sequence_variant_note: Resolved canonical sequence from UniProtKB:P14621 and applied mutation signature C21S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acylphosphatase(Enzyme) mutant C21S


enzyme_display_name: acylphosphatase

organism: Homo sapiens

substrate_name: H2O; Benzoyl phosphate

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

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

km_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB:P14621 and applied mutation signature C21A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: SABIO-RK modifier species: acylphosphatase(Enzyme) mutant C21A

enzyme: acylphosphatase

substrate: H2O; Benzoyl phosphate


organism: Pyrococcus horikoshii

mutation_signature: Unknown

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

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

proof_lines:
at 45°C and pH 5.3
45°C, pH 5.3
at 40°C and pH 5.3

source_databases_merged: sabio_rk brenda skid

source_db: brenda


substrate_name: Benzoyl phosphate

source_db: oed

kcat_over_km_origin: calculated

source_license: CC BY 4.0

data_origin: experimental

substrate: Benzoyl phosphate

source: oed


substrate_name: benzoyl phosphate

km_display: Not reported

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

proof_lines:
pH 5.3, 45°C, mutant enzyme GG91A
pH 5.3, 25°C, mutant enzyme GG91A

substrate: benzoyl phosphate

source: brenda


enzyme_display_name: prephenate dehydratase

organism: Archaeoglobus fulgidus

substrate_name: phenylpyruvate

sequence_source: UniProtKB O30012 FASTA direct check on 2026-06-07

assay_conditions_summary: 350.15 K; buffer 1 mM prephenate in 200 mM Tris

proof_lines: measuring the appearance of phenylpyruvate at 320 nm, performed with 1 mM prephenate in 200 mM Tris buffer

proof_lines: 77°C, pH not specified in the publication

enzyme: prephenate dehydratase

substrate: phenylpyruvate


organism: Corynebacterium glutamicum

substrate_name: Prephenate

substrate: Prephenate


proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant S99A pheA, His-tagged


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P10341 FASTA after direct residue check on 2026-06-07 and applied mutation signature T183S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant T183S pheA, His-tagged


sequence_source: Reconstructed from UniProtKB P10341 FASTA after direct residue check on 2026-06-07


proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant S99C pheA, His-tagged


proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant S99T pheA, His-tagged


organism: Escherichia coli

verification_status: unverified

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9J8 canonical sequence with reconstructed E159A substitution and applied mutation signature E159A to reconstruct the assayed variant sequence.

status: unverified


sequence_source: UniProtKB:P0A9J8 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9J8 canonical sequence with reconstructed W226L substitution and applied mutation signature W226L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9J8 canonical sequence with reconstructed C216S substitution and applied mutation signature C216S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9J8 canonical sequence with reconstructed Q215A substitution and applied mutation signature Q215A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant Q215A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9J8 canonical sequence with reconstructed N160A substitution and applied mutation signature N160A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant N160A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9J8 canonical sequence, reconstructed as S208A after direct residue check on 2026-06-07 and applied mutation signature S208A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant S208A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9J8 canonical sequence, reconstructed as S208C after direct residue check on 2026-06-07 and applied mutation signature S208C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant S208C


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A9J8 and applied mutation signature E232A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters of PDT Mutants), Prephenate block, protein row E232A; column kcat (min-1) = 2401 ± 91; column Km (uM) = 162 ± 17; column kcat/Km = 14.8.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2401 under the Prephenate column head kcat (min-1); one min^-1 is 1/60 s^-1, so 2401 / 60 = 40.016666666666666 s^-1. Km: printed Table 2 cell 162 under the Prephenate column head Km (uM); one uM is 1/1000 mM, so 162 / 1000 = 0.162 mM. kcat/Km: printed Table 2 cell 14.8 in the Prephenate efficiency column; one min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 14.8 x 1000 / 60 = 246.66666666666666 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Prephenate block, protein row E232A: kcat = 2401 ± 91 min-1; Km = 162 ± 17 uM; printed kcat/Km = 14.8.

table_label: Table 2: Kinetic Parameters of PDT Mutants (Biochemistry 2000, volume 39, number 16, pages 4722-4728); Prephenate block, printed column heads protein | kcat (min-1) | Km (uM) | kcat/Km (min-1 mM-1), a column whose every cell is the quotient of the same row's printed kcat in min-1 and printed Km in uM

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9J8 canonical sequence, reconstructed as W226L after direct residue check on 2026-06-07 and applied mutation signature W226L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant W226L


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9J8 canonical sequence, reconstructed as T278S after direct residue check on 2026-06-07 and applied mutation signature T278S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant T278S


row_label: Table 2, Prephenate block, protein row E232A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9J8 canonical sequence, reconstructed as C216A after direct residue check on 2026-06-07 and applied mutation signature C216A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant C216A


sequence_source: UniProtKB:P0A9J8 canonical sequence, reconstructed as T278S after direct residue check on 2026-06-07


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A9J8 FASTA with direct residue-substitution reconstruction and applied mutation signature E159A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant E159A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A9J8 FASTA with direct residue-substitution reconstruction and applied mutation signature C216S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant C216S


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A9J8 FASTA with direct residue-substitution reconstruction and applied mutation signature W226A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant W226A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A9J8 FASTA with direct residue-substitution reconstruction and applied mutation signature E159A/E232A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant E159A/E232A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A9J8 FASTA with direct residue-substitution reconstruction and applied mutation signature N160A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P0A9J8 FASTA with direct residue-substitution reconstruction


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

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant P*300

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant P*285

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant PDT22


sequence_source: UniProtKB reviewed accession P0A9J8 FASTA fetched during review

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


organism: Methanocaldococcus jannaschii

sequence_source: UniProtKB:Q58054 direct accession lookup


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB:P9WIC3 direct accession lookup


organism: Oryza sativa

substrate_name: L-arogenate

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

proof_lines: wild-type, rice PDT is a bifunctional enzyme

substrate: L-arogenate


sequence_variant_note: Resolved canonical sequence from UniProtKB:A8CF65 direct accession lookup plus S298I comparison to UniProtKB:Q6Z3Y3 and applied mutation signature S298I to reconstruct the assayed variant sequence.

proof_lines: mutant S298I, rice PDT is a bifunctional enzyme

proof_lines: mutant enzyme S298I, rice PDT is a bifunctional enzyme


sequence_source: UniProtKB:Q6Z3Y3 direct accession lookup


organism: Pinus pinaster

substrate_name: prephenate

sequence_source: UniProtKB:A0A1I9WKA1 direct accession lookup

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

substrate: prephenate


organism: Amycolatopsis methanolica

sequence_source: UniProtKB reviewed accession Q44104 fetched via UniProt REST on 2026-06-07


proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant


organism: Arabidopsis thaliana

sequence_source: UniProtKB reviewed accession Q9SGD6 fetched via UniProt REST on 2026-06-07


sequence_source: UniProtKB reviewed accession Q9SA96 fetched via UniProt REST on 2026-06-07


sequence_source: UniProtKB reviewed accession Q9SSE7 fetched via UniProt REST on 2026-06-07


organism: Bos taurus

proof_lines: cardiac muscle, phoshoenzyme intermediate of heart sarcolemma Na+,K+-ATPase


organism: Meleagris gallopavo

proof_lines:
erythrocyte isoenzyme
muscular isoenzyme
T1


proof_lines: muscular enzyme recombinant, expressed as fusion protein with glutathione S-transferase


organism: Equus caballus


organism: Oryctolagus cuniculus

sequence_source: UniProtKB reviewed P00820 (ACYP2_RABIT; Oryctolagus cuniculus; Acylphosphatase-2; EC 3.6.1.7; alternative name Acylphosphatase, muscle type isozyme)


organism: Pseudomonas aeruginosa


organism: Unknown


enzyme_display_name: sugar-phosphatase

organism: Streptococcus mutans

substrate_name: D-Fructose 1-phosphate

enzyme: sugar-phosphatase

substrate: D-Fructose 1-phosphate


enzyme_display_name: beta-mannosidase

organism: Helix pomatia

substrate_name: p-nitrophenyl-beta-D-mannopyranoside

enzyme: beta-mannosidase

substrate: p-nitrophenyl-beta-D-mannopyranoside


organism: Homo sapiens

proof_lines:
beta-mannosidase A
beta-mannosidase B


organism: Hordeum vulgare

substrate_name: p-nitrophenyl-beta-D-mannoside

substrate: p-nitrophenyl-beta-D-mannoside


organism: Lissachatina fulica

substrate_name: phenyl beta-D-mannoside

substrate: phenyl beta-D-mannoside


organism: Medicago sativa

substrate_name: mannotriitol

proof_lines:
enzyme from cotyledons
enzyme from endosperm

substrate: mannotriitol


organism: Drosophila melanogaster

substrate_name: benzoylphosphate

source_db: uniprot

substrate: benzoylphosphate

source: uniprot


organism: Escherichia coli (strain K12)


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

substrate_name: benzoylphosphate at 25 degrees Celsius

substrate: benzoylphosphate at 25 degrees Celsius


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


organism: Arabidopsis thaliana

substrate_name: arogenate

substrate: arogenate


substrate_name: chorismate (at pH 7.8 and at 37 degrees Celsius)

proof_lines: kcat is 72 sec(-1) at pH 7.5. kcat is 31 sec(-1) at pH 4.9.


organism: Petunia hybrida

proof_lines: kcat is 0.194 sec(-1) with L-arogenate as substrate (PubMed:20215586). kcat is 0.012 sec(-1) with prephenate as substrate (PubMed:20215586).


proof_lines: kcat is 1.231 sec(-1) with L-arogenate as substrate (PubMed:20215586). kcat is 0.060 sec(-1) with prephenate as substrate (PubMed:20215586).


organism: Komagataeibacter europaeus

substrate_name: 3-oxo-decanoyl homoserine lactone

substrate: 3-oxo-decanoyl homoserine lactone


organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Polyporus sulfureus


organism: Solanum lycopersicum

substrate_name: p-nitrophenyl beta-D-mannopyranoside

substrate: p-nitrophenyl beta-D-mannopyranoside


organism: Thermoascus aurantiacus

assay_conditions_summary: pH 3; buffer sodium citrate


organism: Thermotoga neapolitana


organism: Tremella fuciformis


organism: Trichoderma reesei


organism: Turbo cornutus


enzyme_display_name: alpha,alpha-trehalase

organism: Amanita muscaria

substrate_name: alpha,alpha-trehalose

enzyme: alpha,alpha-trehalase

substrate: alpha,alpha-trehalose


organism: Apis mellifera

substrate_name: trehalose

substrate: trehalose


organism: Ascaris suum


organism: Blastobotrys adeninivorans

proof_lines:
intracellular enzyme
cell wall-bound enzyme
extracellular enzyme


organism: Chironomus riparius


organism: Schizosaccharomyces pombe

assay_conditions_summary: pH 4.6; 303.15 K; buffer 50 mM acetate

proof_lines: in 50 mM acetate buffer, pH 4.6, at 30°C


organism: Spodoptera frugiperda


organism: Sus scrofa

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


organism: Termitoidae

proof_lines:
pH 3.3, 37°C
pH 3.3, 37°C, versus trehalose


organism: Thermochaetoides thermophila


organism: Thermomyces lanuginosus


enzyme_display_name: beta-glucuronidase

organism: Aspergillus oryzae

substrate_name: glycyrrhizin

sequence_variant_note: Resolved canonical sequence from UniProtKB A7XS03 direct REST/FASTA lookup; variant sequence reconstructed only from validated canonical residue substitutions where applicable. and applied mutation signature A365T/R563E to reconstruct the assayed variant sequence.

enzyme: beta-glucuronidase

substrate: glycyrrhizin


sequence_source: UniProtKB A7XS03 direct REST/FASTA lookup; variant sequence reconstructed only from validated canonical residue substitutions where applicable.


sequence_variant_note: Resolved canonical sequence from UniProtKB A7XS03 direct REST/FASTA lookup; variant sequence reconstructed only from validated canonical residue substitutions where applicable. and applied mutation signature A365T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A7XS03 direct REST/FASTA lookup; variant sequence reconstructed only from validated canonical residue substitutions where applicable. and applied mutation signature R563K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A7XS03 direct REST/FASTA lookup; variant sequence reconstructed only from validated canonical residue substitutions where applicable. and applied mutation signature V447Q to reconstruct the assayed variant sequence.


organism: Mycothermus thermophilus

proof_lines: presence of Mn2+, intracellular isoform, pH 6.0, 65°C


organism: Neurospora crassa


organism: Oryctolagus cuniculus

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

assay_conditions_summary: pH 6

proof_lines:
detergent-solubilized trehalase
pH 6.0
proteinase-treated trehalase


organism: Phaseolus vulgaris


organism: Phycomyces blakesleeanus


organism: Rattus norvegicus

assay_conditions_summary: pH 5; buffer pH contexts

proof_lines:
actetate buffer, pH 5.0
actetate buffer, pH 5.7
phosphate buffer, pH 5.7


organism: Rhizopus microsporus var. rhizopodiformis


organism: Rhodnius prolixus

assay_conditions_summary: pH 5.5; 310.15 K; buffer 50 mM phosphate

proof_lines: in 50 mM phosphate buffer, at pH 5.5 and 37°C


organism: Rhodothermus marinus


organism: Rhodotorula mucilaginosa


organism: Rhynchosciara americana


organism: Saccharomyces cerevisiae

proof_lines:
V-trehalase
apparent value, at pH 7.1
C-trehalase


organism: Cicer arietinum


organism: Dictyostelium discoideum

sequence_source: UniProtKB reviewed accession Q54QZ5 (TREA_DICDI); PubMed PMID 6847202 supports D. discoideum trehalase EC 3.2.1.28 on trehalose.


organism: Drosophila melanogaster


organism: Enterobacter cloacae


organism: Escherichia coli

proof_lines:
signal sequenceless TreA
periplasmic TreA
pH 5.5, 30°C, immobilized enzyme


sequence_source: UniProtKB reviewed accession P62601 (TREF_ECOLI); PubMed PMID 10816581 supports cytoplasmic TreF identity.


enzyme_display_name: Beta-glucuronidase

organism: Aspergillus oryzae

sequence_variant_note: Resolved canonical sequence from UniProtKB:A7XS03 REST/FASTA sequence version 1; checked 2026-06-07 and applied mutation signature R563K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 5; 313.15 K; buffer 50 mM sodium acetate buffer, pH 5.0

enzyme: Beta-glucuronidase


sequence_variant_note: Resolved canonical sequence from UniProtKB:A7XS03 REST/FASTA sequence version 1; checked 2026-06-07 and applied mutation signature A365H/R563E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A7XS03 REST/FASTA sequence version 1; checked 2026-06-07 and applied mutation signature A365T to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A7XS03 REST/FASTA sequence version 1; checked 2026-06-07


sequence_variant_note: Resolved canonical sequence from UniProtKB:A7XS03 REST/FASTA sequence version 1; checked 2026-06-07 and applied mutation signature V447Q/R563K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A7XS03 REST/FASTA sequence version 1; checked 2026-06-07 and applied mutation signature V447Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A7XS03 REST/FASTA sequence version 1; checked 2026-06-07 and applied mutation signature A365T/R563E to reconstruct the assayed variant sequence.


organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)

substrate_name: p-nitrophenyl-beta-glucuronic acid (when expressed in P.pastoris)


organism: Mus musculus


organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)

substrate: p-nitrophenyl-beta-glucuronic acid (when expressed in P.pastoris)


organism: Corynebacterium glutamicum

substrate_name: Prephenate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P10341 direct accession lookup on 2026-06-07; E64D reconstructed after confirming residue 64 is E in the fetched canonical sequence. and applied mutation signature E64D to reconstruct the assayed variant sequence.

substrate: Prephenate


sequence_source: UniProtKB:P10341 direct accession lookup on 2026-06-07.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10341 direct accession lookup on 2026-06-07; F185Y reconstructed after confirming residue 185 is F in the fetched canonical sequence. and applied mutation signature F185Y to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant F185Y pheA, His-tagged


sequence_source: UniProtKB:P10341 direct accession lookup on 2026-06-07; row-specific S99M sequence not reconstructed because the fetched canonical sequence already has M at position 99.

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

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant S99M pheA, His-tagged


organism: Rattus norvegicus

substrate_name: H2O; p-Nitrophenyl-beta-D-glucuronide

sequence_source: UniProtKB:P06760 REST direct lookup on 2026-06-07

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

substrate: H2O; p-Nitrophenyl-beta-D-glucuronide


organism: Saccharolobus solfataricus

substrate_name: 4-methylumbelliferyl beta-D-glucuronide

sequence_source: UniProtKB:Q97UI1 REST direct lookup on 2026-06-07

substrate: 4-methylumbelliferyl beta-D-glucuronide


organism: Talaromyces purpureogenus

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


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

proof_lines: pH 5, 55°C, low-shear modeled microgravity

source_databases_merged: brenda skid


organism: Thermotoga maritima

substrate_name: 4-nitrophenyl beta-D-glucoside

sequence_source: UniProtKB:Q9X0F2 REST direct lookup on 2026-06-07

proof_lines:
75°C, pH 6.5, wild-type enzyme
65°C, pH 6.5, wild-type enzyme

substrate: 4-nitrophenyl beta-D-glucoside


substrate_name: 4-nitrophenyl beta-D-glucuronide

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9X0F2 REST direct lookup on 2026-06-07 plus worker6 E383Q reconstruction and applied mutation signature E383Q to reconstruct the assayed variant sequence.

substrate: 4-nitrophenyl beta-D-glucuronide


substrate_name: 4-nitrophenyl beta-D-galactosiduronide

substrate: 4-nitrophenyl beta-D-galactosiduronide


organism: Frankia sp.


organism: Galleria mellonella


organism: Lobosphaera sp.


organism: Metarhizium anisopliae

substrate_name: alpha,alpha-Trehalose; H2O

substrate: alpha,alpha-Trehalose; H2O


organism: Metarhizium flavoviride

substrate_name: H2O; alpha,alpha-Trehalose

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

substrate: H2O; alpha,alpha-Trehalose


organism: Mycolicibacterium smegmatis


sequence_variant_note: Resolved canonical sequence from UniProt A7XS03 direct accession lookup; A365H/R563E reconstructed by residue substitution and applied mutation signature A365H/R563E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt A7XS03 direct accession lookup; V447Q/R563K reconstructed by residue substitution and applied mutation signature V447Q/R563K to reconstruct the assayed variant sequence.


substrate_name: p-Nitrophenyl-beta-D-xylopyranoside

sequence_source: UniProt P05804 direct accession lookup

substrate: p-Nitrophenyl-beta-D-xylopyranoside


proof_lines: SABIO-RK modifier species: beta-glucuronidase(Enzyme) mutant 1.15 (P557/S566/Q568)

proof_lines: SABIO-RK modifier species: beta-glucuronidase(Enzyme) mutant 2.10 (P557/A566/F568)

proof_lines: SABIO-RK modifier species: beta-glucuronidase(Enzyme) mutant 4.7 (P557/S566/Q568)


sequence_source: UniProt P05804 direct accession lookup; canonical sequence used as accession context


substrate_name: p-Nitrophenyl-beta-D-glucuronide

substrate: p-Nitrophenyl-beta-D-glucuronide


organism: Homo sapiens

sequence_source: UniProt P08236 direct accession lookup

proof_lines: pH and temperature not specified in the publication


organism: Neurospora crassa

sequence_source: UniProt Q7SFB0 direct accession lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9X0F2 canonical sequence reconstructed as E383A from the selected mutation signature and applied mutation signature E383A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q9X0F2 canonical wild-type sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9X0F2 canonical sequence reconstructed as E383A from the selected BRENDA mutation note and applied mutation signature E383A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9X0F2 canonical sequence reconstructed as E383Q from the selected mutation signature and applied mutation signature E383Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10341 canonical sequence reconstructed as R184L from the selected mutation signature and applied mutation signature R184L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10341 canonical sequence reconstructed as R184L from the selected SABIO-RK modifier note and applied mutation signature R184L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant R184L pheA, His-tagged


sequence_source: UniProtKB:P10341 reviewed canonical wild-type sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB:P10341 canonical sequence reconstructed as E64D from the selected SABIO-RK modifier note and applied mutation signature E64D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: prephenate dehydratase(Enzyme) mutant E64D pheA, His-tagged


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

substrate_name: p-nitrophenyl-beta-D-glucuronide

proof_lines: kcat is 18 sec(-1) with p-nitrophenyl-beta-D-glucuronide as substrate.

substrate: p-nitrophenyl-beta-D-glucuronide


organism: Clostridium perfringens (strain 13 / Type A)

proof_lines: kcat is 2.6 sec(-1) with p-nitrophenyl-beta-D-glucuronide as substrate.


organism: Escherichia coli (strain K12)

proof_lines: kcat is 120 sec(-1) with p-nitrophenyl-beta-D-glucuronide as substrate.


organism: Paenibacillus borealis

proof_lines: kcat is 12.2 sec(-1) with p-nitrophenyl-beta-D-glucuronide as sustrate.


organism: Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)

proof_lines: kcat is 80 sec(-1) with p-nitrophenyl-beta-D-glucuronide as substrate.


enzyme_display_name: dextranase

organism: Purpureocillium lilacinum

substrate_name: Dextran

proof_lines: isoform D-I, calculated as released reducing sugar, 40°C, pH 6.0

proof_lines: isoform D-II, calculated as released reducing sugar, 40°C, pH 5.0

proof_lines: isoform D-II, calculated as released reducing sugar, 40°C, pH 3.0

enzyme: dextranase

substrate: Dextran


organism: Paenibacillus sp.

substrate_name: isomaltoheptaose

sequence_source: UniProtKB REST H2EI27, checked 2026-06-07

substrate: isomaltoheptaose


substrate_name: isomaltohexaose

substrate: isomaltohexaose


substrate_name: isomaltopentaose

substrate: isomaltopentaose


organism: Trichocladium griseum

substrate_name: alpha,alpha-trehalose

substrate: alpha,alpha-trehalose


organism: Trichoderma reesei

substrate_name: trehalose

substrate: trehalose


organism: Zunongwangia sp.

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


organism: Aspergillus niger


organism: Bos taurus


organism: Escherichia coli

substrate_name: 4-nitrophenyl beta-D-xylopyranoside

proof_lines:
wild-type enzyme
wild type enzyme

substrate: 4-nitrophenyl beta-D-xylopyranoside


substrate_name: methylumbelliferyl-beta-D-glucuronide

proof_lines:
pH 6.5, 38°C, Vmax: 0.026 mM/min
estriol-16-alpha-glucuronide
pH 7.0, 37°C

substrate: methylumbelliferyl-beta-D-glucuronide


substrate_name: quercetin 4'-O-beta-D-glucuronide

proof_lines:
pH 7.2, 37°C
dependency on pH
pH 5, 37°C

substrate: quercetin 4'-O-beta-D-glucuronide


organism: Labeo rohita

substrate_name: phenolphthalein-beta-D-glucuronic acid

substrate: phenolphthalein-beta-D-glucuronic acid


organism: Littorina littorea

substrate_name: 4-methylumbelliferyl beta-D-glucuronide

substrate: 4-methylumbelliferyl beta-D-glucuronide


organism: Mus musculus

substrate_name: 4-nitrophenyl beta-D-glucuronide

substrate: 4-nitrophenyl beta-D-glucuronide


organism: Oryctolagus cuniculus

substrate_name: chondroitin

substrate: chondroitin


organism: Penicillium purpurogenum

substrate_name: H2O; Glycyrrhizinate

sequence_source: GenBank EU095019 / ABU68712.1; UniProtKB A7XS03; PDB 5C70/5C71

substrate: H2O; Glycyrrhizinate


organism: Rattus norvegicus

substrate_name: H2O; Phenolphthalein beta-D-glucuronide

substrate: H2O; Phenolphthalein beta-D-glucuronide


organism: Secale cereale


organism: Sus scrofa


enzyme_display_name: glucan endo-1,3-beta-D-glucosidase

organism: Aplysia kurodai

substrate_name: laminaritetraose

enzyme: glucan endo-1,3-beta-D-glucosidase

substrate: laminaritetraose


organism: Arthrobacter sp.

substrate_name: Laminarin

substrate: Laminarin


organism: Aspergillus versicolor

substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Bacillus tequilensis

substrate_name: Barley beta-glucan

substrate: Barley beta-glucan


organism: Boscia senegalensis


organism: Cellulosimicrobium cellulans

substrate_name: Laminaripentaose

proof_lines: recombinant catalytic domain, pH 7.0, 25°C

substrate: Laminaripentaose


organism: Euglena gracilis


organism: Formosa algae


organism: Hordeum vulgare

substrate_name: alpha-laminaribiosyl fluoride

substrate: alpha-laminaribiosyl fluoride


proof_lines:
isoform GII
isoform GI
isoform GIII


enzyme_display_name: glucosylceramidase

organism: Paenibacillus sp.

substrate_name: p-nitrophenyl beta-D-glucopyranoside

enzyme: glucosylceramidase

substrate: p-nitrophenyl beta-D-glucopyranoside


proof_lines: in presence of phosphatidylserine and heat-stable factor


enzyme_display_name: meprin A

organism: Homo sapiens

substrate_name: bradykinin

proof_lines: hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min

proof_lines: pH and temperature not specified in the publication

enzyme: meprin A

substrate: bradykinin


organism: Mus musculus


organism: Microdochium nivale

substrate_name: laminaritriose

sequence_source: NCBI DDBJ LC773407.1 CDS protein_id BEK81619.1; RCSB PDB 8JHH entity 1 mature MnLam55A cross-check.

substrate: laminaritriose


organism: Nicotiana glutinosa

substrate_name: O-carboxymethyl-pachyman

substrate: O-carboxymethyl-pachyman


organism: Oryza sativa


organism: Saccharomyces cerevisiae

proof_lines:
beta-glucanase I
beta-glucanase IIIB
beta-glucanase V


organism: Thermotoga maritima

substrate_name: lichenan

proof_lines: pH 6.0-7.0, 45°C, wild-type catalytic enzyme domain

substrate: lichenan


organism: Bos taurus


substrate_name: gastrin 17

substrate: gastrin 17


substrate_name: cholecystokinin 8-sulfate

substrate: cholecystokinin 8-sulfate


proof_lines: meprin A hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min

proof_lines: meprin A hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 for between 8-30 min


organism: Rattus norvegicus


enzyme_display_name: insulysin

enzyme: insulysin


substrate_name: Abz-GGFLRKHGQEDDnp

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines: pH 7.4, 37°C, recombinant His6-tagged full-length enzyme

proof_lines: pH 7.4, 37°C, 76 kDa detagged fragment of recombinant His6-tagged enzyme

proof_lines: pH 7.4, 37°C, 56 kDa detagged fragment of recombinant His6-tagged enzyme

substrate: Abz-GGFLRKHGQEDDnp


substrate_name: Abz-GGFLRKHGQ-EDDnp

proof_lines: pH 7.4, 37°C, mutant Y609F IDE:IDE mutant Y609F

substrate: Abz-GGFLRKHGQ-EDDnp


proof_lines: pH 7.4, 37°C, mutant Y609F IDE:IDE mutant E111F/Y609F


proof_lines: pH 7.4, 37°C, mutant Y609F IDE:IDE mutant H112Q/Y609F


assay_conditions_summary: pH 6; 310.15 K; buffer 50 mM MES

proof_lines:
in 50 mM MES buffer, pH 6.0, at 37°C
pH 5.9
taliglucerase alfa, at pH 5.5 and 37°C


substrate_name: p-nitrophenyl-beta-glucopyranoside

sequence_variant_note: Resolved canonical sequence from NCBI Protein BAC16750.1 / UniProt Q8GAT9; PMID 12153721 and applied mutation signature D223E to reconstruct the assayed variant sequence.

substrate: p-nitrophenyl-beta-glucopyranoside


substrate_name: glucosylceramide

sequence_source: NCBI Protein BAC16750.1 / UniProt Q8GAT9; PMID 12153721

substrate: glucosylceramide


organism: Cavia porcellus

substrate_name: Insulin

substrate: Insulin


organism: Drosophila melanogaster

substrate_name: porcine insulin

proof_lines: Drosophila Kc-cell insulin-degrading enzyme

substrate: porcine insulin


substrate_name: amyloid beta

proof_lines:
pH 8.0, 37°C, wild-type enzyme
pH 7.4, 37°C, IDE:IDE, wild-type

substrate: amyloid beta


substrate_name: protein DNP

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

substrate: protein DNP


sequence_source: UniProtKB:P14735 reconstructed variant

sequence_variant_note: Resolved canonical sequence from UniProtKB:P14735 reconstructed variant and applied mutation signature E111F/Y609F to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, IDE:IDE mutant E111F/Y609F


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14735 reconstructed variant and applied mutation signature H112Q/Y609F to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, IDE:IDE mutant H112Q/Y609F


enzyme_display_name: choloylglycine hydrolase

organism: Bifidobacterium longum

substrate_name: taurochenodeoxycholic acid

enzyme: choloylglycine hydrolase

substrate: taurochenodeoxycholic acid


organism: Brevibacillus sp.

substrate_name: glycodeoxycholic acid

proof_lines: apparent value, calculated from a Lineweaver-Burk plot

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

substrate: glycodeoxycholic acid


organism: Clostridium perfringens

substrate_name: glycocholic acid

substrate: glycocholic acid


organism: Lactiplantibacillus plantarum

proof_lines: pH 5.8-6.3, temperature not specified in the publication


organism: Lactobacillus sp.

substrate_name: taurocholic acid

proof_lines:
hydrolase A
hydrolase B

substrate: taurocholic acid


organism: Stenotrophomonas maltophilia

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: urease

organism: Coccidioides immitis

substrate_name: Urea

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication

enzyme: urease

substrate: Urea


organism: Corynebacterium ammoniagenes

assay_conditions_summary: pH 7; buffer the publication value depends on pH and type of

proof_lines: pH 7.0, temperature not specified in the publication


organism: Enterobacter sp.


organism: Glutamicibacter creatinolyticus

proof_lines: pH and temperature not specified in the publication


organism: Glycine max

proof_lines: alginate-immobilized urease, Vmax: 282 micromol/min/mg


organism: Gossypium hirsutum


proof_lines: mutant K898A/K899A/S901A, pH and temperature not specified in the publication

proof_lines: mutant K898A/K899A/S901A, pH 7.4, temperature not specified in the publication


organism: Sus scrofa


organism: Bacteroides fragilis

substrate_name: taurodeoxycholic acid

substrate: taurodeoxycholic acid


organism: Bacteroides thetaiotaomicron


substrate_name: glycocholate

substrate: glycocholate


substrate_name: taurocholate

proof_lines: pH 6.5, 40°C, recombinant wild-type enzyme

substrate: taurocholate


organism: Helicobacter pylori

proof_lines: pH 6.8, 37°C, Vmax: 1200 micromol/min/mg, in the presence of preservatives PEG or glycerol

proof_lines: range Km: 0.2-0.8 mM, pH 8.0, temperature not specified in the publication


organism: Klebsiella aerogenes


organism: Rattus norvegicus

proof_lines: pH 7.4, temperature not specified in the publication, mutant DELTAC lacking the C-terminal region


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

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


proof_lines: pH 7.4, temperature not specified in the publication, mutant I374S, Vmax: 3.45 nmol/min/mg


proof_lines: pH 7.4, temperature not specified in the publication, mutant T609F, Vmax: 2.6 nmol/min/mg


proof_lines: pH 7.4, temperature not specified in the publication, mutant V360S, Vmax: 2 nmol/min/mg


assay_conditions_summary: pH 7.4; cofactor ATP

proof_lines: mutant R429S, pH 7.4, temperature not specified in the publication


organism: Limosilactobacillus reuteri

assay_conditions_summary: pH 2

proof_lines: pH 2, temperature not specified in the publication


organism: Lysinibacillus sphaericus

proof_lines:
pH 7.2, 37°C, immobilized enzyme
pH 7.2, 37°C, soluble enzyme


organism: Methylophilus methylotrophus


organism: Momordica charantia

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication


organism: Morus alba


organism: Mycobacterium tuberculosis


organism: Nitellopsis obtusa

proof_lines: pH and temperature not specified in the publication


organism: Otala lactea

proof_lines: pH 8.4, temperature not specified in the publication


organism: Proteus mirabilis

proof_lines: pH 7.5, temperature not specified in the publication


organism: Proteus vulgaris


organism: Providencia rettgeri


organism: Providencia stuartii


sequence_variant_note: Resolved canonical sequence from UniProt:P18314 FASTA with C319S reconstructed from PMID:1400317 context and applied mutation signature C319S to reconstruct the assayed variant sequence.


proof_lines:
mutant alphaH321A
mutant betaH41A
mutant betaH39A


proof_lines: pH 7.75, temperature not specified in the publication


organism: Lactobacillus fermentum

substrate_name: Urea; H2O

substrate: Urea; H2O


organism: Lathyrus oleraceus


organism: Limosilactobacillus fermentum


organism: Pseudarthrobacter oxydans

proof_lines: pH 7.6, temperature not specified in the publication


organism: Rhodobacter capsulatus


organism: Schizosaccharomyces pombe

proof_lines: pH 8.2, temperature not specified in the publication


organism: Selenomonas ruminantium

proof_lines: pH 8, temperature not specified in the publication


organism: Sporosarcina pasteurii

proof_lines: pH 8.0, temperature not specified in the publication


organism: Staphylococcus leei


organism: Staphylococcus saprophyticus

proof_lines: pH 6, temperature not specified in the publication


organism: Streptococcus mitior

proof_lines: pH 4.5, temperature not specified in the publication


organism: Ureaplasma urealyticum

proof_lines: pH 6.9, temperature not specified in the publication


organism: Yersinia enterocolitica

proof_lines: pH 5.5, 65°C, Vmax: 7.29 micromol of ammonia/min/mg protein


organism: Zea mays


enzyme_display_name: beta-ureidopropionase

organism: Agrobacterium tumefaciens

substrate_name: 3-methyl-3-ureidopropionic acid

enzyme: beta-ureidopropionase

substrate: 3-methyl-3-ureidopropionic acid


organism: Bos taurus

substrate_name: N-Carbamoyl-beta-alanine

substrate: N-Carbamoyl-beta-alanine


organism: Clostridium uracilicum

substrate_name: beta-ureidopropionic acid

substrate: beta-ureidopropionic acid


organism: Euglena gracilis

substrate_name: Beta-ureidoisobutyric acid

substrate: Beta-ureidoisobutyric acid


organism: Lachancea kluyveri


organism: Pseudomonas putida


organism: Rattus norvegicus


organism: Rattus rattus

proof_lines:
pH 8.1
pH 6.8
pH dependent


organism: Rhodobacter capsulatus


enzyme_display_name: biuret amidohydrolase

organism: Rhizobium leguminosarum bv. viciae

substrate_name: Biuret

assay_conditions_summary: pH 8.5; 295.15 K; buffer 0.1 M potassium phosphate

proof_lines: in 0.1 M potassium phosphate buffer, pH 8.5, at 22°C

enzyme: biuret amidohydrolase

substrate: Biuret


enzyme_display_name: fatty acid amide hydrolase

organism: Canis lupus familiaris

substrate_name: anandamide

enzyme: fatty acid amide hydrolase

substrate: anandamide


organism: Homo sapiens

proof_lines:
pH 8.0, 30°C
liver mitochondria, pH 7.3, 37°C
liver microsomes, pH 7.3, 37°C


substrate_name: oleoyl methyl ester

assay_conditions_summary: pH 9

proof_lines: pH 9.0, recombinantly expressed wild-type enzyme

proof_lines: pH 9.0, wild-type enzyme, FAAH protein lacking its N-terminal 39 amino acids is used. This modification removes the predicted N-terminal transmembrane domain of FAAH, the deletion of which is previously found to leave catalytic properties o

substrate: oleoyl methyl ester


substrate_name: oleoyl p-nitroanilide

substrate: oleoyl p-nitroanilide


substrate_name: nonanoyl p-nitroanilide

substrate: nonanoyl p-nitroanilide


substrate_name: myristoyl p-nitroanilide

substrate: myristoyl p-nitroanilide


organism: Medicago truncatula


substrate_name: oleamide

sequence_source: UniProtKB P97612 canonical sequence; N-terminal 39-aa deletion and row mutation reconstructed from selected BRENDA note plus PMID 10433686 mutation context.

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -39, so it is treated as a source-provided variant sequence.

proof_lines: pH 9.0, mutant enzyme H358A, FAAH protein lacking its N-terminal 39 amino acids is used. This modification removes the predicted N-terminal transmembrane domain of FAAH, the deletion of which is previously found to leave catalytic propertie

substrate: oleamide


proof_lines: pH 9.0, mutant enzyme H449A, FAAH protein lacking its N-terminal 39 amino acids is used. This modification removes the predicted N-terminal transmembrane domain of FAAH, the deletion of which is previously found to leave catalytic propertie

proof_lines: pH 9.0, mutant enzyme H449A, FAAH protein lacking its N-terminal 39 amino acids is used. This modification removes the predicted N-terminal transmembrane domain of FAAH , the deletion of which is previously found to leave catalytic properti


proof_lines: pH 9.0, mutant enzyme S217A, FAAH protein lacking its N-terminal 39 amino acids is used. This modification removes the predicted N-terminal transmembrane domain of FAAH, the deletion of which is previously found to leave catalytic propertie


proof_lines: pH 9.0, mutant enzyme S218A, FAAH protein lacking its N-terminal 39 amino acids is used. This modification removes the predicted N-terminal transmembrane domain of FAAH, the deletion of which is previously found to leave catalytic propertie


proof_lines: pH 9.0, mutant enzyme H184Q, FAAH protein lacking its N-terminal 39 amino acids is used. This modification removes the predicted N-terminal transmembrane domain of FAAH, the deletion of which is previously found to leave catalytic propertie


enzyme_display_name: dihydroorotase

organism: Cricetinae

substrate_name: L-dihydroorotate

proof_lines:
wild type (pure) and E301A
wild type

enzyme: dihydroorotase

substrate: L-dihydroorotate


organism: Crithidia fasciculata


organism: Escherichia coli

substrate_name: N-carbamoyl-DL-aspartate

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

proof_lines: with thio-dihydroorotate as substrate, pH. 8.0

proof_lines: with dihydroorotate as substrate, pH. 8.0

proof_lines: with thio-dihydroorotate as substrate, pH. 9.0

substrate: N-carbamoyl-DL-aspartate


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

proof_lines: pH 9.0, recombinantly expressed FAAH protein lacking the N-terminal transmembrane domain


organism: Aquifex aeolicus

substrate_name: dihydroorotate

sequence_source: UniProtKB reviewed accession O66990 (PYRC_AQUAE), fetched from UniProt REST; UniProt references include PMID 15381710.

substrate: dihydroorotate


organism: [Bacillus] caldolyticus

substrate_name: Unknown

proof_lines:
at 37°C
at 60°C

substrate: Unknown


organism: Clostridium oroticum

substrate_name: L-Dihydroorotate; H2O

substrate: L-Dihydroorotate; H2O


organism: Faecalicatena orotica

substrate_name: L-carbamoylaspartate

substrate: L-carbamoylaspartate


organism: Mesocricetus auratus

substrate_name: (S)-dihydroorotate

proof_lines:
pH 7.4, 15°C
at 37°C

substrate: (S)-dihydroorotate


organism: Methanocaldococcus jannaschii

sequence_source: UniProtKB Q58885, paper-linked in PMID 28660315/PMC5624517

proof_lines:
pH 8.3, 25°C, recombinant enzyme
pH 8.3, 45°C, recombinant enzyme
pH 8.3, 80°C, recombinant enzyme


organism: Mus musculus


organism: Plasmodium berghei


organism: Plasmodium falciparum

substrate_name: N-(aminocarbonyl)-L-aspartic acid

proof_lines: Ki above 3.5 mM, for the ring cleavage reaction

substrate: N-(aminocarbonyl)-L-aspartic acid


organism: Pseudomonas putida


organism: Rattus norvegicus


enzyme_display_name: dimethylargininase

organism: Bos taurus

substrate_name: NG-monomethyl-L-arginine

enzyme: dimethylargininase

substrate: NG-monomethyl-L-arginine


organism: Homo sapiens

substrate_name: N,N-dimethyl-L-arginine

substrate: N,N-dimethyl-L-arginine


organism: Pseudomonas aeruginosa

substrate_name: S-methyl-L-thiocitrulline

proof_lines: pH 8.0, temperature not specified in the publication

substrate: S-methyl-L-thiocitrulline


substrate_name: NG,NG-Dimethyl-L-homoarginine

substrate: NG,NG-Dimethyl-L-homoarginine


enzyme_display_name: guanine deaminase

organism: Blastobotrys adeninivorans

substrate_name: guanine

proof_lines:
recombinant enzyme, at pH 6.0 and 37°C
native enzyme, at pH 6.0 and 37°C

enzyme: guanine deaminase

substrate: guanine


organism: Camellia sinensis


organism: Drosophila melanogaster

sequence_source: UniProtKB reviewed Q9VMY9/GUAD_DROME, direct REST lookup on 2026-06-07; EC 3.5.4.3 and catalytic activity evidence cite PMID 19567870.

assay_conditions_summary: pH 7.5; 313.15 K; buffer 100 mM potassium phosphate

proof_lines: in 100 mM potassium phosphate buffer (pH 7.5), at 40°C


organism: Escherichia coli

sequence_source: UniProtKB reviewed P76641/GUAD_ECOLI, direct REST lookup on 2026-06-07; EC 3.5.4.3 and catalytic activity evidence cite PMID 10913105.


organism: Klebsiella pneumoniae


organism: Caenorhabditis elegans

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt Q9U2M7 and RCSB 1KT9 FASTA with PMID 12475970 mutation signature and applied mutation signature K83M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt Q9U2M7 and RCSB 1KT9 FASTA with PMID 12475970 mutation signature and applied mutation signature H31A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt Q9U2M7 and RCSB 1KT9 FASTA with PMID 12475970 mutation signature and applied mutation signature H31V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt Q9U2M7 and RCSB 1KT9 FASTA with PMID 12475970 mutation signature and applied mutation signature Y27D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt Q9U2M7 and RCSB 1KT9 FASTA with PMID 12475970 mutation signature and applied mutation signature H38K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt Q9U2M7 and RCSB 1KT9 FASTA with PMID 12475970 mutation signature and applied mutation signature E103Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9U2M7 canonical sequence with direct Y76A substitution reconstructed during review and applied mutation signature Y76A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9U2M7 canonical sequence with direct K79M substitution reconstructed during review and applied mutation signature K79M to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9U2M7 reviewed canonical sequence; RCSB 1KT9/1KTG full-chain SIFTS match


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9U2M7 canonical sequence with direct K36M substitution reconstructed during review and applied mutation signature K36M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9U2M7 canonical sequence with direct E52Q substitution reconstructed during review and applied mutation signature E52Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9U2M7 canonical sequence with direct Y121A substitution reconstructed during review and applied mutation signature Y121A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9U2M7 wild-type sequence; H38G reconstructed by direct residue-coordinate check against the canonical sequence. and applied mutation signature H38G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9U2M7 wild-type sequence; Y27A reconstructed by direct residue-coordinate check against the canonical sequence. and applied mutation signature Y27A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9U2M7 wild-type sequence; K81M reconstructed by direct residue-coordinate check against the canonical sequence. and applied mutation signature K81M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9U2M7 wild-type sequence; Y76A/Y121A reconstructed by direct residue-coordinate checks against the canonical sequence. and applied mutation signature Y76A/Y121A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9U2M7 wild-type sequence; E56Q reconstructed by direct residue-coordinate check against the canonical sequence. and applied mutation signature E56Q to reconstruct the assayed variant sequence.


organism: Chlamydia trachomatis

substrate_name: diadenosine 5',5''-P1,P4-tetraphosphate

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

proof_lines:
presence of 1.5 mM MnCl2, pH 7.5, 22°C
presence of 5.0 mM MnCl2, pH 7.5, 22°C
presence of 1.5 mM MgCl2, pH 7.5, 22°C

substrate: diadenosine 5',5''-P1,P4-tetraphosphate


organism: Lupinus luteus

substrate_name: ApCHFppA

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

substrate: ApCHFppA


substrate_name: P1-P3-bis(5'-adenosyl) triphosphate

substrate: P1-P3-bis(5'-adenosyl) triphosphate


organism: Saccharomyces cerevisiae


organism: Trypanosoma brucei

proof_lines: in 0.1 M potassium phosphate (pH 6.8), 5 mM MgCl2, at 30°C


substrate_name: cyclic ADP-ribose

assay_conditions_summary: pH 8.5; 298.15 K; cofactor ADP

substrate: cyclic ADP-ribose


enzyme_display_name: 8-oxo-dGTP diphosphatase

organism: Ciona intestinalis

enzyme: 8-oxo-dGTP diphosphatase


substrate_name: P1,P4-bis(5'-guanosyl) tetraphosphate

substrate: P1,P4-bis(5'-guanosyl) tetraphosphate


enzyme_display_name: thiamine-triphosphatase

substrate_name: thiamine triphosphate

proof_lines:
with 10 mM Mg2+, at pH 8.9
enzyme from liver
enzyme from heart

enzyme: thiamine-triphosphatase

substrate: thiamine triphosphate


proof_lines:
membrane-bound enzyme
soluble enzyme


organism: Gallus gallus

proof_lines: apparent value, in the presence of 5 mM Mg2+, pH and temperature not specified in the publication


substrate_name: ATP

assay_conditions_summary: cofactor ATP

proof_lines:
in presence of 8 mM Mg2+
in presence of 8 mM ATP
untagged recombinant enzyme

substrate: ATP


substrate_name: Mg2+-thiamine triphosphate complex

proof_lines: membrane-associated enzyme, activated by Ca2+ or Mg2+

substrate: Mg2+-thiamine triphosphate complex


organism: Lupinus angustifolius

sequence_source: UniProtKB O04841 direct EC+organism lookup

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


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

proof_lines: pH 8.0, 25°C, mutant enzyme E58Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys


proof_lines: pH 8.0, 25°C, mutant enzyme E122Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys


proof_lines: pH 8.0, 25°C, mutant enzyme R54Q fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys


substrate_name: diadenosine 5',5'-P1,P4-tetraphosphate

substrate: diadenosine 5',5'-P1,P4-tetraphosphate


organism: Photinus pyralis

substrate_name: P1,P4-bis(5'-adenosyl) tetraphosphate

substrate: P1,P4-bis(5'-adenosyl) tetraphosphate


organism: Kluyveromyces lactis


organism: Mus musculus


organism: Oryctolagus cuniculus

proof_lines:
at pH 7
liver enzyme at pH 9.0
at pH 7.4


organism: Sus sp.


organism: Artemia salina


sequence_source: UniProtKB Q9U2M7; PubMed 11738085


organism: Klebsiella aerogenes

substrate_name: Urea

substrate: Urea


organism: Escherichia coli

substrate_name: dGDP

proof_lines: pH and temperature not specified in the publication

substrate: dGDP


organism: Homo sapiens


enzyme_display_name: 2-hydroxy-dATP diphosphatase

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

enzyme: 2-hydroxy-dATP diphosphatase


sequence_source: UniProtKB P50583/AP4A_HUMAN reviewed canonical sequence

proof_lines:
in presence of Zn2+
pH 7.4, 37°C
in presence of Mg2+


sequence_source: Reconstructed from UniProtKB O04841 mature sequence, RCSB 1JKN EC/organism anchor, and selected BRENDA PMID 11439089 E59Q fusion-extension note

sequence_variant_note: Mutation signature E59Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.0, 25°C, mutant enzyme E59Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys


sequence_source: Reconstructed from UniProtKB O04841 mature sequence, RCSB 1JKN EC/organism anchor, and selected BRENDA PMID 11439089 E58D fusion-extension note

sequence_variant_note: Mutation signature E58D could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.0, 25°C, mutant enzyme E58D fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys


sequence_source: Reconstructed from UniProtKB O04841 mature sequence, RCSB 1JKN EC/organism anchor, and selected BRENDA PMID 11439089 E55Q fusion-extension note

sequence_variant_note: Mutation signature E55Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.0, 25°C, mutant enzyme E55Q fusion protein containing and N-terminal extension of Gly-Pro-Leu-Gly-Ser


sequence_source: Reconstructed from UniProtKB O04841 mature sequence, RCSB 1JKN EC/organism anchor, and selected BRENDA PMID 11439089 E59D fusion-extension note

sequence_variant_note: Mutation signature E59D could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.0, 25°C, mutant enzyme E59D, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser-Pro-Asn-Cys


sequence_source: Reconstructed from UniProtKB O04841 mature sequence, RCSB 1JKN EC/organism anchor, and selected BRENDA PMID 11439089 E125Q fusion-extension note

sequence_variant_note: Mutation signature E125Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 8.0, 25°C, mutant enzyme E125Q, fusion protein containing and N-terminal extension Gly-Pro-Leu-Gly-Ser


organism: Sus scrofa


organism: Artemia sp.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49789 with H96G reconstructed during review and applied mutation signature H96G to reconstruct the assayed variant sequence.

proof_lines:
mutant H96G, pH 6.6
mutant H96G, pH 8.9
mutant H96G, pH 5.8


assay_conditions_summary: pH 7.3; cofactor NADH

column_label: Table 3: Kinetic Parameters for Catalysis by Wild-Type Fhit (Biochemistry 2004, 43(23):7637-7642); Table 3, substrate row 'Ap3A' (footnote b); column 'substrate'; column 'kcat (s-1)'; column 'Km (uM)'; column 'kcat/Km (M-1 s-1)'; the printed cells for this row are kcat 3.5 s-1, Km 2.9 uM and kcat/Km 11.6 x 10^5 M-1 s-1.

normalized_value_unit_evidence: kcat: printed cell 3.5 s-1; already in s^-1, no unit conversion applies; normalized value 3.5 s^(-1). Km: printed cell 2.9 uM; 1 uM is 0.001 mM, so 2.9 / 1000 = 0.0029 mM; normalized value 0.0029 mM. kcat/Km: printed cell 11.6 x 10^5 M-1 s-1 = 1160000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1160000 / 1000 = 1160 s^-1 mM^-1; normalized value 1160 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row 'Ap3A': kcat = 3.5 s-1; Km = 2.9 uM; printed kcat/Km = 11.6 x 10^5 M-1 s-1.


substrate_name: adenosine 5'-phosphoramidate

proof_lines: in 0.1 M potassium phosphate (pH 6.8), 5 mM MgCl2, at 30°C

substrate: adenosine 5'-phosphoramidate


enzyme_display_name: acylphosphatase

substrate_name: benzoyl phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P14621 plus PMID:7720867 R97Q mature-chain mutation reconstruction and applied mutation signature R97Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

enzyme: acylphosphatase

substrate: benzoyl phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14621 plus PMID:8838587 C21A mature-chain mutation reconstruction and applied mutation signature C21A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P14621 plus PMID:8838587 wild-type muscle acylphosphatase context


sequence_variant_note: Resolved canonical sequence from UniProtKB:P14621 plus PMID:8838587 C21S mature-chain mutation reconstruction and applied mutation signature C21S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Rattus norvegicus

sequence_source: UniProtKB:P35745 cited to PMID:1647162


organism: Saccharolobus solfataricus

sequence_source: UniProtKB:Q97ZL0 cited to PMID:16287076

proof_lines:
0.1 M acetate buffer, pH 5.3, 25°C
0.1 M acetate buffer, pH 5.3, 81°C


enzyme_display_name: kynureninase

organism: Aspergillus niger

substrate_name: H2O; L-Kynurenine

enzyme: kynureninase

substrate: H2O; L-Kynurenine


organism: Cupriavidus metallidurans


substrate_name: L-kynurenine

proof_lines: pH 7.9, at 37ºC, at low substrate concentrations

substrate: L-kynurenine


organism: Neurospora crassa


organism: Penicillium roqueforti


organism: Pseudomonas fluorescens

proof_lines: at 37°C in 0.04 M potassium phosphate, pH 7.8


organism: Rhizopus stolonifer

substrate_name: L-Kynurenine; H2O

substrate: L-Kynurenine; H2O


organism: Saccharomyces cerevisiae


organism: Suncus murinus


substrate_name: pyridoxal 5'-phosphate

substrate: pyridoxal 5'-phosphate


organism: Xanthomonas arboricola pv. pruni


enzyme_display_name: oxaloacetate decarboxylase

organism: Acetobacter aceti

substrate_name: oxaloacetate

enzyme: oxaloacetate decarboxylase

substrate: oxaloacetate


organism: Cavia porcellus

substrate_name: Oxaloacetate

substrate: Oxaloacetate


organism: Corynebacterium glutamicum

proof_lines: in 100 mM Tris-HCl (pH 7.3), 10 mM MgCl2, 2.5 mM EDTA, at 30°C


organism: Helianthus annuus

substrate_name: Unknown

substrate: Unknown


organism: Homo sapiens

proof_lines: wild-type, Vmax = 3 micromol/min/mg. In the presence of GDP


organism: Stutzerimonas stutzeri


organism: Sus scrofa


organism: Veillonella parvula


organism: Zea mays


proof_lines: Y235S mutant, Vmax = 0.1 micromol/min/mg. In the presence of GDP


proof_lines: Y235F mutant, Vmax = 3 micromol/min/mg. In the presence of GDP


proof_lines: Y235A mutant, Vmax = 0.2 micromol/min/mg. In the presence of GDP


organism: Klebsiella pneumoniae


organism: Lactococcus lactis

sequence_source: UniProtKB Q7X4Z5_LACLL, submission name CitM, EMBL AAP22384.1; selected PubMed route 15251467 names citM from Lactococcus lactis CRL264.


organism: Oryctolagus cuniculus


enzyme_display_name: arginine decarboxylase

organism: Chlamydia trachomatis

substrate_name: L-Arg

enzyme: arginine decarboxylase

substrate: L-Arg


organism: Chloroflexus aurantiacus

substrate_name: L-arginine

substrate: L-arginine


organism: Christiangramia forsetii


organism: Clostridioides difficile


organism: Dianthus caryophyllus


organism: Escherichia coli

substrate_name: L-Arginine

substrate: L-Arginine


organism: Myxococcus xanthus

substrate_name: dATP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: in the presence of 5 mM Mn2+, at pH 8.0 and 37°C

proof_lines: in the presence of 0.25 mM Mn2+, at pH 8.0 and 37°C

proof_lines: in the presence of 1 mM Mn2+, at pH 8.0 and 37°C

substrate: dATP


organism: Cavia porcellus


organism: Drosophila melanogaster

substrate_name: benzoylphosphate

substrate: benzoylphosphate


organism: Gallus gallus

proof_lines:
Ch2
Ch1 monomer
Ch1 dimer


organism: Homo sapiens


mutation_signature: Δ6

mutation_type: deletion


organism: Avena sativa

proof_lines:
23000 Da enzyme form
38000 Da enzyme form
66000 Da enzyme form


organism: Bacillus cihuensis

sequence_source: NCBI RefSeq WP_028393003.1; accession named for Bacillus cihuensis in PMID 34560100 full text

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


organism: Bacillus subtilis

proof_lines:
at pH 7.5, 37°C
at pH 7.5, 70°C


organism: Brassica rapa subsp. oleifera


organism: Chlamydia pneumoniae


organism: Shewanella algae


organism: Trypanosoma cruzi

proof_lines: double reciprocal plot is biphasic with a Km-value of 10 mM at higher concentrations of L-Arg


organism: Yersinia pestis

substrate_name: L-canavanine

substrate: L-canavanine


enzyme_display_name: aromatic-L-amino-acid decarboxylase

organism: Bos taurus

proof_lines:
brain enzyme
recombinant enzyme
native enzyme

enzyme: aromatic-L-amino-acid decarboxylase


organism: Calliphora vicina


organism: Ceratitis capitata

proof_lines:
enzyme from white prepupae
enzyme from pharate pupae


organism: Dirofilaria immitis


substrate_name: L-Tyr

substrate: L-Tyr


assay_conditions_summary: pH 7; 310.15 K; buffer 167 mM phosphate

proof_lines: in 167 mM phosphate buffer, pH 7.0, containing 39 mM dithiotreitol and 0.167 mM NaEDTA, for 2 h at 37°C


substrate_name: dopamine

proof_lines: aldehyde formation, mutant enzyme K303A, in 50 mM HEPES, pH 7.5, at 25°C

proof_lines: dopamine formation, mutant enzyme K303A, in 50 mM HEPES, pH 7.5, at 25°C

substrate: dopamine


substrate_name: L-Dopa

proof_lines: wild type enzyme, in 50 mM HEPES, pH 7.5, at 25°C

substrate: L-Dopa


organism: Locusta migratoria


organism: Lycoris aurea

substrate_name: L-tyrosine

substrate: L-tyrosine


organism: Micrococcus percitreus

substrate_name: L-tryptophan

proof_lines: pH and temperature not specified in the publication

substrate: L-tryptophan


organism: Mus musculus

proof_lines: inhibitor purified from mouse kidney homogenate ddc, classical non-competitive inhibitor


organism: Papaver somniferum


organism: Penicillium raistrickii


organism: Glycine max


organism: Lathyrus sativus


organism: Methanimicrococcus blatticola

sequence_source: UniProt A0A484F6I1 / RefSeq WP_133517158.1; PMID 34560100 Figure 2 names WP_133517158 for the Methanimicrococcus blatticola recombinant protein.


organism: Methanocaldococcus jannaschii


organism: Mycolicibacterium smegmatis


organism: Oryza sativa


organism: Periplaneta americana


organism: Psilocybe cubensis


organism: Rattus norvegicus

proof_lines: determined in homogenates of renal cortex of 3/4 nephrectomized rats after 26 weeks

proof_lines: determined in homogenates of renal cortex of 3/4 nephrectomized rats after 10 weeks

proof_lines: determined in homogenates of renal cortex of sham surgery rats (control) after 10 weeks


organism: Rehmannia glutinosa


organism: Sus scrofa

proof_lines:
pH 7.5, 25°C, anaerobiosis
pH 7.5, 25°C, aerobiosis
pH 6.8, 25°C


enzyme_display_name: indole-3-glycerol-phosphate synthase

organism: Escherichia coli

proof_lines:
mutant enzyme Lys55Ser
mutant Lys55Ser

enzyme: indole-3-glycerol-phosphate synthase


proof_lines: genetically engineered monofunctional enzyme form IGPS[1-259]


organism: Mycobacterium tuberculosis


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB:P20577, supported by PMID 22555873 naming Pseudomonas aeruginosa PAO1 and UniProt/NCBI PA0651 trpC identity.


organism: Saccharolobus solfataricus

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q06121 canonical Saccharolobus/Sulfolobus solfataricus P2 TrpC with row-specific P2S/G212E reconstruction. and applied mutation signature P2S/G212E to reconstruct the assayed variant sequence.


proof_lines:
pH 7.0, 75°C, mutant enzyme N90A
pH 7.0, 37°C, mutant enzyme N90A
pH 7.0, 25°C, mutant enzyme N90A


proof_lines:
pH 7.0, 37°C, mutant enzyme R54A/N90Q
pH 7.0, 75°C, mutant enzyme R54A/N90Q


proof_lines:
pH 7.0, 25°C, mutant enzyme R54A
pH 7.0, 37°C, mutant enzyme R54A
pH 7.0, 75°C, mutant enzyme R54A


mutation_signature: truncated mutant

mutation_type: truncation


enzyme_display_name: adenosylmethionine decarboxylase

organism: Homo sapiens

substrate_name: S-adenosyl-L-methionine

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

enzyme: adenosylmethionine decarboxylase

substrate: S-adenosyl-L-methionine


organism: Mammalia

substrate_name: S-Adenosyl-L-methionine

substrate: S-Adenosyl-L-methionine


organism: Mus musculus


organism: Plasmodium falciparum

proof_lines: native wild type AdoMetDC enzyme, in 50 mM KH2PO4 pH 7.5, 1 mM EDTA, 1 mM dithiothreitol, at 37°C


proof_lines: recombinant AdoMetDC enzyme, in 50 mM KH2PO4 pH 7.5, 1 mM EDTA, 1 mM dithiothreitol, at 37°C

proof_lines: bifunctional AdoMetDC/ODC enzyme, in 50 mM KH2PO4 pH 7.5, 1 mM EDTA, 1 mM dithiothreitol, at 37°C


organism: Thermotoga maritima


organism: Acanthamoeba castellanii


organism: Brassica rapa subsp. pekinensis


organism: Caenorhabditis elegans

proof_lines:
in presence of 0.3 mM putrescine
in presence of 0.5 mM putrescine
in presence of 2 mM putrescine


organism: Crithidia fasciculata


substrate_name: S-adenosylmethionine

substrate: S-adenosylmethionine


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q06121 plus selected BRENDA mutation note P2S/F246S and applied mutation signature P2S/F246S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q06121 plus selected BRENDA mutation note G212E and applied mutation signature G212E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q06121 plus selected BRENDA mutation note P2S and applied mutation signature P2S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q06121 plus selected BRENDA mutation note F246S and applied mutation signature F246S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q06121 plus selected BRENDA mutation note N90Q and PMID 24403092/PMC3945838 mutagenesis context and applied mutation signature N90Q to reconstruct the assayed variant sequence.

proof_lines:
pH 7.0, 37°C, mutant enzyme N90Q
pH 7.0, 75°C, mutant enzyme N90Q


sequence_source: UniProtKB reviewed accession Q06121

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

proof_lines:
pH 7.0, 25°C, wild-type enzyme
pH 7.5, 37°C, wild-type enzyme
wild-type enzyme


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

proof_lines: pH 7.5, in presence of 2.5 mM putrescine


organism: Saccharomyces cerevisiae

proof_lines:
in absence of putrescine
in presence of putrescine


organism: Trypanosoma brucei

proof_lines: wild type homodimeric enzyme, with 5 mM putrescine, at pH 8.0 and 37°C

proof_lines: wild type homodimeric enzyme, without putrescine, at pH 8.0 and 37°C


organism: Trypanosoma cruzi

substrate_name: S-adenosyl-methionine

substrate: S-adenosyl-methionine


organism: Zea mays


enzyme_display_name: (R)-mandelonitrile lyase

organism: Arabidopsis thaliana

sequence_source: UniProtKB Q9LFT6, reviewed entry cited by PMID 19433222

enzyme: (R)-mandelonitrile lyase


organism: Nandina domestica

substrate_name: benzaldehyde

proof_lines:
pH 4.0, 25°C, hydroxynitrile lyase L
isoform HNL-L, at pH 4.0 and 25°C

substrate: benzaldehyde


organism: Parafontaria laminata


organism: Phlebodium aureum


organism: Prunus armeniaca


organism: Prunus ilicifolia subsp. lyonii

substrate_name: Mandelonitrile

substrate: Mandelonitrile


organism: Prunus pedunculata


organism: Prunus pseudoarmeniaca

substrate_name: (R)-mandelonitrile

assay_conditions_summary: pH 6; 298.15 K; buffer citrate

proof_lines: enzyme immobilized onto Eupergit C, in 50 mM citrate buffer, pH 6.0, 25°C

proof_lines: enzyme immobilized onto Eupergit C 250L, in 50 mM citrate buffer, pH 6.0, 25°C

proof_lines: free enzyme, in 50 mM citrate buffer, pH 6.0, 25°C

substrate: (R)-mandelonitrile


organism: Prunus turcomanica

proof_lines: enzyme immobilized onto Eupergit C250 L, pH 5.5, 25°C

proof_lines: enzyme immobilized onto Eupergit CM, pH 5.5, 25°C


enzyme_display_name: L-fuculose-phosphate aldolase

organism: Escherichia coli

substrate_name: L-Fuculose 1-phosphate

enzyme: L-fuculose-phosphate aldolase

substrate: L-Fuculose 1-phosphate


organism: Methanocaldococcus jannaschii

substrate_name: glycerone phosphate

substrate: glycerone phosphate


organism: Paramecium bursaria Chlorella virus-1

substrate_name: L-Arg

sequence_source: UniProtKB Q84527; RCSB PDB 2NV9; PMID:17305368 structure paper for PBCV arginine decarboxylase

substrate: L-Arg


enzyme_display_name: Peribacillus simplex ADC

organism: Peribacillus simplex

substrate_name: L-arginine

protein_accession_database: NCBI Protein

sequence_source: NCBI Protein WP_096338298.1 cited for Peribacillus simplex in PMID:34560100/PMC8503589

enzyme: Peribacillus simplex ADC

substrate: L-arginine


organism: Persea americana

proof_lines: enzyme from seed coat of 4-week-old fruitlets


organism: Pseudomonas sp.


enzyme_display_name: Psychrilyobacter sp. S5 ADC

organism: Psychrilyobacter sp. S5

sequence_source: NCBI Protein WP_114642662.1 cited for Psychrilyobacter sp. S5 in PMID:34560100/PMC8503589

enzyme: Psychrilyobacter sp. S5 ADC


organism: Rattus norvegicus

substrate_name: L-Arginine

substrate: L-Arginine


sequence_variant_note: Resolved canonical sequence from UniProtKB Q58813 reviewed EC 4.1.2.17 entry for Methanocaldococcus jannaschii; N25L reconstructed from selected BRENDA mutation note after confirming canonical residue N at position 25. and applied mutation signature N25L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q58813 reviewed EC 4.1.2.17 entry for Methanocaldococcus jannaschii; N25T reconstructed from selected BRENDA mutation note after confirming canonical residue N at position 25. and applied mutation signature N25T to reconstruct the assayed variant sequence.


organism: Arachis hypogaea

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


organism: Phytopseudomonas straminea

substrate_name: oxaloacetate

sequence_source: UniProtKB Q9AQI0 reviewed HMG/CHA aldolase, taxid 47882, EC 4.1.3.17 evidence from PMID 11826967; NCBI taxonomy maps current Phytopseudomonas straminea to the Pseudomonas straminea/Pseudomonas ochracea naming context.

proof_lines:
pH 8.0, 25°C
activated by Mg2+
activated by Mn2+

substrate: oxaloacetate


organism: Pseudomonas putida

sequence_source: UniProtKB A5W059 reviewed Pseudomonas putida F1 HMG/CHA aldolase; RCSB 3NOJ and PMID 20843800 point to the same accession/protein context.

proof_lines: wild type protein, 1.0 mM Mn2+, pH 8.0, 25°C

proof_lines: wild type protein, 1.0 mM Mg2+, pH 8.0, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB A5W059 reviewed Pseudomonas putida F1 HMG/CHA aldolase; R123K reconstructed from selected mutation note after confirming canonical A5W059 residue 123 is R. and applied mutation signature R123K to reconstruct the assayed variant sequence.


enzyme_display_name: malyl-CoA lyase

organism: Methylorubrum extorquens

substrate_name: glyoxylate

assay_conditions_summary: cofactor CoA

enzyme: malyl-CoA lyase

substrate: glyoxylate


organism: Rhodobacter capsulatus

substrate_name: malyl-CoA

substrate: malyl-CoA


enzyme_display_name: glucarate dehydratase

substrate_name: D-glucarate

enzyme: glucarate dehydratase

substrate: D-glucarate


enzyme_display_name: prephenate dehydratase

organism: Corynebacterium glutamicum

substrate_name: prephenate

enzyme: prephenate dehydratase

substrate: prephenate


organism: Cupriavidus necator


proof_lines: recombinant prephenate dehydratase domain, 37°C


proof_lines:
mutant W226L, 37°C
above, mutant W226L, 37°C


organism: Amycolatopsis methanolica

substrate_name: Unknown

substrate: Unknown


organism: Candida maltosa


sequence_variant_note: Resolved canonical sequence from UniProtKB:A5W059 canonical sequence via UniProt REST; E199A applied after residue check. and applied mutation signature E199A to reconstruct the assayed variant sequence.


proof_lines:
1 mM MgCl, pH 8.0, 25°C
1 mM MnCl, pH 8.0, 25°C


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:P40011 canonical sequence via UniProt REST.

proof_lines: pH 8.0, 25°C, RraA-like protein Yer010Cp


organism: Thermus thermophilus

sequence_source: UniProtKB:Q5SIP7 canonical sequence via UniProt REST.


organism: Cereibacter sphaeroides


organism: Chloroflexus aurantiacus

substrate_name: (3S)-3-carboxy-3-hydroxypropanoyl-CoA; beta-methylmalyl-CoA; glyoxylate; propionyl-CoA; acetyl-CoA

sequence_source: UniProtKB:S5N020 canonical sequence via UniProt REST.

assay_conditions_summary: pH 7.1; 328.15 K; cofactor CoA


organism: Pantoea agglomerans


organism: Pinus pinaster

proof_lines: pH 8.0, 37°C, prephenate dehydratase Gmut11

proof_lines: pH 8.0, 37°C, prephenate dehydratase Cmut1

proof_lines: pH 8.0, 37°C, prephenate dehydratase Gmut9


organism: Pseudomonas sp.

proof_lines:
presence of L-Tyr
absence of L-Tyr


proof_lines: Pha2 protein of strain W303, pH 8.2, 37Â°C

proof_lines: Pha2 protein of strain HJ01, pH 8.2, 37Â°C


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Sphingomonas paucimobilis

proof_lines:
presence of 1 mM L-Tyr
presence of 1 mM L-Trp
presence of 1 mM L-Phe


enzyme_display_name: nitrile hydratase

organism: Aeribacillus pallidus

proof_lines:
EupergitC-immobilized NHase, at 50°C
soluble NHase, at 50°C

enzyme: nitrile hydratase


organism: Agrobacterium tumefaciens

substrate_name: phenylacetonitrile

proof_lines: pH 7.5, temperature not specified in the publication

substrate: phenylacetonitrile


organism: Arthrobacter sp.

substrate_name: Propionitrile

substrate: Propionitrile


organism: Bacillus sp. (in: firmicutes)

substrate_name: acetonitrile

substrate: acetonitrile


organism: Brevibacterium sp.

proof_lines:
R312 strain
pH 7, 20ºC
pH 7.2, 28ºC, L-NHase


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

substrate_name: Butyronitrile

substrate: Butyronitrile


organism: Sinapis alba

proof_lines: suggestion from preliminary characterisation of nitrile hydratase activity in crude extracts


organism: Rhodococcus erythropolis

substrate_name: adiponitrile

proof_lines: mutant G196V, pH 7.4, temperature not specified in the publication

substrate: adiponitrile


proof_lines: mutant G196Y, pH 7.4, temperature not specified in the publication


proof_lines: mutant G196N, pH 7.4, temperature not specified in the publication


organism: Rhodococcus rhodochrous

substrate_name: Benzonitrile

assay_conditions_summary: pH 7; 313.15 K; buffer 0.1 M potassium phosphate

proof_lines:
pH 7.0, 20ºC, L-NHase
pH 7.0, 20ºC, H-NHase
pH 7.0, 20ºC

substrate: Benzonitrile


substrate_name: Methacrylonitrile

proof_lines: +/- 0.9, substrate: methacrylonitrile, wild type

substrate: Methacrylonitrile


proof_lines:
mutant betaR56K
mutant alphaQ90N
mutant alphaQ90E


organism: Comamonas testosteroni

proof_lines: +/- 0.04, substrate: 2-nitro-5-thiocyanato-benzoic acid, NilFe


organism: Corynebacterium pseudodiphtheriticum

substrate_name: acrylonitrile

proof_lines: pH 7.5, 25°C, non-competitive with acrylonitrile

substrate: acrylonitrile


organism: Corynebacterium sp.


organism: Mesorhizobium sp.


organism: Microbacterium imperiale


organism: Pseudomonas chlororaphis


organism: Escherichia coli


organism: Methanocaldococcus jannaschii


organism: Methanococcus maripaludis

proof_lines: pH and temperature not specified in the publication


organism: Mycobacterium tuberculosis

sequence_source: uniprotkb:P9WIC3; PMID 15753077 names pheA/Rv3838c


organism: Pseudomonas putida

substrate_name: n-valeronitrile

proof_lines: pH 6.7, 0°C, recombinant wild-type enzyme

substrate: n-valeronitrile


proof_lines: pH 6.7, 0°C, recombinant mutant betaY215F

proof_lines: pH 6.7, 0°C, recombinant mutant alphaR170N

proof_lines: pH 6.7, 0°C, recombinant mutant alphaE168Q


proof_lines: mutant enzyme S113A, in 50 mM sodium phosphate, pH 7.5, at 22°C


proof_lines: wild type enzyme, in 50 mM sodium phosphate, pH 7.5, at 22°C

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


proof_lines: mutant G196H, pH 7.4, temperature not specified in the publication


enzyme_display_name: serine C-palmitoyltransferase

organism: Sphingomonas paucimobilis

substrate_name: caproyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB Q93UV0 canonical sequence with direct R378K reconstruction and applied mutation signature R378K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

enzyme: serine C-palmitoyltransferase

substrate: caproyl-CoA


substrate_name: lauroyl-CoA

sequence_source: UniProtKB Q93UV0 canonical sequence with direct R378K reconstruction

substrate: lauroyl-CoA


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


substrate_name: myristoyl-CoA

substrate: myristoyl-CoA


sequence_source: UniProtKB Q93UV0 canonical sequence


substrate_name: L-serine

source_db: skid

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.5

substrate: L-serine

source: skid


enzyme_display_name: guanylate kinase

organism: Arabidopsis thaliana

substrate_name: GMP; ATP

sequence_source: UniProtKB P93757 canonical sequence

enzyme: guanylate kinase

substrate: GMP; ATP


substrate_name: GMP

substrate: GMP


organism: Brugia malayi


organism: Homo sapiens


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: SABIO-RK modifier species: guanylate kinase(Enzyme) mutant R116Q N-terminal His6-SUMO-tagged


proof_lines: SABIO-RK modifier species: guanylate kinase(Enzyme) mutant V91M N-terminal His6-SUMO-tagged


substrate_name: ATP; GMP

proof_lines: SABIO-RK modifier species: guanylate kinase(Enzyme) mutant G3A N-terminal His6-SUMO-tagged

substrate: ATP; GMP


proof_lines: SABIO-RK modifier species: guanylate kinase(Enzyme) mutant S2L N-terminal His6-SUMO-tagged


sequence_source: UniProtKB reviewed accession Q93UV0 FASTA; REST metadata identifies SPT_SPHPI as serine palmitoyltransferase from Sphingomonas paucimobilis with EC 2.3.1.50.

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


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB reviewed accession Q93UV0 FASTA after validating the canonical residue for N100C. and applied mutation signature N100C to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

proof_lines:
recombinant mutant N100C
pH 7.5, 37°C, recombinant mutant N100C


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB reviewed accession Q93UV0 FASTA after validating the canonical residue for N100W. and applied mutation signature N100W to reconstruct the assayed variant sequence.

proof_lines:
recombinant mutant N100W
pH 7.5, 37°C, recombinant mutant N100W


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB reviewed accession Q93UV0 FASTA after validating the canonical residue for R378N. and applied mutation signature R378N to reconstruct the assayed variant sequence.

proof_lines:
recombinant mutant R378N
pH 7.5, 37°C, recombinant mutant R378N


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB reviewed accession Q93UV0 FASTA after validating the canonical residue for N100Y. and applied mutation signature N100Y to reconstruct the assayed variant sequence.

proof_lines:
recombinant mutant N100Y
pH 7.5, 37°C, recombinant mutant N100Y


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB reviewed accession Q93UV0 FASTA after validating the canonical residue for G385F. and applied mutation signature G385F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:Q16774 and applied mutation signature R96H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: guanylate kinase(Enzyme) mutant R96H N-terminal His6-SUMO-tagged


sequence_variant_note: Resolved canonical sequence from uniprot:Q16774 and applied mutation signature S186Y to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: guanylate kinase(Enzyme) mutant S186Y N-terminal His6-SUMO-tagged


sequence_variant_note: Resolved canonical sequence from uniprot:Q16774 and applied mutation signature S121F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: guanylate kinase(Enzyme) mutant S121F N-terminal His6-SUMO-tagged


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q16774 and applied mutation signature V91M to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer triplicate with 10 nM hGMPK in a; cofactor ATP

column_label: Table 2 (Sedimentation coefficients, thermal stabilities, and kinetic parameters for WT apo-hGMPK and nsSNVs of hGMPK), hGMPK row V91M; column kcat (s^-1) = 132.2 +/- 2.2; column Km (uM) = 54.7 +/- 1.9; column kcat/Km (s^-1 uM^-1) = 2.4 +/- 0.1; column s20,w (S) = 2.14 +/- 0.03; column Tm (oC) = 44.4 +/- 0.8.

normalized_value_unit_evidence: kcat: printed Table 2 cell 132.2 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the value stays 132.2. Km: printed Table 2 cell 54.7 uM; 54.7 / 1000 = 0.0547 mM. kcat/Km: printed Table 2 cell 2.4 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.4 x 1000 = 2400.0 s^-1 mM^-1.

row_label: Table 2, hGMPK row V91M

table_label: Table 2: Sedimentation coefficients, thermal stabilities, and kinetic parameters for WT apo-hGMPK and nsSNVs of hGMPK (J. Biol. Chem. 2019, 294(31):11920-11933)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q16774 and applied mutation signature S2L to reconstruct the assayed variant sequence.

column_label: Table 2 (Sedimentation coefficients, thermal stabilities, and kinetic parameters for WT apo-hGMPK and nsSNVs of hGMPK), hGMPK row S2L; column kcat (s^-1) = 77.7 +/- 1.1; column Km (uM) = 31.5 +/- 0.7; column kcat/Km (s^-1 uM^-1) = 2.5 +/- 0.1; column s20,w (S) = 2.22 +/- 0.03; column Tm (oC) = 45.5 +/- 0.5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 77.7 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the value stays 77.7. Km: printed Table 2 cell 31.5 uM; 31.5 / 1000 = 0.0315 mM. kcat/Km: printed Table 2 cell 2.5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.5 x 1000 = 2500.0 s^-1 mM^-1.

row_label: Table 2, hGMPK row S2L


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

column_label: Table 2 (Sedimentation coefficients, thermal stabilities, and kinetic parameters for WT apo-hGMPK and nsSNVs of hGMPK), hGMPK row WT; column kcat (s^-1) = 58.5 +/- 0.3; column Km (uM) = 20.7 +/- 0.3; column kcat/Km (s^-1 uM^-1) = 2.8 +/- 0.1; column s20,w (S) = 2.04 +/- 0.03; column Tm (oC) = 47.4 +/- 0.4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 58.5 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the value stays 58.5. Km: printed Table 2 cell 20.7 uM; 20.7 / 1000 = 0.0207 mM. kcat/Km: printed Table 2 cell 2.8 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.8 x 1000 = 2800.0 s^-1 mM^-1.

row_label: Table 2, hGMPK row WT


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q16774 and applied mutation signature S121F to reconstruct the assayed variant sequence.

column_label: Table 2 (Sedimentation coefficients, thermal stabilities, and kinetic parameters for WT apo-hGMPK and nsSNVs of hGMPK), hGMPK row S121F; column kcat (s^-1) = 101.4 +/- 5.7; column Km (uM) = 48.6 +/- 3.8; column kcat/Km (s^-1 uM^-1) = 2.1 +/- 0.2; column s20,w (S) = 2.22 +/- 0.03; column Tm (oC) = 43.8 +/- 0.2.

normalized_value_unit_evidence: kcat: printed Table 2 cell 101.4 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the value stays 101.4. Km: printed Table 2 cell 48.6 uM; 48.6 / 1000 = 0.0486 mM. kcat/Km: printed Table 2 cell 2.1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.1 x 1000 = 2100.0 s^-1 mM^-1.

row_label: Table 2, hGMPK row S121F


sequence_variant_note: Resolved canonical sequence from uniprot:Q16774 and applied mutation signature R96G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q93UV0 plus direct V246M reconstruction and applied mutation signature V246M to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q93UV0 plus direct V246M reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q93UV0 plus direct G385F reconstruction and applied mutation signature G385F to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q93UV0 plus direct G385F reconstruction


assay_conditions_summary: pH 7.5; 298.15 K; buffer reaction; cofactor CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q93UV0 plus direct R378K reconstruction and applied mutation signature R378K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R378K, with palmitoyl-CoA as cosubstrate, at pH 7.5 and 25°C

proof_lines: mutant enzyme R378K, with myristoyl-CoA as cosubstrate, at pH 7.5 and 25°C


organism: Bacteriovorax stolpii

sequence_source: UniProtKB reviewed accession A7BFV8 fetched 2026-06-07


substrate_name: L-Serine; Palmitoyl-CoA

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

proof_lines: SABIO-RK modifier species: serine C-palmitoyltransferase(Enzyme) mutant hLCB1-C133W/hLCB2a/ssSPTa

substrate: L-Serine; Palmitoyl-CoA


substrate_name: Palmitoyl-CoA; L-Serine

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

substrate: Palmitoyl-CoA; L-Serine


sequence_source: UniProtKB reviewed accession O15269 fetched 2026-06-07

assay_conditions_summary: pH 8

proof_lines: at pH 8.0, temperature not specified in the publication


organism: Sphingobacterium multivorum

sequence_source: UniProtKB reviewed accession A7BFV6 fetched 2026-06-07

proof_lines:
at pH 7.5 and 37°C
Raw SKiD Env: Temp=-----, pH=-----


organism: Sphingobacterium spiritivorum

sequence_source: UniProtKB reviewed accession A7BFV7 fetched 2026-06-07


mutation_signature: Δ2

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 Reconstructed from UniProtKB reviewed accession Q93UV0 fetched 2026-06-07 by applying R378A to the canonical sequence and applied mutation signature R378A to reconstruct the assayed variant sequence.

proof_lines:
recombinant mutant R378A
pH 7.5, 37°C, recombinant mutant R378A


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q16774 canonical sequence reconstructed with source mutation R96G after confirming Q16774 residue 96 is R. and applied mutation signature R96G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q16774 and applied mutation signature S186Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer triplicate with 10 nM hGMPK in a; cofactor NADH

column_label: Table 2 (Sedimentation coefficients, thermal stabilities, and kinetic parameters for WT apo-hGMPK and nsSNVs of hGMPK), hGMPK row S186Y; column kcat (s^-1) = 96.5 +/- 0.7; column Km (uM) = 36.8 +/- 0.7; column kcat/Km (s^-1 uM^-1) = 2.6 +/- 0.1; column s20,w (S) = 2.14 +/- 0.03; column Tm (oC) = 44.6 +/- 0.2.

normalized_value_unit_evidence: kcat: printed Table 2 cell 96.5 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the value stays 96.5. Km: printed Table 2 cell 36.8 uM; 36.8 / 1000 = 0.0368 mM. kcat/Km: printed Table 2 cell 2.6 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.6 x 1000 = 2600.0 s^-1 mM^-1.

row_label: Table 2, hGMPK row S186Y


sequence_source: UniProtKB REST Q16774 canonical sequence.


substrate_name: dGMP; ATP

substrate: dGMP; ATP


organism: Mus musculus

sequence_source: UniProtKB REST Q64520 canonical sequence.


organism: Oryza sativa Japonica Group

sequence_source: UniProtKB REST Q10M74 canonical sequence.

proof_lines: recombinant chloroplast isozyme, pH 7.5, 30°C


sequence_source: UniProtKB REST Q2QPW1 canonical sequence.

proof_lines: recombinant cytosolic isozyme, pH 7.5, 30°C


enzyme_display_name: lignin peroxidase

organism: Phanerochaete sordida

substrate_name: veratryl alcohol

sequence_source: UniProtKB:B6ZKF4 REST FASTA, fetched 2026-06-07

enzyme: lignin peroxidase

substrate: veratryl alcohol


organism: Rhodococcus jostii

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q0SE24 REST FASTA with N246A reconstruction, fetched 2026-06-07 and applied mutation signature N246A to reconstruct the assayed variant sequence.


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q0SE24 and applied mutation signature N246A to reconstruct the assayed variant sequence.

smiles: OO

assay_conditions_summary: pH 5; 298.15 K; buffer 50 mM sodium malonate

column_label: Table 2 (Kinetic parameters of recombinant Rh_DypB peroxidase on H2O2), row 'Addition of 2 mM Mn2+'; column kcat (s^-1) = 34.0 ± 1.2; column Km (mM) = 0.04 ± 0.01; column kcat/Km (head prints no unit; decoded unit s^-1 mM^-1 from the kcat and Km column heads) = 850 ± 91; column Ki (mM) = 2.8 ± 0.3.

normalized_value_unit_evidence: kcat: printed Table 2 cell 34.0 s^-1; already in s^-1, no unit conversion applies; the exported value is 34.0 s^(-1). Km: printed Table 2 cell 0.04 mM; already in mM, no unit conversion applies; the exported value is 0.04 mM. kcat/Km: printed Table 2 cell 850 in the kcat/Km column, whose unit is s^-1 mM^-1 because kcat is printed in s^-1 and Km in mM (34.0 / 0.04 = 850 confirms it); already in s^-1 mM^-1, no unit conversion applies; the exported value is 850.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row 'Addition of 2 mM Mn2+': kcat = 34.0 ± 1.2 s^-1; Km = 0.04 ± 0.01 mM; printed kcat/Km = 850 ± 91 in the kcat/Km column, whose head prints no unit and whose unit is s^-1 mM^-1 (the kcat column unit s^-1 over the Km column unit mM); Ki = 2.8 ± 0.3 mM.

row_label: Table 2, H2O2 row 'Addition of 2 mM Mn2+' (recombinant Rh_DypB, the N246A variant of R. jostii RHA1 DypB)

table_label: Table 2: Kinetic parameters of recombinant Rh_DypB peroxidase on H2O2 (Appl Microbiol Biotechnol 2018, 102:10579-10588)

status: verified


column_label: Table 1 (Kinetic parameters of recombinant Rh_DypB peroxidase on Mn2+, ABTS, and 2,6-DMP), row (B) In presence of 0.3 mM H2O2, ABTS column group; column kcat (s^-1) = 15.4 ± 0.73; column Km (mM) = 15.6 ± 1.3; column kcat/Km (head prints no unit; decoded unit s^-1 mM^-1 from the kcat and Km column heads) = 0.98 ± 0.1.

normalized_value_unit_evidence: kcat: printed Table 1 row (B) ABTS cell 15.4 s^-1; already in s^-1, no unit conversion applies; the exported value is 15.4 s^(-1). Km: printed Table 1 row (B) ABTS cell 15.6 mM; already in mM, no unit conversion applies; the exported value is 15.6 mM. kcat/Km: printed Table 1 row (B) ABTS cell 0.98 in the kcat/Km column, whose unit is s^-1 mM^-1 because kcat is printed in s^-1 and Km in mM; already in s^-1 mM^-1, no unit conversion applies, so the paper value is 0.98 s^(-1)*mM^(-1); the exported value is 0.9871794871794872 s^(-1)*mM^(-1), which is the full-precision quotient 15.4 / 15.6.

raw_value_unit_evidence: Table 1, row (B) In presence of 0.3 mM H2O2, ABTS column group: kcat = 15.4 ± 0.73 s^-1; Km = 15.6 ± 1.3 mM; printed kcat/Km = 0.98 ± 0.1 in the kcat/Km column, whose head prints no unit and whose unit is s^-1 mM^-1 (the kcat column unit s^-1 over the Km column unit mM).

row_label: Table 1, row (B) In presence of 0.3 mM H2O2, ABTS column group (recombinant Rh_DypB, the N246A variant of R. jostii RHA1 DypB)

table_label: Table 1: Kinetic parameters of recombinant Rh_DypB peroxidase on Mn2+, ABTS, and 2,6-DMP (Appl Microbiol Biotechnol 2018, 102:10579-10588)


substrate_name: Mn(II)

sequence_source: UniProtKB:Q0SE24 REST FASTA with N246A reconstruction, fetched 2026-06-07

substrate: Mn(II)


proof_lines: pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 0.3 mM H2O2

proof_lines: pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 50 mM 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and 2 mM Mn2+

proof_lines: pH 5.0, 25°C, recombinant enzyme mutant N246A, in presence of 1.5 mM H2O2


organism: Trametopsis cervina

sequence_source: UniProtKB:Q60FD2 REST FASTA, fetched 2026-06-07

assay_conditions_summary: pH 3; buffer 20 mM sodium succinate

proof_lines: recombinant enzyme without veratryl alcohol-H2O2 pretreatment, in 20 mM sodium succinate buffer (pH 3.0)

proof_lines: recombinant enzyme with veratryl alcohol-H2O2 pretreatment, in 20 mM sodium succinate buffer (pH 3.0)


organism: Rattus norvegicus

sequence_source: UniProtKB Q71RR7 REST lookup on 2026-06-07

assay_conditions_summary: cofactor ATP


organism: Rickettsia conorii

substrate_name: guanosine monophosphate

sequence_source: UniProtKB Q92GC9 REST lookup on 2026-06-07

substrate: guanosine monophosphate


enzyme_display_name: UDP-N-acetylglucosamine diphosphorylase

substrate_name: N-Acetyl-D-glucosamine 1-phosphate; UTP

sequence_source: UniProtKB Q940S3 REST lookup on 2026-06-07

enzyme: UDP-N-acetylglucosamine diphosphorylase

substrate: N-Acetyl-D-glucosamine 1-phosphate; UTP


sequence_source: UniProtKB O64765 REST lookup on 2026-06-07


organism: Escherichia coli

sequence_source: UniProtKB P0ACC7 canonical sequence only; row-specific G14A His6-tagged sequence unresolved

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant G14A His6-tagged


substrate_name: UTP

sequence_source: UniProtKB P0ACC7 REST lookup on 2026-06-07

substrate: UTP


sequence_variant_note: Resolved canonical sequence from UniProtKB P0ACC7 canonical sequence plus selected R18A mutation reconstructed on 2026-06-07 and applied mutation signature R18A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P0ACC7 canonical sequence only; row-specific truncated His6-tagged sequence unresolved

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant truncated His6-tagged


organism: Saccharomyces cerevisiae

substrate_name: N-Acetyl-D-glucosamine 1-phosphate

sequence_source: UniProtKB:P43123 direct REST lookup on 2026-06-07; variant rows reconstructed from the checked canonical sequence and selected mutation_signature.

substrate: N-Acetyl-D-glucosamine 1-phosphate


substrate_name: UTP; N-Acetyl-D-glucosamine 1-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P43123 direct REST lookup on 2026-06-07; variant rows reconstructed from the checked canonical sequence and selected mutation_signature. and applied mutation signature R116A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: UDP-N-acetylglucosamine diphosphorylase(Enzyme) mutant R116A

substrate: UTP; N-Acetyl-D-glucosamine 1-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43123 direct REST lookup on 2026-06-07; variant rows reconstructed from the checked canonical sequence and selected mutation_signature. and applied mutation signature G111A to reconstruct the assayed variant sequence.