sequence_variant_note: Resolved canonical sequence from UniProtKB:P22567 REST exact accession lookup plus selected BRENDA mutation note E269A and applied mutation signature E269A to reconstruct the assayed variant sequence.


enzyme_display_name: amino-acid N-acetyltransferase

organism: Pseudomonas aeruginosa

substrate_name: acetyl-CoA

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB:P22567 REST exact accession lookup plus selected BRENDA mutation note L353V and applied mutation signature L353V to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: cofactor CoA

enzyme: amino-acid N-acetyltransferase

substrate: acetyl-CoA

source: brenda


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22567 REST exact accession lookup plus selected BRENDA mutation note G368A and applied mutation signature G368A to reconstruct the assayed variant sequence.


organism: Homo sapiens

mutation_signature: Unknown

sequence_source: UniProtKB REST Q8N159 checked 2026-06-17; reviewed human NAGS entry with EC 2.3.1.1 and catalytic-activity evidence citing PMID 7126172

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


organism: Chlorella vulgaris

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


organism: Danio rerio

proof_lines: apparent value, recombinant mature enzyme, pH and temperature not specified in the publication

proof_lines: apparent value, recombinant catalytic domain, pH and temperature not specified in the publication


assay_conditions_summary: pH 8.5; 303.15 K; cofactor CoA

proof_lines: pH and temperature not specified in the publication


organism: Mycobacterium tuberculosis

substrate_name: L-glutamine

substrate: L-glutamine


organism: Neurospora crassa

substrate_name: glutamate

substrate: glutamate


proof_lines: wild-type enzyme, in presence of 2 mM arginine


substrate_name: L-glutamate

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

proof_lines: mutant ins284A, in presence of 2 mM arginine

substrate: L-glutamate


organism: Rattus norvegicus

substrate_name: Acetyl-CoA; L-Glutamate

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

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

substrate: Acetyl-CoA; L-Glutamate


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Xanthomonas campestris

assay_conditions_summary: pH 9; 303.15 K; cofactor CoA


enzyme_display_name: acetylglutamate kinase

organism: Escherichia coli

substrate_name: ATP

assay_conditions_summary: pH 5.5; 310.15 K; cofactor ATP

enzyme: acetylglutamate kinase

substrate: ATP


organism: Lathyrus oleraceus

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: two Km-values: 1.9 and 6.2, pH 7.5, 30°C


organism: Pisum sativum

substrate_name: N-Acetyl-L-glutamate; ATP

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

assay_conditions_summary: cofactor ATP

substrate: N-Acetyl-L-glutamate; ATP


assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP


organism: Synechococcus elongatus

substrate_name: N-acetyl-L-glutamate

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: in the absence of protein PII, in 50 mM imidazole, pH 7.5

proof_lines: in the presence of protein PII, in 50 mM imidazole, pH 7.5

proof_lines: pH 7.5, complex of enzyme and PII protein

substrate: N-acetyl-L-glutamate


enzyme_display_name: isopentenyl phosphate kinase

organism: Thermoplasma acidophilum

substrate_name: (2E)-hex-2-en-1-yl phosphate

enzyme: isopentenyl phosphate kinase

substrate: (2E)-hex-2-en-1-yl phosphate


enzyme_display_name: choline-phosphate cytidylyltransferase

organism: Drosophila melanogaster

substrate_name: choline phosphate

proof_lines: purified His-tagged enzyme, pH 7.0, 37°C

enzyme: choline-phosphate cytidylyltransferase

substrate: choline phosphate


substrate_name: CTP

assay_conditions_summary: pH 7

substrate: CTP


organism: Plasmodium falciparum

substrate_name: phosphocholine

proof_lines:
presence of lipid, pH 7.4, 37°C
absence of lipid, pH 7.4, 37°C

substrate: phosphocholine


proof_lines:
CCTalpha236 mutant, presence of lipid
CCTalpha236 mutant, absence of lipid
pH 7.0, 37°C, enzyme mutant CCTalpha236


proof_lines:
wild-type, absence of lipid
wild-type, presence of lipid
wild-type, purified enzyme, 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22567 and applied mutation signature Y14A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22567 and applied mutation signature K199A to reconstruct the assayed variant sequence.


organism: Thermotoga neapolitana

substrate_name: L-Glutamate; Acetyl-CoA

substrate: L-Glutamate; Acetyl-CoA


organism: Fagopyrum esculentum

substrate_name: phloretin

sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0A1HA03 and applied mutation signature Q383H to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, UDP-glucose as sugar donor, mutant enzyme Q383H

proof_lines: pH 8.0, 30°C, phloretin as acceptor, mutant enzyme Q383H

substrate: phloretin


substrate_name: UDP-alpha-D-glucose

sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0A1HA03 and applied mutation signature D382E to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, phloretin as acceptor, mutant enzyme D382E

proof_lines: pH 8.0, 30°C, UDP-glucose as sugar donor, mutant enzyme D382E

substrate: UDP-alpha-D-glucose


proof_lines: pH 8.0, 30°C, phloretin as acceptor, wild-type enzyme

proof_lines: pH 8.0, 30°C, 2,4,6-trihydroxyacetophenone as acceptor, wild-type enzyme

proof_lines: pH 8.0, 30°C, UDP-glucose as sugar donor, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0A1HA03 and applied mutation signature T150A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, phloretin as acceptor, mutant enzyme T150A

proof_lines: pH 8.0, 30°C, UDP-glucose as sugar donor, mutant enzyme T150A


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0A1HA03 and applied mutation signature Q383A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, UDP-glucose as sugar donor, mutant enzyme Q383A

proof_lines: pH 8.0, 30°C, phloretin as acceptor, mutant enzyme Q383A


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0A1HA03 and applied mutation signature Y102F to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, UDP-glucose as sugar donor, mutant enzyme Y102F

proof_lines: pH 8.0, 30°C, phloretin as acceptor, mutant enzyme Y102F


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0A1HA03 and applied mutation signature F130A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, UDP-glucose as sugar donor, mutant enzyme F130A

proof_lines: pH 8.0, 30°C, phloretin as acceptor, mutant enzyme F130A


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0A1HA03 and applied mutation signature T151A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, phloretin as acceptor, mutant enzyme T151A

proof_lines: pH 8.0, 30°C, UDP-glucose as sugar donor, mutant enzyme T151A


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0A1HA03 and applied mutation signature F198A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, UDP-glucose as sugar donor, mutant enzyme F198A

proof_lines: pH 8.0, 30°C, phloretin as acceptor, mutant enzyme F198A


organism: Fortunella crassifolia

substrate_name: 2-Hydroxynaringenin; UDPglucose

substrate: 2-Hydroxynaringenin; UDPglucose


organism: Oryza sativa Indica Group

proof_lines: pH and temperature not specified in the publication


ki_unit: mM


organism: Homo sapiens

substrate_name: quinolinic acid

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q15274 and applied mutation signature R161A to reconstruct the assayed variant sequence.

proof_lines: +/-0.060 mM, mutant R161A, 0.1 mM 5-phospho-alpha-D-ribose 1-diphosphate, UV-based assay measuring nicotinic acid mononucleotide formation at 266 nm, 30 min, 37°C

substrate: quinolinic acid


enzyme_display_name: RNA-directed RNA polymerase

organism: black beetle virus

substrate_name: UTP

enzyme: RNA-directed RNA polymerase

substrate: UTP


organism: Foot-and-mouth disease virus

substrate_name: Unknown

km_display: Not reported

substrate: Unknown


organism: Hepacivirus hominis

mutation_type: deletion

proof_lines: pH 7.5, 23°C, deletion mutant DELTAC21, poly(A)-oligo(U)18 as template

proof_lines: pH 7.5, 23°C, deletion mutant DELTAC21, poly(C)-oligo(G)18 as template


substrate_name: GTP

assay_conditions_summary: pH 7.5; 296.15 K; cofactor ATP

proof_lines: pH 7.5, 23°C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)

proof_lines: pH 7.5, 23°C, C-terminally truncated enzyme form NS5B(DELTA21), reaction with dT16/poly(rA)

proof_lines: pH 8.2, 25°C, enzyme form DELTA21 that lacks the C-terminal 21 hydrophobic residues

substrate: GTP


assay_conditions_summary: pH 7.5; buffer MgCl2 and dithiothreitol in HEPES

proof_lines: mutant enzyme S282T, with 5 mM MgCl2, and 2 mM dithiothreitol in 50 mM HEPES buffer, pH 7.5


proof_lines: wild type enzyme, with 5 mM MgCl2, and 2 mM dithiothreitol in 50 mM HEPES buffer, pH 7.5


proof_lines: pH 7.5, 23°C, full-length enzyme, poly(C)-oligo(G)18 as template


organism: influenza A virus

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines: pH 8.0, 25°C, Influenza ApG-primed transcription

proof_lines: pH 8.0, 25°C, HCV JFH1a de novo transcription


organism: Qubevirus durum


organism: rhinovirus A16

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines:
pH 7.0, 30°C, sshRNA as template
pH 7.0, 30°C, poly(A) as template
pH 7.0, 30°C, poly(C) as template


organism: Rattus norvegicus

sequence_variant_note: Resolved canonical sequence from UniProt P19836 with PMID 12718547 paper anchor; K122R reconstructed by replacing residue 122 K with R and applied mutation signature K122R to reconstruct the assayed variant sequence.


substrate_name: Choline phosphate; CTP

proof_lines: with choline phosphate, 45000 MW protein

substrate: Choline phosphate; CTP


sequence_source: UniProt P19836 with PMID 7592590 truncation context; residues 257-367 removed

sequence_variant_note: Mutation signature Δ257 references residue 257, which is outside the resolved sequence length.


sequence_source: UniProt P19836 with PMID 7592590 truncation context; residues 231-367 removed

sequence_variant_note: Mutation signature Δ231 references residue 231, which is outside the resolved sequence length.


sequence_source: UniProt P19836 with PMID 7592590 truncation context; residues 312-367 removed

sequence_variant_note: Mutation signature Δ312 references residue 312, which is outside the resolved sequence length.

proof_lines: delta312-367 mutant, presence of lipid, pH 6.5, 37°C

proof_lines: DELTA312-367 mutant, absence of lipid, pH 6.5, 37°C


proof_lines:
H92N mutant, purified enzyme, 37°C
H92N mutant, cytosolic enzyme, 37°C


proof_lines: H92Q mutant, cytosolic and purified enzyme, 37°C


organism: Ricinus communis

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


organism: Saccharomyces cerevisiae

proof_lines:
presence of lipid
absence of lipid


organism: Secale cereale

substrate_name: CTP; Choline phosphate

substrate: CTP; Choline phosphate


organism: Streptococcus pneumoniae

sequence_source: UniProt Q8DPI6, reviewed LicC entry with PMID 11466299 evidence

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


enzyme_display_name: ornithine aminotransferase

substrate_name: 2-Oxoglutarate; L-Ornithine

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

sequence_source: UniProtKB:P04181 direct REST lookup 2026-06-17

proof_lines: pH and temperature not specified in the publication, eye retina enzyme

proof_lines: pH and temperature not specified in the publication, eye iris enzyme

proof_lines: assay based on detection of L-glutamate, pH 8.0, 37°C

source_databases_merged: sabio_rk brenda skid

enzyme: ornithine aminotransferase

substrate: 2-Oxoglutarate; L-Ornithine


organism: Lathyrus oleraceus

substrate_name: L-ornithine

sequence_source: UniProtKB:B1A0U3 direct REST lookup 2026-06-17

proof_lines: pH and temperature not specified in the publication

substrate: L-ornithine


organism: Mus musculus

sequence_source: UniProtKB:P29758 direct REST lookup 2026-06-17

proof_lines: pH and temperature not specified in the publication, enzyme from cerebellar granule cells

proof_lines: pH and temperature not specified in the publication, enzyme from cortical interneurons

proof_lines: pH and temperature not specified in the publication, enzyme from astrocytes


organism: Plasmodium falciparum

sequence_source: UniProtKB:Q6LFH8 direct REST lookup 2026-06-17

proof_lines: wild-type (OAT in parasite cell extract), pH 7.4, 37°C


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

source_databases_merged: brenda skid


sequence_source: UniProtKB:P04182 direct REST lookup 2026-06-17

proof_lines: pH and temperature not specified in the publication, small intestine enzyme

proof_lines: pH and temperature not specified in the publication, liver isolated mitochondria

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


organism: Salmo trutta

sequence_source: UniProtKB:A0A674DA32 direct REST lookup 2026-06-17

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


organism: Toxoplasma gondii

source_db: oed

sequence_source: UniProtKB:S8EY38 direct REST lookup 2026-06-17

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

data_origin: experimental

source: oed


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


substrate_name: D-ornithine

substrate: D-ornithine


substrate_name: L-Ornithine

kcat_over_km_origin: calculated

substrate: L-Ornithine


sequence_variant_note: Resolved canonical sequence from UniProtKB:S8EY38 direct REST lookup 2026-06-17 plus row-specific V79Y reconstruction and applied mutation signature V79Y to reconstruct the assayed variant sequence.


substrate_name: acetylornithine

substrate: acetylornithine


sequence_source: UniProtKB:S8EY38 direct REST lookup 2026-06-17 plus row-specific V79Y reconstruction


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Unknown


organism: Homo sapiens

substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

sequence_source: UniProtKB reviewed accession Q15274 FASTA fetched from rest.uniprot.org on 2026-06-17

proof_lines: +/-0.0036 mM, wild-type, 0.3 mM quinolinic acid, UV-based assay measuring nicotinic acid mononucleotide formation at 266 nm, 30 min, 37°C, KM for 5-phospho-alpha-D-ribose 1-diphosphate increases with decreasing quinolinic acid concentration

proof_lines: +/-0.003 mM, wild-type, 0.1 mM 5-phospho-alpha-D-ribose 1-diphosphate, UV-based assay measuring nicotinic acid mononucleotide formation at 266 nm, 30 min, 37°C, affinity to quinolinic acid is independent of 5-phospho-alpha-D-ribose 1-diphos

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB reviewed accession P9WJJ7 FASTA fetched from rest.uniprot.org on 2026-06-17

proof_lines:
at pH 7.2 and 37°C
Raw SKiD Env: Temp=37°C, pH=7.2


sequence_source: UniProtKB reviewed accession Q11201 FASTA fetched from rest.uniprot.org on 2026-06-17


substrate_name: CMP-N-acetyl-beta-neuraminate

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q11201 and applied mutation signature S148A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADH

column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row S148A, donor CMP-Neu5Ac column group; column KM (uM) = 481; column kcat (min^-1) = 219; column kcat/Km (mM^-1 min^-1) = 455.

raw_value_unit_evidence: Table 1, enzyme row S148A, donor CMP-Neu5Ac column group: KM = 481 uM; kcat = 219 min^-1; printed kcat/Km = 455 mM^-1 min^-1.

table_label: Table 1: Kinetic parameters of MBP-fused hST3Gal1 and variants (Scientific Reports 2019, volume 9, article 17993)

substrate: CMP-N-acetyl-beta-neuraminate

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q11201 and applied mutation signature Y230F to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row Y230F, donor CMP-Neu5Ac column group; column KM (uM) = 176; column kcat (min^-1) = 162; column kcat/Km (mM^-1 min^-1) = 920.

raw_value_unit_evidence: Table 1, enzyme row Y230F, donor CMP-Neu5Ac column group: KM = 176 uM; kcat = 162 min^-1; printed kcat/Km = 920 mM^-1 min^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q11201 and applied mutation signature V315A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row V315A, donor CMP-Neu5Ac column group; column KM (uM) = 180; column kcat (min^-1) = 63; column kcat/Km (mM^-1 min^-1) = 350.

raw_value_unit_evidence: Table 1, enzyme row V315A, donor CMP-Neu5Ac column group: KM = 180 uM; kcat = 63 min^-1; printed kcat/Km = 350 mM^-1 min^-1.


column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row S148A, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group; column KM (uM) = 105; column kcat (min^-1) = 139; column kcat/Km (mM^-1 min^-1) = 1324.

raw_value_unit_evidence: Table 1, enzyme row S148A, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group: KM = 105 uM; kcat = 139 min^-1; printed kcat/Km = 1324 mM^-1 min^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q11201 FASTA fetched from rest.uniprot.org on 2026-06-17; row-specific mutation reconstructed from selected mutation signature and applied mutation signature C59S/C64S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q11201 and applied mutation signature V315Y to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row V315Y, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group; column KM (uM) = 549; column kcat (min^-1) = 12; column kcat/Km (mM^-1 min^-1) = 22.

raw_value_unit_evidence: Table 1, enzyme row V315Y, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group: KM = 549 uM; kcat = 12 min^-1; printed kcat/Km = 22 mM^-1 min^-1.


column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row Y230F, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group; column KM (uM) = 352; column kcat (min^-1) = 208; column kcat/Km (mM^-1 min^-1) = 591.

raw_value_unit_evidence: Table 1, enzyme row Y230F, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group: KM = 352 uM; kcat = 208 min^-1; printed kcat/Km = 591 mM^-1 min^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q11201 FASTA fetched from rest.uniprot.org on 2026-06-17; row-specific mutation reconstructed from selected mutation signature and applied mutation signature Y191A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q11201 FASTA fetched from rest.uniprot.org on 2026-06-17; row-specific mutation reconstructed from selected mutation signature and applied mutation signature N170A to reconstruct the assayed variant sequence.


column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row ST3Gal1 (wild type), acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group; column KM (uM) = 26; column kcat (min^-1) = 189; column kcat/Km (mM^-1 min^-1) = 7269.

raw_value_unit_evidence: Table 1, enzyme row ST3Gal1 (wild type), acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group: KM = 26 uM; kcat = 189 min^-1; printed kcat/Km = 7269 mM^-1 min^-1.


row_label: Table 1, enzyme row ST3Gal1 (wild type), acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group


column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row V315Y, donor CMP-Neu5Ac column group; column KM (uM) = 271; column kcat (min^-1) = 8; column kcat/Km (mM^-1 min^-1) = 28.

raw_value_unit_evidence: Table 1, enzyme row V315Y, donor CMP-Neu5Ac column group: KM = 271 uM; kcat = 8 min^-1; printed kcat/Km = 28 mM^-1 min^-1.


organism: Vigna aconitifolia

sequence_source: UniProtKB reviewed accession P31893 direct REST/FASTA check on 2026-06-17


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q11201 and applied mutation signature Y230A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row Y230A, donor CMP-Neu5Ac column group; column KM (uM) = 205; column kcat (min^-1) = 150; column kcat/Km (mM^-1 min^-1) = 732.

raw_value_unit_evidence: Table 1, enzyme row Y230A, donor CMP-Neu5Ac column group: KM = 205 uM; kcat = 150 min^-1; printed kcat/Km = 732 mM^-1 min^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q11201 and applied mutation signature N147S to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row N147S, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group; column KM (uM) = 211; column kcat (min^-1) = 48; column kcat/Km (mM^-1 min^-1) = 227.

raw_value_unit_evidence: Table 1, enzyme row N147S, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group: KM = 211 uM; kcat = 48 min^-1; printed kcat/Km = 227 mM^-1 min^-1.


sequence_variant_note: Resolved canonical sequence from UniProt Q11201 canonical sequence with PMID 31784620 mutation label reconstruction and applied mutation signature S148A to reconstruct the assayed variant sequence.


column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row N147S, donor CMP-Neu5Ac column group; column KM (uM) = 668; column kcat (min^-1) = 75; column kcat/Km (mM^-1 min^-1) = 112.

raw_value_unit_evidence: Table 1, enzyme row N147S, donor CMP-Neu5Ac column group: KM = 668 uM; kcat = 75 min^-1; printed kcat/Km = 112 mM^-1 min^-1.


verification_status: unverified

sequence_variant_note: Resolved canonical sequence from UniProt Q11201 canonical sequence with PMID 31784620 mutation label reconstruction and applied mutation signature C59S/C64S to reconstruct the assayed variant sequence.

status: unverified


row_label: Table 1, enzyme row Y230A, donor CMP-Neu5Ac column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q11201 and applied mutation signature N170A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row N170A, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group; column KM (uM) = 96; column kcat (min^-1) = 39; column kcat/Km (mM^-1 min^-1) = 406.

raw_value_unit_evidence: Table 1, enzyme row N170A, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group: KM = 96 uM; kcat = 39 min^-1; printed kcat/Km = 406 mM^-1 min^-1.


column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row N170A, donor CMP-Neu5Ac column group; column KM (uM) = 184; column kcat (min^-1) = 37; column kcat/Km (mM^-1 min^-1) = 201.

raw_value_unit_evidence: Table 1, enzyme row N170A, donor CMP-Neu5Ac column group: KM = 184 uM; kcat = 37 min^-1; printed kcat/Km = 201 mM^-1 min^-1.


column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row Y230A, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group; column KM (uM) = 854; column kcat (min^-1) = 178; column kcat/Km (mM^-1 min^-1) = 208.

raw_value_unit_evidence: Table 1, enzyme row Y230A, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group: KM = 854 uM; kcat = 178 min^-1; printed kcat/Km = 208 mM^-1 min^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q11201 and applied mutation signature Y191A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row Y191A, donor CMP-Neu5Ac column group; column KM (uM) = 876; column kcat (min^-1) = 38; column kcat/Km (mM^-1 min^-1) = 43.

raw_value_unit_evidence: Table 1, enzyme row Y191A, donor CMP-Neu5Ac column group: KM = 876 uM; kcat = 38 min^-1; printed kcat/Km = 43 mM^-1 min^-1.


row_label: Table 1, enzyme row Y230F, donor CMP-Neu5Ac column group


sequence_variant_note: Resolved canonical sequence from UniProt Q11201 canonical sequence with PMID 31784620 mutation label reconstruction and applied mutation signature V315A to reconstruct the assayed variant sequence.


column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row Y191A, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group; column KM (uM) = 444; column kcat (min^-1) = 28; column kcat/Km (mM^-1 min^-1) = 63.

raw_value_unit_evidence: Table 1, enzyme row Y191A, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group: KM = 444 uM; kcat = 28 min^-1; printed kcat/Km = 63 mM^-1 min^-1.


row_label: Table 1, enzyme row V315Y, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group


column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row V315A, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group; column KM (uM) = 1388; column kcat (min^-1) = 145; column kcat/Km (mM^-1 min^-1) = 105.

raw_value_unit_evidence: Table 1, enzyme row V315A, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group: KM = 1388 uM; kcat = 145 min^-1; printed kcat/Km = 105 mM^-1 min^-1.


sequence_source: UniProt Q11201 canonical sequence with PMID 31784620 mutation label reconstruction

proof_lines: mutant enzyme C59S/C64S, at pH 7.4 and 37°C


source_db: uniprot

source: uniprot


substrate_name: ganglioside GA1

substrate: ganglioside GA1


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: ornithine (at 37 degrees Celsius, pH 7.4 and with 2-oxoglutarate as cosubstrate)


proof_lines: Vmax is 4 fold higher with Gal-beta-1,3-GalNAc than with Gal-beta-1,3-GlcNAc as substrate.


proof_lines: Relative Vmax is 2:5:1 for Gal-beta-1,3-GlcNAc, Gal-beta-1,4-GlcNAc and Gal-beta-1,3-GalNAc as substrate, respectively.


proof_lines: Vmax is 10 fold higher with Gal-beta-1,3-GalNAc than with Gal-beta-1,3-GlcNAc as substrate.


organism: Arabidopsis thaliana

proof_lines: The activity was enhanced in young plants under salt-stress conditions.


organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

substrate_name: L-ornithine (in the presence of 10 mM 2-oxoglutarate)

proof_lines: kcat is 4.32 sec(-1) with L-ornithine as substrate. kcat is 1.61 sec(-1) with L-lysine as substrate. kcat is 0.493 sec(-1) with D-ornithine as substrate. kcat is 3.25 sec(-1) with D-lysine as substrate. kcat is 3.51 sec(-1) with 2-oxoglutar


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

substrate_name: L-ornithine (in the presence of 5 mM 2-oxoglutarate)

proof_lines: kcat is 77.6 sec(-1) with L-ornithine as substrate. kcat is 86.4 sec(-1) with L-lysine as substrate. kcat is 95.8 sec(-1) with 2-oxoglutarate as substrate. kcat is 124 sec(-1) with 2-oxoadipate as substrate.


enzyme_display_name: mannose-1-phosphate guanylyltransferase

organism: Bos taurus

substrate_name: D-Mannose 1-phosphate; GTP

sequence_source: UniProtKB:Q2YDJ9 canonical sequence; direct lookup 2026-06-17

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

enzyme: mannose-1-phosphate guanylyltransferase

substrate: D-Mannose 1-phosphate; GTP


organism: Burkholderia cenocepacia

substrate_name: GDP-mannose

sequence_source: UniProtKB:B4EMQ6 canonical sequence; direct lookup 2026-06-17

proof_lines: pH 7.6, recombinant enzyme, in presence of 5 mM Mg2+ and 2 mM diphosphate

substrate: GDP-mannose


organism: Burkholderia cepacia

substrate_name: GDP-alpha-D-mannose

sequence_source: UniProtKB:Q06XM8 canonical sequence; direct lookup 2026-06-17

proof_lines: pH 7.6, 10 mM Mn2+, temperature not specified in the publication

proof_lines: pH 7.6, temperature not specified in the publication

substrate: GDP-alpha-D-mannose


organism: Pseudomonas aeruginosa

substrate_name: GTP; D-Mannose 1-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P07874 canonical sequence plus selected-record mutation signature K175Q; direct lookup 2026-06-17 and applied mutation signature K175Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannose-1-phosphate guanylyltransferase(Enzyme) mutant K175Q

substrate: GTP; D-Mannose 1-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07874 canonical sequence plus selected-record mutation signature K175E; direct lookup 2026-06-17 and applied mutation signature K175E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannose-1-phosphate guanylyltransferase(Enzyme) mutant K175E


sequence_source: UniProtKB:P07874 canonical sequence; direct lookup 2026-06-17

proof_lines:
25°C, cosubstrate GTP
25°C, cosubstrate mannose 1-phosphate
pH 8.0, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07874 canonical sequence plus selected-record mutation signature R19L; direct lookup 2026-06-17 and applied mutation signature R19L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannose-1-phosphate guanylyltransferase(Enzyme) mutant R19L


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07874 canonical sequence plus selected-record mutation signature S12A; direct lookup 2026-06-17 and applied mutation signature S12A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannose-1-phosphate guanylyltransferase(Enzyme) mutant S12A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07874 canonical sequence plus selected-record mutation signature R19K; direct lookup 2026-06-17 and applied mutation signature R19K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannose-1-phosphate guanylyltransferase(Enzyme) mutant R19K


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07874 canonical sequence plus selected-record mutation signature K20Q; direct lookup 2026-06-17 and applied mutation signature K20Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannose-1-phosphate guanylyltransferase(Enzyme) mutant K20Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07874 canonical sequence plus selected-record mutation signature R19H; direct lookup 2026-06-17 and applied mutation signature R19H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannose-1-phosphate guanylyltransferase(Enzyme) mutant R19H


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07874 canonical sequence plus selected-record mutation signature K175R; direct lookup 2026-06-17 and applied mutation signature K175R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannose-1-phosphate guanylyltransferase(Enzyme) mutant K175R


organism: Pyrococcus horikoshii

substrate_name: GTP

sequence_source: UniProtKB:O58649 canonical sequence; direct lookup 2026-06-17

proof_lines:
pH 7.6, 85°C
pH 7.6, 85°C, recombinant enzyme


organism: Saccharomyces cerevisiae

substrate_name: GDPmannose

sequence_source: UniProtKB:P41940 canonical sequence; direct lookup 2026-06-17

substrate: GDPmannose


organism: Salmonella enterica

substrate_name: alpha-D-Mannose 1-phosphate; GTP

sequence_source: UniProtKB:P26404 canonical sequence; direct lookup 2026-06-17

substrate: alpha-D-Mannose 1-phosphate; GTP


organism: Sus scrofa

sequence_source: UniProtKB:P0C5I2 canonical sequence; direct lookup 2026-06-17


organism: Trypanosoma brucei

substrate_name: D-mannose 1-phosphate

sequence_source: UniProtKB B9WNA1 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.

proof_lines: mixed-type inhibition with respect to mannose 1-phosphate

proof_lines: competitive inhibitor with respect to GTP

substrate: D-mannose 1-phosphate


organism: Trypanosoma cruzi

substrate_name: alpha-D-mannose 1-phosphate

sequence_source: UniProtKB Q4CMK4 direct REST lookup on 2026-06-17

substrate: alpha-D-mannose 1-phosphate


organism: Homo sapiens

substrate_name: mannose-1-phosphate (at 37 degrees Celsius)

sequence_source: source_record; direct UniProt FASTA check for Q9Y5P6

proof_lines: kcat is 23.71 sec(-1) with mannose-1-phosphate as substrate (PubMed:33986552). kcat is 21.48 sec(-1) with GTP as substrate (PubMed:33986552). kcat is 10.53 sec(-1) with GDP-mannose as substrate (PubMed:33986552).


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: mannose 1-phosphate

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

substrate: mannose 1-phosphate


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

substrate_name: D-mannose 6-phosphate

substrate: D-mannose 6-phosphate


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)


enzyme_display_name: phospholipase A2

organism: Crotalus atrox

substrate_name: lecithin

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

proof_lines:
in ether
in chloroform

enzyme: phospholipase A2

substrate: lecithin


organism: Crotalus durissus terrificus

substrate_name: 1-Palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid; H2O


organism: Daboia russelii

substrate_name: phosphatidylcholine

substrate: phosphatidylcholine


organism: Daboia russelii pulchella

substrate_name: Unknown

substrate: Unknown


organism: Dasyatis pastinaca


organism: Echis carinatus


organism: Escherichia coli

substrate_name: phosphatidylethanolamine

proof_lines:
active enzyme
inactivated enzyme

substrate: phosphatidylethanolamine


organism: Exaiptasia diaphana


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


assay_conditions_summary: pH 7.5; buffer solution, pH 7

proof_lines:
recombinant PLA2
natural PLA2
loop deleted PLA2


organism: Mesocricetus auratus

proof_lines: PLA1- and lysophospholipase activity of the 80-kDa PLA2


organism: Naja naja

proof_lines:
pH 8.5, 30°C
Triton X-100/phospholipid: 2/1


organism: Mycolicibacterium smegmatis

proof_lines: pH 7.5, 37°C, cosubstrate mannose 1-phosphate


organism: Pyrococcus furiosus

proof_lines: cosubstrate GTP, Vmax: 0.63 micromol/min/mg

proof_lines: cosubstrate GTP, Vmax: 14 micromol/min/mg

proof_lines: cosubstrate CTP, Vmax: 11 micromol/min/mg


organism: Salmonella enterica

proof_lines:
pH 8.0, 25°C
pH 8.0, 25°C, recombinant enzyme
uncompetitive vs. mannose 1-phosphate


organism: Sus scrofa

substrate: GTP


organism: Solanum lycopersicum

substrate_name: UTP

proof_lines: in presence of 0.3 mM each of ATP, CTP and GTP

substrate: UTP


organism: Aeropyrum pernix

substrate_name: p-nitrophenyl propionate

substrate: p-nitrophenyl propionate


organism: Arabidopsis thaliana

proof_lines: pH 8.5, 37°C, recombinant AtsPLA2-alpha, substrate below critical micelle concentration

proof_lines: pH 8.5, 37°C, recombinant AtsPLA2-alpha, substrate above critical micelle concentration or in presence of 2 M NaCl


organism: Bos taurus

proof_lines: micellar substrate, enzyme saturated with Ca2+


organism: Bothrocophias hyoprora

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

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


organism: Bothrops jararacussu

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

proof_lines: 0.027 mM bovine serum albumin, 50 mM KCl, 1 mM CaCl2, 50 mM Tris- HCl, pH 8.0, temperature not specified in the publication

proof_lines: 0.027 mM bovine serum albumin,50 mM KCl, 1 mM CaCl2, 50 mM Tris-HCl, pH 8.0, temperature not specified in the publication

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


organism: Camelus dromedarius

substrate_name: phosphatidylserine

substrate: phosphatidylserine


organism: Crotalus adamanteus


organism: Gallus gallus


organism: Homo sapiens

proof_lines:
pH 8, 37°C
transgenic mouse, pH 7.5, 37°C


organism: Lathyrus oleraceus

substrate_name: L-ornithine

substrate: L-ornithine


organism: Lysinibacillus sphaericus


organism: Manduca sexta


organism: Mus musculus


organism: Plasmodium falciparum


organism: Rattus norvegicus

proof_lines: with pyruvate as cosubstrate, pH 7.1, 37°C


organism: Arthrobacter sp.

substrate_name: diphosphate

substrate: diphosphate


organism: Helicobacter pylori

proof_lines:
pH 8.0, 37°C, cosubstrate GTP
pH 8.0, 37°C, cosubstrate diphosphate


organism: Leptospira interrogans serovar Copenhageni


substrate_name: CMP-N-(4-pentynoyl)neuraminic acid

proof_lines: recombinant enzyme DELTA56ST3GalI, at pH 6.2 and 37°C

substrate: CMP-N-(4-pentynoyl)neuraminic acid


organism: Pasteurella dagmatis

substrate_name: lactose

substrate: lactose


organism: Pasteurella multocida

substrate_name: CMP-N-acetylneuraminate

assay_conditions_summary: pH 8.5; 310.15 K; buffer Tris-HCl

proof_lines: mutant enzyme R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C

substrate: CMP-N-acetylneuraminate


proof_lines: wild type enzyme, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C


proof_lines: mutant enzyme E271F/R313Y, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C


proof_lines: mutant enzyme E271F, in Tris-HCl buffer (100 mM, pH 8.5), at 37°C


organism: Ancylostoma ceylanicum


organism: Arabidopsis thaliana

proof_lines:
normal conditions
salt stress conditions


organism: Aspergillus nidulans


organism: Bacillus sp. (in: firmicutes)


organism: Bos taurus


organism: Cucurbita pepo


organism: Homo sapiens

substrate_name: CMP-N-acetyl-beta-neuraminate

sequence_source: UniProtKB REST direct lookup: Q11201

column_label: Table 1 (Kinetic parameters of MBP-fused hST3Gal1 and variants), enzyme row ST3Gal1 (wild type), donor CMP-Neu5Ac column group; column KM (uM) = 106; column kcat (min^-1) = 201; column kcat/Km (mM^-1 min^-1) = 1896.

raw_value_unit_evidence: Table 1, enzyme row ST3Gal1 (wild type), donor CMP-Neu5Ac column group: KM = 106 uM; kcat = 201 min^-1; printed kcat/Km = 1896 mM^-1 min^-1.

substrate: CMP-N-acetyl-beta-neuraminate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q11201 and applied mutation signature N147S to reconstruct the assayed variant sequence.

row_label: Table 1, enzyme row N147S, acceptor Gal-beta-1,3-GalNAc-alpha-O-Bn column group


organism: Sus scrofa

sequence_source: UniProtKB REST direct lookup: Q02745

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: (2E,6E)-farnesyl diphosphate synthase

organism: Artemisia tridentata subsp. spiciformis

substrate_name: Dimethylallyl diphosphate; Isopentenyl diphosphate

sequence_source: UniProtKB REST direct lookup: Q7XYT0

enzyme: (2E,6E)-farnesyl diphosphate synthase


substrate_name: Geranyl diphosphate

sequence_source: UniProtKB REST direct lookup: Q7XYS9

smiles: CC(C)=CCC/C(C)=C/COP(=O)(O)OP(=O)(O)O

substrate: Geranyl diphosphate


substrate_name: Isopentenyl diphosphate; Dimethylallyl diphosphate


substrate_name: dimethylallyl diphosphate

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

substrate: dimethylallyl diphosphate


substrate_name: Isopentenyl diphosphate

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

substrate: Isopentenyl diphosphate


organism: Escherichia coli

sequence_source: UniProtKB REST direct lookup: P22939

substrate: Isopentenyl diphosphate; Dimethylallyl diphosphate


organism: Geobacillus stearothermophilus

substrate_name: Geranyl diphosphate; Isopentenyl diphosphate

sequence_source: UniProtKB REST direct lookup: Q08291

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup: Q08291 and applied mutation signature L34V/R59Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: (2E,6E)-farnesyl diphosphate synthase(Enzyme) mutant L34V/R59Q


substrate: Geranyl diphosphate; Isopentenyl diphosphate


substrate_name: Isopentenyl diphosphate; Geranyl diphosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup: Q08291 and applied mutation signature V157A/H182Y to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: (2E,6E)-farnesyl diphosphate synthase(Enzyme) mutant V157A/H182Y


organism: Haematococcus lacustris

substrate_name: geranyl diphosphate

sequence_source: UniProtKB REST direct lookup: A0A0K0TQ44

substrate: geranyl diphosphate


sequence_source: UniProt REST direct lookup P14324: Farnesyl pyrophosphate synthase (FPPS_HUMAN), organism Homo sapiens, EC 2.5.1.10, length 419.

substrate: Isopentenyl diphosphate; Geranyl diphosphate


organism: Rattus norvegicus

sequence_source: UniProt REST direct lookup P05369: Farnesyl pyrophosphate synthase (FPPS_RAT), organism Rattus norvegicus, EC 2.5.1.10, length 353.


organism: Saccharomyces cerevisiae

sequence_source: UniProt REST direct lookup Q12051 was checked but not accepted: Geranylgeranyl pyrophosphate synthase BTS1 (GGPPS_YEAST), organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c), EC 2.5.1.-.


proof_lines: SABIO-RK modifier species: (2E,6E)-farnesyl diphosphate synthase(Enzyme) mutant S71Y


substrate_name: 2-Oxoglutarate; L-Ornithine

sequence_source: UniProt REST direct lookup Q9FNK4: Ornithine aminotransferase, mitochondrial (OAT_ARATH), organism Arabidopsis thaliana, EC 2.6.1.13, length 475.

substrate: 2-Oxoglutarate; L-Ornithine


sequence_source: UniProt REST direct lookup Q3ZCF5: Ornithine aminotransferase, mitochondrial (OAT_BOVIN), organism Bos taurus, EC 2.6.1.13, length 439.

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


mutation_signature: Δ1

sequence_variant_note: Resolved canonical sequence from UniProt REST direct lookup P04181: Ornithine aminotransferase, mitochondrial (OAT_HUMAN), organism Homo sapiens, EC 2.6.1.13, length 439. and applied mutation signature Δ1 to reconstruct the assayed variant sequence.

proof_lines: assay based on reduction of DELTA1-pyrroline-5-carboxylate, pH 8.0, 37°C


sequence_variant_note: Resolved canonical sequence from UniProt REST direct lookup P04181: Ornithine aminotransferase, mitochondrial (OAT_HUMAN), organism Homo sapiens, EC 2.6.1.13, length 439. and applied mutation signature R217A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 15°C, recombinant mutant R217A, 0.001 mM enzyme

proof_lines: pH 8.0, 25°C, recombinant mutant R217A, 60 nM enzyme


substrate_name: L-Ornithine

sequence_source: UniProt REST direct lookup P04181: Ornithine aminotransferase, mitochondrial (OAT_HUMAN), organism Homo sapiens, EC 2.6.1.13, length 439.

substrate: L-Ornithine


proof_lines: pH 8.0, 15°C, recombinant wild-ype enzyme, 0.001 mM enzyme

proof_lines: pH 8.0, 15°C, recombinant wild-type enzyme, 0.001 mM enzyme

proof_lines: recombinant wild-type enzyme, pH 8.0, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P04181 displayed sequence; R217A reconstructed during review and applied mutation signature R217A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P04181 displayed sequence; R180T reconstructed during review and applied mutation signature R180T to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant R180Tenzyme, pH 8.0, 25°C


sequence_source: UniProtKB reviewed accession P04181 displayed sequence; R180T reconstructed during review


proof_lines: recombinant mutant R180T enzyme, pH 8.0, 25°C


organism: Ricinus communis

substrate_name: isopentenyl diphosphate

proof_lines: 0.042-0.056 mg/ml protein, isoenzyme II, Km values depend on protein concentration

proof_lines: 0.042-0.056 mg/ml protein, isoenzyme I, Km values depend on protein concentration

substrate: isopentenyl diphosphate


organism: Artemisia spiciformis


organism: Hevea brasiliensis

substrate_name: DMAPP

substrate: DMAPP


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: IPP (at 37 degrees Celsius and pH 7.9)

substrate: IPP (at 37 degrees Celsius and pH 7.9)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: farnesyl diphosphate

substrate: farnesyl diphosphate


enzyme_display_name: methylumbelliferyl-acetate deacetylase

substrate_name: p-nitrophenyl acetate

proof_lines: mutant L58F/W197I, Lineweaver-Burke extrapolation

enzyme: methylumbelliferyl-acetate deacetylase

substrate: p-nitrophenyl acetate


substrate_name: diethyl 4-nitrophenyl phosphate

proof_lines: phosphorylation rate, mutant W197H, 22°C

substrate: diethyl 4-nitrophenyl phosphate


substrate_name: dimethyl 4-nitrophenyl phosphate

proof_lines:
phosphorylation rate, wild-type, 22°C
wild-type

substrate: dimethyl 4-nitrophenyl phosphate


proof_lines: phosphorylation rate, double mutant W197I/C60R, 22°C


proof_lines: phosphorylation rate, mutant M162H, 22°C


substrate_name: p-nitrophenyl butyrate

proof_lines: mutant C60S, after removal of beta-mercaptoethanol

substrate: p-nitrophenyl butyrate


proof_lines: phosphorylation rate, mutant W197I, 22°C


substrate_name: S-Lactoylglutathione

substrate: S-Lactoylglutathione


enzyme_display_name: inositol-phosphate phosphatase

organism: Methanocaldococcus jannaschii

substrate_name: D-myo-Inositol 1-phosphate

enzyme: inositol-phosphate phosphatase

substrate: D-myo-Inositol 1-phosphate


organism: Mycobacterium tuberculosis

substrate_name: myo-inositol 1-phosphate

substrate: myo-inositol 1-phosphate


proof_lines: pH 9.3, 37°C, recombinant wild-type enzyme


organism: Mycolicibacterium smegmatis


substrate_name: H2O; 1D-myo-Inositol 1-phosphate

proof_lines:
brain IMPase
duodenal IMPase

substrate: H2O; 1D-myo-Inositol 1-phosphate


organism: Rhizobium leguminosarum


substrate_name: DL-myo-inositol 1-phosphate

substrate: DL-myo-inositol 1-phosphate


organism: Synechocystis sp.

proof_lines: in the presence of 3 mM MgCl2 in 50 mM Tris-Cl (pH 8), at 42°C


organism: Thermotoga maritima


organism: Arthrobacter sp.

substrate_name: maltotetraosyl trehalose

substrate: maltotetraosyl trehalose


organism: Saccharolobus solfataricus

substrate_name: maltooligosyltrehalose

proof_lines: pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme H195A

substrate: maltooligosyltrehalose


proof_lines: pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme R447A


proof_lines: phosphorylation rate, double mutant W197I/C60Q, 22°C


proof_lines: phosphorylation rate, double mutant W197I/C60H, 22°C


organism: Archaeoglobus fulgidus

substrate_name: 4-nitrophenyl phosphate

substrate: 4-nitrophenyl phosphate


proof_lines:
pH 8.0, 85°C
85°C
native enzyme, pH 8.0, 80°C


organism: Bos taurus

substrate_name: myo-Inositol phosphate; H2O

substrate: myo-Inositol phosphate; H2O


organism: Cyberlindnera jadinii


organism: Escherichia coli

substrate_name: L-myo-Inositol 1-phosphate

substrate: L-myo-Inositol 1-phosphate


organism: Gallus gallus


organism: Glycine max

substrate_name: diphosphate

assay_conditions_summary: pH 7; 310.15 K; buffer conditions

proof_lines: at 37°C, in 25 mM phosphate buffer with 2 mM dithiothreitol (pH 7.0) and 2 mM MgCl2

substrate: diphosphate


organism: Homo sapiens


organism: Lilium longiflorum

substrate_name: 1D-myo-Inositol 3-phosphate; H2O

substrate: 1D-myo-Inositol 3-phosphate; H2O


organism: Pumpkin

substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


organism: Streptomyces argenteolus

substrate_name: farnesyl diphosphate

proof_lines: cosubstrate: farnesyl diphosphate, mutant enzyme L58A

substrate: farnesyl diphosphate


substrate_name: isopentenyl diphosphate

proof_lines: cosubstrate: dimethylallyl diphosphate, wild-type enzyme

substrate: isopentenyl diphosphate


organism: Sundstroemia setigera

proof_lines: with dimethylallyl diphosphate as cosubstrate, at pH 7.5% and 30°C

proof_lines: with geranyl diphosphate as cosubstrate, at pH 7.5% and 30°C


organism: Oryctolagus cuniculus


organism: Rattus norvegicus

proof_lines:
pH 8.0, 25°C, recombinant enzyme
neutral nuclear PLA2
pH 7.5


organism: Sus scrofa

proof_lines:
large unilamellar vesicles
small unilamellar vesicles
25.6°C


organism: synthetic construct

substrate_name: phosphatidylcholine

assay_conditions_summary: pH 8.5; 313.15 K; buffer 100 mM Tris-HCl

proof_lines: standard PLA2, in 100 mM Tris-HCl buffer, pH 8.5, at 40°C, 50 mM sodium bis(2-ethylhexyl) sulfosuccinate and 0.05mM phenolsulfonphthalein in isooctane

substrate: phosphatidylcholine


organism: Trimorphodon lambda

substrate_name: Unknown

substrate: Unknown


organism: Trypanosoma congolense

substrate_name: dioleolyl-sn-phosphatidylethanolamine

substrate: dioleolyl-sn-phosphatidylethanolamine


organism: Saccharomyces cerevisiae

substrate_name: p-nitrophenyl acetate

substrate: p-nitrophenyl acetate


substrate_name: diethyl 4-nitrophenyl phosphate

proof_lines: phosphorylation rate, double mutant W197I/C60K, 22°C

substrate: diethyl 4-nitrophenyl phosphate


enzyme_display_name: protein-histidine N-methyltransferase

substrate_name: beta-actin L-histidine73

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q86TU7 and applied mutation signature N256Q to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic properties of wildtype SETD3 and its mutants); the Substrate column carries 'beta-actin' down the block and the enzyme-form column reads 'N256Q'; column 'Vmax (nmol min^-1 mg^-1)' = 10.860; column 'KM (uM)' = 0.784; column 'kcat (min^-1)' = 0.649; column 'kcat/KM (min^-1 uM^-1)' = 0.828.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.784 uM; 0.784 / 1000 = 0.000784 mM, carried exactly. kcat: printed Table 3 cell 0.649 min^-1; 0.649 / 60 = 0.010816666666666667 s^-1; this catalog lane carries kcat at two significant figures, at which that quotient is 0.011 s^-1, and that is the value this record states for the paper. kcat/Km: printed Table 3 cell 0.828 min^-1 uM^-1; 1 min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 0.828 * 1000 / 60 = 13.8 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate block 'beta-actin', enzyme-form row 'N256Q': Vmax = 10.860 nmol min^-1 mg^-1; KM = 0.784 uM; kcat = 0.649 min^-1; printed kcat/KM = 0.828 min^-1 uM^-1.

row_label: Table 3, substrate block 'beta-actin', SETD3 enzyme-form row 'N256Q'

table_label: Table 3: Kinetic properties of wildtype SETD3 and its mutants (eLife 2019, volume 8, article e43676)

enzyme: protein-histidine N-methyltransferase

substrate: beta-actin L-histidine73


substrate_name: S-adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q86TU7 and applied mutation signature N256D to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic properties of wildtype SETD3 and its mutants); the Substrate column carries 'AdoMet' down the block and the enzyme-form column reads 'N256D'; column 'Vmax (nmol min^-1 mg^-1)' = 0.671; column 'KM (uM)' = 0.165; column 'kcat (min^-1)' = 0.040; column 'kcat/KM (min^-1 uM^-1)' = 0.242.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.165 uM; 0.165 / 1000 = 0.000165 mM, carried exactly. kcat: printed Table 3 cell 0.040 min^-1; 0.040 / 60 = 0.0006666666666666666 s^-1; this catalog lane carries kcat at two significant figures, at which that quotient is 0.00067 s^-1, and that is the value this record states for the paper. kcat/Km: printed Table 3 cell 0.242 min^-1 uM^-1; 1 min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 0.242 * 1000 / 60 = 4.033333333333333 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate block 'AdoMet', enzyme-form row 'N256D': Vmax = 0.671 nmol min^-1 mg^-1; KM = 0.165 uM; kcat = 0.040 min^-1; printed kcat/KM = 0.242 min^-1 uM^-1.

row_label: Table 3, substrate block 'AdoMet', SETD3 enzyme-form row 'N256D'

substrate: S-adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q86TU7 direct REST lookup on 2026-06-17 and applied mutation signature N256D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q86TU7 direct REST lookup on 2026-06-17 and applied mutation signature N256A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q86TU7 and applied mutation signature R215A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic properties of wildtype SETD3 and its mutants); the Substrate column carries 'beta-actin' down the block and the enzyme-form column reads 'R215A'; column 'Vmax (nmol min^-1 mg^-1)' = 3.553; column 'KM (uM)' = 1.087; column 'kcat (min^-1)' = 0.212; column 'kcat/KM (min^-1 uM^-1)' = 0.195.

normalized_value_unit_evidence: Km: printed Table 3 cell 1.087 uM; 1.087 / 1000 = 0.001087 mM, carried exactly. kcat: printed Table 3 cell 0.212 min^-1; 0.212 / 60 = 0.003533333333333333 s^-1; this catalog lane carries kcat at two significant figures, at which that quotient is 0.0035 s^-1, and that is the value this record states for the paper. kcat/Km: printed Table 3 cell 0.195 min^-1 uM^-1; 1 min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 0.195 * 1000 / 60 = 3.2500000000000004 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate block 'beta-actin', enzyme-form row 'R215A': Vmax = 3.553 nmol min^-1 mg^-1; KM = 1.087 uM; kcat = 0.212 min^-1; printed kcat/KM = 0.195 min^-1 uM^-1.

row_label: Table 3, substrate block 'beta-actin', SETD3 enzyme-form row 'R215A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q86TU7 and applied mutation signature R75A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic properties of wildtype SETD3 and its mutants); the Substrate column carries 'AdoMet' down the block and the enzyme-form column reads 'R75A'; column 'Vmax (nmol min^-1 mg^-1)' = 0.265; column 'KM (uM)' = 3.601; column 'kcat (min^-1)' = 0.016; column 'kcat/KM (min^-1 uM^-1)' = 0.004.

normalized_value_unit_evidence: Km: printed Table 3 cell 3.601 uM; 3.601 / 1000 = 0.003601 mM, carried exactly. kcat: printed Table 3 cell 0.016 min^-1; 0.016 / 60 = 0.0002666666666666667 s^-1; this catalog lane carries kcat at two significant figures, at which that quotient is 0.00027 s^-1, and that is the value this record states for the paper. kcat/Km: printed Table 3 cell 0.004 min^-1 uM^-1; 1 min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 0.004 * 1000 / 60 = 0.06666666666666668 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate block 'AdoMet', enzyme-form row 'R75A': Vmax = 0.265 nmol min^-1 mg^-1; KM = 3.601 uM; kcat = 0.016 min^-1; printed kcat/KM = 0.004 min^-1 uM^-1.

row_label: Table 3, substrate block 'AdoMet', SETD3 enzyme-form row 'R75A'


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q86TU7 direct REST lookup on 2026-06-17 and applied mutation signature R215A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q86TU7 and applied mutation signature Y313F to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic properties of wildtype SETD3 and its mutants); the Substrate column carries 'AdoMet' down the block and the enzyme-form column reads 'Y313F'; column 'Vmax (nmol min^-1 mg^-1)' = 1.623; column 'KM (uM)' = 6.543; column 'kcat (min^-1)' = 0.097; column 'kcat/KM (min^-1 uM^-1)' = 0.015.

normalized_value_unit_evidence: Km: printed Table 3 cell 6.543 uM; 6.543 / 1000 = 0.006543 mM, carried exactly. kcat: printed Table 3 cell 0.097 min^-1; 0.097 / 60 = 0.0016166666666666666 s^-1; this catalog lane carries kcat at two significant figures, at which that quotient is 0.0016 s^-1, and that is the value this record states for the paper. kcat/Km: printed Table 3 cell 0.015 min^-1 uM^-1; 1 min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 0.015 * 1000 / 60 = 0.25 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate block 'AdoMet', enzyme-form row 'Y313F': Vmax = 1.623 nmol min^-1 mg^-1; KM = 6.543 uM; kcat = 0.097 min^-1; printed kcat/KM = 0.015 min^-1 uM^-1.

row_label: Table 3, substrate block 'AdoMet', SETD3 enzyme-form row 'Y313F'


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q86TU7 direct REST lookup on 2026-06-17 and applied mutation signature Y313F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q86TU7 and applied mutation signature N278A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic properties of wildtype SETD3 and its mutants); the Substrate column carries 'AdoMet' down the block and the enzyme-form column reads 'N278A'; column 'Vmax (nmol min^-1 mg^-1)' = 0.018; column 'KM (uM)' = 0.350; column 'kcat (min^-1)' = 0.001; column 'kcat/KM (min^-1 uM^-1)' = 0.003.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.350 uM; 0.350 / 1000 = 0.00035 mM, carried exactly. kcat: printed Table 3 cell 0.001 min^-1; 0.001 / 60 = 0.000016666666666666667 s^-1; this catalog lane carries kcat at two significant figures, at which that quotient is 0.000017 s^-1, and that is the value this record states for the paper. kcat/Km: printed Table 3 cell 0.003 min^-1 uM^-1; 1 min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 0.003 * 1000 / 60 = 0.05 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate block 'AdoMet', enzyme-form row 'N278A': Vmax = 0.018 nmol min^-1 mg^-1; KM = 0.350 uM; kcat = 0.001 min^-1; printed kcat/KM = 0.003 min^-1 uM^-1.

row_label: Table 3, substrate block 'AdoMet', SETD3 enzyme-form row 'N278A'


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q86TU7 direct REST lookup on 2026-06-17 and applied mutation signature R316A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q86TU7 direct REST lookup on 2026-06-17 and applied mutation signature N278A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q86TU7 and applied mutation signature R316A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic properties of wildtype SETD3 and its mutants); the Substrate column carries 'beta-actin' down the block and the enzyme-form column reads 'R316A'; column 'Vmax (nmol min^-1 mg^-1)' = 2.903; column 'KM (uM)' = 1.115; column 'kcat (min^-1)' = 0.173; column 'kcat/KM (min^-1 uM^-1)' = 0.155.

normalized_value_unit_evidence: Km: printed Table 3 cell 1.115 uM; 1.115 / 1000 = 0.001115 mM, carried exactly. kcat: printed Table 3 cell 0.173 min^-1; 0.173 / 60 = 0.0028833333333333332 s^-1; this catalog lane carries kcat at two significant figures, at which that quotient is 0.0029 s^-1, and that is the value this record states for the paper. kcat/Km: printed Table 3 cell 0.155 min^-1 uM^-1; 1 min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 0.155 * 1000 / 60 = 2.5833333333333335 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate block 'beta-actin', enzyme-form row 'R316A': Vmax = 2.903 nmol min^-1 mg^-1; KM = 1.115 uM; kcat = 0.173 min^-1; printed kcat/KM = 0.155 min^-1 uM^-1.

row_label: Table 3, substrate block 'beta-actin', SETD3 enzyme-form row 'R316A'


sequence_source: UniProtKB:Q86TU7 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.

column_label: Table 3 (Kinetic properties of wildtype SETD3 and its mutants); the Substrate column carries 'beta-actin' down the block and the enzyme-form column reads 'Wildtype'; column 'Vmax (nmol min^-1 mg^-1)' = 13.550; column 'KM (uM)' = 0.502; column 'kcat (min^-1)' = 0.809; column 'kcat/KM (min^-1 uM^-1)' = 1.612.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.502 uM; 0.502 / 1000 = 0.000502 mM, carried exactly. kcat: printed Table 3 cell 0.809 min^-1; 0.809 / 60 = 0.013483333333333333 s^-1; this catalog lane carries kcat at two significant figures, at which that quotient is 0.013 s^-1, and that is the value this record states for the paper. kcat/Km: printed Table 3 cell 1.612 min^-1 uM^-1; 1 min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 1.612 * 1000 / 60 = 26.86666666666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate block 'beta-actin', enzyme-form row 'Wildtype': Vmax = 13.550 nmol min^-1 mg^-1; KM = 0.502 uM; kcat = 0.809 min^-1; printed kcat/KM = 1.612 min^-1 uM^-1.

row_label: Table 3, substrate block 'beta-actin', SETD3 enzyme-form row 'Wildtype'


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q86TU7 direct REST lookup on 2026-06-17 and applied mutation signature R75A to reconstruct the assayed variant sequence.


enzyme_display_name: galacturonan 1,4-alpha-galacturonidase

organism: Butyrivibrio fibrisolvens

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

enzyme: galacturonan 1,4-alpha-galacturonidase


organism: Daucus carota

proof_lines:
0.1 M acetate buffer pH 3.8, 30°C
heptagalacturonate


organism: Fusarium oxysporum


organism: Geotrichum lactis

substrate_name: Pectin

substrate: Pectin


organism: Malus domestica


organism: Marchantia polymorpha


organism: Penicillium janczewskii

substrate_name: citric pectin

substrate: citric pectin


organism: Penicillium janthinellum

substrate_name: polygalacturonic acid

substrate: polygalacturonic acid


organism: Penicillium oxalicum

proof_lines: pH 5.0, 50°C, recombinant wild-type full-length enzyme


proof_lines: pH 5.0, 50°C, recombinant catalytic polygalacturonase domain


organism: Rhizopus arrhizus


organism: Saccharobesus litoralis

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


organism: Saccharolobus solfataricus

substrate_name: maltooligosyltrehalose

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

proof_lines: pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme Y155F

substrate: maltooligosyltrehalose


proof_lines: pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme E450A


proof_lines: pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme D156A


proof_lines: pH 5, 60°C, calculated as the amount of trehalose released from the substrate, mutant enzyme Y155A


proof_lines: pH 5, 60°C, calculated as the amount of trehalose released from the substrate, wild-type enzyme


organism: Sulfolobus acidocaldarius

substrate_name: maltotetraosyl trehalose

substrate: maltotetraosyl trehalose


organism: Aspergillus giganteus


organism: Aspergillus niger

proof_lines:
at pH 4.0 and 40°C
enzyme form PGII
enzyme form PGI


organism: Aspergillus niveus


organism: Aspergillus tubingensis


organism: Bacillus licheniformis


organism: Thermotoga thermophilus

substrate_name: digalacturonic acid

substrate: digalacturonic acid


enzyme_display_name: glucan 1,6-alpha-glucosidase

organism: Arthrobacter globiformis

substrate_name: Dextran

enzyme: glucan 1,6-alpha-glucosidase

substrate: Dextran


organism: Lactiplantibacillus plantarum

substrate_name: isomaltose

substrate: isomaltose


organism: Lipomyces lipofer


enzyme_display_name: carboxypeptidase T

organism: Thermoactinomyces vulgaris

enzyme: carboxypeptidase T


substrate_name: N-carbobenzoxy-Ala-Ala-Phe

substrate: N-carbobenzoxy-Ala-Ala-Phe


enzyme_display_name: glutamate carboxypeptidase II

organism: Canis lupus familiaris

proof_lines: pH and temperature not specified in the publication

enzyme: glutamate carboxypeptidase II


organism: Homo sapiens

substrate_name: N-acetyl-Asp-Glu

proof_lines:
pH 7.4, 37°C
GCPIII
pH 7.4, 37°C, recombinant enzyme

substrate: N-acetyl-Asp-Glu


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

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


enzyme_display_name: peptidyl-tRNA hydrolase

organism: Escherichia coli

substrate_name: Unknown

sequence_source: UniProtKB:P0A7D1 direct REST FASTA/TSV check on 2026-06-17

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

proof_lines: at pH 6.0, with 50 mM sodium acetate and 200 mM NaCl, at 28°C

enzyme: peptidyl-tRNA hydrolase

substrate: Unknown


substrate_name: N-acetyl-Ala-tRNA(Ala)

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7D1 direct REST FASTA/TSV check on 2026-06-17 and applied mutation signature N185A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N185A, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28°C

substrate: N-acetyl-Ala-tRNA(Ala)


proof_lines: wild type enzyme, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28°C

proof_lines: pH 7.5, 28°C, 5-dephosphoylated diacetyl-Lys-tRNALys, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7D1 direct REST FASTA/TSV check on 2026-06-17 and applied mutation signature N185A/H188A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N185A/H188A, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7D1 direct REST FASTA/TSV check on 2026-06-17 and applied mutation signature H188A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H188A, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28°C


substrate_name: diacetyl-Lys-tRNALys

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7D1 direct REST FASTA/TSV check on 2026-06-17 and applied mutation signature F66A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: diacetyl-Lys-tRNALys


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7D1 direct REST FASTA/TSV check on 2026-06-17 and applied mutation signature N10A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7D1 direct REST FASTA/TSV check on 2026-06-17 and applied mutation signature D93A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7D1 direct REST FASTA/TSV check on 2026-06-17 and applied mutation signature M67A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A7D1 direct REST FASTA/TSV check on 2026-06-17 and applied mutation signature H113A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: diacetyl-lysine-tRNA

sequence_source: UniProtKB:Q9Y3E5 direct REST FASTA/TSV check on 2026-06-17

substrate: diacetyl-lysine-tRNA


organism: Staphylococcus aureus

sequence_source: UniProtKB:Q6YP15 direct REST FASTA/TSV check on 2026-06-17


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q86TU7 and applied mutation signature N256A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic properties of wildtype SETD3 and its mutants); the Substrate column carries 'AdoMet' down the block and the enzyme-form column reads 'N256A'; column 'Vmax (nmol min^-1 mg^-1)' = 1.136; column 'KM (uM)' = 0.686; column 'kcat (min^-1)' = 0.068; column 'kcat/KM (min^-1 uM^-1)' = 0.099.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.686 uM; 0.686 / 1000 = 0.000686 mM, carried exactly. kcat: printed Table 3 cell 0.068 min^-1; 0.068 / 60 = 0.0011333333333333334 s^-1; this catalog lane carries kcat at two significant figures, at which that quotient is 0.0011 s^-1, and that is the value this record states for the paper. kcat/Km: printed Table 3 cell 0.099 min^-1 uM^-1; 1 min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 0.099 * 1000 / 60 = 1.6500000000000001 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate block 'AdoMet', enzyme-form row 'N256A': Vmax = 1.136 nmol min^-1 mg^-1; KM = 0.686 uM; kcat = 0.068 min^-1; printed kcat/KM = 0.099 min^-1 uM^-1.

row_label: Table 3, substrate block 'AdoMet', SETD3 enzyme-form row 'N256A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q86TU7 and applied mutation signature N256Q to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic properties of wildtype SETD3 and its mutants); the Substrate column carries 'AdoMet' down the block and the enzyme-form column reads 'N256Q'; column 'Vmax (nmol min^-1 mg^-1)' = 6.368; column 'KM (uM)' = 0.103; column 'kcat (min^-1)' = 0.380; column 'kcat/KM (min^-1 uM^-1)' = 3.689.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.103 uM; 0.103 / 1000 = 0.000103 mM, carried exactly. kcat: printed Table 3 cell 0.380 min^-1; 0.380 / 60 = 0.006333333333333333 s^-1; this catalog lane carries kcat at two significant figures, at which that quotient is 0.0063 s^-1, and that is the value this record states for the paper. kcat/Km: printed Table 3 cell 3.689 min^-1 uM^-1; 1 min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 3.689 * 1000 / 60 = 61.48333333333334 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate block 'AdoMet', enzyme-form row 'N256Q': Vmax = 6.368 nmol min^-1 mg^-1; KM = 0.103 uM; kcat = 0.380 min^-1; printed kcat/KM = 3.689 min^-1 uM^-1.

row_label: Table 3, substrate block 'AdoMet', SETD3 enzyme-form row 'N256Q'


substrate_name: synthetic peptide corresponding to residue 66-80 of actin

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 enzyme N255V, at pH 10.5 and 37°C


proof_lines: mutant enzyme N255A, at pH 10.5 and 37°C

substrate: synthetic peptide corresponding to residue 66-80 of actin


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

substrate_name: fluorescent (boron-dipyrromethene (BODIPY) labeled) lysyl-tRNA(Lys3)


substrate_name: H2O; N-Substituted aminoacyl-tRNA

sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession check; same sequence for P0A7D1, P0A7D2, P0A7D3, Q0TIG6, and Q1RCN4 and applied mutation signature K105R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aminoacyl-tRNA hydrolase(Enzyme) mutant K105R

substrate: H2O; N-Substituted aminoacyl-tRNA


sequence_source: UniProt REST direct accession check; same sequence for P0A7D1, P0A7D2, P0A7D3, Q0TIG6, and Q1RCN4

sequence_variant_note: Mutation signature D93N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: aminoacyl-tRNA hydrolase(Enzyme) mutant D93N


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession check; same sequence for P0A7D1, P0A7D2, P0A7D3, Q0TIG6, and Q1RCN4 and applied mutation signature K103Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aminoacyl-tRNA hydrolase(Enzyme) mutant K103Q


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession check; same sequence for P0A7D1, P0A7D2, P0A7D3, Q0TIG6, and Q1RCN4 and applied mutation signature K105Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aminoacyl-tRNA hydrolase(Enzyme) mutant K105Q


sequence_variant_note: Mutation signature N10D matches the mutant residue at offset +1 and the reference residue at offset +12; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: SABIO-RK modifier species: aminoacyl-tRNA hydrolase(Enzyme) mutant N10D


substrate_name: N-Substituted aminoacyl-tRNA; H2O

sequence_variant_note: Mutation signature H113Q 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.

proof_lines: SABIO-RK modifier species: aminoacyl-tRNA hydrolase(Enzyme) mutant H113Q

substrate: N-Substituted aminoacyl-tRNA; H2O


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession check; same sequence for P0A7D1, P0A7D2, P0A7D3, Q0TIG6, and Q1RCN4 and applied mutation signature K103S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aminoacyl-tRNA hydrolase(Enzyme) mutant K103S


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 UniProt REST direct accession check; same sequence for P0A7D1, P0A7D2, P0A7D3, Q0TIG6, and Q1RCN4 and applied mutation signature K103R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aminoacyl-tRNA hydrolase(Enzyme) mutant K103R


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession check; same sequence for P0A7D1, P0A7D2, P0A7D3, Q0TIG6, and Q1RCN4 and applied mutation signature K105S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aminoacyl-tRNA hydrolase(Enzyme) mutant K105S


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession check; same sequence for P0A7D1, P0A7D2, P0A7D3, Q0TIG6, and Q1RCN4 and applied mutation signature M67E with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aminoacyl-tRNA hydrolase(Enzyme) mutant M67E


enzyme_display_name: pyroglutamyl-peptidase I

organism: Bacillus amyloliquefaciens

substrate_name: L-pyroglutamyl-beta-naphthylamide

sequence_variant_note: Resolved canonical sequence from UniProtKB:P46107 direct EC+organism lookup; F10Y variant reconstructed by residue substitution check and applied mutation signature F10Y to reconstruct the assayed variant sequence.

enzyme: pyroglutamyl-peptidase I

substrate: L-pyroglutamyl-beta-naphthylamide


sequence_source: UniProtKB:P46107 direct EC+organism lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:P46107 direct EC+organism lookup; S185C variant reconstructed by residue substitution check and applied mutation signature S185C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P46107 direct EC+organism lookup; C68S/S185C variant reconstructed by residue substitution check and applied mutation signature C68S/S185C to reconstruct the assayed variant sequence.


substrate_name: thyroliberin-releasing hormone

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

substrate: thyroliberin-releasing hormone


organism: Bacillus subtilis

substrate_name: Pyroglutamyl-beta-naphthylamide

substrate: Pyroglutamyl-beta-naphthylamide


organism: Bos taurus


organism: Cavia porcellus

substrate_name: Thyroliberin

substrate: Thyroliberin


organism: Gallus gallus

substrate_name: pyroglutamate-4-methylcoumarin 7-amide

substrate: pyroglutamate-4-methylcoumarin 7-amide


organism: Leishmania major

substrate_name: L-pyroglutamyl p-nitroanilide

substrate: L-pyroglutamyl p-nitroanilide


organism: Mus musculus


organism: Bacillus cereus

substrate_name: bulk peptidyl-tRNA

substrate: bulk peptidyl-tRNA


substrate_name: N-acetyl-Met-tRNA

substrate: N-acetyl-Met-tRNA


organism: Fusarium culmorum

substrate_name: N-acetyl-Phe-tRNA

substrate: N-acetyl-Phe-tRNA


organism: Mycobacterium tuberculosis

substrate_name: diacetyl-lysyl-tRNALys

substrate: diacetyl-lysyl-tRNALys


organism: Saccharolobus solfataricus

substrate_name: dephosphorylated diacyl-lysine-tRNA

proof_lines:
50°C, pH 7.5
pH 7.5, 50°C, recombinant enzyme
pH 7.5, 50°C

substrate: dephosphorylated diacyl-lysine-tRNA


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


enzyme_display_name: sulfate adenylyltransferase

organism: Allochromatium vinosum

substrate_name: adenylyl sulfate

sequence_source: UniProt REST O66036 direct accession lookup on 2026-06-17

enzyme: sulfate adenylyltransferase

substrate: adenylyl sulfate


organism: Aquifex aeolicus

substrate_name: diphosphate

sequence_source: UniProt REST O67174 direct accession lookup on 2026-06-17

proof_lines:
pH 8.0, 30°C
pH 8.0, 30°C, reaction with MoO42-
pH 8.0, 30°C, reaction with SO42-

substrate: diphosphate


substrate_name: GTP; H2O

substrate: GTP; H2O


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt REST P21156 canonical sequence using S40A on 2026-06-17 and applied mutation signature S40A to reconstruct the assayed variant sequence.


substrate_name: GTP

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt REST P21156 canonical sequence using S35A on 2026-06-17 and applied mutation signature S35A to reconstruct the assayed variant sequence.

substrate: GTP


substrate_name: H2O; GTP

sequence_source: Reconstructed from UniProt REST P21156 canonical sequence using S35A on 2026-06-17

proof_lines: SABIO-RK modifier species: sulfate adenylyltransferase(Enzyme) mutant S35A

substrate: H2O; GTP


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt REST P21156 canonical sequence using G37A on 2026-06-17 and applied mutation signature G37A to reconstruct the assayed variant sequence.


substrate_name: adenylylsulfate

sequence_source: Reconstructed from UniProt REST P21156 canonical sequence using G37A on 2026-06-17

substrate: adenylylsulfate


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt REST P21156 canonical sequence using D39A on 2026-06-17 and applied mutation signature D39A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: sulfate adenylyltransferase(Enzyme) mutant D39A


sequence_source: Reconstructed from UniProt REST P21156 canonical sequence using S40A on 2026-06-17

proof_lines: SABIO-RK modifier species: sulfate adenylyltransferase(Enzyme) mutant S40A


proof_lines: SABIO-RK modifier species: sulfate adenylyltransferase(Enzyme) mutant G37A


sequence_source: Reconstructed from UniProt REST P21156 canonical sequence using D39A on 2026-06-17


organism: Pseudomonas fluorescens

substrate_name: L-pyroglutamyl-beta-naphthylamide

sequence_source: UniProtKB reviewed accession P42673

substrate: L-pyroglutamyl-beta-naphthylamide


sequence_variant_note: Resolved canonical sequence from Reconstructed E22Q variant from UniProtKB reviewed accession P42673 and applied mutation signature E22Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed D89N variant from UniProtKB reviewed accession P42673 and applied mutation signature D89N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed E10Q variant from UniProtKB reviewed accession P42673 and applied mutation signature E10Q to reconstruct the assayed variant sequence.


organism: Rattus norvegicus

substrate_name: L-pyroglutamyl-aminoethylnitrate

sequence_source: UniProtKB reviewed accession Q76IC5

substrate: L-pyroglutamyl-aminoethylnitrate


organism: Streptococcus pyogenes

substrate_name: H2O; L-Pyroglutamyl-beta-naphthylamide

substrate: H2O; L-Pyroglutamyl-beta-naphthylamide


enzyme_display_name: stratum corneum chymotryptic enzyme

organism: Homo sapiens

sequence_source: UniProtKB reviewed accession P49862

enzyme: stratum corneum chymotryptic enzyme


enzyme_display_name: myeloblastin

substrate_name: Suc-Ala-Tyr-Leu-Val-p-nitroanilide

sequence_source: UniProtKB reviewed accession P24158

assay_conditions_summary: pH 7.4; 298.15 K; buffer 0.1 M Tris-HCl

proof_lines: in 0.1 M Tris-HCl buffer, pH 7.5, with 500 mM NaCl at 25°C

enzyme: myeloblastin

substrate: Suc-Ala-Tyr-Leu-Val-p-nitroanilide


enzyme_display_name: signal peptidase I

organism: Escherichia coli

substrate_name: FSASALAKI

sequence_source: Canonical context only: UniProtKB reviewed accession P00803

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

enzyme: signal peptidase I

substrate: FSASALAKI


sequence_source: UniProtKB reviewed accession P00803

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


organism: Glycine max

proof_lines: diphosphate in form of magnesium diphosphate


proof_lines: pH 8.0, 25°C, recombinant wild-type enzyme


substrate_name: adenylyl sulfate, diphosphate

sequence_variant_note: Resolved canonical sequence from UniProt REST accession lookup for Q8SAG1 on 2026-06-17 and applied mutation signature N249D to reconstruct the assayed variant sequence.

substrate: adenylyl sulfate, diphosphate


sequence_variant_note: Resolved canonical sequence from UniProt REST accession lookup for Q8SAG1 on 2026-06-17 and applied mutation signature N249A to reconstruct the assayed variant sequence.


substrate_name: ATP

sequence_source: UniProt REST accession lookup for O95340 on 2026-06-17

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: Sulfate

sequence_source: UniProt REST accession lookup for O43252 on 2026-06-17

substrate: Sulfate


substrate_name: Sulfate; ATP, Sulfate, ATP, Diphosphate, Adenylylsulfate, ATP; Sulfate

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


substrate_name: ATP; Sulfate, ATP, Sulfate, Diphosphate, Adenylylsulfate, Sulfate; ATP, ATP; Molybdate, Molybdate, plus 4 more

source_db: sabio_rk, brenda

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines:
pH 8.0, 30°C, reaction with sulfate
pH 8.0, 30°C, reaction with molybdate
pH 8.0, 30°C

source: sabio_rk, brenda


organism: Penicillium chrysogenum

sequence_source: UniProt REST accession lookup for Q12650 on 2026-06-17


substrate_name: Sulfate; ATP, Sulfate, ATP, Adenylylsulfate, Diphosphate, Adenylylsulfate; Diphosphate, ATP; Molybdate, Molybdate, plus 4 more

source_db: sabio_rk, skid

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

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

source: sabio_rk, skid


substrate_name: ATP, sulfate, MoO42-, adenylylsulfate, diphosphate

mutation_signature: truncated mutant enzyme del396-573

mutation_type: truncation

proof_lines: pH 8.0, 30°C, synthesis of adenylylsulfate, truncated mutant enzyme del396-573

proof_lines: pH 8.0, 30°C, truncated mutant enzyme del396-573

proof_lines: pH 8.0, 30°C, molybdolysis, truncated mutant enzyme del396-573


substrate_name: diphosphate


substrate_name: ATP, sulfate, adenylylsulfate, diphosphate, MoO42-

proof_lines: pH 8.0, 30°C, synthesis of adenylylsulfate, wild-type enzyme

proof_lines: pH 8.0, 30°C, molybdolysis, wild-type enzyme


substrate_name: Sulfate; ATP, Sulfate, ATP, Diphosphate, Adenylylsulfate, Diphosphate; Adenylylsulfate, Molybdate; ATP, Molybdate, plus 1 more

proof_lines: SABIO-RK modifier species: sulfate adenylyltransferase(Enzyme) wildtype truncated C-Terminus


organism: Saccharomyces cerevisiae

substrate_name: ATP; Sulfate, ATP, Sulfate, Adenylylsulfate, Diphosphate

sequence_source: UniProt REST accession lookup for P08536 on 2026-06-17


substrate_name: ATP; Sulfate

sequence_source: UniProtKB P08536 canonical sequence; reconstructed as residues 1-393 using the selected truncation signature and RCSB 1R6X/PubMed 14983089 identity anchor

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

proof_lines: SABIO-RK modifier species: sulfate adenylyltransferase(Enzyme) mutant (aa 1-393) C-terminal truncated

substrate: ATP; Sulfate


organism: Thiobacillus denitrificans ATCC 25259

substrate_name: adenylyl sulfate

sequence_source: UniProtKB Q3SEZ6 canonical sequence retrieved during exact accession lookup

proof_lines:
ATP synthesis
adenylyl sulfate synthesis


organism: Thermosynechococcus vestitus

substrate_name: cyclic di-3',5'-guanylate

sequence_source: UniProtKB:Q8DLK6 direct REST lookup, entry Q8DLK6_THEVB

proof_lines: pH and temperature not specified in the publication, in the presence of the activator cAMP (0.002 mM)

substrate: cyclic di-3',5'-guanylate


organism: Vibrio cholerae serotype O1

substrate_name: 3'3'-cyclic GMP-AMP

sequence_source: UniProtKB:A0A0H3AJ04 direct REST lookup, entry A0A0H3AJ04_VIBC3

substrate: 3'3'-cyclic GMP-AMP


sequence_source: UniProtKB:Q9KRD2 direct REST lookup, entry Q9KRD2_VIBCH

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: streptopain

sequence_source: UniProtKB:P0C0J0 direct REST lookup, reviewed entry SPEB_STRPY

enzyme: streptopain


enzyme_display_name: memapsin 2

sequence_source: UniProtKB:P56817 canonical sequence inspected as context only; not accepted as the row-specific variant sequence

proof_lines: SABIO-RK modifier species: memapsin 2(Enzyme) mutant Leu28p-memapsin 2

proof_lines: SABIO-RK modifier species: memapsin 2(Enzyme) mutant Gly45p-memapsin 2

enzyme: memapsin 2


sequence_source: UniProtKB:P56817 direct REST lookup, reviewed entry BACE1_HUMAN

proof_lines: pH 4, temperature not specified in the publication

proof_lines: Ki less than 0.000001 mM, pH and temperature not specified in the publication


organism: Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / LMG 10263 / NCTC 9343 / Onslow / VPI 2553 / EN-2)

substrate_name: Man-Glc

substrate: Man-Glc


organism: Ruminococcus albus (strain ATCC 27210 / DSM 20455 / JCM 14654 / NCDO 2250 / 7)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)

substrate_name: c-di-GMP

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

substrate: c-di-GMP


organism: Escherichia coli (strain K12)


substrate_name: 3',5'-Cyclic diGMP; H2O

sequence_source: UniProtKB REST direct lookup for P21514 on 2026-06-17

substrate: 3',5'-Cyclic diGMP; H2O


substrate_name: H2O; 3',5'-Cyclic diGMP

sequence_source: UniProtKB REST direct lookup for P76129 on 2026-06-17

substrate: H2O; 3',5'-Cyclic diGMP


organism: Pseudomonas aeruginosa

substrate_name: cyclic-di-GMP

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature T267A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; buffer 100 mM Tris

proof_lines: mutant enzyme T267A, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2

substrate: cyclic-di-GMP


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature Q372A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q372A, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature D296A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D296A, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


verification_status: verified

sequence_source: UniProtKB REST direct lookup for Q9HX69 on 2026-06-17

assay_conditions_summary: pH 8; 296.15 K; buffer 100 mM Tris

column_label: Table 1 carries five columns, printed in this order: Enzyme, kcat (s^-1), Km (uM), kcat/Km (s^-1 uM^-1) and Decrease in kcat (fold). The cited cell set is the Table 1, enzyme row RocR, the wild-type enzyme: kcat (s^-1) = 0.67; Km (uM) = 3.2; kcat/Km (s^-1 uM^-1) = 0.21; the Decrease in kcat (fold) cell is blank on the wild-type row, which is itself the reference of that column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.67 under the column head kcat (s^-1); that column is already per second, so no unit conversion applies and the paper value is 0.67 s^(-1). Km: printed Table 1 cell 3.2 under the column head Km (uM); 1 uM is 0.001 mM, so 3.2 / 1000 = 0.0032 mM. kcat/Km: printed Table 1 cell 0.21 under the column head kcat/Km (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.21 x 1000 = 210.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme row RocR, the wild-type enzyme: kcat = 0.67 under the column head kcat (s^-1); Km = 3.2 under the column head Km (uM); the printed kcat/Km cell = 0.21 under the column head kcat/Km (s^-1 uM^-1).

table_label: Table 1: Steady-state kinetic parameters for RocR and its mutants (J. Bacteriol. 2008, 190(10):3622-3631)

status: verified


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature E352D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E352D, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature E268Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E268Q, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature Q161A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q161A, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature R179A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R179A, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature E352Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E352Q, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature D318A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D318A, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HX69 on 2026-06-17 and applied mutation signature E355A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E355A, in 100 mM Tris buffer (pH 8.0) with 20 mM KCl and 25 mM MgCl2


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9HV27 on 2026-06-17 and applied mutation signature E314A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant enzyme E314A


sequence_source: UniProtKB REST direct lookup for Q9HV27 on 2026-06-17

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

proof_lines: pH 8.0, 30°C, recombinant wild-type enzyme


sequence_source: UniProtKB REST direct lookup for Q9HWS0 on 2026-06-17


organism: Ruminococcus albus

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


substrate_name: sophorose

substrate: sophorose


substrate_name: N,N'-diacetylchitobiose

substrate: N,N'-diacetylchitobiose


substrate_name: laminaribiose

substrate: laminaribiose


substrate_name: N-acetyl-D-glucosamine

substrate: N-acetyl-D-glucosamine


substrate_name: D-Mannose

substrate: D-Mannose


substrate_name: D-glucose

sequence_source: UniProtKB reviewed E6UIS7 direct REST lookup on 2026-06-17

substrate: D-glucose


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed E6UIS7 canonical sequence plus H245A reconstruction by direct residue check on 2026-06-17 and applied mutation signature H245A to reconstruct the assayed variant sequence.


substrate_name: alpha-D-mannose 1-phosphate

substrate: alpha-D-mannose 1-phosphate


sequence_source: UniProtKB reviewed E6UIS7 canonical sequence plus H245A reconstruction by direct residue check on 2026-06-17


organism: Desulfovibrio piger

substrate_name: ATP

assay_conditions_summary: pH 8; 308.15 K; cofactor ATP

substrate: ATP


organism: Euglena gracilis

substrate_name: diphosphate

proof_lines:
pH 8.8, enzyme form ATPSm
pH 8.8, enzyme form ATPSc

substrate: diphosphate


organism: Geobacillus stearothermophilus

substrate_name: dATP

assay_conditions_summary: pH 6; 313.15 K; cofactor ATP

substrate: dATP


proof_lines: pH 8.0, 30°C, at saturating concentrations of MoO42-

proof_lines: pH 8.0, 30°C, at saturating concentrations of SO42-


organism: Penicillium duponti


organism: Pyropia yezoensis

assay_conditions_summary: cofactor ATP

proof_lines:
ATP in form of MgATP2-
less than


organism: Rattus norvegicus

proof_lines:
30°C, pH 8.0
30°C, pH 8.0, reaction with CrO42-
ATP in form of MgATP2-


organism: Rhodovulum sulfidophilum


organism: Saccharomyces cerevisiae

proof_lines:
pH 8.0, 30°C
ATP in form of MgATP2-


organism: Spinacia oleracea

substrate_name: Diphosphate; Adenylylsulfate

proof_lines: pH 8.0, 30°C, chloroplastic enzyme, reaction with MoO42-

proof_lines: pH 8.0, 30°C, cytosolic enzyme, reaction with MoO42-

substrate: Diphosphate; Adenylylsulfate


organism: Synechococcus sp.

substrate_name: adenosine 5'-phosphosulfate

substrate: adenosine 5'-phosphosulfate


organism: Zea mays


organism: Unknown


organism: Abies grandis

substrate_name: Isopentenyl diphosphate; Dimethylallyl diphosphate


organism: Bacillus subtilis

substrate_name: dimethylallyl diphosphate

substrate: dimethylallyl diphosphate


organism: Cucurbita sp.

substrate_name: Geranyl diphosphate; Isopentenyl diphosphate


substrate_name: isopentenyl diphosphate

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

proof_lines:
C73F mutant enzyme at 45°C
C73F mutant enzyme at 55°C

substrate: isopentenyl diphosphate


substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


proof_lines:
wild-type enzyme at 45°C
wild-type enzyme at 55°C


organism: Homo sapiens

substrate_name: Unknown

substrate: Unknown


organism: Leishmania major

proof_lines: pH and temperature not specified in the publication


organism: Mycobacterium tuberculosis


organism: Phaedon cochleariae

proof_lines: fixed substrate geranyl diphosphate (0.05 mM), pH and temperature not specified in the publication, metal cofactor: Co2+

proof_lines: fixed substrate isopentenyl diphosphate (0.05 mM), pH and temperature not specified in the publication, metal cofactor: Mg2+

proof_lines: fixed substrate geranyl diphosphate (0.05 mM), pH and temperature not specified in the publication, metal cofactor: Mg2+


organism: Anabaena cylindrica


organism: Archaeoglobus fulgidus


organism: Astragalus bisulcatus

assay_conditions_summary: pH 9


organism: Astragalus racemosus


organism: Astragalus sinicus


organism: Brassica capitata

proof_lines: pH 8.0, 30°C, synthesis of adenosine 5-phosphosulfate


organism: Desulfomicrobium sp.


enzyme_display_name: Cyclic di-GMP phosphodiesterase RocR

organism: Pseudomonas aeruginosa

substrate_name: cyclic di-3',5'-guanylate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature D296A to reconstruct the assayed variant sequence.

proof_lines: mutant RocR enzyme D296A, in 100 mM Tris buffer (pH 8.0) (23°C), 20 mM KCl, and 25 mM MgCl2

enzyme: Cyclic di-GMP phosphodiesterase RocR

substrate: cyclic di-3',5'-guanylate


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature Q161A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature Q372A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature Q372A/D318A to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 23°C, recombinant mutants Q372A and D318A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HX69 canonical sequence; variant reconstructed from selected mutation_signature after residue-coordinate check and applied mutation signature E268Q to reconstruct the assayed variant sequence.

proof_lines: mutant RocR enzyme E268Q, in 100 mM Tris buffer (pH 8.0) (23°C), 20 mM KCl, and 25 mM MgCl2