proof_lines: wild type enzyme, with NADPH as cosubstrate, pH and temperature not specified in the publication

proof_lines: wild type enzyme, with NADH as cosubstrate, pH and temperature not specified in the publication


organism: Escherichia coli

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

source: brenda


organism: Priestia megaterium

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


organism: Pseudomonas aeruginosa

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH


organism: Staphylococcus aureus

substrate_name: NADH

assay_conditions_summary: pH 8; 303.15 K; buffer HEPES; cofactor NADPH

proof_lines: using NADPH as cosubstrate, in HEPES buffer, pH 8.0, at 30°C

substrate: NADH


organism: Zea mays

substrate_name: dihydrodipicolinate

substrate: dihydrodipicolinate


organism: Deinococcus radiodurans

substrate_name: homoisocitrate

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

substrate: homoisocitrate


mutation_type: substitution


substrate_name: isocitrate

mutation_signature: A80 deletion mutant

mutation_type: deletion

substrate: isocitrate


enzyme_display_name: xyloglucan:xyloglucosyl transferase

organism: Arabidopsis thaliana

substrate_name: XXXGol; Xyloglucan

protein_accession_database: UniProt

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

sequence_source: UniProtKB REST P93046 (UniProtKB reviewed (Swiss-Prot))

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

proof_lines: xyloglucan endotransglucosylase activity, pH 5.5, 20°C

enzyme: xyloglucan:xyloglucosyl transferase

substrate: XXXGol; Xyloglucan


substrate_name: xyloglucan oligosaccharide

sequence_source: UniProtKB REST Q9LJR7 (UniProtKB reviewed (Swiss-Prot))

proof_lines: donor substrate hydroxylethyl cellulose, pH not specified in the publication, 30°C

proof_lines: donor substrate tamarind xyloglucan, pH not specified in the publication, 30°C

proof_lines: donor substrate barley beta-glucan, pH not specified in the publication, 30°C

substrate: xyloglucan oligosaccharide


organism: Fragaria chiloensis

substrate_name: xyloglucan

sequence_source: UniProtKB REST D5HP43 (UniProtKB unreviewed (TrEMBL))

substrate: xyloglucan


organism: Hordeum vulgare

sequence_source: UniProtKB REST P93668 (UniProtKB unreviewed (TrEMBL))

assay_conditions_summary: pH 6; 303.15 K; buffer 100 mM sodium succinate

proof_lines: purified isozyme XET5, at 30°C in 100 mM sodium succinate buffer, pH 6.0, containing 5 mM CaCl2


sequence_source: UniProtKB REST B1P1S7 (UniProtKB unreviewed (TrEMBL))

assay_conditions_summary: pH 6; 303.15 K; buffer pH 6

proof_lines: isoform XET6, using xyloglycan as donor substrate, at 30°C, in 50 mM ammonium acetate buffer pH 6.0

proof_lines: recombinant isozyme XET6, at 30°C in 100 mM sodium succinate buffer, pH 6.0, containing 5 mM CaCl2


sequence_source: UniProtKB REST P93672 (UniProtKB unreviewed (TrEMBL))

proof_lines: isoform XET4, using xyloglycan as donor substrate, at 30°C, in 50 mM ammonium acetate buffer pH 6.0


sequence_source: UniProtKB REST P93671 (UniProtKB unreviewed (TrEMBL))

proof_lines: isoform XET3, using xyloglycan as donor substrate, at 30°C, in 50 mM ammonium acetate buffer pH 6.0


organism: Pinus radiata


organism: Populus tomentosa

substrate_name: xyloglucan oligosaccharide XXXG

sequence_source: UniProtKB REST A0A2L0E8V5 (UniProtKB unreviewed (TrEMBL))

substrate: xyloglucan oligosaccharide XXXG


sequence_source: UniProtKB REST A0A2L0E8U4 (UniProtKB unreviewed (TrEMBL))


organism: Populus tremula x Populus tremuloides

substrate_name: nonasaccharide XLLG-ol

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

proof_lines: pH 5.5, 25°C, recombinant N93S mutant enzyme

substrate: nonasaccharide XLLG-ol


sequence_source: UniProtKB REST Q8GZD5 (UniProtKB reviewed (Swiss-Prot))

proof_lines: pH 5.5, 25°C, recombinant wild-type enzyme


enzyme_display_name: isopentenyl phosphate kinase

substrate_name: isopentenyl phosphate

sequence_source: UniProtKB REST Q8H1F7 (UniProtKB reviewed (Swiss-Prot))

proof_lines: pH and temperature not specified in the publication

enzyme: isopentenyl phosphate kinase

substrate: isopentenyl phosphate


organism: Haloferax volcanii

substrate_name: ATP

sequence_source: UniProtKB REST D4GWT7 (UniProtKB reviewed (Swiss-Prot))

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

substrate: ATP


organism: Methanocaldococcus jannaschii

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

sequence_source: UniProtKB REST Q60352 (UniProtKB reviewed (Swiss-Prot))

proof_lines:
pH 7.5, 55°C
Raw SKiD Env: Temp=-----, pH=8
Raw SKiD Env: Temp=55°C, pH=7.5

source_databases_merged: brenda skid


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST Q60352 canonical sequence by H60Q substitution and applied mutation signature H60Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

proof_lines: mutant H60Q, pH 8.0, temperature not specified in the publication


organism: Eimeria tenella

substrate_name: malonyl-CoA

assay_conditions_summary: pH 6.8; 301.15 K; cofactor CoA

substrate: malonyl-CoA


substrate_name: malonyl CoA

assay_conditions_summary: cofactor CoA

proof_lines: reaction with E. coli acyl-carrier-protein

substrate: malonyl CoA


assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines: acyl carrier protein mutant Q66R, pH 7.5, 25°C


substrate_name: methylmalonyl-CoA

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

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

proof_lines: wild-type acyl carrier protein, pH 7.5, 25°C

substrate: methylmalonyl-CoA


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

proof_lines: mutant enzyme R117A, with acetoacetyl-CoA as cosubstrate, pH and temperature not specified in the publication

proof_lines: mutant enzyme R117A, with malonyl-CoA as cosubstrate, pH and temperature not specified in the publication


organism: Escherichia coli K-12


organism: Glycine max


organism: Mycobacterium tuberculosis

substrate_name: holo-acyl-carrier protein

proof_lines: holo-acyl-carrier protein from Mycobacterium tuberculosis

substrate: holo-acyl-carrier protein


organism: Persea americana

substrate_name: acyl-carrier protein

substrate: acyl-carrier protein


organism: Plasmodium falciparum

proof_lines: acyl carrier protein mutant Q67R, pH 7.5, 25°C


proof_lines: acyl carrier protein mutant E20A, pH 7.5, 25°C


proof_lines: acyl carrier protein mutant T65A, pH 7.5, 25°C


substrate_name: pea xyloglucan

proof_lines: recombinant TCH4 protein, with XLLG-ol as acceptor

substrate: pea xyloglucan


organism: Brassica oleracea

proof_lines:
isoenzyme C30
isoenzymes C45a and C45b


organism: Tropaeolum majus

proof_lines:
isozyme eXET, pH 5.5, 30°C
isozyme sXET, pH 5.5, 30°C


organism: Unknown


organism: Vigna radiata var. radiata

proof_lines:
isoenzyme M55b
isoenzyme M45
isoenzyme M55a


organism: Methanothermobacter thermautotrophicus

substrate_name: dimethylallyl phosphate

source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

sequence_source: UniProt REST accession check O26153 on 2026-06-17; matched curation accession cache.

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

data_origin: experimental

substrate: dimethylallyl phosphate

status: unverified

source: oed


substrate_name: isopentenyl thiolophosphate

smiles: C=C(C)CCSP(=O)(O)O

substrate: isopentenyl thiolophosphate


substrate_name: geranyl phosphate

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

substrate: geranyl phosphate


organism: Thermoplasma acidophilum

verification_status: verified

sequence_source: UniProt REST accession check Q9HLX1 on 2026-06-17; matched curation accession cache.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH

column_label: Table 2, enzyme block 'THA IPK', substrate row 'GP (geranyl phosphate)': kcat (s^-1) = 0.047 ± 0.008; Km (uM) = 4700 ± 1300; kcat/Km (M^-1 s^-1) = 10; Relative kcat/Km (%) = 0.00055.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.047 s^-1 is already in the export unit; the exported value is 0.047 s^(-1). Km: printed Table 2 cell 4700 uM (the JATS source sets the MICRO SIGN in the column header and means micromolar); 4700 / 1000 = 4.7 mM; the exported value is 4.7 mM. kcat/Km: printed Table 2 kcat/Km cell 10 M^-1 s^-1; 10.0 / 1000 = 0.01 s^(-1)*mM^(-1); the exported value is 0.01 s^(-1)*mM^(-1). The cited Table 2 row prints one further column, Relative kcat/Km (%) = 0.00055, which is a percentage of the IP reference row and is not a kinetic metric the export carries.

row_label: Table 2, enzyme block 'THA IPK', substrate row 'GP (geranyl phosphate)' (catalog accession Q9HLX1)

table_label: Table 2. Apparent kinetic constants with alternate substrates.

status: verified


substrate_name: butyl phosphate

smiles: CCCCOP(=O)(O)O

substrate: butyl phosphate


substrate_name: but-3-en-1-yl phosphate

smiles: C=CCCOP(=O)(O)O

substrate: but-3-en-1-yl phosphate


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

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


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


substrate_name: fosfomycin

sequence_variant_note: Resolved canonical sequence from UniProt REST accession check Q9HLX1 on 2026-06-17; matched curation accession cache. and applied mutation signature K204A to reconstruct the assayed variant sequence.

substrate: fosfomycin


assay_conditions_summary: pH 7.5; 204.00 K; cofactor ATP


organism: Bacillus subtilis

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


organism: Klebsiella pneumoniae

sequence_source: UniProtKB:O32717 direct accession lookup

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WNG5 direct accession lookup and applied mutation signature H90A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P9WNG5 direct accession lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WNG5 direct accession lookup and applied mutation signature N155A to reconstruct the assayed variant sequence.


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Rattus norvegicus

substrate_name: Malonyl-CoA; Pantetheine

substrate: Malonyl-CoA; Pantetheine


organism: Schizochytrium sp.

assay_conditions_summary: pH 6.8; cofactor CoA

proof_lines: recombinant enzyme, pH 6.8, temperature not specified in the publication


organism: Arabidopsis thaliana

sequence_source: UniProtKB:Q9ZSU4 direct accession lookup


substrate_name: XXXGol; Xyloglucan

sequence_source: UniProtKB:Q38911 direct accession lookup

proof_lines: xyloglucan endotransglucosylase activity, pH 5.5, 20°C

substrate: XXXGol; Xyloglucan


organism: Methanocaldococcus jannaschii

sequence_source: UniProtKB:Q60352 direct accession lookup

assay_conditions_summary: pH 8; cofactor ATP

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


sequence_source: UniProtKB:O26153 direct accession lookup


verification_status: corrected

assay_conditions_summary: pH 7.5; 310.15 K; buffer the assay; cofactor ATP

column_label: Table 2: Apparent kinetic constants with alternate substrates. (Biochemistry 2010, 49(1), NIH Public Access author manuscript), enzyme block 'MTH IPK', substrate row 'DMAP'; column 'kcat (s-1)' = 34.0; column 'Km (uM)' = 43.2; column 'kcat/Km (M-1 s-1)' = 7.9 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 34.0 s-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 34.0 s^(-1); the exported value is 34.0 s^(-1). Km: printed Table 2 cell 43.2 uM; 43.2 / 1000 = 0.0432 mM; the paper value is 0.0432 mM; the exported value is 0.0076 mM. kcat/Km: printed Table 2 cell 7.9 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.9 x 10^5 / 1000 = 790.0 s^-1 mM^-1; the paper value is 790.0 s^(-1)*mM^(-1); the export row for this identity stores no catalytic-efficiency value.

raw_value_unit_evidence: Table 2, enzyme block 'MTH IPK', substrate row 'DMAP': kcat = 34.0 s-1; Km = 43.2 uM; printed kcat/Km = 7.9 x 10^5 M^-1 s^-1.

status: corrected


source_db: uniprot

source: uniprot


organism: Homo sapiens


substrate_name: acetyl-CoA

assay_conditions_summary: cofactor NADPH

substrate: acetyl-CoA


organism: Mus musculus


substrate_name: Unknown

km_display: Not reported

substrate: Unknown


organism: Populus tremula x Populus tremuloides

substrate_name: reduced xyloglucan-derived nonasaccharide as acceptor substrate (at pH 5.5 and 25 degrees Celsius)


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

substrate_name: isopentenyl phosphate

assay_conditions_summary: cofactor ATP

substrate: isopentenyl phosphate


organism: Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)


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


substrate_name: XXXGol

proof_lines: KM for xyloglucan as donor substrate is 2.87 mg/ml. KM is quoted in mg/ml, not uM, because XTHs are able to utilise any segment of the polysaccharide chain equally well, not just one site per molecule as with the acceptor.

substrate: XXXGol


proof_lines: KM for xyloglucan as donor substrate is 1.6 mg/ml. KM is quoted in mg/ml, not uM, because XTHs are able to utilise any segment of the polysaccharide chain equally well, not just one site per molecule as with the acceptor.


proof_lines: kcat is 1.9 sec(-1) with isopentenyl phosphate (PubMed:24327557). kcat is 3.7 sec(-1) with isopentenyl phosphate (PubMed:26216978). kcat is 2.7 sec(-1) with dimethylallyl diphosphate (PubMed:26216978). kcat is 0.0039 sec(-1) with geranyl ph


organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)


substrate_name: malonyl CoA

substrate: malonyl CoA


organism: Spinacia oleracea

proof_lines:
ping-pong mechanism
sequential mechanism
with respect to acyl carrier protein


organism: Streptomyces coelicolor

substrate_name: N-acetylcysteamine

substrate: N-acetylcysteamine


proof_lines: hexahistidine-tagged fusion protein, reaction with Streptomyces coelicolor acyl-carrier-protein

proof_lines: hexahistidine-tagged fusion protein, reaction with E. coli acyl-carrier-protein


substrate_name: malonyl-CoA

substrate: malonyl-CoA


substrate_name: [acyl-carrier protein]

proof_lines: pH 6.8, recombinant mutants M137L and F200S

substrate: [acyl-carrier protein]


enzyme_display_name: starch synthase

organism: Hordeum vulgare

substrate_name: ADPglucose

proof_lines:
isoenzyme I, primed reaction
isoenzyme III, primed reaction
isoenzyme IV, primed reaction

enzyme: starch synthase

substrate: ADPglucose


proof_lines:
isoenzyme I
isoenzyme IV
isoenzyme III


organism: Unknown


organism: Zea mays

assay_conditions_summary: pH 8; 303.15 K; cofactor ADP

proof_lines: starch synthase I, primer amylopectin, 500 mM citrate


enzyme_display_name: thyroxine 5'-deiodinase

organism: Suncus murinus

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

enzyme: thyroxine 5'-deiodinase


organism: Sus scrofa

substrate_name: L-thyroxine

substrate: L-thyroxine


organism: Trichomonas vaginalis (strain ATCC PRA-98 / G3)

substrate_name: UDP-glucose

assay_conditions_summary: cofactor ADP

substrate: UDP-glucose


organism: Canis lupus familiaris


organism: Felis catus


organism: Fundulus heteroclitus

substrate_name: thyroxine

substrate: thyroxine


organism: Gallus gallus


organism: Halocynthia roretzi


organism: Homo sapiens


organism: Mus musculus


organism: Rattus norvegicus


substrate_name: ADP-alpha-D-glucose

sequence_source: UniProtKB REST Q9M5A3; retrieved 2026-06-17

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ADP

proof_lines: isoform SSI with maltotriose as cosubstrate, at pH 8.5 and 30°C

substrate: ADP-alpha-D-glucose


sequence_source: UniProtKB REST P09842; retrieved 2026-06-17

proof_lines: isoform GBSSI, with maltobiose as cosubstrate, at pH 8.5 and 30°C


sequence_source: UniProtKB REST F2CUZ5; retrieved 2026-06-17

proof_lines: isoform SSIV, with maltotriose as cosubstrate, at pH 8.5 and 30°C


sequence_source: UniProtKB REST I1W6L2; retrieved 2026-06-17

proof_lines: isoform SSIIIb, with maltotriose as cosubstrate, at pH 8.5 and 30°C


organism: Phaseolus vulgaris

substrate_name: glycogen

sequence_source: UniProtKB REST A4F2M4; retrieved 2026-06-17

proof_lines:
pH 8.0, 30°C
pH 8.0, 30°C, at 10 mg/ml glycogen
pH 8.0, 30°C, at 10 mg/ml amylopectin

substrate: glycogen


organism: Solanum tuberosum

substrate_name: Amylopectin; ADP alpha-D-glucoside

sequence_source: UniProtKB REST Q00775; retrieved 2026-06-17

substrate: Amylopectin; ADP alpha-D-glucoside


substrate_name: ADP alpha-D-glucoside; Amylopectin

sequence_source: UniProtKB REST Q43847; retrieved 2026-06-17

substrate: ADP alpha-D-glucoside; Amylopectin


substrate_name: Glycogen; ADP alpha-D-glucoside

sequence_source: UniProtKB REST O49064; retrieved 2026-06-17

substrate: Glycogen; ADP alpha-D-glucoside


substrate_name: ADP alpha-D-glucoside; Glycogen

sequence_source: UniProtKB REST O64923; retrieved 2026-06-17

substrate: ADP alpha-D-glucoside; Glycogen


organism: Streptomyces coelicolor


proof_lines: pH 6.8, recombinant mutants M126I and G198A


proof_lines: pH 6.8, recombinant mutants A197D and G198Y


proof_lines: N-acetylcysteamine as acceptor thiol, wild-type enzyme

proof_lines: pH 6.8, recombinant wild-type enzyme and mutant V98Q


proof_lines: pH 6.8, recombinant mutants G198Y and G198A


enzyme_display_name: inositol-phosphate phosphatase

organism: Arabidopsis thaliana

substrate_name: D-myoinositol 3-phosphate

enzyme: inositol-phosphate phosphatase

substrate: D-myoinositol 3-phosphate


organism: Bacillus subtilis (strain 168)

substrate_name: myo-inositol phosphate

substrate: myo-inositol phosphate


organism: Escherichia coli (strain K12)


substrate_name: D-myo-inositol 1-phosphate

substrate: D-myo-inositol 1-phosphate


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: inositol-1-phosphate (at pH 8.5 and 37 degrees Celsius)

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


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: inositol 1-phosphate

substrate: inositol 1-phosphate


organism: Escherichia coli

substrate_name: D-myo-Inositol 1-phosphate

sequence_variant_note: Resolved canonical sequence from UniProt P0ADG4 canonical sequence with selected mutation R121A applied after residue-position check and applied mutation signature R121A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R121A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C

substrate: D-myo-Inositol 1-phosphate


sequence_variant_note: Resolved canonical sequence from UniProt P0ADG4 canonical sequence with selected mutation V249A applied after residue-position check and applied mutation signature V249A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V249A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProt P0ADG4 canonical sequence with selected mutation R184A applied after residue-position check and applied mutation signature R184A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R184A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProt P0ADG4 canonical sequence with selected mutation H98F applied after residue-position check and applied mutation signature H98F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H98F, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProt P0ADG4 canonical sequence with selected mutation R248A applied after residue-position check and applied mutation signature R248A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R248A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProt P0ADG4 canonical sequence with selected mutation R183A applied after residue-position check and applied mutation signature R183A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R183A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProt P0ADG4 canonical sequence with selected mutation R184I applied after residue-position check and applied mutation signature R184I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R184I, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C


sequence_source: UniProt P0ADG4 canonical sequence from direct REST check

proof_lines: wild type enzyme, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C


substrate_name: H2O; 1-Phosphatidyl-D-myo-inositol 4,5-bisphosphate; H2O; 1-Phosphatidyl-D-myo-inositol 4,5-bisphosphate; 1-Phosphatidyl-1D-myo-inositol 4-phosphate; Phosphate


substrate_name: Unknown

ki_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProt P29218 canonical sequence with selected mutation H217A applied after residue-position check and applied mutation signature H217A to reconstruct the assayed variant sequence.

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from UniProt P29218 canonical sequence with selected mutation H217A/C218A applied after residue-position check and applied mutation signature H217A/C218A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, recombinant mutant H217A/C218A


sequence_source: UniProt P29218 canonical sequence from direct REST check

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

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


sequence_variant_note: Resolved canonical sequence from UniProt P29218 canonical sequence with selected mutation C218A applied after residue-position check and applied mutation signature C218A to reconstruct the assayed variant sequence.


substrate_name: 1D-myo-Inositol 1-phosphate

sequence_variant_note: Resolved canonical sequence from UniProt P29218 canonical sequence with selected mutation K36Q applied after residue-position check and applied mutation signature K36Q to reconstruct the assayed variant sequence.

substrate: 1D-myo-Inositol 1-phosphate


sequence_source: UniProt P29218 canonical sequence with selected mutation K36Q applied after residue-position check


enzyme_display_name: carboxypeptidase T

organism: Thermoactinomyces vulgaris

substrate_name: N-benzyloxycarbonyl-Ala-Ala-Leu

sequence_source: UniProtKB:P29068 canonical context only

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

proof_lines:
mutant CPT6
mutant CPT5

enzyme: carboxypeptidase T

substrate: N-benzyloxycarbonyl-Ala-Ala-Leu


substrate_name: benzyloxycarbonyl-Ala-Ala-Leu

sequence_source: UniProtKB:P29068; PubMed PMID 25619204; RCSB PDB 3V7Z/4DUK

substrate: benzyloxycarbonyl-Ala-Ala-Leu


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29068; PubMed PMID 25619204; RCSB PDB 3V7Z/4DUK and applied mutation signature D260N with inferred residue-numbering offset +98 to reconstruct the assayed variant sequence.


substrate_name: benzyloxycarbonyl-Ala-Ala-Arg

substrate: benzyloxycarbonyl-Ala-Ala-Arg


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29068; PubMed PMID 25619204; RCSB PDB 3V7Z/4DUK and applied mutation signature T257D with inferred residue-numbering offset +98 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29068; PubMed PMID 25619204; RCSB PDB 3V7Z/4DUK and applied mutation signature D263N with inferred residue-numbering offset +98 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29068; PubMed PMID 25619204; RCSB PDB 3V7Z/4DUK and applied mutation signature L254S with inferred residue-numbering offset +98 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29068; PubMed PMID 25619204; RCSB PDB 3V7Z/4DUK and applied mutation signature T262G with inferred residue-numbering offset +98 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29068; PubMed PMID 25619204; RCSB PDB 3V7Z/4DUK and applied mutation signature L211Q with inferred residue-numbering offset +98 to reconstruct the assayed variant sequence.


substrate_name: H2O; 1D-myo-Inositol 1-phosphate

sequence_source: UniProtKB REST exact accession lookup on 2026-06-17

substrate: H2O; 1D-myo-Inositol 1-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession lookup on 2026-06-17 and applied mutation signature K36Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: inositol-phosphate phosphatase(Enzyme) mutant K36Q


organism: Hordeum vulgare

substrate_name: DL-myo-inositol 1-phosphate

proof_lines: recombinant protein, 9.7 microM substrate, higher affinity as compared with reported Km values for other eukaryotic IMPases

substrate: DL-myo-inositol 1-phosphate


organism: Medicago truncatula

substrate_name: L-histidinol phosphate

substrate: L-histidinol phosphate


organism: Methanocaldococcus jannaschii


substrate_name: 1D-myo-Inositol 1-phosphate; H2O

substrate: 1D-myo-Inositol 1-phosphate; H2O


organism: Mycobacterium tuberculosis

substrate_name: myo-Inositol phosphate; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB REST exact accession lookup on 2026-06-17 and applied mutation signature L71A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: inositol-phosphate phosphatase(Enzyme) mutant L71A

substrate: myo-Inositol phosphate; H2O


organism: Mycolicibacterium smegmatis

substrate_name: Inositol 1-phosphate

substrate: Inositol 1-phosphate


substrate_name: 1D-myo-Inositol 3-phosphate; H2O

substrate: 1D-myo-Inositol 3-phosphate; H2O


organism: Saccharomyces cerevisiae


organism: Staphylococcus aureus

proof_lines: pH and temperature not specified in the publication


organism: Thermotoga maritima


sequence_source: UniProtKB:P29068 direct REST FASTA/JSON check; RCSB 4DUK SIFTS alignment for PMID 25619204 context.

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -14, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29068 direct REST FASTA/JSON check; RCSB 4DUK SIFTS alignment for PMID 25619204 context. and applied mutation signature L254S with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P29068 direct REST FASTA/JSON check. and applied mutation signature L211Q with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P29068 direct REST FASTA/JSON check.

sequence_variant_note: Mutation signature T262G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: N-Carbobenzoxy-Ala-Ala-Leu

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

substrate: N-Carbobenzoxy-Ala-Ala-Leu


substrate_name: N-benzyloxycarbonyl-L-Ala-L-Ala-L-Lys

proof_lines:
at pH 7.5 and 25°C
at pH 7.5 and 25Â°C

substrate: N-benzyloxycarbonyl-L-Ala-L-Ala-L-Lys


organism: Homo sapiens

substrate_name: Acetyl-[acyl-carrier protein]; Malonyl-[acyl-carrier protein]

sequence_source: UniProtKB direct lookup accession Q9NWU1 on 2026-06-17


sequence_source: UniProtKB direct lookup accession P9WQD9 on 2026-06-17


sequence_source: UniProtKB direct lookup accession P9WQD7 on 2026-06-17


substrate_name: butyryl-CoA

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

substrate: butyryl-CoA


organism: Streptococcus pneumoniae

substrate_name: malonyl-[acyl-carrier protein]

substrate: malonyl-[acyl-carrier protein]


organism: Actinidia deliciosa

sequence_source: UniProtKB direct lookup accession Q5U789 on 2026-06-17

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


organism: Arabidopsis thaliana

substrate_name: D-myo-Inositol 1-phosphate

sequence_source: UniProtKB direct lookup accession Q94F00 on 2026-06-17

substrate: D-myo-Inositol 1-phosphate


substrate_name: D-galactose 1-phosphate

substrate: D-galactose 1-phosphate


organism: Archaeoglobus fulgidus

sequence_source: UniProtKB direct lookup accession O30298 on 2026-06-17


substrate_name: 1D-myo-Inositol 1-phosphate

substrate: 1D-myo-Inositol 1-phosphate


organism: Bos taurus

sequence_source: UniProtKB direct lookup accession P20456 on 2026-06-17


sequence_source: UniProtKB direct lookup accession P0ADG4 on 2026-06-17


sequence_variant_note: Resolved canonical sequence from UniProtKB P0ADG4 canonical sequence plus reconstructed R199A substitution on 2026-06-17 and applied mutation signature R199A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R199A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P0ADG4 canonical sequence plus reconstructed K251A substitution on 2026-06-17 and applied mutation signature K251A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K251A, in 50 mM Tris-HCl with 8 mM MgCl2, pH 8.0, at 37°C


organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

substrate_name: inositol-1-phosphate (at 85 degrees Celsius)

proof_lines: kcat is 2.5 sec(-1) for IMPase activity (at 85 degrees Celsius) and 2.7 sec(-1) for FBPase activity (at 85 degrees Celsius).


substrate_name: myo-inositol 1-monophosphate

proof_lines: Inositol monophosphatase activity is less efficient than for IMPA1.

substrate: myo-inositol 1-monophosphate


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

proof_lines: kcat is 4.2 sec(-1) for IMPase activity (at 85 degrees Celsius) and 7.0 sec(-1) for FBPase activity (at 85 degrees Celsius).

substrate: inositol-1-phosphate (at 85 degrees Celsius)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: 3'-phosphoadenosine 5'-phosphate (at pH 9.0 and 30 degrees Celsius)

proof_lines: The second-order rate constant for PAP was determined to be over 3 orders of magnitude greater than those determined for IMP and FBP.


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

substrate_name: D-fructose 1,6-bisphosphate (at 85 degrees Celsius)

proof_lines: kcat is 23.4 sec(-1) for FBPase activity (at 85 degrees Celsius). FBPase activity is 5-fold higher than the IMPase activity.


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

substrate_name: DL-inositol-1-phosphate (at 95 degrees Celsius)

proof_lines: kcat is 207 sec(-1) for IMPase activity (at 95 degrees Celsius) and 268 sec(-1) for FBPase activity (at 95 degrees Celsius).


enzyme_display_name: galacturonan 1,4-alpha-galacturonidase

organism: Bacillus subtilis (strain 168)

substrate_name: pNPalphaGalUA (at about 37 degrees Celsius)

proof_lines: kcat is 3.6 sec(-1) with pNPalphaGalUA as substrate (at about 37 degrees Celsius).

enzyme: galacturonan 1,4-alpha-galacturonidase


enzyme_display_name: long-chain fatty acid omega-monooxygenase

substrate_name: palmitic acid

smiles: CCCCCCCCCCCCCCCC(=O)O

proof_lines: 27°C, pH not specified in the publication

substrate: palmitic acid


substrate_name: lauric acid

smiles: CCCCCCCCCCCC(=O)O

enzyme: long-chain fatty acid omega-monooxygenase

substrate: lauric acid


substrate_name: myristic acid

smiles: CCCCCCCCCCCCCC(=O)O

substrate: myristic acid


substrate_name: NADPH; H+; Dodecanoate; O2

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

substrate: NADPH; H+; Dodecanoate; O2


substrate_name: arachidonic acid

sequence_variant_note: Resolved canonical sequence from UniProtKB Q02928 canonical sequence plus reconstructed Y152N substitution on 2026-06-17 and applied mutation signature Y152N to reconstruct the assayed variant sequence.

substrate: arachidonic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB Q02928 canonical sequence plus reconstructed F434S substitution on 2026-06-17 and applied mutation signature F434S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q02928 canonical sequence plus reconstructed L509S substitution on 2026-06-17 and applied mutation signature L509S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q02928 canonical sequence plus reconstructed V185F substitution on 2026-06-17 and applied mutation signature V185F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q02928 canonical sequence plus reconstructed K276T substitution on 2026-06-17 and applied mutation signature K276T to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q02928 canonical sequence plus reconstructed K276T substitution on 2026-06-17

proof_lines: pH 7.4, 37°C, recombinant mutant K276T with cytochrome B5


sequence_variant_note: Resolved canonical sequence from UniProtKB Q02928 canonical sequence plus reconstructed S353G substitution on 2026-06-17 and applied mutation signature S353G to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q02928 canonical sequence plus reconstructed S353G substitution on 2026-06-17


proof_lines: pH 7.4, 37°C, recombinant wild-type enzyme with cytochrome B5

proof_lines: pH 7.4, 37°C, recombinant wild-type enzyme, with cytochrome B5


organism: Zea mays

substrate_name: ADP-glucose

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

proof_lines: mutant enzyme K193Q, amylopectin as primer

substrate: ADP-glucose


organism: Zea mays subsp. mays

substrate_name: phytoglycogen

substrate: phytoglycogen


enzyme_display_name: dextransucrase

organism: Acetobacter tropicalis

substrate_name: sucrose

proof_lines: pH 5.5, 37°C, enzyme immobilized on calcium-alginate

enzyme: dextransucrase

substrate: sucrose


organism: Leuconostoc mesenteroides

proof_lines:
pH 5.2, 28°C, recombinant mutant DRN4
pH 5.2, 28°C, recombinant mutant DRN3
pH 5.2, 28°C, recombinant mutant DRN1


proof_lines: pH 5.2, 28°C, recombinant wild-type enzyme

proof_lines: partially purified wild-type enzyme, pH 4.5, 30°C


proof_lines: dextran-QCM-immobilized enzyme, pH 5.2, 25°C

proof_lines: directly QCM-immobilized enzyme, pH 5.2, 25°C

proof_lines: transfer of D-glucose from the non-reducing ends of dextran chains to maltose


organism: Limosilactobacillus reuteri


proof_lines: pH 5.4, 25°C, recombinant wild-type enzyme


organism: Pediococcus pentosaceus


organism: Streptococcus mutans


mutation_signature: truncated protein lacking starch-binding domains 12 truncated protein lacking starch-binding domains 12

mutation_type: truncation


mutation_signature: truncated protein lacking starch binding domain 1 and medium part of starch binding domain 2 truncated protein lacking starch binding domain 1 and medium part o


organism: Arthrobacter sp.

substrate_name: maltotriose

substrate: maltotriose


organism: Escherichia coli

substrate_name: ADPglucose

substrate: ADPglucose


organism: Lathyrus oleraceus

proof_lines:
synthase I, absence of citrate
synthase I, presence of citrate
synthase II, absence of citrate


organism: Solanum tuberosum

proof_lines: granule bound starch synthase I, 5 mg/ml amylopectin


organism: Sorghum bicolor


organism: Trichomonas vaginalis

substrate_name: ADP-alpha-D-glucose

sequence_source: UniProtKB reviewed A2E926/GYS_TRIV3; direct EC 2.4.1.21 + organism lookup; FASTA fetched 2026-06-17

assay_conditions_summary: pH 7.8; cofactor ADP

proof_lines: at pH 7.8, temperature not specified in the publication

substrate: ADP-alpha-D-glucose


organism: Triticum aestivum

assay_conditions_summary: 298.15 K; cofactor ADP


proof_lines: mutant enzyme K193E, amylopectin as primer


proof_lines:
wild-type enzyme, amylopectin as primer
wild-type enzyme, glycogen as primer


proof_lines: mutant enzyme K193R, amylopectin as primer


organism: Brachypodium distachyon

substrate_name: xyloglucan oligosaccharide

proof_lines: donor substrate tamarind xyloglucan, pH not specified in the publication, 30°C

proof_lines: donor substrate hydroxylethyl cellulose, pH not specified in the publication, 30°C

substrate: xyloglucan oligosaccharide


organism: Fragaria vesca

substrate_name: xyloglucan XXLGol

proof_lines:
isoform XTH6, at pH 5.5 and 25°C
isoform XTH9, at pH 5.5 and 25°C

substrate: xyloglucan XXLGol


organism: Populus alba

proof_lines: XXXGXXXG-ol XXXG-ol


organism: Populus tremula x Populus tremuloides


organism: Populus trichocarpa

proof_lines: donor substrate barley beta-glucan, pH not specified in the publication, 30°C


organism: Arabidopsis thaliana


proof_lines: catalytic domain co-expressed with starch-binding domains 23

proof_lines: catalytic domain co-expressed with starch-binding domain 2 and part of starch-binding domain 3


mutation_signature: truncated protein lacking starch-binding domain 1 truncated protein lacking starch-binding domain 1


mutation_signature: truncated protein lacking starch binding domain 1 and large part of starch binding domain 2 truncated protein lacking starch binding domain 1 and large part of


mutation_signature: truncated protein lacking starch binding domain 1 and small part of starch binding domain 2 truncated protein lacking starch binding domain 1 and small part of


organism: Plasmodium falciparum

substrate_name: dodecanoyl-[acyl-carrier protein]

substrate: dodecanoyl-[acyl-carrier protein]


organism: Rattus norvegicus

substrate_name: Unknown

proof_lines: pH 7.0, 22°C, inactivation of the whole reaction of FAS

substrate: Unknown


organism: Spinacia oleracea

substrate_name: malonyl-CoA

assay_conditions_summary: cofactor CoA

proof_lines:
in presence of [acyl-carrier-protein]
synthase II
without [acyl-carrier-protein]

substrate: malonyl-CoA


organism: Streptomyces glaucescens

substrate_name: acetyl-CoA

substrate: acetyl-CoA


organism: Homo sapiens

substrate_name: N-acetyllactosamine

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

proof_lines: mutant enzyme N101Q, at pH 4.5 and 37°C C

proof_lines: mutant enzyme N101Q, in citrate/phosphate buffer, pH 4.5, at 37°C

substrate: N-acetyllactosamine


substrate_name: GDP-beta-L-fucose

proof_lines: wild type enzyme, in citrate/phosphate buffer, pH 4.5, at 37°C

proof_lines: recombinant wild type enzyme, at pH 4.5 and 37°C

substrate: GDP-beta-L-fucose


proof_lines: mutant enzyme N62Q, at pH 4.5 and 37°C C

proof_lines: mutant enzyme N62Q, in citrate/phosphate buffer, pH 4.5, at 37°C


proof_lines:
fucosyltransferase V
pH 7.4, 22°C
LacNAc as substrate


proof_lines: fucosyltransferase V mutant enzyme A349D


organism: Lymnaea stagnalis


organism: Schistosoma mansoni

substrate_name: lacto-N-neotetraose

substrate: lacto-N-neotetraose


organism: Actinidia deliciosa

proof_lines: reduced xyloglucan-derived heptasaccharide XXXG-ol, derived from kiwifruit xyloglucan


substrate_name: palmitic acid

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02928 (UniProtKB reviewed (Swiss-Prot); https://rest.uniprot.org/uniprotkb/Q02928.json; accessed 2026-06-17) and applied mutation signature S353G to reconstruct the assayed variant sequence.

substrate: palmitic acid


substrate_name: lauric acid

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q02928 (UniProtKB reviewed (Swiss-Prot); https://rest.uniprot.org/uniprotkb/Q02928.json; accessed 2026-06-17) and applied mutation signature K276T to reconstruct the assayed variant sequence.

substrate: lauric acid


substrate_name: myristic acid

sequence_source: UniProtKB:Q02928 (UniProtKB reviewed (Swiss-Prot); https://rest.uniprot.org/uniprotkb/Q02928.json; accessed 2026-06-17)

proof_lines: pH 7.4, 37°C, recombinant mutant S353G with cytochrome B5

substrate: myristic acid


sequence_source: UniProtKB:P08516 (UniProtKB reviewed (Swiss-Prot); https://rest.uniprot.org/uniprotkb/P08516.json; accessed 2026-06-17)


sequence_source: UniProtKB:P20817 (UniProtKB reviewed (Swiss-Prot); https://rest.uniprot.org/uniprotkb/P20817.json; accessed 2026-06-17)


sequence_source: UniProtKB:P20816 (UniProtKB reviewed (Swiss-Prot); https://rest.uniprot.org/uniprotkb/P20816.json; accessed 2026-06-17)


sequence_source: UniProtKB:P24464 (UniProtKB reviewed (Swiss-Prot); https://rest.uniprot.org/uniprotkb/P24464.json; accessed 2026-06-17)


organism: Starmerella bombicola

substrate_name: Oleate; O2; NADPH; H+

sequence_source: UniProtKB:B8QHP1 (UniProtKB reviewed (Swiss-Prot); https://rest.uniprot.org/uniprotkb/B8QHP1.json; accessed 2026-06-17)

assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+

substrate: Oleate; O2; NADPH; H+


organism: Bos taurus

sequence_source: UniProtKB:Q9BDR5 (UniProtKB unreviewed (TrEMBL); https://rest.uniprot.org/uniprotkb/Q9BDR5.json; accessed 2026-06-17)


organism: Gallus gallus

sequence_source: UniProtKB:Q9IAX2 (UniProtKB reviewed (Swiss-Prot); https://rest.uniprot.org/uniprotkb/Q9IAX2.json; accessed 2026-06-17)


sequence_source: UniProtKB:O42411 (UniProtKB reviewed (Swiss-Prot); https://rest.uniprot.org/uniprotkb/O42411.json; accessed 2026-06-17)


substrate_name: L-thyroxine

sequence_source: UniProtKB:Q92813 (UniProtKB reviewed (Swiss-Prot); https://rest.uniprot.org/uniprotkb/Q92813.json; accessed 2026-06-17)

proof_lines: wild-type enzyme, in presence of 20 mM dithiothreitol

substrate: L-thyroxine


substrate_name: thyroxine

substrate: thyroxine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q92813 (UniProtKB reviewed (Swiss-Prot); https://rest.uniprot.org/uniprotkb/Q92813.json; accessed 2026-06-17) and applied mutation signature A131S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A131S, in presence of 20 mM dithiothreitol


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q92813 (UniProtKB reviewed (Swiss-Prot); https://rest.uniprot.org/uniprotkb/Q92813.json; accessed 2026-06-17) and applied mutation signature A131C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme SeC133C/A131C, in presence of 20 mM dithiothreitol

proof_lines: mutant enzyme A131C, in presence of 20 mM dithiothreitol


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

proof_lines: mutant enzyme SeC133C, in presence of 20 mM dithiothreitol


substrate_name: Reduced acceptor; L-Thyroxine

sequence_variant_note: Resolved canonical sequence from UniProtKB Q92813 canonical sequence plus selected source mutation P135S and applied mutation signature P135S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thyroxine 5'-deiodinase(Enzyme) mutant P135S

substrate: Reduced acceptor; L-Thyroxine


sequence_variant_note: Resolved canonical sequence from UniProtKB P49895 canonical sequence plus selected source mutation E214A and applied mutation signature E214A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thyroxine 5'-deiodinase(Enzyme) mutant E214A


sequence_variant_note: Resolved canonical sequence from UniProtKB P49895 canonical sequence plus selected source mutation E156D and applied mutation signature E156D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thyroxine 5'-deiodinase(Enzyme) mutant E156D


sequence_source: UniProtKB P49895 canonical sequence retrieved 2026-06-17

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


organism: Mus musculus

sequence_source: UniProtKB Q9Z1Y9 canonical sequence retrieved 2026-06-17


sequence_source: UniProtKB Q61153 canonical sequence retrieved 2026-06-17


substrate_name: 3,3',5-triiodo-L-thyronine sulfate

sequence_variant_note: Resolved canonical sequence from UniProtKB P24389 canonical sequence plus selected source mutation S101A and applied mutation signature S101A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S101A, duplicate determination give the values: 0.0022 mM and 0.0032 mM

proof_lines: mutant enzyme S101A, duplicate determination give the values: 0.0022 mM and 3.2 mM

substrate: 3,3',5-triiodo-L-thyronine sulfate


sequence_variant_note: Resolved canonical sequence from UniProtKB P24389 canonical sequence plus selected source mutation N94Q/N203Q and applied mutation signature N94Q/N203Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P24389 canonical sequence plus selected source mutation G2A and applied mutation signature G2A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme G2A, duplicate determination give the values: 0.0015 mM and 0.0024 mM


sequence_variant_note: Resolved canonical sequence from UniProtKB P24389 canonical sequence plus selected source mutation S176A and applied mutation signature S176A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S176A, duplicate determination give the values: 0.002 mM and 0.0024 mM

proof_lines: mutant enzyme S176A, duplicate determination give the values: 0.0024 mM and 0.0024 mM


sequence_variant_note: Resolved canonical sequence from UniProtKB P24389 canonical sequence plus selected source mutation N94Q and applied mutation signature N94Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P24389 canonical sequence checked 2026-06-17; row-specific variant unresolved

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

proof_lines: mutant enzymes, in which selenocysteine residues in the core catalytic center is replaced by cysteine


sequence_variant_note: Resolved canonical sequence from UniProtKB P24389 canonical sequence plus selected source mutation N203Q and applied mutation signature N203Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P24389 canonical sequence retrieved 2026-06-17


organism: Sus scrofa

sequence_source: UniProtKB Q6QN13 canonical sequence retrieved 2026-06-17


organism: Rhizopus arrhizus

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

proof_lines:
isozyme RPG15, pH 4.0, 30°C
isozyme RPG16, pH 4.0, 30°C


proof_lines:
pH 7.4, 37°C, isozyme Dio2
DTT 10 mM
type I, liver


organism: Rattus sp.

proof_lines:
in hypothyroid medium
type I
DTT 20 mM


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

proof_lines: type I mutant, exchange of selenocysteine by cysteine


proof_lines:
DTT 10 mM
type I, liver


organism: Streptomyces coelicolor


organism: Trichormus variabilis

proof_lines:
ping-pong mechanism
sequential mechanism
with respect to malonyl-CoA


organism: Cuphea lanceolata

substrate_name: decanoyl-[acyl-carrier protein]

substrate: decanoyl-[acyl-carrier protein]


organism: Escherichia coli

substrate_name: lauroyl-ACP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A953 canonical ecFabB reconstructed with PMID:22017312 mutagenesis evidence and applied mutation signature K63Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 298.15 K; cofactor CoA

proof_lines: K63Q mutant protein, acceptor malonyl-CoA, 0.2 mM malonyl-CoA, pH 6.5, 25°C

substrate: lauroyl-ACP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A953 canonical ecFabB reconstructed with PMID:22017312 mutagenesis evidence and applied mutation signature K151Q to reconstruct the assayed variant sequence.

proof_lines: K151Q mutant protein, acceptor malonyl-CoA, 0.2 mM malonyl-CoA, pH 6.5, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A953 canonical ecFabB reconstructed with PMID:22017312 mutagenesis evidence and applied mutation signature R66Q to reconstruct the assayed variant sequence.

proof_lines: R66Q mutant protein, acceptor malonyl-CoA, 0.2 mM malonyl-CoA, pH 6.5, 25°C


sequence_source: UniProtKB:P0A953 reviewed ecFabB supported by PMID:22017312

proof_lines: wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C

proof_lines: wild type protein, acceptor malonyl-ACP, 0.01 mM malonyl-ACP, pH 6.5, 25°C

proof_lines: wild type protein, acceptor malonyl-CoA, 0.2 mM malonyl-CoA, pH 6.5, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A953 canonical ecFabB reconstructed with PMID:22017312 mutagenesis evidence and applied mutation signature R62Q to reconstruct the assayed variant sequence.

proof_lines: R62Q mutant protein, acceptor malonyl-CoA, 0.2 mM malonyl-CoA, pH 6.5, 25°C


substrate_name: Acetyl-[acyl-carrier protein]; Malonyl-[acyl-carrier protein]

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: acyl-carrier-protein, fatty acyl transfer between tetradecanoyl-CoA and acyl-carrier-protein


organism: Helicobacter pylori

substrate_name: hexanoyl-[acyl-carrier protein]

proof_lines: pH and temperature not specified in the publication

substrate: hexanoyl-[acyl-carrier protein]


substrate_name: arachidonic acid

substrate: arachidonic acid


substrate_name: dodecanoate

smiles: CCCCCCCCCCCC(=O)[O-]

substrate: dodecanoate


enzyme_display_name: cathepsin E

substrate_name: hemoglobin

enzyme: cathepsin E

substrate: hemoglobin


substrate_name: laurate

substrate: laurate


substrate_name: dodecanoic acid

proof_lines: kcat is 42 min(-1) with dodecanoic acid as substrate. kcat is 50 min(-1) with tetradecanoic acid as substrate. kcat is 10 min(-1) with hexadecanoic acid as substrate. kcat is 0.4 min(-1) with (9Z)-octadecenoic acid as substrate. kcat is 0.4

substrate: dodecanoic acid


proof_lines: Vmax is nearly the same for myristic acid and for lauric acid and reduced about 30% for palmitic acid.


substrate_name: hexadecanoic acid

proof_lines: kcat is 0.088 min(-1) with menaquinone-4 (MK-4) as substrate (PubMed:24138531). kcat is 1.8 min(-1) with hexadecanoic acid as substrate. kcat is 1.0 min(-1) with (9Z)-octadecenoic acid as substrate. kcat is 0.54 min(-1) with (5Z,8Z,11Z,14Z)

substrate: hexadecanoic acid


organism: Rattus norvegicus

proof_lines: kcat is 649 min-1 for dodecanoate. kcat is 230 min-1 for tetradecanoate. kcat is 60 min-1 for hexadecanoate. kcat is 1.4 min-1 for (9Z)-octadecenoate. kcat is 6 min-1 for (5Z,8Z,11Z,14Z)-eicosatetraenoate.


organism: Homo sapiens

substrate_name: myristic acid; lauric acid; palmitic acid

sequence_source: UniProtKB Q6ZWL3 reviewed Swiss-Prot; direct CYP4V2/Homo sapiens lookup shows EC 1.14.14.79 and 1.14.14.80.


organism: Cavia porcellus


organism: Crocodylus porosus

proof_lines: type I-like activity in liver microsomes

proof_lines: type I-like activity in kidney microsomes


organism: Felis catus

substrate_name: reverse triiodothyronine; sulfated reverse triiodothyronine

sequence_source: UniProtKB Q6V915 reviewed Swiss-Prot; direct EC 1.21.99.4/Felis catus lookup returns cat Type I iodothyronine deiodinase.


sequence_source: UniProtKB O42411 reviewed Swiss-Prot; direct Gallus gallus EC query returns DIO1 and DIO2, and the selected source note says type I.

proof_lines:
DTT 10 mM
type I,l iver


sequence_source: UniProtKB Q92813 reviewed Swiss-Prot; source notes specify wild type type 2 iodothyronine deiodinase.

assay_conditions_summary: pH 7.5; 310.15 K; buffer Tris-EDTA

proof_lines: wild type type 2 iodothyronine deiodinase, with 20 mM dithiothreitol as cofactor, in Tris-EDTA buffer (pH 7.5), at 37°C

proof_lines: wild type type 2 iodothyronine deiodinase, with 20 mM glutathione as cofactor, in Tris-EDTA buffer (pH 7.5), at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q92813 reviewed Swiss-Prot plus direct P135S reconstruction from the selected mutation note. and applied mutation signature P135S to reconstruct the assayed variant sequence.

proof_lines: mutant P135S type 2 iodothyronine deiodinase, with 20 mM glutathione as cofactor, in Tris-EDTA buffer (pH 7.5), at 37°C

proof_lines: mutant P135S type 2 iodothyronine deiodinase, with 20 mM dithiothreitol as cofactor, in Tris-EDTA buffer (pH 7.5), at 37°C


sequence_source: UniProtKB Q61153 reviewed Swiss-Prot; direct Mus musculus EC query returns DIO1 and DIO2, and the selected source note says type I.

proof_lines:
DTT 10 mM
type I, liver


organism: Oncorhynchus mykiss


organism: Ovis aries


organism: Rhodothermus marinus

substrate_name: digalacturonic acid

sequence_source: UniProtKB:D0MEP1 direct JSON lookup on 2026-06-17

substrate: digalacturonic acid


substrate_name: polygalacturonic acid

substrate: polygalacturonic acid


substrate_name: trigalacturonic acid

substrate: trigalacturonic acid


organism: Thermotoga maritima

sequence_source: UniProtKB:Q9WYR8 direct JSON lookup on 2026-06-17


organism: Thermoactinomyces vulgaris

substrate_name: benzyloxycarbonyl-alanyl-alanyl-leucine

sequence_source: UniProtKB:P29068 direct JSON lookup on 2026-06-17; canonical sequence retained as context only

substrate: benzyloxycarbonyl-alanyl-alanyl-leucine


proof_lines: mutant enzyme A243G, pH and temperature not specified in the publication


substrate_name: N-benzyloxycarbonyl-Ala-Ala-Leu

substrate: N-benzyloxycarbonyl-Ala-Ala-Leu


substrate_name: N-benzyloxycarbonyl-Ala-Ala-Glu

substrate: N-benzyloxycarbonyl-Ala-Ala-Glu


substrate_name: DED(EDANS)KPILFFRLGK(Dabcyl)E; H2O

sequence_source: UniProtKB:P14091 direct JSON lookup on 2026-06-17

substrate: DED(EDANS)KPILFFRLGK(Dabcyl)E; H2O


enzyme_display_name: glycerol dehydratase

organism: Klebsiella pneumoniae

substrate_name: glycerol

sequence_source: UniProtKB REST FASTA accession A8CIU9; selected OED source snapshot links A8CIU9 to PMID 22042303.

smiles: OCC(O)CO

enzyme: glycerol dehydratase

substrate: glycerol


proof_lines: mutant enzyme KpG525, at pH 6.0 and 37°C


sequence_source: UniProtKB REST FASTA accession A8CIU9; selected BRENDA source notes label this row wild type.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA accession Q59476 with T200S reconstructed after direct residue check: canonical residue 200 is T. and applied mutation signature T200S to reconstruct the assayed variant sequence.


proof_lines: 37°C, pH 7.0, linked complex of the fusion protein of alpha- and beta-subunits and the gamma subunit


sequence_source: UniProtKB REST FASTA accession A8CIU9; selected BRENDA source snapshot lists A8CIU9 for 1,2-propanediol.


sequence_source: UniProtKB REST FASTA accession Q59475; selected BRENDA/SKiD snapshots list Q59475 for the same organism.

proof_lines:
pH 8.0, 37°C
Raw SKiD Env: Temp=37°C, pH=8


enzyme_display_name: aminocyclopropanecarboxylate oxidase

organism: Solanum lycopersicum

proof_lines: pH 7.2, 25°C, 20 mM ascorbate, recombinant enzyme

proof_lines: pH 7.2, 25°C, 2 mM ascorbate, recombinant enzyme

enzyme: aminocyclopropanecarboxylate oxidase


organism: Unknown


organism: Agaricus bisporus

sequence_source: UniProtKB REST direct check for accession H9ZYN5 on 2026-06-17.


organism: Malus domestica

sequence_source: UniProtKB REST direct check for accession Q00985 on 2026-06-17.


substrate_name: 1-aminocyclopropane-1-carboxylic acid

sequence_source: UniProtKB REST direct check for accession O48882 on 2026-06-17.

substrate: 1-aminocyclopropane-1-carboxylic acid


organism: Persea americana

sequence_source: UniProtKB:P19464 direct REST lookup 2026-06-17


sequence_source: UniProtKB:P05116 direct REST lookup 2026-06-17

proof_lines: recombinant isozyme ACO1, in presence of 3mM L-ascorbate and 10 mM HCO3-, pH 7.2, 29°C

proof_lines: recombinant isozyme ACO1, in presence of 3mM L-ascorbate, pH 7.2, 29°C


sequence_source: UniProtKB:P24157 direct REST lookup 2026-06-17


sequence_source: UniProtKB:P07920 direct REST lookup 2026-06-17


sequence_source: UniProtKB:Q6P1A2 direct REST lookup 2026-06-17

assay_conditions_summary: pH 6; 310.15 K; cofactor CoA

proof_lines: Vmax: 12.4 pmol/min/microgram protein for arachidonoyl-CoA


substrate_name: Unknown

sequence_source: UniProtKB:P16228 direct REST lookup 2026-06-17

proof_lines: non-competitive competitive

substrate: Unknown


enzyme_display_name: mandelamide amidase

organism: Pseudomonas putida

substrate_name: (R,S)-methyl mandelate

sequence_source: UniProtKB:Q84DC4 direct REST lookup 2026-06-17

enzyme: mandelamide amidase

substrate: (R,S)-methyl mandelate


substrate_name: (S)-mandelamide

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q84DC4 direct REST lookup 2026-06-17 and applied mutation signature S181A to reconstruct the assayed variant sequence.

substrate: (S)-mandelamide


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q84DC4 direct REST lookup 2026-06-17 and applied mutation signature S180A 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:Q84DC4 direct REST lookup 2026-06-17 and applied mutation signature F433L to reconstruct the assayed variant sequence.


substrate_name: (R)-mandelamide (at 30 degrees Celsius, pH 7.8)


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 reviewed canonical sequence; row-specific mutant sequence reconstructed from validated mutation signature and applied mutation signature K158E to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant K158E, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 reviewed canonical sequence; row-specific mutant sequence reconstructed from validated mutation signature and applied mutation signature R299K to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant R299K, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 reviewed canonical sequence; row-specific mutant sequence reconstructed from validated mutation signature and applied mutation signature K158Q to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant K158Q, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 reviewed canonical sequence; row-specific mutant sequence reconstructed from validated mutation signature and applied mutation signature F300Y to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant F300Y, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 reviewed canonical sequence; row-specific mutant sequence reconstructed from validated mutation signature and applied mutation signature Y251F to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant Y251F, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 reviewed canonical sequence; row-specific mutant sequence reconstructed from validated mutation signature and applied mutation signature K158Q/R175E to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant K158Q/R175E, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 reviewed canonical sequence; row-specific mutant sequence reconstructed from validated mutation signature and applied mutation signature Q188N to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant Q188N, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 reviewed canonical sequence; row-specific mutant sequence reconstructed from validated mutation signature and applied mutation signature E301L to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant E301L, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 reviewed canonical sequence; row-specific mutant sequence reconstructed from validated mutation signature and applied mutation signature K158R to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant K158R, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 reviewed canonical sequence; row-specific mutant sequence reconstructed from validated mutation signature and applied mutation signature R244K/S246A to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant R244K/S246A, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 reviewed canonical sequence; row-specific mutant sequence reconstructed from validated mutation signature and applied mutation signature K158Q/R175Q to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant K158Q/R175Q, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 reviewed canonical sequence; row-specific mutant sequence reconstructed from validated mutation signature and applied mutation signature R175E/S246A to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant R175E/S246A, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 reviewed canonical sequence; row-specific mutant sequence reconstructed from validated mutation signature and applied mutation signature C28A to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant C28A, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 reviewed canonical sequence; row-specific mutant sequence reconstructed from validated mutation signature and applied mutation signature R175K to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant R175K, pH 7.2, 20°C


sequence_source: UniProtKB Q00985 reviewed canonical sequence

proof_lines: recombinant His-tagged wild-type enzyme, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 reviewed canonical sequence; row-specific mutant sequence reconstructed from validated mutation signature and applied mutation signature S246A/R244K/T157A to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant S246A/R244K/T157A , pH 7.2, 20°C


organism: Callistephus chinensis

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

proof_lines:
pH 7.0, 25°C, in vitro
pH 7.0, 25°C, in vivo


organism: Cucumis melo


organism: Cucurbita maxima

proof_lines: under atmospheric conditions, pH 7.2, 30°C


proof_lines:
recombinant enzyme, pH 7.0, 30°C
pH 7.0, 30°C
pH7.0, 30°C


substrate_name: ascorbate

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

substrate: ascorbate


organism: plant


organism: Pyrus communis


proof_lines: recombinant wild-type enzyme, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C


proof_lines: recombinant mutant H56Q, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C


proof_lines: recombinant mutant D179E, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C


proof_lines: recombinant mutant H177E, in presence of 5 mM L-ascorbate and 10 mM HCO3-, pH 7.2, 28°C


organism: Homo sapiens

substrate_name: myristoyl-[acyl-carrier protein]

substrate: myristoyl-[acyl-carrier protein]


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 8.5; 298.15 K; cofactor CoA

proof_lines: donor palmitoyl-ACP, 0.012 mM palmitoyl-ACP, pH 8.5, 25°C

proof_lines: acceptor malonyl-ACP, 0.01 mM malonyl-ACP, pH 8.5, 25°C


organism: Streptococcus oralis

substrate_name: sucrose

substrate: sucrose


enzyme_display_name: amidophosphoribosyltransferase

organism: Escherichia coli

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

enzyme: amidophosphoribosyltransferase

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


substrate_name: L-glutamine

proof_lines: R73H mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity

proof_lines: R73H mutant enzyme, aminotransferase activity

substrate: L-glutamine


proof_lines: wild-type enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity

proof_lines: wild-type enzyme, aminotransferase activity


proof_lines: G102A mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity

proof_lines: G102A mutant enzyme, aminotransferase activity


proof_lines: N101G mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity

proof_lines: N101G mutant enzyme, aminotransferase activity


proof_lines: R73L mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity

proof_lines: R73L mutant enzyme, aminotransferase activity


proof_lines: D127A mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity

proof_lines: D127A mutant enzyme, aminotransferase activity


proof_lines: N101D mutant enzyme, 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutaminase activity

proof_lines: N101D mutant enzyme, aminotransferase activity


organism: Glycine max


assay_conditions_summary: buffer Tris

proof_lines:
adenocarcinoma 755
in Tris buffer


organism: Mus musculus


organism: Rattus norvegicus


organism: Weissella cibaria


organism: Aquifex aeolicus


organism: Artemia sp.

proof_lines:
cosubstrate NH3
cosubstrate glutamine


organism: Bacillus subtilis


organism: Bos taurus


organism: Columba livia


proof_lines: 5-phospho-alpha-D-ribose 1-diphosphate-dependent glutamine hydrolysis

proof_lines: 5-phospho-alpha-D-ribose 1-diphosphate-independent glutamine hydrolysis


organism: Escherichia coli (strain K12)

substrate_name: 5-phospho-alpha-D-ribose (at pH 7.8)

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

substrate: 5-phospho-alpha-D-ribose (at pH 7.8)


substrate_name: QA (at 0.1 mM PRPP)

substrate: QA (at 0.1 mM PRPP)


enzyme_display_name: methenyltetrahydrofolate cyclohydrolase

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24186 and applied mutation signature R191E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADP+

column_label: Table 3 (Kinetic Properties of the Dehydrogenase and Cyclohydrolase of FolD), Cyclohydrolase section, enzyme row 'R191E', substrate column '5,10-CH+-THF'; column 'Km (uM)' = 28 +/- 9; column 'Vmax (umol min^-1 mg^-1)' = 55 +/- 8; column 'kcat (min^-1)' = 3446 +/- 487; column 'kcat/Km (min^-1 uM^-1)' = 124.

raw_value_unit_evidence: Table 3, Cyclohydrolase section, enzyme row R191E, substrate 5,10-CH+-THF: Km = 28 +/- 9 uM; kcat = 3446 +/- 487 min^-1; printed kcat/Km = 124 min^-1 uM^-1.

row_label: Table 3, Cyclohydrolase section, enzyme row R191E, substrate column value 5,10-CH+-THF

table_label: Table 3: Kinetic Properties of the Dehydrogenase and Cyclohydrolase of FolD (Biochemistry 2015, 54(22):3504-3513)

enzyme: methenyltetrahydrofolate cyclohydrolase


sequence_variant_note: Resolved canonical sequence from >sp|P24186|FOLD_ECOLI Bifunctional protein FolD OS=Escherichia coli (strain K12) OX=83333 GN=folD PE=1 SV=4 via UniProt REST FASTA on 2026-06-17 and applied mutation signature C58Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from >sp|P24186|FOLD_ECOLI Bifunctional protein FolD OS=Escherichia coli (strain K12) OX=83333 GN=folD PE=1 SV=4 via UniProt REST FASTA on 2026-06-17 and applied mutation signature R191E to reconstruct the assayed variant sequence.


sequence_source: >sp|P24186|FOLD_ECOLI Bifunctional protein FolD OS=Escherichia coli (strain K12) OX=83333 GN=folD PE=1 SV=4 via UniProt REST FASTA on 2026-06-17

column_label: Table 3 (Kinetic Properties of the Dehydrogenase and Cyclohydrolase of FolD), Cyclohydrolase section, enzyme row 'WT', substrate column '5,10-CH+-THF'; column 'Km (uM)' = 26 +/- 7; column 'Vmax (umol min^-1 mg^-1)' = 39 +/- 7; column 'kcat (min^-1)' = 2453 +/- 329; column 'kcat/Km (min^-1 uM^-1)' = 95.

raw_value_unit_evidence: Table 3, Cyclohydrolase section, enzyme row WT, substrate 5,10-CH+-THF: Km = 26 +/- 7 uM; kcat = 2453 +/- 329 min^-1; printed kcat/Km = 95 min^-1 uM^-1.

row_label: Table 3, Cyclohydrolase section, enzyme row WT, substrate column value 5,10-CH+-THF


sequence_variant_note: Resolved canonical sequence from >sp|P24186|FOLD_ECOLI Bifunctional protein FolD OS=Escherichia coli (strain K12) OX=83333 GN=folD PE=1 SV=4 via UniProt REST FASTA on 2026-06-17 and applied mutation signature D121A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from >sp|P24186|FOLD_ECOLI Bifunctional protein FolD OS=Escherichia coli (strain K12) OX=83333 GN=folD PE=1 SV=4 via UniProt REST FASTA on 2026-06-17 and applied mutation signature G122D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24186 and applied mutation signature G122D to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Properties of the Dehydrogenase and Cyclohydrolase of FolD), Cyclohydrolase section, enzyme row 'G122D', substrate column '5,10-CH+-THF'; column 'Km (uM)' = 4.5 +/- 1.5; column 'Vmax (umol min^-1 mg^-1)' = 0.025; column 'kcat (min^-1)' = 1.5; column 'kcat/Km (min^-1 uM^-1)' = 0.345.

raw_value_unit_evidence: Table 3, Cyclohydrolase section, enzyme row G122D, substrate 5,10-CH+-THF: Km = 4.5 +/- 1.5 uM; kcat = 1.5 min^-1; printed kcat/Km = 0.345 min^-1 uM^-1.

row_label: Table 3, Cyclohydrolase section, enzyme row G122D, substrate column value 5,10-CH+-THF


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24186 and applied mutation signature D121A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Properties of the Dehydrogenase and Cyclohydrolase of FolD), Cyclohydrolase section, enzyme row 'D121A', substrate column '5,10-CH+-THF'; column 'Km (uM)' = 15 +/- 8; column 'Vmax (umol min^-1 mg^-1)' = 0.011; column 'kcat (min^-1)' = 0.6; column 'kcat/Km (min^-1 uM^-1)' = 0.045.

raw_value_unit_evidence: Table 3, Cyclohydrolase section, enzyme row D121A, substrate 5,10-CH+-THF: Km = 15 +/- 8 uM; kcat = 0.6 min^-1; printed kcat/Km = 0.045 min^-1 uM^-1.

row_label: Table 3, Cyclohydrolase section, enzyme row D121A, substrate column value 5,10-CH+-THF


sequence_variant_note: Resolved canonical sequence from >sp|P11586|C1TC_HUMAN C-1-tetrahydrofolate synthase, cytoplasmic OS=Homo sapiens OX=9606 GN=MTHFD1 PE=1 SV=4 via UniProt REST FASTA on 2026-06-17 and applied mutation signature S49Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from >sp|P11586|C1TC_HUMAN C-1-tetrahydrofolate synthase, cytoplasmic OS=Homo sapiens OX=9606 GN=MTHFD1 PE=1 SV=4 via UniProt REST FASTA on 2026-06-17 and applied mutation signature S49A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from >sp|P11586|C1TC_HUMAN C-1-tetrahydrofolate synthase, cytoplasmic OS=Homo sapiens OX=9606 GN=MTHFD1 PE=1 SV=4 via UniProt REST FASTA on 2026-06-17 and applied mutation signature Y52A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from >sp|P11586|C1TC_HUMAN C-1-tetrahydrofolate synthase, cytoplasmic OS=Homo sapiens OX=9606 GN=MTHFD1 PE=1 SV=4 via UniProt REST FASTA on 2026-06-17 and applied mutation signature Y52F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from >sp|P11586|C1TC_HUMAN C-1-tetrahydrofolate synthase, cytoplasmic OS=Homo sapiens OX=9606 GN=MTHFD1 PE=1 SV=4 via UniProt REST FASTA on 2026-06-17 and applied mutation signature C147Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from >sp|P11586|C1TC_HUMAN C-1-tetrahydrofolate synthase, cytoplasmic OS=Homo sapiens OX=9606 GN=MTHFD1 PE=1 SV=4 via UniProt REST FASTA on 2026-06-17 and applied mutation signature C147A/T148A to reconstruct the assayed variant sequence.


organism: Malus domestica

sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 FASTA; variant reconstructed from selected mutation signature and checked against canonical residue positions and applied mutation signature F187Y to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant F187Y, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 FASTA; variant reconstructed from selected mutation signature and checked against canonical residue positions and applied mutation signature K158R/R175Q to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant K158R/R175Q, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 FASTA; variant reconstructed from selected mutation signature and checked against canonical residue positions and applied mutation signature R175G to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant R175G, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 FASTA; variant reconstructed from selected mutation signature and checked against canonical residue positions and applied mutation signature K158L to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant K158L, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 FASTA; variant reconstructed from selected mutation signature and checked against canonical residue positions and applied mutation signature R175E/T157A to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant R175E/T157A, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 FASTA; variant reconstructed from selected mutation signature and checked against canonical residue positions and applied mutation signature F300Q to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant F300Q, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 FASTA; variant reconstructed from selected mutation signature and checked against canonical residue positions and applied mutation signature R299H to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant R299H, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 FASTA; variant reconstructed from selected mutation signature and checked against canonical residue positions and applied mutation signature R175A to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant R175A, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 FASTA; variant reconstructed from selected mutation signature and checked against canonical residue positions and applied mutation signature W203F to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant W203F, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 FASTA; variant reconstructed from selected mutation signature and checked against canonical residue positions and applied mutation signature P298A to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant P298A, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 FASTA; variant reconstructed from selected mutation signature and checked against canonical residue positions and applied mutation signature R175H to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant R175H, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 FASTA; variant reconstructed from selected mutation signature and checked against canonical residue positions and applied mutation signature N216F to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant N216F, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 FASTA; variant reconstructed from selected mutation signature and checked against canonical residue positions and applied mutation signature R299L to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant R299L, pH 7.2, 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q00985 FASTA; variant reconstructed from selected mutation signature and checked against canonical residue positions and applied mutation signature R175E to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant R175E, pH 7.2, 20°C


organism: Persea americana

substrate_name: L-Ascorbate

sequence_source: UniProtKB P19464 FASTA; canonical wild-type sequence from direct accession lookup

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

substrate: L-Ascorbate


organism: Unknown

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


organism: Pseudomonas putida

sequence_source: UniProtKB:Q84DC4 direct REST lookup

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q84DC4 direct REST lookup and applied mutation signature F433A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q84DC4 direct REST lookup and applied mutation signature F150W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q84DC4 direct REST lookup and applied mutation signature F433L to reconstruct the assayed variant sequence.


proof_lines: recombinant wild-type enzyme, pH 7.8, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q84DC4 direct REST lookup and applied mutation signature F433W to reconstruct the assayed variant sequence.


organism: Clostridium perfringens

proof_lines: pH 7.6, temperature not specified in the publication


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from reconstructed_from_UniProtKB:P11586 and applied mutation signature K56R 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.

proof_lines:
30°C, recombinant loop5G mutant
30°C, recombinant loop3G mutant


proof_lines:
30°C, recombinant wild-type enzyme
wild-type DC301


sequence_variant_note: Resolved canonical sequence from reconstructed_from_UniProtKB:P11586 and applied mutation signature R250A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_UniProtKB:P11586 and applied mutation signature Y240A to reconstruct the assayed variant sequence.


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


organism: Leishmania major

substrate_name: 5,6,7,8-Tetrahydrofolate; One carbon pool

proof_lines: SABIO-RK modifier species: Enzyme mutant dhch1-/pXNG4-DHCH1

proof_lines: SABIO-RK modifier species: Enzyme mutant ftl−/+pXG-FTL


substrate_name: One carbon pool; 5,6,7,8-Tetrahydrofolate


proof_lines: SABIO-RK modifier species: Enzyme mutant ftl- (BS)

proof_lines: SABIO-RK modifier species: Enzyme mutant ftl- (SB)

substrate: One carbon pool; 5,6,7,8-Tetrahydrofolate


proof_lines:
with NPP1, pH 7.3, 37°C
, pH 7.3, 37°C


organism: Photobacterium phosphoreum


substrate_name: H2O; 5,10-Methenyltetrahydrofolate

substrate: H2O; 5,10-Methenyltetrahydrofolate


organism: Pseudomonas aeruginosa

proof_lines:
at pH 7.9 and 22°C
Raw SKiD Env: Temp=22°C, pH=7.9


organism: Citrobacter freundii


organism: Klebsiella pneumoniae

smiles: CCCC(O)CO


enzyme_display_name: acetylglutamate kinase

organism: Corynebacterium glutamicum

substrate_name: N-acetyl-L-glutamate

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

proof_lines: mutant E19R, pH 8.0, 37°C, with 1 mM L-arginine

proof_lines: mutant E19R, pH and temperature not specified in the publication, with 1 mM L-arginine

enzyme: acetylglutamate kinase

substrate: N-acetyl-L-glutamate


proof_lines: mutant H268N/H26E/E19R, pH 8.0, 37°C, with 1 mM L-arginine


proof_lines: wild-type, pH 8.0, 37°C, with 1 mM L-arginine

proof_lines: wild-type, pH and temperature not specified in the publication, with 1 mM L-arginine


proof_lines: mutant H268N/H26E, pH 8.0, 37°C, with 1 mM L-arginine


proof_lines: mutant H26E, pH 8.0, 37°C, with 1 mM L-arginine


proof_lines: mutant W23A, pH and temperature not specified in the publication, with 1 mM L-arginine


proof_lines: mutant G287D, pH and temperature not specified in the publication, with 1 mM L-arginine


proof_lines: mutant E281A, pH and temperature not specified in the publication, with 1 mM L-arginine


proof_lines: mutant DELTA25, pH and temperature not specified in the publication, with 1 mM L-arginine


proof_lines: mutant R209K, pH and temperature not specified in the publication, with 1 mM L-arginine


proof_lines: mutant H268A, pH and temperature not specified in the publication, with 1 mM L-arginine


proof_lines: mutant H26A, pH and temperature not specified in the publication, with 1 mM L-arginine


enzyme_display_name: uridine phosphorylase

organism: Acholeplasma laidlawii

substrate_name: uridine

sequence_source: UniProtKB A9NG34 from direct EC 2.4.2.3 + Acholeplasma laidlawii lookup; paper identity context from PMID 6619095.

enzyme: uridine phosphorylase

substrate: uridine


organism: Dictyostelium discoideum

substrate_name: Uracil

substrate: Uracil


organism: Escherichia coli

proof_lines:
addition of uracil
addition of uridine


organism: Haemophilus influenzae

sequence_source: UniProtKB P43770 from direct EC 2.4.2.3 + Haemophilus influenzae lookup; paper identity context from PMID 5316215.


substrate_name: ribose 1-phosphate

proof_lines: in 50 mM Tris, 1 mM EDTA, pH 7.4, at 37°C

substrate: ribose 1-phosphate


organism: Hymenolepis diminuta

substrate_name: ribose 1-phosphate; uridine; Uracil; phosphate


organism: Klebsiella aerogenes

proof_lines:
at 60°C
at 40°C


organism: Lacticaseibacillus casei

substrate_name: 5-methyluridine; uridine

substrate: 5-methyluridine; uridine


organism: Mus musculus

substrate_name: phosphate; deoxyuridine; uridine; thymidine; 5'-deoxy-5-fluorouridine


organism: Rattus norvegicus

substrate_name: alpha-D-ribose-1-phosphate; 5-fluorouracil; Uracil; uridine; ribose 1-phosphate

proof_lines: cosubstrate: alpha-D-ribose-1-phosphate, enzyme from colon tumor

proof_lines: cosubstrate: 5-fluorouracil, enzyme from colon tumor


enzyme_display_name: nucleoside deoxyribosyltransferase

organism: Lactobacillus helveticus

substrate_name: Adenine; Deoxyinosine; Deoxyadenosine; Hypoxanthine; deoxycytidine; cytosine

proof_lines:
reaction with cytosine
reaction with deoxycytidine
reaction with deoxyguanosine

enzyme: nucleoside deoxyribosyltransferase


organism: Lactobacillus leichmannii


substrate_name: guanine; thymidine; cytosine; deoxyadenosine; deoxyguanosine; adenine; deoxyinosine; deoxycytidine; adenosine; thymine

proof_lines:
reactioin with deoxyinosine
reaction with cytosine
reaction with thymidine


substrate_name: dGMP

substrate: dGMP


substrate_name: dUMP; dAMP; dIMP; dGMP; dCMP; dTMP

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

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

substrate: dUMP; dAMP; dIMP; dGMP; dCMP; dTMP


organism: Chlamydomonas reinhardtii

substrate_name: N-acetyl-L-glutamate; ATP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines:
pH 8.0, 37°C, allosteric
pH 5.5, 37°C

substrate: N-acetyl-L-glutamate; ATP


organism: Homo sapiens

substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


substrate_name: NAD

substrate: NAD


organism: Photobacterium phosphoreum

substrate_name: NADP(+)

substrate: NADP(+)


substrate_name: NAD(+)

proof_lines: Has similar catalytic efficiencies, at physiological concentrations, with either NAD(+) or NADP(+) as substrates for the dehydrogenation of (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate.

substrate: NAD(+)


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: oleoyl-CoA (in the presence of LPE C18:1 as cosubstrate)

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


substrate_name: arachidonoyl-CoA (in the presence of LPC C16:0 as cosubstrate)


substrate_name: oleoyl-CoA (in the presence of LPC C16:0 as cosubstrate)


substrate_name: dipalmitoyl phosphatidylcholine

substrate: dipalmitoyl phosphatidylcholine


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: oleoyl-CoA (with lysophosphoethanolamine as cosubstrate)


organism: Cavia porcellus


substrate_name: stearoyl-CoA

proof_lines:
Vmax: 996 nmol/min/mg protein
Vmax: 1782 nmol/min/mg protein
Vmax: 4698 nmol/min/mg protein

substrate: stearoyl-CoA


organism: Mammalia

substrate_name: acyl-CoA

proof_lines: saturated and unsaturated acyl donors, human platelets

substrate: acyl-CoA


substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


organism: Oncorhynchus mykiss

assay_conditions_summary: 293.15 K; cofactor CoA

proof_lines:
at 20°C
at 5°C


organism: Oryctolagus cuniculus


organism: Saccharomyces cerevisiae


organism: Solanum tuberosum


organism: Corynebacterium glutamicum

substrate_name: N-acetyl-L-glutamate

proof_lines: mutant E19A, pH and temperature not specified in the publication, with 1 mM L-arginine

substrate: N-acetyl-L-glutamate


proof_lines: mutant R209A, pH and temperature not specified in the publication, with 1 mM L-arginine


mutation_signature: Δ2

proof_lines: mutant DELTA2-15, pH and temperature not specified in the publication

proof_lines: mutant DELTA2-29, pH and temperature not specified in the publication, with 1 mM L-arginine

proof_lines: mutant DELTA2-19, pH and temperature not specified in the publication


enzyme_display_name: amino-acid N-acetyltransferase

organism: Mycobacterium tuberculosis

substrate_name: Acetyl-CoA

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

enzyme: amino-acid N-acetyltransferase

substrate: Acetyl-CoA


substrate_name: L-Glutamine

substrate: L-Glutamine


sequence_source: UniProt REST exact accession Q6P1A2

proof_lines: Vmax: 12.4 pmol/min/microgram protein for arachidonoyl-CoA


sequence_source: UniProt REST exact accession Q643R3

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


substrate_name: arachidonyl-CoA

sequence_source: UniProt REST exact accession Q8NF37

proof_lines: pH and temperature not specified in the publication

substrate: arachidonyl-CoA


substrate_name: palmitoyl-CoA

sequence_source: UniProt REST exact accession Q3TFD2

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA

substrate: palmitoyl-CoA


substrate_name: docosahexanoyl-CoA

sequence_source: UniProt REST exact accession Q6NVG1

proof_lines: with 1-palmitoyl-sn-glycero-3-phosphoethanolamine, pH and temperature not specified in the publication

proof_lines: with 1-octadecenyl-sn-glycero-3-phosphoethanolamine, pH and temperature not specified in the publication

substrate: docosahexanoyl-CoA


sequence_source: UniProt REST exact accession Q08548


organism: Citrullus lanatus

substrate_name: N(2)-acetyl-L-ornithine (at pH 7.0)

assay_conditions_summary: pH 7

substrate: N(2)-acetyl-L-ornithine (at pH 7.0)


organism: Danio rerio


organism: Geobacillus stearothermophilus

substrate_name: acetyl-CoA (AGSase activity)

substrate: acetyl-CoA (AGSase activity)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: acetyl-CoA


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

substrate_name: glutamate

substrate: glutamate


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


organism: Bos taurus

assay_conditions_summary: pH 4


organism: Homo sapiens

substrate_name: palmitoyl-CoA (in the presence of 1-palmitoyl-LPC as cosubstrate)

assay_conditions_summary: cofactor CoA


substrate_name: lysophosphatidylethanolamine

substrate: lysophosphatidylethanolamine


substrate_name: palmitoyl-CoA (lysophosphatidylcholine acyltransferase activity at pH 4.0)

assay_conditions_summary: pH 4; cofactor CoA


organism: Pseudomonas aeruginosa

substrate_name: L-glutamate

proof_lines: mutant ins284A, in presence of 2 mM arginine

substrate: L-glutamate


organism: Allium ampeloprasum


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

substrate_name: maltopentaose

sequence_source: UniProtKB reviewed P95867 (TREZ_SACS2), direct UniProt REST lookup for treZ / EC 3.2.1.141 / Sulfolobus solfataricus ATCC 35092

substrate: maltopentaose


organism: Citrus japonica

substrate_name: UDP-alpha-D-glucose

proof_lines: 50 mM potassium phosphate buffer, pH 8.0, containing 5 mM 2-mercaptoethanol and 0.01% BSA, 30°C, nothofagin as sugar acceptor

substrate: UDP-alpha-D-glucose


organism: Nelumbo lutea


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

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


organism: Cupriavidus necator


substrate_name: quinolinate

substrate: quinolinate


organism: Lentinula edodes


organism: Nicotiana tabacum


organism: Rattus norvegicus

proof_lines:
enzyme from liver
enzyme from liver and brain
enzyme from brain


organism: Ricinus communis


organism: Salmonella enterica subsp. enterica serovar Typhimurium


substrate_name: quinolinic acid

substrate: quinolinic acid


substrate_name: nicotinic acid

substrate: nicotinic acid


organism: Oryza sativa subsp. indica

proof_lines: kcat is 0.76 sec(-1) with 2,5,7-trihydroxyflavanone as substrate. kcat is 3.13 sec(-1) with 2-hydroxynaringenin as substrate. kcat is 0.75 sec(-1) with 2',4',6'-trihydroxydihydrochalcone as substrate. kcat is 10.84 sec(-1) with phoretin as


proof_lines:
wild-type
wild-type, at 25°C


organism: Sus scrofa

proof_lines:
enzyme from liver
enzyme from kidney


organism: Corynebacterium glutamicum

substrate_name: N-acetyl-L-glutamate

proof_lines: mutant G287A, pH and temperature not specified in the publication, with 1 mM L-arginine

substrate: N-acetyl-L-glutamate


mutation_signature: Δ8

proof_lines: mutant DELTA8, pH and temperature not specified in the publication, with 1 mM L-arginine


proof_lines: mutant H268N, pH and temperature not specified in the publication, with 1 mM L-arginine

proof_lines: mutant H268N, pH 8.0, 37°C, with 1 mM L-arginine


substrate_name: phloretin

substrate: phloretin


organism: Fagopyrum esculentum


substrate_name: maltotriosyltrehalose

substrate: maltotriosyltrehalose


organism: Streptococcus pyogenes


organism: Saccharolobus solfataricus

substrate_name: maltotetraosyl trehalose

sequence_source: UniProtKB REST P95867 checked 2026-06-17

substrate: maltotetraosyl trehalose


substrate_name: maltohexaose

sequence_variant_note: Resolved canonical sequence from UniProtKB REST P95867 canonical sequence plus single-substitution reconstruction checked 2026-06-17 and applied mutation signature R356K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

proof_lines: mutant enzyme R356K, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation

substrate: maltohexaose


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P95867 canonical sequence plus single-substitution reconstruction checked 2026-06-17 and applied mutation signature F355Y to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

proof_lines: mutant enzyme F355Y, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P95867 canonical sequence plus single-substitution reconstruction checked 2026-06-17 and applied mutation signature A259S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

proof_lines: mutant enzyme A259S, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation


substrate_name: maltopentaosyltrehalose

sequence_variant_note: Resolved canonical sequence from UniProtKB REST P95867 canonical sequence plus single-substitution reconstruction checked 2026-06-17 and applied mutation signature Y328F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation

proof_lines: mutant enzyme Y328F, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

substrate: maltopentaosyltrehalose


proof_lines: wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

proof_lines: wild-type enzyme, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation


substrate_name: maltotetraosyltrehalose

sequence_variant_note: Resolved canonical sequence from UniProtKB REST P95867 canonical sequence plus single-substitution reconstruction checked 2026-06-17 and applied mutation signature W218A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W218A, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation

proof_lines: mutant enzyme W218A, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

substrate: maltotetraosyltrehalose


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P95867 canonical sequence plus single-substitution reconstruction checked 2026-06-17 and applied mutation signature W218F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W218F, 60°C, 50 mM citrate phosphate buffer, pH 5, glucose formation

proof_lines: mutant enzyme W218F, 60°C, 50 mM citrate phosphate buffer, pH 5, trehalose formation


substrate_name: maltosyltriosyltrehalose

sequence_source: UniProtKB REST Q55088 checked 2026-06-17

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

proof_lines:
pH 5.5, 60°C
Raw SKiD Env: Temp=60°C, pH=5.5

substrate: maltosyltriosyltrehalose


organism: Escherichia coli

substrate_name: Acetyl-CoA; L-Glutamate

sequence_source: UniProtKB:P0A6C5 REST exact accession lookup (reviewed entry ARGA_ECOLI)

substrate: Acetyl-CoA; L-Glutamate


organism: Geobacillus stearothermophilus

sequence_source: UniProtKB:Q07908 REST exact accession lookup (reviewed entry ARGJ_GEOSE)


organism: Homo sapiens

substrate_name: acetyl-CoA

sequence_source: UniProtKB:Q8N159 REST exact accession lookup (reviewed entry NAGS_HUMAN); canonical precursor only

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

proof_lines: mature enzyme without affinity tag, in presence of 1 mM Arg

substrate: acetyl-CoA


organism: Mus musculus

sequence_source: UniProtKB:Q8R4H7 REST exact accession lookup (reviewed entry NAGS_MOUSE); canonical precursor only

proof_lines: mature enzyme with polyhistidine tag and thrombin protease recognition sequence


organism: Mycobacterium tuberculosis

substrate_name: L-Glutamate; Acetyl-CoA

sequence_source: UniProtKB:O33289 REST exact accession lookup (reviewed entry ARGA_MYCTU)

substrate: L-Glutamate; Acetyl-CoA


organism: Neisseria gonorrhoeae

sequence_source: UniProtKB:Q5FAK7 REST exact accession lookup (unreviewed entry Q5FAK7_NEIG1)

proof_lines:
in presence of 0.1 mM L-arginine
in presence of 1 mM L-arginine


organism: Pseudomonas aeruginosa

sequence_variant_note: Resolved canonical sequence from UniProtKB:P22567 REST exact accession lookup plus selected BRENDA mutation note V358A and applied mutation signature V358A to reconstruct the assayed variant sequence.


substrate_name: L-glutamate

sequence_source: UniProtKB:P22567 REST exact accession lookup plus selected BRENDA mutation note G339A

substrate: L-glutamate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22567 REST exact accession lookup plus selected BRENDA mutation note E352D and applied mutation signature E352D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22567 REST exact accession lookup plus selected BRENDA mutation note G146C and applied mutation signature G146C to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P22567 REST exact accession lookup (reviewed entry ARGA_PSEAE)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22567 REST exact accession lookup plus selected BRENDA mutation note E352A and applied mutation signature E352A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P22567 REST exact accession lookup plus selected BRENDA mutation note G275A and applied mutation signature G275A to reconstruct the assayed variant sequence.