sequence_source: UniProt P09598 direct FASTA; variant reconstructed from mature-chain local mutation coordinates mapped to full-sequence positions by chain start 39.

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

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant Y56V


enzyme_display_name: phospholipase C

organism: Bacillus cereus

substrate_name: Phosphatidylcholine; H2O

km_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

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

sequence_variant_note: Resolved canonical sequence from UniProt P09598 direct FASTA; variant reconstructed from mature-chain local mutation coordinates mapped to full-sequence positions by chain start 39. and applied mutation signature E4K/Y56V with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant E4K/Y56V

enzyme: phospholipase C

substrate: Phosphatidylcholine; H2O


substrate_name: H2O; Phosphatidylcholine

sequence_variant_note: Mutation signature Y56T could not be applied safely because the resolved sequence does not match the expected reference residue(s).

mutation_type: substitution

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant Y56T

substrate: H2O; Phosphatidylcholine


sequence_variant_note: Resolved canonical sequence from UniProt P09598 direct FASTA; variant reconstructed from mature-chain local mutation coordinates mapped to full-sequence positions by chain start 39. and applied mutation signature E4P/Y56S/F66N with inferred residue-numbering offset +38 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant E4P/Y56S/F66N


organism: Listeria monocytogenes

source_db: brenda

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

source: brenda


organism: Plasmodium falciparum

substrate_name: sphingomyelin

kcat_display: Not reported

substrate: sphingomyelin


organism: Pseudomonas aeruginosa

substrate_name: p-Nitrophenylphosphorylcholine

substrate: p-Nitrophenylphosphorylcholine


organism: Rattus norvegicus

substrate_name: phosphatidylinositol 4,5-bisphosphate

proof_lines:
PLC-beta1a, 2mM free Ca2+
PLC-beta1b, 2mM free Ca2+

substrate: phosphatidylinositol 4,5-bisphosphate


organism: Streptomyces hachijoensis

substrate_name: phosphatidylcholine

substrate: phosphatidylcholine


organism: Tetrahymena pyriformis


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: triacetin

source_db: uniprot

verification_status: unverified

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

proof_lines: kcat is 581.2 sec(-1) for triacetin. kcat is 223.7 sec(-1) for tributyrin. kcat is 122.9 sec(-1) for tricaproin. kcat is 15.6 sec(-1) for tricaprylin. kcat is 501.8 sec(-1) for p-nitrophenyl acetate. kcat is 119.7 sec(-1) for p-nitrophenyl

substrate: triacetin

status: unverified

source: uniprot


sequence_source: UniProtKB REST P09598; reviewed Swiss-Prot PHLC_BACCE, Bacillus cereus phospholipase C, EC 3.1.4.3.

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

proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant E4G


proof_lines: SABIO-RK modifier species: phospholipase C(Enzyme) mutant E4Q


sequence_variant_note: Resolved canonical sequence from UniProtKB REST A0A7T1JQH0; unreviewed TrEMBL Bacillus cereus phospholipase C fragment, EC 3.1.4.3; F96 and Q153 checked directly before substitution. and applied mutation signature F96R/Q153P to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST A0A7T1JQH0; unreviewed TrEMBL Bacillus cereus phospholipase C fragment, EC 3.1.4.3.


substrate_name: Phosphatidylserine

source_db: oed

kcat_over_km_origin: calculated

data_origin: experimental

substrate: Phosphatidylserine

source: oed


substrate_name: Phosphatidylcholine

substrate: Phosphatidylcholine


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

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

proof_lines: pH and temperature not specified in the publication


substrate_name: phosphatidylethanolamine

substrate: phosphatidylethanolamine


organism: Homo sapiens

proof_lines:
Vmax 367 nmol/min mg
Vmax 463 nmol/min mg
Vmax 484 nmol/min mg


organism: Streptomyces sp. NA684


substrate_name: L-alpha-lysophosphatidylcholine

substrate: L-alpha-lysophosphatidylcholine


enzyme_display_name: diacylglycerol kinase (ATP)

organism: Arabidopsis thaliana

assay_conditions_summary: cofactor ATP

enzyme: diacylglycerol kinase (ATP)


substrate_name: ATP

substrate: ATP


organism: Dictyostelium discoideum

substrate_name: ATP (in the presence of 1,2-dioctanoyl-sn-glycerol)


organism: Escherichia coli (strain K12)


organism: Mus musculus

substrate_name: diacylglycerol

substrate: diacylglycerol


substrate_name: Unknown

substrate: Unknown


sequence_source: UniProtKB accession P34125 FASTA; direct REST check plus selected source accession evidence


organism: Drosophila melanogaster

substrate_name: ATP; 1,2-Diacyl-sn-glycerol

sequence_source: UniProtKB accession Q09103 FASTA resolved only as canonical context

proof_lines: SABIO-RK modifier species: diacylglycerol kinase(Enzyme) mutant K014/+

substrate: ATP; 1,2-Diacyl-sn-glycerol


organism: Sus scrofa

substrate_name: ATP (at pH 7.4)

assay_conditions_summary: pH 7.4; cofactor ATP

substrate: ATP (at pH 7.4)


enzyme_display_name: 4-dimethylallyltryptophan synthase

organism: Claviceps purpurea

substrate_name: L-tryptophan

sequence_source: UniProtKB M1WA41 direct lookup; reviewed Swiss-Prot entry DMAW_CLAP2

enzyme: 4-dimethylallyltryptophan synthase

substrate: L-tryptophan


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

substrate_name: dimethylallyl diphosphate

substrate: dimethylallyl diphosphate


organism: Claviceps fusiformis

substrate_name: dimethylallyl diphosphate (in metal-free EDTA buffer)


organism: Aspergillus fumigatus

sequence_source: UniProtKB Q50EL0 direct lookup plus accession reuse cache accession_48079d2e36550d03

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


substrate_name: L-Tryptophan

substrate: L-Tryptophan


substrate_name: L-o-tyrosine

substrate: L-o-tyrosine


substrate_name: L-m-tyrosine

substrate: L-m-tyrosine


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

assay_conditions_summary: pH 7.2; 298.15 K; cofactor ATP

proof_lines: N-terminally trucated protein, FLAG-tag, pH 7.2, 25°C


proof_lines: wild-type protein, FLAG-tag, pH 7.2, 25°C

proof_lines: wild-type protein with C-terminal His-tag, pH 7.2, 25°C


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines:
pH 7.0, 37°C, microsomal enzyme
pH 7.4, 30°C, enzyme form DGK IV
pH 7.0, 37°C, soluble enzyme


assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP


organism: Triticum aestivum


substrate_name: sn-1,2-Dioleoylglycerol; ATP

sequence_source: UniProtKB reviewed direct accession lookup: P23743 / DGKA_HUMAN

substrate: sn-1,2-Dioleoylglycerol; ATP


substrate_name: ATP; sn-1,2-Dioleoylglycerol

sequence_source: UniProtKB reviewed direct accession lookup: P49619 / DGKG_HUMAN

substrate: ATP; sn-1,2-Dioleoylglycerol


sequence_source: UniProtKB reviewed direct accession lookup: Q13574 / DGKZ_HUMAN


sequence_source: UniProtKB reviewed direct accession lookup: Q9ESW4 / AGK_MOUSE


sequence_source: UniProtKB reviewed direct accession lookup: P20192 / DGKA_PIG


organism: Escherichia coli


assay_conditions_summary: pH 6.9; 298.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB P0ABN1 with PMID 17722884 mutation context and applied mutation signature C46A/C113A/E28C with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0ABN1 with PMID 17722884 mutation context and applied mutation signature C46A/C113A/F31C with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0ABN1 with PMID 17722884 mutation context and applied mutation signature C46A/C113A/R32C with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0ABN1 with PMID 17722884 mutation context and applied mutation signature C46A/C113A/E34C with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: ADP

sequence_source: UniProtKB P0ABN1

assay_conditions_summary: pH 6.8; 303.15 K; cofactor ATP

proof_lines: about, pH 6.8, 30°C, reaction with sn-2,3-dihexanoylglycerol

substrate: ADP


organism: Gallus gallus

substrate_name: GTP

assay_conditions_summary: pH 6.6; 303.15 K; cofactor ATP

substrate: GTP


sequence_source: UniProtKB reviewed accession Q9FFN7

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


sequence_source: UniProtKB reviewed accession P34125


substrate_name: 1,2-Diacyl-sn-glycerol; ATP

sequence_source: UniProtKB reviewed accession Q09103

substrate: 1,2-Diacyl-sn-glycerol; ATP


sequence_source: UniProtKB reviewed accession Q09103 canonical sequence, retained as context only for unresolved variant


substrate_name: 1,2-Dipalmitoyl glycerol; ATP

sequence_source: UniProtKB reviewed accession P0ABN1

substrate: 1,2-Dipalmitoyl glycerol; ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P52429 canonical sequence, retained with unresolved P32A mutation annotation and applied mutation signature P32A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P52429


sequence_source: UniProtKB reviewed accession Q9Y6T7


organism: Catharanthus roseus


substrate_name: ATP

sequence_source: UniProtKB:P0ABN1 via lit_pubmed:10220339; variant reconstructed from P0ABN1 FT MUTAGEN position 15

sequence_variant_note: Mutation signature A14Q matches the mutant residue at offset +1 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ABN1 via lit_pubmed:10220339; variant reconstructed from P0ABN1 FT MUTAGEN position 73 and applied mutation signature N72S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0ABN1 via lit_pubmed:10220339; variant reconstructed from P0ABN1 FT MUTAGEN position 77

sequence_variant_note: Mutation signature E76L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


proof_lines:
wild-type enzyme
wild-type, pH 6.9, 25°C


sequence_source: UniProtKB:P0ABN1 via lit_pubmed:10220339; variant reconstructed from P0ABN1 FT MUTAGEN position 96

sequence_variant_note: Mutation signature D95N matches the mutant residue at offset +1 and the reference residue at offset -14; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


organism: Unknown


proof_lines: mutant E89Q, pH and temperature not specified in the publication


proof_lines: pH 8.0, 30°C, recombinant His-tagged 4-DMATS


organism: Claviceps sp.


proof_lines: 37°C, pH not specified in the publication

proof_lines: in 50 mM Tris/HCl (pH 7.5) with 5 mM CaCl2


proof_lines: mutant K174A, pH and temperature not specified in the publication


sequence_source: UniProtKB:Q50EL0 FASTA; RCSB 3I4X/3I4Z FgaPT2 structure cross-check

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


proof_lines: mutants K174Q and K175A, pH and temperature not specified in the publication


proof_lines: below, mutant E89A, pH and temperature not specified in the publication


proof_lines: mutant K174Q, pH and temperature not specified in the publication


substrate_name: L-Tryptophan; Dimethylallyl diphosphate

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 Q50EL0 direct lookup

proof_lines:
pH 7.5, 37°C
pH 7.5, 37°C, recombinant enzyme
Raw SKiD Env: Temp=37°C, pH=7.5

source_databases_merged: sabio_rk brenda skid

substrate: L-Tryptophan; Dimethylallyl diphosphate


substrate_name: cyclo-L-Trp-Gly

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q50EL0 direct lookup plus selected mutation_signature R244L and applied mutation signature R244L to reconstruct the assayed variant sequence.

substrate: cyclo-L-Trp-Gly


substrate_name: cyclo-L-Trp-L-Leu

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q50EL0 direct lookup plus selected mutation_signature R244Y and applied mutation signature R244Y to reconstruct the assayed variant sequence.

substrate: cyclo-L-Trp-L-Leu


substrate_name: cyclo-L-Trp-L-Trp

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q50EL0 direct lookup plus selected mutation_signature R244M and applied mutation signature R244M to reconstruct the assayed variant sequence.

substrate: cyclo-L-Trp-L-Trp


substrate_name: ardeemin fumiquinazoline

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

substrate: ardeemin fumiquinazoline


substrate_name: Dimethylallyl diphosphate; L-Tryptophan

sequence_source: UniProtKB Q12594 direct lookup

substrate: Dimethylallyl diphosphate; L-Tryptophan


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


organism: Malbranchea aurantiaca

substrate_name: L-tryptophan

sequence_source: UniProtKB B1A4C4 direct lookup

proof_lines:
presence of D-tryptophan, pH 7.4, 30°C
pH 7.4, 30°C

substrate: L-tryptophan


enzyme_display_name: inulinase

organism: Aspergillus niger

substrate_name: inulin

enzyme: inulinase

substrate: inulin


organism: Talaromyces purpureogenus

sequence_variant_note: Resolved canonical sequence from UniProtKB O00056 direct accession lookup and applied mutation signature Y128H to reconstruct the assayed variant sequence.


sequence_source: UniProtKB O00056 direct accession lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB O00056 direct accession lookup and applied mutation signature Y128H/E344K/T504M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y128H/A316T/E344K/T504M to reconstruct the assayed variant sequence.


enzyme_display_name: ceramidase

organism: Homo sapiens

substrate_name: D-erythro-C(6:0)-ceramide (at 37 degrees Celsius and pH 9.0)

assay_conditions_summary: pH 9

enzyme: ceramidase


proof_lines: pH 4.5, 37°C, recombinant AC expressed in CHO cells, 14C-labeled substrate

proof_lines: pH 4.5, 37°C, recombinant AC expressed in CHO cells, BODIPY-conjugated substrate


sequence_source: identity_reuse_cache accession_87f6aa3bf247ebde plus UniProt REST direct accession lookup for Q9NR71.


organism: Xanthomonas phaseoli pv. phaseoli

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


organism: Kluyveromyces marxianus

substrate_name: chicory inulin

proof_lines: native wild type enzyme, at pH 4.5 and 50°C

proof_lines: recombinant wild type enzyme, at pH 4.5 and 50°C

substrate: chicory inulin


substrate_name: agavin

sequence_variant_note: Resolved canonical sequence from UniProtKB:P28999 and applied mutation signature Q339A to reconstruct the assayed variant sequence.

substrate: agavin


sequence_variant_note: Resolved canonical sequence from UniProtKB:P28999 and applied mutation signature T235A to reconstruct the assayed variant sequence.


substrate_name: sucrose

sequence_variant_note: Resolved canonical sequence from UniProtKB:P28999 and applied mutation signature Q236A to reconstruct the assayed variant sequence.

substrate: sucrose


sequence_variant_note: Resolved canonical sequence from UniProtKB:P28999 and applied mutation signature F113A to reconstruct the assayed variant sequence.


proof_lines: pH 5.4, 55°C, recombinant untagged wild-type enzyme

proof_lines: pH 5.4, 55°C, recombinant MBP-tagged wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:O00056 and applied mutation signature Y128H/E344K/T504M to reconstruct the assayed variant sequence.

proof_lines: pH 5.4, 55°C, recombinant MBP-tagged mutant Y128H/E344K/T504M enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:O00056 and applied mutation signature Y128H/A316T/E344K/T504M to reconstruct the assayed variant sequence.

proof_lines: pH 5.4, 55°C, recombinant MBP-tagged mutant Y128H/A316T/E344K/T504M enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:O00056 canonical sequence; Y128H variant reconstructed from selected BRENDA mutation_signature and direct coordinate check. and applied mutation signature Y128H to reconstruct the assayed variant sequence.

proof_lines: pH 5.4, 55°C, recombinant MBP-tagged mutant Y128H enzyme


organism: Aspergillus terreus

assay_conditions_summary: pH 5

proof_lines:
at pH 5.0 and 30Â°C
at pH 5.0 and 55Â°C
at pH 5.0 and 50Â°C


organism: Bacillus smithii

substrate_name: raffinose

proof_lines: calculatedas fructose units released from inulin

substrate: raffinose


organism: Helianthus tuberosus

substrate_name: (2,1-beta-D-Fructosyl)n; H2O

substrate: (2,1-beta-D-Fructosyl)n; H2O


organism: Lipomyces starkeyi


organism: Penicillium sp.


organism: Pseudomonas mucidolens

proof_lines: Spy-Tag-fused enzyme, at pH 6.0 and 50°C


organism: Aspergillus ficuum

proof_lines:
endoinulinase I
endoinulinase III
endoinulinase II


organism: Aspergillus fumigatus


organism: Aspergillus neotritici

proof_lines:
at pH 5.5 and 55°C
at pH 5.5 and °C


proof_lines:
at pH 4.0 and 55°C
at pH 4.5 and 60°C
immobilized enzyme


organism: Aspergillus sp.


organism: Aspergillus tamarii


organism: Arthrobacter sp.


organism: Arthrobacter sp. S37

sequence_variant_note: Resolved canonical sequence from Reconstructed from NCBI Protein CAB63119.1; UniProt cross-reference Q9RBA5 and applied mutation signature D460A to reconstruct the assayed variant sequence.

proof_lines: mutant D460A, calculated as fructose units released from inulin


sequence_source: NCBI Protein CAB63119.1; UniProt cross-reference Q9RBA5

proof_lines: wild-type, calculated as fructose units released from inulin


sequence_variant_note: Resolved canonical sequence from Reconstructed from NCBI Protein CAB63119.1; UniProt cross-reference Q9RBA5 and applied mutation signature E519A to reconstruct the assayed variant sequence.

proof_lines: mutant E519A, calculated as fructose units released from inulin


sequence_variant_note: Resolved canonical sequence from Reconstructed from NCBI Protein CAB63119.1; UniProt cross-reference Q9RBA5 and applied mutation signature D460E to reconstruct the assayed variant sequence.

proof_lines: mutant D460E, calculated as fructose units released from inulin


sequence_variant_note: Resolved canonical sequence from Reconstructed from NCBI Protein CAB63119.1; UniProt cross-reference Q9RBA5 and applied mutation signature E323A to reconstruct the assayed variant sequence.

proof_lines: mutant E323A, calculated as fructose units released from inulin


organism: Rattus norvegicus

substrate_name: ceramide

substrate: ceramide


organism: Homo sapiens

substrate_name: N-palmitoylethanolamine

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

smiles: CCCCCCCCCCCCCCCC(=O)NCCO

substrate: N-palmitoylethanolamine


substrate_name: D-erythro-C12-NBD-ceramide (at 37 degrees Celsius and pH 7.5); N-octanoylsphing-4-enine (at 37 degrees Celsius and pH 7.0)


substrate_name: D-erythro-C(6:0)-ceramide (at 37 degrees Celsius and pH 9.0); D-erythro-C(12:0)-ceramide (at 37 degrees Celsius and pH 9.0); D-erythro-C(14:0)-ceramide (at 37 degrees Celsius and pH 9.0); D-erythro-C(16:0)-ceramide (at 37 degrees Celsius and pH 9.0); D-erythro-C(18:0)-ceramide (at 37 degrees Celsius and pH 9.0); D-erythro-C(18:1)-ceramide (at 37 degrees Celsius and pH 9.0); D-erythro-C(20:0)-ceramide (at 37 degrees Celsius and pH 9.0); D-erythro-C(20:1)-ceramide (at 37 degrees Celsius and pH 9.0); D-erythro-C(24:0)-ceramide (at 37 degrees Celsius and pH 9.0); D-erythro-C(24:1)-ceramide (at 37 degrees Celsius and pH 9.0)

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


substrate_name: N-dodecanoylsphing-4-enine (at 37 degrees Celsius and pH 4.2); N-dodecanoylsphing-4-enine (at 37 degrees Celsius and pH 4.5); sphingosine (at 37 degrees Celsius and pH 6.0); dodecanoate (at 37 degrees Celsius and pH 6.0); N-dodecanoylethanolamine (at 37 degrees Celsius and pH 4.5)


organism: Mus musculus


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: N-dodecanoyl-7-nitrobenz-2-oxa-1,3-4-diazole (NBD)-D-erythro-sphingosine (C12-NBD-Cer) (at pH 8 and at 37 degrees Celsius)

assay_conditions_summary: pH 8


enzyme_display_name: Neutral ceramidase

organism: Aspergillus oryzae RIB40

sequence_source: UniProtKB accession Q2UN98; direct REST accession lookup

enzyme: Neutral ceramidase


sequence_source: UniProtKB accession Q9NR71; direct REST accession lookup

proof_lines:
pH 7.0, 28°C, recombinant enzyme
pH 7.4, 37°C
pH 7.5, 37°C, recombinant enzyme


enzyme_display_name: Alkaline ceramidase 2

substrate_name: N-Hexanoyl-D-erythro-sphingosine; H2O

sequence_source: UniProtKB accession Q5QJU3; direct REST accession lookup

enzyme: Alkaline ceramidase 2

substrate: N-Hexanoyl-D-erythro-sphingosine; H2O


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

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: Alkaline ceramidase 3

sequence_variant_note: Resolved canonical sequence from UniProtKB accession Q9NUN7; direct REST accession lookup and applied mutation signature S77C to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, mutant enzyme S77C, i.e. D-ribo-C12-NBD-phytoceramide

enzyme: Alkaline ceramidase 3


sequence_variant_note: Resolved canonical sequence from UniProtKB accession Q9NUN7; direct REST accession lookup and applied mutation signature S77A to reconstruct the assayed variant sequence.

proof_lines: pH 9.4, 37°C, mutant enzyme S77A, i.e. D-ribo-C12-NBD-phytoceramide


sequence_source: UniProtKB accession Q9NUN7; direct REST accession lookup

proof_lines: pH 9.4, 37°C, wild-type enzyme, i.e. D-ribo-C12-NBD-phytoceramide


enzyme_display_name: Acid ceramidase

substrate_name: N-Dodecanoylsphingosine; H2O

sequence_source: UniProtKB accession Q13510; direct REST accession lookup

proof_lines: pH 4.5, 37°C, BODIPY-conjugated substrate

enzyme: Acid ceramidase

substrate: N-Dodecanoylsphingosine; H2O


organism: Camelus dromedarius


proof_lines: pH 4.5, 37°C, recombinant AC expressed in CHO cells, 14C-labeled substrate

proof_lines: pH 4.5, 37°C, recombinant AC expressed in CHO cells, BODIPY-conjugated substrate


organism: Mycobacterium tuberculosis


organism: Oryza sativa


organism: Pseudomonas aeruginosa


substrate_name: N-Acylsphingosine; H2O

sequence_source: UniProtKB reviewed accession Q9JHE3 direct lookup

substrate: N-Acylsphingosine; H2O


sequence_source: UniProtKB reviewed accession Q9WV54 direct lookup


substrate_name: Unknown

ki_unit: mM

sequence_source: UniProtKB reviewed accession Q9I596 direct lookup

substrate: Unknown


substrate_name: H2O; N-Palmitoylsphingosine

sequence_source: UniProtKB reviewed accession Q91XT9 direct lookup

substrate: H2O; N-Palmitoylsphingosine


organism: Oryza sativa subsp. japonica

substrate_name: D-erythro-C12-NBD-ceramide (at pH 5.7 and 37 degrees Celsius)


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

substrate_name: N-palmitoylsphingosine

substrate: N-palmitoylsphingosine


proof_lines: More efficiently hydrolyzes N-lauroylsphingosine/C12:0-ceramides compared to N-palmitoylsphingosine/C16:0-ceramides and N-stearoylsphingosine/C18:0-ceramides (PubMed:11328816). The catalytic efficiency towards dihydroceramides and phytocera


enzyme_display_name: alpha-N-acetylgalactosaminidase

organism: Elizabethkingia meningoseptica

substrate_name: Galalpha-pNP

enzyme: alpha-N-acetylgalactosaminidase

substrate: Galalpha-pNP


organism: Enterococcus faecalis

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q833V2 direct REST lookup; RCSB 7F7Q/7F7R SIFTS map the PMID 34826537 structures to Q833V2 and applied mutation signature W221N to reconstruct the assayed variant sequence.

status: corrected


organism: Phocaeicola vulgatus


enzyme_display_name: homoserine O-succinyltransferase

organism: Acinetobacter baylyi

substrate_name: Succinyl-CoA; L-Homoserine

assay_conditions_summary: cofactor CoA

enzyme: homoserine O-succinyltransferase

substrate: Succinyl-CoA; L-Homoserine


organism: Escherichia coli

smiles: NCCCO

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

column_label: Table 1 (Kinetic Parameters for the Reaction Catalyzed by Homoserine Transsuccinylase), substrate row '3-amino-1-propanol'; column 'KM (mM)' = 20; column 'kcat (s-1)' = 0.13; column 'kcat/KM (s-1 M-1)' = 6.7.

normalized_value_unit_evidence: Km: printed Table 1 cell 20 under the column head KM (mM); the column is already in millimolar, so no unit conversion applies and the paper value is 20.0 mM. kcat: printed Table 1 cell 0.13 under the column head kcat (s-1); the column is already per second, so no unit conversion applies and the paper value is 0.13 s^(-1). kcat/Km: Printed Table 1 kcat/KM cell 6.7 under the column head kcat/KM (s-1 M-1), that is 6.7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.7 / 1000 = 0.0067 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row '3-amino-1-propanol': KM = 20 mM; kcat = 0.13 s^-1; printed kcat/KM = 6.7 s^-1 M^-1.

table_label: Table 1: Kinetic Parameters for the Reaction Catalyzed by Homoserine Transsuccinylase (Biochemistry 1999, 38(43):14416-14423)


substrate_name: succinyl-CoA

verification_status: verified

column_label: Table 1 (Kinetic Parameters for the Reaction Catalyzed by Homoserine Transsuccinylase), substrate row 'succinyl-CoA'; column 'KM (mM)' = 0.17; column 'kcat (s-1)' = 24; column 'kcat/KM (s-1 M-1)' = 1.4 x 10^5.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.17 under the column head KM (mM); the column is already in millimolar, so no unit conversion applies and the paper value is 0.17 mM. kcat: printed Table 1 cell 24 under the column head kcat (s-1); the column is already per second, so no unit conversion applies and the paper value is 24.0 s^(-1). kcat/Km: Printed Table 1 kcat/KM cell 1.4 x 10^5 under the column head kcat/KM (s-1 M-1), that is 140000.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 140000.0 / 1000 = 140.0 s^-1 mM^-1. The catalog value 141.17647058823528 s^(-1)*mM^(-1) is the full-precision quotient 24.0 / 0.17 of the same two printed component cells, and that quotient re-expressed in the printed column's units is 141176.47058823527 M^-1 s^-1, which lies inside the rounding interval of the printed cell 1.4 x 10^5.

raw_value_unit_evidence: Table 1, substrate row 'succinyl-CoA': KM = 0.17 mM; kcat = 24 s^-1; printed kcat/KM = 1.4 x 10^5 s^-1 M^-1.

row_label: Table 1, substrate row 'succinyl-CoA'

substrate: succinyl-CoA

status: verified


substrate_name: L-Threonine

column_label: Table 1 (Kinetic Parameters for the Reaction Catalyzed by Homoserine Transsuccinylase), substrate row 'L-threonine'; column 'KM (mM)' = 31; column 'kcat (s-1)' = 0.015; column 'kcat/KM (s-1 M-1)' = 0.49.

normalized_value_unit_evidence: Km: printed Table 1 cell 31 under the column head KM (mM); the column is already in millimolar, so no unit conversion applies and the paper value is 31.0 mM. kcat: printed Table 1 cell 0.015 under the column head kcat (s-1); the column is already per second, so no unit conversion applies and the paper value is 0.015 s^(-1). kcat/Km: Printed Table 1 kcat/KM cell 0.49 under the column head kcat/KM (s-1 M-1), that is 0.49 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.49 / 1000 = 0.00049 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 'L-threonine': KM = 31 mM; kcat = 0.015 s^-1; printed kcat/KM = 0.49 s^-1 M^-1.

row_label: Table 1, substrate row 'L-threonine'

substrate: L-Threonine


substrate_name: glutaryl-CoA

column_label: Table 1 (Kinetic Parameters for the Reaction Catalyzed by Homoserine Transsuccinylase), substrate row 'glutaryl-CoA'; column 'KM (mM)' = 0.18; column 'kcat (s-1)' = 1.6; column 'kcat/KM (s-1 M-1)' = 8.9 x 10^3.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.18 under the column head KM (mM); the column is already in millimolar, so no unit conversion applies and the paper value is 0.18 mM. kcat: printed Table 1 cell 1.6 under the column head kcat (s-1); the column is already per second, so no unit conversion applies and the paper value is 1.6 s^(-1). kcat/Km: Printed Table 1 kcat/KM cell 8.9 x 10^3 under the column head kcat/KM (s-1 M-1), that is 8900.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8900.0 / 1000 = 8.9 s^-1 mM^-1. The catalog value 8.88888888888889 s^(-1)*mM^(-1) is the full-precision quotient 1.6 / 0.18 of the same two printed component cells, and that quotient re-expressed in the printed column's units is 8888.888888888889 M^-1 s^-1, which lies inside the rounding interval of the printed cell 8.9 x 10^3.

raw_value_unit_evidence: Table 1, substrate row 'glutaryl-CoA': KM = 0.18 mM; kcat = 1.6 s^-1; printed kcat/KM = 8.9 x 10^3 s^-1 M^-1.

row_label: Table 1, substrate row 'glutaryl-CoA'

substrate: glutaryl-CoA


substrate_name: L-Serine

column_label: Table 1 (Kinetic Parameters for the Reaction Catalyzed by Homoserine Transsuccinylase), substrate row 'L-serine'; column 'KM (mM)' = 25; column 'kcat (s-1)' = 0.023; column 'kcat/KM (s-1 M-1)' = 0.92.

normalized_value_unit_evidence: Km: printed Table 1 cell 25 under the column head KM (mM); the column is already in millimolar, so no unit conversion applies and the paper value is 25.0 mM. kcat: printed Table 1 cell 0.023 under the column head kcat (s-1); the column is already per second, so no unit conversion applies and the paper value is 0.023 s^(-1). kcat/Km: Printed Table 1 kcat/KM cell 0.92 under the column head kcat/KM (s-1 M-1), that is 0.92 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.92 / 1000 = 0.00092 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 'L-serine': KM = 25 mM; kcat = 0.023 s^-1; printed kcat/KM = 0.92 s^-1 M^-1.

row_label: Table 1, substrate row 'L-serine'

substrate: L-Serine


substrate_name: L-Homoserine

column_label: Table 1 (Kinetic Parameters for the Reaction Catalyzed by Homoserine Transsuccinylase), substrate row 'L-homoserine'; column 'KM (mM)' = 1.6; column 'kcat (s-1)' = 24; column 'kcat/KM (s-1 M-1)' = 1.5 x 10^4.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.6 under the column head KM (mM); the column is already in millimolar, so no unit conversion applies and the paper value is 1.6 mM. kcat: printed Table 1 cell 24 under the column head kcat (s-1); the column is already per second, so no unit conversion applies and the paper value is 24.0 s^(-1). kcat/Km: Printed Table 1 kcat/KM cell 1.5 x 10^4 under the column head kcat/KM (s-1 M-1), that is 15000.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 15000.0 / 1000 = 15.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 'L-homoserine': KM = 1.6 mM; kcat = 24 s^-1; printed kcat/KM = 1.5 x 10^4 s^-1 M^-1.

row_label: Table 1, substrate row 'L-homoserine'

substrate: L-Homoserine


substrate_name: O-Succinyl-L-homoserine

column_label: Table 1 (Kinetic Parameters for the Reaction Catalyzed by Homoserine Transsuccinylase), substrate row 'O-succinylhomoserine'; column 'KM (mM)' = 3.5; column 'kcat (s-1)' = 5.23; column 'kcat/KM (s-1 M-1)' = 1.5 x 10^3.

normalized_value_unit_evidence: Km: printed Table 1 cell 3.5 under the column head KM (mM); the column is already in millimolar, so no unit conversion applies and the paper value is 3.5 mM. kcat: printed Table 1 cell 5.23 under the column head kcat (s-1); the column is already per second, so no unit conversion applies and the paper value is 5.23 s^(-1). kcat/Km: Printed Table 1 kcat/KM cell 1.5 x 10^3 under the column head kcat/KM (s-1 M-1), that is 1500.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1500.0 / 1000 = 1.5 s^-1 mM^-1. The catalog value 1.4942857142857144 s^(-1)*mM^(-1) is the full-precision quotient 5.23 / 3.5 of the same two printed component cells, and that quotient re-expressed in the printed column's units is 1494.2857142857144 M^-1 s^-1, which lies inside the rounding interval of the printed cell 1.5 x 10^3.

raw_value_unit_evidence: Table 1, substrate row 'O-succinylhomoserine': KM = 3.5 mM; kcat = 5.23 s^-1; printed kcat/KM = 1.5 x 10^3 s^-1 M^-1.

substrate: O-Succinyl-L-homoserine


substrate_name: Coenzyme A

column_label: Table 1 (Kinetic Parameters for the Reaction Catalyzed by Homoserine Transsuccinylase), substrate row 'coenzyme A'; column 'KM (mM)' = 0.64; column 'kcat (s-1)' = 5.23; column 'kcat/KM (s-1 M-1)' = 8.2 x 10^3.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.64 under the column head KM (mM); the column is already in millimolar, so no unit conversion applies and the paper value is 0.64 mM. kcat: printed Table 1 cell 5.23 under the column head kcat (s-1); the column is already per second, so no unit conversion applies and the paper value is 5.23 s^(-1). kcat/Km: Printed Table 1 kcat/KM cell 8.2 x 10^3 under the column head kcat/KM (s-1 M-1), that is 8200.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8200.0 / 1000 = 8.2 s^-1 mM^-1. The catalog value 8.171875 s^(-1)*mM^(-1) is the full-precision quotient 5.23 / 0.64 of the same two printed component cells, and that quotient re-expressed in the printed column's units is 8171.875 M^-1 s^-1, which lies inside the rounding interval of the printed cell 8.2 x 10^3.

raw_value_unit_evidence: Table 1, substrate row 'coenzyme A': KM = 0.64 mM; kcat = 5.23 s^-1; printed kcat/KM = 8.2 x 10^3 s^-1 M^-1.

row_label: Table 1, substrate row 'coenzyme A'

substrate: Coenzyme A


substrate_name: D-Homoserine

column_label: Table 1 (Kinetic Parameters for the Reaction Catalyzed by Homoserine Transsuccinylase), substrate row 'D-homoserine'; column 'KM (mM)' = 10; column 'kcat (s-1)' = 12; column 'kcat/KM (s-1 M-1)' = 1.2 x 10^3.

normalized_value_unit_evidence: Km: printed Table 1 cell 10 under the column head KM (mM); the column is already in millimolar, so no unit conversion applies and the paper value is 10.0 mM. kcat: printed Table 1 cell 12 under the column head kcat (s-1); the column is already per second, so no unit conversion applies and the paper value is 12.0 s^(-1). kcat/Km: Printed Table 1 kcat/KM cell 1.2 x 10^3 under the column head kcat/KM (s-1 M-1), that is 1200.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1200.0 / 1000 = 1.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row 'D-homoserine': KM = 10 mM; kcat = 12 s^-1; printed kcat/KM = 1.2 x 10^3 s^-1 M^-1.

row_label: Table 1, substrate row 'D-homoserine'

substrate: D-Homoserine


sequence_variant_note: Resolved canonical sequence from direct_uniprot_rest:P07623 and applied mutation signature I124L to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant I124L, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from direct_uniprot_rest:P07623 and applied mutation signature I229Y to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant I229Y, pH and temperature not specified in the publication


substrate_name: L-homoserine

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

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

substrate: L-homoserine


sequence_variant_note: Resolved canonical sequence from direct_uniprot_rest:P07623 and applied mutation signature T242A to reconstruct the assayed variant sequence.


organism: Haemophilus influenzae

substrate_name: L-Homoserine; Succinyl-CoA

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

proof_lines: SABIO-RK modifier species: homoserine O-succinyltransferase(Enzyme) mutant MetX L306R

substrate: L-Homoserine; Succinyl-CoA


organism: Aspergillus niger


organism: Bacteroides caccae

sequence_source: UniProtKB:I9PNY0 direct REST lookup 2026-06-09

proof_lines:
pH 7.0, 37°C
pH 7.0, 37°C, full-length enzyme


substrate_name: GalNAc-alpha-pNP

sequence_source: UniProtKB:I9PNY0 direct REST lookup 2026-06-09 plus source-note C-terminal truncation reconstruction

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

mutation_type: truncation

proof_lines: pH 7.0, 37°C, truncated enzyme missing 337 amino acids at the C-terminus

substrate: GalNAc-alpha-pNP


organism: Clostridium perfringens

sequence_source: UniProtKB:I1SB20 direct REST lookup 2026-06-09


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q833V2 direct REST lookup 2026-06-09 plus source-note substitution reconstruction and applied mutation signature D508N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q833V2 direct REST lookup 2026-06-09 plus source-note substitution reconstruction and applied mutation signature Y386A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q833V2 direct REST lookup 2026-06-09 plus source-note substitution reconstruction and applied mutation signature W570A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q833V2 direct REST lookup 2026-06-09 plus source-note substitution reconstruction and applied mutation signature W221N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WJY9 direct REST lookup on 2026-06-09; row-specific variant reconstructed only after canonical residue checks. and applied mutation signature L322R to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, homoserine O-succinyltransferase activity, mutant enzyme L322R


proof_lines: pH 7.5, 25°C, homoserine O-succinyltransferase activity, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q833V2 direct accession lookup and applied mutation signature Y386F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q833V2 direct accession lookup and applied mutation signature L492R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q833V2 direct accession lookup and applied mutation signature I542F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q833V2 direct accession lookup and applied mutation signature D455A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q833V2 direct accession lookup

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q833V2 direct accession lookup and applied mutation signature V456A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q833V2 direct accession lookup and applied mutation signature D455N to reconstruct the assayed variant sequence.


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from UniProtKB:P17050 direct accession lookup and applied mutation signature N201Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 4.5; 310.15 K; buffer 100 mM citrate/phosphate


organism: Todarodes pacificus

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

proof_lines:
isoenzyme I
isoenzyme II


organism: Spirosoma linguale

sequence_source: UniProtKB:D2QUW2 live REST/FASTA lookup on 2026-06-09; entry version 58, sequence version 1.

proof_lines:
pH 7.0, 20°C, steady state kinetics
pH 7.0, 40°C, steady state kinetics
pH 7.0, 45°C, steady state kinetics


organism: Asterina amurensis

proof_lines: pH 4.2, 37°C, isozyme alpha-GalNAcase II


enzyme_display_name: nicotinamide phosphoribosyltransferase

organism: Mus musculus

substrate_name: nicotinamide

enzyme: nicotinamide phosphoribosyltransferase

substrate: nicotinamide


sequence_source: UniProtKB Q99KQ4 FASTA direct lookup on 2026-06-09.


sequence_source: UniProtKB A2QL72 FASTA direct lookup on 2026-06-09; EC/function conflict retained for manual arbitration.

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


organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)


organism: Escherichia coli (strain K12)

normalized_value_unit_evidence: Km: printed Table 1 cell 0.17 under the column head KM (mM); the column is already in millimolar, so no unit conversion applies and the paper value is 0.17 mM. kcat: printed Table 1 cell 24 under the column head kcat (s-1); the column is already per second, so no unit conversion applies and the paper value is 24.0 s^(-1). kcat/Km: the catalog carries no catalytic-efficiency value on this row, so no efficiency value is exported here; the paper's own printed cell for the row is 1.4 x 10^5 s^-1 M^-1, recorded as the row's typed ratio provenance.


proof_lines: kcat is 0.12 sec(-1) with nicotinamide as substrate. kcat is 0.020 sec(-1) with nicotinate as substrate.


organism: Xanthomonas campestris pv. campestris (strain 8004)

proof_lines: kcat is 1.84 sec(-1) with nicotinamide as substrate. kcat is 6.99 sec(-1) with 5-phospho-alpha-D-ribose 1-diphosphate as substrate. kcat is 4.40 sec(-1) with ATP as substrate.


proof_lines: dissociation constant of enzyme-substrate-inhibitor complex


assay_conditions_summary: pH 7.2; 298.15 K; cofactor CoA


proof_lines: pH 7.2, 25°C, recombinant wild-type enzyme

proof_lines: pH 7.5, 25°C, recombinant wild-type enzyme


proof_lines: pH 7.2, 25°C, recombinant mutant K46R/K47R


organism: Acremonium sp.


organism: Arenibacter latericius


organism: Bos taurus

substrate_name: phenyl-alpha-N-acetylglucosaminide

substrate: phenyl-alpha-N-acetylglucosaminide


proof_lines:
pH 6.5, 37°C, recombinant enzyme
pH 7.0, 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P07623/METAS_ECOLI, cross-checked against PMID 17442255 mutagenesis scope. and applied mutation signature R193A/E246A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, recombinant mutant R193A/E246A


sequence_variant_note: Resolved canonical sequence from UniProtKB P07623/METAS_ECOLI, cross-checked against PMID 17442255 mutagenesis scope. and applied mutation signature E237A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07623/METAS_ECOLI, cross-checked against PMID 17442255 mutagenesis scope. and applied mutation signature K46L to reconstruct the assayed variant sequence.


organism: Mycobacterium tuberculosis

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


organism: Elizabethkingia meningoseptica


organism: Gallus gallus


proof_lines: enzyme from HIV patient serum, at pH 6.1


organism: Human immunodeficiency virus 1

substrate_name: serum vitamin D3-binding protein

substrate: serum vitamin D3-binding protein


organism: Katsuwonus pelamis

substrate_name: ovine submaxillary asialoglycoprotein

substrate: ovine submaxillary asialoglycoprotein


organism: Patella vulgata


organism: [Ruminococcus] torques


organism: Solenocera melantho


organism: Sus scrofa


organism: Escherichia coli


proof_lines: pH 7.5, 25°C, recombinant mutant Y238F/E246A


organism: Homo sapiens

sequence_source: UniProtKB:P17050 direct accession lookup


proof_lines:
pH 5.2, 37°C
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=37°C, pH=5.2


organism: Phocaeicola plebeius

sequence_source: UniProtKB:B5CUU2 direct accession lookup

proof_lines:
pH 7.0, 37°C
pH 7.0, 37°C, full-length enzyme


sequence_source: UniProtKB:B5CUU2 canonical sequence context only

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

proof_lines: pH 7.0, 37°C, truncated mutant enzyme D465S missing 329 amino acids at the C-terminus


proof_lines: pH 7.0, 37°C, truncated enzyme missing 329 amino acids at the C-terminus


proof_lines: pH 7.0, 37°C, truncated mutant enzyme D465A missing 329 amino acids at the C-terminus


proof_lines: pH 7.0, 37°C, truncated mutant enzyme D465G missing 329 amino acids at the C-terminus


organism: Phocaeicola vulgatus

sequence_source: UniProtKB:I9J6R7 direct accession lookup


enzyme_display_name: iodotyrosine deiodinase

organism: Danio rerio

substrate_name: diiodotyrosine (L-DIT)

proof_lines: kcat 4.1 min(-1) for the deiodination of diiodotyrosine (L-DIT).

enzyme: iodotyrosine deiodinase

substrate: diiodotyrosine (L-DIT)


organism: Daphnia pulex

proof_lines: Kcat 17.6 min(-1) for the deiodination of diiodotyrosine (L-DIT).


organism: Drosophila melanogaster

proof_lines: kcat is 12 sec(-1) for the dehalogenation of 3-iodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) (PubMed:27643701). kcat is 6.9 sec(-1) for the dehalogenation of 3-bromo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) (PubMed:27643701). kcat


organism: Haliscomenobacter hydrossis (strain ATCC 27775 / DSM 1100 / LMG 10767 / O)

proof_lines: kcat 0.09 sec(-1) for the deiodination of 3,5-diiodo-L-tyrosine (PubMed:24153409). kcat is 0.27 sec(-1) for the dehalogenation of 3-iodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) (PubMed:28157283). kcat is 0.0029 sec(-1) for the dehalog


substrate_name: L-DIT

proof_lines: kcat is 0.102 sec(-1) for the dehalogenation of 3-iodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) (PubMed:28157283). kcat is 0.004 sec(-1) for the dehalogenation of 2-iodophenol (at pH 7.4 and 25 degrees Celsius) (PubMed:28157283).

substrate: L-DIT


organism: Hydra vulgaris

proof_lines: Kcat 14 min(-1) for the deiodination of diiodotyrosine (L-DIT).


organism: Bos taurus

substrate_name: NADPH; H+; 3,5-Diiodo-L-tyrosine

sequence_source: UniProtKB REST direct accession check

substrate: NADPH; H+; 3,5-Diiodo-L-tyrosine


assay_conditions_summary: pH 7.6; cofactor FMN

proof_lines: pH 7.6, temperature not specified in the publication, recombinant enzyme


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines:
without ATP, pH 7.5, 37°C
with 1 mM ATP, pH 7.5, 37°C
free enzyme


organism: Mus musculus


organism: Rattus norvegicus

assay_conditions_summary: cofactor ATP

proof_lines:
in the absence of ATP
in the presence of ATP


sequence_source: UniProtKB reviewed accession Q99KQ4 (NAMPT_MOUSE), direct REST/FASTA check

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


sequence_source: UniProtKB reviewed accession Q80Z29 (NAMPT_RAT), direct REST/FASTA check


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

sequence_variant_note: Resolved canonical sequence from UniProtKB P43490 canonical sequence with row-specific mutation reconstruction from PMID 35120922 and applied mutation signature K68S/K71S to reconstruct the assayed variant sequence.

proof_lines: Km below 0.0001 mM, mutant enzyme K68S/K71S, at pH 7.5, temperature not specified in the publication

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


sequence_source: UniProtKB P43490 canonical sequence with row-specific mutation reconstruction from PMID 35120922

proof_lines: Km below 0.0001 mM, wild type enzyme, at pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P43490 canonical sequence with row-specific mutation reconstruction from PMID 35120922 and applied mutation signature K42A/K43A/K48A/R50A/K51A to reconstruct the assayed variant sequence.

proof_lines: Km below 0.0001 mM, mutant enzyme K42A/K43A/K48A/R50A/K51A, at pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P43490 canonical sequence with row-specific mutation reconstruction from PMID 35120922 and applied mutation signature K68A/K71A/K73A to reconstruct the assayed variant sequence.

proof_lines: Km below 0.0001 mM, mutant enzyme K68A/K71A/K73A, at pH 7.5, temperature not specified in the publication


sequence_variant_note: Mutation signature ΔK42 could not be applied safely because the resolved sequence does not match the expected reference residue(s).

mutation_type: deletion

proof_lines: kinetic parameter for the second phase, biphasic mutant enzyme DELTAK42-51, at pH 7.5, temperature not specified in the publication

proof_lines: kinetic parameter for the sexond phase, biphasic mutant enzyme DELTAK42-51, at pH 7.5, temperature not specified in the publication

proof_lines: Km below 0.0001 mM, kinetic parameter for the first phase, biphasic mutant enzyme DELTAK42-51, at pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB P43490 canonical sequence with row-specific mutation reconstruction from PMID 35120922 and applied mutation signature K42A/K48A to reconstruct the assayed variant sequence.

proof_lines: Km below 0.0001 mM, mutant enzyme K42A/K48A, at pH 7.5, temperature not specified in the publication


proof_lines: in the presence of NP-A1S, at pH 7.5 and 25°C


proof_lines: in the presence of NP-A1R, at pH 7.5 and 25°C


sequence_source: UniProtKB:P43490 reviewed Swiss-Prot NAMPT_HUMAN; sequence version 1; checked 2026-06-09

assay_conditions_summary: pH 7.5; 297.15 K; cofactor ATP

proof_lines: +/-0.00002, in presence of 2 mM phosphate, KM/kcat = 6100 1/M*s, pH 7.5, 100 microM PRPP, 88 nM NAMPT

proof_lines: +/-0.00150, in presence of 2 mM ATP the catalytic efficiency (KM/kcat = 1800000 1/M*s) is improved 1100-fold, pH 7.5, 100 microM PRPP, 88 nM NAMPT

proof_lines: ATPase activity in presence of 1 mM imidodiphosphate (PNP) is higher than in presence of pyophosphate, 2 mM ATP


organism: Nematostella vectensis

sequence_source: source_record; UniProt A7S5D9 direct check

proof_lines: Kcat 32 min(-1) for the deiodination of diiodotyrosine (L-DIT).


organism: Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E)

sequence_source: source_record; UniProt B9K712 direct check

proof_lines: kcat is 1.6 min(-1) for the dehalogenation of 3-iodo-L-tyrosine (at pH 7.4 and 25 degrees Celsius) (PubMed:34748729). kcat is 27 min(-1) for the dehalogenation of 3-iodo-L-tyrosine (at pH 7.4 and 60 degrees Celsius) (PubMed:34748729). kcat


enzyme_display_name: deoxyadenosine kinase

substrate_name: ATP; Deoxyadenosine

proof_lines:
pH 7.5, 37°C
pH 7.5, 37°C, substrate deoxyadenosine
pH 7.5, 37°C, substrate ribavirin

enzyme: deoxyadenosine kinase

substrate: ATP; Deoxyadenosine


organism: Staphylococcus aureus

substrate_name: Deoxyadenosine; ATP

sequence_source: UniProtKB REST accession Q0H0H0 checked 2026-06-09

assay_conditions_summary: pH 8; cofactor ATP

substrate: Deoxyadenosine; ATP


organism: Dictyostelium discoideum

substrate_name: thymidine

proof_lines: Catalytic efficiency is 100-fold higher for deoxyadenosine than for thymidine.

substrate: thymidine


organism: Gallus gallus

substrate_name: deoxyguanosine

proof_lines: kcat is 0.67 sec(-1) with deoxyguanosine as substrate. kcat is 0.52 sec(-1) with deoxycytidine as substrate. kcat is 2.56 sec(-1) with deoxyadenosine as substrate. kcat is 0.53 sec(-1) with deoxyuridine as substrate. kcat is 0.26 sec(-1) wi

substrate: deoxyguanosine


substrate_name: deoxycytidine

proof_lines: kcat is 0.05 sec(-1) with deoxycytodine as substrate. kcat is 4.07 sec(-1) with deoxyadenosine as substrate. kcat is 1.23 sec(-1) with deoxyguanosine as substrate. kcat is 1.05 sec(-1) with deoxyuridine as substrate. kcat is 1.08 sec(-1) wi

substrate: deoxycytidine


organism: Xenopus laevis

proof_lines: kcat is 0.09 sec(-1) with deoxycytodine as substrate. kcat is 3.40 sec(-1) with deoxyguanosine as substrate. kcat is 2.73 sec(-1) with deoxyadenosine as substrate. kcat is 0.29 sec(-1) with deoxythymidine as substrate. kcat is 1.27 sec(-1)


proof_lines: kcat is 1.26 sec(-1) with deoxyguanosine as substrate. kcat is 4.87 sec(-1) with deoxyadenosine as substrate. kcat is 0.42 sec(-1) with deoxycytidine as substrate. kcat is 0.36 sec(-1) with deoxyuridine as substrate. kcat is 0.14 sec(-1) wi


substrate_name: deoxyadenosine

sequence_source: UniProt Q3MHR2 direct EC 2.7.1.76 plus organism Bos taurus lookup

substrate: deoxyadenosine


substrate_name: 2'-fluoro-arabinosyl adenine

sequence_source: UniProt Q54YL2 direct EC 2.7.1.76 plus organism Dictyostelium discoideum lookup

substrate: 2'-fluoro-arabinosyl adenine


organism: Homo sapiens

proof_lines:
pH 7.5, 37°C, with deoxyadenosine
pH 7.4, 37°C, CCRF-CEM leukemia cells
pH 7.4, 37°C, erythrocyte


organism: Lactobacillus acidophilus

sequence_source: UniProt P0C1F9 direct EC 2.7.1.76 plus organism Lactobacillus acidophilus lookup


proof_lines: SABIO-RK modifier species: deoxyadenosine kinase(Enzyme) mutant R79K:dGK


organism: Mycoplasma mycoides

substrate_name: ATP

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines: with CTP as phosphoryl donor, at room temperature in 0.01 M HEPES (pH 7.4) containing 0.15 M NaCl and 0.002 M MgCl2

proof_lines: with ATP as phosphoryl donor, at room temperature in 0.01 M HEPES (pH 7.4) containing 0.15 M NaCl and 0.002 M MgCl2

substrate: ATP


sequence_source: UniProtKB reviewed accession P0C1F9

assay_conditions_summary: pH 8; 293.15 K; cofactor ATP

proof_lines:
ATP in form of MgATP2-
pH 8.0, 20°C, recombinant dAK
pH 8.0, 20°C, competitive vs. ATP


organism: Lactobacillus johnsonii

sequence_source: UniProtKB reviewed accession Q74HC3, selected from source bundle Q74HC2 Q74HC3 Q74HC2


substrate_name: CTP

sequence_source: UniProtKB unreviewed accession Q93IG4

substrate: CTP


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


substrate_name: dTTP

substrate: dTTP


substrate_name: UTP

substrate: UTP


organism: Bacillus subtilis (strain 168)

substrate_name: deoxyadenosine (with GTP at pH 8.5 and at 37 degrees Celsius)


substrate_name: deoxycytidine (dC)

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

substrate: deoxycytidine (dC)


organism: Bacillus cereus

sequence_source: UniProtKB REST accession Q0H0H5 (TrEMBL)

proof_lines: in 50 mM Tris/HCl, pH 8.0, 10 mM dithiothreitol, 2.5 mM ATP, 2.5 mM MgCl2, 3 mg/ml of bovine serum albumin and 0.5 mM CHAPS


organism: Bacillus subtilis

substrate_name: Deoxyadenosine; GTP

sequence_source: UniProtKB REST accession P37529 (reviewed Swiss-Prot)

substrate: Deoxyadenosine; GTP


sequence_source: UniProtKB REST accession Q54YL2 (reviewed Swiss-Prot)


substrate_name: fludarabine

substrate: fludarabine


sequence: MIVLSGPIGAGKSSLTGLLAEYLGTNPF

wild_type_sequence: MIVLSGPIGAGKSSLTGLLAEYLGTNPF

sequence_source: UniProtKB REST accession Q7M0X4 returns a TrEMBL fragment sequence only


sequence_source: UniProtKB REST accession P0C1F9 (reviewed Swiss-Prot canonical sequence)

proof_lines:
pH 8.0, 20°C, R79K:dGK mutant dAK
pH 8.0, 20°C, R79K mutant dAK


substrate_name: NADPH; H+; 3,5-Diiodo-L-tyrosine

sequence_source: UniProtKB A7MBC8 direct lookup

assay_conditions_summary: cofactor NADPH


organism: Drosophila melanogaster

sequence_source: UniProtKB E1JIB2 direct lookup

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


organism: Haliscomenobacter hydrossis

substrate_name: hhIYD-FMN; 3-Iodo-L-tyrosine

sequence_source: UniProtKB F4KU78 direct lookup

unit: M

substrate: hhIYD-FMN; 3-Iodo-L-tyrosine


sequence_source: UniProtKB Q6PHW0 direct lookup

proof_lines: pH 7.6, temperature not specified in the publication, recombinant enzyme

substrate: NADPH; H+; 3,5-Diiodo-L-tyrosine


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

proof_lines: pH and temperature not specified in the publication

source_databases_merged: brenda skid


substrate_name: NADPH; H+; 3-Iodo-L-tyrosine

mutation_signature: Δ2

sequence_source: UniProtKB Q6PHW0 direct lookup for canonical sequence only

proof_lines: SABIO-RK modifier species: iodotyrosine deiodinase(Enzyme) wildtype delta2-31, C-terminal His-tag

substrate: NADPH; H+; 3-Iodo-L-tyrosine


sequence_variant_note: Resolved canonical sequence from UniProtKB Q6PHW0 direct lookup plus explicit T239S reconstruction and applied mutation signature T239S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T239S, pH and temperature not specified in the publication


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

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


organism: Bos taurus


organism: Danio rerio

sequence_source: UniProtKB reviewed Swiss-Prot E7FDV5/IYD_DANRE; direct EC 1.21.1.1 plus Danio rerio lookup fetched 2026-06-09.

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


organism: Daphnia pulex

sequence_source: UniProtKB reviewed Swiss-Prot E9FR69/IYD_DAPPU; direct EC 1.21.1.1 plus Daphnia pulex lookup fetched 2026-06-09.


sequence_source: UniProtKB reviewed Swiss-Prot F4KU78/IYD_HALH1; direct EC 1.21.1.1 plus Haliscomenobacter hydrossis lookup fetched 2026-06-09.


organism: Hydra vulgaris

sequence_source: UniProtKB reviewed Swiss-Prot T2MBC4/IYD_HYDVU; direct EC 1.21.1.1 plus Hydra vulgaris lookup fetched 2026-06-09.


organism: Rattus norvegicus

sequence_source: UniProtKB reviewed Swiss-Prot Q5BK17/IYD1_RAT; direct EC 1.21.1.1 plus Rattus norvegicus lookup fetched 2026-06-09.

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

proof_lines:
method NADPH oxidation, pH 7.4, 37°C
method 125I release, pH 7.4, 37°C


enzyme_display_name: thiosulfate sulfurtransferase

substrate_name: thiosulfate

sequence_variant_note: Resolved canonical sequence from UniProtKB P97532 canonical sequence reconstructed with PMID 8910318 paper-numbered mutation offset +1 and applied mutation signature S249K with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

enzyme: thiosulfate sulfurtransferase

substrate: thiosulfate


substrate_name: Cyanide; Thiosulfate

sequence_source: UniProtKB P97532 canonical sequence reconstructed with PMID 8910318 paper-numbered mutation offset +1

sequence_variant_note: Mutation signature R196G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: thiosulfate sulfurtransferase(Enzyme) mutant R196G

substrate: Cyanide; Thiosulfate


substrate_name: Thiosulfate; Cyanide

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

proof_lines: SABIO-RK modifier species: thiosulfate sulfurtransferase(Enzyme) mutant R187G

substrate: Thiosulfate; Cyanide


sequence_variant_note: Resolved canonical sequence from UniProtKB P97532 canonical sequence reconstructed with PMID 8910318 paper-numbered mutation offset +1 and applied mutation signature S249A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiosulfate sulfurtransferase(Enzyme) mutant S249A


sequence_variant_note: Resolved canonical sequence from UniProtKB P97532 canonical sequence reconstructed with PMID 8910318 paper-numbered mutation offset +1 and applied mutation signature G248R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiosulfate sulfurtransferase(Enzyme) mutant G248R


proof_lines: SABIO-RK modifier species: thiosulfate sulfurtransferase(Enzyme) mutant S249K


sequence_source: UniProtKB P97532 reviewed Swiss-Prot FASTA, fetched 2026-06-09


sequence_source: UniProtKB P24329 reviewed Swiss-Prot FASTA, fetched 2026-06-09


sequence_variant_note: Resolved canonical sequence from UniProtKB P24329 canonical FASTA plus UniProt mutagenesis features R249G and K250S from PMID 7608189, fetched 2026-06-09 and applied mutation signature R248G/K249S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P24329 canonical FASTA plus UniProt mutagenesis feature K250S from PMID 7608189, fetched 2026-06-09

sequence_variant_note: Mutation signature K249S could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB P24329 canonical FASTA plus UniProt mutagenesis features R249G and K250S from PMID 7608189, fetched 2026-06-09

proof_lines: SABIO-RK modifier species: thiosulfate sulfurtransferase(Enzyme) mutant R248G K249S


proof_lines: SABIO-RK modifier species: thiosulfate sulfurtransferase(Enzyme) mutant K249S


sequence_variant_note: Resolved canonical sequence from UniProtKB P97532 canonical FASTA plus UniProt mutagenesis feature S250A from PMID 8910318, fetched 2026-06-09 and applied mutation signature S249A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


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


substrate_name: cyanide

proof_lines:
37°C, pH 7.4
cosubstrate cyanide, 37°C, pH 7.4
cosubstrate thioredoxin, 37°C, pH 7.4

substrate: cyanide


smiles: C#N


organism: Mus musculus

sequence_source: UniProtKB reviewed accession P52196 FASTA, THTR_MOUSE, direct REST lookup on 2026-06-09


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB reviewed accession P9WHF9 FASTA, THTR_MYCTU, direct REST lookup on 2026-06-09


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed accession P24329 FASTA using PubMed 7608189 UniProt mutagenesis feature R249G; selected source labels the same variant as R248G and applied mutation signature R248G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiosulfate sulfurtransferase(Enzyme) mutant R248G


sequence_source: UniProtKB reviewed accession P24329 FASTA, THTR_RAT, direct REST lookup on 2026-06-09


sequence_source: Reconstructed from UniProtKB reviewed accession P24329 FASTA using PubMed 7608189 UniProt mutagenesis feature R249G; selected source labels the same variant as R248G


organism: Unknown


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from UniProtKB Q6PHW0 direct lookup on 2026-06-09 plus selected-batch mutation signature T239A applied after residue-coordinate validation. and applied mutation signature T239A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T239A, pH and temperature not specified in the publication


substrate_name: 3-iodo-L-tyrosine; 2-iodophenol

sequence_variant_note: Resolved canonical sequence from UniProtKB Q6PHW0 direct lookup on 2026-06-09 plus selected-batch mutation signature E158Y/M162A applied after residue-coordinate validation. and applied mutation signature E158Y/M162A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E158Y/M162A, at pH 7.4 and 25°C

substrate: 3-iodo-L-tyrosine; 2-iodophenol


substrate_name: 2-iodophenol; 3-iodo-L-tyrosine

sequence_variant_note: Resolved canonical sequence from UniProtKB Q6PHW0 direct lookup on 2026-06-09 plus selected-batch mutation signature E157D/E158Y/M162A applied after residue-coordinate validation. and applied mutation signature E157D/E158Y/M162A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E157D/E158Y/M162A , at pH 7.4 and 25°C

substrate: 2-iodophenol; 3-iodo-L-tyrosine


sequence_variant_note: Resolved canonical sequence from UniProtKB Q6PHW0 direct lookup on 2026-06-09 plus selected-batch multi-substitution signature applied after residue-coordinate validation. and applied mutation signature E157S/E158Y/I159E/Y161W/M162A/K163R/M165F/H167D/R168E/T171E/R177N/T178L/N179D/I181R/K182H to reconstruct the assayed variant sequence.


source_db: brenda; skid

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH

proof_lines: enzyme expressed in Escherichia coli and lacking the transmembrane domain, pH not specified in the publication, temperature not specified in the publication

proof_lines: enzyme expressed in Pichia pastoris, pH not specified in the publication, temperature not specified in the publication

source: brenda; skid


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 Y157F, expressed in Escherichia coli and lacking the transmembrane domain, pH not specified in the publication, temperature not specified in the publication


organism: Arabidopsis thaliana

sequence_source: UniProtKB Q24JL3 direct lookup on 2026-06-09.


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


organism: Escherichia coli (strain K12)

substrate_name: thioredoxin 1

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

proof_lines: kcat is 230 sec(-1) with cyanide as substrate.

substrate: thioredoxin 1


organism: Cavia porcellus


organism: Eidolon helvum


organism: Escherichia coli


organism: Fusarium oxysporum

substrate_name: CN-

substrate: CN-


organism: Fusarium solani


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_q16762_and_selected_mutation_signature and applied mutation signature E102D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_q16762_and_selected_mutation_signature and applied mutation signature P285A to reconstruct the assayed variant sequence.


organism: Methanosarcina mazei


proof_lines: 37°C, pH 6.5, mitochondrial enzyme of p-dimethylaminoazobenzene-treated mice

proof_lines: 37°C, pH 6.5, mitochondrial enzyme of untreated mice


organism: Oncorhynchus mykiss


organism: Pseudomonas aeruginosa

proof_lines:
25°C, pH-independent
25°C, pH 7.3
25°C, pH 8.6


organism: Rana temporaria


proof_lines: 25°C, mitochondrial enzyme of cholestatic liver

proof_lines: 25°C, cytosolic enzyme of apparently operated liver

proof_lines: 25°C, cytosolic enzyme of cholestatic liver


organism: Trametes sanguinea


organism: Trichoderma harzianum

proof_lines:
30°C, pH 8.5, strain O82
30°C, pH 8.5, strain O80
30°C, pH 8.5, strain O90 and strain O10


substrate_name: thiosulfate (at pH 8.6 and at 25 degrees Celsius)


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

substrate_name: thiosulfate (at pH 7.3 and 25 degrees Celsius)


organism: Acinetobacter calcoaceticus


organism: Ancylobacter novellus


organism: Aquifex aeolicus

proof_lines: apparent value, in 100 mM Tris-HCl, pH 9.0, 10 mM KCN, at 85°C


organism: Bos taurus

proof_lines:
25°C, pH 8.5
liver rhodanese
recombinant rhodanese


enzyme_display_name: beta-amylase

organism: Thermococcus sp.

substrate_name: maltopentaose

enzyme: beta-amylase

substrate: maltopentaose


substrate_name: maltotetraose

substrate: maltotetraose


substrate_name: maltotriose

substrate: maltotriose


organism: Bacillus cereus

substrate_name: maltoheptaose

sequence_source: UniProt Q9Z4N9 direct FASTA lookup

substrate: maltoheptaose


substrate_name: Maltohexaose

substrate: Maltohexaose


organism: Arabidopsis thaliana

substrate_name: Thiosulfate

sequence_source: UniProtKB reviewed direct lookup: https://rest.uniprot.org/uniprotkb/Q39129.json

substrate: Thiosulfate


sequence_source: UniProtKB reviewed direct lookup: https://rest.uniprot.org/uniprotkb/Q9FKW8.json


sequence_source: UniProtKB reviewed direct lookup: https://rest.uniprot.org/uniprotkb/O64530.json

assay_conditions_summary: pH 9


organism: Escherichia coli

sequence_source: UniProtKB reviewed direct lookup: https://rest.uniprot.org/uniprotkb/P23857.json


substrate_name: Cyanide

substrate: Cyanide


organism: Escherichia coli (strain K12)

substrate_name: N-acetyl-glucosamine 6-phosphate (at 30 degrees Celsius and pH 7.5)

proof_lines: kcat is 102 sec(-1) for the deacetylation of N-acetyl-D-glucosamine-6-phosphate by the Zn-enzyme. The Cd-NagA catalyzes the hydrolysis of N-thioacetyl-D-glucosamine-6-phosphate substrate about an order of magnitude better than does the Zn-s


organism: Alteromonas sp.

substrate_name: N-acetylglucosamine

proof_lines:
at 30°C
at 10°C

substrate: N-acetylglucosamine


organism: Candida albicans

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

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


organism: Chitiniphilus shinanonensis

proof_lines: recombinant wild-type enzyme, pH 7.0, 37°C


organism: Homo sapiens

substrate_name: N-acetylglucosamine 6-phosphate

substrate: N-acetylglucosamine 6-phosphate


organism: Staphylococcus aureus


organism: Bacillus subtilis

substrate_name: N-Acetyl-D-glucosamine 6-phosphate; H2O

substrate: N-Acetyl-D-glucosamine 6-phosphate; H2O


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P0AF18:E131A and applied mutation signature E131A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P0AF18:D273N and applied mutation signature D273N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P0AF18:H143N and applied mutation signature H143N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P0AF18:Q59A and applied mutation signature Q59A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P0AF18:Q59H and applied mutation signature Q59H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P0AF18:E131Q and applied mutation signature E131Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P0AF18:D273A and applied mutation signature D273A to reconstruct the assayed variant sequence.


organism: Mycobacterium marinum

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


proof_lines: pH 7.0, 37°C, recombinant His6-tagged enzyme


organism: Mycolicibacterium smegmatis


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AF18 canonical sequence; in-review reconstruction of H251N and applied mutation signature H251N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AF18 canonical sequence; in-review reconstruction of N61A and applied mutation signature N61A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AF18 canonical sequence; in-review reconstruction of K139M and applied mutation signature K139M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AF18 canonical sequence; in-review reconstruction of H143Q and applied mutation signature H143Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AF18 canonical sequence; in-review reconstruction of N61H and applied mutation signature N61H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AF18 canonical sequence; in-review reconstruction of Y223F and applied mutation signature Y223F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0AF18 direct FASTA check

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

proof_lines:
Zn in acitve site changed to Cd
Zn in acitve site changed to Mn
Zn in acitve site changed to Ni


organism: Thermotoga maritima

sequence_source: UniProtKB Q9WZS1, supported by RCSB PDB 1O12 SIFTS mapping and PDB Primary Data EC 3.5.1.25


organism: Vibrio cholerae serotype O1

sequence_source: UniProtKB/Swiss-Prot O32445, supported by RCSB PDB 3EGJ and 3IV8 SIFTS mappings and PDB Primary Data EC 3.5.1.25


proof_lines: pH 7.0, 37°C, recombinant His6-tagged wild-type enzyme expressed from Escherichia coli

proof_lines: pH 7.0, 37°C, recombinant His6-tagged wild-type enzyme expressed from Mycobacterium smegmatis

proof_lines: pH 7.0, 37°C, recombinant wild-type His6-tagged enzyme expressed from Escherichia coli


organism: Rattus norvegicus

sequence_source: UniProtKB reviewed accession Q5BJY6 direct lookup on 2026-06-10

assay_conditions_summary: pH 8


enzyme_display_name: cytokinin dehydrogenase

sequence_source: UniProtKB reviewed accession Q9FUJ2

enzyme: cytokinin dehydrogenase


sequence_source: UniProtKB reviewed accession Q9LTS3


sequence_source: UniProtKB reviewed accession Q9FUJ3


sequence_source: UniProtKB reviewed accession O22213


organism: Zea mays

sequence_source: UniProtKB reviewed accession Q9T0N8

proof_lines:
pH 6.5, recombinant enzyme
below, pH 8.0, recombinant enzyme
30°C, pH 7.4


substrate_name: Kinetin

substrate: Kinetin


enzyme_display_name: riboflavin synthase

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AFU8 canonical sequence; variant reconstructed from source mutation E66G and applied mutation signature E66G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: riboflavin synthase(Enzyme) mutant E66G

enzyme: riboflavin synthase


sequence_source: UniProtKB:P0AFU8 canonical sequence

proof_lines:
partial mechanism, Ki value
partial mechanism, Kis value
Ki value, mechanism is partial


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AFU8 canonical sequence; variant reconstructed from source mutation N83G and applied mutation signature N83G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: riboflavin synthase(Enzyme) mutant N83G


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AFU8 canonical sequence; variant reconstructed from source mutation T3R and applied mutation signature T3R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: riboflavin synthase(Enzyme) mutant T3R


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AFU8 canonical sequence; variant reconstructed from source mutation T71A and applied mutation signature T71A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: riboflavin synthase(Enzyme) mutant T71A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AFU8 canonical sequence; variant reconstructed from source mutation N45G and applied mutation signature N45G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: riboflavin synthase(Enzyme) mutant N45G


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AFU8 canonical sequence; variant reconstructed from source mutation F2A and applied mutation signature F2A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: riboflavin synthase(Enzyme) mutant F2A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AFU8 canonical sequence; variant reconstructed from source mutation E183G and applied mutation signature E183G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: riboflavin synthase(Enzyme) mutant E183G


organism: Acinetobacter calcoaceticus

substrate_name: 1-Hexadecanol; Palmitoyl-CoA

sequence_source: UniProtKB direct lookup for Q8GGG1 on 2026-06-10

assay_conditions_summary: cofactor CoA

substrate: 1-Hexadecanol; Palmitoyl-CoA


organism: Marinobacter nauticus

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


organism: Mus musculus

sequence_source: UniProtKB direct lookup for Q6E1M8 on 2026-06-10

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA


organism: Thraustochytrium roseum

substrate_name: myristoyl-CoA

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

substrate: myristoyl-CoA


substrate_name: eicosapentaenoyl-CoA

substrate: eicosapentaenoyl-CoA


substrate_name: Arachidonoyl-CoA

sequence_source: UniProtKB direct lookup for A0A1Z2RWY4 on 2026-06-10

proof_lines:
pH 7.4, 37°C, recombinant enzyme
isoform WSD4, at pH 7.4 and 37°C

substrate: Arachidonoyl-CoA


substrate_name: octadecatrienoyl-CoA

substrate: octadecatrienoyl-CoA


substrate_name: octanoyl-CoA

substrate: octanoyl-CoA


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature F2del to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: riboflavin synthase(Enzyme) mutant F2delta


organism: Schizosaccharomyces pombe

proof_lines:
pH 7.2, 37°C, recombinant enzyme
Raw SKiD Env: Temp=37°C, pH=7.2


enzyme_display_name: 2-aminoadipate transaminase

organism: Candida albicans

enzyme: 2-aminoadipate transaminase


substrate_name: L-Glutamine

substrate: L-Glutamine


substrate_name: L-Methionine

substrate: L-Methionine


substrate_name: Glyoxylate; L-2-Aminoadipate

substrate: Glyoxylate; L-2-Aminoadipate


substrate_name: 2-Oxoadipate; L-Glutamate

substrate: 2-Oxoadipate; L-Glutamate


substrate_name: stearoyl-CoA

substrate: stearoyl-CoA


substrate_name: lauroyl-CoA

substrate: lauroyl-CoA


substrate_name: decanoyl-CoA

substrate: decanoyl-CoA


sequence_source: UniProt REST direct accession lookup for A0A3G1ICG7; source notes identify isoform WSD5.

proof_lines:
pH 7.4, 37°C, recombinant enzyme
isoform WSD5, at pH 7.4 and 37°C


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


sequence_source: UniProt REST direct accession lookup for P16440; source bundle also included P11998, which is not EC 2.5.1.9.


sequence_source: UniProtKB reviewed Swiss-Prot Q9T0N8 direct lookup


substrate_name: Isopentenyladenine riboside

column_label: Table 2: Activity of ZmCKX1 with various cytokinins (Biochem. J. 2004, 380:121-130); Table 2, row Isopentenyladenine riboside, column Q0 (0.5 mM), paired with the Results prose Km for iPR with 0.5 mM Q0; the kcat value 129.8 s-1 comes from the 'Turnover rate (s-1), sub-column Q0 (0.5 mM)' cell of the Table 2 row 'Isopentenyladenine riboside', and the Michaelis constant 0.044 mM comes from the Results prose (Other cytokinins as potential substrates of CKX): 'apparent Km values of 0.040 and 0.044 mM for iP and iPR'. Neither table prints a kcat/Km column and the article prints no kcat/Km value.

normalized_value_unit_evidence: kcat: printed cell 129.8 s-1; already in s^-1, no conversion applies (this article prints no min^-1 kinetic value); the paper value is 129.8 s^(-1). Km: printed value 0.044 mM; already in mM, no conversion applies; the paper value is 0.044 mM. kcat/Km: this article prints no kcat/Km value for this measurement, so the exported 2950.0000000000005 s^(-1)*mM^(-1) is not a printed value; it is the quotient 129.8 / 0.044 of this measurement's own two printed values, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, row Isopentenyladenine riboside, column Q0 (0.5 mM), paired with the Results prose Km for iPR with 0.5 mM Q0: kcat = 129.8 s-1 (printed column head 'Turnover rate (s-1), sub-column Q0 (0.5 mM)' of the Table 2 row 'Isopentenyladenine riboside'); Km = 0.044 mM (printed in the Results prose (Other cytokinins as potential substrates of CKX): 'apparent Km values of 0.040 and 0.044 mM for iP and iPR'). No kcat/Km value is printed for this measurement.

substrate: Isopentenyladenine riboside


column_label: Table 1: Kinetic constants of ZmCKX1 with various electron acceptors (Biochem. J. 2004, 380:121-130); Table 1, row DCPIP, column pH 6.5, paired with the Results prose Km for DCPIP; the kcat value 178.4 s-1 comes from the 'Turnover rate (s-1), sub-column pH 6.5' cell of the Table 1 row 'DCPIP', and the Michaelis constant 0.036 mM comes from the Results prose (Search for electron acceptors of CKX): 'DCPIP, 0.036 mM'. Neither table prints a kcat/Km column and the article prints no kcat/Km value.

normalized_value_unit_evidence: kcat: printed cell 178.4 s-1; already in s^-1, no conversion applies (this article prints no min^-1 kinetic value); the paper value is 178.4 s^(-1). Km: printed value 0.036 mM; already in mM, no conversion applies; the paper value is 0.036 mM. kcat/Km: this article prints no kcat/Km value for this measurement, so the exported 4955.555555555556 s^(-1)*mM^(-1) is not a printed value; it is the quotient 178.4 / 0.036 of this measurement's own two printed values, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, row DCPIP, column pH 6.5, paired with the Results prose Km for DCPIP: kcat = 178.4 s-1 (printed column head 'Turnover rate (s-1), sub-column pH 6.5' of the Table 1 row 'DCPIP'); Km = 0.036 mM (printed in the Results prose (Search for electron acceptors of CKX): 'DCPIP, 0.036 mM'). No kcat/Km value is printed for this measurement.


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


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Swiss-Prot Q9T0N8 direct lookup plus selected E381A mutation note and applied mutation signature E381A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E381A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Swiss-Prot Q9T0N8 direct lookup plus selected E381S mutation note and applied mutation signature E381S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E381S, pH and temperature not specified in the publication


organism: Acinetobacter baylyi ADP1

sequence_source: UniProtKB reviewed Swiss-Prot Q8GGG1 direct lookup

assay_conditions_summary: pH 7.4; 308.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from UniProt P0AFU8 canonical FASTA; S146G reconstructed from the SABIO-RK modifier label after direct coordinate check. and applied mutation signature S146G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: riboflavin synthase(Enzyme) mutant S146G


sequence_variant_note: Resolved canonical sequence from UniProt P0AFU8 canonical FASTA; H97Q reconstructed from the SABIO-RK modifier label after direct coordinate check. and applied mutation signature H97Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: riboflavin synthase(Enzyme) mutant H97Q


sequence_variant_note: Resolved canonical sequence from UniProt P0AFU8 canonical FASTA; F2Y reconstructed from the SABIO-RK modifier label after direct coordinate check. and applied mutation signature F2Y to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: riboflavin synthase(Enzyme) mutant F2Y


sequence_variant_note: Resolved canonical sequence from UniProt P0AFU8 canonical FASTA; K137A reconstructed from the SABIO-RK modifier label after direct coordinate check. and applied mutation signature K137A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: riboflavin synthase(Enzyme) mutant K137A


sequence_variant_note: Resolved canonical sequence from UniProt P0AFU8 canonical FASTA; D185L reconstructed from the SABIO-RK modifier label after direct coordinate check. and applied mutation signature D185L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: riboflavin synthase(Enzyme) mutant D185L


sequence_variant_note: Resolved canonical sequence from UniProt P0AFU8 canonical FASTA; H102Q reconstructed from the SABIO-RK modifier label after direct coordinate check. and applied mutation signature H102Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: riboflavin synthase(Enzyme) mutant H102Q


sequence_variant_note: Resolved canonical sequence from UniProt P0AFU8 canonical FASTA; S41A reconstructed from the SABIO-RK modifier label after direct coordinate check. and applied mutation signature S41A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: riboflavin synthase(Enzyme) mutant S41A


sequence_variant_note: Resolved canonical sequence from UniProt P0AFU8 canonical FASTA; E85G reconstructed from the SABIO-RK modifier label after direct coordinate check. and applied mutation signature E85G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: riboflavin synthase(Enzyme) mutant E85G


organism: Thermus thermophilus

substrate_name: L-glutamate

sequence_source: UniProtKB reviewed Q72LL6 direct lookup on 2026-06-10; canonical context only because S20E/H4C was not safely reconstructed

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

substrate: L-glutamate


enzyme_display_name: adenylyl-sulfate kinase

organism: Arabidopsis thaliana

substrate_name: ATP; Adenylylsulfate

sequence_source: UniProtKB reviewed Q84JF0 direct lookup on 2026-06-10

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

enzyme: adenylyl-sulfate kinase

substrate: ATP; Adenylylsulfate


substrate_name: Adenylylsulfate; ATP

sequence_source: UniProtKB reviewed O49196 direct lookup on 2026-06-10

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ATP

substrate: Adenylylsulfate; ATP


sequence_source: UniProtKB reviewed Q9SRW7 direct lookup on 2026-06-10


sequence_source: UniProtKB reviewed Q43295 direct lookup on 2026-06-10

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines:
25°C
Raw SKiD Env: Temp=17°C, pH=7.5
Raw SKiD Env: Temp=25°C, pH=7.5


substrate_name: adenosine 5'-phosphosulfate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q43295 direct lookup on 2026-06-10; C86A/C119A reconstructed from canonical residues C86 and C119 and applied mutation signature C86A/C119A to reconstruct the assayed variant sequence.

proof_lines: oxidized mutant enzyme C86A/C119A, at pH 7.5 and 25°C

proof_lines: reduced mutant enzyme C86A/C119A, at pH 7.5 and 25°C

substrate: adenosine 5'-phosphosulfate


sequence_source: UniProtKB reviewed Q43295 direct lookup on 2026-06-10; C86A/C119A reconstructed from canonical residues C86 and C119


proof_lines: reduced wild type enzyme, at pH 7.5 and 25°C

proof_lines: oxidized wild type enzyme, at pH 7.5 and 25°C


sequence_source: UniProtKB:Q43295 direct REST lookup

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q43295 direct REST lookup and applied mutation signature D136A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q43295 direct REST lookup and applied mutation signature D136N to reconstruct the assayed variant sequence.


organism: Homo sapiens

sequence_source: UniProtKB:O43252 direct REST lookup

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: pH 8.0, 37°C, E. coli expressed N-terminal fragment


organism: Penicillium chrysogenum

sequence_source: UniProtKB:Q12657 direct REST lookup

assay_conditions_summary: pH 8.1; 303.15 K; cofactor ATP

proof_lines: pH 8.1, 30°C, wild-type enzyme at 100 mM ammonium sulfate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12657 direct REST lookup and applied mutation signature S107A to reconstruct the assayed variant sequence.

proof_lines: pH 8.1, 30°C, S107A mutant enzyme at 100 mM ammonium sulfate


substrate_name: ATP

sequence_source: UniProtKB reviewed accession Q12657 direct REST lookup on 2026-06-10

proof_lines:
ATP in form of MgATP2-
Raw SKiD Env: Temp=30°C, pH=8.1

substrate: ATP


sequence_source: UniProtKB reviewed accession P69834 direct REST lookup on 2026-06-10


substrate_name: 2-C-Methyl-D-erythritol 4-phosphate

substrate: 2-C-Methyl-D-erythritol 4-phosphate


substrate_name: CTP

substrate: CTP


organism: Bacillus subtilis

substrate_name: 2-C-methyl-D-erythritol 4-phosphate

sequence_source: UniProtKB reviewed accession Q06755 direct REST lookup on 2026-06-10

proof_lines: recombinant detagged enzyme, pH 8.0, 30°C

substrate: 2-C-methyl-D-erythritol 4-phosphate


sequence_source: UniProtKB reviewed accession Q46893 direct REST lookup on 2026-06-10


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature R20K to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature R19K to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase(Enzyme) mutant R109A


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


proof_lines: SABIO-RK modifier species: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase(Enzyme) mutant D106E


sequence_variant_note: Resolved canonical sequence from UniProtKB Q46893 canonical sequence reconstructed with R19K from BRENDA/PubMed mutant evidence and applied mutation signature R19K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase(Enzyme) mutant R19K


sequence_variant_note: Resolved canonical sequence from UniProtKB Q46893 canonical sequence reconstructed with R20K from BRENDA/PubMed mutant evidence and applied mutation signature R20K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase(Enzyme) mutant R20K


sequence_variant_note: Resolved canonical sequence from UniProtKB Q46893 canonical sequence reconstructed with R20A from BRENDA/PubMed mutant evidence and applied mutation signature R20A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase(Enzyme) mutant R20A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q46893 canonical sequence reconstructed with R19A from BRENDA/PubMed mutant evidence and applied mutation signature R19A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q46893 canonical sequence reconstructed with D106E from BRENDA/PubMed mutant evidence and applied mutation signature D106E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q46893 canonical sequence reconstructed with R109A from BRENDA/PubMed mutant evidence and applied mutation signature R109A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q46893 canonical sequence reconstructed with R20K from BRENDA/PubMed mutant evidence


sequence_variant_note: Resolved canonical sequence from UniProtKB Q46893 canonical sequence reconstructed with R19A from BRENDA mutant evidence and applied mutation signature R19A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q46893 direct lookup plus D106E reconstruction from the Q46893 canonical sequence and applied mutation signature D106E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q46893 direct lookup plus R19K reconstruction from the Q46893 canonical sequence and applied mutation signature R19K to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q46893 direct lookup plus D106E reconstruction from the Q46893 canonical sequence


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q46893 and applied mutation signature T140V to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-State Kinetic Parameters for E. coli wt YgbP and Mutants (Biochemistry 2004, volume 43, number 38, pages 12189-12197). The table is printed as two halves. The MEP half carries the column heads Km (mM), appkcat (s-1), Calckcat (s-1) and kcat/Km (s-1 mM-1); the CTP half carries Km (mM), Ki (mM), Obskcat (s-1) and kcat/Km (s-1 mM-1). This record reads the enzyme row T140V along its MEP half: column Km (mM) = 49.0; column Calckcat (s-1) = 4.0; column kcat/Km (s-1 mM-1) = 0.08.

normalized_value_unit_evidence: kcat: printed cell 4.0 in the column Calckcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 4.0 s^(-1). Km: printed cell 49.0 in the column Km (mM); mM is already canonical, so no unit conversion applies and the value is 49.0 mM. kcat/Km: the MEP half of this line prints the catalytic-efficiency cell 0.08 s-1 mM-1; 1 s-1 mM-1 is already the canonical s^(-1)*mM^(-1), so no unit conversion applies. The exact quotient of the two printed component cells of the same line is 4.0 / 49.0 = 0.08163265306122448 s^(-1)*mM^(-1), and the printed cell is that same quotient carried to the precision the table prints.

raw_value_unit_evidence: Table 1, enzyme row T140V, MEP half: Km = 49.0 mM; Calckcat = 4.0 s-1; printed kcat/Km = 0.08 s-1 mM-1.

row_label: Table 1, enzyme row T140V, MEP half (MEP as the varied substrate)


sequence_source: UniProtKB Q46893 direct lookup plus R19K reconstruction from the Q46893 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB Q46893 direct lookup plus R109A reconstruction from the Q46893 canonical sequence and applied mutation signature R109A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q46893 and applied mutation signature K27S to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-State Kinetic Parameters for E. coli wt YgbP and Mutants (Biochemistry 2004, volume 43, number 38, pages 12189-12197). The table is printed as two halves. The MEP half carries the column heads Km (mM), appkcat (s-1), Calckcat (s-1) and kcat/Km (s-1 mM-1); the CTP half carries Km (mM), Ki (mM), Obskcat (s-1) and kcat/Km (s-1 mM-1). This record reads the enzyme row K27S along its MEP half: column Km (mM) = 3.0; column Calckcat (s-1) = 0.75; column kcat/Km (s-1 mM-1) = 0.25; column Ki (mM) of the CTP half = 12.3.

normalized_value_unit_evidence: kcat: printed cell 0.75 in the column Calckcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.75 s^(-1). Km: printed cell 3.0 in the column Km (mM); mM is already canonical, so no unit conversion applies and the value is 3.0 mM. Ki: printed cell 12.3 in the column Ki (mM); mM is already canonical, so no unit conversion applies and the value is 12.3 mM. kcat/Km: the MEP half of this line prints the catalytic-efficiency cell 0.25 s-1 mM-1; 1 s-1 mM-1 is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell is 0.25 s^(-1)*mM^(-1). This catalog row carries no kcat_over_km field, so that printed cell is recorded as typed provenance only and no efficiency value is proposed.

raw_value_unit_evidence: Table 1, enzyme row K27S, MEP half: Km = 3.0 mM; Calckcat = 0.75 s-1; printed kcat/Km = 0.25 s-1 mM-1; Ki = 12.3 mM.

row_label: Table 1, enzyme row K27S, MEP half (MEP as the varied substrate)


sequence_source: UniProtKB Q46893 canonical sequence from direct lookup

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


sequence_source: UniProt Q46893; RCSB 1I52 entity maps full sequence to UniProt Q46893

column_label: Table 1: Steady-State Kinetic Parameters for E. coli wt YgbP and Mutants (Biochemistry 2004, volume 43, number 38, pages 12189-12197). The table is printed as two halves. The MEP half carries the column heads Km (mM), appkcat (s-1), Calckcat (s-1) and kcat/Km (s-1 mM-1); the CTP half carries Km (mM), Ki (mM), Obskcat (s-1) and kcat/Km (s-1 mM-1). This record reads the enzyme row wt along its CTP half: column Km (mM) = 0.76; column Obskcat (s-1) = 54.1; column kcat/Km (s-1 mM-1) = 71.

normalized_value_unit_evidence: kcat: printed cell 54.1 in the column Obskcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 54.1 s^(-1). Km: printed cell 0.76 in the column Km (mM); mM is already canonical, so no unit conversion applies and the value is 0.76 mM. kcat/Km: the CTP half of this line prints the catalytic-efficiency cell 71 s-1 mM-1; 1 s-1 mM-1 is already the canonical s^(-1)*mM^(-1), so no unit conversion applies. The exact quotient of the two printed component cells of the same line is 54.1 / 0.76 = 71.1842105263158 s^(-1)*mM^(-1), and the printed cell is that same quotient carried to the precision the table prints.

raw_value_unit_evidence: Table 1, enzyme row wt, CTP half: Km = 0.76 mM; Obskcat = 54.1 s-1; printed kcat/Km = 71 s-1 mM-1.

row_label: Table 1, enzyme row wt, CTP half (CTP as the varied substrate)