature with +1 paper-to-UniProt coordinate offset. and applied mutation signature R275A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R275A


sequence_variant_note: Resolved canonical sequence from UniProtKB P00803 FASTA fetched 2026-06-17; row-specific variant reconstructed from PMID 15195997 mutation signature with +1 paper-to-UniProt coordinate offset. and applied mutation signature R146A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R146A


sequence_variant_note: Resolved canonical sequence from UniProtKB P00803 FASTA fetched 2026-06-17; row-specific variant reconstructed from PMID 15195997 mutation signature with +1 paper-to-UniProt coordinate offset. and applied mutation signature R198A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R318A


sequence_variant_note: Resolved canonical sequence from UniProtKB P00803 FASTA fetched 2026-06-17; row-specific variant reconstructed from PMID 15195997 mutation signature with +1 paper-to-UniProt coordinate offset. and applied mutation signature R318K with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature R222K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from UniProtKB P00803 FASTA fetched 2026-06-17; row-specific variant reconstructed from PMID 15195997 mutation signature with +1 paper-to-UniProt coordinate offset. and applied mutation signature R295A with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R222K


sequence_source: UniProtKB:A0A3Q0KZG4 direct REST check on 2026-06-17

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


substrate_name: L-lysine

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

substrate: L-lysine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q06408 plus selected mutation_signature reconstruction and applied mutation signature I335Y to reconstruct the assayed variant sequence.


substrate_name: 3-methyl-2-oxobutanoic acid

sequence_source: UniProtKB:Q06408 direct REST check on 2026-06-17

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

substrate: 3-methyl-2-oxobutanoic acid


substrate_name: 2-oxohexanoic acid

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q06408 plus selected mutation_signature reconstruction and applied mutation signature M624W to reconstruct the assayed variant sequence.


substrate_name: 2-oxo-4-phenylbutanoic acid

proof_lines: wild type enzyme, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C

substrate: 2-oxo-4-phenylbutanoic acid


substrate_name: 2-oxopentanoic acid


column_label: Table 1: ScPPDC substrate profile (FEBS Journal 2011, 278(11):1842-1853); printed column heads Substrate | Amino acid | Km (mM) | kcat (s^-1) | kcat/Km (mM^-1 s^-1) | % of the kcat/Km for PPA. Table 1, body row '4-Hydroxyphenylpyruvic acid' (amino acid Tyr); column 'Km (mM)' = 0.09; column 'kcat (s^-1)' = 11; column 'kcat/Km (mM^-1 s^-1)' = 125. captured primary segment: ScPPDC-His | 4-Hydroxyphenylpyruvic acid | Tyr | Km 0.09 ± 0.01 mM | kcat 11 ± 0.8 s^-1 | kcat/Km 125 mM^-1 s^-1 | 63 %

normalized_value_unit_evidence: Km: printed Table 1 cell 0.09 mM; the printed concentration column is already in mM, so no unit conversion applies and the value is 0.09 mM. kcat: printed Table 1 cell 11 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 11.0 s^(-1). kcat/Km: printed Table 1 cell 125 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the value is 125.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 11 / 0.09 = 122.22222222222223 s^-1 mM^-1, against the printed efficiency cell 125 s^-1 mM^-1, which the paper's own percentage column tracks at 63 %.

raw_value_unit_evidence: Table 1, body row '4-Hydroxyphenylpyruvic acid': Km = 0.09 mM; kcat = 11 s^-1; printed kcat/Km = 125 mM^-1 s^-1.


sequence_source: UniProtKB:Q06408 plus selected mutation_signature reconstruction


substrate_name: phenylpyruvate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q06408 plus selected mutation_signature reconstruction and applied mutation signature Q448W to reconstruct the assayed variant sequence.


substrate_name: 4-methyl-2-oxopentanoic acid

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

substrate: 4-methyl-2-oxopentanoic acid


substrate_name: Pyruvic acid


substrate_name: 2-oxobutanoic acid

proof_lines: mutant enzyme M624W, in 100 mM KPO4 buffer (pH 7.0), 1 mM MgSO4, 0.5 mM thiamine diphosphate, at pH 7.0 and 30°C


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

proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant S128A


proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant S130A


proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant K209A


proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant D215A


proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant E227A


organism: Aliivibrio salmonicida


organism: Aquifex aeolicus


organism: Bartonella henselae


proof_lines: noncompetitive inhibition, at pH 6.5, between 4°C and 10°C

proof_lines: uncompetitive inhibition, at pH 6.5, between 4°C and 10°C


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot_sequence_reconstruction and applied mutation signature F14C/K44C to reconstruct the assayed variant sequence.


proof_lines: pH 5.6, 45°C, recombinant His6-tagged wild-type enzyme


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot_sequence_reconstruction and applied mutation signature F14C/K44C/L7M/N8G to reconstruct the assayed variant sequence.


organism: Bacillus subtilis

substrate_name: preprotein substrate PONA

sequence_source: UniProt:P28628 canonical sequence from REST check on 2026-06-17

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

substrate: preprotein substrate PONA


sequence_source: UniProt:P28628 canonical sequence checked, but not attached as a resolved variant sequence

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


sequence_source: UniProt:P00803 canonical sequence checked, but not attached as a resolved variant sequence


sequence_variant_note: Resolved canonical sequence from UniProt:P00803 canonical sequence plus selected source mutation signature R222A and applied mutation signature R222A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R222A


substrate_name: Peptide

sequence_variant_note: Resolved canonical sequence from UniProt:P00803 canonical sequence plus selected source mutation signature R199A and applied mutation signature R199A to reconstruct the assayed variant sequence.


substrate_name: m n n+m n m n+m n m n+m n m n+m n m n+m m n n+m m n n+m n m n+m n m n+m m n n+m m n n+m n m n+m m n n+m n m n+m n m n...

sequence_variant_note: Resolved canonical sequence from UniProt:P00803 canonical sequence plus selected source mutation signature R77K and applied mutation signature R77K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R77K


sequence_variant_note: Resolved canonical sequence from UniProt:P00803 canonical sequence plus selected source mutation signature R226A and applied mutation signature R226A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: H2O; m n n+m n m n+m n m n+m n m n+m n m n+m m n n+m m n n+m n m n+m n m n+m m n n+m m n n+m n m n+m m n n+m n m n+m ...

sequence_variant_note: Resolved canonical sequence from UniProt:P00803 canonical sequence plus selected source mutation signature R318K and applied mutation signature R318K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R318K


sequence_variant_note: Resolved canonical sequence from UniProt:P00803 canonical sequence plus selected source mutation signature R127A and applied mutation signature R127A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProt:P00803 canonical sequence from REST check on 2026-06-17


sequence_variant_note: Resolved canonical sequence from UniProt:P00803 canonical sequence plus selected source mutation signature R198A and applied mutation signature R198A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R198A


sequence_variant_note: Resolved canonical sequence from UniProt:P00803 canonical sequence plus selected source mutation signature R275A and applied mutation signature R275A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProt:P00803 canonical sequence plus selected source mutation signature R127A

proof_lines: SABIO-RK modifier species: signal peptidase I(Enzyme) mutant SPase I  R127A


sequence_source: UniProt:P00803 canonical sequence plus selected source mutation signature R77K


sequence_variant_note: Resolved canonical sequence from UniProt:P00803 canonical sequence plus selected source mutation signature R146A and applied mutation signature R146A with inferred residue-numbering offset +1 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.


enzyme_display_name: Inducible lysine decarboxylase

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9H3 canonical sequence with direct residue-substitution reconstruction and applied mutation signature F14C/K44C/L7M/N8G to reconstruct the assayed variant sequence.

proof_lines: pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C/L7M/N8G

enzyme: Inducible lysine decarboxylase


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9H3 canonical sequence with direct residue-substitution reconstruction and applied mutation signature F14C/K44C to reconstruct the assayed variant sequence.

proof_lines: pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C


organism: Giardia lamblia

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


organism: Klebsiella aerogenes


sequence_source: UniProtKB:A0A0H3FP92 exact accession sequence


organism: Methanosarcina mazei


organism: Morus alba

proof_lines: recombinant His-tagged enzyme, pH 8.0, 37°C


organism: Nitrosomonas europaea


organism: Pseudomonas aeruginosa


enzyme_display_name: Lysine/ornithine decarboxylase

sequence_source: UniProtKB:O50657 exact accession sequence

enzyme: Lysine/ornithine decarboxylase


proof_lines:
pH 6.0, 40°C
pH 6.0, 40°C, reaction with L-Lys
pH 6.0, 40°C, reaction with L-Orn


substrate_name: L-Lys

sequence_variant_note: Resolved canonical sequence from UniProtKB:O50657 canonical sequence with direct residue-substitution reconstruction and applied mutation signature A44V/G45T/V46P/P54D to reconstruct the assayed variant sequence.

proof_lines: pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D


enzyme_display_name: branched-chain-2-oxoacid decarboxylase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

enzyme: branched-chain-2-oxoacid decarboxylase


substrate_name: pyruvate

substrate: pyruvate


organism: Lactococcus lactis subsp. lactis

sequence_source: UniProtKB Q684J7 FASTA/JSON direct lookup on 2026-06-17; entry Q684J7_LACLL, protein name Alpha-keto-acid decarboxylase, organism Lactococcus lactis subsp. lactis, gene kivd.


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB P9WG37 FASTA/JSON direct lookup on 2026-06-17; reviewed Swiss-Prot entry KDC_MYCTU, Alpha-keto-acid decarboxylase, organism Mycobacterium tuberculosis H37Rv, gene kdc/Rv0853c.

proof_lines: weak substrate inhibition is detected for pyruvate

substrate: phenylpyruvate


organism: Thermoplasma acidophilum

sequence_source: UniProtKB direct lookup on 2026-06-17 resolved Q9HIA4 as Thermoplasma dehydrogenase E1 beta chain and Q9HIA3 as E1 alpha chain; source value is a bundled two-accession complex signal, not one canonical sequence.


sequence_source: UniProtKB Q9HIA4 FASTA/JSON direct lookup on 2026-06-17 resolved the beta chain of the Thermoplasma dehydrogenase E1 component; PMID 15556640 describes activity for the alpha2-beta2 complex, so beta-chain sequence alone was not accepted as complete row sequence.


organism: Cricetulus griseus

substrate_name: CTP

substrate: CTP


organism: Rattus norvegicus


organism: Selenomonas ruminantium


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q04789 canonical sequence using selected mutation_signature Q487G and applied mutation signature Q487G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q04789 canonical sequence using selected mutation_signature Q487A and applied mutation signature Q487A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q04789 canonical sequence using selected mutation_signature Q487I and applied mutation signature Q487I to reconstruct the assayed variant sequence.


sequence_source: UniProt REST Q04789, fetched 2026-06-17


sequence_source: Reconstructed from UniProt Q04789 canonical sequence using selected mutation_signature Q487A


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q04789 canonical sequence using selected mutation_signature Q487L and applied mutation signature Q487L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q04789 canonical sequence using selected mutation_signature Q487S and applied mutation signature Q487S to reconstruct the assayed variant sequence.


organism: Lactococcus lactis

sequence_source: UniProt REST Q6QBS4, fetched 2026-06-17

proof_lines:
Hill coefficient 1.0, pH 7.0, 30°C
Hill coefficient 1.1, pH 7.0, 30°C
Hill coefficient 1.2, pH 7.0, 30°C


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q6QBS4 canonical sequence using selected mutation_signature V461I and applied mutation signature V461I to reconstruct the assayed variant sequence.

proof_lines:
mutant V461I, pH 6.5, 30°C
mutant V461I, pH 7.0, 37°C


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


proof_lines:
wild-type, pH 6.5, 30°C
wild-type, pH 7.0, 37°C


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q6QBS4 canonical sequence using selected mutation_signature V461I/A290M and applied mutation signature V461I/A290M to reconstruct the assayed variant sequence.


enzyme_display_name: nucleoside deoxyribosyltransferase

organism: Unknown

substrate_name: deoxycytidine

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

enzyme: nucleoside deoxyribosyltransferase

substrate: deoxycytidine


organism: Trypanosoma brucei brucei

sequence_source: UniProtKB Q57VC7 canonical sequence direct check on 2026-06-17.


substrate_name: adenine

sequence_variant_note: Resolved canonical sequence from UniProtKB Q57VC7 canonical sequence direct check plus row-specific mutation reconstruction (V11S). and applied mutation signature V11S to reconstruct the assayed variant sequence.

proof_lines: pH 6.0, 50°C, recombinant mutant V11S, transglycosylation, with 2-deoxyinosine

proof_lines: pH 6.0, 50°C, recombinant mutant V11S, transglycosylation, with adenine

proof_lines: pH 6.0, 50°C, recombinant mutant V11S, nucleobase release

substrate: adenine


sequence_variant_note: Resolved canonical sequence from UniProtKB Q57VC7 canonical sequence direct check plus row-specific mutation reconstruction (V11A). and applied mutation signature V11A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q57VC7 canonical sequence direct check plus row-specific mutation reconstruction (V11S).


sequence_source: UniProtKB Q57VC7 canonical sequence direct check plus row-specific mutation reconstruction (V11A).

proof_lines: pH 6.0, 50°C, recombinant mutant V11A, transglycosylation, with 2-deoxyinosine

proof_lines: pH 6.0, 50°C, recombinant mutant V11A, transglycosylation, with adenine

proof_lines: pH 6.0, 50°C, recombinant mutant V11A, nucleobase release


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from UniProtKB Q06408 canonical sequence direct check plus row-specific mutation reconstruction (I335Y/M624W). and applied mutation signature I335Y/M624W to reconstruct the assayed variant sequence.

substrate: 2-oxohexanoic acid


sequence_source: UniProtKB Q06408 canonical sequence direct check on 2026-06-17.

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


sequence_variant_note: Resolved canonical sequence from UniProtKB Q06408 canonical sequence direct check plus row-specific mutation reconstruction (M624W). and applied mutation signature M624W to reconstruct the assayed variant sequence.

substrate: Pyruvic acid


organism: Streptomyces virginiae

proof_lines: allosteric enzyme, Hill coefficient 4.7, pH 7.5, temperature not specified in the publication


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from UniProtKB Q04789 canonical sequence direct check plus row-specific mutation reconstruction (Q487I). and applied mutation signature Q487I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q04789 canonical sequence direct check plus row-specific mutation reconstruction (Q487S). and applied mutation signature Q487S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q04789 canonical sequence direct check plus row-specific mutation reconstruction (Q487G). and applied mutation signature Q487G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q04789 canonical sequence direct check plus row-specific mutation reconstruction (Q487L). and applied mutation signature Q487L to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q04789 canonical sequence direct check on 2026-06-17.

column_label: Table 2: Kinetic parameters of the wild-type AlsS (B. subtilis) and the variants for acetolactate synthase and decarboxylase activity (Applied and Environmental Microbiology 2009, 75(19):6306-6311), amino-acid-at-residue-487 row Q, KIV column group; column 'Km (mM)' = 300; column 'kcat (s^-1)' = 8.9; column 'kcat/Km ratio' = 0.03.

normalized_value_unit_evidence: Km: printed Table 2 cell 300 mM; the printed unit is already mM, so no unit conversion applies, and the value carried here is 300.0 mM. kcat: printed Table 2 cell 8.9 s^-1; no unit conversion applies, and the value carried here is 0.03 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, amino-acid-at-residue-487 row Q, KIV column group: Km = 300 mM; kcat = 8.9 s^-1

row_label: Table 2, amino-acid-at-residue-487 row Q (wild-type AlsS (B. subtilis)), KIV column group


organism: Lactobacillus helveticus

substrate_name: 2'-Deoxycytidine; Adenine

sequence_source: UniProtKB Q8RLY5 direct REST check on 2026-06-17

substrate: 2'-Deoxycytidine; Adenine


organism: Lactobacillus leichmannii


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


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q9R5V5 canonical sequence after direct REST check on 2026-06-17 and applied mutation signature F13R/D92S to reconstruct the assayed variant sequence.


sequence_source: Reconstructed from UniProtKB Q9R5V5 canonical sequence after direct REST check on 2026-06-17


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q9R5V5 canonical sequence after direct REST check on 2026-06-17 and applied mutation signature F13R/D92S/N123S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9R5V5 direct REST check on 2026-06-17


organism: Limosilactobacillus fermentum

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q6YNI5 canonical sequence after direct REST check on 2026-06-17 and applied mutation signature A15T to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q6YNI5 direct REST check on 2026-06-17


organism: Limosilactobacillus reuteri

sequence_source: UniProtKB A5VK58 direct REST check on 2026-06-17


substrate_name: cytosine

substrate: cytosine


sequence_source: UniProtKB Q57VC7 direct REST check on 2026-06-17


proof_lines: pH 6.0, 50°C, recombinant wild-type enzyme, transglycosylation, with adenine

proof_lines: pH 6.0, 50°C, recombinant wild-type enzyme, nucleobase release

proof_lines: pH 6.0, 50°C, recombinant wild-type enzyme, transglycosylation, with 2-deoxyinosine


enzyme_display_name: RNA-directed RNA polymerase

organism: Dengue virus type 2 (strain Thailand/NGS-C/1944)

substrate_name: triphosphorylated RNA

proof_lines: Vmax with 0.65 nmol/s/ug enzyme for RTPase activity with triphosphorylated RNA as substrate.

enzyme: RNA-directed RNA polymerase

substrate: triphosphorylated RNA


organism: Poliovirus type 1 (strain Mahoney)

substrate_name: ATP

substrate: ATP


organism: Severe acute respiratory syndrome coronavirus

substrate_name: peptide TSAVLQSGFRK-NH(2)

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

substrate: peptide TSAVLQSGFRK-NH(2)


organism: Crotalus viridis viridis

substrate_name: Unknown

substrate: Unknown


organism: Gloydius intermedius

sequence: NLLQFNKMIKVETGKNAIPFYAF

wild_type_sequence: NLLQFNKMIKVETGKNAIPFYAF


organism: Homo sapiens

proof_lines: The specific activity is 0.8 nmol/min/ug enzyme with 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine as substrate. The specific activity is 0.3 nmol/min/ug enzyme with 1-hexadecanoyl-2-(9Z,12Z-octadecadien

proof_lines: The specific activity is 2.1 nmol/min/ug enzyme with 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine as substrate. The specific activity is 0.6 nmol/min/ug enzyme with 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetr


organism: Mus musculus

proof_lines: The specific activity is 394 nmol/min/ug enzyme with 1-hexadecanoyl-sn-glycero-3-phosphocholine. The specific PLA2 activity is 11 nmol/min/ug enzyme with 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine (in the


organism: Protobothrops mangshanensis

sequence: NLLQFNKMIKIMTKKNAIPFYSS

wild_type_sequence: NLLQFNKMIKIMTKKNAIPFYSS


organism: Sistrurus miliarius barbouri

sequence: NLLQFNKMIKIMTKKNAFPFYTS

wild_type_sequence: NLLQFNKMIKIMTKKNAFPFYTS


organism: Sistrurus tergeminus


organism: Vipera renardi

proof_lines: Vmax=1736 umol/min/mg enzyme (Vur-PL2A).


enzyme_display_name: methylumbelliferyl-acetate deacetylase

substrate_name: p-nitrophenyl acetate

proof_lines: kcat is 59 min(-1), 29 min(-1), 90 min(-1) with 2-arachidonoylglycerol, prostaglandin F2alpha 1-glyceryl ester and prostaglandin E2 1-glyceryl ester as substrates, respectively.

enzyme: methylumbelliferyl-acetate deacetylase

substrate: p-nitrophenyl acetate


substrate_name: 4-yethylumbelliferyl acetate

proof_lines: pH 5.2, 37°C, isoenzymes Es D1 and Es D2

substrate: 4-yethylumbelliferyl acetate


organism: Venezuelan equine encephalitis virus (strain 3880)

substrate_name: a 12 residues substrate for nsp2 protease activity


organism: Venezuelan equine encephalitis virus (strain Trinidad donkey)

substrate: a 12 residues substrate for nsp2 protease activity


organism: Vesicular stomatitis Indiana virus (strain San Juan)


organism: Classical swine fever virus (strain Alfort/Tuebingen)

substrate_name: Sub-UpU

substrate: Sub-UpU


organism: Crimean-Congo hemorrhagic fever virus (strain Nigeria/IbAr10200/1970)

substrate_name: Ub-AMC

substrate: Ub-AMC


organism: Deformed wing virus

substrate_name: a 15 AA peptide

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

substrate: a 15 AA peptide


organism: Dengue virus type 2 (strain Puerto Rico/PR159-S1/1969)

substrate_name: N-acetyl-Gly-Arg-Arg-AMC

substrate: N-acetyl-Gly-Arg-Arg-AMC


organism: Dugbe virus (isolate ArD44313)


organism: Hepatitis E virus genotype 1 (isolate Human/China/HeBei/1987)

substrate_name: GTP

substrate: GTP


organism: Hepatitis GB virus B

substrate_name: ATP for NS3 NTPase

substrate: ATP for NS3 NTPase


organism: Kokobera virus

substrate_name: ATPase of serine protease NS3

substrate: ATPase of serine protease NS3


organism: Semliki forest virus

substrate_name: nsP2 RNA triphosphatase activity (at pH 8.0)


organism: Tick-borne encephalitis virus European subtype (strain Neudoerfl)


organism: Tobacco vein mottling virus


organism: Turnip yellow mosaic virus


organism: Severe acute respiratory syndrome coronavirus 2

substrate_name: remdesivir triphosphate

sequence_source: UniProtKB direct accession lookup: P0DTD1 (retrieved 2026-06-17)

substrate: remdesivir triphosphate


substrate_name: UTP; ATP; remdesivir triphosphate; dATP; ara-ATP; 2-C-methyl-ATP; CTP

source_db: brenda; skid

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

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines:
pH 7.0, 37°C
pH 8, 30°C
Raw SKiD Env: Temp=37°C, pH=7

source: brenda; skid


organism: Zaire ebolavirus

substrate_name: ATP; remdesivir triphosphate

sequence_source: UniProtKB direct accession lookup: A0A068J9B1 (retrieved 2026-06-17)

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

substrate: ATP; remdesivir triphosphate


organism: Homo sapiens

substrate_name: 4-Methylumbelliferyl acetate; H2O

sequence_source: UniProtKB direct accession lookup: O00748 (retrieved 2026-06-17)

substrate: 4-Methylumbelliferyl acetate; H2O


sequence_source: UniProtKB direct accession lookup: P23141 (retrieved 2026-06-17)


substrate_name: cocaine

proof_lines: kcat is 43 min(-1), 49 min(-1), 150 min(-1) with 2-arachidonoylglycerol, prostaglandin F2alpha 1-glyceryl ester and prostaglandin E2 1-glyceryl ester as substrates, respectively.

substrate: cocaine


enzyme_display_name: ornithine decarboxylase

substrate_name: L-ornithine

proof_lines: kcat is 3.3 sec(-1) with L-ornithine as substrate.

enzyme: ornithine decarboxylase

substrate: L-ornithine


organism: Leishmania donovani

proof_lines: kcat is 8.1 sec(-1) with L-ornithine as substrate.


organism: Nicotiana glutinosa

substrate_name: L-ornithine (at pH 8.0)

proof_lines: kcat is 77.78 sec(-1) with L-ornithine as substrate (at pH 8.0) (PubMed:11736657). kcat is 0.236 sec(-1) with L-lysine as substrate (at pH 6.8) (PubMed:11736657).

substrate: L-ornithine (at pH 8.0)


organism: Trypanosoma brucei brucei

proof_lines: kcat is 15 sec(-1) with L-ornithine as substrate.


organism: Sulfolobus acidocaldarius

substrate_name: isocitrate

sequence_source: UniProtKB REST Q4J6C9 canonical sequence, retrieved 2026-06-17

substrate: isocitrate


substrate_name: homoisocitrate

substrate: homoisocitrate


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


organism: Thermococcus kodakarensis

sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q5JFV8 canonical sequence plus reviewer-reconstructed substitution, retrieved 2026-06-17 and applied mutation signature S80A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST Q5JFV8 canonical sequence, retrieved 2026-06-17

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


sequence_source: UniProtKB REST Q5JFV8 canonical sequence plus reviewer-reconstructed substitution, retrieved 2026-06-17


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q5JFV8 canonical sequence plus reviewer-reconstructed substitution, retrieved 2026-06-17 and applied mutation signature I82N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 333.15 K; cofactor NAD+

proof_lines: pH 8.0, 60°C, recombinant His6-tagged mutant I82N, with isocitrate

proof_lines: pH 8.0, 60°C, recombinant His6-tagged mutant I82N, with homoisocitrate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q5JFV8 canonical sequence plus reviewer-reconstructed substitution, retrieved 2026-06-17 and applied mutation signature L81P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q5JFV8 canonical sequence plus reviewer-reconstructed substitution, retrieved 2026-06-17 and applied mutation signature T71V to reconstruct the assayed variant sequence.


proof_lines: pH 8.0, 60°C, recombinant His6-tagged mutant L81P, with isocitrate

proof_lines: pH 8.0, 60°C, recombinant His6-tagged mutant L81P, with 3-isopropylmalate


proof_lines: pH 8.0, 60°C, recombinant His6-tagged wild-type enzyme, with isocitrate

proof_lines: pH 8.0, 60°C, recombinant His6-tagged wild-type enzyme, with 3-isopropylmalate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q5JFV8 canonical sequence plus reviewer-reconstructed substitution, retrieved 2026-06-17 and applied mutation signature L83R 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: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

substrate_name: isocitrate (at 70 degrees Celsius and pH 7.8)

proof_lines: kcat is 14.8 sec(-1) with isocitrate as substrate and 13.7 sec(-1) with homoisocitrate as substrate.


organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

proof_lines: kcat is 33 sec(-1) with (1R,2S)-homoisocitrate as substrate. kcat is 76 sec(-1) with D-threo-isocitrate as substrate.


organism: Pseudomonas aeruginosa

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


proof_lines:
mutant Y385F, at pH 8.0 and 30°C
mutant enzyme Y385F


organism: Pseudomonas fluorescens

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines:
pH 8, monomeric form
pH 8, dimeric form
reaction with 2,4-dihydroxybenzoate


substrate_name: NADPH

substrate: NADPH


proof_lines: mutant enzyme H162R, H162Y, H162K, R269K, R269Y, R269N, R269S and R269T


proof_lines: mutant enzyme H162N, H162S, H162T and H162D


organism: Hepacivirus hominis

substrate_name: Unknown

sequence_source: UniProtKB:B6EAV7 REST lookup

proof_lines:
clinical isolate GT-1b
clinical isolate GT-1a

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from UniProtKB:B6EAV7 REST lookup with S282T reconstruction and applied mutation signature S282T to reconstruct the assayed variant sequence.


organism: Human respiratory syncytial virus A

sequence_source: UniProtKB:P28887 REST lookup

proof_lines:
pH 8, 30°C
Raw SKiD Env: Temp=30°C, pH=8


organism: Lassa virus

substrate_name: ATP; RNA

sequence_source: UniProtKB:A0A097F4L1 REST lookup

substrate: ATP; RNA


organism: Rabbit hemorrhagic disease virus

substrate_name: rGTP

sequence_source: UniProtKB:P27411 REST lookup

proof_lines: Michaelis-Menten kinetic model, pH 7.5, 30°C, recombinant enzyme

proof_lines: substrate inhibition, pH 7.5, 30°C, recombinant enzyme

substrate: rGTP


organism: Respiratory syncytial virus type A

substrate_name: RNAn

sequence_source: UniProtKB:X5F520 REST lookup

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: 30°C, pH 7.5, RNA template with the first 25 nucleotides from the TrC (Trailer complement) sequence

proof_lines: 30°C, pH 7.5, cosubstrate: RNA template with the first 25 nucleotides from the TrC (Trailer complement) sequence

substrate: RNAn


organism: SARS coronavirus

sequence_source: UniProtKB:P0C6X7 REST lookup

assay_conditions_summary: cofactor ATP


substrate_name: RNA; ATP

sequence_source: UniProtKB:P0DTD1 REST lookup

substrate: RNA; ATP


substrate_name: UTP

substrate: UTP


substrate_name: ATP

assay_conditions_summary: pH 7; 310.15 K; buffer Reaction; cofactor ATP

column_label: Table 1 (Kinetic Parameters for Nucleotide Incorporation) carries four columns: Nucleotide | kcat/Km (uM^-1 s^-1) | kcat (s^-1) | Km (uM). The cited cell set is the Nucleotide row ATP: kcat/Km (uM^-1 s^-1) = 0.74; kcat (s^-1) = 240; Km (uM) = 320.

normalized_value_unit_evidence: kcat: printed Table 1 cell 240 s^-1 on the ATP line; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 240.0 s^(-1). Km: printed Table 1 cell 320 uM on the ATP line; 1 uM is 0.001 mM, so 320 / 1000 = 0.32 mM. kcat/Km: printed Table 1 cell 0.74 uM^-1 s^-1 on the ATP line; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.74 x 1000 = 740.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, Nucleotide row ATP: kcat = 240 s^-1; Km = 320 uM; printed kcat/Km = 0.74 uM^-1 s^-1.

row_label: Table 1, Nucleotide row ATP

table_label: Table 1: Kinetic Parameters for Nucleotide Incorporation (iScience 23, 101849, December 18, 2020)

substrate: ATP


substrate_name: remdesivir triphosphate

assay_conditions_summary: pH 7; 310.15 K; buffer Reaction

column_label: Table 1 (Kinetic Parameters for Nucleotide Incorporation) carries four columns: Nucleotide | kcat/Km (uM^-1 s^-1) | kcat (s^-1) | Km (uM). The cited cell set is the Nucleotide row RTP-1: kcat/Km (uM^-1 s^-1) = 1.29; kcat (s^-1) = 68; Km (uM) = 53.

normalized_value_unit_evidence: kcat: printed Table 1 cell 68 s^-1 on the RTP-1 line; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 68.0 s^(-1). Km: printed Table 1 cell 53 uM on the RTP-1 line; 1 uM is 0.001 mM, so 53 / 1000 = 0.053 mM. kcat/Km: printed Table 1 cell 1.29 uM^-1 s^-1 on the RTP-1 line; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 1.29 x 1000 = 1290.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, Nucleotide row RTP-1: kcat = 68 s^-1; Km = 53 uM; printed kcat/Km = 1.29 uM^-1 s^-1.

row_label: Table 1, Nucleotide row RTP-1


organism: Severe acute respiratory syndrome coronavirus 2


enzyme_display_name: glutamate carboxypeptidase II

organism: Homo sapiens

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

sequence_source: UniProtKB:Q04609 REST lookup

proof_lines:
pH 7.4, 37°C
at pH 8.0 and 37°C
37°C, pH 7.4

enzyme: glutamate carboxypeptidase II

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


substrate_name: pteroyl-di-L-glutamate

substrate: pteroyl-di-L-glutamate


sequence_variant_note: Resolved canonical sequence from UniProt Q04609 canonical FASTA direct lookup plus reconstructed substitution Y552I and applied mutation signature Y552I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q04609 canonical FASTA direct lookup plus reconstructed substitution R210A and applied mutation signature R210A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q04609 canonical FASTA direct lookup plus reconstructed substitution R210K and applied mutation signature R210K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q04609 canonical FASTA direct lookup plus reconstructed substitution E424H and applied mutation signature E424H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q04609 canonical FASTA direct lookup plus reconstructed substitution E424S and applied mutation signature E424S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q04609 canonical FASTA direct lookup plus reconstructed substitution Y700F and applied mutation signature Y700F to reconstruct the assayed variant sequence.


sequence_source: UniProt Q04609 canonical FASTA direct lookup


sequence_variant_note: Resolved canonical sequence from UniProt Q04609 canonical FASTA direct lookup plus reconstructed substitution F209W and applied mutation signature F209W to reconstruct the assayed variant sequence.


organism: Mus musculus

sequence_source: UniProt O35409 canonical FASTA direct lookup


assay_conditions_summary: cofactor NADPH


organism: Pseudomonas sp.

substrate_name: NADH

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

assay_conditions_summary: 318.15 K; cofactor NADPH

substrate: NADH


organism: Rhodococcus opacus

proof_lines:
strain 557
strain 420
strain IG


organism: Rhodococcus rhodnii


organism: Rhodococcus rhodochrous


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

assay_conditions_summary: cofactor NADH


organism: Bacillus cereus

substrate_name: dihydrodipicolinate

substrate: dihydrodipicolinate


organism: Corynebacterium glutamicum

proof_lines: pH and temperature not specified in the publication


proof_lines: mutant enzyme K11A, with NADH as cosubstrate, pH and temperature not specified in the publication

proof_lines: mutant enzyme K11A, with NADPH as cosubstrate, pH and temperature not specified in the publication


proof_lines: mutant enzyme R13A, with NADPH as cosubstrate, pH and temperature not specified in the publication

proof_lines: mutant enzyme R13A, with NADH as cosubstrate, pH and temperature not specified in the publication


proof_lines: wild type enzyme, with NADH as cosubstrate, pH and temperature not specified in the publication

proof_lines: wild type enzyme, with NADPH as cosubstrate, pH and temperature not specified in the publication


organism: Thermococcus kodakarensis

sequence_variant_note: Resolved canonical sequence from UniProt Q5JFV8 direct lookup; reconstructed S80A after residue-coordinate check and applied mutation signature S80A to reconstruct the assayed variant sequence.


sequence_source: UniProt Q5JFV8 direct lookup; reconstructed S80A after residue-coordinate check

proof_lines: pH 8.0, 60°C, recombinant His6-tagged mutant S80A, with 3-isopropylmalate

proof_lines: pH 8.0, 60°C, recombinant His6-tagged mutant S80A, with isocitrate


sequence_variant_note: Resolved canonical sequence from UniProt Q5JFV8 direct lookup; reconstructed T71V after residue-coordinate check and applied mutation signature T71V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q5JFV8 direct lookup; reconstructed L83R after residue-coordinate check and applied mutation signature L83R to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 60°C, recombinant His6-tagged mutant L83R, with homoisocitrate

proof_lines: pH 8.0, 60°C, recombinant His6-tagged mutant L83R, with isocitrate


sequence_variant_note: Resolved canonical sequence from UniProt Q5JFV8 direct lookup; reconstructed I82N after residue-coordinate check and applied mutation signature I82N to reconstruct the assayed variant sequence.


sequence_source: UniProt Q5JFV8 direct lookup


sequence_source: UniProt Q5JFV8 direct lookup; reconstructed L83R after residue-coordinate check


sequence_source: UniProt Q5JFV8 direct lookup; reconstructed T71V after residue-coordinate check

proof_lines: pH 8.0, 60°C, recombinant His6-tagged mutant T71V, with 3-isopropylmalate

proof_lines: pH 8.0, 60°C, recombinant His6-tagged mutant T71V, with isocitrate


sequence_variant_note: Resolved canonical sequence from UniProt Q5JFV8 direct lookup; reconstructed L81P after residue-coordinate check and applied mutation signature L81P to reconstruct the assayed variant sequence.


organism: Thermus thermophilus

sequence_source: UniProt Q72IW9 direct lookup and required identity cache


proof_lines:
pH 8.0, 60°C, recombinant enzyme
60°C, pH 8.0
Raw SKiD Env: Temp=60°C, pH=8


organism: Dengue virus

substrate_name: GTP

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

substrate: GTP


organism: Ebola virus


organism: Hepacivirus C

substrate_name: CTP

substrate: CTP


organism: Acinetobacter calcoaceticus


assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH


organism: Klebsiella pneumoniae