assay_conditions_summary: pH 7.3; 299.65 K; cofactor NADH

column_label: Table 3: Kinetic Parameters for Catalysis by Wild-Type Fhit (Biochemistry 2004, 43(23):7637-7642); Table 3, substrate row 'AMP-N-MeIm' (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 4.2 s-1, Km 5.3 uM and kcat/Km 7.2 x 10^5 M-1 s-1.

normalized_value_unit_evidence: kcat: printed cell 4.2 s-1; already in s^-1, no unit conversion applies; normalized value 4.2 s^(-1). Km: printed cell 5.3 uM; 1 uM is 0.001 mM, so 5.3 / 1000 = 0.0053 mM; normalized value 0.0053 mM. kcat/Km: printed cell 7.2 x 10^5 M-1 s-1 = 720000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 720000 / 1000 = 720 s^-1 mM^-1; normalized value 720 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row 'AMP-N-MeIm': kcat = 4.2 s-1; Km = 5.3 uM; printed kcat/Km = 7.2 x 10^5 M-1 s-1.


organism: Homo sapiens

substrate_name: P1,P3-Bis(5'-adenosyl) triphosphate

source_db: oed

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

mutation_type: substitution

data_origin: experimental

substrate: P1,P3-Bis(5'-adenosyl) triphosphate

status: unverified

source: oed


sequence_source: UniProtKB:P49789 canonical FASTA with H96G reconstruction


kcat_over_km_display: Not reported

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_source: UniProtKB:P49789 canonical FASTA

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

assay_conditions_summary: pH 6.8; 310.15 K; cofactor ADP

proof_lines: nonphosphorylated recombinant enzyme, pH 6.8, 37°C

proof_lines: monophosphorylated recombinant enzyme, pH 6.8, 37°C

proof_lines: diphosphorylated recombinant enzyme, pH 6.8, 37°C

source_databases_merged: sabio_rk brenda skid


enzyme_display_name: glutamate 5-kinase

organism: Escherichia coli

substrate_name: ATP

source_db: brenda

kcat_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProt REST P0A7B5 canonical sequence reconstructed with D170A and applied mutation signature D170A to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ATP

enzyme: glutamate 5-kinase

substrate: ATP

source: brenda


sequence_variant_note: Resolved canonical sequence from UniProt REST P0A7B5 canonical sequence reconstructed with K217A and applied mutation signature K217A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P0A7B5 canonical sequence reconstructed with N149A and applied mutation signature N149A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P0A7B5 canonical sequence reconstructed with D148A and applied mutation signature D148A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P0A7B5 canonical sequence reconstructed with D170N and applied mutation signature D170N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P0A7B5 canonical sequence reconstructed with T169A and applied mutation signature T169A to reconstruct the assayed variant sequence.


substrate_name: ATP; L-Glutamate

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

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

substrate: ATP; L-Glutamate


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

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: glutamate 5-kinase(Enzyme) mutant ProB (3,4-dehydroproline resistant)


organism: Xanthomonas campestris

substrate_name: UDP-glucuronate

verification_status: corrected

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

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GCH2 reviewed canonical sequence with reconstructed E272D variant and applied mutation signature E272D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant E272D His-tagged

substrate: UDP-glucuronate

status: corrected


sequence_source: UniProtKB:Q8GCH2 reviewed canonical sequence with reconstructed E272D variant


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GCH2 reviewed canonical sequence with reconstructed Q310A variant and applied mutation signature Q310A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant Q310A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GCH2 reviewed canonical sequence with reconstructed E192A variant and applied mutation signature E192A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GCH2 reviewed canonical sequence with reconstructed D234A variant and applied mutation signature D234A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GCH2 reviewed canonical sequence with reconstructed M231A variant and applied mutation signature M231A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant M231A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GCH2 reviewed canonical sequence with reconstructed Y292A variant and applied mutation signature Y292A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant Y292A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GCH2 reviewed canonical sequence with reconstructed D207A variant and applied mutation signature D207A to reconstruct the assayed variant sequence.


enzyme_display_name: adenosylmethionine decarboxylase

organism: Arabidopsis thaliana

substrate_name: S-Adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB Q96286 reviewed REST lookup on 2026-06-04; C230A variant reconstructed from canonical sequence after residue check. and applied mutation signature C230A to reconstruct the assayed variant sequence.

enzyme: adenosylmethionine decarboxylase

substrate: S-Adenosyl-L-methionine


sequence_source: UniProtKB Q96286 reviewed REST lookup on 2026-06-04.

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


sequence_variant_note: Resolved canonical sequence from UniProtKB Q96286 reviewed REST lookup on 2026-06-04; C83A variant reconstructed from canonical sequence after residue check. and applied mutation signature C83A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosylmethionine decarboxylase(Enzyme) mutant C83A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q96286 reviewed REST lookup on 2026-06-04; K81A variant reconstructed from canonical sequence after residue check. and applied mutation signature K81A to reconstruct the assayed variant sequence.


substrate_name: L-Lysine

sequence_source: UniProtKB Q96286 reviewed REST lookup on 2026-06-04; canonical sequence preserved as accession context because no mutation_signature is present.

substrate: L-Lysine


sequence_variant_note: Resolved canonical sequence from UniProtKB Q96286 reviewed REST lookup on 2026-06-04; C50A variant reconstructed from canonical sequence after residue check. and applied mutation signature C50A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q96286 reviewed REST lookup on 2026-06-04; K81A variant reconstructed from canonical sequence after residue check.

proof_lines: SABIO-RK modifier species: adenosylmethionine decarboxylase(Enzyme) mutant K81A


sequence_source: UniProtKB Q96286 reviewed REST lookup on 2026-06-04; C83A variant reconstructed from canonical sequence after residue check.


organism: Leishmania donovani

sequence_source: UniProtKB A0A0R6Y3I5 direct REST check on 2026-06-04

assay_conditions_summary: pH 7.4; 355.15 K; cofactor ATP


substrate_name: L-Glutamate; ATP

assay_conditions_summary: pH 7.4; cofactor ATP

substrate: L-Glutamate; ATP


substrate_name: L-glutamate

substrate: L-glutamate


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB P9WHU9 direct REST check on 2026-06-04


organism: Vigna aconitifolia

sequence_variant_note: Resolved canonical sequence from UniProtKB P32296 direct REST check on 2026-06-04 plus one-based F129A reconstruction from SABIO-RK mutation note and applied mutation signature F129A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutamate 5-kinase(Enzyme) mutant F129A


km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProtKB P32296 direct REST check on 2026-06-04 plus one-based D126A reconstruction from SABIO-RK mutation note and applied mutation signature D126A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutamate 5-kinase(Enzyme) mutant D126A


sequence_source: UniProtKB P32296 direct REST check on 2026-06-04


sequence_source: UniProtKB Q9Y6X5 direct REST check on 2026-06-04

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


enzyme_display_name: oxaloacetate decarboxylase

organism: Rattus norvegicus

substrate_name: Oxaloacetate

enzyme: oxaloacetate decarboxylase

substrate: Oxaloacetate


organism: Saccharomyces cerevisiae

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


proof_lines: SABIO-RK modifier species: oxaloacetate decarboxylase(Enzyme) mutant R336Q


proof_lines: SABIO-RK modifier species: oxaloacetate decarboxylase(Enzyme) mutant R336K


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


sequence_variant_note: Resolved canonical sequence from UniProtKB Q96286 canonical sequence fetched by exact accession lookup; C50A substitution applied after confirming residue 50 is C. and applied mutation signature C50A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosylmethionine decarboxylase(Enzyme) mutant C50A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q96286 canonical sequence fetched by exact accession lookup; C230A substitution applied after confirming residue 230 is C. and applied mutation signature C230A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosylmethionine decarboxylase(Enzyme) mutant C230A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7B5 checked by UniProt REST on 2026-06-04 and applied mutation signature D148N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P0A7B5 checked by UniProt REST on 2026-06-04


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7B5 checked by UniProt REST on 2026-06-04 and applied mutation signature D150N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7B5 checked by UniProt REST on 2026-06-04 and applied mutation signature G51A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7B5 checked by UniProt REST on 2026-06-04 and applied mutation signature K10A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7B5 checked by UniProt REST on 2026-06-04 and applied mutation signature M214A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7B5 checked by UniProt REST on 2026-06-04 and applied mutation signature K217R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7B5 checked by UniProt REST on 2026-06-04 and applied mutation signature T169S to reconstruct the assayed variant sequence.


enzyme_display_name: Histidinol-phosphate aminotransferase

organism: Corynebacterium glutamicum

substrate_name: L-phenylalanine

sequence_variant_note: Resolved canonical sequence from uniprot:Q9KJU4 and applied mutation signature Y123F to reconstruct the assayed variant sequence.

enzyme: Histidinol-phosphate aminotransferase

substrate: L-phenylalanine


sequence_variant_note: Resolved canonical sequence from uniprot:Q9KJU4 and applied mutation signature Y21F to reconstruct the assayed variant sequence.


substrate_name: L-leucine

sequence_variant_note: Resolved canonical sequence from uniprot:Q9KJU4 and applied mutation signature Y257F to reconstruct the assayed variant sequence.

substrate: L-leucine


substrate_name: L-histidinol phosphate

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

substrate: L-histidinol phosphate


sequence_variant_note: Resolved canonical sequence from uniprot:Q9KJU4 and applied mutation signature N99D to reconstruct the assayed variant sequence.


substrate_name: L-tyrosine

substrate: L-tyrosine


ki_unit: mM

sequence_source: UniProtKB REST direct lookup, accession P0A7F6


sequence_source: UniProtKB REST direct lookup, accession P17707


organism: Methanocaldococcus jannaschii

sequence_source: UniProtKB REST direct lookup, accession Q57763


organism: Saccharolobus solfataricus

substrate_name: S-adenosyl-L-methionine

sequence_source: UniProtKB REST direct lookup, accession Q9UWY8

substrate: S-adenosyl-L-methionine


organism: Streptomyces griseochromogenes

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup, accession Q841K9; M37Y reconstructed from canonical residue 37 and applied mutation signature M37Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; buffer condition '50 mM HEPES

proof_lines: mutant enzyme M37Y, in 50 mM HEPES buffer (pH 8.0), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup, accession Q841K9; M37F reconstructed from canonical residue 37 and applied mutation signature M37F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M37F, in 50 mM HEPES buffer (pH 8.0), at 25°C


sequence_source: UniProtKB REST direct lookup, accession Q841K9; M37Y reconstructed from canonical residue 37


sequence_source: UniProt REST Q841K9, unreviewed TrEMBL blsE entry

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM HEPES

proof_lines: wild type enzyme, in 50 mM HEPES buffer (pH 8.0), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt REST Q841K9 plus direct M37W reconstruction and applied mutation signature M37W to reconstruct the assayed variant sequence.


sequence_source: UniProt REST Q841K9 plus direct M37W reconstruction

proof_lines: mutant enzyme M37W, in 50 mM HEPES buffer (pH 8.0), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt REST Q841K9 plus direct M37F reconstruction and applied mutation signature M37F to reconstruct the assayed variant sequence.


organism: Sulfolobus solfataricus

sequence_source: UniProt REST Q9UWY8, reviewed Swiss-Prot SPEH_SACS2


organism: Thermotoga maritima

sequence_source: UniProt REST Q9WZC3, reviewed Swiss-Prot SPEH_THEMA


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

proof_lines:
at pH 6.8 and 65°C
Raw SKiD Env: Temp=65°C, pH=6.8

source_databases_merged: brenda skid


substrate_name: NAD+; H2O; N6-Acetyl-L-lysyl peptide

assay_conditions_summary: cofactor NAD+

substrate: NAD+; H2O; N6-Acetyl-L-lysyl peptide


substrate_name: [histone H3]-N6-myristoyl-L-lysine9

proof_lines: pH 7.5, temperature not specified in the publication

substrate: [histone H3]-N6-myristoyl-L-lysine9


substrate_name: NAD+

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

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NAD+

substrate: NAD+


substrate_name: acetylated Acetyl-CoA synthetase; H2O; NAD+


organism: Plasmodium falciparum

substrate_name: acetylated Histone H3-peptide; NAD+; H2O


substrate_name: acetylated p300-peptide; NAD+; H2O

substrate: acetylated p300-peptide; NAD+; H2O


substrate_name: H2O; NAD+

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

proof_lines: Km above 10 1/sec*mM, at pH 8.0 and 37°C

substrate: H2O; NAD+


substrate_name: acetylated Histone H3-peptide; NAD+; Methanol


substrate_name: L-Phenylalanine

sequence_source: UniProtKB reviewed entry P9WML7, sequence version 1, retrieved 2026-06-04

substrate: L-Phenylalanine


substrate_name: L-Phenylalanine; 2-Oxoglutarate

sequence_source: UniProtKB reviewed entry Q9X0D0, sequence version 1, retrieved 2026-06-04

proof_lines:
pH 8.0, 25°C
pH 8.0, 20°C
Raw SKiD Env: Temp=25°C, pH=8

substrate: L-Phenylalanine; 2-Oxoglutarate


substrate_name: L-Histidinol phosphate

substrate: L-Histidinol phosphate


substrate_name: L-Tryptophan

substrate: L-Tryptophan


substrate_name: L-Tyrosine

substrate: L-Tyrosine


organism: Zymomonas mobilis

substrate_name: 2-Oxoglutarate; L-Histidinol phosphate

sequence_source: UniProtKB reviewed entry P34037, sequence version 3, retrieved 2026-06-04

substrate: 2-Oxoglutarate; L-Histidinol phosphate


sequence_source: UniProtKB reviewed entry P49775, sequence version 2, retrieved 2026-06-04


substrate_name: acetylated Histone H4-peptide; H2O; NAD+


substrate_name: acetylated Histone H4-peptide; NAD+; H2O


sequence_variant_note: Resolved canonical sequence from direct_uniprot:P53686|reconstructed_variant and applied mutation signature D118N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: mutant enzyme D118N, at pH 8.0, temperature not specified in the publication


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


sequence_variant_note: Resolved canonical sequence from direct_uniprot:P53686|reconstructed_variant and applied mutation signature I117F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I117F, at pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from direct_uniprot:P53686|reconstructed_variant and applied mutation signature I117V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I117V, at pH 8.0, temperature not specified in the publication


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Trypanosoma brucei

substrate_name: S-adenosyl-L-methionine

sequence_source: UniProtKB:P50244 canonical sequence; A5HNV7 redirects to P50244 in the live UniProt REST entry.

proof_lines: enzyme in complex with prozyme, absence of putrescine, 37°C, pH 8.0

proof_lines: enzyme in complex with prozyme, presence of putrescine, 37°C, pH 8.0

proof_lines: free enzyme, absence of putrescine, 37°C, pH 8.0


organism: Trypanosoma brucei brucei

substrate_name: S-Adenosyl-L-methionine

sequence_source: UniProtKB:P50244 canonical sequence from live UniProt REST check.

substrate: S-Adenosyl-L-methionine


organism: Trypanosoma cruzi

sequence_source: UniProtKB:O76240 canonical sequence from live UniProt REST check.


enzyme_display_name: L-fuculose-phosphate aldolase

organism: Escherichia coli

substrate_name: L-Fuculose 1-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific Y209F substitution reconstructed after residue check. and applied mutation signature Y209F to reconstruct the assayed variant sequence.

enzyme: L-fuculose-phosphate aldolase

substrate: L-Fuculose 1-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific T26A substitution reconstructed after residue check. and applied mutation signature T26A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific F131A substitution reconstructed after residue check. and applied mutation signature F131A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant F131A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific R212A substitution reconstructed after residue check. and applied mutation signature R212A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific F206W substitution reconstructed after residue check. and applied mutation signature F206W to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant F206W


organism: Lactococcus lactis subsp. lactis bv. Diacetylactis

substrate_name: oxaloacetate

sequence_source: UniProtKB Q7X4Z5 FASTA/JSON direct lookup; PubMed 15251467 supports CitM as the Lactococcus oxaloacetate decarboxylase.

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

substrate: oxaloacetate


substrate_name: Oxaloacetate

substrate: Oxaloacetate


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB reviewed Q9HUU1/OADC_PSEAE direct lookup; PubMed 18081320 and PDB 3B8I map PA4872 to the full UniProt sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

proof_lines: wild type enzyme, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9HUU1/OADC_PSEAE direct lookup plus UniProt mutagenesis feature H235A from PubMed 18081320. and applied mutation signature H235A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H235A, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C


proof_lines: in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9HUU1/OADC_PSEAE direct lookup plus UniProt mutagenesis feature Y212F from PubMed 18081320. and applied mutation signature Y212F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y212F, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9HUU1/OADC_PSEAE direct lookup plus UniProt mutagenesis feature H235Q from PubMed 18081320. and applied mutation signature H235Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H235Q, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C


organism: Catharanthus roseus

sequence_source: UniProtKB reviewed Q42679/DCAM_CATRO direct lookup; PubMed 7883014 supports the Catharanthus roseus SAMDC cDNA/proenzyme sequence.

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


enzyme_display_name: 8-oxo-dGTP diphosphatase

organism: Arabidopsis thaliana

substrate_name: dTTP

sequence_source: UniProtKB reviewed accession Q9CA40 direct lookup on 2026-06-04

normalized_value_unit_evidence: kcat: printed cell 0.25 s^-1 -> 0.25 s^(-1) (the printed column is already in export units); the exported value is 0.25 s^(-1). Km: printed cell 15.6 uM -> 0.0156 mM (divide by 1000); the exported value is 0.016 mM, the same measurement flattened to three decimals (issue category source_km_precision_flattened_to_three_decimals). kcat/Km: the paper PRINTS the kcat/Km cell 1.5 x 10^4 s^-1 M^-1 for this row -> 15.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 15.625 s^(-1)*mM^(-1), which is the bare quotient of the exported kcat and the flattened Km, not a printed cell.

row_label: Table III, row evidence block `Table III row: dTTP / AtNUDT1`, substrate row `dTTP`, protein `AtNUDT1`

table_label: Table III (JBC 280:25277-25283) 'Comparison of the kinetic parameters of AtNUDT1/MutT1 in A. thaliana with those of MutT-like proteins in E. coli, human, and yeast'

enzyme: 8-oxo-dGTP diphosphatase

substrate: dTTP


normalized_value_unit_evidence: kcat: printed cell 0.25 s^-1 -> 0.25 s^(-1) (the printed column is already in export units); the exported value is 0.25 s^(-1). Km: printed cell 6.8 uM -> 0.0068 mM (divide by 1000); the exported value is 0.007 mM, the same measurement flattened to three decimals (issue category source_km_precision_flattened_to_three_decimals). kcat/Km: the paper PRINTS the kcat/Km cell 3.7 x 10^4 s^-1 M^-1 for this row -> 37.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 35.714285714285715 s^(-1)*mM^(-1), which is the bare quotient of the exported kcat and the flattened Km, not a printed cell.

row_label: Table III, row evidence block `Table III row: 8-oxo-dGTP / AtNUDT1`, substrate row `8-oxo-dGTP`, protein `AtNUDT1`


substrate_name: H2O; 8-oxo-dGTP

substrate: H2O; 8-oxo-dGTP


substrate_name: dATP

normalized_value_unit_evidence: kcat: printed cell 0.17 s^-1 -> 0.17 s^(-1) (the printed column is already in export units); the exported value is 0.17 s^(-1). Km: printed cell 16.1 uM -> 0.0161 mM (divide by 1000); the exported value is 0.016 mM, the same measurement flattened to three decimals (issue category source_km_precision_flattened_to_three_decimals). kcat/Km: the paper PRINTS the kcat/Km cell 1.1 x 10^4 s^-1 M^-1 for this row -> 11.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 10.625 s^(-1)*mM^(-1), which is the bare quotient of the exported kcat and the flattened Km, not a printed cell.

row_label: Table III, row evidence block `Table III row: dATP / AtNUDT1`, substrate row `dATP`, protein `AtNUDT1`

substrate: dATP


substrate_name: dGTP

normalized_value_unit_evidence: kcat: printed cell 0.83 s^-1 -> 0.83 s^(-1) (the printed column is already in export units); the exported value is 0.83 s^(-1). Km: printed cell 58.3 uM -> 0.0583 mM (divide by 1000); the exported value is 0.058 mM, the same measurement flattened to three decimals (issue category source_km_precision_flattened_to_three_decimals). kcat/Km: the paper PRINTS the kcat/Km cell 1.4 x 10^4 s^-1 M^-1 for this row -> 14.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 14.310344827586205 s^(-1)*mM^(-1), which is the bare quotient of the exported kcat and the flattened Km, not a printed cell.

row_label: Table III, row evidence block `Table III row: dGTP / AtNUDT1`, substrate row `dGTP`, protein `AtNUDT1`

substrate: dGTP


substrate_name: H2O; Coenzyme A

assay_conditions_summary: cofactor NADH

substrate: H2O; Coenzyme A


sequence_source: UniProtKB reviewed accession P08337 direct lookup on 2026-06-04


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific Y113F reconstruction and applied mutation signature Y113F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AB87 and applied mutation signature E214Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; buffer A [60 mM Tris; cofactor NADH

column_label: Table 3 (Kinetics for the Cleavage of Fuc1P by FucA Mutants), row label 'E214Q'; column 'relative specific activitya (%)' = 71; column 'kcatb (s-1)' = 20.5 (1.0); column 'KM (mM)' = 6 (0.3). Table 3 has no further data column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 20.5 s-1; s-1 is the canonical export unit s^(-1), so no unit conversion applies and the normalized value is 20.5 s^(-1). Km: printed Table 3 cell 6 mM; mM is the canonical export unit, so no unit conversion applies and the normalized value is 6.0 mM. kcat/Km: this paper prints no catalytic-efficiency cell; the full-precision quotient of the two printed cells of this one Table 3 row is 20.5 / 6.0 = 3.4166666666666665 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, row 'E214Q': kcat = 20.5 s-1 (printed with its parenthesised uncertainty 1.0); KM = 6 mM (printed with its parenthesised uncertainty 0.3). Table 3 prints no catalytic-efficiency cell.

row_label: Table 3, mutant row 'E214Q'

table_label: Table 3: Kinetics for the Cleavage of Fuc1P by FucA Mutants (Biochemistry 2000, 39, 6033-6041)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AB87 and applied mutation signature E214A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetics for the Cleavage of Fuc1P by FucA Mutants), row label 'E214A'; column 'relative specific activitya (%)' = 48; column 'kcatb (s-1)' = 18.5 (3); column 'KM (mM)' = 8 (1.3). Table 3 has no further data column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 18.5 s-1; s-1 is the canonical export unit s^(-1), so no unit conversion applies and the normalized value is 18.5 s^(-1). Km: printed Table 3 cell 8 mM; mM is the canonical export unit, so no unit conversion applies and the normalized value is 8.0 mM. kcat/Km: this paper prints no catalytic-efficiency cell; the full-precision quotient of the two printed cells of this one Table 3 row is 18.5 / 8.0 = 2.3125 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, row 'E214A': kcat = 18.5 s-1 (printed with its parenthesised uncertainty 3); KM = 8 mM (printed with its parenthesised uncertainty 1.3). Table 3 prints no catalytic-efficiency cell.

row_label: Table 3, mutant row 'E214A'


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific Y209F reconstruction and applied mutation signature Y209F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant Y209F


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific E214D reconstruction and applied mutation signature E214D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific E214Q reconstruction and applied mutation signature E214Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant E214Q


verification_status: verified

column_label: Table 3 (Kinetics for the Cleavage of Fuc1P by FucA Mutants), row label 'wild type'; column 'relative specific activitya (%)' = 100; column 'kcatb (s-1)' = 19.3 (2); column 'KM (mM)' = 2.2 (0.2). Table 3 has no further data column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 19.3 s-1; s-1 is the canonical export unit s^(-1), so no unit conversion applies and the normalized value is 19.3 s^(-1). Km: printed Table 3 cell 2.2 mM; mM is the canonical export unit, so no unit conversion applies and the normalized value is 2.2 mM. kcat/Km: this paper prints no catalytic-efficiency cell; the full-precision quotient of the two printed cells of this one Table 3 row is 19.3 / 2.2 = 8.772727272727272 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, row 'wild type': kcat = 19.3 s-1 (printed with its parenthesised uncertainty 2); KM = 2.2 mM (printed with its parenthesised uncertainty 0.2). Table 3 prints no catalytic-efficiency cell.

row_label: Table 3, wild-type row 'wild type'

status: verified


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 canonical sequence with selected source mutation signature applied and applied mutation signature K207A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 canonical sequence with selected source mutation signature applied and applied mutation signature E214D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant E214D


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AB87 and applied mutation signature E214L to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetics for the Cleavage of Fuc1P by FucA Mutants), row label 'E214L'; column 'relative specific activitya (%)' = 6; column 'kcatb (s-1)' = 12.8 (5); column 'KM (mM)' = 74 (30). Table 3 has no further data column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 12.8 s-1; s-1 is the canonical export unit s^(-1), so no unit conversion applies and the normalized value is 12.8 s^(-1). Km: printed Table 3 cell 74 mM; mM is the canonical export unit, so no unit conversion applies and the normalized value is 74.0 mM. kcat/Km: this paper prints no catalytic-efficiency cell; the full-precision quotient of the two printed cells of this one Table 3 row is 12.8 / 74.0 = 0.17297297297297298 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, row 'E214L': kcat = 12.8 s-1 (printed with its parenthesised uncertainty 5); KM = 74 mM (printed with its parenthesised uncertainty 30). Table 3 prints no catalytic-efficiency cell.

row_label: Table 3, mutant row 'E214L'


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 canonical sequence with selected source mutation signature applied and applied mutation signature E214Q/T26A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 canonical sequence with selected source mutation signature applied and applied mutation signature T26A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant T26A


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 canonical sequence with selected source mutation signature applied and applied mutation signature R212A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant R212A


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 canonical sequence with selected source mutation signature applied and applied mutation signature F206W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 canonical sequence with selected source mutation signature applied and applied mutation signature Y113F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant Y113F


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AB87 and applied mutation signature E215A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetics for the Cleavage of Fuc1P by FucA Mutants), row label 'E215A'; column 'relative specific activitya (%)' = 90; column 'kcatb (s-1)' = 21.5 (3); column 'KM (mM)' = 3.1 (0.4). Table 3 has no further data column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 21.5 s-1; s-1 is the canonical export unit s^(-1), so no unit conversion applies and the normalized value is 21.5 s^(-1). Km: printed Table 3 cell 3.1 mM; mM is the canonical export unit, so no unit conversion applies and the normalized value is 3.1 mM. kcat/Km: this paper prints no catalytic-efficiency cell; the full-precision quotient of the two printed cells of this one Table 3 row is 21.5 / 3.1 = 6.935483870967742 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, row 'E215A': kcat = 21.5 s-1 (printed with its parenthesised uncertainty 3); KM = 3.1 mM (printed with its parenthesised uncertainty 0.4). Table 3 prints no catalytic-efficiency cell.

row_label: Table 3, mutant row 'E215A'


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB FASTA lookup for reviewed accession P0AB87 plus computed E215A substitution. and applied mutation signature E215A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant E215A


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB FASTA lookup for reviewed accession P0AB87 plus computed N29Q substitution. and applied mutation signature N29Q to reconstruct the assayed variant sequence.


sequence_source: Direct UniProtKB FASTA lookup for reviewed accession P0AB87.

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

proof_lines: pH 7.5, 37°C, wild-type enzyme and E214A mutant


substrate_name: dihydroxyacetone phosphate

sequence_source: Direct UniProtKB FASTA lookup for reviewed accession Q58813.

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

proof_lines: assay with DL-glyceraldehyde, pH and temperature not specified in the publication

substrate: dihydroxyacetone phosphate


organism: Pseudomonas putida

sequence_variant_note: Resolved canonical sequence from Direct UniProtKB FASTA lookup for reviewed accession A5W059 plus computed R123K substitution. and applied mutation signature R123K to reconstruct the assayed variant sequence.


sequence_source: Direct UniProtKB FASTA lookup for reviewed accession A5W059.

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


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


sequence_source: UniProtKB:A5W059 FASTA/JSON direct lookup 2026-06-04


sequence_variant_note: Resolved canonical sequence from UniProtKB:A5W059 canonical sequence plus selected-record R123K mutation signature and applied mutation signature R123K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-4-methyl-2-oxoglutarate aldolase(Enzyme) mutant R123K

proof_lines: mutant enzyme R123K, in the presence of 2 mM phosphate, at pH 8.0 and 25°C

proof_lines: mutant enzyme R123K, in the absence of phosphate, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5W059 and applied mutation signature R195A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; buffer 0.1 M HEPES

column_label: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556); enzyme line 'R195A'; column head 'Km (uM)' under the '+ 2 mM Pi' block = 2890; column head 'kcat (s-1)' under the '+ 2 mM Pi' block = 11.5; column head 'kcat/Km (M-1s-1)' under the '+ 2 mM Pi' block = 3.98 x 10^3.

normalized_value_unit_evidence: Km: printed cell 2890 uM; 2890 / 1000 = 2.89 mM. kcat: printed cell 11.5 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed cell 3.98 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.98 x 10^3 / 1000 = 3.98 s^-1 mM^-1. The exact quotient of the two printed component cells is 11.5 / 2.89 = 3.979238754325259 s^-1 mM^-1, and the printed efficiency cell reproduces that quotient at its own printed precision of three significant figures.

raw_value_unit_evidence: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556) enzyme line 'R195A', the '+ 2 mM Pi' block: Km cell 2890 under column head 'Km (uM)'; kcat cell 11.5 under column head 'kcat (s-1)'; catalytic efficiency cell 3.98 x 10^3 under column head 'kcat/Km (M-1s-1)'. Printed with uncertainties as kcat 11.5 ± 0.67 s^-1, Km 2890 ± 210 uM, kcat/Km (3.98 ± 0.37) x 10^3 M^-1 s^-1.

row_label: Table 3, enzyme line 'R195A', the three '+ 2 mM Pi' kinetic columns


sequence_variant_note: Resolved canonical sequence from UniProtKB:A5W059 canonical sequence plus selected-record T145A mutation signature and applied mutation signature T145A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T145A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C

proof_lines: mutant enzyme T145A, in the absence of phosphate, at pH 8.0 and 25°C


proof_lines: wild type enzyme, in the absence of phosphate, at pH 8.0 and 25°C

proof_lines: wild type enzyme, in the presence of 2 mM phosphate, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5W059 and applied mutation signature R40A to reconstruct the assayed variant sequence.

column_label: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556); enzyme line 'R40A'; column head 'Km (uM)' under the '+ 2 mM Pi' block = 3260; column head 'kcat (s-1)' under the '+ 2 mM Pi' block = 36.6; column head 'kcat/Km (M-1s-1)' under the '+ 2 mM Pi' block = 1.12 x 10^4.

normalized_value_unit_evidence: Km: printed cell 3260 uM; 3260 / 1000 = 3.26 mM. kcat: printed cell 36.6 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed cell 1.12 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.12 x 10^4 / 1000 = 11.2 s^-1 mM^-1. The exact quotient of the two printed component cells is 36.6 / 3.26 = 11.226993865030677 s^-1 mM^-1, and the printed efficiency cell reproduces that quotient at its own printed precision of three significant figures.

raw_value_unit_evidence: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556) enzyme line 'R40A', the '+ 2 mM Pi' block: Km cell 3260 under column head 'Km (uM)'; kcat cell 36.6 under column head 'kcat (s-1)'; catalytic efficiency cell 1.12 x 10^4 under column head 'kcat/Km (M-1s-1)'. Printed with uncertainties as kcat 36.6 ± 1.0 s^-1, Km 3260 ± 340 uM, kcat/Km (1.12 ± 0.12) x 10^4 M^-1 s^-1.

row_label: Table 3, enzyme line 'R40A', the three '+ 2 mM Pi' kinetic columns


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5W059 and applied mutation signature N71A to reconstruct the assayed variant sequence.

column_label: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556); enzyme line 'N71A'; column head 'Km (uM)' under the '+ 2 mM Pi' block = 1110; column head 'kcat (s-1)' under the '+ 2 mM Pi' block = 0.0184; column head 'kcat/Km (M-1s-1)' under the '+ 2 mM Pi' block = 16.5.

normalized_value_unit_evidence: Km: printed cell 1110 uM; 1110 / 1000 = 1.11 mM. kcat: printed cell 0.0184 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed cell 16.5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 16.5 / 1000 = 0.0165 s^-1 mM^-1. That printed cell is the paper's own independently fitted catalytic efficiency, and it is the value this record carries for kcat_over_km.

raw_value_unit_evidence: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556) enzyme line 'N71A', the '+ 2 mM Pi' block: Km cell 1110 under column head 'Km (uM)'; kcat cell 0.0184 under column head 'kcat (s-1)'; catalytic efficiency cell 16.5 under column head 'kcat/Km (M-1s-1)'. Printed with uncertainties as kcat 0.0184 ± 0.00034 s^-1, Km 1110 ± 82.7 uM, kcat/Km 16.5 ± 1.3 M^-1 s^-1.

row_label: Table 3, enzyme line 'N71A', the three '+ 2 mM Pi' kinetic columns


enzyme_display_name: biuret amidohydrolase

organism: Rhizobium leguminosarum bv. viciae

substrate_name: Biuret

sequence_variant_note: Resolved canonical sequence from UniProtKB Q1M7F4 direct FASTA/JSON lookup; K142A reconstructed from the canonical sequence after confirming residue 142 is K. and applied mutation signature K142A to reconstruct the assayed variant sequence.

smiles: NC(=O)NC(N)=O

enzyme: biuret amidohydrolase

substrate: Biuret


sequence_variant_note: Resolved canonical sequence from UniProtKB Q1M7F4 direct FASTA/JSON lookup; F41W reconstructed from the canonical sequence after confirming residue 41 is F. and applied mutation signature F41W to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q1M7F4 direct FASTA/JSON lookup; K142A reconstructed from the canonical sequence after confirming residue 142 is K.


sequence_source: UniProtKB Q1M7F4 direct FASTA/JSON lookup; F41W reconstructed from the canonical sequence after confirming residue 41 is F.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q1M7F4 direct FASTA/JSON lookup; Q215A reconstructed from the canonical sequence after confirming residue 215 is Q. and applied mutation signature Q215A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q1M7F4 direct FASTA/JSON lookup; Q215N reconstructed from the canonical sequence after confirming residue 215 is Q. and applied mutation signature Q215N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q1M7F4 direct FASTA/JSON lookup.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q1M7F4 direct FASTA/JSON lookup; Q215E reconstructed from the canonical sequence after confirming residue 215 is Q. and applied mutation signature Q215E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q1M7F4 direct FASTA/API check on 2026-06-04


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1M7F4 direct FASTA/API check on 2026-06-04 and applied mutation signature F41A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1M7F4 direct FASTA/API check on 2026-06-04 and applied mutation signature Q215E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1M7F4 direct FASTA/API check on 2026-06-04 and applied mutation signature F41Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1M7F4 direct FASTA/API check on 2026-06-04 and applied mutation signature Q215N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1M7F4 direct FASTA/API check on 2026-06-04 and applied mutation signature F41L to reconstruct the assayed variant sequence.


enzyme_display_name: N(1)-aminopropylagmatine synthase

organism: Thermus thermophilus

substrate_name: Agmatine; S-Adenosylmethioninamine

sequence_source: UniProtKB reviewed accession Q5SK28 direct FASTA/REST lookup on 2026-06-04.

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

proof_lines:
pH 9.0, 37°C
Raw SKiD Env: Temp=37°C, pH=9

enzyme: N(1)-aminopropylagmatine synthase

substrate: Agmatine; S-Adenosylmethioninamine


substrate_name: agmatine

smiles: N=C(N)NCCCCN

substrate: agmatine


substrate_name: spermidine

smiles: NCCCCNCCCN

substrate: spermidine


substrate_name: norspermidine

smiles: NCCCNCCCN

substrate: norspermidine


smiles: NCCCN(CCCN)CCCN


substrate_name: S-adenosyl 3-(methylthio)propylamine

substrate: S-adenosyl 3-(methylthio)propylamine


organism: Homo sapiens

sequence_source: UniProtKB reviewed accession P36639 direct FASTA/REST lookup on 2026-06-04.

assay_conditions_summary: pH 8; 310.15 K; buffer Tris-HCl

proof_lines:
in Tris-HCl buffer (pH 8.0), at 37°C
Raw SKiD Env: Temp=37°C, pH=8


organism: Saccharomyces cerevisiae

substrate_name: Coenzyme A

sequence_source: UniProtKB reviewed accession Q12524 direct FASTA/REST lookup on 2026-06-04.

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

substrate: Coenzyme A


organism: Pyrococcus furiosus

sequence_source: UniProtKB direct REST lookup for Q8U4G1

proof_lines:
pH 7.4, 70°C
Raw SKiD Env: Temp=70°C, pH=7.4


substrate_name: putrescine

smiles: NCCCCN

substrate: putrescine


smiles: NCCCN


organism: Thermococcus kodakarensis

sequence_source: UniProtKB direct REST lookup for Q5JFG9


substrate_name: cadaverine

smiles: NCCCCCN

substrate: cadaverine


sequence_variant_note: Resolved canonical sequence from UniProtKB A5W059 direct REST/FASTA lookup and applied mutation signature H75A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A5W059 direct REST/FASTA lookup and applied mutation signature K147A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K147A, in the absence of phosphate, at pH 8.0 and 25°C

proof_lines: mutant enzyme K147A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB A5W059 direct REST/FASTA lookup and applied mutation signature G144V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme G144V, in the absence of phosphate, at pH 8.0 and 25°C

proof_lines: mutant enzyme G144V, in the presence of 2 mM phosphate, at pH 8.0 and 25°C


sequence_source: UniProtKB A5W059 direct REST/FASTA lookup


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5W059 and applied mutation signature T145A to reconstruct the assayed variant sequence.

column_label: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556); enzyme line 'T145A'; column head 'Km (uM)' under the '+ 2 mM Pi' block = 1780; column head 'kcat (s-1)' under the '+ 2 mM Pi' block = 10.7; column head 'kcat/Km (M-1s-1)' under the '+ 2 mM Pi' block = 6.01 x 10^3.

normalized_value_unit_evidence: Km: printed cell 1780 uM; 1780 / 1000 = 1.78 mM. kcat: printed cell 10.7 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed cell 6.01 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.01 x 10^3 / 1000 = 6.01 s^-1 mM^-1. The exact quotient of the two printed component cells is 10.7 / 1.78 = 6.011235955056179 s^-1 mM^-1, and the printed efficiency cell reproduces that quotient at its own printed precision of three significant figures.

raw_value_unit_evidence: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556) enzyme line 'T145A', the '+ 2 mM Pi' block: Km cell 1780 under column head 'Km (uM)'; kcat cell 10.7 under column head 'kcat (s-1)'; catalytic efficiency cell 6.01 x 10^3 under column head 'kcat/Km (M-1s-1)'. Printed with uncertainties as kcat 10.7 ± 0.33 s^-1, Km 1780 ± 210 uM, kcat/Km (6.01 ± 0.73) x 10^3 M^-1 s^-1.

row_label: Table 3, enzyme line 'T145A', the three '+ 2 mM Pi' kinetic columns


proof_lines: mutant enzyme H75A, in the absence of phosphate, at pH 8.0 and 25°C

proof_lines: mutant enzyme H75A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C


column_label: Table 1. Pi activation with different substrates. (PLoS ONE 2016, 11(10): e0164556); enzyme line 'CHA + 2 mM Pi'; column head 'Km (uM)' under the '+ 2 mM Pi' block = 104; column head 'kcat (s-1)' under the '+ 2 mM Pi' block = 145; column head 'kcat/Km (M-1s-1)' under the '+ 2 mM Pi' block = 1.40 x 10^6. The 'Ksi (mM)' column prints ND for this line.

normalized_value_unit_evidence: Km: printed cell 104 uM; 104 / 1000 = 0.104 mM. kcat: printed cell 145 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed cell 1.40 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.40 x 10^6 / 1000 = 1400.0 s^-1 mM^-1. That printed cell is the paper's own independently fitted catalytic efficiency, and it is the value this record carries for kcat_over_km.

raw_value_unit_evidence: Table 1. Pi activation with different substrates. (PLoS ONE 2016, 11(10): e0164556) enzyme line 'CHA + 2 mM Pi', the '+ 2 mM Pi' block: Km cell 104 under column head 'Km (uM)'; kcat cell 145 under column head 'kcat (s-1)'; catalytic efficiency cell 1.40 x 10^6 under column head 'kcat/Km (M-1s-1)'. Printed with uncertainties as kcat 145 ± 1.3 s^-1, Km 104 ± 9.9 uM, kcat/Km (1.40 ± 0.13) x 10^6 M^-1 s^-1.

row_label: Table 1, substrate line 'CHA', the three '+ 2 mM Pi' kinetic columns


sequence_variant_note: Resolved canonical sequence from UniProtKB A5W059 direct REST/FASTA lookup and applied mutation signature R40A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R40A, in the absence of phosphate, at pH 8.0 and 25°C

proof_lines: mutant enzyme R40A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C


enzyme_display_name: lactaldehyde dehydrogenase

substrate_name: (S)-lactaldehyde

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P25553 direct lookup; N286H reconstructed on 2026-06-04 and applied mutation signature N286H to reconstruct the assayed variant sequence.

enzyme: lactaldehyde dehydrogenase

substrate: (S)-lactaldehyde


sequence_source: UniProtKB reviewed P25553 direct lookup on 2026-06-04


sequence_source: UniProtKB reviewed P25553 direct lookup; N286H reconstructed on 2026-06-04


substrate_name: NAD+; H2O; L-Glyceraldehyde

assay_conditions_summary: pH 7; 310.15 K; cofactor NAD+

substrate: NAD+; H2O; L-Glyceraldehyde


organism: Methanocaldococcus jannaschii

substrate_name: H2O; NAD+; Lactaldehyde

sequence_source: UniProtKB reviewed Q58806 direct lookup on 2026-06-04

assay_conditions_summary: pH 7.5; cofactor NAD+

substrate: H2O; NAD+; Lactaldehyde


substrate_name: Lactaldehyde

smiles: CC(O)C=O

substrate: Lactaldehyde


substrate_name: propanal

smiles: CCC=O

substrate: propanal


substrate_name: L-Fuculose 1-phosphate

sequence_source: UniProtKB P0AB87 direct lookup, canonical context only

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

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant Del(207-215)

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant Del(211-215)

substrate: L-Fuculose 1-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 direct lookup plus explicit mutation reconstruction and applied mutation signature E214D/K207A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 direct lookup plus explicit mutation reconstruction and applied mutation signature E214L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant E214L


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 direct lookup plus explicit mutation reconstruction and applied mutation signature K207A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant K207A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5W059 and applied mutation signature G144V to reconstruct the assayed variant sequence.

column_label: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556); enzyme line 'G144V'; column head 'Km (uM)' under the '+ 2 mM Pi' block = 6830; column head 'kcat (s-1)' under the '+ 2 mM Pi' block = 0.394; column head 'kcat/Km (M-1s-1)' under the '+ 2 mM Pi' block = 57.7.

normalized_value_unit_evidence: Km: printed cell 6830 uM; 6830 / 1000 = 6.83 mM. kcat: printed cell 0.394 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed cell 57.7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 57.7 / 1000 = 0.0577 s^-1 mM^-1. The exact quotient of the two printed component cells is 0.394 / 6.83 = 0.057686676427525625 s^-1 mM^-1, and the printed efficiency cell reproduces that quotient at its own printed precision of three significant figures.

raw_value_unit_evidence: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556) enzyme line 'G144V', the '+ 2 mM Pi' block: Km cell 6830 under column head 'Km (uM)'; kcat cell 0.394 under column head 'kcat (s-1)'; catalytic efficiency cell 57.7 under column head 'kcat/Km (M-1s-1)'. Printed with uncertainties as kcat 0.394 ± 0.0090 s^-1, Km 6830 ± 440 uM, kcat/Km 57.7 ± 3.9 M^-1 s^-1.

row_label: Table 3, enzyme line 'G144V', the three '+ 2 mM Pi' kinetic columns


sequence_variant_note: Resolved canonical sequence from UniProtKB A5W059 direct lookup plus explicit mutation reconstruction and applied mutation signature R195A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R195A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C

proof_lines: mutant enzyme R195A, in the absence of phosphate, at pH 8.0 and 25°C


substrate_name: oxaloacetate

sequence_source: UniProtKB A5W059 direct lookup

substrate: oxaloacetate


sequence_variant_note: Resolved canonical sequence from UniProtKB A5W059 direct lookup plus explicit mutation reconstruction and applied mutation signature N71A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N71A, in the absence of phosphate, at pH 8.0 and 25°C

proof_lines: mutant enzyme N71A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C


organism: Rhizobium leguminosarum

substrate_name: H2O; Biuret

sequence_source: UniProtKB reviewed entry Q1M7F4; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/Q1M7F4.json).

substrate: H2O; Biuret


substrate_name: Biuret

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q1M7F4; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/Q1M7F4.json). and applied mutation signature Q215A to reconstruct the assayed variant sequence.

substrate: Biuret


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q1M7F4; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/Q1M7F4.json). and applied mutation signature F41L to reconstruct the assayed variant sequence.


substrate_name: Coenzyme A; H2O

sequence_source: UniProtKB reviewed entry Q12524; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/Q12524.json).

assay_conditions_summary: cofactor CoA

substrate: Coenzyme A; H2O


substrate_name: CoA-disulfide

substrate: CoA-disulfide


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry P0AB87; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/P0AB87.json). and applied mutation signature F131A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry P0AB87; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/P0AB87.json). and applied mutation signature E214A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant E214A


enzyme_display_name: alpha-L-fucosidase

substrate_name: p-nitrophenyl alpha-L-fucopyranoside

sequence_source: uniprot:P04066 canonical sequence checked 2026-06-04

proof_lines: mutant E70G, 50 mM sodium phosphate buffer, pH 6.8, 37°C

enzyme: alpha-L-fucosidase

substrate: p-nitrophenyl alpha-L-fucopyranoside


proof_lines: mutant E135G, 50 mM sodium phosphate buffer, pH 6.8, 37°C


proof_lines: mutant E289G, 50 mM sodium phosphate buffer, pH 6.8, 37°C, loss of catalytic activity


proof_lines: mutant D225G, 50 mM sodium phosphate buffer, pH 6.8, 37°C, loss of catalytic activity


proof_lines: mutant D258G, 50 mM sodium phosphate buffer, pH 6.8, 37°C


proof_lines: mutant E289Q, 50 mM sodium phosphate buffer, pH 6.8, 37°C, loss of catalytic activity


proof_lines: mutant D158G, 50 mM sodium phosphate buffer, pH 6.8, 37°C


proof_lines: mutant E275G, 50 mM sodium phosphate buffer, pH 6.8, 37°C


organism: Thermotoga maritima

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 canonical FASTA; row-specific variant reconstructed after validating mutation_signature residues. and applied mutation signature T264A/L322P to reconstruct the assayed variant sequence.

proof_lines:
40°C, mutant enzyme T264A/L322P
70°C, mutant enzyme T264A/L322P


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 canonical FASTA; row-specific variant reconstructed after validating mutation_signature residues. and applied mutation signature G226S/Y237H/T264A to reconstruct the assayed variant sequence.

proof_lines: 70°C, mutant enzyme G226S/Y237H/T264A/L322P4


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 canonical FASTA; row-specific variant reconstructed after validating mutation_signature residues. and applied mutation signature P196L/Y237H/Y267F to reconstruct the assayed variant sequence.

proof_lines:
40°C, mutant enzyme P196L/Y237H/Y267F
70°C, mutant enzyme P196L/Y237H/Y267F


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 canonical FASTA; row-specific variant reconstructed after validating mutation_signature residues. and applied mutation signature Y237H/Y267F/L322P to reconstruct the assayed variant sequence.

proof_lines:
70°C, mutant enzyme Y237H/Y267F/L322P
40°C, mutant enzyme Y237H/Y267F/L322P


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 canonical FASTA; row-specific variant reconstructed after validating mutation_signature residues. and applied mutation signature T264A to reconstruct the assayed variant sequence.

proof_lines:
40°C, mutant enzyme T264A
70°C, mutant enzyme T264A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 canonical FASTA; row-specific variant reconstructed after validating mutation_signature residues. and applied mutation signature T264A/Y267F/L322P to reconstruct the assayed variant sequence.

proof_lines:
40°C, mutant enzyme T264A/Y267F/L322P
70°C, mutant enzyme T264A/Y267F/L322P


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 canonical FASTA; row-specific variant reconstructed after validating mutation_signature residues. and applied mutation signature G226S/T264A/Y267F/L322P to reconstruct the assayed variant sequence.

proof_lines: 70°C, mutant enzyme G226S/T264A/Y267F/L322P

proof_lines: 40°C, mutant enzyme G226S/T264A/Y267F/L322P


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 canonical FASTA; row-specific variant reconstructed after validating mutation_signature residues. and applied mutation signature M210V/Y237H/T264A/Y267F to reconstruct the assayed variant sequence.

proof_lines: 40°C, mutant enzyme M210V/Y237H/T264A/Y267F

proof_lines: 70°C, mutant enzyme M210V/Y237H/T264A/Y267F


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

proof_lines: mutant E79G, 50 mM sodium phosphate buffer, pH 6.8, 37°C


substrate_name: 4-nitrophenyl alpha-L-fucopyranoside

substrate: 4-nitrophenyl alpha-L-fucopyranoside


sequence_source: UniProtKB P04066 canonical reviewed sequence; RCSB 7PLS/7PM4 structural entity maps to P04066

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


sequence_source: UniProtKB P04066 canonical reviewed sequence

assay_conditions_summary: pH 6.8; 310.15 K; buffer P04066 sequence identity preserved. 50 mM sodium phosphate

proof_lines: 50 mM sodium phosphate buffer, pH 6.8, 37°C


sequence_source: UniProtKB Q9BTY2 canonical reviewed sequence


organism: Mus musculus

sequence_source: UniProtKB Q99LJ1 canonical reviewed sequence


organism: Paenibacillus thiaminolyticus

sequence_source: UniProtKB K0JCW6 canonical unreviewed sequence; RCSB 6TVK polymer entity maps to K0JCW6


organism: Rattus norvegicus

substrate_name: p-Nitrophenyl-alpha-L-fucoside; H2O

sequence_source: UniProtKB reviewed entry P17164; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/P17164.json).

substrate: p-Nitrophenyl-alpha-L-fucoside; H2O


organism: Sulfolobus solfataricus

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

proof_lines: SABIO-RK modifier species: alpha-L-fucosidase(Enzyme) mutant Ssalpha-fuc


substrate_name: H2O; p-Nitrophenyl-alpha-L-fucoside

proof_lines: SABIO-RK modifier species: alpha-L-fucosidase(Enzyme) mutant Asp242Gly

substrate: H2O; p-Nitrophenyl-alpha-L-fucoside


substrate_name: p-Nitrophenyl-alpha-L-fucoside

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

substrate: p-Nitrophenyl-alpha-L-fucoside


organism: Tannerella forsythia

sequence_source: UniProtKB TrEMBL entry G8UMQ6; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/G8UMQ6.json).


substrate_name: alpha-L-fucosyl fluoride

sequence_source: UniProtKB TrEMBL entry Q9WYE2; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/Q9WYE2.json).

substrate: alpha-L-fucosyl fluoride


proof_lines:
70°C, wild-type enzyme
40°C, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB lookup of Q9WYE2 on 2026-06-04 plus row-specific reconstruction from the selected mutation_signature. and applied mutation signature M210V/Y237H/T264A to reconstruct the assayed variant sequence.

proof_lines:
70°C, mutant enzyme M210V/Y237H/T264A
40°C, mutant enzyme M210V/Y237H/T264A


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB lookup of Q9WYE2 on 2026-06-04 plus row-specific reconstruction from the selected mutation_signature. and applied mutation signature G226S/Y237H/T264A/L322P to reconstruct the assayed variant sequence.

proof_lines: 40°C, mutant enzyme G226S/Y237H/T264A/L322P


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB lookup of Q9WYE2 on 2026-06-04 plus row-specific reconstruction from the selected mutation_signature. and applied mutation signature R147G/L322P to reconstruct the assayed variant sequence.

proof_lines:
40°C, mutant enzyme R147G/L322P
70°C, mutant enzyme R147G/L322P


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB lookup of Q9WYE2 on 2026-06-04 plus row-specific reconstruction from the selected mutation_signature. and applied mutation signature M210V/Y237H/T264A/Y267F/L322P to reconstruct the assayed variant sequence.

proof_lines: 70°C, mutant enzyme M210V/Y237H/T264A/Y267F/L322P

proof_lines: 40°C, mutant enzyme M210V/Y237H/T264A/Y267F/L322P


organism: uncultured bacterium


organism: Wenyingzhuangia fucanilytica

sequence_source: UniProtKB:A0A1B1NX89 direct lookup on 2026-06-04


enzyme_display_name: malyl-CoA lyase

organism: Cereibacter sphaeroides

substrate_name: beta-methylmalyl-CoA

sequence_source: UniProtKB:Q3J5L6 direct lookup on 2026-06-04

assay_conditions_summary: 303.15 K; cofactor CoA

proof_lines: condensation of acetyl-CoA and glyoxylate, at 30°C

proof_lines: condensation of propionyl-CoA and glyoxylate, at 30°C

enzyme: malyl-CoA lyase

substrate: beta-methylmalyl-CoA


organism: Haloarcula marismortui

substrate_name: Glyoxylate; Propanoyl-CoA

substrate: Glyoxylate; Propanoyl-CoA


sequence_source: UniProtKB:Q5V463 direct lookup on 2026-06-04


organism: Rhodobacter sphaeroides

substrate_name: Acetyl-CoA

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

column_label: Table 1, Mcl1 condensation of acetyl-CoA + glyoxylate: kcat 8.6 s^-1 and target-substrate Km 0.1 mM, yielding current 85.99999999999999 s^-1 mM^-1. The table's printed 2.8 × 10^3 M^-1 s^-1 reaction efficiency uses glyoxylate (Km 3.1 mM); it is preserved separately and is not used as the target-substrate efficiency.

normalized_value_unit_evidence: Same-row Table 1 cells give kcat=8.6 s^-1 and target-substrate Km=0.1 mM. Their stored-precision quotient is 8.6 / 0.1 = 85.99999999999999 s^-1 mM^-1. The separately printed reaction efficiency is not the target-substrate quotient.

raw_value_unit_evidence: kcat raw_value=8.6 raw_unit=s^-1; Km raw_value=0.1 raw_unit=mM; printed reaction efficiency 2.8 × 10^3 M^-1 s^-1, denominator=glyoxylate (Km 3.1 mM)

row_label: Mcl1 / condensation of acetyl-CoA + glyoxylate

table_label: Table 1: Molecular and catalytic properties of recombinant (3S)-malyl-CoA/β-methylmalyl-CoA lyase and (3S)-malyl-CoA thioesterase from R. sphaeroides

substrate: Acetyl-CoA


enzyme_display_name: glucarate dehydratase

organism: Escherichia coli

substrate_name: D-Glucarate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AES2 FASTA and JSON direct REST check on 2026-06-04 and applied mutation signature H339Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant H339Q

enzyme: glucarate dehydratase

substrate: D-Glucarate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AES2 FASTA and JSON direct REST check on 2026-06-04 and applied mutation signature D366A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant D366A


substrate_name: L-idarate

sequence_source: UniProtKB:P0AES2 FASTA and JSON direct REST check on 2026-06-04

substrate: L-idarate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AES2 FASTA and JSON direct REST check on 2026-06-04 and applied mutation signature K207Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant K207Q


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AES2 FASTA and JSON direct REST check on 2026-06-04 and applied mutation signature Y150F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant Y150F


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AES2 FASTA and JSON direct REST check on 2026-06-04 and applied mutation signature H339N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant H339N


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AES2 FASTA and JSON direct REST check on 2026-06-04 and applied mutation signature H339A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant H339A


organism: Aspergillus niger

substrate_name: 4-nitrophenyl alpha-L-fucoside

substrate: 4-nitrophenyl alpha-L-fucoside


organism: Bombyx mori


organism: Clostridium perfringens

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


organism: Flavobacterium algicola


organism: Fusarium proliferatum


organism: Homo sapiens

proof_lines: mutant D276G, 50 mM sodium phosphate buffer, pH 6.8, 37°C


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot_reconstructed_variant and applied mutation signature D225N to reconstruct the assayed variant sequence.

proof_lines: mutant D225N, 50 mM sodium phosphate buffer, pH 6.8, 37°C


substrate_name: Glyoxylate

sequence_source: UniProtKB reviewed accession Q3J5L6 direct REST lookup on 2026-06-04

smiles: O=CC(=O)O

column_label: Table 1, Mcl1 condensation of propionyl-CoA plus glyoxylate: kcat 12 s^-1; target-substrate glyoxylate Km 4.1 mM; independently printed reaction efficiency 3.0 × 10^3 M^-1 s^-1 = 3.0 s^-1 mM^-1. The current stored specificity 2.9268292682926833 s^-1 mM^-1 is the deterministic quotient of the exact kcat and target-substrate Km cells; the independently printed value is not substituted for it.

normalized_value_unit_evidence: Same-reaction Table 1 cells give kcat=12 s^-1 and target-substrate Km=4.1 mM; their stored-precision quotient is 12 / 4.1 = 2.9268292682926833 s^-1 mM^-1; the independently printed efficiency normalizes separately to 3.0 s^-1 mM^-1 and is preserved as a distinct primary cell.

raw_value_unit_evidence: kcat raw_value=12 raw_unit=s^-1; glyoxylate Km raw_value=4.1 raw_unit=mM; independently printed reaction efficiency raw_value=3.0 × 10^3 raw_unit=M^-1 s^-1.

row_label: Mcl1 / condensation of propionyl-CoA plus glyoxylate

table_label: Table 1: Molecular and catalytic properties of recombinant (3S)-malyl-CoA/beta-methylmalyl-CoA lyase and (3S)-malyl-CoA thioesterase from R. sphaeroides

substrate: Glyoxylate


column_label: Table 1, Mcl1 cleavage of β-methylmalyl-CoA: kcat 2.8 s^-1; target-substrate Km 0.01 mM; printed kcat/Km 2.8 × 10^5 M^-1 s^-1 = 280 s^-1 mM^-1. Current 280 lies in the printed-efficiency rounding interval [275, 285) s^-1 mM^-1.

normalized_value_unit_evidence: Same-row Table 1 cells give kcat=2.8 s^-1 and target-substrate Km=0.01 mM. Their stored-precision quotient is 2.8 / 0.01 = 280 s^-1 mM^-1. Printed efficiency normalizes separately to 280 s^-1 mM^-1.

raw_value_unit_evidence: kcat raw_value=2.8 raw_unit=s^-1; Km raw_value=0.01 raw_unit=mM; printed kcat/Km raw_value=2.8 × 10^5 raw_unit=M^-1 s^-1

row_label: Mcl1 / cleavage of β-methylmalyl-CoA


substrate_name: Acetyl-CoA; Glyoxylate

substrate: Acetyl-CoA; Glyoxylate


substrate_name: Propanoyl-CoA

column_label: Table 1, Mcl1 condensation of propionyl-CoA + glyoxylate: kcat 12 s^-1 and target-substrate Km 0.2 mM, yielding current 60 s^-1 mM^-1. The table's printed 3.0 × 10^3 M^-1 s^-1 reaction efficiency uses glyoxylate (Km 4.1 mM); it is preserved separately and is not used as the target-substrate efficiency.

normalized_value_unit_evidence: Same-row Table 1 cells give kcat=12 s^-1 and target-substrate Km=0.2 mM. Their stored-precision quotient is 12 / 0.2 = 60 s^-1 mM^-1. The separately printed reaction efficiency is not the target-substrate quotient.

raw_value_unit_evidence: kcat raw_value=12 raw_unit=s^-1; Km raw_value=0.2 raw_unit=mM; printed reaction efficiency 3.0 × 10^3 M^-1 s^-1, denominator=glyoxylate (Km 4.1 mM)

row_label: Mcl1 / condensation of propionyl-CoA + glyoxylate

substrate: Propanoyl-CoA


substrate_name: L-Malyl-CoA

column_label: Table 1, Mcl1 cleavage of (3S)-malyl-CoA: kcat 2.5 s^-1; target-substrate Km 0.02 mM; printed kcat/Km 1.3 × 10^5 M^-1 s^-1 = 130 s^-1 mM^-1. Current 125 lies in the printed-efficiency rounding interval [125, 135) s^-1 mM^-1.

normalized_value_unit_evidence: Same-row Table 1 cells give kcat=2.5 s^-1 and target-substrate Km=0.02 mM. Their stored-precision quotient is 2.5 / 0.02 = 125 s^-1 mM^-1. Printed efficiency normalizes separately to 130 s^-1 mM^-1.

raw_value_unit_evidence: kcat raw_value=2.5 raw_unit=s^-1; Km raw_value=0.02 raw_unit=mM; printed kcat/Km raw_value=1.3 × 10^5 raw_unit=M^-1 s^-1

row_label: Mcl1 / cleavage of (3S)-malyl-CoA

substrate: L-Malyl-CoA


organism: Acinetobacter baylyi

sequence_source: UniProtKB reviewed accession Q6FFQ2 direct REST lookup on 2026-06-04

assay_conditions_summary: pH 7.5; 295.15 K; buffer 0.35 ug of D-glucarate dehydratase in 500 ul of Activity

column_label: Table label: TABLE 3 Kinetic parameters for D-glucarate dehydratase and KDG dehydratase. Row: D-Glucarate dehydratase. Columns read: Km (uM) cell 101, kcat (s^-1) cell 6.39, kcat/Km (s^-1 M^-1) cell 6.33 x 10^4. metric: kcat; raw value: 6.39; raw unit: s^-1; normalized value: 6.39 s^(-1); metric: Km; raw value: 101; raw unit: uM; normalized value: 0.101 mM; metric: kcat/Km; raw value: 6.33 x 10^4; raw unit: s^-1 M^-1; normalized value: 63.26732673267326 s^-1 mM^-1; assay condition: D-glucarate dehydratase assayed in Activity Buffer (50 mM Hepes/NaOH, pH 7.5, 100 mM NaCl, and 10% glycerol) containing 5 mM MgCl2; all enzymatic reactions were performed at 25 °C; kinetic parameters obtained from duplicate experiments by nonlinear analysis of initial rates.

normalized_value_unit_evidence: Table 3 row D-Glucarate dehydratase: Km 101 uM = 0.101 mM (1 uM = 0.001 mM); kcat 6.39 s^-1 = 6.39 s^(-1); kcat/Km 6.33 x 10^4 s^-1 M^-1 = 63.3 s^-1 mM^-1 at the printed cell's three-significant-figure precision, carried in the export at full precision as 63.26732673267326 s^-1 mM^-1, which is this row's own quotient 6.39 s^-1 / 0.101 mM and rounds back to the printed cell. In the Europe PMC PDF text render the plus-minus sign is written ⫾, the multiplication sign ⫻, the micro sign ␮ and the superscript minus one ⫺1, and superscript exponents are flattened, so the printed cell `6.33 ⫻ 104` is the paper's 6.33 x 10^4 s^-1 M^-1 and the unit header `␮M s⫺1 s⫺1 M⫺1` is uM, s^-1 and s^-1 M^-1.

raw_value_unit_evidence: TABLE 3 Kinetic parameters for D-glucarate dehydratase and KDG dehydratase; Values correspond to the average of two replicates. | metric header row of Table 3: `Enzyme Km kcat kcat/Km` | unit header row: `␮M s⫺1 s⫺1 M⫺1` | data row: `D-Glucarate dehydratase 101 ⫾ 15 6.39 ⫾ 0.26 6.33 ⫻ 104` | the D-Glucarate dehydratase cells read: Km = 101 ± 15 uM; kcat = 6.39 ± 0.26 s^-1; kcat/Km = 6.33 x 10^4 s^-1 M^-1.

row_label: D-Glucarate dehydratase


assay_conditions_summary: pH 7.5; 298.15 K; buffer 0.35 ug of D-glucarate dehydratase in 500 ul of Activity

table_label: TABLE 3 Kinetic parameters for D-glucarate dehydratase and KDG dehydratase


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0AES2 direct REST lookup plus K207R reconstruction on 2026-06-04 and applied mutation signature K207R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant K207R


organism: Paenibacillus thiaminolyticus

sequence_source: UniProtKB REST K0JCW6 canonical sequence checked 2026-06-04


sequence_source: UniProtKB REST E3PQQ9 canonical sequence checked 2026-06-04


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST E3PQQ9 canonical sequence checked 2026-06-04 and applied mutation signature W392A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST K0JCW6 canonical sequence checked 2026-06-04 and applied mutation signature H503A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST K0JCW6 canonical sequence checked 2026-06-04 and applied mutation signature E235Q to reconstruct the assayed variant sequence.


organism: Pedobacter sp. CAU209

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


enzyme_display_name: 8-amino-7-oxononanoate synthase

organism: Unknown

substrate_name: L-alanine

enzyme: 8-amino-7-oxononanoate synthase

substrate: L-alanine


sequence_variant_note: Resolved canonical sequence from direct UniProtKB lookup for P0AES2; D366N reconstructed from the reviewed canonical sequence and applied mutation signature D366N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant D366N


sequence_variant_note: Resolved canonical sequence from direct UniProtKB lookup for P0AES2; N341D reconstructed from the reviewed canonical sequence and applied mutation signature N341D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant N341D


sequence_variant_note: Resolved canonical sequence from direct UniProtKB lookup for P0AES2; N341L reconstructed from the reviewed canonical sequence and applied mutation signature N341L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant N341L


sequence_source: direct UniProtKB lookup for reviewed P0AES2 canonical sequence

assay_conditions_summary: pH 8; 295.15 K; buffer pH 8

column_label: Table 1: Kinetic Constants for Enzymes in the (D)-Glucarate/Galactarate Catabolic Pathway (Biochemistry 1998, volume 37, pages 14369-14375); printed column heads kcat (s^-1) | Km (uM) | kcat/Km (M^-1 s^-1). Table 1, row GlucD (glucarate); column kcat (s^-1) = 20; column Km (uM) = 60; column kcat/Km (M^-1 s^-1) = 3.3 x 10^5. captured primary segment: GlucD (glucarate) | kcat 20 ± 1 s^-1 | Km 60 ± 2 uM | kcat/Km 3.3 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 20 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 20.0 s^(-1); the exported value is 20.0 s^(-1). Km: printed Table 1 cell 60 uM; 1 uM is 1/1000 mM, so 60 / 1000 = 0.06 mM; the exported value is 0.06 mM. kcat/Km: printed Table 1 cell 3.3 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.3 x 10^5 / 1000 = 330.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 20.0 / 0.06 = 333.33333333333337 s^-1 mM^-1, the exported value, and the printed efficiency cell is that quotient written to the two significant figures the table uses.

raw_value_unit_evidence: Table 1, row GlucD (glucarate): kcat = 20 s^-1; Km = 60 uM; printed kcat/Km = 3.3 x 10^5 M^-1 s^-1.

row_label: Table 1, row GlucD (glucarate)


substrate_name: L-Idarate

substrate: L-Idarate


organism: Pseudomonas putida


substrate_name: UDP-N-acetylglucosamine

substrate: UDP-N-acetylglucosamine


enzyme_display_name: nitrile hydratase

organism: Comamonas testosteroni

substrate_name: acrylonitrile

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

proof_lines: pH 7.0, 25°C, alpha-subunit mutant enzyme H80W/H81W

enzyme: nitrile hydratase

substrate: acrylonitrile


proof_lines: pH 7.0, 25°C, alpha-subunit mutant enzyme R157K


sequence_source: UniProtKB:J9PBS0 direct accession lookup on 2026-06-04


proof_lines: pH 7.0, 25°C, alpha-subunit mutant enzyme H80A


proof_lines: pH 7.0, 25°C, alpha-subunit mutant enzyme H80A/H81A


organism: Klebsiella oxytoca

sequence_source: UniProtKB:A0A0H3HE78 direct accession lookup on 2026-06-04


organism: Monosiga brevicollis

substrate_name: Benzonitrile; acrylonitrile

sequence_source: UniProtKB:A9V2C1 direct accession lookup on 2026-06-04

substrate: Benzonitrile; acrylonitrile


smiles: C=CC#N


substrate_name: Benzonitrile

sequence_source: UniProtKB A9V2C1 direct lookup

substrate: Benzonitrile


organism: Nocardia sp.

sequence_source: UniProtKB Q8GJG6 direct lookup


proof_lines: recombinant NHase with modified start codon only


proof_lines: 25°C, pH not specified in the publication, beta-subunit mutant enzyme T173Y


proof_lines: 25°C, pH not specified in the publication, beta-subunit mutant enzyme S189E


proof_lines: 25°C, pH not specified in the publication, beta-subunit mutant enzyme M150C


proof_lines: 25°C, pH not specified in the publication, subunit-fused wild-type nitrile hydratase


organism: Pseudonocardia thermophila


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y114T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T109S to reconstruct the assayed variant sequence.


substrate_name: Methacrylonitrile

smiles: C=C(C)C#N

substrate: Methacrylonitrile


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y68F to reconstruct the assayed variant sequence.


organism: Escherichia coli

proof_lines:
isoenzyme B
isoenzyme A


enzyme_display_name: beta-ureidopropionase

substrate_name: N-Carbamoyl-beta-alanine

enzyme: beta-ureidopropionase

substrate: N-Carbamoyl-beta-alanine


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


organism: Rhodococcus rhodochrous

smiles: N#CCCCCC(=N)O


substrate_name: cyanoacetamide

smiles: N#CCC(=N)O

substrate: cyanoacetamide


substrate_name: Methacrylonitrile / 4-cyanopyridine / 3-Cyanopyridine / Benzonitrile / acrylonitrile

proof_lines: pH 7.6, 25°C, recombinant wild-type enzyme


substrate_name: Benzonitrile / acrylonitrile / Methacrylonitrile

proof_lines: pH 7.6, 25°C, recombinant mutant betaY68F

proof_lines: pH 7.6, 25°C, recombinant mutant alphaY114T

proof_lines: pH 7.6, 25°C, recombinant mutant alphaT109S


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature Y114T to reconstruct the assayed variant sequence.


source_db: brenda/skid

proof_lines:
pH 7.5, 25°C
Raw SKiD Env: Temp=25°C, pH=7.6

substrate: Methacrylonitrile / 4-cyanopyridine / 3-Cyanopyridine / Benzonitrile / acrylonitrile

source: brenda/skid


organism: Rhodococcus erythropolis

substrate_name: H2O; Methacrylonitrile

sequence_variant_note: Resolved canonical sequence from UniProt P13448 canonical alpha sequence with alpha-Q90E reconstructed as UniProt Q91E; P13449 beta partner checked by UniProt. and applied mutation signature Q90E with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: nitrile hydratase(Enzyme) mutant alpha-Q90E

substrate: H2O; Methacrylonitrile


substrate_name: (S)-mandelonitrile

sequence_variant_note: Resolved canonical sequence from UniProt P29379 canonical beta sequence with beta-F37H reconstructed; P29378 alpha partner checked by UniProt. and applied mutation signature F37H to reconstruct the assayed variant sequence.

substrate: (S)-mandelonitrile


sequence_source: UniProt P29378 canonical alpha-subunit sequence; source-listed P29379 beta partner checked by UniProt when present.


substrate_name: (R)-mandelonitrile

substrate: (R)-mandelonitrile


sequence_variant_note: Resolved canonical sequence from UniProt P29379 canonical beta sequence with beta-F37H reconstructed; BRENDA-listed P29378 alpha accession checked by UniProt. and applied mutation signature F37H to reconstruct the assayed variant sequence.


sequence_source: UniProt P29378 canonical alpha-subunit sequence.

proof_lines:
pH 7.4, 10°C, wild-type enzyme
pH 7.4, 35°C, wild-type enzyme


substrate_name: synthetic histone H3K18 decanoyllysine peptide

source_db: uniprot

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

source: uniprot


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: NAD(+)

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

substrate: NAD(+)


assay_conditions_summary: cofactor NAD+


organism: Escherichia coli (strain K12)

substrate_name: pimeloyl-CoA (at pH 7.5 and at 30 degrees Celsius)

assay_conditions_summary: pH 7.5; cofactor CoA


organism: Lysinibacillus sphaericus

substrate_name: pimeloyl-CoA (at pH 7.0 and at 37 degrees Celsius)

assay_conditions_summary: pH 7; cofactor CoA


organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: L-glycine (with acetyl-CoA at pH 6 and at 70 degrees Celsius)


organism: Xanthomonas campestris pv. campestris

substrate_name: UDP-glucuronate

substrate: UDP-glucuronate


enzyme_display_name: uracil phosphoribosyltransferase

organism: Bacillus caldolyticus

substrate_name: uracil

enzyme: uracil phosphoribosyltransferase

substrate: uracil


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

substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate (in the presence of 1 mM GTP)


organism: Toxoplasma gondii


enzyme_display_name: acetyl-CoA C-acyltransferase

organism: Arabidopsis thaliana

substrate_name: acetoacetyl-CoA (at 25 degrees Celsius)

enzyme: acetyl-CoA C-acyltransferase

substrate: acetoacetyl-CoA (at 25 degrees Celsius)


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


organism: Rattus norvegicus


organism: Sinorhizobium meliloti

substrate_name: acetamiprid

sequence_source: UniProtKB:V5RFK1 direct lookup; NCBI Protein AHB33637.1

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

substrate: acetamiprid


substrate_name: thiacloprid

substrate: thiacloprid


substrate_name: Benzonitrile


organism: Streptomyces rimosus

sequence_source: UniProtKB:B6CWJ3 direct lookup; NCBI Protein ACF06641.1

assay_conditions_summary: pH 65

proof_lines: pH 65, temperature not specified in the publication, recombinant trimeric enzyme

proof_lines: pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme


enzyme_display_name: serine--glyoxylate transaminase

organism: Hyphomicrobium methylovorum

substrate_name: glyoxylate

enzyme: serine--glyoxylate transaminase

substrate: glyoxylate


enzyme_display_name: histidinol-phosphate transaminase

organism: Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)

substrate_name: histidinol phosphate

enzyme: histidinol-phosphate transaminase

substrate: histidinol phosphate


enzyme_display_name: rhodopsin kinase

organism: Danio rerio

substrate_name: rhodopsin

enzyme: rhodopsin kinase

substrate: rhodopsin


organism: Homo sapiens

assay_conditions_summary: cofactor ATP


enzyme_display_name: mitogen-activated protein kinase

substrate_name: ATP

enzyme: mitogen-activated protein kinase

substrate: ATP


organism: Caldalkalibacillus thermarum


organism: Comamonas testosteroni

substrate_name: acrylonitrile

sequence_source: UniProtKB:J9PBS0; RCSB:4FM4 entity 1

proof_lines: pH 7.0, 25°C, alpha-subunit mutant enzyme H81A

substrate: acrylonitrile


proof_lines: pH 7.0, 25°C, alpha-subunit mutant enzyme R157A


organism: Rhodococcus erythropolis

substrate_name: Methacrylonitrile; H2O

substrate: Methacrylonitrile; H2O


substrate_name: H2O; Methacrylonitrile

proof_lines: SABIO-RK modifier species: nitrile hydratase(Enzyme) mutant alpha-Q90N


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13449 with direct R56K substitution check and applied mutation signature R56K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: nitrile hydratase(Enzyme) mutant beta-R56K


enzyme_display_name: membrane alanyl aminopeptidase

substrate_name: Cys-Gly

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

enzyme: membrane alanyl aminopeptidase

substrate: Cys-Gly


organism: Brucella melitensis

sequence_source: UniProtKB:Q8YG38 direct REST lookup, fetched 2026-06-04


organism: Escherichia coli

substrate_name: H2O; Leu-p-nitroanilide

sequence_source: UniProtKB:P04825 direct REST lookup, fetched 2026-06-04

substrate: H2O; Leu-p-nitroanilide


sequence_source: UniProtKB:P15144 direct REST lookup, fetched 2026-06-04


substrate_name: H2O; Arg-4-methylcoumaryl-7-amide

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

substrate: H2O; Arg-4-methylcoumaryl-7-amide


organism: Lactococcus lactis subsp. cremoris

substrate_name: H2O; Arg-Phe

sequence_source: UniProtKB:P0C2T8 direct REST lookup, fetched 2026-06-04

substrate: H2O; Arg-Phe


organism: Neisseria meningitidis serogroup B

substrate_name: Unknown

sequence_source: UniProtKB:Q9JYV4 direct REST lookup, fetched 2026-06-04

substrate: Unknown


enzyme_display_name: pyridoxal phosphatase

substrate_name: pyridoxal 5'-phosphate

enzyme: pyridoxal phosphatase

substrate: pyridoxal 5'-phosphate


substrate_name: lacto-N-fucopentaose II

substrate: lacto-N-fucopentaose II


enzyme_display_name: glucan 1,3-beta-glucosidase

organism: Candida albicans (strain SC5314 / ATCC MYA-2876)

substrate_name: laminaribiose

enzyme: glucan 1,3-beta-glucosidase

substrate: laminaribiose


organism: Escherichia coli (strain K12)


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)


organism: Mus musculus

substrate_name: ATP (when both Thr-180 and Tyr-182 are phosphorylated)


enzyme_display_name: ribokinase

enzyme: ribokinase


substrate_name: ribose (in the presence of 10 mM inorganic phosphate)


organism: Staphylococcus aureus (strain COL)

substrate_name: ATP (in absence of K(+))

substrate: ATP (in absence of K(+))


enzyme_display_name: glutamate 5-kinase

organism: Leishmania donovani

substrate_name: L-glutamate

enzyme: glutamate 5-kinase

substrate: L-glutamate


substrate_name: dTTP

substrate: dTTP


organism: Arabidopsis thaliana


organism: Rattus norvegicus

substrate_name: N-carbamoyl-beta-alanine

smiles: C(CNC(=O)N)C(=O)O

substrate: N-carbamoyl-beta-alanine


enzyme_display_name: dimethylargininase

substrate_name: asymmetric dimethylarginine (ADMA)

enzyme: dimethylargininase

substrate: asymmetric dimethylarginine (ADMA)


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

substrate_name: N-methyl-L-arginine

substrate: N-methyl-L-arginine


enzyme_display_name: thiamine-triphosphatase

organism: Homo sapiens

substrate_name: thiamine triphosphate

enzyme: thiamine-triphosphatase

substrate: thiamine triphosphate


substrate_name: adenosine 5'-phosphoramidate (at pH 6.8)


organism: Plasmodium falciparum


substrate_name: H2O; L-Alanylglycine

substrate: H2O; L-Alanylglycine


organism: Sus scrofa

substrate_name: H2O; Leu-p-nitroanilide


organism: Trypanosoma congolense


substrate_name: P(1)-P(3)-bis(5'-adenosyl) triphosphate

substrate: P(1)-P(3)-bis(5'-adenosyl) triphosphate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


enzyme_display_name: 8-oxo-dGTP diphosphatase

substrate_name: NADH (in the presence of 5 mM of manganese)

assay_conditions_summary: cofactor NADH

enzyme: 8-oxo-dGTP diphosphatase


organism: Bacillus subtilis (strain 168)

substrate_name: dGTP

substrate: dGTP


enzyme_display_name: oxaloacetate decarboxylase

organism: Pseudomonas putida (strain ATCC 700007 / DSM 6899 / JCM 31910 / BCRC 17059 / LMG 24140 / F1)

substrate_name: oxaloacetate (in presence of 1 mM of magnesium)

enzyme: oxaloacetate decarboxylase


organism: Pseudomonas straminea


enzyme_display_name: histone acetyltransferase

substrate_name: histone H4 peptide

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accessions endpoint checked 2026-06-04; accession O14929 and applied mutation signature E64A to reconstruct the assayed variant sequence.

proof_lines: mutant E64A, pH not specified in the publication, temperature not specified in the publication

enzyme: histone acetyltransferase

substrate: histone H4 peptide


substrate_name: acetyl-CoA

sequence_source: UniProtKB REST accessions endpoint checked 2026-06-04; accession Q9H7Z6

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines: at 0.030 mM histone H4 peptide, pH and temperature not specified in the publication

proof_lines: at 0.090 mM histone H4 peptide, pH and temperature not specified in the publication

substrate: acetyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accessions endpoint checked 2026-06-04; accession Q92830 and applied mutation signature T612G to reconstruct the assayed variant sequence.

proof_lines: mutant GCN5 T612G, pH and temperature not specified in the publication


sequence_source: UniProtKB REST accessions endpoint checked 2026-06-04; accession Q92830

proof_lines: wild-type GCN5, pH and temperature not specified in the publication


sequence_source: UniProtKB REST accessions endpoint checked 2026-06-04; accession Q09472

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

proof_lines: pH and temperature not specified in the publication


substrate_name: Unknown

sequence_source: UniProtKB REST accessions endpoint checked 2026-06-04; accession Q92831


sequence_source: UniProtKB REST accessions endpoint checked 2026-06-04; accession O14929

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accessions endpoint checked 2026-06-04; accession O14929 and applied mutation signature Y282A to reconstruct the assayed variant sequence.

proof_lines: 30°C, pH not specified in the publication, mutant enzyme Y282A


substrate_name: histone H3

assay_conditions_summary: pH 8

proof_lines: mutant having m-fluorophenylalanine incorporated, pH 8.0, temperature not specified in the publication

proof_lines: mutant having p-fluorophenylalanine incorporated, pH 8.0, temperature not specified in the publication

substrate: histone H3


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


sequence_variant_note: Resolved canonical sequence from UniProt O14929 canonical sequence with BRENDA/PMID 22615379 mutation W199A reconstructed after residue check and applied mutation signature W199A to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor CoA

proof_lines: mutant W199A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt O14929 canonical sequence with BRENDA/PMID 22615379 mutation E187Q reconstructed after residue check and applied mutation signature E187Q to reconstruct the assayed variant sequence.

proof_lines: mutant E187Q, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt O14929 canonical sequence with BRENDA/PMID 22615379 mutation D277N reconstructed after residue check and applied mutation signature D277N to reconstruct the assayed variant sequence.

proof_lines: mutant D277N, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt O14929 canonical sequence with BRENDA/PMID 22615379 mutation D62A reconstructed after residue check and applied mutation signature D62A to reconstruct the assayed variant sequence.

proof_lines: mutant D62A, pH not specified in the publication, temperature not specified in the publication


sequence_source: UniProt O14929 canonical reviewed sequence checked directly against PubMed/RCSB HAT1 context

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