sequence_source: UniProt P17989 canonical sequence; row-specific substitution reconstructed with paper numbering mapped to UniProt position by +23 offset.

sequence_variant_note: Mutation signature W203F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 6

proof_lines: mutant W203F, calculated as D-glucose units released from lichenan

proof_lines: mutant W203F, pH 6.0, temperature not specified in the publication


enzyme_display_name: licheninase

organism: Fibrobacter succinogenes

substrate_name: lichenan

source_db: brenda

km_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

sequence_variant_note: Mutation signature D206M could not be applied safely because the resolved sequence does not match the expected reference residue(s).

mutation_type: substitution

proof_lines: mutant D206M, calculated as D-glucose units released from lichenan

enzyme: licheninase

substrate: lichenan

source: brenda


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +5, so it is treated as a source-provided variant sequence.

proof_lines: mutant D202L, calculated as D-glucose units released from lichenan


sequence_variant_note: Mutation signature F205L matches the mutant residue at offset +2 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: mutant F205L, calculated as D-glucose units released from lichenan


mutation_signature: Unknown

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

proof_lines: mutant G207-, calculated as D-glucose units released from lichenan


sequence_variant_note: Mutation signature G201S matches the mutant residue at offset +2 and the reference residue at offset +0; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: mutant G201S, calculated as D-glucose units released from lichenan


sequence_variant_note: Mutation signature D202N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant D202N, calculated as D-glucose units released from lichenan


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17989 direct REST lookup; mutation reconstructed with +23 residue-numbering offset and applied mutation signature K200M with inferred residue-numbering offset +23 to reconstruct the assayed variant sequence.

proof_lines: mutant K200M, calculated as D-glucose units released from lichenan


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17989 direct REST lookup; mutation reconstructed with +23 residue-numbering offset and applied mutation signature G207N with inferred residue-numbering offset +23 to reconstruct the assayed variant sequence.

proof_lines: mutant G207N, calculated as D-glucose units released from lichenan


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17989 direct REST lookup; mutation reconstructed with +23 residue-numbering offset and applied mutation signature D206R with inferred residue-numbering offset +23 to reconstruct the assayed variant sequence.

proof_lines: mutant D206R, calculated as D-glucose units released from lichenan


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17989 direct REST lookup; mutation reconstructed with +23 residue-numbering offset and applied mutation signature N208G with inferred residue-numbering offset +23 to reconstruct the assayed variant sequence.

proof_lines: mutant N208G, calculated as D-glucose units released from lichenan


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17989 direct REST lookup; mutation reconstructed with +23 residue-numbering offset and applied mutation signature D206N with inferred residue-numbering offset +23 to reconstruct the assayed variant sequence.

proof_lines: mutant D206N, calculated as D-glucose units released from lichenan


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17989 direct REST lookup; mutation reconstructed with +23 residue-numbering offset and applied mutation signature T204F with inferred residue-numbering offset +23 to reconstruct the assayed variant sequence.

proof_lines: mutant T204F, calculated as D-glucose units released from lichenan


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17989 direct REST lookup; mutation reconstructed with +23 residue-numbering offset and applied mutation signature W203R with inferred residue-numbering offset +23 to reconstruct the assayed variant sequence.

proof_lines: mutant W203R, calculated as D-glucose units released from lichenan


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17989 direct REST lookup; mutation reconstructed with +23 residue-numbering offset and applied mutation signature Y42L with inferred residue-numbering offset +23 to reconstruct the assayed variant sequence.

proof_lines: mutant Y42L, 45°C, pH not specified in the publication


proof_lines: mutant Q70N, calculated as D-glucose units released from lichenan


proof_lines: mutant Q70R, calculated as D-glucose units released from lichenan


proof_lines: mutant E85D, calculated as D-glucose units released from lichenan


proof_lines: mutant Q70I, calculated as D-glucose units released from lichenan


proof_lines: mutant Q81N, calculated as D-glucose units released from lichenan


proof_lines: mutant E85I, calculated as D-glucose units released from lichenan


proof_lines: mutant N72A, calculated as D-glucose units released from lichenan


proof_lines: mutant K200F, calculated as D-glucose units released from lichenan


organism: Evansstolkia leycettana

substrate_name: lichenin

substrate: lichenin


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


proof_lines: mutant Q70D, calculated as D-glucose units released from lichenan


proof_lines: mutant Q70A, calculated as D-glucose units released from lichenan


mutation_signature: truncated enzyme / calculated as D-glucose units released from lichenan truncated enzyme

mutation_type: truncation

proof_lines: truncated enzyme, calculated as D-glucose units released from lichenan


proof_lines: mutant N72Q, calculated as D-glucose units released from lichenan


proof_lines: mutant Q81I, calculated as D-glucose units released from lichenan


proof_lines: mutant Q70E, calculated as D-glucose units released from lichenan


organism: Acetivibrio thermocellus

substrate_name: Beta-D-glucan

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

substrate: Beta-D-glucan


organism: Aspergillus fumigatus

substrate_name: carboxymethyl cellulose

substrate: carboxymethyl cellulose


organism: Bacillus amyloliquefaciens

substrate_name: H2O; 1,3-beta-D-Glucan

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

km_unit: mM

unit: lgwedgeoneswedgeone

substrate: H2O; 1,3-beta-D-Glucan


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

proof_lines: fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, pH 6.0, 70°C


organism: Bacillus licheniformis

ki_unit: mM


organism: Bacillus pumilus

substrate_name: Barley beta-glucan

substrate: Barley beta-glucan


organism: Bacillus sp. SJ-10


proof_lines: mutant N139A, 45°C, pH not specified in the publication


proof_lines: mutant N44Q, 55°C, pH not specified in the publication


proof_lines: mutant E47I, 45°C, pH not specified in the publication


proof_lines: mutant R137Q, 40°C, pH not specified in the publication


proof_lines: mutant R137M, 40°C, pH not specified in the publication


proof_lines: mutant F40I, 45°C, pH not specified in the publication


proof_lines: mutant N44L, 55°C, pH not specified in the publication


organism: Bacillus subtilis

substrate_name: Lichenin; H2O

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

sequence_source: UniProtKB:P04957 direct accession lookup; reviewed Swiss-Prot beta-glucanase from Bacillus subtilis strain 168 with EC 3.2.1.73.

substrate: Lichenin; H2O


source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

data_origin: experimental

status: unverified

source: oed


organism: Bacillus tequilensis

substrate_name: azo-barley glucan

substrate: azo-barley glucan


organism: Chaetomium sp. CQ31

sequence_source: UniProtKB:A0A915Q9D1 direct accession lookup with PDB cross-reference 7EE2; RCSB 7EE2 entity sequence matches the UniProt sequence and title names Chaetomium sp. CQ31 beta-1,3-1,4-glucanase.


proof_lines:
pH 7.0, 35°C
isozyme EG1, pH 5.0, 50°C
pH 7.2, 30°C


enzyme_display_name: 3-deoxy-8-phosphooctulonate synthase

organism: Arabidopsis thaliana

substrate_name: phosphoenolpyruvate

enzyme: 3-deoxy-8-phosphooctulonate synthase

substrate: phosphoenolpyruvate


organism: Campylobacter jejuni

substrate_name: D-arabinose 5-phosphate

kcat_display: Not reported

substrate: D-arabinose 5-phosphate


organism: Escherichia coli

substrate_name: Phosphoenolpyruvate; H2O; D-Arabinose 5-phosphate

assay_conditions_summary: pH 7.6; 310.15 K; buffer 10 mM ammonium acetate

proof_lines: in 10 mM ammonium acetate buffer, pH 7.8

proof_lines: pH and temperature not specified in the publication


organism: Helicobacter pylori

proof_lines:
pH 7.8, Cd2+-reconstituted enzyme
pH 7.8, Zn2+-reconstituted enzyme
pH 7.8, Co2+-reconstituted enzyme


organism: Neisseria gonorrhoeae


organism: Neisseria meningitidis

proof_lines: mutant N59DELTA, pH 7.5, temperature not specified in the publication


organism: Streptococcus bovis

sequence_source: UniProtKB O07856 direct accession lookup


organism: Thermotoga maritima

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

sequence_source: UniProtKB Q9X274 direct accession lookup

proof_lines:
pH 6.6, 70°C
Raw SKiD Env: Temp=70°C, pH=6.6

source_databases_merged: brenda skid


organism: uncultured bacterium


organism: Fibrobacter succinogenes

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 K64M, 50°C, pH not specified in the publication


proof_lines: mutant L62G, 45°C, pH not specified in the publication


proof_lines: mutant K64A, 50°C, pH not specified in the publication


sequence_source: UniProtKB:P17989 FASTA direct lookup

proof_lines: wild-type, expressed in Escherichia coli, pH 5.0, 50°C

proof_lines: wild-type, calculated as D-glucose units released from lichenan


proof_lines: mutant W203Y, expressed in Escherichia coli, pH 5.0, 50°C

proof_lines: pH 5.0, 50°C, mutant W203Y, calculated as reducing sugar released from substrate


proof_lines: mutant V18Y/W203Y, expressed in Escherichia coli, pH 5.0, 50°C

proof_lines: pH 5.0, 50°C, mutant V18Y/W203Y, calculated as reducing sugar released from substrate


proof_lines: mutant V18Y, expressed in Escherichia coli, pH 5.0, 50°C

proof_lines: pH 5.0, 50°C, mutant V18Y, calculated as reducing sugar released from substrate


organism: Macrotermes barneyi

substrate_name: Laminarin

sequence_source: UniProtKB:A0A6C0TJL0 FASTA direct lookup

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

substrate: Laminarin


organism: Malbranchea cinnamomea

sequence_source: UniProtKB REST FASTA direct lookup for accession S6DXG7

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


organism: Neocallimastix patriciarum

sequence_source: UniProtKB REST FASTA direct lookup for accession I3W8N1


sequence_source: UniProtKB REST FASTA direct lookup for accession I3W8N2


sequence_source: UniProtKB REST FASTA direct lookup for accession I3W8N3


sequence_source: UniProtKB REST FASTA direct lookup for accession I3W8N0


organism: Paenibacillus sp. X4

sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA direct lookup for accession A0A088BCU2 and applied mutation signature C17R/Q87T/D152G/Y307H/V330A/N344D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C17R/Q87T/D152G/Y307H/V330A/N344D, at pH 5.0 and 60°C

proof_lines: mutant enzyme C17R/Q87T/D152G/Y307H/V330A/N344D, at pH 5.0 and 40°C


sequence_source: UniProtKB REST FASTA direct lookup for accession A0A088BCU2

proof_lines:
wild type enzyme, at pH 5.0 and 60°C
wild type enzyme, at pH 5.0 and 40°C


organism: Rhizomucor miehei

sequence_source: UniProtKB REST FASTA direct lookup for accession H9BZ70


enzyme_display_name: tannase

organism: Bacillus subtilis

substrate_name: tannic acid at 40 degrees Celsius and pH 5.0

source_db: uniprot

verification_status: corrected

sequence: VQPPHSHGDNFYIWT

wild_type_sequence: VQPPHSHGDNFYIWT

assay_conditions_summary: pH 5

proof_lines: Exhibits salt tolerance as it retains 67% of activity after 24 h exposure to 4 M NaCl.

enzyme: tannase

status: corrected

source: uniprot


sequence_source: RCSB PDB FASTA and UniProt Q9JZ55

sequence_variant_note: Resolved canonical sequence from RCSB PDB FASTA and UniProt Q9JZ55 and applied mutation signature N59A to reconstruct the assayed variant sequence.

proof_lines: mutant N59A, pH 7.5, temperature not specified in the publication


proof_lines: wild-type, pH 7.5, temperature not specified in the publication

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


sequence_variant_note: Resolved canonical sequence from RCSB PDB FASTA and UniProt Q9JZ55 and applied mutation signature F114R to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant F114R


sequence_variant_note: Resolved canonical sequence from RCSB PDB FASTA and UniProt Q9JZ55 and applied mutation signature F114R/R117Q/F139G to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, F114R/R117Q/F139G


sequence_variant_note: Resolved canonical sequence from RCSB PDB FASTA and UniProt Q9JZ55 and applied mutation signature F114R/R117Q to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant F114R/R117Q


proof_lines: pH and temperature not specified in the publication


organism: Acidithiobacillus ferrooxidans

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


substrate_name: 2-deoxy-D-ribose 5-phosphate

substrate: 2-deoxy-D-ribose 5-phosphate


proof_lines: mutant N57A, pH 7.5, temperature not specified in the publication


substrate_name: Unknown

substrate: Unknown


organism: Aquifex aeolicus

sequence_source: UniProtKB:O66496; PMID:10491295; direct lit_pubmed and EC+organism lookup


organism: Aquifex pyrophilus

sequence_source: UniProtKB:Q8GLK7; PMID:12955602; direct EC+organism lookup


enzyme_display_name: rhodopsin kinase

organism: Bos taurus

substrate_name: ATP

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

enzyme: rhodopsin kinase

substrate: ATP


organism: Homo sapiens

substrate_name: rhodopsin

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines: recombinant wild-type GRK7, pH 7.0, 30°C

proof_lines: recombinant wild-type GRK1, pH 7.0, 30°C

substrate: rhodopsin


substrate_name: RRREEEEESAAA

substrate: RRREEEEESAAA


organism: Musca domestica

assay_conditions_summary: pH 7.5; 293.15 K; cofactor ATP


enzyme_display_name: histidinol-phosphate transaminase

organism: Zymomonas mobilis

substrate_name: L-histidinol phosphate

enzyme: histidinol-phosphate transaminase

substrate: L-histidinol phosphate


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines:
pH 7.5, 25°C, freshly bleached
pH 7.5, 25°C
pH 7.4, 37°C


proof_lines:
pH 7.5, 30°C, wild-type RK
pH 7.5, 30°C, wild-type RK and mutants


organism: Salmonella enterica subsp. enterica serovar Typhimurium

proof_lines:
pH 7.4, 25°C, mutant enzyme P145S
pH 7.4, 37°C, mutant enzyme P145S


proof_lines:
pH 7.4, 37°C, wild-type enzyme
pH 7.4, 25°C, wild-type enzyme


proof_lines:
42°C, mutant strain PR32
37°C, mutant strain PR32


proof_lines:
28°C, parent strain PR122
37°C, parent strain PR122
42°C, parent strain PR122


enzyme_display_name: adenosyl-fluoride synthase

organism: Streptantibioticus cattleyicolor

substrate_name: fluoride

sequence_source: UniProtKB:Q70GK9 reviewed fluorinase; EC 2.5.1.63; organism Streptantibioticus cattleyicolor; PubMed 14765200 and 17985882 evidence.

enzyme: adenosyl-fluoride synthase

substrate: fluoride


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q70GK9 reviewed fluorinase sequence and UniProt mutagenesis evidence for T80A from PMID 17985882. and applied mutation signature T80A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; 298.15 K; buffer 20 mM sodium phosphate

proof_lines: mutant enzyme T80A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C


enzyme_display_name: mitogen-activated protein kinase

substrate_name: protein ATF2

proof_lines: pH 7.6, 27°C, purified, recombinant detagged, activated p38 MAPKalpha

enzyme: mitogen-activated protein kinase

substrate: protein ATF2


organism: Mus musculus

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

proof_lines: pH 7.0, 25°C, monophosphorylated p38alpha

proof_lines: above, pH 7.6, 27°C, recombinant p38 MAPK


organism: synthetic construct


organism: Zea mays

assay_conditions_summary: cofactor ATP


enzyme_display_name: ribokinase

substrate_name: D-Ribose; ATP

proof_lines:
30°C, pH 7, in presence of Mg2+
30°C, pH 7

enzyme: ribokinase

substrate: D-Ribose; ATP


organism: Escherichia coli

substrate_name: D-ribose

proof_lines:
37°C, pH 7.4
37°C, pH 6.2, 5 mM arsenate
37°C, pH 6.2, 20 mM phosphate

substrate: D-ribose


enzyme_display_name: serine--glyoxylate transaminase

organism: Methylosinus trichosporium

substrate_name: glyoxylate

sequence_source: UniProtKB:A0A2D2D0N7 direct EC+organism lookup

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication, recombinant enzyme, with L-serine

proof_lines: pH 7.0, temperature not specified in the publication, recombinant enzyme, with pyruvate

proof_lines: pH 7.0, temperature not specified in the publication, recombinant enzyme, with glyoxylate

enzyme: serine--glyoxylate transaminase

substrate: glyoxylate


organism: Phaseolus vulgaris

proof_lines:
pH 8.0, 30°C, cosubstrate L-serine
pH 8.0, 30°C
cosubstrate pyruvate


organism: Secale cereale

substrate_name: L-serine

substrate: L-serine


organism: Spinacia oleracea


organism: Bacillus subtilis


organism: Neurospora sp.


organism: Neisseria meningitidis

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 canonical sequence plus RCSB 4JTK mutant FASTA cross-check and applied mutation signature R117Q to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, R117Q


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 canonical sequence plus RCSB 4JTG mutant FASTA cross-check and applied mutation signature F114R/R117A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant F114R/R117A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 canonical sequence plus RCSB 4JTE mutant FASTA cross-check and applied mutation signature F114A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant F114A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 canonical sequence plus RCSB 4JTJ mutant FASTA cross-check and applied mutation signature R117K to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, R117K


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 canonical sequence plus selected BRENDA/PubMed mutation annotation and applied mutation signature F139A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant F139A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 canonical sequence plus selected BRENDA/PubMed mutation annotation and applied mutation signature R117A to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, R117A


sequence_variant_note: Resolved canonical sequence from UniProt Q70GK9 plus PMID 17985882-linked PDB 2V7X and applied mutation signature S158A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S158A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt Q70GK9 plus PMID 17985882-linked PDB 2V7W/2V7U/2V7T and applied mutation signature S158G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S158G, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C


substrate_name: S-adenosyl-L-methionine

sequence_source: UniProt Q70GK9 plus PMID 17985882-linked PDB 2V7V

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

proof_lines: wild type enzyme, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C

substrate: S-adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProt Q70GK9 plus PMID 17985882 mutation context and applied mutation signature T80S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T80S, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C


organism: Hyphomicrobium methylovorum

sequence_source: UniProt O08374 EC+organism direct lookup

proof_lines:
pH 8.0
pH 7.0, 30°C
recombinant enzyme


organism: Lathyrus oleraceus

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

proof_lines:
pH 8.1, 30°C, cosubstrate glyoxylate
pH 8.1, 30°C, cosubstrate pyruvate
pH 8.1, 30°C, cosubstrate L-serine


organism: Homo sapiens

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines: 37°C, pH 7.0, in presence of 1 mM phosphate

proof_lines: 37°C, pH 7.0, in presence of 5 mM phosphate

proof_lines: 37°C, pH 7.0, in presence of 2 mM phosphate


organism: Lactiplantibacillus plantarum


organism: Leishmania major

assay_conditions_summary: pH 8.5; 295.15 K; cofactor ATP


organism: Salmonella enterica


organism: Salmonella enterica subsp. enterica serovar Typhimurium


enzyme_display_name: glutamate 5-kinase

proof_lines: pH 7.0, 37°C, gamma-glutamyl kinase DHPr

enzyme: glutamate 5-kinase


enzyme_display_name: Xaa-Pro dipeptidase

organism: Xanthomonas campestris pv. campestris

substrate_name: Val-Pro

sequence_source: UniProtKB Q8P839 direct accession lookup; RCSB 5FCF/5FCH SIFTS alignment to Q8P839; PMID 27816563 structural paper anchor

enzyme: Xaa-Pro dipeptidase

substrate: Val-Pro


substrate_name: Lys-Pro

substrate: Lys-Pro


substrate_name: Tyr-Pro

substrate: Tyr-Pro


substrate_name: Met-Pro

substrate: Met-Pro


substrate_name: Leu-Pro

substrate: Leu-Pro


substrate_name: Gly-Pro

substrate: Gly-Pro


substrate_name: Pro-Pro

substrate: Pro-Pro


substrate_name: Arg-Pro

substrate: Arg-Pro


organism: Deinococcus radiodurans

substrate_name: Met-Pro-Ala

substrate: Met-Pro-Ala


substrate_name: Met-Ala-Ala

substrate: Met-Ala-Ala


substrate_name: Arg-Pro-Ala

substrate: Arg-Pro-Ala


organism: Escherichia coli


substrate_name: paraoxon

substrate: paraoxon


organism: Lactococcus lactis

substrate_name: H2O; Leu-Pro

proof_lines: SABIO-RK modifier species: Xaa-Pro dipeptidase(Enzyme) mutant R293S

substrate: H2O; Leu-Pro


organism: Mycobacterium tuberculosis

substrate_name: Met-Pro; Met-Ala-Ala; Met-Pro-Ala

substrate: Met-Pro; Met-Ala-Ala; Met-Pro-Ala


organism: Pyrococcus furiosus

sequence_source: UniProtKB:P81535 direct REST/FASTA lookup


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P81535 canonical sequence plus selected batch mutation_signature R19G/G39E/K71E/S229T and applied mutation signature R19G/G39E/K71E/S229T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P81535 canonical sequence plus selected batch mutation_signature G39E and applied mutation signature G39E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P81535 canonical sequence plus selected batch mutation_signature R19G/K71E/S229T and applied mutation signature R19G/K71E/S229T to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 35°C, mutant enzyme R19G/K71E/S229T

proof_lines: pH 7.0, 70°C, mutant enzyme R19G/K71E/S229T

proof_lines: pH 7.0, 100°C, mutant enzyme R19G/K71E/S229T


proof_lines:
pH 7.0, 70°C, wild-type enzyme
pH 7.0, 35°C, wild-type enzyme
pH 7.0, 100°C, wild-type enzyme


sequence_source: Reconstructed from UniProtKB:P81535 canonical sequence plus selected batch mutation_signature R19G/G39E/K71E/S229T

proof_lines: pH 7.0, 35°C, mutant enzyme R19G/G39E/K71E/S229T

proof_lines: pH 7.0, 70°C, mutant enzyme R19G/G39E/K71E/S229T

proof_lines: pH 7.0, 100°C, mutant enzyme R19G/G39E/K71E/S229T


sequence_source: Reconstructed from UniProtKB:P81535 canonical sequence plus selected batch mutation_signature G39E


sequence_source: UniProtKB A8WBX8 FASTA checked directly; active TrEMBL entry for Lactococcus lactis pepQ/prolidase.


substrate_name: Leu-Pro; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB A8WBX8 canonical sequence with row-specific S307D reconstruction from the selected SABIO-RK mutation signature. and applied mutation signature S307D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: Xaa-Pro dipeptidase(Enzyme) mutant S307D

substrate: Leu-Pro; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB A8WBX8 canonical sequence with row-specific S307R reconstruction from the selected SABIO-RK mutation signature. and applied mutation signature S307R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: Xaa-Pro dipeptidase(Enzyme) mutant S307R


sequence_variant_note: Resolved canonical sequence from UniProtKB A8WBX8 canonical sequence with row-specific S307G reconstruction from the selected SABIO-RK mutation signature. and applied mutation signature S307G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: Xaa-Pro dipeptidase(Enzyme) mutant S307G


sequence_variant_note: Resolved canonical sequence from UniProtKB A8WBX8 canonical sequence with row-specific R293S/S307G reconstruction from the selected SABIO-RK mutation signature. and applied mutation signature R293S/S307G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: Xaa-Pro dipeptidase(Enzyme) mutant R293S/S307G


organism: Microbacterium esteraromaticum

substrate_name: H2O; Gly-Pro

sequence_source: UniProtKB Q9WX55 FASTA checked directly; active TrEMBL entry for Microbacterium esteraromaticum prolidase.

substrate: H2O; Gly-Pro


sequence_source: UniProtKB P9WHS7 FASTA checked directly; reviewed Swiss-Prot PepE entry for Mycobacterium tuberculosis H37Rv.


substrate_name: His-Pro

sequence_source: UniProtKB:Q8P839 direct REST/FASTA lookup; RCSB 5FCF SIFTS cross-reference

substrate: His-Pro


substrate_name: Val-Pro

substrate: Val-Pro


substrate_name: Phe-Pro

substrate: Phe-Pro


sequence_variant_note: Resolved canonical sequence from UniProtKB P81535 canonical FASTA plus selected-row mutation signature reconstruction and applied mutation signature R19G/K71E/S229T to reconstruct the assayed variant sequence.


organism: Pyrococcus horikoshii


sequence_source: UniProtKB O58885 canonical FASTA


sequence_source: UniProtKB O58691 canonical FASTA, supported by PMID 22162664 PH0974/Ph1prol identity

assay_conditions_summary: pH 7; 343.15 K; buffer pH 7

column_label: Table 2 (Kinetic parameters of wild type Pyrococcus horikoshii prolidase, Ph1prol, and prolidase variants with Leu-Pro at 70 C), prolidase row 'WT-Ph1prol'; column 'Km (mM)' = 0.92 ± 0.16; column 'Vmax (umol/min/mg)' = 809 ± 55; column 'kcat (s-1)' = 1079; column 'kcat/Km (mM-1 s-1)' = 1172.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1079 s-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 1079.0 s^(-1). Km: printed Table 2 cell 0.92 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 0.92 mM. kcat/Km: printed Table 2 cell 1172 mM-1 s-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 1172.0 s^(-1)*mM^(-1); the exported kcat_over_km 1172.8260869565217 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (1079.0 / 0.92), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 2, prolidase row 'WT-Ph1prol': Km = 0.92 mM; Vmax = 809 umol/min/mg; kcat = 1079 s-1; printed kcat/Km = 1172 mM-1 s-1.

row_label: Table 2, prolidase row WT-Ph1prol

table_label: Table 2: Kinetic parameters of wild type Pyrococcus horikoshii prolidase, Ph1prol, and prolidase variants with Leu-Pro at 70 C (Archaea 2011, Article ID 565127)


sequence_variant_note: Resolved canonical sequence from UniProtKB O58691 canonical FASTA plus selected-row A195T/G306S reconstruction and applied mutation signature A195T/G306S to reconstruct the assayed variant sequence.


organism: Escherichia coli (strain K12)

substrate_name: Ala-Pro

proof_lines: Among the dipeptides described above, the highest catalytic efficiency is observed with dipeptides containing charge residues.

substrate: Ala-Pro


organism: Alteromonas sp

substrate_name: diisopropylfluorophosphate

substrate: diisopropylfluorophosphate


organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

substrate_name: Met-Pro

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

substrate: Met-Pro


organism: Solanum lycopersicum

substrate_name: Unknown

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

substrate: Unknown


enzyme_display_name: dTMP kinase

substrate_name: ATP

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines: pH 7.4, 30°C, independent of cosubstrate

enzyme: dTMP kinase

substrate: ATP


substrate_name: dTMP

substrate: dTMP


substrate_name: TMP

substrate: TMP


organism: Homo sapiens

proof_lines: wild-type enzyme fused to the protein transduction domain of Tat


organism: Pseudomonas aeruginosa

substrate_name: L-glutamate

substrate: L-glutamate


sequence_source: UniProtKB:Q40136 canonical context only

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q40136 plus selected BRENDA mutation note and applied mutation signature I149F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q40136 plus selected BRENDA mutation note and applied mutation signature S159P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q40136 plus selected BRENDA mutation note and applied mutation signature E153K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q40136 plus selected BRENDA mutation note and applied mutation signature D147G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank U27454.1 CDS 279..1094 / protein_id AAB67876.1; UniProt cross-reference Q40136 maps EMBL U27454 protein AAB67876.1 to tomato PRO1 gamma-glutamyl kinase. and applied mutation signature A62T to reconstruct the assayed variant sequence.


sequence_source: NCBI GenBank U27454.1 CDS 279..1094 / protein_id AAB67876.1; UniProt cross-reference Q40136 maps EMBL U27454 protein AAB67876.1 to tomato PRO1 gamma-glutamyl kinase.

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 NCBI GenBank U27454.1 CDS 279..1094 / protein_id AAB67876.1; UniProt cross-reference Q40136 maps EMBL U27454 protein AAB67876.1 to tomato PRO1 gamma-glutamyl kinase. and applied mutation signature I79T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank U27454.1 CDS 279..1094 / protein_id AAB67876.1; UniProt cross-reference Q40136 maps EMBL U27454 protein AAB67876.1 to tomato PRO1 gamma-glutamyl kinase. and applied mutation signature A62V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank U27454.1 CDS 279..1094 / protein_id AAB67876.1; UniProt cross-reference Q40136 maps EMBL U27454 protein AAB67876.1 to tomato PRO1 gamma-glutamyl kinase. and applied mutation signature M94T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank U27454.1 CDS 279..1094 / protein_id AAB67876.1; UniProt cross-reference Q40136 maps EMBL U27454 protein AAB67876.1 to tomato PRO1 gamma-glutamyl kinase. and applied mutation signature L154S to reconstruct the assayed variant sequence.


substrate_name: Leu-Pro

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58691 and applied mutation signature Y301C/K342N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 1; 343.15 K; buffer pH 7

column_label: Table 2 (Kinetic parameters of wild type Pyrococcus horikoshii prolidase, Ph1prol, and prolidase variants with Leu-Pro at 70 C), prolidase row 'Y301C/K342N'; column 'Km (mM)' = 2.92 ± 0.40; column 'Vmax (umol/min/mg)' = 2146 ± 177; column 'kcat (s-1)' = 2861; column 'kcat/Km (mM-1 s-1)' = 980.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2861 s-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 2861.0 s^(-1). Km: printed Table 2 cell 2.92 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 2.92 mM. kcat/Km: printed Table 2 cell 980 mM-1 s-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 980.0 s^(-1)*mM^(-1); the exported kcat_over_km 979.7945205479452 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (2861.0 / 2.92), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 2, prolidase row 'Y301C/K342N': Km = 2.92 mM; Vmax = 2146 umol/min/mg; kcat = 2861 s-1; printed kcat/Km = 980 mM-1 s-1.

row_label: Table 2, prolidase row Y301C/K342N

substrate: Leu-Pro


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58691 and applied mutation signature A195T/G306S to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of wild type Pyrococcus horikoshii prolidase, Ph1prol, and prolidase variants with Leu-Pro at 70 C), prolidase row 'A195T/G306S'; column 'Km (mM)' = 0.81 ± 0.26; column 'Vmax (umol/min/mg)' = 1245 ± 149; column 'kcat (s-1)' = 1660; column 'kcat/Km (mM-1 s-1)' = 2049.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1660 s-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 1660.0 s^(-1). Km: printed Table 2 cell 0.81 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 0.81 mM. kcat/Km: printed Table 2 cell 2049 mM-1 s-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 2049.0 s^(-1)*mM^(-1); the exported kcat_over_km 2049.3827160493825 s^(-1)*mM^(-1) is the exact full-precision quotient 1660 / 0.81 of the same two printed cells, and the printed efficiency cell is that quotient written to the precision this column uses.

raw_value_unit_evidence: Table 2, prolidase row 'A195T/G306S': Km = 0.81 mM; Vmax = 1245 umol/min/mg; kcat = 1660 s-1; printed kcat/Km = 2049 mM-1 s-1.

row_label: Table 2, prolidase row A195T/G306S

status: verified


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58691 and applied mutation signature E36V to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of wild type Pyrococcus horikoshii prolidase, Ph1prol, and prolidase variants with Leu-Pro at 70 C), prolidase row 'E36V'; column 'Km (mM)' = 1.6 ± 0.37; column 'Vmax (umol/min/mg)' = 1597 ± 174; column 'kcat (s-1)' = 2129; column 'kcat/Km (mM-1 s-1)' = 1331.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2129 s-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 2129.0 s^(-1). Km: printed Table 2 cell 1.6 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 1.6 mM. kcat/Km: printed Table 2 cell 1331 mM-1 s-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 1331.0 s^(-1)*mM^(-1); the exported kcat_over_km 1330.625 s^(-1)*mM^(-1) is the exact full-precision quotient 2129 / 1.6 of the same two printed cells, and the printed efficiency cell is that quotient written to the precision this column uses.

raw_value_unit_evidence: Table 2, prolidase row 'E36V': Km = 1.6 mM; Vmax = 1597 umol/min/mg; kcat = 2129 s-1; printed kcat/Km = 1331 mM-1 s-1.

row_label: Table 2, prolidase row E36V


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O58691 and applied mutation signature E127G/E252D to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters of wild type Pyrococcus horikoshii prolidase, Ph1prol, and prolidase variants with Leu-Pro at 70 C), prolidase row 'E127G/E252D'; column 'Km (mM)' = 0.98 ± 0.24; column 'Vmax (umol/min/mg)' = 1119 ± 101; column 'kcat (s-1)' = 1492; column 'kcat/Km (mM-1 s-1)' = 1522.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1492 s-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 1492.0 s^(-1). Km: printed Table 2 cell 0.98 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 0.98 mM. kcat/Km: printed Table 2 cell 1522 mM-1 s-1; the efficiency column of this table is already in s^-1 mM^-1, so no unit conversion applies and the printed cell is 1522.0 s^(-1)*mM^(-1); the exported kcat_over_km 1522.4489795918369 s^(-1)*mM^(-1) is the exact full-precision quotient 1492 / 0.98 of the same two printed cells, and the printed efficiency cell is that quotient written to the precision this column uses.

raw_value_unit_evidence: Table 2, prolidase row 'E127G/E252D': Km = 0.98 mM; Vmax = 1119 umol/min/mg; kcat = 1492 s-1; printed kcat/Km = 1522 mM-1 s-1.

row_label: Table 2, prolidase row E127G/E252D


sequence_source: UniProtKB:O58691 canonical sequence


proof_lines: mutant carrying a substitution of the LID domain in human enzyme by the Escherichia coli LID sequence and mutation of the P-loop Arg residue to Gly and fused to the protein transduction domain of Tat


sequence_variant_note: Resolved canonical sequence from UniProt P23919 canonical sequence with explicit F105Y reconstruction and applied mutation signature F105Y to reconstruct the assayed variant sequence.

proof_lines: mutant F105Y fused to the protein transduction domain of Tat


sequence_source: UniProt P23919 reviewed canonical sequence

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


organism: Human alphaherpesvirus 1

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

proof_lines:
verus thymidylate
versus thymidylate
versus ATP*Mg2+


organism: Mus musculus

sequence_source: UniProt P97930 reviewed canonical sequence

proof_lines:
pH 7.4, 37°C
pH 7.5, 37°C
ATP in form of MgATP2-


sequence_source: UniProt P9WKE1 reviewed canonical sequence linked to PMID 11369858

proof_lines: in 50 mM Tris-HCl pH 7.4, 50 mM KCl, 2 mM MgCl2, temperature not specified in the publication

proof_lines: pH and temperature not specified in the publication


organism: Mycobacterium tuberculosis variant bovis

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


organism: Plasmodium falciparum

proof_lines: with TMP as substrate, in Tris-HCl (50 mM, pH 7.2), phosphoenolpyruvate (0.5 mM), KCl (40 mM), MgCl2 (2 mM), at 30°C


assay_conditions_summary: pH 7.4; cofactor ATP

proof_lines: wild-type enzyme, pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme S108A, pH 7.4, temperature not specified in the publication


substrate_name: dGMP

proof_lines: mutant enzyme S108T, pH 7.4, temperature not specified in the publication

substrate: dGMP


proof_lines: mutant enzyme Y153F, pH 7.4, temperature not specified in the publication


enzyme_display_name: succinyl-CoA:acetate CoA-transferase

organism: Trichomonas vaginalis

substrate_name: succinate

assay_conditions_summary: cofactor CoA

enzyme: succinyl-CoA:acetate CoA-transferase

substrate: succinate


organism: Tritrichomonas foetus


enzyme_display_name: arylesterase

organism: Archaeoglobus fulgidus

substrate_name: ketoprofen ethyl ester

assay_conditions_summary: pH 8

enzyme: arylesterase

substrate: ketoprofen ethyl ester


organism: Bos taurus

substrate_name: phenyl acetate

proof_lines: enzyme of breed Swiss Black, pH 8.0, 25°C

substrate: phenyl acetate


organism: Cavia porcellus

substrate_name: p-nitrophenyl acetate

substrate: p-nitrophenyl acetate


organism: Felis catus

substrate_name: Alpha-naphthyl acetate

substrate: Alpha-naphthyl acetate


organism: Salmonella enterica typhimurium

substrate_name: dTTP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: wild type enzyme, apparent value, with 10 mM glucose-1-phosphate, 5 mM MgCl2, 10 units/ml inorganic pyrophosphatase, in 100 mM Tris-HCl, pH 8.0, at 37°C

proof_lines: apparent value, wild type enzyme, in 100 mM Tris-HCl, pH 8.0, at 37°C

substrate: dTTP


proof_lines: mutant enzyme Q83S, apparent value, with 10 mM glucose-1-phosphate, 5 mM MgCl2, 10 units/ml inorganic pyrophosphatase, in 100 mM Tris-HCl, pH 8.0, at 37°C

proof_lines: apparent value, mutant enzyme Q83S, in 100 mM Tris-HCl, pH 8.0, at 37°C


organism: Sphingomonas elodea

substrate_name: dTDP-glucose

proof_lines:
RmlA protein
UgpG protein

substrate: dTDP-glucose


organism: Streptococcus pneumoniae

proof_lines: cosubstrate dTTP, pH 7.5, temperature not specified in the publication

proof_lines: cosubstrate UTP, pH 7.5, temperature not specified in the publication


organism: Streptomyces globisporus


organism: Acetobacter aceti

substrate_name: succinyl-CoA

assay_conditions_summary: pH 5; cofactor CoA

proof_lines: pH: 5.0, shows an increased substrate inhibition at a lower pH

proof_lines: pH: 6.0, shows an increased substrate inhibition at a lower pH

substrate: succinyl-CoA


organism: Rattus norvegicus

substrate_name: ATP; Thiamine monophosphate

substrate: ATP; Thiamine monophosphate


organism: Saccharomyces cerevisiae


assay_conditions_summary: pH 8.5; 298.15 K; cofactor ATP

proof_lines: pH 8.5, 25°C, dTMP as variable substrate

proof_lines: pH 8.5, 25°C, with ATP as variable substrate


organism: white spot syndrome virus

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: pH 7.5, temperature not specified in the publication


organism: Yersinia pestis


organism: Acinetobacter calcoaceticus

substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


enzyme_display_name: S-methyl-5'-thioadenosine phosphorylase

organism: Arabidopsis thaliana

enzyme: S-methyl-5'-thioadenosine phosphorylase


proof_lines:
at 0.05 mM
at 0.005 mM
Raw SKiD Env: Temp=-----, pH=-----


organism: Brucella melitensis


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

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


organism: Pyrococcus horikoshii

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines:
pH 7.6, 37°C
pH 7.6, 70°C
cosubstrate UTP, pH 7.6, 37°C


organism: Salmonella enterica

substrate_name: UTP

substrate: UTP


proof_lines: mutant enzyme Q83D, apparent value, with 10 mM glucose-1-phosphate, 5 mM MgCl2, 10 units/ml inorganic pyrophosphatase, in 100 mM Tris-HCl, pH 8.0, at 37°C

proof_lines: apparent value, mutant enzyme Q83D, in 100 mM Tris-HCl, pH 8.0, at 37°C


organism: Gluconobacter oxydans

substrate_name: 1-naphthyl butyrate

proof_lines: immobilized cross-linked enzyme aggregate, at pH 7.0 and 25°C

proof_lines: immobilized cross-linked enzyme aggregate, at pH 8.0 and 30°C

substrate: 1-naphthyl butyrate


organism: Homo sapiens


organism: Lacticaseibacillus rhamnosus

substrate_name: 4-nitrophenyl laurate

substrate: 4-nitrophenyl laurate


substrate_name: adenosine

substrate: adenosine


organism: Mus musculus

substrate_name: L-citrulline

substrate: L-citrulline


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)


organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)


organism: Caldariella acidophila


organism: Drosophila melanogaster

substrate_name: phosphate

substrate: phosphate


organism: Escherichia coli

substrate_name: Unknown

substrate: Unknown


sequence_source: UniProtKB reviewed accession Q13126 (MTAP_HUMAN)

proof_lines:
recombinant enzyme
pH 7.5, 25°C
pH 7.4, 25°C


organism: Pyrococcus furiosus

sequence_source: UniProtKB reviewed accession Q8U4Q8 (MTAP_PYRFU; PF0016)


organism: Rattus norvegicus


organism: Saccharolobus solfataricus

substrate_name: Inosine

proof_lines:
pH 7.4, 70°C
recombinant enzyme

substrate: Inosine


organism: Trypanosoma brucei


organism: Mycobacterium tuberculosis


organism: Pseudomonas aeruginosa

substrate_name: TDP-glucose

substrate: TDP-glucose


organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)

substrate_name: 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (at pH 4.5 and 40 degrees Celsius)

proof_lines: kcat is 13000 min(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate. kcat is 33300 min(-1) with syringaldazine as substrate (at pH 4.5 and 40 degrees Celsius).


organism: Escherichia coli (strain K12)

proof_lines: kcat is 1450 min(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate. kcat is 21720 min(-1) with syringaldazine as substrate (at pH 4.5 and 40 degrees Celsius).

substrate: 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (at pH 4.5 and 40 degrees Celsius)


organism: Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)

proof_lines: kcat is 4.5 sec(-1) with 5'-methylthioadenosine as substrate. kcat is 6.7 sec(-1) with 5'-deoxyadenosine as substrate (PubMed:23042035). kcat is 0.06 sec(-1) with adenine as substrate (PubMed:31950558).


organism: Unknown prokaryotic organism

proof_lines: kcat is 18 sec(-1) with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) as substrate. kcat is 660 sec(-1) with syringaldazine as substrate. kcat is 1175 sec(-1) with 2,6-dimethoxyphenol as substrate (at pH 4.5 and 40 degrees Celsius).


organism: Lacticaseibacillus rhamnosus

substrate_name: 4-nitrophenyl caprate

proof_lines: N-terminal extensional long alpha-helix-deleted mutant, at pH 7.5 and 45Â°C

proof_lines: N-terminal extensional long alpha-helix- deleted mutant, at pH 7.5 and 45Â°C

substrate: 4-nitrophenyl caprate


organism: Macrobrachium lamarrei

substrate_name: beta-naphthyl acetate

substrate: beta-naphthyl acetate


organism: Oryctolagus cuniculus

substrate_name: 4-nitrophenyl acetate

assay_conditions_summary: pH 7.4; buffer 20 mM Tris-HCl

proof_lines: in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication

substrate: 4-nitrophenyl acetate


organism: Saccharococcus caldoxylosilyticus


proof_lines: mutant enzyme PHPM1, at pH 8.0 and 50Â°C

proof_lines: mutant enzyme PHPM1-M2, at pH 8.0 and 50Â°C

proof_lines: mutant enzyme PHPM1-M2-M3, at pH 8.0 and 50Â°C


organism: Triticum aestivum


organism: Aspergillus ficuum

substrate_name: Tannic acid

substrate: Tannic acid


organism: Aspergillus flavus


organism: Aspergillus fumigatus


organism: Aspergillus nidulans

substrate_name: propyl gallate

substrate: propyl gallate


organism: Aspergillus niger

substrate_name: gallotannin

assay_conditions_summary: pH 5; 303.15 K; buffer 50 mM citrate

proof_lines: at 30°C, in 50 mM citrate buffer at pH 5.0

proof_lines: at 20°C, in 50 mM citrate buffer at pH 5.0

substrate: gallotannin


enzyme_display_name: adenosine kinase

organism: Unknown

substrate_name: ATP

assay_conditions_summary: cofactor ATP

enzyme: adenosine kinase

substrate: ATP


organism: Leishmania donovani

substrate_name: Adenosine; ATP

sequence_variant_note: Resolved canonical sequence from UniProt REST direct check for O96439 plus SABIO-RK PMID 15606359 source hints and applied mutation signature R69K/R131A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine kinase(Enzyme) mutant R69K, R131A

substrate: Adenosine; ATP


substrate_name: ATP; Adenosine

sequence_variant_note: Resolved canonical sequence from UniProt REST direct check for O96439 plus SABIO-RK PMID 15606359 source hints and applied mutation signature R69A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine kinase(Enzyme) mutant R69A

substrate: ATP; Adenosine


sequence_variant_note: Resolved canonical sequence from UniProt REST direct check for O96439 plus SABIO-RK PMID 15606359 source hints and applied mutation signature G62D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine kinase(Enzyme) mutant G62D


organism: Mus musculus

sequence_source: identity reuse cache plus UniProt REST direct check for P55264

proof_lines: recombinant isozymes AK-S and AK-L, pH 7.5, 37°C


organism: Mycobacterium tuberculosis

sequence_source: identity reuse cache plus UniProt REST direct check for A5U4N0

proof_lines: native enzyme, pH 8.0, 37°C, in presence of 10 mM KCl

proof_lines: native enzyme, pH 8.0, 37°C, in absence of KCl


sequence_source: UniProt REST direct check for P9WID5 plus BRENDA/SKiD source hints

proof_lines: pH 7.5, temperature not specified in the publication


organism: Toxoplasma gondii

sequence_source: UniProt REST direct check for Q9TVW2 plus BRENDA/SKiD source hints

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


organism: Arabidopsis thaliana


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Homo sapiens

sequence_source: UniProtKB:P55263 direct FASTA/JSON lookup; canonical sequence only

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


sequence_source: UniProtKB:P55263 direct FASTA/JSON lookup

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


substrate_name: ATP; 2'-Deoxycytidine

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

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

source_databases_merged: sabio_rk brenda skid

substrate: ATP; 2'-Deoxycytidine


sequence_variant_note: Resolved canonical sequence from UniProtKB:O96439 direct FASTA/JSON lookup plus PMID 15606359 mutation context and applied mutation signature R131A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine kinase(Enzyme) mutant R131A


sequence_source: UniProtKB:O96439 direct FASTA/JSON lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:O96439 direct FASTA/JSON lookup plus PMID 15606359 mutation context and applied mutation signature R69K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosine kinase(Enzyme) mutant R69K


organism: Anopheles gambiae

substrate_name: TTP; adenosine; CTP; ATP; GTP; UTP

assay_conditions_summary: pH 7.4; 300.15 K; buffer 50 mM Tris; cofactor ATP

proof_lines: with GTP as cosubstrate, at 27°C in 50 mM Tris buffer (pH 7.4) containing 5 mM MgCl2, 50 mM KCl, and 0.2 mM dithiothreitol

proof_lines: with ATP as cosubstrate, at 27°C in 50 mM Tris buffer (pH 7.4) containing 5 mM MgCl2, 50 mM KCl, and 0.2 mM dithiothreitol

substrate: TTP; adenosine; CTP; ATP; GTP; UTP


organism: Babesia canis rossi

substrate_name: adenosine

sequence_source: NCBI Protein CAA11263.1 / EMBL AJ223322.1; PMID 10518797; UniProtKB/TrEMBL O44015 cross-reference

substrate: adenosine


organism: Bombyx mori

sequence_source: UniProtKB/TrEMBL Q2F635; PMID 29803677 full text reports BmADK as a 1050 bp/349 aa cloned sequence


organism: Bos taurus

substrate_name: adenosine; ATP

proof_lines: pH 7.5, 37ºC, with respect to adenosine and MgATP2-

substrate: adenosine; ATP


organism: Cavia porcellus


organism: Cricetulus griseus

substrate_name: adenosine; viramidine; ribavirin

assay_conditions_summary: pH 7.2; 310.15 K; buffer recombinant enzyme

proof_lines: recombinant enzyme, pH 7.2, 37°C, in presence of 10 mM phosphate

proof_lines: recombinant enzyme, pH 9.0, 37°C, phosphate buffered saline

proof_lines: recombinant enzyme, pH 7.2, 37°C, in presence of 20 mM phosphoenolpyruvate

substrate: adenosine; viramidine; ribavirin


sequence_variant_note: Resolved canonical sequence from UniProtKB P55263 direct REST/FASTA accession lookup; Q78A reconstructed with paper-numbering offset +17 and applied mutation signature Q78A with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P55263 direct REST/FASTA accession lookup; K341A reconstructed with paper-numbering offset +17 and applied mutation signature K341A with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P55263 direct REST/FASTA accession lookup; K341A reconstructed with paper-numbering offset +17


sequence_variant_note: Resolved canonical sequence from UniProtKB P55263 direct REST/FASTA accession lookup; Q74A reconstructed with paper-numbering offset +17 and applied mutation signature Q74A with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P55263 direct REST/FASTA accession lookup; Q78A reconstructed with paper-numbering offset +17


sequence_variant_note: Resolved canonical sequence from UniProtKB P55263 direct REST/FASTA accession lookup; F338A reconstructed with paper-numbering offset +17 and applied mutation signature F338A with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P55263 direct REST/FASTA accession lookup; canonical displayed sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB P55263 direct REST/FASTA accession lookup; H107A reconstructed with paper-numbering offset +17 and applied mutation signature H107A with inferred residue-numbering offset +17 to reconstruct the assayed variant sequence.


proof_lines: kcat is 0.19 sec(-1) with adenosine as substrate. kcat is 0.28 sec(-1) with N(6)-methyladenosine (m6A) as substrate. kcat is 0.27 sec(-1) with N(6),N(6)-dimethyladenosine as substrate. kcat is 0.18 sec(-1) with N(6)-isopentenyladenosine (i6


organism: Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)

substrate_name: adenosine (in the presence of 10 mM KCl)

proof_lines: GTP and dGTP are the best phosphate donors, with 2.5 and 4.7 times the activity observed with ATP, respectively. UTP, dATP, and dTTP exhibit about 33% of the activity observed with ATP, while CTP and dCTP are the worst phosphate donors, wit


organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

substrate_name: guanosine (at pH 8.0 and 22 degrees Celsius)

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: kcat is 0.072 sec(-1) with ATP and guanosine as substrates. kcat is 0.16 sec(-1) with ATP and inosine as substrates. kcat is 0.064 sec(-1) with ATP and cytidine as substrates. kcat is 0.084 sec(-1) with ATP and adenosine as substrates. kcat


organism: Brucella melitensis


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


sequence_source: UniProtKB Q13126 FASTA direct lookup on 2026-06-05 (MTAP_HUMAN).

proof_lines:
pH 7.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7


sequence_source: UniProtKB Q8IV20 FASTA direct lookup on 2026-06-05 (LACC1_HUMAN).


organism: Mycobacterium smegmatis

sequence_source: UniProtKB A0QR54 FASTA direct lookup on 2026-06-05 (MTAP_MYCS2).


organism: Schistosoma mansoni

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup for I0B503 on 2026-06-05 and applied mutation signature S12T/N87T to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S12T/N87T, at pH 7.4 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:I0B503 and applied mutation signature S12T/N87T to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), adenosine block, enzyme row 2M; column KM (uM) = 3.68 ± 0.14; column kcat (s^-1) = 308.9 ± 4.48; column Vmax (nM/min) = 30.89; column kcat/Km (s^-1 uM^-1) = 83.94 ± 3.42.

normalized_value_unit_evidence: kcat: printed Table 2 cell 308.9 s^-1; already in s^-1, so no conversion is applied; the exported value is 308.9 s^(-1). Km: printed Table 2 cell 3.68 uM; 3.68 / 1000 = 0.00368 mM; the exported value is 0.00368 mM. kcat/Km: printed Table 2 cell 83.94 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 83.94 * 1000 = 83940.0 s^-1 mM^-1; the exported value is 83940.21739130434.

raw_value_unit_evidence: Table 2, adenosine block, enzyme row 2M: KM = 3.68 ± 0.14 uM; kcat = 308.9 ± 4.48 s^-1; printed kcat/Km = 83.94 ± 3.42 s^-1 uM^-1.

row_label: Table 2, adenosine block, enzyme row 2M

table_label: Table 2: Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis (PLoS Negl Trop Dis 2016, 10(12): e0005178)


sequence_source: UniProtKB direct accession lookup for I0B503 on 2026-06-05


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:I0B503 and applied mutation signature S12T to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), adenosine block, enzyme row S12T; column KM (uM) = 2.1 ± 0.13; column kcat (s^-1) = 98.42 ± 2.36; column Vmax (nM/min) = 36.91; column kcat/Km (s^-1 uM^-1) = 46.86 + 3.11.

normalized_value_unit_evidence: kcat: printed Table 2 cell 98.42 s^-1; already in s^-1, so no conversion is applied; the exported value is 98.42 s^(-1). Km: printed Table 2 cell 2.1 uM; 2.1 / 1000 = 0.0021 mM; the exported value is 0.0021 mM. kcat/Km: printed Table 2 cell 46.86 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 46.86 * 1000 = 46860.0 s^-1 mM^-1; the exported value is 46866.66666666667.

raw_value_unit_evidence: Table 2, adenosine block, enzyme row S12T: KM = 2.1 ± 0.13 uM; kcat = 98.42 ± 2.36 s^-1; printed kcat/Km = 46.86 + 3.11 s^-1 uM^-1.


sequence_source: UniProtKB direct accession lookup for Q2F635 on 2026-06-05


sequence_source: UniProtKB direct accession lookup for P55263 on 2026-06-05; row-specific F338A sequence unresolved


sequence_source: UniProtKB direct accession lookup for P55263 on 2026-06-05; row-specific H107A sequence unresolved


substrate_name: phosphate

sequence_source: UniProt REST O06401 FASTA/TSV retrieved 2026-06-05

proof_lines: pH and temperature not specified in the publication, co-substrate: 0.2 mM 5-methylthioadenosine

proof_lines: pH and temperature not specified in the publication, co-substrate: 50 mM phosphate

substrate: phosphate


organism: Pyrococcus furiosus

sequence_source: UniProt REST Q8U4Q8 FASTA/TSV retrieved 2026-06-05


organism: Saccharolobus solfataricus

sequence_source: UniProt REST P50389 FASTA/TSV retrieved 2026-06-05


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:I0B503 and applied mutation signature S12T/N87T/Q289L to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), 2'deoxy adenosine block, enzyme row 3M; column KM (uM) = 6.52 ± 0.32; column kcat (s^-1) = 299.2 ± 5.28; column Vmax (nM/min) = 29.92; column kcat/Km (s^-1 uM^-1) = 45.88 ± 2.39.

normalized_value_unit_evidence: kcat: printed Table 2 cell 299.2 s^-1; already in s^-1, so no conversion is applied; the exported value is 299.2 s^(-1). Km: printed Table 2 cell 6.52 uM; 6.52 / 1000 = 0.00652 mM; the exported value is 0.00652 mM. kcat/Km: printed Table 2 cell 45.88 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 45.88 * 1000 = 45880.0 s^-1 mM^-1; the exported value is 45889.57055214724.

raw_value_unit_evidence: Table 2, 2'deoxy adenosine block, enzyme row 3M: KM = 6.52 ± 0.32 uM; kcat = 299.2 ± 5.28 s^-1; printed kcat/Km = 45.88 ± 2.39 s^-1 uM^-1.


column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), adenosine block, enzyme row 3M; column KM (uM) = 7.35 ± 0.36; column kcat (s^-1) = 280.3 ± 5.09; column Vmax (nM/min) = 28.03; column kcat/Km (s^-1 uM^-1) = 38.13 ± 1.99.

normalized_value_unit_evidence: kcat: printed Table 2 cell 280.3 s^-1; already in s^-1, so no conversion is applied; the exported value is 280.3 s^(-1). Km: printed Table 2 cell 7.35 uM; 7.35 / 1000 = 0.00735 mM; the exported value is 0.00735 mM. kcat/Km: printed Table 2 cell 38.13 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 38.13 * 1000 = 38130.0 s^-1 mM^-1; the exported value is 38136.05442176871.

raw_value_unit_evidence: Table 2, adenosine block, enzyme row 3M: KM = 7.35 ± 0.36 uM; kcat = 280.3 ± 5.09 s^-1; printed kcat/Km = 38.13 ± 1.99 s^-1 uM^-1.

row_label: Table 2, adenosine block, enzyme row 3M


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:I0B503 and applied mutation signature N87T to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), 2'deoxy adenosine block, enzyme row N87T; column KM (uM) = 10.33 ± 0.78; column kcat (s^-1) = 441.2 ± 16.23; column Vmax (nM/min) = 41.04; column kcat/Km (s^-1 uM^-1) = 42.71 3.59.

normalized_value_unit_evidence: kcat: printed Table 2 cell 441.2 s^-1; already in s^-1, so no conversion is applied; the exported value is 441.2 s^(-1). Km: printed Table 2 cell 10.33 uM; 10.33 / 1000 = 0.01033 mM; the exported value is 0.01033 mM. kcat/Km: printed Table 2 cell 42.71 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 42.71 * 1000 = 42710.0 s^-1 mM^-1; the exported value is 42710.55179090029.

raw_value_unit_evidence: Table 2, 2'deoxy adenosine block, enzyme row N87T: KM = 10.33 ± 0.78 uM; kcat = 441.2 ± 16.23 s^-1; printed kcat/Km = 42.71 3.59 s^-1 uM^-1.


sequence_source: UniProt REST I0B503 FASTA/TSV retrieved 2026-06-05

column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), MTA block, enzyme row Wild Type; column KM (uM) = 3.63 ± 0.14; column kcat (s^-1) = 443.8 ± 5.72; column Vmax (nM/min) = 66.57; column kcat/Km (s^-1 uM^-1) = 122.25 ± 4.97.

normalized_value_unit_evidence: kcat: printed Table 2 cell 443.8 s^-1; already in s^-1, so no conversion is applied; the exported value is 443.8 s^(-1). Km: printed Table 2 cell 3.63 uM; 3.63 / 1000 = 0.00363 mM; the exported value is 0.00314 mM. kcat/Km: printed Table 2 cell 122.25 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 122.25 * 1000 = 122250.0 s^-1 mM^-1; the exported value is not stored for this row.

raw_value_unit_evidence: Table 2, MTA block, enzyme row Wild Type: KM = 3.63 ± 0.14 uM; kcat = 443.8 ± 5.72 s^-1; printed kcat/Km = 122.25 ± 4.97 s^-1 uM^-1.


column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), MTA block, enzyme row 3M; column KM (uM) = 3.12 ± 0.12; column kcat (s^-1) = 253.9 ± 3.61; column Vmax (nM/min) = 25.39; column kcat/Km (s^-1 uM^-1) = 81.37 ± 3.34.

normalized_value_unit_evidence: kcat: printed Table 2 cell 253.9 s^-1; already in s^-1, so no conversion is applied; the exported value is 253.9 s^(-1). Km: printed Table 2 cell 3.12 uM; 3.12 / 1000 = 0.00312 mM; the exported value is 0.00312 mM. kcat/Km: printed Table 2 cell 81.37 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 81.37 * 1000 = 81370.0 s^-1 mM^-1; the exported value is 81378.20512820513.

raw_value_unit_evidence: Table 2, MTA block, enzyme row 3M: KM = 3.12 ± 0.12 uM; kcat = 253.9 ± 3.61 s^-1; printed kcat/Km = 81.37 ± 3.34 s^-1 uM^-1.

row_label: Table 2, MTA block, enzyme row 3M


column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), 2'deoxy adenosine block, enzyme row 2M; column KM (uM) = 3.89 ± 0.16; column kcat (s^-1) = 372.8 ± 6.31; column Vmax (nM/min) = 37.28; column kcat/Km (s^-1 uM^-1) = 95.83 ± 4.26.

normalized_value_unit_evidence: kcat: printed Table 2 cell 372.8 s^-1; already in s^-1, so no conversion is applied; the exported value is 372.8 s^(-1). Km: printed Table 2 cell 3.89 uM; 3.89 / 1000 = 0.00389 mM; the exported value is 0.00389 mM. kcat/Km: printed Table 2 cell 95.83 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 95.83 * 1000 = 95830.0 s^-1 mM^-1; the exported value is 95835.47557840617.

raw_value_unit_evidence: Table 2, 2'deoxy adenosine block, enzyme row 2M: KM = 3.89 ± 0.16 uM; kcat = 372.8 ± 6.31 s^-1; printed kcat/Km = 95.83 ± 4.26 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:I0B503 and applied mutation signature Q289L to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), MTA block, enzyme row Q289L; column KM (uM) = 2.49 ± 0.1; column kcat (s^-1) = 241.6 ± 3.91; column Vmax (nM/min) = 72.48; column kcat/Km (s^-1 uM^-1) = 97.02 ± 4.20.

normalized_value_unit_evidence: kcat: printed Table 2 cell 241.6 s^-1; already in s^-1, so no conversion is applied; the exported value is 241.6 s^(-1). Km: printed Table 2 cell 2.49 uM; 2.49 / 1000 = 0.00249 mM; the exported value is 0.00249 mM. kcat/Km: printed Table 2 cell 97.02 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 97.02 * 1000 = 97020.0 s^-1 mM^-1; the exported value is 97028.1124497992.

raw_value_unit_evidence: Table 2, MTA block, enzyme row Q289L: KM = 2.49 ± 0.1 uM; kcat = 241.6 ± 3.91 s^-1; printed kcat/Km = 97.02 ± 4.20 s^-1 uM^-1.

row_label: Table 2, MTA block, enzyme row Q289L


column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), MTA block, enzyme row 2M; column KM (uM) = 2.12 ± 0.08; column kcat (s^-1) = 416.2 ± 7.20; column Vmax (nM/min) = 41.62; column kcat/Km (s^-1 uM^-1) = 196.32 ± 8.15.

normalized_value_unit_evidence: kcat: printed Table 2 cell 416.2 s^-1; already in s^-1, so no conversion is applied; the exported value is 416.2 s^(-1). Km: printed Table 2 cell 2.12 uM; 2.12 / 1000 = 0.00212 mM; the exported value is 0.002124 mM. kcat/Km: printed Table 2 cell 196.32 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 196.32 * 1000 = 196320.0 s^-1 mM^-1; the exported value is 195951.03578154425.

raw_value_unit_evidence: Table 2, MTA block, enzyme row 2M: KM = 2.12 ± 0.08 uM; kcat = 416.2 ± 7.20 s^-1; printed kcat/Km = 196.32 ± 8.15 s^-1 uM^-1.

row_label: Table 2, MTA block, enzyme row 2M


sequence_variant_note: Resolved canonical sequence from UniProtKB:I0B503 canonical sequence with reconstructed N87T variant; substrate tuple unresolved and applied mutation signature N87T to reconstruct the assayed variant sequence.


column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), MTA block, enzyme row S12T; column KM (uM) = 1.22 ± 0.09; column kcat (s^-1) = 145.1 ± 4.53; column Vmax (nM/min) = 54.4; column kcat/Km (s^-1 uM^-1) = 118.93 ± 9.53.

normalized_value_unit_evidence: kcat: printed Table 2 cell 145.1 s^-1; already in s^-1, so no conversion is applied; the exported value is 145.1 s^(-1). Km: printed Table 2 cell 1.22 uM; 1.22 / 1000 = 0.00122 mM; the exported value is 0.00122 mM. kcat/Km: printed Table 2 cell 118.93 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 118.93 * 1000 = 118930.0 s^-1 mM^-1; the exported value is 118934.4262295082.

raw_value_unit_evidence: Table 2, MTA block, enzyme row S12T: KM = 1.22 ± 0.09 uM; kcat = 145.1 ± 4.53 s^-1; printed kcat/Km = 118.93 ± 9.53 s^-1 uM^-1.

row_label: Table 2, MTA block, enzyme row S12T


sequence_source: UniProtKB:I0B503 canonical wild-type sequence; selected OED source accession exact match


column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), 2'deoxy adenosine block, enzyme row S12T; column KM (uM) = 0.99 ± 0.09; column kcat (s^-1) = 48.44 ± 1.40; column Vmax (nM/min) = 18.18; column kcat/Km (s^-1 uM^-1) = 48.92 ±4.67.

normalized_value_unit_evidence: kcat: printed Table 2 cell 48.44 s^-1; already in s^-1, so no conversion is applied; the exported value is 48.44 s^(-1). Km: printed Table 2 cell 0.99 uM; 0.99 / 1000 = 0.00099 mM; the exported value is 0.00099 mM. kcat/Km: printed Table 2 cell 48.92 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 48.92 * 1000 = 48920.0 s^-1 mM^-1; the exported value is 48929.292929292926.

raw_value_unit_evidence: Table 2, 2'deoxy adenosine block, enzyme row S12T: KM = 0.99 ± 0.09 uM; kcat = 48.44 ± 1.40 s^-1; printed kcat/Km = 48.92 ±4.67 s^-1 uM^-1.


column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), MTA block, enzyme row N87T; column KM (uM) = 0.71 ± 0.04; column kcat (s^-1) = 84.62 ± 2.24; column Vmax (nM/min) = 31.73; column kcat/Km (s^-1 uM^-1) = 119.18 ± 7.42.

normalized_value_unit_evidence: kcat: printed Table 2 cell 84.62 s^-1; already in s^-1, so no conversion is applied; the exported value is 84.62 s^(-1). Km: printed Table 2 cell 0.71 uM; 0.71 / 1000 = 0.00071 mM; the exported value is 0.00071 mM. kcat/Km: printed Table 2 cell 119.18 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 119.18 * 1000 = 119180.0 s^-1 mM^-1; the exported value is 119183.0985915493.

raw_value_unit_evidence: Table 2, MTA block, enzyme row N87T: KM = 0.71 ± 0.04 uM; kcat = 84.62 ± 2.24 s^-1; printed kcat/Km = 119.18 ± 7.42 s^-1 uM^-1.

row_label: Table 2, MTA block, enzyme row N87T


sequence_variant_note: Resolved canonical sequence from UniProtKB:I0B503 direct JSON/FASTA lookup; variant reconstructed from canonical residue checks and PMID 27935959 mutation label. and applied mutation signature S12T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:I0B503 direct JSON/FASTA lookup; variant reconstructed from canonical residue checks and PMID 27935959 mutation label. and applied mutation signature S12T/N87T/Q289L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S12T/N87T/Q289L, at pH 7.4 and 25°C


sequence_source: UniProtKB:I0B503 direct JSON/FASTA 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:I0B503 direct JSON/FASTA lookup; variant reconstructed from canonical residue checks and PMID 27935959 mutation label. and applied mutation signature Q289L to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:I0B503 direct JSON/FASTA lookup; variant reconstructed from canonical residue checks and PMID 27935959 mutation label.


column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), adenosine block, enzyme row N87T; column KM (uM) = 3.3 ± 0.21; column kcat (s^-1) = 62.63 ± 1.51; column Vmax (nM/min) = 23.49; column kcat/Km (s^-1 uM^-1) = 18.97 + 1.29.

normalized_value_unit_evidence: kcat: printed Table 2 cell 62.63 s^-1; already in s^-1, so no conversion is applied; the exported value is 62.63 s^(-1). Km: printed Table 2 cell 3.3 uM; 3.3 / 1000 = 0.0033 mM; the exported value is 0.0033 mM. kcat/Km: printed Table 2 cell 18.97 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 18.97 * 1000 = 18970.0 s^-1 mM^-1; the exported value is 18978.78787878788.

raw_value_unit_evidence: Table 2, adenosine block, enzyme row N87T: KM = 3.3 ± 0.21 uM; kcat = 62.63 ± 1.51 s^-1; printed kcat/Km = 18.97 + 1.29 s^-1 uM^-1.


column_label: Table 2 (Kinetic parameters for wt SmMTAP and their mutants for adenosine, MTA, 2'-deoxyadenosine, and for adenosine hydrolysis), adenosine block, enzyme row Q289L; column KM (uM) = 1.81 ± 0.08; column kcat (s^-1) = 95.79 ± 1.69; column Vmax (nM/min) = 35.92; column kcat/Km (s^-1 uM^-1) = 54.58 ± 2.59.

normalized_value_unit_evidence: kcat: printed Table 2 cell 95.79 s^-1; already in s^-1, so no conversion is applied; the exported value is 95.79 s^(-1). Km: printed Table 2 cell 1.81 uM; 1.81 / 1000 = 0.00181 mM; the exported value is 0.00181 mM. kcat/Km: printed Table 2 cell 54.58 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 54.58 * 1000 = 54580.0 s^-1 mM^-1; the exported value is 52922.65193370166.

raw_value_unit_evidence: Table 2, adenosine block, enzyme row Q289L: KM = 1.81 ± 0.08 uM; kcat = 95.79 ± 1.69 s^-1; printed kcat/Km = 54.58 ± 2.59 s^-1 uM^-1.


enzyme_display_name: adenosylhomocysteine nucleosidase

substrate_name: S-adenosyl-L-homocysteine

sequence_source: UniProtKB:Q7XA67 direct lookup on 2026-06-05

assay_conditions_summary: pH 8; 310.15 K; buffer 100 mM sodium phosphate

proof_lines: in 100 mM sodium phosphate buffer, at pH 8.0 and 37°C

enzyme: adenosylhomocysteine nucleosidase

substrate: S-adenosyl-L-homocysteine


organism: Borreliella burgdorferi

sequence_source: UniProtKB:O50860 direct lookup on 2026-06-05

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication


sequence_source: UniProtKB:O50162 direct lookup on 2026-06-05

assay_conditions_summary: pH 5

proof_lines: pH 5.0, temperature not specified in the publication


sequence_source: UniProtKB:O51534 direct lookup on 2026-06-05


organism: Campylobacter jejuni

sequence_source: UniProtKB:Q0PC20 direct lookup on 2026-06-05

assay_conditions_summary: pH 7; 298.15 K; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer, pH 7.0, at 25°C


organism: Escherichia coli

substrate_name: H2O; 5'-Deoxy-5'-(methylthio)adenosine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature S76A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters for Ribose Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 2, enzyme row Ser76Ala, substrate row MTA; column Km (uM) cell = 2.7; column kcat (s-1) cell = 1.3; column kcat/Km (s-1 uM-1) cell = 0.5; column catalytic efficiency (%) cell = 13.4; column apparent Tma (C) cell = 70. captured primary segment: MTA | S76A MTAN | Table 2 | pH 7.0 | Km 2.7 uM | kcat 1.3 s^-1 | kcat/Km 0.5 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 2.7 uM; 1 uM is 1/1000 mM, so 2.7 / 1000 = 0.0027 mM. kcat: printed Table 2 kcat cell 1.3 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 1.3 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 0.5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.5 x 1000 = 500.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.3 / 0.0027 = 481.48148148148147 s^-1 mM^-1, beside the printed efficiency cell 500.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 2, enzyme row Ser76Ala, substrate row MTA: Km = 2.7 uM; kcat = 1.3 s^-1; kcat/Km = 0.5 s^-1 uM^-1.

substrate: H2O; 5'-Deoxy-5'-(methylthio)adenosine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature F105A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Phe105Ala, substrate row MTA; column Km (uM) cell = 3.3; column kcat (s-1) cell = 10.2; column kcat/Km (s-1 uM-1) cell = 3.1; column catalytic efficiency (%) cell = 87.4; column apparent Tma (C) cell = 66. captured primary segment: MTA | F105A MTAN | Table 3 | pH 7.0 | Km 3.3 uM | kcat 10.2 s^-1 | kcat/Km 3.1 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 3.3 uM; 1 uM is 1/1000 mM, so 3.3 / 1000 = 0.0033 mM. kcat: printed Table 3 kcat cell 10.2 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 10.2 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 3.1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 3.1 x 1000 = 3100.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 10.2 / 0.0033 = 3090.9090909090905 s^-1 mM^-1, beside the printed efficiency cell 3100.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Phe105Ala, substrate row MTA: Km = 3.3 uM; kcat = 10.2 s^-1; kcat/Km = 3.1 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AF12 direct lookup on 2026-06-05 plus direct F151A substitution from selected mutation_signature and applied mutation signature F151A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosylhomocysteine nucleosidase(Enzyme) mutant F151A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature S196A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Parameters for Purine Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11052 (PDF page 4). Table 1, enzyme row Ser196Ala, substrate row MTA; column Km (uM) cell = 2.9; column kcat (s-1) cell = 0.23; column kcat/Km (s-1 uM-1) cell = 0.081; column catalytic efficiency (%) cell = 2.3; column apparent Tma (C) cell = 66. captured primary segment: MTA | S196A MTAN | Table 1 | pH 7.0 | Km 2.9 uM | kcat 0.23 s^-1 | kcat/Km 0.081 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 2.9 uM; 1 uM is 1/1000 mM, so 2.9 / 1000 = 0.0029 mM. kcat: printed Table 1 kcat cell 0.23 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.23 s^(-1). kcat/Km: printed Table 1 kcat/Km cell 0.081 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.081 x 1000 = 81.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.23 / 0.0029 = 79.31034482758622 s^-1 mM^-1, beside the printed efficiency cell 81.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11052, Table 1, enzyme row Ser196Ala, substrate row MTA: Km = 2.9 uM; kcat = 0.23 s^-1; kcat/Km = 0.081 s^-1 uM^-1.


row_label: Table 2, enzyme row Ser76Ala, substrate row MTA

table_label: Table 2: Kinetic Parameters for Ribose Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C)


substrate_name: S-Adenosyl-L-homocysteine

column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Phe105Ala, substrate row AdoHcy; column Km (uM) cell = 2.8; column kcat (s-1) cell = 7.5; column kcat/Km (s-1 uM-1) cell = 2.7; column catalytic efficiency (%) cell = 128; column apparent Tma (C) prints one cell per enzyme, on the MTA line of that enzyme. captured primary segment: AdoHcy | F105A MTAN | Table 3 | pH 7.0 | Km 2.8 uM | kcat 7.5 s^-1 | kcat/Km 2.7 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 2.8 uM; 1 uM is 1/1000 mM, so 2.8 / 1000 = 0.0028 mM. kcat: printed Table 3 kcat cell 7.5 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 7.5 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 2.7 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.7 x 1000 = 2700.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 7.5 / 0.0028 = 2678.5714285714284 s^-1 mM^-1, beside the printed efficiency cell 2700.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Phe105Ala, substrate row AdoHcy: Km = 2.8 uM; kcat = 7.5 s^-1; kcat/Km = 2.7 s^-1 uM^-1.

substrate: S-Adenosyl-L-homocysteine


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AF12 canonical sequence with selected mutation_signature applied and applied mutation signature M9A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature I50A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Ile50Ala, substrate row MTA; column Km (uM) cell = 7.1; column kcat (s-1) cell = 3.0; column kcat/Km (s-1 uM-1) cell = 0.42; column catalytic efficiency (%) cell = 11.8; column apparent Tma (C) cell = 75. captured primary segment: MTA | I50A MTAN | Table 3 | pH 7.0 | Km 7.1 uM | kcat 3.0 s^-1 | kcat/Km 0.42 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 7.1 uM; 1 uM is 1/1000 mM, so 7.1 / 1000 = 0.0071 mM. kcat: printed Table 3 kcat cell 3.0 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 3.0 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 0.42 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.42 x 1000 = 420.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.0 / 0.0071 = 422.53521126760563 s^-1 mM^-1, beside the printed efficiency cell 420.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Ile50Ala, substrate row MTA: Km = 7.1 uM; kcat = 3.0 s^-1; kcat/Km = 0.42 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature M173A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters for Ribose Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 2, enzyme row Met173Ala, substrate row AdoHcy; column Km (uM) cell = 490; column kcat (s-1) cell = 0.8; column kcat/Km (s-1 uM-1) cell = 0.0017; column catalytic efficiency (%) cell = 0.1; column apparent Tma (C) prints one cell per enzyme, on the MTA line of that enzyme. captured primary segment: AdoHcy | M173A MTAN | Table 2 | pH 7.0 | Km 490 uM | kcat 0.8 s^-1 | kcat/Km 0.0017 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 490 uM; 1 uM is 1/1000 mM, so 490 / 1000 = 0.49 mM. kcat: printed Table 2 kcat cell 0.8 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.8 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 0.0017 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.0017 x 1000 = 1.7 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.8 / 0.49 = 1.6326530612244898 s^-1 mM^-1, beside the printed efficiency cell 1.7 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 2, enzyme row Met173Ala, substrate row AdoHcy: Km = 490 uM; kcat = 0.8 s^-1; kcat/Km = 0.0017 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AF12 canonical sequence with selected mutation_signature applied and applied mutation signature R193A to reconstruct the assayed variant sequence.


substrate_name: 5'-Deoxy-5'-(methylthio)adenosine; H2O

row_label: Table 1, enzyme row Ser196Ala, substrate row MTA

table_label: Table 1: Kinetic Parameters for Purine Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C)

substrate: 5'-Deoxy-5'-(methylthio)adenosine; H2O


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature M9A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Met9Ala, substrate row MTA; column Km (uM) cell = 1.4; column kcat (s-1) cell = 0.63; column kcat/Km (s-1 uM-1) cell = 0.5; column catalytic efficiency (%) cell = 12.6; column apparent Tma (C) cell = 71. captured primary segment: MTA | M9A MTAN | Table 3 | pH 7.0 | Km 1.4 uM | kcat 0.63 s^-1 | kcat/Km 0.5 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 1.4 uM; 1 uM is 1/1000 mM, so 1.4 / 1000 = 0.0014 mM. kcat: printed Table 3 kcat cell 0.63 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.63 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 0.5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.5 x 1000 = 500.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.63 / 0.0014 = 450.0 s^-1 mM^-1, beside the printed efficiency cell 500.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Met9Ala, substrate row MTA: Km = 1.4 uM; kcat = 0.63 s^-1; kcat/Km = 0.5 s^-1 uM^-1.


row_label: Table 3, enzyme row Ile50Ala, substrate row MTA

table_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C)


column_label: Table 2: Kinetic Parameters for Ribose Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 2, enzyme row Met173Ala, substrate row MTA; column Km (uM) cell = 34; column kcat (s-1) cell = 0.72; column kcat/Km (s-1 uM-1) cell = 0.021; column catalytic efficiency (%) cell = 0.6; column apparent Tma (C) cell = 71. captured primary segment: MTA | M173A MTAN | Table 2 | pH 7.0 | Km 34 uM | kcat 0.72 s^-1 | kcat/Km 0.021 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 2 Km cell 34 uM; 1 uM is 1/1000 mM, so 34 / 1000 = 0.034 mM. kcat: printed Table 2 kcat cell 0.72 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.72 s^(-1). kcat/Km: printed Table 2 kcat/Km cell 0.021 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.021 x 1000 = 21.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.72 / 0.034 = 21.176470588235293 s^-1 mM^-1, beside the printed efficiency cell 21.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 2, enzyme row Met173Ala, substrate row MTA: Km = 34 uM; kcat = 0.72 s^-1; kcat/Km = 0.021 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature V102A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Val102Ala, substrate row MTA; column Km (uM) cell = 3.0; column kcat (s-1) cell = 10.2; column kcat/Km (s-1 uM-1) cell = 3.4; column catalytic efficiency (%) cell = 95.0; column apparent Tma (C) cell = 67. captured primary segment: MTA | V102A MTAN | Table 3 | pH 7.0 | Km 3.0 uM | kcat 10.2 s^-1 | kcat/Km 3.4 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 3.0 uM; 1 uM is 1/1000 mM, so 3.0 / 1000 = 0.003 mM. kcat: printed Table 3 kcat cell 10.2 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 10.2 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 3.4 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 3.4 x 1000 = 3400.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 10.2 / 0.003 = 3399.9999999999995 s^-1 mM^-1, beside the printed efficiency cell 3400.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Val102Ala, substrate row MTA: Km = 3.0 uM; kcat = 10.2 s^-1; kcat/Km = 3.4 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprotkb:P0AF12:F151A and applied mutation signature F151A to reconstruct the assayed variant sequence.


column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Ile50Ala, substrate row AdoHcy; column Km (uM) cell = 3.7; column kcat (s-1) cell = 1.8; column kcat/Km (s-1 uM-1) cell = 0.5; column catalytic efficiency (%) cell = 23.3; column apparent Tma (C) prints one cell per enzyme, on the MTA line of that enzyme. captured primary segment: AdoHcy | I50A MTAN | Table 3 | pH 7.0 | Km 3.7 uM | kcat 1.8 s^-1 | kcat/Km 0.5 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 3.7 uM; 1 uM is 1/1000 mM, so 3.7 / 1000 = 0.0037 mM. kcat: printed Table 3 kcat cell 1.8 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 1.8 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 0.5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.5 x 1000 = 500.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 1.8 / 0.0037 = 486.48648648648646 s^-1 mM^-1, beside the printed efficiency cell 500.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Ile50Ala, substrate row AdoHcy: Km = 3.7 uM; kcat = 1.8 s^-1; kcat/Km = 0.5 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature F207A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Phe207Ala, substrate row AdoHcy; column Km (uM) cell = 5.5; column kcat (s-1) cell = 0.31; column kcat/Km (s-1 uM-1) cell = 0.056; column catalytic efficiency (%) cell = 2.7; column apparent Tma (C) prints one cell per enzyme, on the MTA line of that enzyme. captured primary segment: AdoHcy | F207A MTAN | Table 3 | pH 7.0 | Km 5.5 uM | kcat 0.31 s^-1 | kcat/Km 0.056 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 5.5 uM; 1 uM is 1/1000 mM, so 5.5 / 1000 = 0.0055 mM. kcat: printed Table 3 kcat cell 0.31 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.31 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 0.056 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.056 x 1000 = 56.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.31 / 0.0055 = 56.36363636363637 s^-1 mM^-1, beside the printed efficiency cell 56.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Phe207Ala, substrate row AdoHcy: Km = 5.5 uM; kcat = 0.31 s^-1; kcat/Km = 0.056 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AF12 and applied mutation signature Y107F to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Tyr107Phe, substrate row MTA; column Km (uM) cell = 2.2; column kcat (s-1) cell = 2.5; column kcat/Km (s-1 uM-1) cell = 1.2; column catalytic efficiency (%) cell = 32.2; column apparent Tma (C) cell = 67. captured primary segment: MTA | Y107F MTAN | Table 3 | pH 7.0 | Km 2.2 uM | kcat 2.5 s^-1 | kcat/Km 1.2 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 2.2 uM; 1 uM is 1/1000 mM, so 2.2 / 1000 = 0.0022 mM. kcat: printed Table 3 kcat cell 2.5 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 2.5 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 1.2 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.2 x 1000 = 1200.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 2.5 / 0.0022 = 1136.3636363636363 s^-1 mM^-1, beside the printed efficiency cell 1200.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Tyr107Phe, substrate row MTA: Km = 2.2 uM; kcat = 2.5 s^-1; kcat/Km = 1.2 s^-1 uM^-1.


column_label: Table 3: Kinetic Parameters for 5'-Alkylthio Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11053 (PDF page 5). Table 3, enzyme row Phe207Ala, substrate row MTA; column Km (uM) cell = 1.7; column kcat (s-1) cell = 0.13; column kcat/Km (s-1 uM-1) cell = 0.080; column catalytic efficiency (%) cell = 2.2; column apparent Tma (C) cell = 72. captured primary segment: MTA | F207A MTAN | Table 3 | pH 7.0 | Km 1.7 uM | kcat 0.13 s^-1 | kcat/Km 0.080 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 3 Km cell 1.7 uM; 1 uM is 1/1000 mM, so 1.7 / 1000 = 0.0017 mM. kcat: printed Table 3 kcat cell 0.13 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.13 s^(-1). kcat/Km: printed Table 3 kcat/Km cell 0.080 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.080 x 1000 = 80.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.13 / 0.0017 = 76.47058823529413 s^-1 mM^-1, beside the printed efficiency cell 80.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11053, Table 3, enzyme row Phe207Ala, substrate row MTA: Km = 1.7 uM; kcat = 0.13 s^-1; kcat/Km = 0.080 s^-1 uM^-1.


row_label: Table 3, enzyme row Tyr107Phe, substrate row MTA


sequence_source: UniProtKB REST FASTA P0AF12 direct lookup on 2026-06-05.

column_label: Table 1: Kinetic Parameters for Purine Binding Subsite Mutants, printed column heads enzyme | substrate | Km (uM) | kcat (s-1) | kcat/Km (s-1 uM-1) | catalytic efficiency (%) | apparent Tma (C). Journal page 11052 (PDF page 4). Table 1, enzyme row WT, substrate row MTA; column Km (uM) cell = 0.8; column kcat (s-1) cell = 3.0; column kcat/Km (s-1 uM-1) cell = 3.6; column catalytic efficiency (%) cell = 100; column apparent Tma (C) cell = 68. captured primary segment: MTA | WT MTAN | Table 1 | pH 7.0 | Km 0.8 uM | kcat 3.0 s^-1 | kcat/Km 3.6 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 Km cell 0.8 uM; 1 uM is 1/1000 mM, so 0.8 / 1000 = 0.0008 mM. kcat: printed Table 1 kcat cell 3.0 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 3.0 s^(-1). kcat/Km: printed Table 1 kcat/Km cell 3.6 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 3.6 x 1000 = 3600.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.0 / 0.0008 = 3750.0 s^-1 mM^-1, beside the printed efficiency cell 3600.0 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 11052, Table 1, enzyme row WT, substrate row MTA: Km = 0.8 uM; kcat = 3.0 s^-1; kcat/Km = 3.6 s^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA P0AF12 direct lookup on 2026-06-05; selected F151A mutation applied once after confirming canonical residue F151. and applied mutation signature F151A to reconstruct the assayed variant sequence.