organism: Streptomyces coelicolor

substrate_name: GTP

sequence_variant_note: Resolved canonical sequence from UniProt Q9ZBP9 with G222V reconstructed during review and applied mutation signature G222V to reconstruct the assayed variant sequence.

substrate: GTP


enzyme_display_name: signal-recognition-particle GTPase

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProt Q9ZBP9 with T226S reconstructed during review and applied mutation signature T226S to reconstruct the assayed variant sequence.

mutation_type: substitution

enzyme: signal-recognition-particle GTPase

source: brenda


sequence_variant_note: Resolved canonical sequence from UniProt O69874 with A145S reconstructed during review and applied mutation signature A145S to reconstruct the assayed variant sequence.


enzyme_display_name: indolepyruvate decarboxylase

organism: Enterobacter cloacae

substrate_name: 4-ethyl-benzoylformic acid

mutation_signature: Unknown

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

enzyme: indolepyruvate decarboxylase

substrate: 4-ethyl-benzoylformic acid


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


enzyme_display_name: nucleoside diphosphate phosphatase

organism: Acer pseudoplatanus

substrate_name: GDP

proof_lines:
isoenzyme 1
isoenzyme 2

enzyme: nucleoside diphosphate phosphatase

substrate: GDP


enzyme_display_name: carboxypeptidase M

organism: Unknown

substrate_name: bradykinin

enzyme: carboxypeptidase M

substrate: bradykinin


enzyme_display_name: omega-amidase

organism: Zea mays

source_db: oed

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

enzyme: omega-amidase

source: oed


sequence_source: UniProtKB:B8A0E5 direct lookup

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


organism: Homo sapiens

sequence_source: UniProtKB:O75354 direct lookup

proof_lines: in presence of Ca2+, wild-type and mutant enzyme


organism: Rattus norvegicus

substrate_name: UDP; H2O

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

sequence_source: UniProtKB:Q8K4Y7 direct lookup

assay_conditions_summary: pH 7

substrate: UDP; H2O


organism: Staphylococcus aureus

substrate_name: UDP

verification_status: unverified

sequence_source: UniProtKB:Q7A4T2 direct lookup

data_origin: experimental

substrate: UDP

status: unverified


substrate_name: TDP

assay_conditions_summary: pH 7.5; 299.15 K; cofactor ADP

substrate: TDP


substrate_name: ADP

substrate: ADP


organism: Toxoplasma gondii

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q27895 direct REST/FASTA check; R492G reconstructed from the checked canonical sequence. and applied mutation signature R492G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; cofactor ATP

proof_lines: mutant enzyme R492G, at pH 7.4, temperature not specified in the publication


sequence_source: UniProtKB reviewed accession Q27895 direct REST/FASTA check.

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


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q27895 direct REST/FASTA check; R492G/E493G reconstructed from the checked canonical sequence. and applied mutation signature R492G/E493G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R492G/E493G, at pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q27895 direct REST/FASTA check; E493G reconstructed from the checked canonical sequence. and applied mutation signature E493G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E493G, at pH 7.4, temperature not specified in the publication


substrate_name: H2O; Dansyl-Ala-Arg

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

sequence_source: UniProtKB P14384 canonical sequence, release 2026_02; variant reconstructed from UniProt mutagenesis feature E277Q with PubMed evidence 12457462.

sequence_variant_note: Mutation signature E260Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: carboxypeptidase M(Enzyme) mutant E260Q

substrate: H2O; Dansyl-Ala-Arg


substrate_name: Dansyl-Ala-Arg; H2O

sequence_source: UniProtKB P14384 canonical sequence, release 2026_02; variant reconstructed from UniProt mutagenesis feature E277A with PubMed evidence 12457462.

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +13, so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: carboxypeptidase M(Enzyme) mutant E260A

substrate: Dansyl-Ala-Arg; H2O


substrate_name: Bradykinin

sequence_source: UniProtKB P14384 canonical sequence, release 2026_02.

substrate: Bradykinin


substrate_name: Met-enkephalin-Arg; H2O

proof_lines:
CPMwt, pH 7.2, 37°C
hCPM, pH 7.2, 37°C
CPMwt, pH 7.4, 37°C

substrate: Met-enkephalin-Arg; H2O


substrate_name: Leu-enkephalin-Arg

substrate: Leu-enkephalin-Arg


enzyme_display_name: chymosin

organism: Alces alces alces

substrate_name: kappa-casein

enzyme: chymosin

substrate: kappa-casein


organism: Bos taurus

substrate_name: AFPLEFEREL

sequence_source: UniProtKB P00794 canonical sequence, release 2026_02.

substrate: AFPLEFEREL


substrate_name: AFPLEFFREL

substrate: AFPLEFFREL


sequence_source: UniProt REST FASTA exact accession Q7A4T2


substrate_name: CDP

substrate: CDP


sequence_variant_note: Resolved canonical sequence from UniProt REST FASTA exact accession Q7A4T2 with W58A applied and applied mutation signature W58A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor ADP

proof_lines: mutant W58A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt REST FASTA exact accession Q7A4T2 with Y88A applied and applied mutation signature Y88A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: mutant Y88A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from UniProt REST FASTA exact accession Q7A4T2 with N45A applied and applied mutation signature N45A to reconstruct the assayed variant sequence.

proof_lines: mutant N45A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication

substrate: ATP


proof_lines: wild-type, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt REST FASTA exact accession Q7A4T2 with E126A applied and applied mutation signature E126A to reconstruct the assayed variant sequence.

proof_lines: mutant E126A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication


sequence_source: UniProt REST FASTA exact accession Q9FBN7


enzyme_display_name: spermidine synthase

organism: Escherichia coli

substrate_name: S-adenosylmethioninamine

sequence_variant_note: Resolved canonical sequence from UniProtKB P09158 direct lookup; P165A reconstructed from canonical sequence after residue check. and applied mutation signature P165A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant SPS mutant P165A

enzyme: spermidine synthase

substrate: S-adenosylmethioninamine


sequence_variant_note: Resolved canonical sequence from UniProtKB P09158 direct lookup; P162A reconstructed from canonical sequence after residue check. and applied mutation signature P162A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant SPS mutant P162A


sequence_variant_note: Resolved canonical sequence from UniProtKB P09158 direct lookup; C159A reconstructed from canonical sequence after residue check. and applied mutation signature C159A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant SPS mutant C159A


sequence_source: UniProtKB P09158 direct FASTA/JSON lookup.

proof_lines: pH 7.5, 37°C, recombinant wild-type enzyme and SPS mutant C159S


sequence_variant_note: Resolved canonical sequence from UniProtKB P09158 direct lookup; I163A reconstructed from canonical sequence after residue check. and applied mutation signature I163A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant SPS mutant I163A


sequence_source: UniProtKB P09158 direct lookup; I163A reconstructed from canonical sequence after residue check.


sequence_variant_note: Resolved canonical sequence from UniProtKB P09158 direct lookup; T160A reconstructed from canonical sequence after residue check. and applied mutation signature T160A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant SPS mutant T160A


sequence_source: UniProtKB P09158 direct lookup; P165A reconstructed from canonical sequence after residue check.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P09158 (SPEE_ECOLI), direct REST lookup during curation review and applied mutation signature C159A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P09158 (SPEE_ECOLI), direct REST lookup during curation review and applied mutation signature P162A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P09158 (SPEE_ECOLI), direct REST lookup during curation review and applied mutation signature T160A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P09158 (SPEE_ECOLI), direct REST lookup during curation review and applied mutation signature C159S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed P09158 (SPEE_ECOLI), direct REST lookup during curation review

proof_lines: pH 7.5, 37°C, recombinant SPS mutant C159S


source_db: skid

source_license: CC BY-NC-ND 4.0

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

source: skid


substrate_name: Putrescine

sequence_source: UniProtKB reviewed P19623 (SPEE_HUMAN), direct REST lookup during curation review

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

smiles: NCCCCN

substrate: Putrescine


substrate_name: Putrescine; S-Adenosylmethioninamine

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

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

source_databases_merged: sabio_rk brenda skid

substrate: Putrescine; S-Adenosylmethioninamine


substrate_name: AFPLEFIREL

sequence_source: UniProtKB:P00794 direct accession lookup

substrate: AFPLEFIREL


substrate_name: AFPLEFKREL

substrate: AFPLEFKREL


substrate_name: Casein; H2O

unit: lgwedgeoneswedgeone

substrate: Casein; H2O


substrate_name: H2O; Casein

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: chymosin(Enzyme) mutant GTPP(21-24)GG pseudochymosin

proof_lines: SABIO-RK modifier species: chymosin(Enzyme) mutant GTPP(21-24)SG pseudochymosin

substrate: H2O; Casein


organism: Capra hircus

substrate_name: fluorescein thiocarbamoyl-kappa-casein

sequence_source: UniProtKB:Q5VK60 direct accession lookup

substrate: fluorescein thiocarbamoyl-kappa-casein


organism: Cervus canadensis sibiricus

sequence_source: UniProtKB:A0A7D3Q7Y7 direct accession lookup


organism: Arabidopsis thaliana

substrate_name: H2O; 2-Oxosuccinamate

sequence_source: UniProtKB:Q8RUF8 direct accession lookup

proof_lines: pH 8.5, 30°C, recombinant His-tagged enzyme

substrate: H2O; 2-Oxosuccinamate


sequence_source: UniProtKB:B8A2V8 direct accession lookup


organism: Plasmodium falciparum

substrate_name: putrescine

sequence_source: UniProtKB unreviewed Q9NFS5 (Q9NFS5_PLAFA), direct UniProt REST lookup during curation review

substrate: putrescine


organism: Pyrococcus furiosus

sequence_source: UniProtKB reviewed Q8U4G1 (SPEE_PYRFU), direct UniProt REST lookup during curation review


substrate_name: S-Adenosylmethioninamine; Putrescine

substrate: S-Adenosylmethioninamine; Putrescine


organism: Synechococcus elongatus

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

sequence_source: UniProtKB reviewed Q31QK9 (SPEE_SYNE7), direct UniProt REST lookup during curation review

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

source_databases_merged: brenda skid


organism: Thermotoga maritima

km_display: Not reported

sequence_source: UniProtKB reviewed Q9WZC2 (SPEE_THEMA), direct UniProt REST lookup during curation review

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

proof_lines: pH 7.5, 80°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9WZC2 (SPEE_THEMA), direct UniProt REST lookup during curation review and applied mutation signature D101I to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: spermidine synthase(Enzyme) mutant D101I


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9WZC2 (SPEE_THEMA), direct UniProt REST lookup during curation review and applied mutation signature D170A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: spermidine synthase(Enzyme) mutant D170A


sequence_source: UniProtKB:Q9WZC2 direct REST lookup; selected SABIO-RK/BRENDA/SKiD records also name Q9WZC2.

proof_lines:
pH 7.5, 37°C, recombinant enzyme
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=80°C, pH=7.5


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9WZC2 direct REST lookup plus selected mutation signature Y76F. and applied mutation signature Y76F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: spermidine synthase(Enzyme) mutant Y76F


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9WZC2 direct REST lookup plus selected mutation signature D173A. and applied mutation signature D173A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: spermidine synthase(Enzyme) mutant D173A


organism: Trypanosoma brucei

sequence_source: UniProtKB:Q38EH6 direct REST lookup; selected BRENDA records name Q38EH6.


enzyme_display_name: carbamate kinase

organism: Enterococcus faecalis

substrate_name: ADP

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

assay_conditions_summary: pH 8.15; 298.15 K; cofactor ADP

enzyme: carbamate kinase

substrate: ADP


substrate_name: Carbamoyl phosphate; GDP

substrate: Carbamoyl phosphate; GDP


substrate_name: ADP; Carbamoyl phosphate

assay_conditions_summary: cofactor ATP

substrate: ADP; Carbamoyl phosphate


substrate_name: Acetate; ATP

sequence_source: UniProtKB:P0A2X7 direct REST lookup; selected SABIO-RK record names P0A2X7.

substrate: Acetate; ATP


enzyme_display_name: RNA uridylyltransferase

substrate_name: UTP

sequence_variant_note: Resolved canonical sequence from UniProtKB Q381M1 direct accession FASTA; variant sequence reconstructed from selected mutation note and applied mutation signature N147A to reconstruct the assayed variant sequence.

enzyme: RNA uridylyltransferase

substrate: UTP


sequence_variant_note: Resolved canonical sequence from UniProtKB Q381M1 direct accession FASTA; variant sequence reconstructed from selected mutation note and applied mutation signature R141A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q381M1 direct accession FASTA; variant sequence reconstructed from selected mutation note and applied mutation signature S188A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q381M1 direct accession FASTA; variant sequence reconstructed from selected mutation note and applied mutation signature D297N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q381M1 direct accession FASTA; variant sequence reconstructed from selected mutation note and applied mutation signature E300A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q381M1 direct accession FASTA; variant sequence reconstructed from selected mutation note and applied mutation signature D297A to reconstruct the assayed variant sequence.


substrate_name: RNA

sequence_variant_note: Resolved canonical sequence from UniProtKB Q381M1 direct accession FASTA; variant sequence reconstructed from selected mutation note and applied mutation signature R121A to reconstruct the assayed variant sequence.

substrate: RNA


sequence_source: UniProtKB Q381M1 direct accession FASTA


substrate_name: GTP; H2O

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

proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant E250K

substrate: GTP; H2O


substrate_name: H2O; GTP

proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant R196Q

substrate: H2O; GTP


proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant R98G


proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant G192D


proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant G147E


proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant V220M


proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant Y207C


organism: Sulfolobus acidocaldarius

substrate_name: GTP

sequence_variant_note: Resolved canonical sequence from UniProtKB O07853 direct accession lookup; G187K reconstructed from the canonical SRP54 sequence and applied mutation signature G187K to reconstruct the assayed variant sequence.

proof_lines: SRP54(G187K)-FtsY, in the presence of 7S RNA, pH and temperature not specified in the publication

substrate: GTP


proof_lines: SRP54, in the absence of 7S RNA, pH and temperature not specified in the publication

proof_lines: SRP54-FtsY, in the absence of 7S RNA, pH and temperature not specified in the publication


organism: Unknown

substrate_name: menadione

substrate: menadione


organism: Enterococcus faecium

substrate_name: acetate

sequence_source: UniProtKB reviewed accession P0A2X8 (organism-correct Enterococcus faecium carbamate kinase 1, EC 2.7.2.2); source accession P0A2X7 has the same sequence but is annotated to Enterococcus faecalis.

substrate: acetate


substrate_name: Carbamate; ATP

sequence_source: UniProtKB reviewed accession P37306 (Escherichia coli K-12 carbamate kinase, EC 2.7.2.2).

substrate: Carbamate; ATP


organism: Giardia duodenalis

substrate_name: Carbamate

sequence_source: UniProtKB accession A8BB85 (Giardia intestinalis strain ATCC 50803 / WB clone C6 carbamate kinase); accession references PMID 20383005 and PDB 3KZF.

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

substrate: Carbamate


organism: Giardia intestinalis

substrate_name: Carbamoyl phosphate

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

smiles: NC(=O)OP(=O)(O)O

substrate: Carbamoyl phosphate


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ADP


sequence_source: UniProtKB accession A8BB85 (Giardia intestinalis strain ATCC 50803 / WB clone C6 carbamate kinase).


sequence_source: UniProtKB reviewed accession P95474 (Pyrococcus furiosus carbamate kinase, EC 2.7.2.2); accession references PMID 10860751 and PDB 1E19.

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


organism: Homo sapiens

proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant G218E


proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant G274S


proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant K276E


proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant R359G


proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant D292V


proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant G188R


proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant T243N


proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant R209S


organism: Escherichia coli (strain K12)

substrate_name: S-adenosylmethionine

source_db: uniprot

substrate: S-adenosylmethionine

source: uniprot


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

substrate_name: S-adenosylmethioninamine (at 78 degrees Celsius and at pH 7.5)


substrate_name: carbamoyl phosphate (at 28 degrees Celsius and pH 8)

assay_conditions_summary: pH 8; cofactor ADP


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

substrate_name: carbamoyl phosphate (at 2 mM ADP)

assay_conditions_summary: cofactor ADP

substrate: carbamoyl phosphate (at 2 mM ADP)


substrate_name: synthetic dansyl-Ala-Arg

substrate: synthetic dansyl-Ala-Arg


organism: Lathyrus oleraceus

sequence_source: UniProtKB Q9LKR1 direct accession lookup

proof_lines: G-domain of Toc159 monomer, at pH 8.0 and 23°C


sequence_source: UniProtKB Q41009 direct accession lookup

proof_lines: G-domain of Toc34 monomer, at pH 8.0 and 4°C

proof_lines: G-domains of Toc34-Toc159 heterodimer, at pH 8.0 and 4°C

proof_lines: G-domain of Toc34 monomer, at pH 8.0 and 23°C


organism: Mycobacterium tuberculosis

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: signal-recognition-particle GTPase(Enzyme) mutant K236A N-terminal GST-tag


sequence_source: UniProtKB P9WGD9 direct accession lookup


proof_lines: SABIO-RK modifier species: signal-recognition-particle GTPase(Enzyme) mutant D367A N-terminal GST-tag

proof_lines: mutant enzyme D367A, in the presence of 10 mM Mg2+, at pH 8.0 and 37°C


proof_lines: wild type enzyme, in the presence of 20 mM Mg2+, at pH 8.0 and 37°C

proof_lines: wild type enzyme, in the presence of 20 mM Mn2+, at pH 8.0 and 37°C

proof_lines: wild type enzyme, in the presence of 10 mM Mg2+, at pH 8.0 and 37°C


organism: Semliki forest virus


proof_lines: SRP54(K108A)-FtsY, in the presence of 7S RNA, pH and temperature not specified in the publication


substrate_name: putrescine

proof_lines: kcat is 1.9 sec(-1) for aminopropyltransferase activity with putrescine as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:17585781). Inactive at 80 degrees Celsius (PubMed:17585781).

substrate: putrescine


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

substrate_name: agmatine

proof_lines: kcat is 2.09 sec(-1) for aminopropyl transferase activity with cadaverine as amine acceptor. kcat is 0.18 sec(-1) for aminopropyl transferase activity with putrescine as amine acceptor. kcat is 0.1 sec(-1) for aminopropyl transferase activi

substrate: agmatine


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

substrate_name: agmatine (at pH 9 and 70 degrees Celsius)

assay_conditions_summary: pH 9

proof_lines: kcat is 0.3 sec(-1) for aminopropyl transferase activity with putrescine as substrate (at pH 9 and 70 degrees Celsius). kcat is 0.28 sec(-1) for aminopropyl transferase activity with agmatine as substrate (at pH 9 and 70 degrees Celsius). k


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

substrate_name: S-adenosylmethioninamine (at pH 7.5 and 37 degrees Celsius)

proof_lines: kcat is 0.77 sec(-1) for aminopropyltransferase activity with putrescine as substrate (at pH 7.5 and 37 degrees Celsius). kcat is 22.7 sec(-1) for aminopropyltransferase activity with putrescine as substrate (at pH 7.5 and 80 degrees Celsiu


substrate_name: UTP

proof_lines: kcat is 0.059 sec(-1) with UTP as substrate. kcat is 0.002 sec(-1) with ATP as substrate. kcat is 0.061 sec(-1) with U6 snRNA-u4 as substrate.


organism: Leishmania tarentolae

substrate_name: Unknown

proof_lines: KM is 45-65 uM for UTP (at 27 degrees Celsius) (PubMed:15060068). KM is 18-30 uM for RNA (at 27 degrees Celsius) (PubMed:15060068).

substrate: Unknown


organism: Arabidopsis thaliana

substrate_name: alpha-ketosuccinamate

substrate: alpha-ketosuccinamate


substrate_name: GDP (in the presence of Ca(2+))

substrate: GDP (in the presence of Ca(2+))


substrate_name: GDP

substrate: GDP


organism: Rattus norvegicus


substrate_name: UDP

substrate: UDP


organism: Trypanosoma brucei

sequence_variant_note: Resolved canonical sequence from UniProtKB Q381M1 canonical sequence; S148A reconstructed by direct residue substitution. and applied mutation signature S148A to reconstruct the assayed variant sequence.

substrate: UTP


substrate_name: RNA

sequence_variant_note: Resolved canonical sequence from UniProtKB Q381M1 canonical sequence; R307A reconstructed by direct residue substitution. and applied mutation signature R307A to reconstruct the assayed variant sequence.

substrate: RNA


substrate_name: N-Methyldihydronicotinamide

sequence_source: UniProtKB:P16083 direct FASTA/JSON lookup

substrate: N-Methyldihydronicotinamide


substrate_name: N-Methyldihydronicotinamide; Menadione

ki_unit: mM

proof_lines: pH 8, 25°C, uncompetitive against menadione

proof_lines: substrate 2,6-dichloroindophenol, pH 7.4, 24°C

proof_lines: pH 8, 25°C, competitive inhibitor against N-methyldihydronicotinamide

substrate: N-Methyldihydronicotinamide; Menadione


substrate_name: menadione

substrate: menadione


proof_lines: SABIO-RK modifier species: ribosyldihydronicotinamide dehydrogenase (quinone)(Enzyme) mutant hNQO2-hDT43 chimeric His6-tagged


substrate_name: Methyl red

substrate: Methyl red


organism: Camelus dromedarius

proof_lines: kcat is 5.1 sec(-1) for undecapeptide analog to chymosin sensitive region of camel kappa-chain of casein and kcat is 11.7 sec(-1) for undecapeptide analog to chymosin sensitive region of bovine kappa-chain of casein (PubMed:16488399). Activ


substrate_name: 2-oxoglutaramate (open-chain form at pH 8.5 and 37 degrees Celsius)

proof_lines: In solution, 2-oxoglutaramate is in equilibrium with a cyclic form (2-hydroxy-5-oxoproline), and at pH 8.0 or above, the rate of ring opening is no longer limiting for the omega-amidase reaction (PubMed:19595734, PubMed:22674578). The kinet


organism: Mus musculus

substrate_name: 2-oxoglutaramate (at pH 8.5)

assay_conditions_summary: pH 8

proof_lines: In solution, 2-oxoglutaramate is in equilibrium with a cyclic form (2-hydroxy-5-oxoproline), and at pH 8.0 or above, the rate of ring opening is no longer limiting for the omega-amidase reaction (PubMed:19596042). kcat is 10.7 sec(-1) with

substrate: 2-oxoglutaramate (at pH 8.5)


substrate_name: 2-oxoglutaramate (open-chain form)

proof_lines: In solution, 2-oxoglutaramate is in equilibrium with a cyclic form (2-hydroxy-5-oxoproline), and at pH 8.0 or above, the rate of ring opening is no longer limiting for the omega-amidase reaction.

substrate: 2-oxoglutaramate (open-chain form)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 23.5 sec(-1) with 2-oxoglutaramate as substrate.


organism: Caenorhabditis elegans


enzyme_display_name: dipeptidyl-peptidase I

organism: Homo sapiens

enzyme: dipeptidyl-peptidase I


mutation_signature: recombinant truncated cathepsin C

mutation_type: truncation

proof_lines: recombinant truncated cathepsin C, pH 5.5, 25°C


substrate_name: Hydroxylamine; Glycyl-Tyrosyl-amide

sequence_source: UniProtKB:P80067 direct REST lookup; reviewed Swiss-Prot entry CATC_RAT

substrate: Hydroxylamine; Glycyl-Tyrosyl-amide


organism: Trichinella spiralis

sequence_source: UniProtKB:E5S2D3 direct REST lookup; active unreviewed TrEMBL entry E5S2D3_TRISP


substrate_name: NADH

sequence_source: UniProtKB P16083 direct accession lookup; reviewed Swiss-Prot canonical sequence

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH

substrate: NADH


organism: Streptococcus pyogenes

substrate_name: Carbamoyl phosphate

assay_conditions_summary: pH 6.5; 310.15 K; cofactor ADP

substrate: Carbamoyl phosphate


organism: Trichomonas vaginalis

sequence_source: UniProtKB O96432 direct accession lookup; reviewed Swiss-Prot canonical sequence

proof_lines: pH and temperature not specified in the publication


substrate_name: UTP; RNA

sequence_source: UniProtKB Q9H6E5 direct accession lookup; reviewed Swiss-Prot canonical sequence

substrate: UTP; RNA


substrate_name: U6 snRNAn

sequence_source: UniProtKB F5H0R1 direct accession lookup; unreviewed TrEMBL sequence

substrate: U6 snRNAn


substrate_name: RNA; UTP

proof_lines: SABIO-RK modifier species: RNA uridylyltransferase(Enzyme) mutant deltaPRR

proof_lines: SABIO-RK modifier species: RNA uridylyltransferase(Enzyme) mutant deltaKA-1

proof_lines: SABIO-RK modifier species: RNA uridylyltransferase(Enzyme) mutant deltaZ

substrate: RNA; UTP


substrate_name: UTP

sequence_variant_note: Resolved canonical sequence from UniProtKB Q381M1 direct accession lookup plus Y189F reconstruction from canonical residue 189 and applied mutation signature Y189F to reconstruct the assayed variant sequence.


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: ADP

proof_lines: kcat is 24.9 min(-1) with ADP as substrate. kcat is 21.4 min(-1) with GDP as substrate. kcat is 45.8 min(-1) with CDP as substrate. kcat is 83.3 min(-1) with UDP as substrate. kcat is 40.8 min(-1) with TDP as substrate.

proof_lines: kcat is 34 min(-1) with ATP as substrate. kcat is 138 min(-1) with ADP as substrate. kcat is 104 min(-1) with GTP as substrate. kcat is 42 min(-1) with GDP as substrate.

substrate: ADP


organism: Bos taurus

substrate_name: reduced N1-(n-propyl)-nicotinamide

proof_lines: pH 7.6, with reduced N1-(n-propyl)-nicotinamide as acceptor

substrate: reduced N1-(n-propyl)-nicotinamide


assay_conditions_summary: pH 8.5; 298.15 K; buffer pH 8.5; cofactor NADH

proof_lines: at 25°C in pH 8.5 buffer (50 mM Tris, 140 mM NaCl, and 0.1% Tween 20) with 0.1 mM menadione as co-substrate

proof_lines: chimeric enzyme of the human NQO2 with 43 amino acids from the carboxyl terminus of human DT-diaphorase


organism: Mesocricetus auratus


organism: Brassica rapa subsp. pekinensis

substrate_name: S-Adenosylmethioninamine; Putrescine

proof_lines:
pH 8.8, 37ºC, crude extracts
pH 7.4, 37ºC, partially purified enzyme

substrate: S-Adenosylmethioninamine; Putrescine


substrate_name: S-adenosylmethioninamine

substrate: S-adenosylmethioninamine


organism: Escherichia coli

proof_lines:
pH 8.2, 37ºC, spectrophotometric assay
pH 8.8, 37ºC, spectrophotometric assay
pH 7.5, 37ºC


organism: Glycine max


organism: Mammalia

substrate_name: Putrescine; S-Adenosylmethioninamine

substrate: Putrescine; S-Adenosylmethioninamine


organism: Rattus norvegicus

proof_lines: pH 7.5, 37ºC, in the presence of 2-mercaptoethylamine


organism: Senecio vulgaris


substrate_name: H2O; Gly-Phe-4-methoxynaphthylamide

sequence_source: UniProtKB reviewed Swiss-Prot accession P53634 FASTA, checked 2026-06-11: https://rest.uniprot.org/uniprotkb/P53634.fasta

substrate: H2O; Gly-Phe-4-methoxynaphthylamide


enzyme_display_name: beta-aspartyl-peptidase

organism: Arabidopsis thaliana

substrate_name: L-Asparagine

sequence_source: UniProtKB reviewed Swiss-Prot accession P50287 FASTA, checked 2026-06-11: https://rest.uniprot.org/uniprotkb/P50287.fasta

enzyme: beta-aspartyl-peptidase

substrate: L-Asparagine


substrate_name: L-Aspartyl-beta-hydroxamate

substrate: L-Aspartyl-beta-hydroxamate


substrate_name: beta-L-Aspartyl-L-histidine

substrate: beta-L-Aspartyl-L-histidine


substrate_name: beta-Asp-Leu

sequence_variant_note: Resolved canonical sequence from UniProtKB:P39377 canonical sequence reconstructed with selected source mutation E77D and applied mutation signature E77D to reconstruct the assayed variant sequence.

substrate: beta-Asp-Leu


sequence_variant_note: Resolved canonical sequence from UniProtKB:P39377 canonical sequence reconstructed with selected source mutation S289A and applied mutation signature S289A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P39377 canonical sequence reconstructed with selected source mutation Y137F and applied mutation signature Y137F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P39377 canonical sequence reconstructed with selected source mutation D285N and applied mutation signature D285N to reconstruct the assayed variant sequence.


substrate_name: beta-Asp-Phe

sequence_source: UniProtKB:P39377 canonical sequence

substrate: beta-Asp-Phe


sequence_variant_note: Resolved canonical sequence from UniProtKB:P39377 canonical sequence reconstructed with selected source mutation Y137A and applied mutation signature Y137A to reconstruct the assayed variant sequence.


substrate_name: L-Isoaspartyl-L-leucine; H2O

proof_lines: Co/Co reconstituted enzyme, pH 8.1, 30°C

proof_lines: Zn/Zn reconstituted enzyme, pH 8.1, 30°C

proof_lines: Ni/Ni reconstituted enzyme, pH 8.1, 30°C

substrate: L-Isoaspartyl-L-leucine; H2O


organism: Lupinus luteus

substrate_name: H2O; beta-L-Aspartyl-L-leucine

proof_lines: SABIO-RK modifier species: beta-aspartyl-peptidase(Enzyme) wildtype L1A

substrate: H2O; beta-L-Aspartyl-L-leucine


enzyme_display_name: phenol 2-monooxygenase (NADPH)

organism: Bacillus thermoglucosidasius

substrate_name: riboflavin

sequence_source: UniProtKB Q9LAG2 REST direct lookup on 2026-06-11

enzyme: phenol 2-monooxygenase (NADPH)

substrate: riboflavin


substrate_name: NADH

assay_conditions_summary: pH 7; 326.15 K; cofactor NADH

substrate: NADH


substrate_name: 3-Acetylpyridine-adenine dinucleotide

substrate: 3-Acetylpyridine-adenine dinucleotide


substrate_name: H+; FAD; NADH

assay_conditions_summary: cofactor NADH

substrate: H+; FAD; NADH


substrate_name: FAD

assay_conditions_summary: pH 7; 298.15 K; cofactor FAD

substrate: FAD


substrate_name: Unknown

sequence_source: UniProtKB Q3ZCJ8 REST direct lookup on 2026-06-11

substrate: Unknown


enzyme_display_name: aminodeoxychorismate synthase

organism: Agaricus bisporus

substrate_name: L-glutamine

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

enzyme: aminodeoxychorismate synthase

substrate: L-glutamine


substrate_name: chorismate

substrate: chorismate


substrate_name: L-Glutamine

sequence_source: UniProtKB REST Q8LPN3 reviewed entry checked 2026-06-11

substrate: L-Glutamine


substrate_name: Chorismate

substrate: Chorismate


substrate_name: L-Glutamine; Chorismate

substrate: L-Glutamine; Chorismate


smiles: N


organism: Bacillus subtilis


substrate_name: Acetate

smiles: CC(=O)O

substrate: Acetate


substrate_name: NH3; Chorismate

proof_lines: SABIO-RK modifier species: aminodeoxychorismate synthase(Enzyme) mutant E258D

substrate: NH3; Chorismate


substrate_name: Chorismate; L-Glutamine

substrate: Chorismate; L-Glutamine


organism: Pseudomonas aeruginosa

proof_lines:
cosubstrate L-glutamine, pH 7.0, 25°C
cosubstrate NH3, pH 7.0, 25°C
pH 7.0, 25°C


organism: Pseudomonas putida


sequence_variant_note: Resolved canonical sequence from UniProtKB P05041 canonical sequence with K274A substitution applied after direct residue check and applied mutation signature K274A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P05041 canonical sequence with K274A substitution applied after direct residue check

proof_lines: SABIO-RK modifier species: aminodeoxychorismate synthase(Enzyme) mutant K274A


sequence_variant_note: Resolved canonical sequence from UniProtKB P05041 canonical sequence with E258A substitution applied after direct residue check and applied mutation signature E258A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aminodeoxychorismate synthase(Enzyme) mutant E258A


sequence_variant_note: Resolved canonical sequence from UniProtKB P05041 canonical sequence with E258D substitution applied after direct residue check and applied mutation signature E258D to reconstruct the assayed variant sequence.


substrate_name: Chorismate; NH3

sequence_source: UniProtKB P05041 canonical sequence with E258A substitution applied after direct residue check

substrate: Chorismate; NH3


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05041 direct REST lookup; K274R reconstructed from the checked canonical P05041 sequence and applied mutation signature K274R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aminodeoxychorismate synthase(Enzyme) mutant K274R


sequence_source: UniProtKB:P05041 direct REST lookup


sequence_source: UniProtKB:P05041 direct REST lookup; K274R reconstructed from the checked canonical P05041 sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB:P05041 direct REST lookup; K274A reconstructed from the checked canonical P05041 sequence and applied mutation signature K274A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P05041 direct REST lookup; K274A reconstructed from the checked canonical P05041 sequence


enzyme_display_name: dephospho-CoA kinase

organism: Entamoeba histolytica

sequence_source: UniProtKB REST/FASTA accession C4MB67, fetched 2026-06-11

enzyme: dephospho-CoA kinase


substrate_name: ATP

substrate: ATP


assay_conditions_summary: pH 8; 310.15 K; cofactor CoA


sequence_source: UniProtKB REST/FASTA accession C4LWC7, fetched 2026-06-11

proof_lines:
pH 8.0, 37°C, isozyme Ehddpck2
pH 8.0, 37°C, isozyme Ehdpck2


substrate_name: ATP; Dephospho-CoA

sequence_source: UniProtKB REST/FASTA accession P0A6I9, fetched 2026-06-11

substrate: ATP; Dephospho-CoA


organism: Homo sapiens

sequence_source: UniProtKB REST/FASTA accession Q13057, fetched 2026-06-11


substrate_name: dephospho-CoA

substrate: dephospho-CoA


assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


substrate_name: Dephospho-CoA; ATP

sequence_source: UniProtKB reviewed accession Q6AY55 (DCAKD_RAT)

substrate: Dephospho-CoA; ATP


organism: Sus scrofa

sequence_source: UniProtKB reviewed accession Q8MIR4 (COASY_PIG)

proof_lines:
recombinant enzyme, pH 8.0, 25°C
native enzyme, pH 8.0, 25°C


organism: Thermococcus kodakarensis

assay_conditions_summary: pH 8; 353.15 K; cofactor ATP


substrate_name: GTP

substrate: GTP


sequence_source: UniProtKB reviewed accession Q03521 (MRAY_BACSU)


substrate_name: Undecaprenyl phosphate

substrate: Undecaprenyl phosphate


substrate_name: undecaprenyl phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q03521 canonical sequence reconstructed with D98N and applied mutation signature D98N to reconstruct the assayed variant sequence.

substrate: undecaprenyl phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB Q03521 canonical sequence reconstructed with D231N and applied mutation signature D231N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q03521 canonical sequence reconstructed with D177N and applied mutation signature D177N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q03521 canonical sequence reconstructed with E299Q and applied mutation signature E299Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q03521 canonical sequence reconstructed with D174N and applied mutation signature D174N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q03521 canonical sequence reconstructed with D99N and applied mutation signature D99N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q03521 canonical sequence reconstructed with H45R and applied mutation signature H45R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q03521 canonical sequence reconstructed with N168A and applied mutation signature N168A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03521 and applied mutation signature H290R 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 UniProtKB:Q03521 and applied mutation signature H289R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03521 and applied mutation signature H291R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03521 and applied mutation signature K116Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03521 and applied mutation signature N171A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03521 and applied mutation signature K48Q to reconstruct the assayed variant sequence.


organism: Staphylococcus aureus


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


organism: Mycobacterium tuberculosis

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WPA3 and applied mutation signature L114A to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed DCoA and a three-column span headed ATP; the kinetic column heads printed under each span are Km(uM) | Kcat (min^-1) | Kcat/Km (uM^-1 min^-1). The cited cell set is Table 2, DCoA span, enzyme row L114A: Km(uM) = 80.9; Kcat (min^-1) = 3.414; Kcat/Km (uM^-1 min^-1) = 0.0422.

normalized_value_unit_evidence: Km: printed Table 2 DCoA-span cell 80.9 uM; 80.9 / 1000 = 0.08090000000000001 mM. kcat: printed Table 2 DCoA-span cell 3.414 min^-1; 3.414 / 60 = 0.0569 s^(-1). kcat/Km: printed Table 2 DCoA-span cell 0.0422 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000 / 60 s^-1 mM^-1, so 0.0422 x 1000 / 60 = 0.7033333333333334 s^(-1)*mM^(-1). The exported values of this row are kcat 0.0569, km 0.0639; the metrics this record corrects are km.

raw_value_unit_evidence: Table 2, DCoA span, enzyme row L114A: Km = 80.9 uM; Kcat = 3.414 min^-1; printed Kcat/Km = 0.0422 uM^-1 min^-1.

row_label: Table 2, DCoA block, enzyme row L114A

table_label: Table 2: Kinetic parameters of the wild type and mutant mycobacterial dephosphocoenzyme A kinases (nr- no reaction; nd-not determined) (PLoS One 2011)

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProt P9WPA3 FASTA plus direct D32N substitution reconstruction and applied mutation signature D32N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D32N, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C


column_label: Table 2 carries one enzyme-label column, then a three-column span headed DCoA and a three-column span headed ATP; the kinetic column heads printed under each span are Km(uM) | Kcat (min^-1) | Kcat/Km (uM^-1 min^-1). The cited cell set is Table 2, ATP span, enzyme row L114A: Km(uM) = 63.9; Kcat (min^-1) = 1.152; Kcat/Km (uM^-1 min^-1) = 0.0180.

normalized_value_unit_evidence: Km: printed Table 2 ATP-span cell 63.9 uM; 63.9 / 1000 = 0.0639 mM. kcat: printed Table 2 ATP-span cell 1.152 min^-1; 1.152 / 60 = 0.0192 s^(-1). kcat/Km: printed Table 2 ATP-span cell 0.0180 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000 / 60 s^-1 mM^-1, so 0.0180 x 1000 / 60 = 0.3 s^(-1)*mM^(-1). The exported values of this row are kcat 0.0192, kcat_over_km 0.3004694835680751, km 0.0639; the metrics this record corrects are kcat_over_km.

raw_value_unit_evidence: Table 2, ATP span, enzyme row L114A: Km = 63.9 uM; Kcat = 1.152 min^-1; printed Kcat/Km = 0.0180 uM^-1 min^-1.

row_label: Table 2, ATP block, enzyme row L114A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WPA3 and applied mutation signature K14A to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed DCoA and a three-column span headed ATP; the kinetic column heads printed under each span are Km(uM) | Kcat (min^-1) | Kcat/Km (uM^-1 min^-1). The cited cell set is Table 2, DCoA span, enzyme row K14A: Km(uM) = 75.8; Kcat (min^-1) = 1.532; Kcat/Km (uM^-1 min^-1) = 0.0202.

raw_value_unit_evidence: Table 2, DCoA span, enzyme row K14A: Km = 75.8 uM; Kcat = 1.532 min^-1; printed Kcat/Km = 0.0202 uM^-1 min^-1.

row_label: Table 2, DCoA block, enzyme row K14A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WPA3 and applied mutation signature D32E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

column_label: Table 2 carries one enzyme-label column, then a three-column span headed DCoA and a three-column span headed ATP; the kinetic column heads printed under each span are Km(uM) | Kcat (min^-1) | Kcat/Km (uM^-1 min^-1). The cited cell set is Table 2, DCoA span, enzyme row D32E: Km(uM) = 21.7; Kcat (min^-1) = 1.962; Kcat/Km (uM^-1 min^-1) = 0.0904.

normalized_value_unit_evidence: Km: printed Table 2 DCoA-span cell 21.7 uM; 21.7 / 1000 = 0.0217 mM. kcat: printed Table 2 DCoA-span cell 1.962 min^-1; 1.962 / 60 = 0.0327 s^(-1). kcat/Km: printed Table 2 DCoA-span cell 0.0904 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000 / 60 s^-1 mM^-1, so 0.0904 x 1000 / 60 = 1.5066666666666666 s^(-1)*mM^(-1). The exported values of this row are kcat 0.0327, kcat_over_km 1.5069124423963134, km 0.0217; the metrics this record corrects are kcat_over_km.

raw_value_unit_evidence: Table 2, DCoA span, enzyme row D32E: Km = 21.7 uM; Kcat = 1.962 min^-1; printed Kcat/Km = 0.0904 uM^-1 min^-1.

row_label: Table 2, DCoA block, enzyme row D32E


column_label: Table 2 carries one enzyme-label column, then a three-column span headed DCoA and a three-column span headed ATP; the kinetic column heads printed under each span are Km(uM) | Kcat (min^-1) | Kcat/Km (uM^-1 min^-1). The cited cell set is Table 2, ATP span, enzyme row K14A: Km(uM) = 86.7; Kcat (min^-1) = 2.34; Kcat/Km (uM^-1 min^-1) = 0.0269.

normalized_value_unit_evidence: Km: printed Table 2 ATP-span cell 86.7 uM; 86.7 / 1000 = 0.0867 mM. kcat: printed Table 2 ATP-span cell 2.34 min^-1; 2.34 / 60 = 0.039 s^(-1). kcat/Km: printed Table 2 ATP-span cell 0.0269 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000 / 60 s^-1 mM^-1, so 0.0269 x 1000 / 60 = 0.44833333333333336 s^(-1)*mM^(-1). The exported values of this row are kcat 0.039, km 0.0758; the metrics this record corrects are km.

raw_value_unit_evidence: Table 2, ATP span, enzyme row K14A: Km = 86.7 uM; Kcat = 2.34 min^-1; printed Kcat/Km = 0.0269 uM^-1 min^-1.

row_label: Table 2, ATP block, enzyme row K14A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WPA3 and applied mutation signature D32N to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed DCoA and a three-column span headed ATP; the kinetic column heads printed under each span are Km(uM) | Kcat (min^-1) | Kcat/Km (uM^-1 min^-1). The cited cell set is Table 2, DCoA span, enzyme row D32N: Km(uM) = 87.7; Kcat (min^-1) = 2.004; Kcat/Km (uM^-1 min^-1) = 0.0228.

normalized_value_unit_evidence: Km: printed Table 2 DCoA-span cell 87.7 uM; 87.7 / 1000 = 0.0877 mM. kcat: printed Table 2 DCoA-span cell 2.004 min^-1; 2.004 / 60 = 0.0334 s^(-1). kcat/Km: printed Table 2 DCoA-span cell 0.0228 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000 / 60 s^-1 mM^-1, so 0.0228 x 1000 / 60 = 0.38000000000000006 s^(-1)*mM^(-1). The exported values of this row are kcat 0.0334, kcat_over_km 0.3808437856328392, km 0.0877; the metrics this record corrects are kcat_over_km.

raw_value_unit_evidence: Table 2, DCoA span, enzyme row D32N: Km = 87.7 uM; Kcat = 2.004 min^-1; printed Kcat/Km = 0.0228 uM^-1 min^-1.

row_label: Table 2, DCoA block, enzyme row D32N


substrate_name: L-Asparagine

sequence_source: UniProtKB reviewed accession Q9ZSD6 direct lookup on 2026-06-11

substrate: L-Asparagine


substrate_name: beta-L-Aspartyl-L-leucine

substrate: beta-L-Aspartyl-L-leucine


substrate_name: beta-L-aspartyl-L-leucine

substrate: beta-L-aspartyl-L-leucine


organism: Nostoc sp.

substrate_name: H2O; beta-L-Aspartyl-L-alanine

sequence_source: UniProtKB reviewed accession Q8YQB1 direct lookup on 2026-06-11

substrate: H2O; beta-L-Aspartyl-L-alanine


organism: Synechocystis sp.

sequence_source: UniProtKB reviewed accession P74383 direct lookup on 2026-06-11


enzyme_display_name: 4-hydroxy-2-oxoheptanedioate aldolase

organism: Escherichia coli

sequence_source: UniProtKB reviewed accession Q47098 direct lookup on 2026-06-11

proof_lines:
i.e. KDO, pH 8.0, 25°C
pH 8.0, 25°C
Km (app) with Co2+, pH 8.0, 25°C

enzyme: 4-hydroxy-2-oxoheptanedioate aldolase


substrate_name: 3-deoxy-D-manno-oct-2-ulosonic acid

substrate: 3-deoxy-D-manno-oct-2-ulosonic acid


organism: Colwellia psychrerythraea

substrate_name: alpha-Asp-Leu

sequence_source: UniProtKB Q484B6 direct REST check on 2026-06-11; Q484B6_COLP3, Colwellia psychrerythraea strain 34H, isoaspartyl dipeptidase iadA, sequence length 395.

proof_lines:
pH 8.0, 30°C
Raw SKiD Env: Temp=30°C, pH=8

substrate: alpha-Asp-Leu


substrate_name: beta-L-Aspartyl-L-leucine; H2O

sequence_source: UniProtKB P37595 direct REST check on 2026-06-11; reviewed IAAA_ECOLI, Escherichia coli K12, isoaspartyl peptidase, EC 3.4.19.5, sequence length 321.

substrate: beta-L-Aspartyl-L-leucine; H2O


substrate_name: beta-Asp-Leu

sequence_variant_note: Resolved canonical sequence from UniProtKB P39377 direct REST check on 2026-06-11; reviewed IADA_ECOLI, Escherichia coli K12, isoaspartyl dipeptidase iadA, sequence length 390. and applied mutation signature R169K to reconstruct the assayed variant sequence.

substrate: beta-Asp-Leu


sequence_variant_note: Resolved canonical sequence from UniProtKB P39377 direct REST check on 2026-06-11; reviewed IADA_ECOLI, Escherichia coli K12, isoaspartyl dipeptidase iadA, sequence length 390. and applied mutation signature D285A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P39377 direct REST check on 2026-06-11; reviewed IADA_ECOLI, Escherichia coli K12, isoaspartyl dipeptidase iadA, sequence length 390. and applied mutation signature R233K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P39377 direct REST check on 2026-06-11; reviewed IADA_ECOLI, Escherichia coli K12, isoaspartyl dipeptidase iadA, sequence length 390. and applied mutation signature E77Q to reconstruct the assayed variant sequence.


organism: Arabidopsis thaliana

substrate_name: H2O; L-Asparagine

sequence_source: UniProtKB accession P50287 direct REST lookup on 2026-06-11

substrate: H2O; L-Asparagine


substrate_name: beta-Asp-Lys

verification_status: verified

sequence_source: UniProtKB accession Q484B6 direct REST lookup on 2026-06-11

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

column_label: Table 2 'Steady-state kinetic parameters of CpsIadA', substrate row `beta-Asp-Lys`: kcat (s^-1) = 256; Km (mM) = 1.1; kcat/Km (M^-1 s^-1) = 2.3 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 256 s^-1; already per second, no conversion; the exported value is 256.0 s^(-1). Km: printed Table 2 cell 1.1 mM; already millimolar, no conversion; the exported value is 1.1 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.3 x 10^5 M^-1 s^-1 for this substrate row; 2.3 x 10^5 M^-1 s^-1 divided by 1000 is 230.0 s^(-1)*mM^(-1); the exported value is 230.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded plain-numeral transcription, substrate row `beta-Asp-Lys`

substrate: beta-Asp-Lys

status: verified


substrate_name: beta-Asp-Phe

column_label: Table 2 'Steady-state kinetic parameters of CpsIadA', substrate row `beta-Asp-Phe`: kcat (s^-1) = 145; Km (mM) = 0.49; kcat/Km (M^-1 s^-1) = 3.0 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 145 s^-1; already per second, no conversion; the exported value is 145.0 s^(-1). Km: printed Table 2 cell 0.49 mM; already millimolar, no conversion; the exported value is 0.49 mM. kcat/Km: the paper PRINTS the kcat/Km cell 3.0 x 10^5 M^-1 s^-1 for this substrate row; 3.0 x 10^5 M^-1 s^-1 divided by 1000 is 300.0 s^(-1)*mM^(-1); the exported value is 300.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded plain-numeral transcription, substrate row `beta-Asp-Phe`

substrate: beta-Asp-Phe


substrate_name: beta-Asp-His

column_label: Table 2 'Steady-state kinetic parameters of CpsIadA', substrate row `beta-Asp-His`: kcat (s^-1) = 74; Km (mM) = 5.3; kcat/Km (M^-1 s^-1) = 1.4 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 74 s^-1; already per second, no conversion; the exported value is 74.0 s^(-1). Km: printed Table 2 cell 5.3 mM; already millimolar, no conversion; the exported value is 5.3 mM. kcat/Km: the paper PRINTS the kcat/Km cell 1.4 x 10^4 M^-1 s^-1 for this substrate row; 1.4 x 10^4 M^-1 s^-1 divided by 1000 is 14.0 s^(-1)*mM^(-1); the exported value is 14.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded plain-numeral transcription, substrate row `beta-Asp-His`

substrate: beta-Asp-His


substrate_name: beta-Asp-Gly

column_label: Table 2 'Steady-state kinetic parameters of CpsIadA', substrate row `beta-Asp-Gly`: kcat (s^-1) = 181; Km (mM) = 4.7; kcat/Km (M^-1 s^-1) = 3.8 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 181 s^-1; already per second, no conversion; the exported value is 181.0 s^(-1). Km: printed Table 2 cell 4.7 mM; already millimolar, no conversion; the exported value is 4.7 mM. kcat/Km: the paper PRINTS the kcat/Km cell 3.8 x 10^4 M^-1 s^-1 for this substrate row; 3.8 x 10^4 M^-1 s^-1 divided by 1000 is 38.0 s^(-1)*mM^(-1); the exported value is 38.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded plain-numeral transcription, substrate row `beta-Asp-Gly`

substrate: beta-Asp-Gly


column_label: Table 2 'Steady-state kinetic parameters of CpsIadA', substrate row `beta-Asp-Leu`: kcat (s^-1) = 164; Km (mM) = 0.71; kcat/Km (M^-1 s^-1) = 2.3 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 164 s^-1; already per second, no conversion; the exported value is 164.0 s^(-1). Km: printed Table 2 cell 0.71 mM; already millimolar, no conversion; the exported value is 0.71 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.3 x 10^5 M^-1 s^-1 for this substrate row; 2.3 x 10^5 M^-1 s^-1 divided by 1000 is 230.0 s^(-1)*mM^(-1); the exported value is 230.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded plain-numeral transcription, substrate row `beta-Asp-Leu`


column_label: Table 2 'Steady-state kinetic parameters of CpsIadA', substrate row `alpha-Asp-Leu`: kcat (s^-1) = 89; Km (mM) = 6.9; kcat/Km (M^-1 s^-1) = 1.3 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 2 cell 89 s^-1; already per second, no conversion; the exported value is 89.0 s^(-1). Km: printed Table 2 cell 6.9 mM; already millimolar, no conversion; the exported value is 6.9 mM. kcat/Km: the paper PRINTS the kcat/Km cell 1.3 x 10^4 M^-1 s^-1 for this substrate row; 1.3 x 10^4 M^-1 s^-1 divided by 1000 is 13.0 s^(-1)*mM^(-1); the exported value is 13.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded plain-numeral transcription, substrate row `alpha-Asp-Leu`


substrate_name: beta-Asp-Ala

column_label: Table 2 'Steady-state kinetic parameters of CpsIadA', substrate row `beta-Asp-Ala`: kcat (s^-1) = 166; Km (mM) = 1.2; kcat/Km (M^-1 s^-1) = 1.4 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 166 s^-1; already per second, no conversion; the exported value is 166.0 s^(-1). Km: printed Table 2 cell 1.2 mM; already millimolar, no conversion; the exported value is 1.2 mM. kcat/Km: the paper PRINTS the kcat/Km cell 1.4 x 10^5 M^-1 s^-1 for this substrate row; 1.4 x 10^5 M^-1 s^-1 divided by 1000 is 140.0 s^(-1)*mM^(-1); the exported value is 140.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded plain-numeral transcription, substrate row `beta-Asp-Ala`

substrate: beta-Asp-Ala


sequence_source: UniProtKB reviewed accession Q47098 direct REST/FASTA lookup on 2026-06-11

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


substrate_name: oxaloacetate

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

substrate: oxaloacetate


substrate_name: Pyruvate; Acetaldehyde

sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB reviewed accession Q47098 direct REST/FASTA lookup on 2026-06-11 and applied mutation signature R70A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-2-oxoheptanedioate aldolase(Enzyme) mutant R70A

substrate: Pyruvate; Acetaldehyde


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

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


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB reviewed accession Q47098 direct REST/FASTA lookup on 2026-06-11 and applied mutation signature H45A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-2-oxoheptanedioate aldolase(Enzyme) mutant H45A


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB reviewed accession Q47098 direct REST/FASTA lookup on 2026-06-11 and applied mutation signature H45Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-2-oxoheptanedioate aldolase(Enzyme) mutant H45Q


substrate_name: 4-hydroxy-2-oxopentanoic acid

sequence_source: Variant reconstructed from UniProtKB reviewed accession Q47098 direct REST/FASTA lookup on 2026-06-11

substrate: 4-hydroxy-2-oxopentanoic acid


enzyme_display_name: NAD(P)H oxidase (H2O2-forming)

substrate_name: O2; NADPH

assay_conditions_summary: cofactor NADPH

enzyme: NAD(P)H oxidase (H2O2-forming)

substrate: O2; NADPH


substrate_name: NADPH; O2

substrate: NADPH; O2


organism: Pseudomonas fluorescens

substrate_name: NADPH

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

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

substrate: NADPH


substrate_name: H+; NADPH; O2

proof_lines: SABIO-RK modifier species: NAD(P)H oxidase(Enzyme) mutant G490A

substrate: H+; NADPH; O2


substrate_name: NADPH; O2; H+

substrate: NADPH; O2; H+


organism: Pyrococcus horikoshii

substrate_name: NADH; O2; H+

substrate: NADH; O2; H+


assay_conditions_summary: pH 7.5; 348.15 K; cofactor NADPH


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P9WPA3 / COAE_MYCTU FASTA+JSON direct check on 2026-06-11; EC 2.7.1.24 dephospho-CoA kinase from Mycobacterium tuberculosis H37Rv. and applied mutation signature D32A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D32A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C

substrate: ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P9WPA3 / COAE_MYCTU FASTA+JSON direct check on 2026-06-11; EC 2.7.1.24 dephospho-CoA kinase from Mycobacterium tuberculosis H37Rv. and applied mutation signature K14A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P9WPA3 / COAE_MYCTU FASTA+JSON direct check on 2026-06-11; EC 2.7.1.24 dephospho-CoA kinase from Mycobacterium tuberculosis H37Rv. and applied mutation signature R140K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R140K, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C


sequence_source: UniProtKB reviewed P9WPA3 / COAE_MYCTU FASTA+JSON direct check on 2026-06-11; EC 2.7.1.24 dephospho-CoA kinase from Mycobacterium tuberculosis H37Rv.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P9WPA3 / COAE_MYCTU FASTA+JSON direct check on 2026-06-11; EC 2.7.1.24 dephospho-CoA kinase from Mycobacterium tuberculosis H37Rv. and applied mutation signature G8A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P9WPA3 / COAE_MYCTU FASTA+JSON direct check on 2026-06-11; EC 2.7.1.24 dephospho-CoA kinase from Mycobacterium tuberculosis H37Rv. and applied mutation signature L114A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P9WPA3 / COAE_MYCTU FASTA+JSON direct check on 2026-06-11; EC 2.7.1.24 dephospho-CoA kinase from Mycobacterium tuberculosis H37Rv. and applied mutation signature D32N to reconstruct the assayed variant sequence.


substrate_name: L-Homocysteine; Betaine

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

sequence_source: UniProtKB:Q93088 FASTA direct lookup (reviewed Swiss-Prot)

substrate: L-Homocysteine; Betaine


organism: Rattus norvegicus

substrate_name: L-homocysteine

sequence_variant_note: Resolved canonical sequence from UniProtKB:O09171 FASTA direct lookup (reviewed Swiss-Prot) and applied mutation signature A119G to reconstruct the assayed variant sequence.

substrate: L-homocysteine


sequence_source: UniProtKB:O09171 FASTA direct lookup (reviewed Swiss-Prot)


sequence_variant_note: Resolved canonical sequence from UniProtKB:O09171 FASTA direct lookup (reviewed Swiss-Prot) and applied mutation signature E159G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O09171 FASTA direct lookup (reviewed Swiss-Prot) and applied mutation signature T184G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O09171 FASTA direct lookup (reviewed Swiss-Prot) and applied mutation signature D26A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O09171 FASTA direct lookup (reviewed Swiss-Prot) and applied mutation signature E21A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O09171 FASTA direct lookup (reviewed Swiss-Prot) and applied mutation signature T73G to reconstruct the assayed variant sequence.

proof_lines:
37°C, mutant enzyme T73G
37°C, mutant enzym T73G


substrate_name: FAD

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; 348.15 K; cofactor NADH

substrate: FAD


substrate_name: NADH

substrate: NADH


organism: Sulfolobus solfataricus

substrate_name: NADH; H+; O2

substrate: NADH; H+; O2


assay_conditions_summary: pH 5.5; 338.15 K; cofactor NADH


assay_conditions_summary: pH 5.5; 338.15 K; cofactor FAD


substrate_name: betaine

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

substrate: betaine


proof_lines: wild-type, presence of 150 mM KCl, pH 7.5, 37 C

proof_lines: wild-type, cosubstrate S-methylmethionine, presence of 150 mM KCl, pH 7.5, 37 C


sequence_variant_note: Resolved canonical sequence from UniProt O09171 canonical sequence reconstructed with row-specific PMID 12487625 mutagenesis feature and applied mutation signature C186S to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from UniProt O09171 canonical sequence reconstructed with row-specific PMID 12487625 mutagenesis feature and applied mutation signature Y77A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O09171 canonical sequence reconstructed with row-specific PMID 12487625 mutagenesis feature and applied mutation signature C186A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O09171 canonical sequence reconstructed with row-specific PMID 12487625 mutagenesis feature and applied mutation signature E159K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O09171 canonical sequence reconstructed with row-specific PMID 12487625 mutagenesis feature and applied mutation signature E21K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O09171 canonical sequence reconstructed with row-specific PMID 12487625 mutagenesis feature and applied mutation signature F74A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O09171 canonical sequence reconstructed with row-specific PMID 12487625 mutagenesis feature and applied mutation signature D26I to reconstruct the assayed variant sequence.


enzyme_display_name: brevianamide F prenyltransferase (deoxybrevianamide E-forming)

organism: Aspergillus sp.

substrate_name: brevianamide F

sequence_source: UniProtKB E0Y3X1 direct lookup

substrate: brevianamide F


substrate_name: dimethylallyl diphosphate

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

enzyme: brevianamide F prenyltransferase (deoxybrevianamide E-forming)

substrate: dimethylallyl diphosphate


proof_lines:
pH 7.5, 22°C
Raw SKiD Env: Temp=22°C, pH=7.5


organism: Aspergillus terreus

substrate_name: cyclo-L-Tyr-L-Tyr

substrate: cyclo-L-Tyr-L-Tyr


organism: Aspergillus versicolor

sequence_source: UniProtKB I4AY86 direct lookup


substrate_name: cyclo-L-Trp-L-Ala

substrate: cyclo-L-Trp-L-Ala


organism: Unknown

substrate_name: dephospho-CoA

assay_conditions_summary: cofactor CoA

substrate: dephospho-CoA


enzyme_display_name: chitin deacetylase

organism: Bombyx mori

substrate_name: (GlcNAc)3 / (GlcNAc)5 / colloidal chitin / (GlcNAc)6 / ethylene glycol chitin / (GlcNAc)4

sequence_source: UniProtKB:H9JW43 REST/FASTA direct lookup on 2026-06-11

enzyme: chitin deacetylase


organism: Colletotrichum lindemuthianum

substrate_name: H2O; beta-1,4-Di-(N-acetyl-D-glucosamine) and related chitooligosaccharide source rows

sequence_source: UniProtKB:Q6DWK3 REST/FASTA direct lookup on 2026-06-11

proof_lines: pH 8.5, 30°C, continuous spectrophotometric assay

proof_lines: pH 7.0, 37°C, fluorogenic labeling method assay


organism: Sinorhizobium meliloti

sequence_source: UniProtKB:P02963 REST/FASTA direct lookup on 2026-06-11


proof_lines: pH 7.2, 30°C, recombinant His-tagged enzyme


substrate_name: 4-hydroxy-2-oxopentanoic acid

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q47098 REST/FASTA direct lookup on 2026-06-11 and applied mutation signature H45Q to reconstruct the assayed variant sequence.

substrate: 4-hydroxy-2-oxopentanoic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB:B1IS70 REST/FASTA direct lookup on 2026-06-11 and applied mutation signature R70K to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:B1IS70 REST/FASTA direct lookup on 2026-06-11


enzyme_display_name: beta-D-fucosidase

organism: Thermococcus kodakarensis

substrate_name: 4-nitrophenyl beta-D-mannopyranoside

proof_lines: 80°C, pH is not specified in the publication, wild-type

enzyme: beta-D-fucosidase

substrate: 4-nitrophenyl beta-D-mannopyranoside


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

proof_lines: 80°C, pH is not specified in the publication, mutant enzyme D206N


organism: uncultured microorganism

substrate_name: 4-nitrophenyl beta-D-glucopyranoside

substrate: 4-nitrophenyl beta-D-glucopyranoside


substrate_name: 4-nitrophenyl beta-D-fucopyranoside

substrate: 4-nitrophenyl beta-D-fucopyranoside


proof_lines: pH 6.0, 60°C, additive: 25 mM cellobiose

proof_lines: pH 6.0, 60°C, additive: 250 mM D-galactose


substrate_name: 4-nitrophenyl beta-D-galactopyranoside

substrate: 4-nitrophenyl beta-D-galactopyranoside


organism: Aspergillus nidulans

substrate_name: penta-N-acetyl-chitopentaose

substrate: penta-N-acetyl-chitopentaose


enzyme_display_name: arogenate dehydratase

substrate_name: L-Arogenate

sequence_source: UniProtKB Q9SA96

enzyme: arogenate dehydratase

substrate: L-Arogenate


sequence_source: UniProtKB Q9FNJ8


sequence_source: UniProtKB Q9SGD6


sequence_source: UniProtKB Q9SSE7


sequence_source: UniProtKB Q9ZUY3


organism: Escherichia coli

sequence_source: UniProtKB reviewed entry B1IS70 / HPCH_ECOLC direct REST+FASTA lookup

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


proof_lines: wild type enzyme, with 0.5 mM Co2+, at pH 8.0 and 25°C


proof_lines: using H2O as solvent, in the presence of 0.5 mM Co2+, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry B1IS70 / HPCH_ECOLC direct REST+FASTA lookup plus direct R70K substitution and applied mutation signature R70K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R70K, with 0.5 mM Co2+, at pH 8.0 and 25°C


substrate_name: cyclo-L-Trp-Gly

sequence_source: UniProtKB reviewed accession I4AY86 (NOTF_ASPVE), direct REST/FASTA lookup on 2026-06-11

substrate: cyclo-L-Trp-Gly


substrate_name: cyclo-L-Trp-L-Tyr

substrate: cyclo-L-Trp-L-Tyr


substrate_name: cyclo-L-Trp-D-Pro

substrate: cyclo-L-Trp-D-Pro


substrate_name: cyclo-D-Trp-L-Ala

substrate: cyclo-D-Trp-L-Ala


substrate_name: cyclo-L-Trp-D-Ala

substrate: cyclo-L-Trp-D-Ala


substrate_name: cyclo-L-Trp-L-Leu

substrate: cyclo-L-Trp-L-Leu


substrate_name: brevianamide F

substrate: brevianamide F


substrate_name: cyclo-D-Trp-D-Ala

substrate: cyclo-D-Trp-D-Ala


organism: Oryza sativa

substrate_name: arogenate

proof_lines: mutant S298I, rice ADT is a bifunctional enzyme

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

substrate: arogenate


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


organism: Petunia x hybrida

substrate_name: prephenate

assay_conditions_summary: pH 8.2; 310.15 K; buffer 250 mM Na-phosphate

proof_lines: at 37°C, in 250 mM Na-phosphate buffer, pH 8.2, 1 mM EDTA

substrate: prephenate


substrate_name: L-arogenate

substrate: L-arogenate


sequence_source: reconstructed from UniProtKB:D3U715

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB:D3U715 and applied mutation signature R353A to reconstruct the assayed variant sequence.


organism: Mycobacterium tuberculosis

substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WPA3 canonical sequence with G8A reconstructed during review and applied mutation signature G8A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme G8A, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C

substrate: ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WPA3 canonical sequence with D32E reconstructed during review and applied mutation signature D32E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D32E, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WPA3 and applied mutation signature R140K to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed DCoA and a three-column span headed ATP; the kinetic column heads printed under each span are Km(uM) | Kcat (min^-1) | Kcat/Km (uM^-1 min^-1). The cited cell set is Table 2, DCoA span, enzyme row R140K: Km(uM) = 181; Kcat (min^-1) = 0.453; Kcat/Km (uM^-1 min^-1) = 0.00250.

normalized_value_unit_evidence: Km: printed Table 2 DCoA-span cell 181 uM; 181 / 1000 = 0.181 mM. kcat: printed Table 2 DCoA-span cell 0.453 min^-1; 0.453 / 60 = 0.00755 s^(-1). kcat/Km: printed Table 2 DCoA-span cell 0.00250 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000 / 60 s^-1 mM^-1, so 0.00250 x 1000 / 60 = 0.04166666666666667 s^(-1)*mM^(-1). The exported values of this row are kcat 0.0076, kcat_over_km 0.041988950276243095, km 0.181; the metrics this record corrects are kcat, kcat_over_km.

raw_value_unit_evidence: Table 2, DCoA span, enzyme row R140K: Km = 181 uM; Kcat = 0.453 min^-1; printed Kcat/Km = 0.00250 uM^-1 min^-1.

row_label: Table 2, DCoA block, enzyme row R140K


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WPA3 and applied mutation signature D32A to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed DCoA and a three-column span headed ATP; the kinetic column heads printed under each span are Km(uM) | Kcat (min^-1) | Kcat/Km (uM^-1 min^-1). The cited cell set is Table 2, ATP span, enzyme row D32A: Km(uM) = 57.5; Kcat (min^-1) = 0.84; Kcat/Km (uM^-1 min^-1) = 0.0146.

normalized_value_unit_evidence: Km: printed Table 2 ATP-span cell 57.5 uM; 57.5 / 1000 = 0.0575 mM. kcat: printed Table 2 ATP-span cell 0.84 min^-1; 0.84 / 60 = 0.013999999999999999 s^(-1). kcat/Km: printed Table 2 ATP-span cell 0.0146 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000 / 60 s^-1 mM^-1, so 0.0146 x 1000 / 60 = 0.24333333333333335 s^(-1)*mM^(-1). The exported values of this row are kcat 0.014, kcat_over_km 0.2434782608695652, km 0.0575; the metrics this record corrects are kcat_over_km.

raw_value_unit_evidence: Table 2, ATP span, enzyme row D32A: Km = 57.5 uM; Kcat = 0.84 min^-1; printed Kcat/Km = 0.0146 uM^-1 min^-1.

row_label: Table 2, ATP block, enzyme row D32A


organism: Bifidobacterium breve

substrate_name: p-Nitrophenyl-beta-D-fucoside

sequence_source: UniProtKB:P94248 canonical sequence

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

substrate: p-Nitrophenyl-beta-D-fucoside


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

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


organism: Haloferax volcanii

substrate_name: 2-nitrophenyl beta-D-galactoside

sequence_source: UniProtKB:P94804 checked but not accepted because of EC and organism contradiction

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

proof_lines: pH 7.2, 22°C, the enzyme also shows beta-fucosidase activity

substrate: 2-nitrophenyl beta-D-galactoside


organism: Putranjiva roxburghii

substrate_name: cellobiose

sequence_source: UniProtKB:A0A023MIF8 canonical sequence

proof_lines:
pH 4.6, 37°C, recombinant enzyme
pH 4.6, 37°C, native enzyme

substrate: cellobiose


substrate_name: cyclo-L-Trp-L-Phe

sequence_source: UniProtKB REST direct accession lookup: I4AY86 / NOTF_ASPVE, reviewed entry, retrieved 2026-06-11.

substrate: cyclo-L-Trp-L-Phe


substrate_name: cyclo-D-Trp-D-Pro

substrate: cyclo-D-Trp-D-Pro


substrate_name: cyclo-D-Trp-L-Pro

substrate: cyclo-D-Trp-L-Pro


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WPA3 and applied mutation signature G8A to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed DCoA and a three-column span headed ATP; the kinetic column heads printed under each span are Km(uM) | Kcat (min^-1) | Kcat/Km (uM^-1 min^-1). The cited cell set is Table 2, ATP span, enzyme row G8A: Km(uM) = 59.8; Kcat (min^-1) = 2.563; Kcat/Km (uM^-1 min^-1) = 0.0428.

normalized_value_unit_evidence: Km: printed Table 2 ATP-span cell 59.8 uM; 59.8 / 1000 = 0.0598 mM. kcat: printed Table 2 ATP-span cell 2.563 min^-1; 2.563 / 60 = 0.04271666666666667 s^(-1). kcat/Km: printed Table 2 ATP-span cell 0.0428 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000 / 60 s^-1 mM^-1, so 0.0428 x 1000 / 60 = 0.7133333333333334 s^(-1)*mM^(-1). The exported values of this row are kcat 0.043, kcat_over_km 0.7190635451505016, km 0.0598; the metrics this record corrects are kcat, kcat_over_km.

raw_value_unit_evidence: Table 2, ATP span, enzyme row G8A: Km = 59.8 uM; Kcat = 2.563 min^-1; printed Kcat/Km = 0.0428 uM^-1 min^-1.

row_label: Table 2, ATP block, enzyme row G8A


sequence_source: UniProtKB REST direct accession lookup: P9WPA3 / COAE_MYCTU, reviewed entry, retrieved 2026-06-11.

proof_lines: wild type enzyme, in 50 mM Tris with MgCl2 (10 mM) and KCl (20 mM), pH 8.0, at 25°C


column_label: Table 2 carries one enzyme-label column, then a three-column span headed DCoA and a three-column span headed ATP; the kinetic column heads printed under each span are Km(uM) | Kcat (min^-1) | Kcat/Km (uM^-1 min^-1). The cited cell set is Table 2, DCoA span, enzyme row WT: Km(uM) = 34.9; Kcat (min^-1) = 1.758; Kcat/Km (uM^-1 min^-1) = 0.0503.

normalized_value_unit_evidence: Km: printed Table 2 DCoA-span cell 34.9 uM; 34.9 / 1000 = 0.0349 mM. kcat: printed Table 2 DCoA-span cell 1.758 min^-1; 1.758 / 60 = 0.0293 s^(-1). kcat/Km: printed Table 2 DCoA-span cell 0.0503 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000 / 60 s^-1 mM^-1, so 0.0503 x 1000 / 60 = 0.8383333333333334 s^(-1)*mM^(-1). The exported values of this row are kcat 0.0293, kcat_over_km 0.839541547277937, km 0.0349; the metrics this record corrects are kcat_over_km.

raw_value_unit_evidence: Table 2, DCoA span, enzyme row WT: Km = 34.9 uM; Kcat = 1.758 min^-1; printed Kcat/Km = 0.0503 uM^-1 min^-1.

row_label: Table 2, DCoA block, enzyme row WT


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WPA3 and applied mutation signature D32E to reconstruct the assayed variant sequence.

column_label: Table 2 carries one enzyme-label column, then a three-column span headed DCoA and a three-column span headed ATP; the kinetic column heads printed under each span are Km(uM) | Kcat (min^-1) | Kcat/Km (uM^-1 min^-1). The cited cell set is Table 2, ATP span, enzyme row D32E: Km(uM) = 34.5; Kcat (min^-1) = 3.996; Kcat/Km (uM^-1 min^-1) = 0.1158.

normalized_value_unit_evidence: Km: printed Table 2 ATP-span cell 34.5 uM; 34.5 / 1000 = 0.0345 mM. kcat: printed Table 2 ATP-span cell 3.996 min^-1; 3.996 / 60 = 0.06659999999999999 s^(-1). kcat/Km: printed Table 2 ATP-span cell 0.1158 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000 / 60 s^-1 mM^-1, so 0.1158 x 1000 / 60 = 1.9300000000000002 s^(-1)*mM^(-1). The exported values of this row are kcat 0.067, kcat_over_km 1.9420289855072463, km 0.0345; the metrics this record corrects are kcat, kcat_over_km.

raw_value_unit_evidence: Table 2, ATP span, enzyme row D32E: Km = 34.5 uM; Kcat = 3.996 min^-1; printed Kcat/Km = 0.1158 uM^-1 min^-1.

row_label: Table 2, ATP block, enzyme row D32E


enzyme_display_name: squalene monooxygenase

organism: Rattus norvegicus

substrate_name: H+; O2; Squalene; NADPH

mutation_signature: Δ1

mutation_type: deletion

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) wildtype delta1-99, C-terminal His-tag

enzyme: squalene monooxygenase

substrate: H+; O2; Squalene; NADPH


substrate_name: Squalene; O2; H+; NADPH

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant F523A delta1-99, C-terminal His-tag

substrate: Squalene; O2; H+; NADPH


substrate_name: NADPH; Squalene; O2; H+

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant Y528A delta1-99, C-terminal His-tag

substrate: NADPH; Squalene; O2; H+


substrate_name: H+; O2; NADPH; Squalene

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant Y209A delta1-99, C-terminal His-tag

substrate: H+; O2; NADPH; Squalene


substrate_name: NADPH; O2; Squalene; H+

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant F223A delta1-99, C-terminal His-tag

substrate: NADPH; O2; Squalene; H+


proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant F476A delta1-99, C-terminal His-tag


proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant F228A delta1-99, C-terminal His-tag


substrate_name: NADPH; O2; H+; Squalene

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant F491A delta1-99, C-terminal His-tag

substrate: NADPH; O2; H+; Squalene


organism: Homo sapiens

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) wildtype (aa 118–574), N-terminally truncated and N-terminal His-tag


substrate_name: O2; H+; Squalene; NADPH

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant Y194A delta1-99, C-terminal His-tag

substrate: O2; H+; Squalene; NADPH


substrate_name: O2; NADPH; H+; Squalene

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant Y493A delta1-99, C-terminal His-tag

substrate: O2; NADPH; H+; Squalene


substrate_name: Squalene; O2; NADPH; H+

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant Y334A delta1-99, C-terminal His-tag

substrate: Squalene; O2; NADPH; H+


proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant Y473A delta1-99, C-terminal His-tag


substrate_name: H+; NADPH; O2; Squalene

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant F522A delta1-99, C-terminal His-tag

substrate: H+; NADPH; O2; Squalene


substrate_name: H+; Squalene; NADPH; O2

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant F305A delta1-99, C-terminal His-tag

substrate: H+; Squalene; NADPH; O2


substrate_name: NADPH; H+; Squalene; O2

proof_lines: SABIO-RK modifier species: squalene monooxygenase(Enzyme) mutant F287A delta1-99, C-terminal His-tag

substrate: NADPH; H+; Squalene; O2


enzyme_display_name: linoleate 8R-lipoxygenase

organism: Colletotrichum gloeosporioides

substrate_name: palmitoleate

sequence_source: EBI Proteins API / UniProt accession A0A0S2SWE4

smiles: CCCCCC/C=C\CCCCCCCC(=O)O

enzyme: linoleate 8R-lipoxygenase

substrate: palmitoleate


substrate_name: oleate

smiles: CCCCCCCC/C=C\CCCCCCCC(=O)O

substrate: oleate


organism: Gaeumannomyces graminis

substrate_name: Linoleate; O2

sequence_source: EBI Proteins API / UniProt accession Q9UUS2

substrate: Linoleate; O2


organism: Candida albicans

substrate_name: H+; Squalene; NADH; O2

sequence_source: EBI Proteins API / UniProt accession Q92206

substrate: H+; Squalene; NADH; O2


substrate_name: Squalene

sequence_source: EBI Proteins API / UniProt accession Q14534

substrate: Squalene


substrate_name: Protein

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

substrate: Protein


substrate_name: H+; Squalene; O2; NADPH

sequence_source: EBI Proteins API UniProtKB accession P52020

substrate: H+; Squalene; O2; NADPH


substrate_name: O2; H+; NADPH; Squalene

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: squalene monooxygenase(Enzyme) mutant delta-N-99 His-tagged

substrate: O2; H+; NADPH; Squalene


organism: Saccharomyces cerevisiae

substrate_name: H+; O2; Squalene; NADPH

sequence_source: EBI Proteins API UniProtKB accession P32476

substrate: H+; O2; Squalene; NADPH


organism: Candidatus Liberibacter asiaticus

proof_lines: pH 8.2, 37°C, AICAR TFase activity of CLasATIC


organism: Cryptococcus neoformans

sequence_source: EBI Proteins API UniProtKB accession J9VJP1


sequence_source: EBI Proteins API UniProtKB accession P15639

proof_lines: pH 7.5, temperature not specified in the publication


organism: Gallus gallus

sequence_source: EBI Proteins API UniProtKB accession P31335


sequence_source: EBI Proteins API UniProtKB:P31939 (Swiss-Prot), checked 2026-06-11

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


organism: Staphylococcus lugdunensis

proof_lines: full length bifunctional AICAR transformylase/IMP cyclohydrolase (ATIC), pH 7.4, temperature not specified in the publication


mutation_signature: AICAR transformylase activity of domain truncation pET- -AICARTF1

proof_lines: AICAR transformylase activity of domain truncation mutant pET-28c-AICARTF1, pH 7.4, temperature not specified in the publication


enzyme_display_name: deoxyhypusine synthase

organism: Cryptosporidium parvum

substrate_name: spermidine

sequence_source: EBI Proteins API UniProtKB:A3FQA5 (TrEMBL), checked 2026-06-11

enzyme: deoxyhypusine synthase

substrate: spermidine


substrate_name: Spermidine; [eIF5A-precursor]-lysine

sequence_source: EBI Proteins API UniProtKB:P49366 (Swiss-Prot), checked 2026-06-11

proof_lines: pH and temperature not specified in the publication

substrate: Spermidine; [eIF5A-precursor]-lysine


organism: Leishmania donovani

sequence_source: EBI Proteins API UniProtKB:B5APK2 (Swiss-Prot), checked 2026-06-11


substrate_name: [eIF5A-precursor]-lysine; Spermidine

substrate: [eIF5A-precursor]-lysine; Spermidine


organism: Senecio vernalis

sequence_source: EBI Proteins API UniProtKB:Q9SC14 (Swiss-Prot), checked 2026-06-11


substrate_name: Putrescine

sequence_source: EBI Proteins API UniProt-backed record Q9SC14 checked 2026-06-11

substrate: Putrescine


substrate_name: Spermidine

smiles: NCCCCNCCCN

substrate: Spermidine


organism: Theileria parva


organism: Trichomonas vaginalis

sequence_source: EBI Proteins API UniProt-backed record F1AQF9 checked 2026-06-11


organism: Trypanosoma brucei brucei

sequence_source: EBI Proteins API UniProt-backed record Q38BX0 checked 2026-06-11


substrate_name: NAD+

sequence_source: EBI Proteins API UniProt-backed record Q38BX0 checked 2026-06-11; H266A coordinate check failed

assay_conditions_summary: cofactor NAD+

proof_lines: mutant H266A, pH not specified in the publication, temperature not specified in the publication

substrate: NAD+


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


sequence_variant_note: Resolved canonical sequence from EBI Proteins API UniProt-backed record Q38BX0 checked 2026-06-11; E166A reconstructed from direct 1-based residue check and applied mutation signature E166A to reconstruct the assayed variant sequence.

proof_lines: mutant E166A, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: phosphoserine transaminase

organism: Arabidopsis thaliana

substrate_name: 3-Phosphohydroxypyruvate; L-Glutamate

sequence_source: EBI Proteins API UniProt accession Q96255

proof_lines:
pH 8.2, 25°C
Raw SKiD Env: Temp=25°C, pH=8.2

enzyme: phosphoserine transaminase

substrate: 3-Phosphohydroxypyruvate; L-Glutamate


substrate_name: L-Glutamate; 3-Phosphohydroxypyruvate

proof_lines: SABIO-RK modifier species: phosphoserine transaminase(Enzyme) wildtype truncated

substrate: L-Glutamate; 3-Phosphohydroxypyruvate


organism: Bombyx mori

sequence_source: EBI Proteins API UniProt accession Q2F5M8

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


organism: Bos taurus

sequence_source: EBI Proteins API UniProt accession A0A3S5ZPF7


organism: Entamoeba histolytica

sequence_source: EBI Proteins API UniProt accession Q60I38

proof_lines:
pH 8.5, 25°C
Raw SKiD Env: Temp=25°C, pH=8.5
Raw SKiD Env: Temp=-----, pH=8.5


substrate_name: O-phospho-L-serine

proof_lines: pH 8.5, temperature not specified in the publication, recombinant mutant EhPSAT_DELTA15

substrate: O-phospho-L-serine


proof_lines: pH 8.5, temperature not specified in the publication, recombinant wild-type enzyme


mutation_signature: Δ4

proof_lines: pH 8.5, temperature not specified in the publication, recombinant mutant EhPSAT_DELTA4


organism: Aspergillus nidulans

substrate_name: linoleate

sequence_source: EBI Proteins API UniProt accession Q6RET3

smiles: CCCCC/C=C\C/C=C\CCCCCCCC(=O)O

substrate: linoleate


substrate_name: palmitoleate

substrate: palmitoleate


substrate_name: (11Z)-icos-11-enoic acid

smiles: CCCCCCCC/C=C\CCCCCCCCCC(=O)O

substrate: (11Z)-icos-11-enoic acid


substrate_name: oleate

substrate: oleate


organism: Colletotrichum gloeosporioides

sequence_source: EBI Proteins API UniProt accession A0A0S2SWE4


substrate_name: eicosenoic acid

sequence_source: EBI Proteins API UniProt accession A0A0S2SWE4 canonical context only

proof_lines: N-terminal 8-dioxygenase domain, pH 6.5, 40°C

proof_lines: recombinant enzyme, N-terminal domain activity, pH 6.5, 40°C

proof_lines: recombinant enzyme, whole enzyme activity, pH 6.5, 40°C

substrate: eicosenoic acid


substrate_name: alpha-linolenate

smiles: CC/C=C\C/C=C\C/C=C\CCCCCCCC(=O)O

substrate: alpha-linolenate


enzyme_display_name: triokinase

organism: Homo sapiens

substrate_name: dihydroxyacetone

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q3LXA3 and applied mutation signature T112A to reconstruct the assayed variant sequence.

smiles: O=C(CO)CO

assay_conditions_summary: pH 7.5; 310.15 K; cofactor FMN

column_label: Table 1: Kinetic parameters of hTKFC and mutants (J. Biol. Chem. 2014, volume 289, number 15, pages 10620-10636); the table's stub column is 'Assay performed (substrate)' and its seven data column heads are 'Wild type', 'L domain', 'H221A', 'C404A', 'S446A', 'T112A' and 'K204A'; block 'DHA kinase (DHA) activity'; column 'T112A'; line 'kcat (s^-1)' = 0.51; line '10^6 Km (M)' = 6.63; line '10^-4 kcat/Km (M^-1 s^-1)' = 7.6.

normalized_value_unit_evidence: kcat: the printed cell 0.51 is already in s^-1, so no unit conversion applies and the canonical value is 0.51 s^(-1). Km: the column head is '10^6 Km (M)', so the printed cell 6.63 is 6.63 x 10^-6 M = 6.63 uM, and 6.63 / 1000 gives 0.00663 mM. kcat/Km: the column head is '10^-4 kcat/Km (M^-1 s^-1)', so the printed cell 7.6 is 7.6 x 10^4 M^-1 s^-1, and since 1 M^-1 s^-1 is 0.001 s^-1 mM^-1 that gives 76.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, DHA kinase (DHA) activity block, column 'T112A': printed 'kcat (s^-1)' cell 0.51; printed '10^6 Km (M)' cell 6.63; printed '10^-4 kcat/Km (M^-1 s^-1)' cell 7.6.

row_label: Table 1, DHA kinase (DHA) activity block, column head 'hTKFC forms' entry 'T112A' (hTKFC form T112A)

enzyme: triokinase

substrate: dihydroxyacetone


substrate_name: D-glyceraldehyde

sequence_source: UniProtKB Q3LXA3 direct REST/FASTA check on 2026-06-11

substrate: D-glyceraldehyde


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB Q3LXA3 direct REST/FASTA check on 2026-06-11 and applied mutation signature C404A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C404A, with D-glyceraldehyde as cosubstrate,at pH 7.5 and 37°C

proof_lines: mutant enzyme C404A, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C

substrate: ATP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q3LXA3 and applied mutation signature C404A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of hTKFC and mutants (J. Biol. Chem. 2014, volume 289, number 15, pages 10620-10636); the table's stub column is 'Assay performed (substrate)' and its seven data column heads are 'Wild type', 'L domain', 'H221A', 'C404A', 'S446A', 'T112A' and 'K204A'; block 'GA kinase (GA) activity'; column 'C404A'; line 'kcat (s^-1)' = 2.27; line '10^6 Km (M)' = 16.2; line '10^-4 kcat/Km (M^-1 s^-1)' = 14.0.

normalized_value_unit_evidence: kcat: the printed cell 2.27 is already in s^-1, so no unit conversion applies and the canonical value is 2.27 s^(-1). Km: the column head is '10^6 Km (M)', so the printed cell 16.2 is 16.2 x 10^-6 M = 16.2 uM, and 16.2 / 1000 gives 0.0162 mM. kcat/Km: the column head is '10^-4 kcat/Km (M^-1 s^-1)', so the printed cell 14.0 is 14.0 x 10^4 M^-1 s^-1, and since 1 M^-1 s^-1 is 0.001 s^-1 mM^-1 that gives 140.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, GA kinase (GA) activity block, column 'C404A': printed 'kcat (s^-1)' cell 2.27; printed '10^6 Km (M)' cell 16.2; printed '10^-4 kcat/Km (M^-1 s^-1)' cell 14.0.

row_label: Table 1, GA kinase (GA) activity block, column head 'hTKFC forms' entry 'C404A' (hTKFC form C404A)


proof_lines: wild type enzyme, with D-glyceraldehyde as cosubstrate, at pH 7.5 and 37°C

proof_lines: wild type enzyme, with dihydroxyacetone as cosubstrate, at pH 7.5 and 37°C


column_label: Table 1, Wild type column, DHA kinase (DHA) activity / Wild type: kcat 5.00 s^-1; Km 1.55 uM; kcat/Km 321 x 10^4 M^-1*s^-1.

raw_value_unit_evidence: Table 1; measurement Wild type; construct wild-type hTKFC; substrate dihydroxyacetone (DHA); condition pH 7.5; 37 °C; DHA kinase (DHA) activity; kcat raw_value=5.00 raw_unit=s^-1; Km raw_value=1.55 raw_unit=uM; kcat/Km raw_value=321 x 10^4 raw_unit=M^-1*s^-1.

row_label: DHA kinase (DHA) activity / Wild type

table_label: Table 1. Kinetic parameters of hTKFC and mutants


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q3LXA3 and applied mutation signature K204A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of hTKFC and mutants (J. Biol. Chem. 2014, volume 289, number 15, pages 10620-10636); the table's stub column is 'Assay performed (substrate)' and its seven data column heads are 'Wild type', 'L domain', 'H221A', 'C404A', 'S446A', 'T112A' and 'K204A'; block 'DHA kinase (DHA) activity'; column 'K204A'; line 'kcat (s^-1)' = 2.79; line '10^6 Km (M)' = 2.52; line '10^-4 kcat/Km (M^-1 s^-1)' = 115.

normalized_value_unit_evidence: kcat: the printed cell 2.79 is already in s^-1, so no unit conversion applies and the canonical value is 2.79 s^(-1). Km: the column head is '10^6 Km (M)', so the printed cell 2.52 is 2.52 x 10^-6 M = 2.52 uM, and 2.52 / 1000 gives 0.00252 mM. kcat/Km: the column head is '10^-4 kcat/Km (M^-1 s^-1)', so the printed cell 115 is 115 x 10^4 M^-1 s^-1, and since 1 M^-1 s^-1 is 0.001 s^-1 mM^-1 that gives 1150.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, DHA kinase (DHA) activity block, column 'K204A': printed 'kcat (s^-1)' cell 2.79; printed '10^6 Km (M)' cell 2.52; printed '10^-4 kcat/Km (M^-1 s^-1)' cell 115.

row_label: Table 1, DHA kinase (DHA) activity block, column head 'hTKFC forms' entry 'K204A' (hTKFC form K204A)


organism: Escherichia coli

sequence_source: UniProtKB:P23721 direct lookup on 2026-06-11

proof_lines:
pH 8.2, 25°C, recombinant enzyme
Raw SKiD Env: Temp=25°C, pH=8.2
Raw SKiD Env: Temp=30°C, pH=8.2


substrate_name: L-homoserine

proof_lines: pH 8.2, 30°C, recombinant wild-type enzyme

substrate: L-homoserine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P23721 direct lookup plus R42W/R77W reconstruction on 2026-06-11 and applied mutation signature R42W/R77W to reconstruct the assayed variant sequence.

proof_lines: pH 8.2, 30°C, recombinant mutant R42W/R77W


organism: Glycine max

sequence_source: UniProtKB:I1JCA9 direct lookup on 2026-06-11


substrate_name: 2-Oxoglutarate; O-Phospho-L-serine

sequence_source: UniProtKB:Q9Y617 direct lookup on 2026-06-11

substrate: 2-Oxoglutarate; O-Phospho-L-serine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9Y617 direct lookup plus D100A reconstruction on 2026-06-11 and applied mutation signature D100A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: phosphoserine transaminase(Enzyme) mutant D100A N-terminal His-tag


organism: Niallia circulans

sequence_source: UniProtKB:Q59196 direct lookup on 2026-06-11

assay_conditions_summary: pH 7

proof_lines:
pH 7.0
pH 9.0
Raw SKiD Env: Temp=-----, pH=7


substrate_name: L-glutamate

proof_lines: pH 9.5, 25°C, recombinant enzyme mutant K2G

proof_lines: pH 8.2, 25°C, recombinant enzyme mutant K2G

substrate: L-glutamate


enzyme_display_name: N-acylmannosamine kinase

sequence_source: UniProtKB:P45425 direct REST lookup on 2026-06-11

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

enzyme: N-acylmannosamine kinase


substrate_name: D-Glucose

substrate: D-Glucose


substrate_name: ATP; D-Glucose

assay_conditions_summary: cofactor ATP

substrate: ATP; D-Glucose


substrate_name: N-Acetyl-D-mannosamine

substrate: N-Acetyl-D-mannosamine