enzyme_display_name: 2-hydroxyisoflavanone dehydratase

organism: Pueraria montana var. lobata

enzyme: 2-hydroxyisoflavanone dehydratase


enzyme_display_name: dihydroneopterin aldolase

organism: Haemophilus influenzae

source_db: brenda

verification_status: unverified

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

proof_lines: cleavage epimerization

enzyme: dihydroneopterin aldolase

status: unverified

source: brenda


enzyme_display_name: dihydroxy-acid dehydratase

organism: Mycobacterium tuberculosis

proof_lines: pH 8.0, temperature not specified in the publication

enzyme: dihydroxy-acid dehydratase


organism: Cupriavidus necator


organism: Aspergillus fumigatus

substrate_name: L-threonate

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

substrate: L-threonate


enzyme_display_name: cyanase

organism: Thermomyces lanuginosus

substrate_name: Cyanate

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

mutation_type: substitution

proof_lines: mutant enzyme A128V, pH and temperature not specified in the publication

enzyme: cyanase

substrate: Cyanate


proof_lines: mutant enzyme E104D, pH and temperature not specified in the publication


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


proof_lines: mutant enzyme Y14A, pH and temperature not specified in the publication


enzyme_display_name: cyclohexyl-isocyanide hydratase

organism: Streptomyces thioluteus

enzyme: cyclohexyl-isocyanide hydratase


substrate_name: cyclohexyl isocyanide

substrate: cyclohexyl isocyanide


organism: Geobacter metallireducens

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA


assay_conditions_summary: cofactor CoA


organism: Homo sapiens

substrate_name: S-methyl-5-thio-D-ribulose 1-phosphate

source_db: uniprot

protein_accession_database: UniProt

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

smiles: CSCC(C(C(=O)COP(=O)(O)O)O)O

data_origin: experimental

substrate: S-methyl-5-thio-D-ribulose 1-phosphate

source: uniprot


enzyme_display_name: aldos-2-ulose dehydratase

organism: Phanerodontia chrysosporium

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

sequence_source: multiple

source_databases_merged: brenda skid

enzyme: aldos-2-ulose dehydratase


organism: Syntrophus aciditrophicus


enzyme_display_name: 16alpha-hydroxyprogesterone dehydratase

organism: Eubacterium sp.

enzyme: 16alpha-hydroxyprogesterone dehydratase


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines: pH 6.8, reaction with 16alpha-hydroxyprogesterone

proof_lines: pH 6.8, reaction with 16alpha-hydroxypregnenolone

substrate: Unknown


enzyme_display_name: 2-methylisocitrate dehydratase

organism: Yarrowia lipolytica

enzyme: 2-methylisocitrate dehydratase


enzyme_display_name: nitrile hydratase

organism: Pseudonocardia thermophila

substrate_name: Benzonitrile

source_db: oed

enzyme: nitrile hydratase

substrate: Benzonitrile

source: oed


substrate_name: acrylonitrile

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.

smiles: C=CC#N

substrate: acrylonitrile


substrate_name: Methacrylonitrile

smiles: C=C(C)C#N

substrate: Methacrylonitrile


organism: Glycine max

verification_status: corrected

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

column_label: PMC1065389 Table 2; row Soybean HIDH / 2,7-Dihydroxy-4'-methoxyisoflavanone -> Formononetin; columns Km=29 uM, kcat=1.6 s^-1, kcat/Km=46 s^-1 mM^-1.

normalized_value_unit_evidence: km normalized_value=0.029 normalized_unit=mM; kcat normalized_value=1.6 normalized_unit=s^-1; kcat/Km normalized_value=46 normalized_unit=s^-1*mM^-1; current_export_kcat=1.6 s^-1; current_export_km=0.029 mM; current_export_kcat_over_km=55.17241379310345 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=29 raw_unit=uM; kcat raw_value=1.6 raw_unit=s^-1; kcat/Km raw_value=46 raw_unit=s^-1 mM^-1

table_label: PMC1065389 Table 2 - kinetic parameters of G. echinata HIDM and soybean HIDH

source_databases_merged: sabio_rk brenda uniprot

status: corrected


column_label: PMC1065389 Table 2; row Soybean HIDH / 2,7,4'-Trihydroxyisoflavanone -> Daidzein; columns Km=114 uM, kcat=5.3 s^-1, kcat/Km=47 s^-1 mM^-1.

normalized_value_unit_evidence: km normalized_value=0.114 normalized_unit=mM; kcat normalized_value=5.3 normalized_unit=s^-1; kcat/Km normalized_value=47 normalized_unit=s^-1*mM^-1; current_export_kcat=5.3 s^-1; current_export_km=0.114 mM; current_export_kcat_over_km=46.49122807017544 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=114 raw_unit=uM; kcat raw_value=5.3 raw_unit=s^-1; kcat/Km raw_value=47 raw_unit=s^-1 mM^-1


column_label: PMC1065389 Table 2; row Soybean HIDH / 2,5,7,4'-Tetrahydroxyisoflavanone -> Genistein; columns Km=170 uM, kcat=18.1 s^-1, kcat/Km=106 s^-1 mM^-1.

normalized_value_unit_evidence: km normalized_value=0.17 normalized_unit=mM; kcat normalized_value=18.1 normalized_unit=s^-1; kcat/Km normalized_value=106 normalized_unit=s^-1*mM^-1; current_export_kcat=18.1 s^-1; current_export_km=0.17 mM; current_export_kcat_over_km=106.47058823529412 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=170 raw_unit=uM; kcat raw_value=18.1 raw_unit=s^-1; kcat/Km raw_value=106 raw_unit=s^-1 mM^-1


organism: Arthrobacter pascens

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


enzyme_display_name: bile-acid 7alpha-dehydratase

enzyme: bile-acid 7alpha-dehydratase


organism: [Clostridium] scindens

assay_conditions_summary: pH 7.3; 298.15 K; cofactor CoA

column_label: Official PMC HTML Table III scindens rows BaiE_12708 and BaiE_35704, kinetic-parameter rows kcat, KM, and kcat/KM under the 3-oxo-Delta4-CDCA column.

normalized_value_unit_evidence: Closest kcat-matching row normalizes to kcat 24.0 s^-1; KM 0.0099 mM; kcat/KM 2400 s^-1 mM^-1. The alternate scindens row with KM 0.011 mM has kcat 18.0 s^-1 and kcat/KM 1600 s^-1 mM^-1. Exported row has KM 11.0 mM and kcat/KM 2.1818181818181817 s^-1 mM^-1.

raw_value_unit_evidence: Table III BaiE_12708 free-acid column: kcat 24.0 (1.4) sec^-1; KM 9.9 (2.1) uM; kcat/KM 2.4 uM^-1 sec^-1. BaiE_35704 free-acid column instead has kcat 18.0 (0.9) sec^-1; KM 11.0 (1.9) uM; kcat/KM 1.6 uM^-1 sec^-1.

row_label: BaiE_12708 / 3-oxo-Delta4-CDCA; alternate scindens row BaiE_35704 / 3-oxo-Delta4-CDCA

table_label: Table III. Steady state kinetic parameters of different homologs of BaiE


kcat_over_km_origin: calculated

column_label: Official PMC HTML Table III row BaiE_12708, kinetic-parameter rows kcat, KM, and kcat/KM under the 3-oxo-Delta4-CDC-CoA column.

normalized_value_unit_evidence: kcat 98.0 s^-1; KM 0.004 mM; primary metric-labeled kcat/KM 24500 s^-1 mM^-1; exported row has KM 4.0 mM and kcat/KM 24.5 s^-1 mM^-1.

raw_value_unit_evidence: Table III BaiE_12708 CoA-ester column: kcat 98.0 (2.7) sec^-1; KM 4.0 (0.56) uM; kcat/KM 24.5 uM^-1 sec^-1.

row_label: BaiE_12708 / 3-oxo-Delta4-CDC-CoA


enzyme_display_name: o-succinylbenzoate synthase

organism: Geobacillus kaustophilus

substrate_name: N-succinyl-L-alanine

proof_lines: kcat is 43 sec(-1) with N-succinyl-L-alanine as substrate. kcat is 15 sec(-1) with N-succinyl-D-alanine as substrate. kcat is 5 sec(-1) with N-succinyl-L-phenylalanine as substrate. kcat is 2 sec(-1) with N-succinyl-D-phenylalanine as subst

enzyme: o-succinylbenzoate synthase

substrate: N-succinyl-L-alanine


substrate_name: N-succinyl-L-phenylalanine

substrate: N-succinyl-L-phenylalanine


substrate_name: N-acetyl-L-methionine

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

substrate: N-acetyl-L-methionine


substrate_name: N-acetyl-L-phenylalanine

substrate: N-acetyl-L-phenylalanine


substrate_name: N-carbamoyl-L-methionine

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

substrate: N-carbamoyl-L-methionine


organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)

substrate_name: cis-aconitate (at pH 8)

verification_status: verified

assay_conditions_summary: pH 8; buffer 100 mM Tris-HCl

column_label: ScienceDirect Table 4 row cis-Aconitate, column Km (uM); caption states assays in 100 mM Tris-HCl buffer pH 8.0.

row_label: cis-Aconitate

table_label: Table 4: Kinetic parameters of aconitase from C. glutamicum

substrate: cis-aconitate (at pH 8)

status: verified


substrate_name: citrate (at pH 8)

column_label: ScienceDirect Table 4 row Citrate, column Km (uM); caption states assays in 100 mM Tris-HCl buffer pH 8.0.

row_label: Citrate

substrate: citrate (at pH 8)


substrate_name: isocitrate (at pH 8)

column_label: ScienceDirect Table 4 row Isocitrate, column Km (uM); caption states assays in 100 mM Tris-HCl buffer pH 8.0.

row_label: Isocitrate

substrate: isocitrate (at pH 8)


organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

substrate_name: N-succinyl-L-phenylglycine

proof_lines: kcat is 520 sec(-1) with N-succinyl-L-phenylglycine as substrate (PubMed:24872444). kcat is 8.5 min(-1) with N-acetyl-D-methionine as substrate (PubMed:15313614). kcat is 9.9 min(-1) with N-acetyl-L-methionine as substrate (PubMed:15313614)

substrate: N-succinyl-L-phenylglycine


substrate_name: SHCHC

substrate: SHCHC


organism: Enterococcus faecalis (strain ATCC 700802 / V583)

proof_lines: kcat is 120 sec(-1) with SHCHC as substrate. kcat is 24 sec(-1) with N-succinyl-L-phenylglycine as substrate.


organism: [Clostridium] hylemonae

assay_conditions_summary: pH 7.3; cofactor CoA

column_label: Official PMC HTML Table III row BaiE_15053, kinetic-parameter rows kcat, KM, and kcat/KM under the 3-oxo-Delta4-CDC-CoA column.

normalized_value_unit_evidence: kcat 12.6 s^-1; KM 0.0114 mM; primary metric-labeled kcat/KM 1100 s^-1 mM^-1; exported row has KM 11.4 mM and kcat/KM 1.1052631578947367 s^-1 mM^-1.

raw_value_unit_evidence: Table III BaiE_15053 CoA-ester column: kcat 12.6 (0.6) sec^-1; KM 11.4 (1.9) uM; kcat/KM 1.1 uM^-1 sec^-1.

row_label: BaiE_15053 / 3-oxo-Delta4-CDC-CoA


column_label: Official PMC HTML Table III row BaiE_15053, kinetic-parameter rows kcat, KM, and kcat/KM under the 3-oxo-Delta4-CDCA column.

normalized_value_unit_evidence: kcat 18.6 s^-1; KM 0.021 mM; primary metric-labeled kcat/KM 900 s^-1 mM^-1; exported row has KM 21.0 mM and kcat/KM 0.8857142857142858 s^-1 mM^-1.

raw_value_unit_evidence: Table III BaiE_15053 free-acid column: kcat 18.6 (0.6) sec^-1; KM 21.0 (2.0) uM; kcat/KM 0.9 uM^-1 sec^-1.

row_label: BaiE_15053 / 3-oxo-Delta4-CDCA


organism: Peptacetobacter hiranonis

column_label: Official PMC HTML Table III row BaiE_13275, kinetic-parameter rows kcat, KM, and kcat/KM under the 3-oxo-Delta4-CDCA column.

normalized_value_unit_evidence: kcat 4.4 s^-1; KM 0.025 mM; primary metric-labeled kcat/KM 200 s^-1 mM^-1; exported row has KM 25.0 mM and kcat/KM 0.176 s^-1 mM^-1.

raw_value_unit_evidence: Table III BaiE_13275 free-acid column: kcat 4.4 (0.1) sec^-1; KM 25.0 (1.8) uM; kcat/KM 0.2 uM^-1 sec^-1.

row_label: BaiE_13275 / 3-oxo-Delta4-CDCA


column_label: Official PMC HTML Table III row BaiE_13275, kinetic-parameter rows kcat, KM, and kcat/KM under the 3-oxo-Delta4-CDC-CoA column.

normalized_value_unit_evidence: kcat 22.2 s^-1; KM 0.208 mM; primary metric-labeled kcat/KM 100 s^-1 mM^-1; exported row has KM 208.0 mM and kcat/KM 0.10673076923076923 s^-1 mM^-1.

raw_value_unit_evidence: Table III BaiE_13275 CoA-ester column: kcat 22.2 (2.6) sec^-1; KM 208.0 (40.0) uM; kcat/KM 0.1 uM^-1 sec^-1.

row_label: BaiE_13275 / 3-oxo-Delta4-CDC-CoA


enzyme_display_name: 3-hydroxypropionyl-CoA dehydratase

organism: Nitrosopumilus maritimus

substrate_name: (E)-octenoyl-CoA

assay_conditions_summary: pH 7.8; 338.15 K; cofactor CoA

enzyme: 3-hydroxypropionyl-CoA dehydratase

substrate: (E)-octenoyl-CoA


assay_conditions_summary: pH 7.8; 315.15 K; cofactor CoA


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


substrate_name: acryloyl-CoA

substrate: acryloyl-CoA


substrate_name: methacrylyl-CoA

substrate: methacrylyl-CoA


enzyme_display_name: tryptophan synthase (indole-salvaging)

organism: Thermotoga maritima

substrate_name: O-Phospho-L-serine

enzyme: tryptophan synthase (indole-salvaging)

substrate: O-Phospho-L-serine


enzyme_display_name: enoyl-CoA hydratase 2

organism: Cucumis sativus

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

enzyme: enoyl-CoA hydratase 2


enzyme_display_name: 3-dehydroshikimate dehydratase

organism: Gluconobacter oxydans

enzyme: 3-dehydroshikimate dehydratase


enzyme_display_name: 4-hydroxybutanoyl-CoA dehydratase

organism: Metallosphaera sedula

assay_conditions_summary: pH 8; 343.15 K; cofactor CoA

enzyme: 4-hydroxybutanoyl-CoA dehydratase


substrate_name: L-serine

proof_lines: at 80°C, pH not specified in the publication

substrate: L-serine


substrate_name: indole

proof_lines: Km below 0.00077 mM, at 80°C, pH not specified in the publication

proof_lines: KCAT_KM below 0.0006 mM, at 80°C, pH not specified in the publication

substrate: indole


organism: Penicillium parvum

proof_lines: 37°C, pH 7.5, in the presence of 10 mM Mg2+


organism: Thermococcus kodakarensis


organism: Geobacillus kaustophilus (strain HTA426)

substrate_name: N-succinyl-L-valine

proof_lines: kcat is 180 sec(-1) with SHCHC as substrate. kcat is 92 sec(-1) with N-succinyl-L-valine as substrate. kcat is 89 sec(-1) with N-succinyl-L-alanine as substrate. kcat is 53 sec(-1) with N-succinyl-L-methionine as substrate. kcat is 52 sec(-

substrate: N-succinyl-L-valine


substrate_name: N-succinyl-L-alanine

substrate: N-succinyl-L-alanine


substrate_name: N-succinyl-L-methionine

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

substrate: N-succinyl-L-methionine


substrate_name: N-succinyl-L-tyrosine

substrate: N-succinyl-L-tyrosine


substrate_name: N-succinyl-L-serine

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

substrate: N-succinyl-L-serine


substrate_name: N-succinyl-L-isoleucine

substrate: N-succinyl-L-isoleucine


substrate_name: N-succinyl-L-phenylalanine

substrate: N-succinyl-L-phenylalanine


substrate_name: N-succinyl-L-leucine

substrate: N-succinyl-L-leucine


enzyme_display_name: D-lactate dehydratase

organism: Homo sapiens

substrate_name: methylglyoxal

smiles: CC(=O)C=O

proof_lines: 30°C, pH not specified in the publication, wild-type enzyme

enzyme: D-lactate dehydratase

substrate: methylglyoxal


proof_lines: 30°C, pH not specified in the publication, mutant enzyme L166P


enzyme_display_name: short-chain-enoyl-CoA hydratase

organism: Meiothermus ruber

enzyme: short-chain-enoyl-CoA hydratase


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: L-threonine

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

proof_lines: recombinant wild-type enzyme, pH 7.8, 37°C

substrate: L-threonine


organism: Zea mays


organism: Syntrophothermus lipocalidus

assay_conditions_summary: pH 7.8; cofactor CoA


substrate_name: (E)-octenoyl-CoA

substrate: (E)-octenoyl-CoA


proof_lines: pH 7.5, 85°C, recombinant TrpB2, with or without TrpA

proof_lines: pH 7.5, 85°C, recombinant TrpB1 with TrpA


enzyme_display_name: UniProt O52793

organism: Amycolatopsis orientalis

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt O52793

source: skid


organism: Arabidopsis thaliana

assay_conditions_summary: pH 8; cofactor ATP

column_label: Table I row Arabidopsis NADHX gives Km 1.15 microM, Kcat 0.26 s^-1, and Kcat/Km 262 mM^-1 s^-1.

row_label: Arabidopsis / NADHX

table_label: Table I. Kinetic properties of Arabidopsis and maize NADHX and NADPHX dehydratases.


column_label: Table I row Arabidopsis NADPHX gives Km 0.69 microM, Kcat 0.34 s^-1, and Kcat/Km 509 mM^-1 s^-1.

row_label: Arabidopsis / NADPHX


substrate_name: Indole; O-Phospho-L-serine

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

substrate: Indole; O-Phospho-L-serine


enzyme_display_name: pterocarpan synthase

organism: Lathyrus oleraceus

enzyme: pterocarpan synthase


organism: Medicago sativa


enzyme_display_name: (R)-2-hydroxyisocaproyl-CoA dehydratase

organism: Clostridium difficile

enzyme: (R)-2-hydroxyisocaproyl-CoA dehydratase


substrate_name: Phenylglyoxal

proof_lines: pH and temperature not specified in the publication

substrate: Phenylglyoxal


enzyme_display_name: squalene--hopanol cyclase

organism: Tetrahymena thermophila

substrate_name: squalene

enzyme: squalene--hopanol cyclase

substrate: squalene


organism: Nitrosopumilus maritimus


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


enzyme_display_name: gluconate/galactonate dehydratase

organism: Picrophilus oshimae

substrate_name: D-galactonate

enzyme: gluconate/galactonate dehydratase

substrate: D-galactonate


organism: Metallosphaera sedula


organism: Alicyclobacillus acidocaldarius

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature F434A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 318.15 K; buffer 60 mM sodium citrate

column_label: Table 4 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutant SHCs in Category C), SHC row 'F434A', product row '3'; column 'Km (uM)' = 8.16 x 10; column 'kcat (min^-1)' = 9.2; column 'kcat/Km' = 1.13 x 10^-1.

raw_value_unit_evidence: Table 4, SHC row F434A, product row 3: Km = 8.16 x 10 uM; kcat = 9.2 min^-1; printed kcat/Km = 1.13 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 4, SHC row F434A, product row 3

table_label: Table 4: Kinetic Data and Optimal Temperatures for the Wild-type and Mutant SHCs in Category C (Bioscience, Biotechnology, and Biochemistry 2004, 68(3):728-738)


column_label: Table 3 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B), SHC row 'Wild-type', product row '3'; column 'Km (uM)' = 1.62 x 10; column 'kcat (min^-1)' = 9.8; column 'kcat/Km' = 6.05 x 10^-1.

raw_value_unit_evidence: Table 3, SHC row Wild-type, product row 3: Km = 1.62 x 10 uM; kcat = 9.8 min^-1; printed kcat/Km = 6.05 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

table_label: Table 3: Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B (Bioscience, Biotechnology, and Biochemistry 2004, 68(3):728-738)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature T41A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B), SHC row 'T41A', product row '3'; column 'Km (uM)' = 1.67 x 10; column 'kcat (min^-1)' = 9.8; column 'kcat/Km' = 5.87 x 10^-1.

raw_value_unit_evidence: Table 3, SHC row T41A, product row 3: Km = 1.67 x 10 uM; kcat = 9.8 min^-1; printed kcat/Km = 5.87 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 3, SHC row T41A, product row 3


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature E93A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B), SHC row 'E93A', product row '3'; column 'Km (uM)' = 1.89 x 10; column 'kcat (min^-1)' = 10.4; column 'kcat/Km' = 5.50 x 10^-1.

raw_value_unit_evidence: Table 3, SHC row E93A, product row 3: Km = 1.89 x 10 uM; kcat = 10.4 min^-1; printed kcat/Km = 5.50 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 3, SHC row E93A, product row 3


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature W133A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B), SHC row 'W133A', product row '3'; column 'Km (uM)' = 1.69 x 10; column 'kcat (min^-1)' = 11.5; column 'kcat/Km' = 6.80 x 10^-1.

raw_value_unit_evidence: Table 3, SHC row W133A, product row 3: Km = 1.69 x 10 uM; kcat = 11.5 min^-1; printed kcat/Km = 6.80 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 3, SHC row W133A, product row 3


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature R127Q to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B), SHC row 'R127Q', product row '3'; column 'Km (uM)' = 2.55 x 10; column 'kcat (min^-1)' = 12.8; column 'kcat/Km' = 5.02 x 10^-1.

raw_value_unit_evidence: Table 3, SHC row R127Q, product row 3: Km = 2.55 x 10 uM; kcat = 12.8 min^-1; printed kcat/Km = 5.02 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 3, SHC row R127Q, product row 3


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature Y267A to reconstruct the assayed variant sequence.

column_label: Table 4 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutant SHCs in Category C), SHC row 'Y267A', product row '3'; column 'Km (uM)' = 1.97 x 10^2; column 'kcat (min^-1)' = 12.6; column 'kcat/Km' = 6.40 x 10^-2.

raw_value_unit_evidence: Table 4, SHC row Y267A, product row 3: Km = 1.97 x 10^2 uM; kcat = 12.6 min^-1; printed kcat/Km = 6.40 x 10^-2 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 4, SHC row Y267A, product row 3


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature E45A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category B), SHC row 'E45A', product row '3'; column 'Km (uM)' = 2.13 x 10; column 'kcat (min^-1)' = 13.3; column 'kcat/Km' = 6.24 x 10^-1.

raw_value_unit_evidence: Table 3, SHC row E45A, product row 3: Km = 2.13 x 10 uM; kcat = 13.3 min^-1; printed kcat/Km = 6.24 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 3, SHC row E45A, product row 3


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature F437A to reconstruct the assayed variant sequence.

column_label: Table 4 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutant SHCs in Category C), SHC row 'F437A', product row '3'; column 'Km (uM)' = 9.55 x 10; column 'kcat (min^-1)' = 29.6; column 'kcat/Km' = 3.10 x 10^-1.

raw_value_unit_evidence: Table 4, SHC row F437A, product row 3: Km = 9.55 x 10 uM; kcat = 29.6 min^-1; printed kcat/Km = 3.10 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 4, SHC row F437A, product row 3


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature Q262A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category A), SHC row 'Q262A', product row '3'; column 'Km (uM)' = 1.02 x 10^2; column 'kcat (min^-1)' = 121.9; column 'kcat/Km' = 1.20.

raw_value_unit_evidence: Table 2, SHC row Q262A, product row 3: Km = 1.02 x 10^2 uM; kcat = 121.9 min^-1; printed kcat/Km = 1.20 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 2, SHC row Q262A, product row 3

table_label: Table 2: Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category A (Bioscience, Biotechnology, and Biochemistry 2004, 68(3):728-738)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature P263A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category A), SHC row 'P263A', product row '3'; column 'Km (uM)' = 1.85 x 10^2; column 'kcat (min^-1)' = 226.6; column 'kcat/Km' = 1.22.

raw_value_unit_evidence: Table 2, SHC row P263A, product row 3: Km = 1.85 x 10^2 uM; kcat = 226.6 min^-1; printed kcat/Km = 1.22 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 2, SHC row P263A, product row 3


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature P263G to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category A), SHC row 'P263G', product row '3'; column 'Km (uM)' = 2.37 x 10^2; column 'kcat (min^-1)' = 231.5; column 'kcat/Km' = 9.77 x 10^-1.

raw_value_unit_evidence: Table 2, SHC row P263G, product row 3: Km = 2.37 x 10^2 uM; kcat = 231.5 min^-1; printed kcat/Km = 9.77 x 10^-1 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 2, SHC row P263G, product row 3


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33247 and applied mutation signature Q262G to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Data and Optimal Temperatures for the Wild-type and Mutated SHCs in Category A), SHC row 'Q262G', product row '3'; column 'Km (uM)' = 1.56 x 10^2; column 'kcat (min^-1)' = 263.2; column 'kcat/Km' = 1.69.

raw_value_unit_evidence: Table 2, SHC row Q262G, product row 3: Km = 1.56 x 10^2 uM; kcat = 263.2 min^-1; printed kcat/Km = 1.69 uM^-1 min^-1. The kcat/Km column head prints no unit of its own; section 4 of the local extract reads that column in uM^-1 min^-1 off the Km and kcat column heads and checks the reading against every cell of the three tables.

row_label: Table 2, SHC row Q262G, product row 3


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


assay_conditions_summary: pH 7; 323.15 K; cofactor CoA

proof_lines: pH 7.0, 50°C, recombinant His-tagged enzyme


enzyme_display_name: L-talarate dehydratase

substrate_name: L-talarate

assay_conditions_summary: pH 8

enzyme: L-talarate dehydratase

substrate: L-talarate


enzyme_display_name: L-lyxonate dehydratase

organism: Roseibium aggregatum

substrate_name: L-lyxonate

enzyme: L-lyxonate dehydratase

substrate: L-lyxonate


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


substrate_name: D-gulonate

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

substrate: D-gulonate


enzyme_display_name: (R)-2-hydroxyglutaryl-CoA dehydratase

organism: [Clostridium] symbiosum

enzyme: (R)-2-hydroxyglutaryl-CoA dehydratase


enzyme_display_name: linalool dehydratase

organism: Castellaniella defragrans

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M125A to reconstruct the assayed variant sequence.

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

enzyme: linalool dehydratase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H129A with inferred residue-numbering offset +25 to reconstruct the assayed variant sequence.


substrate_name: myrcene

smiles: CC(=CCCC(=C)C=C)C

substrate: myrcene


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y66F with inferred residue-numbering offset +25 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.


enzyme_display_name: tetracenomycin F2 cyclase

organism: Streptomyces glaucescens

substrate_name: tetracenomycin F2

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39890 and applied mutation signature R40G to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic data for the TcmI active site mutants), variant row 'R40G'; column 'Km (uM)' = 1.20 x 10^3; column 'Vmax (umol min^-1 mg^-1)' = 0.0703; column 'Relative activity' = 10; column 'kcat (s^-1)' = 0.0146; column 'Kcat/Km (M^-1 s^-1)' = 12.1.

normalized_value_unit_evidence: Km: printed Table I cell 1.20 x 10^3 uM; 1.20 x 10^3 uM / 1000 = 1.2 mM; the exported value is 1.2 mM. kcat: printed Table I cell 0.0146 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.0146 s^(-1). kcat/Km: printed Table I cell 12.1 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 12.1 M^-1 s^-1 / 1000 = 0.0121 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, variant row 'R40G': Km = 1.20 x 10^3 uM; Vmax = 0.0703 umol min^-1 mg^-1; relative activity = 10; kcat = 0.0146 s^-1; printed Kcat/Km = 12.1 M^-1 s^-1.

row_label: Table I, variant row 'R40G'

table_label: Table I: Kinetic data for the TcmI active site mutants (J. Biol. Chem. 2004, 279(36):37956-37963)

enzyme: tetracenomycin F2 cyclase

substrate: tetracenomycin F2


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39890 and applied mutation signature H26A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic data for the TcmI active site mutants), variant row 'H26A'; column 'Km (uM)' = 732; column 'Vmax (umol min^-1 mg^-1)' = 0.0920; column 'Relative activity' = 15; column 'kcat (s^-1)' = 0.0192; column 'Kcat/Km (M^-1 s^-1)' = 26.2.

normalized_value_unit_evidence: Km: printed Table I cell 732 uM; 732 uM / 1000 = 0.732 mM; the exported value is 0.732 mM. kcat: printed Table I cell 0.0192 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.0192 s^(-1). kcat/Km: printed Table I cell 26.2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 26.2 M^-1 s^-1 / 1000 = 0.0262 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, variant row 'H26A': Km = 732 uM; Vmax = 0.0920 umol min^-1 mg^-1; relative activity = 15; kcat = 0.0192 s^-1; printed Kcat/Km = 26.2 M^-1 s^-1.

row_label: Table I, variant row 'H26A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39890 and applied mutation signature D27N to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic data for the TcmI active site mutants), variant row 'D27N'; column 'Km (uM)' = 1.05 x 10^3; column 'Vmax (umol min^-1 mg^-1)' = 0.0948; column 'Relative activity' = 14; column 'kcat (s^-1)' = 0.0198; column 'Kcat/Km (M^-1 s^-1)' = 18.8.

normalized_value_unit_evidence: Km: printed Table I cell 1.05 x 10^3 uM; 1.05 x 10^3 uM / 1000 = 1.05 mM; the exported value is 1.05 mM. kcat: printed Table I cell 0.0198 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.0198 s^(-1). kcat/Km: printed Table I cell 18.8 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 18.8 M^-1 s^-1 / 1000 = 0.0188 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, variant row 'D27N': Km = 1.05 x 10^3 uM; Vmax = 0.0948 umol min^-1 mg^-1; relative activity = 14; kcat = 0.0198 s^-1; printed Kcat/Km = 18.8 M^-1 s^-1.

row_label: Table I, variant row 'D27N'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39890 and applied mutation signature H51A to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic data for the TcmI active site mutants), variant row 'H51A'; column 'Km (uM)' = 892; column 'Vmax (umol min^-1 mg^-1)' = 0.105; column 'Relative activity' = 16; column 'kcat (s^-1)' = 0.0219; column 'Kcat/Km (M^-1 s^-1)' = 24.5.

normalized_value_unit_evidence: Km: printed Table I cell 892 uM; 892 uM / 1000 = 0.892 mM; the exported value is 0.892 mM. kcat: printed Table I cell 0.0219 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.0219 s^(-1). kcat/Km: printed Table I cell 24.5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 24.5 M^-1 s^-1 / 1000 = 0.0245 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, variant row 'H51A': Km = 892 uM; Vmax = 0.105 umol min^-1 mg^-1; relative activity = 16; kcat = 0.0219 s^-1; printed Kcat/Km = 24.5 M^-1 s^-1.

row_label: Table I, variant row 'H51A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39890 and applied mutation signature R40K to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic data for the TcmI active site mutants), variant row 'R40K'; column 'Km (uM)' = 816; column 'Vmax (umol min^-1 mg^-1)' = 0.108; column 'Relative activity' = 16; column 'kcat (s^-1)' = 0.0250; column 'Kcat/Km (M^-1 s^-1)' = 30.6.

normalized_value_unit_evidence: Km: printed Table I cell 816 uM; 816 uM / 1000 = 0.816 mM; the exported value is 0.816 mM. kcat: printed Table I cell 0.0250 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.025 s^(-1). kcat/Km: printed Table I cell 30.6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 30.6 M^-1 s^-1 / 1000 = 0.0306 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, variant row 'R40K': Km = 816 uM; Vmax = 0.108 umol min^-1 mg^-1; relative activity = 16; kcat = 0.0250 s^-1; printed Kcat/Km = 30.6 M^-1 s^-1.

row_label: Table I, variant row 'R40K'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39890 and applied mutation signature H26Q to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic data for the TcmI active site mutants), variant row 'H26Q'; column 'Km (uM)' = 203; column 'Vmax (umol min^-1 mg^-1)' = 0.627; column 'Relative activity' = 91; column 'kcat (s^-1)' = 0.131; column 'Kcat/Km (M^-1 s^-1)' = 645.

normalized_value_unit_evidence: Km: printed Table I cell 203 uM; 203 uM / 1000 = 0.203 mM; the exported value is 0.203 mM. kcat: printed Table I cell 0.131 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.131 s^(-1). kcat/Km: printed Table I cell 645 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 645 M^-1 s^-1 / 1000 = 0.645 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, variant row 'H26Q': Km = 203 uM; Vmax = 0.627 umol min^-1 mg^-1; relative activity = 91; kcat = 0.131 s^-1; printed Kcat/Km = 645 M^-1 s^-1.

row_label: Table I, variant row 'H26Q'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39890 and applied mutation signature H51Q to reconstruct the assayed variant sequence.

column_label: Table I (Kinetic data for the TcmI active site mutants), variant row 'H51Q'; column 'Km (uM)' = 191; column 'Vmax (umol min^-1 mg^-1)' = 0.651; column 'Relative activity' = 96; column 'kcat (s^-1)' = 0.136; column 'Kcat/Km (M^-1 s^-1)' = 712.

normalized_value_unit_evidence: Km: printed Table I cell 191 uM; 191 uM / 1000 = 0.191 mM; the exported value is 0.191 mM. kcat: printed Table I cell 0.136 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.136 s^(-1). kcat/Km: printed Table I cell 712 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 712 M^-1 s^-1 / 1000 = 0.712 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, variant row 'H51Q': Km = 191 uM; Vmax = 0.651 umol min^-1 mg^-1; relative activity = 96; kcat = 0.136 s^-1; printed Kcat/Km = 712 M^-1 s^-1.

row_label: Table I, variant row 'H51Q'


column_label: Table I (Kinetic data for the TcmI active site mutants), variant row 'Wild type'; column 'Km (uM)' = 155; column 'Vmax (umol min^-1 mg^-1)' = 0.680; column 'Relative activity' = 100; column 'kcat (s^-1)' = 0.142; column 'Kcat/Km (M^-1 s^-1)' = 916.

normalized_value_unit_evidence: Km: printed Table I cell 155 uM; 155 uM / 1000 = 0.155 mM; the exported value is 0.155 mM. kcat: printed Table I cell 0.142 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 0.142 s^(-1). kcat/Km: printed Table I cell 916 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 916 M^-1 s^-1 / 1000 = 0.916 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table I, variant row 'Wild type': Km = 155 uM; Vmax = 0.680 umol min^-1 mg^-1; relative activity = 100; kcat = 0.142 s^-1; printed Kcat/Km = 916 M^-1 s^-1.

row_label: Table I, variant row 'Wild type'


enzyme_display_name: cis-L-3-hydroxyproline dehydratase

organism: Azospirillum brasilense

enzyme: cis-L-3-hydroxyproline dehydratase


organism: Micromonospora viridifaciens


organism: Aeromonas caviae

substrate_name: hexenoyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L65A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

substrate: hexenoyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V130G to reconstruct the assayed variant sequence.


enzyme_display_name: colneleate synthase

organism: Allium sativum

smiles: CCCCCC(C=CC=CCCCCCCCC(=O)[O-])OO

proof_lines: kcat is 550 sec(-1) with (13S)-hydroperoxy-(9Z,11E)-octadecadienoate as substrate (PubMed:18326559). kcat is 40 sec(-1) with (13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate as substrate (PubMed:18326559). kcat is 70 sec (-1) with (9S)-hydr

enzyme: colneleate synthase


organism: Caenorhabditis elegans

assay_conditions_summary: pH 6; buffer pH 6

column_label: Table 1 row cDJR-1.2; Methylglyoxal Km (mM) column reports 0.39.

raw_value_unit_evidence: Table 1 reports cDJR-1.2 methylglyoxal Km 0.39 mM.

row_label: cDJR-1.2 row, Methylglyoxal columns

table_label: Table 1. Enzymatic constants for purified DJ-1s


substrate_name: glyoxal

smiles: C(=O)C=O

column_label: Table 1 row cDJR-1.2; Glyoxal Km (mM) column reports 0.78.

raw_value_unit_evidence: Table 1 reports cDJR-1.2 glyoxal Km 0.78 mM.

row_label: cDJR-1.2 row, Glyoxal columns

substrate: glyoxal


column_label: Table 1 row cDJR-1.1; Methylglyoxal Km (mM) column reports 0.30.

raw_value_unit_evidence: Table 1 reports cDJR-1.1 methylglyoxal Km 0.30 mM.

row_label: cDJR-1.1 row, Methylglyoxal columns


column_label: Table 1 row cDJR-1.1; Glyoxal Km (mM) column reports 3.61.

raw_value_unit_evidence: Table 1 reports cDJR-1.1 glyoxal Km 3.61 mM.

row_label: cDJR-1.1 row, Glyoxal columns


organism: Homo sapiens

substrate_name: all-trans-retinol

proof_lines: kcat is 0.15 min(-1) for retinol, 0.77 min(-1) for retinal, 2.86 min(-1) for 7,12-dimethyltetraphene, 0.48 min(-1) for arachidonic acid.

substrate: all-trans-retinol


substrate_name: all-trans-retinal

substrate: all-trans-retinal


substrate_name: arachidonic acid

smiles: CCCCCC=CCC=CCC=CCC=CCCCC(=O)O

substrate: arachidonic acid


enzyme_display_name: 2-hydroxyisoflavanone dehydratase

organism: Glycyrrhiza echinata

column_label: PMC1065389 Table 2; row G. echinata HIDM / 2,7-Dihydroxy-4'-methoxyisoflavanone -> Formononetin; columns Km=58 uM, kcat=9.8 s^-1, kcat/Km=170 s^-1 mM^-1.

normalized_value_unit_evidence: km normalized_value=0.058 normalized_unit=mM; kcat normalized_value=9.8 normalized_unit=s^-1; kcat/Km normalized_value=170 normalized_unit=s^-1*mM^-1; current_export_kcat=9.8 s^-1; current_export_km=0.058 mM; current_export_kcat_over_km=168.9655172413793 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=58 raw_unit=uM; kcat raw_value=9.8 raw_unit=s^-1; kcat/Km raw_value=170 raw_unit=s^-1 mM^-1

enzyme: 2-hydroxyisoflavanone dehydratase


column_label: PMC1065389 Table 2; row G. echinata HIDM / 2,7,4'-Trihydroxyisoflavanone -> Daidzein; columns Km=210 uM, kcat=0.12 s^-1, kcat/Km=0.56 s^-1 mM^-1.

normalized_value_unit_evidence: km normalized_value=0.21 normalized_unit=mM; kcat normalized_value=0.12 normalized_unit=s^-1; kcat/Km normalized_value=0.56 normalized_unit=s^-1*mM^-1; current_export_kcat=0.12 s^-1; current_export_km=0.21 mM; current_export_kcat_over_km=0.5714285714285714 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=210 raw_unit=uM; kcat raw_value=0.12 raw_unit=s^-1; kcat/Km raw_value=0.56 raw_unit=s^-1 mM^-1


column_label: PMC1065389 Table 2; row G. echinata HIDM / 2,5,7,4'-Tetrahydroxyisoflavanone -> Genistein; columns Km=304 uM, kcat=0.19 s^-1, kcat/Km=0.62 s^-1 mM^-1.

normalized_value_unit_evidence: km normalized_value=0.304 normalized_unit=mM; kcat normalized_value=0.19 normalized_unit=s^-1; kcat/Km normalized_value=0.62 normalized_unit=s^-1*mM^-1; current_export_kcat=0.19 s^-1; current_export_km=0.304 mM; current_export_kcat_over_km=0.625 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=304 raw_unit=uM; kcat raw_value=0.19 raw_unit=s^-1; kcat/Km raw_value=0.62 raw_unit=s^-1 mM^-1


organism: Escherichia coli (strain K12)

substrate_name: Lys-AMC (at 37 degrees Celsius and pH 8.5)

proof_lines: kcat is 156.9 min(-1) for glyoxalase activity with methylglyoxal as substrate (PubMed:21696459). kcat is 0.43 min(-1) for aminopeptidase activity with Lys-AMC as substrate. kcat is 0.51 min(-1) for aminopeptidase activity with Arg-AMC as su


substrate_name: Arg-AMC (at 37 degrees Celsius and pH 8.5)


substrate_name: Ala-AMC (at 37 degrees Celsius and pH 8.5)


enzyme_display_name: o-succinylbenzoate synthase

organism: Geobacillus stearothermophilus

substrate_name: N-formyl-D-methionine

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

proof_lines: kcat is 74.6 sec(-1) with N-formyl-D-methionine as substrate. kcat is 52.9 sec(-1) with N-formyl-L-methionine as substrate. kcat is 12.3 sec(-1) with N-formyl-D-norleucine as substrate. kcat is 8.0 sec(-1) with N-formyl-L-norleucine as subs

enzyme: o-succinylbenzoate synthase

substrate: N-formyl-D-methionine


substrate_name: N-formyl-D-norleucine

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

substrate: N-formyl-D-norleucine


enzyme_display_name: pectate lyase

organism: Streptomyces nitrosporeus

substrate_name: tetragalacturonic acid

enzyme: pectate lyase

substrate: tetragalacturonic acid


substrate_name: trigalacturonic acid

substrate: trigalacturonic acid


enzyme_display_name: UniProt P39116

organism: Bacillus subtilis

substrate_name: trigalacturonate

enzyme: UniProt P39116

substrate: trigalacturonate


enzyme_display_name: trans-4-hydroxy-L-proline dehydratase

organism: Clostridioides difficile

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y450F to reconstruct the assayed variant sequence.

enzyme: trans-4-hydroxy-L-proline dehydratase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T645A to reconstruct the assayed variant sequence.


organism: Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)

substrate_name: SHCHC

column_label: Supporting Information PDF page 9, Table S1, Listeria innocua row, OSBS Km (uM) column: 59 +/- 20.

row_label: Listeria innocua

table_label: Table S1. Enzymatic activity of enzymes in the OSBS family

substrate: SHCHC


substrate_name: N-succinyl-L-phenylglycine

column_label: Supporting Information PDF page 9, Table S1, Listeria innocua row, NSAR Km (uM) column: 640 +/- 20; table footnote identifies N-succinyl-L-phenylglycine as substrate.

raw_value_unit_evidence: NSAR Km=640 +/- 20 uM; N-succinyl-L-phenylglycine is the substrate.

substrate: N-succinyl-L-phenylglycine


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

proof_lines: kcat is 33 sec(-1) with N-succinyl-L-phenylglycine as substrate (PubMed:24872444). kcat is 6.1 sec(-1) with SHCHC as substrate (PubMed:24872444).


enzyme_display_name: difructose-anhydride-I synthase

organism: Aspergillus fumigatus

substrate_name: bis-D-fructose 2',1:2,1' dianhydride

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

enzyme: difructose-anhydride-I synthase

substrate: bis-D-fructose 2',1:2,1' dianhydride


substrate_name: bis-D-fructose 2',1:2,1'-dianhydride

substrate: bis-D-fructose 2',1:2,1'-dianhydride


substrate_name: Inulobiose

proof_lines:
pH 6, 37°C
at pH 6.0 and 37°C

substrate: Inulobiose


enzyme_display_name: D-lactate dehydratase

organism: Schizosaccharomyces pombe

substrate_name: methylglyoxal

proof_lines: recombinant Hsp3101, pH and temperature not specified in the publication

proof_lines: kcat is 31.1 min(-1) with methylglyoxal as substrate.

source_databases_merged: brenda uniprot

enzyme: D-lactate dehydratase

substrate: methylglyoxal


proof_lines: recombinant Hsp3102, pH and temperature not specified in the publication

proof_lines: kcat is 58.0 min(-1) with methylglyoxal as substrate.


proof_lines: kcat is 85.7 min(-1) with methylglyoxal as substrate.

source_databases_merged: skid uniprot


organism: Solanum lycopersicum

smiles: CCCCCC=CC=CC(CCCCCCCC(=O)[O-])OO

assay_conditions_summary: pH 7

proof_lines: kcat is 890 sec(-1) for (9S)-hydroperoxy-(10E,12Z)-octadecadienoate (PubMed:11060314). kcat is 500 sec(-1) for (10E,12Z,15Z)-(9S)-9-hydroperoxyoctadeca-10,12,15-trienoic acid (PubMed:11060314).


smiles: CCC=CCC=CC=CC(CCCCCCCC(=O)[O-])OO


enzyme_display_name: difructose-dianhydride-III synthase

organism: Paenarthrobacter ureafaciens

enzyme: difructose-dianhydride-III synthase


enzyme_display_name: etheroleic acid synthase

organism: Asparagus officinalis

enzyme: etheroleic acid synthase


organism: Pseudarthrobacter chlorophenolicus

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


organism: uncultured bacterium

substrate_name: Pectin

proof_lines: 50-70% methylated substrate, pH 9.8, 45°C, recombinant enzyme

proof_lines: over 80% methylated substrate, pH 9.8, 45°C, recombinant enzyme

substrate: Pectin


substrate_name: polygalacturonic acid

proof_lines: 20-34% methylated substrate, pH 9.8, 45°C, recombinant enzyme

proof_lines: unmethylated substrate, pH 9.8, 45°C, recombinant enzyme

substrate: polygalacturonic acid


organism: Paenarthrobacter aurescens

substrate_name: di-D-fructofuranose 1,2:2,3 dianhydride

substrate: di-D-fructofuranose 1,2:2,3 dianhydride


organism: Actinomadura keratinilytica

substrate_name: Polygalacturonate

substrate: Polygalacturonate


organism: Arthrobacter sp. H65-7

assay_conditions_summary: pH 6


organism: Thermobifida fusca

substrate_name: Unknown

substrate: Unknown


organism: Thermotoga maritima


enzyme_display_name: pterocarpan synthase

organism: Glycyrrhiza echinata

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D50A to reconstruct the assayed variant sequence.

enzyme: pterocarpan synthase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D83A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y181F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y103F 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.


organism: Mus musculus

substrate_name: all-trans-retinol

proof_lines: kcat is 0.04 min(-1) for retinol, 0.08 min(-1) for retinal, 1.24 min(-1) for 7,12-dimethyltetraphene, 0.13 min(-1) for arachidonic acid.

substrate: all-trans-retinol


substrate_name: all-trans-retinal

substrate: all-trans-retinal


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


substrate_name: arachidonic acid

substrate: arachidonic acid


enzyme_display_name: methanogen homoaconitase

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

substrate_name: cis-homoaconitate

proof_lines: kcat is 0.75 sec(-1) for cis-aconitate hydration reaction (PubMed:20170198). Kinetic parameters measured using the HacAB complex.

enzyme: methanogen homoaconitase

substrate: cis-homoaconitate


substrate_name: maleate

substrate: maleate


substrate_name: (R)-homocitrate

substrate: (R)-homocitrate


organism: Homo sapiens

smiles: CCCCCC=CCC(C=CC=CCC=CCCCC(=O)[O-])OO

proof_lines: Has a 5 to 10 fold higher activity toward (12R)-HPETE (hydroperoxyeicosatetraenoic acid) compared to (12S)-HPETE and (15S)-HPETE (PubMed:12881489). From (12R)-HPETE produces a stereoisomer of hepoxilin A3 (PubMed:12881489). More active on h


smiles: CCCCCC(C=CC=CCC=CCC=CCCCC(=O)[O-])OO


substrate_name: 17-beta-estradiol (2-hydroxylation)

proof_lines: kcat is 0.15 min(-1) for retinol, 0.77 min(-1) for retinal, 2.86 min(-1) for 7,12-dimethyltetraphene, 0.48 min(-1) for arachidonic acid.

substrate: 17-beta-estradiol (2-hydroxylation)


substrate_name: progesterone (6-beta-hydroxylation)

substrate: progesterone (6-beta-hydroxylation)


organism: Amycolatopsis orientalis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R381A to reconstruct the assayed variant sequence.


enzyme_display_name: methylthioacryloyl-CoA hydratase

organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)

substrate_name: 3-(methylthio)acryloyl-CoA (for CoA ester hydrolysis)

assay_conditions_summary: cofactor CoA

column_label: Table 2 row CoA ester hydrolysis; substrate MTA-CoA; Wild-type DmdD Km (uM) = 8.2 +/- 2.0

row_label: CoA ester hydrolysis / MTA-CoA

table_label: Table 2

enzyme: methylthioacryloyl-CoA hydratase


substrate_name: 3-(methylthio)propanoyl-CoA (for CoA ester hydrolysis)

column_label: Table 2 row CoA ester hydrolysis; substrate MMPA-CoA; Wild-type DmdD Km (uM) = 69.0 +/- 16.4

row_label: CoA ester hydrolysis / MMPA-CoA


substrate_name: 3-hydroxybutyryl-CoA (for CoA ester hydrolysis)

column_label: Table 2 row CoA ester hydrolysis; substrate 3-hydroxybutyryl-CoA; Wild-type DmdD Km (uM) = 119 +/- 20

row_label: CoA ester hydrolysis / 3-hydroxybutyryl-CoA


substrate_name: crotonyl-CoA (for hydration)

column_label: Table 2 row Hydration; substrate Crotonyl-CoA; Wild-type DmdD Km (uM) = 19.0 +/- 3.1

row_label: Hydration / Crotonyl-CoA

substrate: crotonyl-CoA (for hydration)


enzyme_display_name: (R)-3-(aryl)lactoyl-CoA dehydratase

organism: Clostridium sporogenes

substrate_name: (E)-cinnamoyl-CoA (at pH 8 and 20 degrees Celsius)

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: kcat is 1 sec(-1) (at pH 8 and 20 degrees Celsius). Values have been measured with the FldABC complex.

enzyme: (R)-3-(aryl)lactoyl-CoA dehydratase


substrate_name: cinnamoyl-CoA (at pH 8 and 20 degrees Celsius)


substrate_name: cis-aconitate

substrate: cis-aconitate


organism: Amycolatopsis sp.

proof_lines: kcat is 110 sec(-1) with N-succinyl-R/S-methionine as substrate (PubMed:14705949). kcat is 190 sec(-1) with N-succinyl-R/S-phenylglycine as substrate (PubMed:14705949). kcat is 42 sec(-1) with N-succinyl-L-phenylglycine as substrate (PubMed


enzyme_display_name: ectoine synthase

organism: Sphingopyxis alaskensis

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

column_label: PLOS PDF page 11 lines 566-580; section label Kinetic parameters of EctC for N-gamma-ADABA and N-alpha-ADABA; N-gamma-ADABA prose; metric labels apparent Km, kcat, and catalytic efficiency kcat/Km.

normalized_value_unit_evidence: kcat=7.2 s^-1; Km=4.9 mM; kcat/Km=1.4693877551020407 s^-1 mM^-1 from central values 7.2/4.9; source rounded efficiency=1.47 mM^-1 s^-1.

raw_value_unit_evidence: Prose reports N-gamma-ADABA Km 4.9 +/- 0.5 mM; kcat 7.2 s^-1; catalytic efficiency 1.47 mM^-1 s^-1.

row_label: N-gamma-ADABA / natural substrate

table_label: Results prose: Kinetic parameters of EctC for N-gamma-ADABA and N-alpha-ADABA

enzyme: ectoine synthase


organism: Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100)

substrate_name: SHCHC

proof_lines: kcat is 17 sec(-1) with SHCHC as substrate.

substrate: SHCHC


organism: Amycolatopsis sp

substrate_name: N-acetyl-L-methionine

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

substrate: N-acetyl-L-methionine


organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)

substrate_name: N-acetyl-D-methionine

proof_lines: kcat is 520 sec(-1) with N-succinyl-L-phenylglycine as substrate (PubMed:24872444). kcat is 8.5 min(-1) with N-acetyl-D-methionine as substrate (PubMed:15313614). kcat is 9.9 min(-1) with N-acetyl-L-methionine as substrate (PubMed:15313614)

substrate: N-acetyl-D-methionine


organism: Echinicola rosea

substrate_name: Polygalacturonate

proof_lines: pH and temperature not specified in the publication


organism: Bifidobacterium dentium

substrate_name: 4-nitrophenyl alpha-D-arabinofuranoside

substrate: 4-nitrophenyl alpha-D-arabinofuranoside


substrate_name: difructose dianhydride I

substrate: difructose dianhydride I


substrate_name: Inulobiose

substrate: Inulobiose


proof_lines: kcat is 122 sec(-1) with SHCHC as substrate.


substrate_name: (R)-homocitrate (at 60 degrees Celsius)

substrate: (R)-homocitrate (at 60 degrees Celsius)


organism: Selaginella moellendorffii

proof_lines: kcat is 193.5 sec(-1) with (13S)-hydroperoxy-(9Z,11E)-octadecadienoate as substrate (PubMed:26776054). kcat is 266.7 sec(-1) with (13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate as substrate (PubMed:26776054).


smiles: CCC=CCC(C=CC=CCCCCCCCC(=O)[O-])OO


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

proof_lines: kcat is 261.1 sec(-1) with (13S)-hydroperoxy-(9Z,11E)-octadecadienoate as substrate (PubMed:26776054). kcat is 185.3 sec(-1) with (13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate as substrate (PubMed:26776054).


enzyme_display_name: enoyl-CoA hydratase 2

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: dodecenoyl-CoA

proof_lines: kcat is 45 sec(-1) with dodecenoyl-CoA as substrate.

enzyme: enoyl-CoA hydratase 2

substrate: dodecenoyl-CoA


enzyme_display_name: 3-dehydroshikimate dehydratase

organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

enzyme: 3-dehydroshikimate dehydratase


enzyme_display_name: cyanase

organism: Sordaria macrospora

substrate_name: Cyanate

enzyme: cyanase

substrate: Cyanate


enzyme_display_name: linalool dehydratase

organism: Castellaniella defragrans

substrate_name: linalool

proof_lines: kcat is 4.37 min(-1) for linalool dehydration. kcat is 9.0 min(-1) for beta-myrcene hydration. kcat is 1.66 min(-1) for geraniol isomerization.

source_databases_merged: brenda skid uniprot

enzyme: linalool dehydratase

substrate: linalool


enzyme_display_name: phosphomevalonate dehydratase

organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)

substrate_name: tAHMP

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

assay_conditions_summary: pH 7; 343.15 K; buffer 70 mM Tris-HCl

column_label: Results prose referring to Supplementary Figure 4 states: Km 18.3 uM and kcat 15.2 s^-1 for reconstructed ApPMDh with tAHMP as substrate.

normalized_value_unit_evidence: tAHMP Km 18.3 uM normalized to 0.0183 mM; CatLog Km = 0.0183 mM.

raw_value_unit_evidence: The Results prose states the reconstructed ApPMDh Km for tAHMP as 18.3 uM and kcat as 15.2 s^-1.

row_label: Reconstructed Aeropyrum pernix phosphomevalonate dehydratase assayed with tAHMP

table_label: Results prose; Supplementary Figure 4 kinetic study of reconstructed ApPMDh

enzyme: phosphomevalonate dehydratase

substrate: tAHMP


enzyme_display_name: squalene--hopanol cyclase

organism: Alicyclobacillus acidocaldarius

substrate_name: squalene

proof_lines:
pH 6.0, 60°C
kcat is 72 min(-1).

enzyme: squalene--hopanol cyclase

substrate: squalene


enzyme_display_name: heparin lyase

organism: Pedobacter heparinus

substrate_name: heparin

sequence_variant_note: Mutation signature I133T/P316T could not be applied safely because the resolved sequence does not match the expected reference residue(s).

enzyme: heparin lyase

substrate: heparin


enzyme_display_name: pectate disaccharide-lyase

organism: Pectobacterium carotovorum

substrate_name: trigalacturonate

enzyme: pectate disaccharide-lyase

substrate: trigalacturonate


organism: Escherichia coli (strain K12)

substrate_name: methylglyoxal

smiles: CC(=O)C=O

column_label: Abstract reports Hsp31 exhibits Michaelis-Menten kinetics for methylglyoxal with K(m) and k(cat) of 1.43+/-0.12 mM and 156.9+/-5.5 min(-1), respectively.

raw_value_unit_evidence: Km raw_value=1.43+/-0.12 mM raw_unit=mM

row_label: Escherichia coli K-12 Hsp31 glyoxalase III / methylglyoxal

table_label: PubMed XML abstract PMID 21696459

substrate: methylglyoxal


organism: Bacillus subtilis (strain 168)

substrate_name: ADP

assay_conditions_summary: cofactor ADP

proof_lines: kcat is 0.35 sec(-1) for the ADP-dependent dehydration of NADHX.

substrate: ADP


organism: Ranunculus acris

smiles: CCCCCC(C=CC=CCCCCCCCC(=O)O)OO


enzyme_display_name: mannuronate-specific alginate lyase

organism: Bacteroides cellulosilyticus

substrate_name: alginate

proof_lines:
at pH 7.5 and 30°C
at pH 7.3 and 37°C

enzyme: mannuronate-specific alginate lyase

substrate: alginate


substrate_name: poly(beta-(1->4)-D-mannuronic acid)

substrate: poly(beta-(1->4)-D-mannuronic acid)


organism: Bacillus weihaiensis


organism: Flammeovirga sp. NJ-04

proof_lines:
pH 7.0, 50°C
at pH 9.0 and 45°C


organism: Saccharophagus degradans

substrate_name: sodium alginate

substrate: sodium alginate


enzyme_display_name: pectin lyase

organism: Curvularia inaequalis

substrate_name: Pectin

enzyme: pectin lyase

substrate: Pectin


organism: Wenyingzhuangia fucanilytica


organism: Persicobacter sp. CCB-QB2

mutation_type: truncation

proof_lines: truncated protein lacking both the CBM16 and CBM32 domains, pH 7.0, 23°C


proof_lines: truncated protein lacking the CBM16 domain, pH 7.0, 23°C


organism: Isoptericola halotolerans

substrate_name: poly(alpha-(1,4)-L-guluronic acid)

substrate: poly(alpha-(1,4)-L-guluronic acid)


enzyme_display_name: guluronate-specific alginate lyase

enzyme: guluronate-specific alginate lyase


enzyme_display_name: exo-(1->4)-alpha-D-glucan lyase

organism: Gracilariopsis chorda

substrate_name: glycogen

enzyme: exo-(1->4)-alpha-D-glucan lyase

substrate: glycogen


substrate_name: amylopectin

proof_lines: pH 5.0, 35°C, barley amylopectin or potato amylopectin

substrate: amylopectin


substrate_name: maltotetraose

substrate: maltotetraose


substrate_name: maltopentaose

substrate: maltopentaose


substrate_name: maltohexaose

substrate: maltohexaose


substrate_name: maltoheptaose

substrate: maltoheptaose


substrate_name: maltotriose

substrate: maltotriose


substrate_name: maltose

substrate: maltose


enzyme_display_name: oligogalacturonide lyase

organism: Erwinia aroidea

substrate_name: unsaturated digalacturonic acid

enzyme: oligogalacturonide lyase

substrate: unsaturated digalacturonic acid


substrate_name: digalacturonic acid

substrate: digalacturonic acid


organism: Vibrio xiamenensis


mutation_signature: truncated enzyme TM1

proof_lines: truncated enzyme TM1, at pH 7.3 and 40°C


mutation_signature: truncated enzyme TM2

proof_lines: truncated enzyme TM2, at pH 7.3 and 40°C


enzyme_display_name: glucuronan lyase

organism: Trichoderma harzianum

substrate_name: deacetylated glucuronan

enzyme: glucuronan lyase

substrate: deacetylated glucuronan


proof_lines: fusion construct with linker 1, pH 5.5, 25°C

proof_lines: fusion construct with linker 2, pH 5.5, 25°C

proof_lines: fusion construct without linker, pH 5.5, 25°C


organism: Flavobacterium sp.

proof_lines: recombinant His-tagged enzyme, pH 8.5, 45°C


organism: Fusarium lateritium

substrate_name: citrus pectin

substrate: citrus pectin


organism: Marinimicrobium sp. H1

proof_lines: recombinant enzyme AlgH-II, at pH 10.0 and 45°C

proof_lines: recombinant enzyme AlgH-I, at pH 10.0 and 45°C


organism: Pseudomonas aeruginosa

substrate_name: acetylated alginate

substrate: acetylated alginate


substrate_name: alginate

substrate: alginate


organism: Microbulbifer sp. BY17

substrate_name: poly(beta-(1->4)-D-mannuronic acid)

proof_lines:
at pH 8.9 and 43°C
at pH and ?C

substrate: poly(beta-(1->4)-D-mannuronic acid)


organism: Microbulbifer sp. ALW1


organism: Vibrio splendidus


organism: Zobellia galactanivorans

substrate_name: sodium alginate

proof_lines: with L-guluronate content of 66.7%, pH 7.5, 30°C, recombinant enzyme

proof_lines: with L-guluronate content of 52.6%, pH 7.5, 30°C, recombinant enzyme

proof_lines: with L-guluronate content of 33.3%, pH 7.5, 30°C, recombinant enzyme

substrate: sodium alginate


organism: Paenarthrobacter ureafaciens

substrate_name: inulin

substrate: inulin


organism: Trichoderma parareesei

substrate_name: glucuronan

proof_lines:
isoform PL20A, at pH 6.0 and 30°C
isoform PL20B, at pH 6.0 and 30°C
isoform PL38A, at pH 6.0 and 30°C

substrate: glucuronan


organism: Rubrivirga marina

substrate_name: poly(alpha-(1->4)-L-guluronic acid)

substrate: poly(alpha-(1->4)-L-guluronic acid)


organism: Leifsonia sp. T88-4


organism: Microbacterium sp. S48-1


organism: Saccharophagus degradans


organism: Thalassotalea algicola


organism: Littorina sp.


organism: Pseudarthrobacter chlorophenolicus


enzyme_display_name: chondroitin AC lyase

organism: Paenarthrobacter aurescens

substrate_name: chondroitin 4-sulfate

enzyme: chondroitin AC lyase

substrate: chondroitin 4-sulfate


organism: Niallia circulans

substrate_name: heparan sulfate

substrate: heparan sulfate


enzyme_display_name: pectate lyase

organism: Penicillium occitanis (nom. inval.)

substrate_name: polygalacturonic acid

enzyme: pectate lyase

substrate: polygalacturonic acid


enzyme_display_name: o-succinylbenzoate synthase

organism: Amycolatopsis sp

proof_lines: kcat is 110 sec(-1) with N-succinyl-R/S-methionine as substrate (PubMed:14705949). kcat is 190 sec(-1) with N-succinyl-R/S-phenylglycine as substrate (PubMed:14705949). kcat is 42 sec(-1) with N-succinyl-L-phenylglycine as substrate (PubMed

enzyme: o-succinylbenzoate synthase


enzyme_display_name: etheroleic acid synthase

organism: Allium sativum

proof_lines: kcat is 550 sec(-1) with (13S)-hydroperoxy-(9Z,11E)-octadecadienoate as substrate (PubMed:18326559). kcat is 40 sec(-1) with (13S)-hydroperoxy-(9Z,11E,15Z)-octadecatrienoate as substrate (PubMed:18326559). kcat is 70 sec (-1) with (9S)-hydr

enzyme: etheroleic acid synthase


organism: Pseudopedobacter saltans

substrate_name: heparin

substrate: heparin


organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)

substrate_name: tAHMP

proof_lines: kcat is 15.2 sec(-1) with tAHMP as substrate.

substrate: tAHMP


organism: Exiguobacterium sp.


organism: Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)

substrate_name: SHCHC

proof_lines: kcat is 80 sec(-1) with SHCHC as substrate.

substrate: SHCHC


organism: Staphylococcus aureus (strain COL)

column_label: Supporting Information PDF page 9, Table S1, Staphylococcus aureus row, OSBS Km (uM) column: 287 +/- 60.

row_label: Staphylococcus aureus


enzyme_display_name: 3-hydroxypropionyl-CoA dehydratase

organism: Metallosphaera sedula

assay_conditions_summary: pH 8.6; 338.15 K; cofactor CoA

proof_lines:
pH 8.6, 65°C
recombinant enzyme, pH 6.5, 65°C
42°C, pH 7.8

enzyme: 3-hydroxypropionyl-CoA dehydratase


organism: Desulfotalea psychrophila (strain LSv54 / DSM 12343)

column_label: Supporting Information PDF page 9, Table S1, Desulfotalea psychrophila row, OSBS Km (uM) column: 15 +/- 3.

raw_value_unit_evidence: OSBS Km=15 +/- 3 uM.

row_label: Desulfotalea psychrophila


enzyme_display_name: N-acetylmuramic acid 6-phosphate etherase

organism: Escherichia coli (strain K12)

substrate_name: N-acetylmuramic acid 6-phosphate

substrate: N-acetylmuramic acid 6-phosphate


enzyme_display_name: enoyl-CoA hydratase 2

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

substrate_name: crotonyl-CoA

proof_lines: kcat is 728 sec(-1) with crotonyl-CoA as substrate. kcat is 204 sec(-1) with trans-2,3-pentenoyl-CoA as substrate. kcat is 252 sec(-1) with trans-2,3-hexenoyl-CoA as substrate.

enzyme: enoyl-CoA hydratase 2

substrate: crotonyl-CoA


organism: Vibrio splendidus

proof_lines:
isoform OalC, at pH 7.5 and 35°C
isoform OalA, at pH 6.5 and 16°C


substrate_name: N-succinyl-L-phenylglycine

substrate: N-succinyl-L-phenylglycine


organism: Aspergillus flavus


enzyme_display_name: linalool dehydratase

organism: Castellaniella defragrans (strain DSM 12143 / CCUG 39792 / 65Phen)

substrate_name: beta-myrcene

proof_lines: kcat is 4.37 min(-1) for linalool dehydration. kcat is 9.0 min(-1) for beta-myrcene hydration. kcat is 1.66 min(-1) for geraniol isomerization.

enzyme: linalool dehydratase

substrate: beta-myrcene


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

column_label: PMID 16963641 Activity measurements prose, wild-type Rv0130 / crotonoyl-CoA, KM = 55 uM.

raw_value_unit_evidence: Activity measurements prose reports KM = 55 uM for crotonoyl-CoA.

row_label: wild-type Rv0130 / crotonoyl-CoA (2-butenoyl-CoA)

table_label: Activity measurements prose


enzyme_display_name: D-lactate dehydratase

organism: Escherichia coli

substrate_name: methylglyoxal

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H184A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, temperature not specified in the publication, mutant enzyme H184A

enzyme: D-lactate dehydratase

substrate: methylglyoxal


substrate_name: alginate

proof_lines:
pH 8.5, 25°C
pH 7.5, 25°C
at pH 7.5 and 35°C

substrate: alginate


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

column_label: Abstract reports purified Glx3p has an in vitro methylglyoxalase activity (Km = 5.5 mM and kcat = 7.8 s(-1)).

raw_value_unit_evidence: Km raw_value=5.5 mM raw_unit=mM

row_label: Candida albicans Glx3p / methylglyoxal

table_label: PubMed XML abstract PMID 24302734


substrate_name: geraniol

smiles: CC(=CCCC(=CCO)C)C

substrate: geraniol


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 75.0 min(-1) with methylglyoxal as substrate.


enzyme_display_name: xanthan lyase

organism: Bacillus sp. GL1

substrate_name: Xanthan

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R313A to reconstruct the assayed variant sequence.

enzyme: xanthan lyase

substrate: Xanthan


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y315F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R612A to reconstruct the assayed variant sequence.


enzyme_display_name: (+)-caryolan-1-ol synthase

organism: Streptomyces griseus subsp. griseus (strain JCM 4626 / CBS 651.72 / NBRC 13350 / KCC S-0626 / ISP 5235)

substrate_name: farnesyl diphosphate (at pH 7.5 and 30 degrees Celsius)

proof_lines: kcat is 0.025 sec(-1) for (+)-caryolan-1-ol formation (at pH 7.5 and 30 degrees Celsius).

enzyme: (+)-caryolan-1-ol synthase


enzyme_display_name: mannuronate-specific alginate lyase

organism: Defluviitalea phaphyphila

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

proof_lines: mutant enzyme D238E, in the absence of Ca2+, at pH 6.5 and 75°C

proof_lines: mutant enzyme D238E, in the presence of 2.5 mM Ca2+, at pH 6.5 and 75°C


proof_lines: wild type enzyme, in the absence of Ca2+, at pH 6.5 and 75°C

proof_lines: wild type enzyme, in the presence of 2.5 mM Ca2+, at pH 6.5 and 75°C


enzyme_display_name: 3-amino-5-hydroxybenzoate synthase

organism: Amycolatopsis mediterranei

proof_lines: kcat is 6.82 sec(-1) for AHBA synthase activity.

enzyme: 3-amino-5-hydroxybenzoate synthase


enzyme_display_name: 2-methylfumaryl-CoA hydratase

organism: Chloroflexus aurantiacus

assay_conditions_summary: 328.15 K; cofactor CoA

proof_lines: 55°C, pH not specified in the publication, dehydration of erythro-beta-methylmalyl-CoA to mesaconyl-CoA

enzyme: 2-methylfumaryl-CoA hydratase


organism: Methylorubrum extorquens

substrate_name: formaldehyde

smiles: C=O

proof_lines: The KM for H(4)MPT is higher than 60 uM.

substrate: formaldehyde


enzyme_display_name: gluconate/galactonate dehydratase

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

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

proof_lines: kcat is 10.4 sec(-1) for gluconate and 1.08 sec(-1) for galactonate (at 70 degrees Celsius and pH 6). kcat is 12.6 sec(-1) for gluconate (at 78 degrees Celsius and pH 7).

enzyme: gluconate/galactonate dehydratase


organism: Pseudomonas aeruginosa

substrate_name: UDP-N-acetylglucosamine

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

assay_conditions_summary: pH 10

proof_lines: pH 10.0, 30°C, recombinant soluble truncated WbpM mutant His-S262

substrate: UDP-N-acetylglucosamine


organism: Cereibacter sphaeroides

proof_lines: 30°C, pH not specified in the publication, dehydration of erythro-beta-methylmalyl-CoA to mesaconyl-CoA


enzyme_display_name: 3-methylfumaryl-CoA hydratase

organism: Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)

proof_lines: kcat is 1045 sec(-1) for hydratase activity with 3-methylfumaryl-CoA (at 45 degrees Celsius).

enzyme: 3-methylfumaryl-CoA hydratase


enzyme_display_name: L-talarate dehydratase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: L-talarate

proof_lines: kcat is 2.1 sec(-1) with L-talarate as substrate (PubMed:17649980). kcat is 3.6 sec(-1) with galactarate as substrate (PubMed:17649980). kcat is 4.8 sec(-1) with galactarate as substrate (PubMed:29248502).

enzyme: L-talarate dehydratase

substrate: L-talarate


enzyme_display_name: chorismate dehydratase

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

substrate_name: chorismate

enzyme: chorismate dehydratase

substrate: chorismate


organism: Oceanobacillus iheyensis

substrate_name: galactarate

proof_lines:
pH 8.0, 30°C
Raw SKiD Env: Temp=30°C, pH=8
kcat is 6.8 sec(-1).

substrate: galactarate


organism: Saccharopolyspora spinosa

proof_lines: kcat is 2.6 min(-1) for dTDP-4-keto-2,6-dideoxy-alpha-D-glucose as substrate.


organism: Saccharolobus solfataricus

substrate_name: D-galactonate

substrate: D-galactonate


organism: Bacillus sp. (in: firmicutes)

substrate_name: inulin

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

substrate: inulin


enzyme_display_name: (2S)-3-sulfopropanediol dehydratase

organism: Klebsiella oxytoca

enzyme: (2S)-3-sulfopropanediol dehydratase


enzyme_display_name: guluronate-specific alginate lyase

organism: Persicobacter sp. CCB-QB2

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

proof_lines: truncated protein lacking both the CBM16 and CBM32 domains, pH 7.0, 23°C

enzyme: guluronate-specific alginate lyase


proof_lines: truncated protein lacking the CBM16 domain, pH 7.0, 23°C


enzyme_display_name: pectin lyase

organism: Aspergillus terricola

substrate_name: Pectin

enzyme: pectin lyase

substrate: Pectin


enzyme_display_name: trans-4-hydroxy-L-proline dehydratase

organism: Clostridioides difficile

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

proof_lines: kcat is 45 sec(-1) for trans-4-hydroxy-L-proline as substrate.

enzyme: trans-4-hydroxy-L-proline dehydratase


organism: Streptomyces peucetius subsp. caesius


proof_lines:
wild-type
30°C, pH 5.5, wild-type enzyme


organism: Bacillus sp. (strain GL1)

substrate_name: xanthan

substrate: xanthan


organism: Yersinia pseudotuberculosis

substrate_name: GDP-4-keto-6-deoxy-D-mannose (at pH 7 and 37 degrees Celsius)

proof_lines: kcat is 0.6 sec(-1) (at pH 7 and 37 degrees Celsius).


substrate_name: L-glutamate (at pH 7 and 37 degrees Celsius)

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


enzyme_display_name: galactonate dehydratase

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

substrate_name: gluconate

enzyme: galactonate dehydratase

substrate: gluconate


organism: Vibrio sp. NJ-04


organism: Zobellia galactanivorans

substrate_name: sodium alginate

substrate: sodium alginate


enzyme_display_name: crotonobetainyl-CoA hydratase

organism: Escherichia coli

substrate_name: H2O; Crotonobetainyl-CoA

enzyme: crotonobetainyl-CoA hydratase

substrate: H2O; Crotonobetainyl-CoA


organism: Proteus sp. (in: enterobacteria)

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


enzyme_display_name: short-chain-enoyl-CoA hydratase

organism: Clostridium acetobutylicum

substrate_name: H2O; Crotonoyl-CoA

enzyme: short-chain-enoyl-CoA hydratase

substrate: H2O; Crotonoyl-CoA


organism: Homo sapiens


enzyme_display_name: (R)-2-hydroxyisocaproyl-CoA dehydratase

enzyme: (R)-2-hydroxyisocaproyl-CoA dehydratase


enzyme_display_name: pectate lyase

organism: Massilia eurypsychrophila

substrate_name: polygalacturonic acid

enzyme: pectate lyase

substrate: polygalacturonic acid


organism: Streptomyces nitrosporeus

substrate_name: pentagalacturonic acid

substrate: pentagalacturonic acid


organism: Microbulbifer sp. 6532A

substrate_name: poly(alpha-(1->4)-L-guluronic acid)

proof_lines:
at pH 8.0 and 50°C
at pH 8.0 and 35°C

enzyme: mannuronate-specific alginate lyase

substrate: poly(alpha-(1->4)-L-guluronic acid)


organism: Paenibacillus sp. FPU-7


organism: Vibrio sp. Ni1

proof_lines:
at pH 8.0 and 35°C
at pH and ?C
at pH 9.0 and 40°C


enzyme_display_name: heparin lyase

organism: Pedobacter heparinus

substrate_name: H2O; m n n+m m n n+m n m n+m n m n+m m n n+m m n n+m m n n+m m n n+m n m n+m m n n+m m n n+m m n n+m n m n+m m n n+m Heparin

enzyme: heparin lyase


organism: Aspergillus terricola

substrate_name: citrus pectin

substrate: citrus pectin


organism: Isoptericola halotolerans


organism: Saccharophagus degradans


enzyme_display_name: anhydrosialidase

organism: Macrobdella decora

enzyme: anhydrosialidase


organism: Streptomyces davaonensis


organism: Bacillus subtilis

substrate_name: tetragalacturonate

substrate: tetragalacturonate


organism: Sphingobacterium sp.

substrate_name: N-acetyl-de-O-sulfated heparin

substrate: N-acetyl-de-O-sulfated heparin


enzyme_display_name: heparin-sulfate lyase

organism: Bacteroides stercoris

substrate_name: Heparin

enzyme: heparin-sulfate lyase

substrate: Heparin


organism: Bacteroides thetaiotaomicron

substrate_name: Heparan sulfate

substrate: Heparan sulfate


organism: Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1)

substrate_name: ulvan

substrate: ulvan


enzyme_display_name: pectate disaccharide-lyase

organism: Pectobacterium carotovorum

substrate_name: polygalacturonate I

enzyme: pectate disaccharide-lyase

substrate: polygalacturonate I


enzyme_display_name: cis-L-3-hydroxyproline dehydratase

organism: Agrobacterium tumefaciens

enzyme: cis-L-3-hydroxyproline dehydratase


enzyme_display_name: cyclohexyl-isocyanide hydratase

organism: Pseudomonas putida

substrate_name: Unknown

enzyme: cyclohexyl-isocyanide hydratase

substrate: Unknown


enzyme_display_name: cyanase

organism: Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell)

enzyme: cyanase


enzyme_display_name: ectoine synthase

organism: Halomonas elongata

substrate_name: L-homoectoine

proof_lines: pH 9.5, 15°C, in presence of 0.77 M NaCl

proof_lines: pH 9.5, 15°C, in presence of 0.05 M NaCl

enzyme: ectoine synthase

substrate: L-homoectoine


organism: Sphingopyxis alaskensis

proof_lines:
pH 8.5, 15°C, recombinant enzyme
Raw SKiD Env: Temp=15°C, pH=8.5


organism: Bacillus subtilis (strain 168)


organism: Homo sapiens


enzyme_display_name: bile-acid 7alpha-dehydratase

organism: Clostridium scindens (strain JCM 10418 / VPI 12708)

enzyme: bile-acid 7alpha-dehydratase


substrate_name: trans-Dec-2-enoyl-CoA; H2O

substrate: trans-Dec-2-enoyl-CoA; H2O


enzyme_display_name: 3-dehydroshikimate dehydratase

organism: Bacillus anthracis

enzyme: 3-dehydroshikimate dehydratase


organism: Neurospora crassa


enzyme_display_name: enoyl-CoA hydratase 2

organism: Aeromonas caviae

substrate_name: Crotonoyl-CoA; H2O

enzyme: enoyl-CoA hydratase 2

substrate: Crotonoyl-CoA; H2O


substrate_name: H2O; trans-Hex-2-enoyl-CoA

substrate: H2O; trans-Hex-2-enoyl-CoA


organism: Clostridioides difficile


organism: Amycolatopsis orientalis

substrate_name: dTDP-glucose

substrate: dTDP-glucose


enzyme_display_name: hyaluronate lyase

organism: Streptococcus pneumoniae

substrate_name: Hyaluronate

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

enzyme: hyaluronate lyase

substrate: Hyaluronate


organism: Streptococcus pyogenes

substrate_name: H2O; Hyaluronate

substrate: H2O; Hyaluronate


organism: Streptococcus pyogenes phage


organism: Thermasporomyces composti

substrate_name: hyaluronate

substrate: hyaluronate


enzyme_display_name: tryptophan synthase (indole-salvaging)

organism: Thermotoga maritima

substrate_name: Indole; O-Phospho-L-serine

enzyme: tryptophan synthase (indole-salvaging)

substrate: Indole; O-Phospho-L-serine


enzyme_display_name: tetrahymanol synthase

organism: Tetrahymena thermophila (strain SB210)

substrate_name: sqna!ene

enzyme: tetrahymanol synthase

substrate: sqna!ene


enzyme_display_name: carotenoid 1,2-hydratase

organism: Rhodobacter capsulatus

substrate_name: H2O; Neurosporene

enzyme: carotenoid 1,2-hydratase

substrate: H2O; Neurosporene


organism: Rubrivivax gelatinosus

substrate_name: Neurosporene; H2O

substrate: Neurosporene; H2O


organism: Escherichia coli (strain K12)

substrate_name: (S)-NADHX

substrate: (S)-NADHX


organism: Methylobacterium extorquens


organism: Pseudomonas aeruginosa


organism: Roseibium aggregatum (strain ATCC 25650 / DSM 13394 / JCM 20685 / NBRC 16684 / NCIMB 2208 / IAM 12614 / B1)

proof_lines: kcat is 14 sec(-1) for c3LHyp epimerization, and 9 sec(-1) for c3LHyp dehydration.


organism: Drosophila melanogaster

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: pH 7.5, 22°C, recombinant full-length enzyme

proof_lines: Catalytic efficiency is similar using full-length protein or the individual (3R)-hydroxyacyl-CoA dehydrogenase and enoyl-CoA hydratase 2 domains in a 1:1 mixture.


enzyme_display_name: mannuronate-specific alginate lyase

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

substrate_name: alginate (dp value of 263)

proof_lines: kcat is 32 sec(-1) for the depolymerization of mannuronan (dp value of 133). kcat is 1.5 sec(-1) for the depolymerization of acetylated mannuronan (dp value of 133). kcat is 32 sec(-1) for the depolymerization of alginate (dp value of 263).

substrate: alginate (dp value of 263)


organism: Hypocrea jecorina (strain QM6a)

substrate_name: cis-3-hydroxy-L-proline (at pH 8.0)

proof_lines: kcat is 535 min(-1). kcat/KM is 22.8 min(-1) mM(-1).

substrate: cis-3-hydroxy-L-proline (at pH 8.0)


organism: Stenotrophomonas maltophilia

substrate_name: alginate

proof_lines: at pH 8.5, temperature not specified in the publication

substrate: alginate


enzyme_display_name: acetylene hydratase

organism: Syntrophotalea acetylenica

substrate_name: Unknown

enzyme: acetylene hydratase

substrate: Unknown


enzyme_display_name: o-succinylbenzoate synthase

organism: Amycolatopsis sp

substrate_name: N-succinyl-R-methionine

proof_lines: kcat is 110 sec(-1) with N-succinyl-R/S-methionine as substrate (PubMed:14705949). kcat is 190 sec(-1) with N-succinyl-R/S-phenylglycine as substrate (PubMed:14705949). kcat is 42 sec(-1) with N-succinyl-L-phenylglycine as substrate (PubMed

enzyme: o-succinylbenzoate synthase

substrate: N-succinyl-R-methionine


organism: Bacillus subtilis (strain 168)

proof_lines: kcat is 150 sec(-1) with SHCHC as substrate.


proof_lines: kcat is 19 sec(-1) with SHCHC as substrate.


organism: Geobacillus kaustophilus

substrate_name: N-succinyl-D-alanine

proof_lines: kcat is 43 sec(-1) with N-succinyl-L-alanine as substrate. kcat is 15 sec(-1) with N-succinyl-D-alanine as substrate. kcat is 5 sec(-1) with N-succinyl-L-phenylalanine as substrate. kcat is 2 sec(-1) with N-succinyl-D-phenylalanine as subst

substrate: N-succinyl-D-alanine


organism: Geobacillus stearothermophilus

substrate_name: N-formyl-D-aminobutyric acid

proof_lines: kcat is 74.6 sec(-1) with N-formyl-D-methionine as substrate. kcat is 52.9 sec(-1) with N-formyl-L-methionine as substrate. kcat is 12.3 sec(-1) with N-formyl-D-norleucine as substrate. kcat is 8.0 sec(-1) with N-formyl-L-norleucine as subs

substrate: N-formyl-D-aminobutyric acid


organism: Rhodospirillum rubrum

substrate_name: Crotonoyl-CoA; H2O

proof_lines: kcat is 728 sec(-1) with crotonyl-CoA as substrate. kcat is 204 sec(-1) with trans-2,3-pentenoyl-CoA as substrate. kcat is 252 sec(-1) with trans-2,3-hexenoyl-CoA as substrate.

substrate: Crotonoyl-CoA; H2O


enzyme_display_name: colneleate synthase

organism: Solanum tuberosum

enzyme: colneleate synthase


enzyme_display_name: linalool dehydratase

organism: Castellaniella defragrans (strain DSM 12143 / CCUG 39792 / 65Phen)

proof_lines: kcat is 4.37 min(-1) for linalool dehydration. kcat is 9.0 min(-1) for beta-myrcene hydration. kcat is 1.66 min(-1) for geraniol isomerization.

enzyme: linalool dehydratase


organism: Thiocapsa roseopersicina


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


substrate_name: NADHX

proof_lines: kcat is 0.35 sec(-1) for the ADP-dependent dehydration of NADHX.

substrate: NADHX


organism: Escherichia coli


enzyme_display_name: pterocarpan synthase

organism: Glycyrrhiza echinata

enzyme: pterocarpan synthase


enzyme_display_name: gluconate/galactonate dehydratase

organism: Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)

enzyme: gluconate/galactonate dehydratase


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

proof_lines: kcat is 10.4 sec(-1) for gluconate and 1.08 sec(-1) for galactonate (at 70 degrees Celsius and pH 6). kcat is 12.6 sec(-1) for gluconate (at 78 degrees Celsius and pH 7).


enzyme_display_name: 5'-oxoaverantin cyclase

organism: Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1)

enzyme: 5'-oxoaverantin cyclase


enzyme_display_name: versicolorin B synthase

organism: Aspergillus parasiticus

enzyme: versicolorin B synthase


organism: Methanosarcina barkeri (strain Fusaro / DSM 804)


enzyme_display_name: 2-methylfumaryl-CoA hydratase

organism: Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM B-1755)

enzyme: 2-methylfumaryl-CoA hydratase


organism: Danio rerio


organism: Homo sapiens

proof_lines: kcat is 0.15 min(-1) for retinol, 0.77 min(-1) for retinal, 2.86 min(-1) for 7,12-dimethyltetraphene, 0.48 min(-1) for arachidonic acid.


enzyme_display_name: methanogen homoaconitase

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

substrate_name: cis-homo(2)-aconitate (at 60 degrees Celsius)

proof_lines: kcat is 0.75 sec(-1) for cis-aconitate hydration reaction (PubMed:20170198). Kinetic parameters measured using the HacAB complex.

enzyme: methanogen homoaconitase


substrate: cis-homo(2)-aconitate (at 60 degrees Celsius)


enzyme_display_name: 3-dehydroshikimate dehydratase

organism: Pseudomonas putida


enzyme_display_name: enoyl-CoA hydratase 2

organism: Aeromonas caviae

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature V130G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature L65A to reconstruct the assayed variant sequence.


substrate_name: synthetic fatty acid 9E,11Z,14Z-20:3omega6 (at pH 7.5)

proof_lines: Has a 5 to 10 fold higher activity toward (12R)-HPETE (hydroperoxyeicosatetraenoic acid) compared to (12S)-HPETE and (15S)-HPETE (PubMed:12881489). From (12R)-HPETE produces a stereoisomer of hepoxilin A3 (PubMed:12881489). More active on h


organism: Sus scrofa


enzyme_display_name: tetracenomycin F2 cyclase

organism: Streptomyces glaucescens

enzyme: tetracenomycin F2 cyclase


enzyme_display_name: cis-L-3-hydroxyproline dehydratase

organism: Agrobacterium fabrum (strain C58 / ATCC 33970)

enzyme: cis-L-3-hydroxyproline dehydratase


organism: Hypocrea jecorina (strain QM6a)


enzyme_display_name: pectate lyase

organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)

proof_lines: kcat is 280 sec(-1) for homogalacturonan (HG) (at 45 degrees Celsius and at pH 8) (PubMed:35802235). kcat is 357 sec(-1) for apple pectin (at 45 degrees Celsius and at pH 8) (PubMed:35802235). kcat is 272 sec(-1) for citrus peel pectin (at

enzyme: pectate lyase


organism: Paenibacillus barcinonensis


organism: Zinnia elegans


organism: Defluviitalea phaphyphila

substrate_name: poly(beta-(1->4)-D-mannuronic acid)

enzyme: mannuronate-specific alginate lyase

substrate: poly(beta-(1->4)-D-mannuronic acid)


organism: Pseudoalteromonas sp. SM0524

substrate_name: sodium alginate

sequence_variant_note: Mutation signature E226K/I211T/R294V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme E226K/I211T/R294V, at pH 7.0 and 50°C

substrate: sodium alginate


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +6, so it is treated as a source-provided variant sequence.


enzyme_display_name: hyaluronate lyase

organism: Streptococcus pyogenes phage H4489A

substrate_name: hyaluronic acid

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature Q295E with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

enzyme: hyaluronate lyase

substrate: hyaluronic acid


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature Y298F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


enzyme_display_name: pectin lyase

organism: Bacillus subtilis (strain 168)

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

enzyme: pectin lyase


enzyme_display_name: guluronate-specific alginate lyase

organism: Corynebacterium sp.

substrate_name: saturated deca((1-4)-alpha-L-guluronan)

assay_conditions_summary: pH 7; buffer pH 7

enzyme: guluronate-specific alginate lyase

substrate: saturated deca((1-4)-alpha-L-guluronan)


enzyme_display_name: xanthan lyase

organism: Bacillus sp. GL1

enzyme: xanthan lyase


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


enzyme_display_name: (E)-benzylidenesuccinyl-CoA hydratase

organism: Thauera aromatica

assay_conditions_summary: pH 6.2; 303.15 K; cofactor CoA

enzyme: (E)-benzylidenesuccinyl-CoA hydratase


enzyme_display_name: 2-methylisocitrate dehydratase

organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)

proof_lines: kcat is 19.6 sec(-1) for aconitase activity with citrate as substrate (at pH 8). kcat is 28.9 sec(-1) for aconitase activity with isocitrate as substrate (at pH 8). kcat is 71 sec(-1) for aconitase activity with cis-aconitate as substrate (

enzyme: 2-methylisocitrate dehydratase


organism: Escherichia coli (strain K12)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Stenotrophomonas maltophilia (strain K279a)

substrate_name: poly-GlcA

proof_lines: Vmax for poly-GlcA is about 10-fold greater versus poly-ManA or HA (PubMed:24257754). kcat is 31.9 sec(-1) with poly-GlcA as substrate (at pH 7) (PubMed:24808176). kcat is 3.3 sec(-1) with poly-ManA as substrate (at pH 9) (PubMed:24808176).

substrate: poly-GlcA


enzyme_display_name: mannuronate-specific alginate lyase

substrate_name: mannuronan (dp value of 133)

proof_lines: kcat is 32 sec(-1) for the depolymerization of mannuronan (dp value of 133). kcat is 1.5 sec(-1) for the depolymerization of acetylated mannuronan (dp value of 133). kcat is 32 sec(-1) for the depolymerization of alginate (dp value of 263).

substrate: mannuronan (dp value of 133)


organism: Stenotrophomonas maltophilia

proof_lines: at pH 8.5, temperature not specified in the publication


enzyme_display_name: chondroitin AC lyase

organism: Pedobacter heparinus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R292A to reconstruct the assayed variant sequence.

enzyme: chondroitin AC lyase


proof_lines: recombinant enzyme, pH 8.0, 35°C, dependent on expression system


substrate_name: chondroitin 6-sulfate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y234F to reconstruct the assayed variant sequence.

substrate: chondroitin 6-sulfate


proof_lines:
pH 6.8, 30°C, wild-type enzyme
wild-type enzyme, pH 8.0, 37°C


enzyme_display_name: glucuronan lyase

enzyme: glucuronan lyase


organism: Paenarthrobacter aurescens

substrate_name: inulin

proof_lines:
pH 5.5, 60°C, pressure of 0.1 MPa
pH 5.5, 60°C, pressure of 100 MPa
pH 5.5, 60°C, pressure of 150 MPa

substrate: inulin


organism: Aspergillus luchuensis var. saitoi

substrate_name: Polygalacturonate

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.

substrate: Polygalacturonate


organism: Bacillus sp. (in: firmicutes)

substrate_name: polygalacturonic acid

substrate: polygalacturonic acid


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

proof_lines: pH 10.5, 30°C, mutant enzyme chimeric enzyme composed of Ala1 to Tyr105 of Pel-15 in the N-terminal regions, Asp133 to Arg 159 of pectate lyase B from Fusarium solani in the internal regions, and Gln133 to Tyr197 of Pel-15 in the C-terminal


sequence_variant_note: Mutation signature D80N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Bacillus sp. N16-5


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E241I with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V132F with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K47E/V132F with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K47D/V132F with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K47D/V132F/R272W with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: heparin-sulfate lyase

substrate_name: heparan sulfate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H424A to reconstruct the assayed variant sequence.

enzyme: heparin-sulfate lyase

substrate: heparan sulfate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H234A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H241A with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H110A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H539A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H152A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H139A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


substrate_name: hyaluronate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K130C to reconstruct the assayed variant sequence.

proof_lines: mutant K130C, pH not specified in the publication, temperature not specified in the publication

substrate: hyaluronate


organism: Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)

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

proof_lines: kcat is 94 sec(-1). kcat is 78 sec(-1) with recombinant enzyme.


enzyme_display_name: rhamnogalacturonan endolyase

organism: Acetivibrio thermocellus

substrate_name: potato galactan

mutation_signature: truncated mutant

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

enzyme: rhamnogalacturonan endolyase

substrate: potato galactan


substrate_name: Pectin

substrate: Pectin


organism: Ruminiclostridium cellulolyticum

substrate_name: potato pectic galactan

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

substrate: potato pectic galactan


enzyme_display_name: oligo-alginate lyase

organism: Zobellia galactanivorans

enzyme: oligo-alginate lyase


enzyme_display_name: o-succinylbenzoate synthase

organism: Thermobifida fusca

sequence_variant_note: Resolved canonical sequence from uniprotkb:Q47Q21;rcsb_sifts:2OPJ,2QVH and applied mutation signature R17A/F39A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: Table 2 / T. fusca OSBS / row R17A/F39A / columns kcat (s^-1), K_M (μM), and kcat/K_M (M^-1 s^-1).

normalized_value_unit_evidence: Normalized Table 2 row R17A/F39A: kcat 0.2 s^-1; K_M 0.048 mM; printed Table 2 kcat/K_M 4.2 s^-1 mM^-1 after M^-1-to-mM^-1 unit conversion.

enzyme: o-succinylbenzoate synthase


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q47Q21;rcsb_sifts:2OPJ,2QVH and applied mutation signature R17A/Y42A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

column_label: Table 2 / T. fusca OSBS / row R17A/Y42A / columns kcat (s^-1), K_M (μM), and kcat/K_M (M^-1 s^-1).

normalized_value_unit_evidence: Normalized Table 2 row R17A/Y42A: kcat 0.36 s^-1; K_M 0.038 mM; printed Table 2 kcat/K_M 9.5 s^-1 mM^-1 after M^-1-to-mM^-1 unit conversion.