substrate_name: L-homocysteine

column_label: Table 1: Comparison of the kinetic parameters for the polymorphic variants and pathogenic mutants of CGL (Biochemistry 2008, 47(23):6226-6232); the printed table is transposed: each printed column is one enzyme form and each printed line inside a substrate block is one parameter. Table 1, substrate block 'Hcy', printed variant column 'T67I'; row 'KM, mM' = 8.0; row 'kcat, s-1' = 0.82; row 'kcat/KM' = 0.10. captured primary segment: Table 1 | substrate Hcy | human CGL T67I | KM 8.0 mM | kcat 0.82 s-1 | kcat/KM 0.10 mM-1 s-1 | assay 40 mM borate pH 7.0 lead acetate H2S release, at 37 °C

normalized_value_unit_evidence: KM: printed Table 1 cell 8.0 mM; the printed row head is 'KM, mM', so no unit conversion applies and the paper value is 8.0 mM. kcat: printed Table 1 cell 0.82 s-1; the printed row head is 'kcat, s-1', already per second, so no unit conversion applies and the paper value is 0.82 s^(-1). kcat/KM: printed Table 1 cell 0.10 mM-1 s-1; footnote c states that kcat/KM is expressed in units of mM-1 s-1, which is the canonical unit, so no unit conversion applies and the printed cell is 0.1 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.82 / 8.0 = 0.1025 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.10 mM-1 s-1, which is that quotient written to the place the printed literal carries.

raw_value_unit_evidence: Table 1, substrate block 'Hcy', printed variant column 'T67I': kcat = 0.82 s-1; KM = 8.0 mM; printed kcat/KM = 0.10 mM-1 s-1.

row_label: Table 1, substrate block 'Hcy' (homocysteine), printed variant column 'T67I'

substrate: L-homocysteine


enzyme_display_name: cystathionine gamma-lyase

organism: Homo sapiens

substrate_name: L-cystathionine

source_db: brenda

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S403I to reconstruct the assayed variant sequence.

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

mutation_type: substitution

proof_lines:
for variante S403
for variante I403
for variant S403

data_origin: experimental

enzyme: cystathionine gamma-lyase

substrate: L-cystathionine

source: brenda


mutation_signature: Unknown

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

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


substrate_name: L-cysteine

kcat_over_km_origin: calculated

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

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

assay_conditions_summary: pH 8.2; 310.15 K; buffer 50 mM sodium phosphate

proof_lines: wild type enzyme, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C

substrate: L-cysteine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E339K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E339K, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E339Y to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E339Y, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E339A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E339A, in 50 mM sodium phosphate buffer (pH 8.2) , at 37°C


enzyme_display_name: homocysteine desulfhydrase

organism: Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)

substrate_name: L-methionine

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

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

proof_lines: kcat is 2.90 sec(-1) for the alpha,gamma-elimination of L-methionine. kcat is 1.67 sec(-1) for the alpha,gamma-elimination of L-homocysteine. kcat is 0.03 sec(-1) for the alpha,beta-elimination of L-cysteine.

enzyme: homocysteine desulfhydrase

substrate: L-methionine

source: uniprot


enzyme_display_name: 7-carboxy-7-deazaguanine synthase

organism: Bacillus subtilis (strain 168)

enzyme: 7-carboxy-7-deazaguanine synthase


enzyme_display_name: choline trimethylamine-lyase

organism: Oleidesulfovibrio alaskensis

substrate_name: choline

km_display: Not reported

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T502A to reconstruct the assayed variant sequence.

smiles: C[N+](C)(C)CCO

enzyme: choline trimethylamine-lyase

substrate: choline


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y208F/Y506F to reconstruct the assayed variant sequence.


organism: Brevibacterium aurantiacum

proof_lines: kcat is 15.51 sec(-1) with L-methionine as substrate. kcat is 72.44 sec(-1) with L-homocysteine as substrate.


organism: Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355)

proof_lines: kcat is 0.69 sec(-1) for the production of H(2)S from L-cysteine.


enzyme_display_name: dimethylpropiothetin dethiomethylase

organism: Acinetobacter bereziniae

substrate_name: beta-dimethylsulfoniopropanoate

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: dimethylpropiothetin dethiomethylase

substrate: beta-dimethylsulfoniopropanoate

source: skid


organism: Alcaligenes faecalis

verification_status: unverified

status: unverified


organism: Arabidopsis thaliana

substrate_name: H2O; L-Cystathionine

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

substrate: H2O; L-Cystathionine


organism: Bacillus subtilis

substrate_name: Cystathionine; H2O

substrate: Cystathionine; H2O


substrate_name: H2O; Cystathionine

substrate: H2O; Cystathionine


organism: Escherichia coli

substrate_name: L-Cystine; H2O

substrate: L-Cystine; H2O


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

proof_lines: kcat is 18.25 sec(-1) with dimethylsulfoniopropionate (in the presence of Fe(2+)). kcat is 17.33 sec(-1) with dimethylsulfoniopropionate (in the presence of Mn(2+)).


organism: Pseudomonas putida

proof_lines: kcat is 33.4 sec(-1) for the alpha,gamma-elimination of L-methionine. kcat is 71.0 sec(-1) for the alpha,gamma-elimination of DL-homocysteine. kcat is 2.13 sec(-1) for the alpha,beta-elimination of L-cysteine. kcat is 1.58 sec(-1) for the a


organism: Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)

substrate_name: Unknown

proof_lines: kcat is 747 sec(-1). Kinetic parameters measured with a CutC -52 AA truncated variant.

substrate: Unknown


organism: Saccharomyces cerevisiae

sequence_variant_note: Mutation signature E333Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme E333Y, in 50 mM potassium phosphate, pH 7.8, at 25°C


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +28, so it is treated as a source-provided variant sequence.

proof_lines: pH 7.2, 25°C, recombinant mutant E48A/E333A


sequence_variant_note: Mutation signature E48Q/E333Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.2, 25°C, recombinant mutant E48Q/E333Q


sequence_variant_note: Mutation signature E48D/E333D could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.2, 25°C, recombinant mutant E48D/E333D


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Aspergillus fumigatus

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


substrate_name: O-acetyl-L-serine

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

substrate: O-acetyl-L-serine


sequence_variant_note: Mutation signature E333D could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature E48D could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


proof_lines: pH 7.2, 25°C, recombinant wild-type enzyme and mutant E48D


sequence_variant_note: Mutation signature E333Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature E48Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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.


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

proof_lines: pH 7.2, 25°C, recombinant wild-type enzyme


proof_lines: mutant enzyme E48A, in 50 mM potassium phosphate, pH 7.8, at 25°C


organism: Lactobacillus delbrueckii subsp. bulgaricus

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


organism: Roseovarius nubinhibens

sequence_source: multiple

source_databases_merged: brenda uniprot


organism: Ruegeria lacuscaerulensis

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


organism: Ruegeria pomeroyi

substrate_name: dimethylseleniopropionate

substrate: dimethylseleniopropionate


organism: Streptococcus anginosus

substrate_name: L-Cysteine; H2O

substrate: L-Cysteine; H2O


organism: Streptococcus gordonii


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


organism: Homo sapiens

substrate_name: L-Cystathionine; H2O

substrate: L-Cystathionine; H2O


organism: Mus musculus


organism: Treponema denticola


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -12, so it is treated as a source-provided variant sequence.

proof_lines: mutant enzyme E48F, in 50 mM potassium phosphate, pH 7.8, at 25°C


proof_lines: mutant enzyme E333A, in 50 mM potassium phosphate, pH 7.8, at 25°C


proof_lines: mutant enzyme E48D, in 50 mM potassium phosphate, pH 7.8, at 25°C


proof_lines: native wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C

proof_lines: His-tagged recombinant wild type enzyme, in 50 mM potassium phosphate, pH 7.8, at 25°C


substrate_name: DL-homocysteine

verification_status: verified

column_label: Table 1, wild-type kinetic constants rows; row Wild type / DL-homocysteine; column Km (mM); raw value 1.1 mM; normalized 1.1 mM.

raw_value_unit_evidence: Km 1.1 mM

row_label: Wild type / DL-homocysteine

substrate: DL-homocysteine

status: verified


column_label: Table 1, wild-type kinetic constants rows; row Wild type / L-cysteine; column Km (mM); raw value 0.2 mM; normalized 0.2 mM.

raw_value_unit_evidence: Km 0.2 mM

row_label: Wild type / L-cysteine


substrate_name: S-methyl-L-cysteine

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

column_label: Table 1, wild-type kinetic constants rows; row Wild type / S-methyl-L-cysteine; column Km (mM); raw value 0.7 mM; normalized 0.7 mM.

raw_value_unit_evidence: Km 0.7 mM

row_label: Wild type / S-methyl-L-cysteine

substrate: S-methyl-L-cysteine


substrate_name: O-succinyl-L-homoserine

smiles: C(COC(=O)CCC(=O)O)C(C(=O)O)N

column_label: Table 4: Kinetic Constants for the Elimination Reaction Catalyzed by the Wild Type and the Asp241 mutant enzymes; row Wild type / O-succinyl-L-homoserine; Km raw 7.2 mM normalized 7.2 mM; kcat raw 2.56 s^-1 normalized 2.56 s^-1; kcat/Km raw 0.36 mM^-1 s^-1 normalized 0.36 s^-1 mM^-1.

row_label: Wild type / O-succinyl-L-homoserine

substrate: O-succinyl-L-homoserine


organism: Bacillus subtilis

substrate_name: H2O; L-Homocysteine

substrate: H2O; L-Homocysteine


organism: Brevibacterium aurantiacum

proof_lines: kcat is 15.51 sec(-1) with L-methionine as substrate. kcat is 72.44 sec(-1) with L-homocysteine as substrate.


organism: Porphyromonas gingivalis (strain ATCC BAA-308 / W83)


organism: Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104)


organism: Escherichia coli


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: cysteine

substrate: cysteine


organism: Bacillus cereus

substrate_name: L-cystathionine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E321A to reconstruct the assayed variant sequence.

substrate: L-cystathionine


organism: Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)

substrate_name: choline

substrate: choline


substrate_name: S,S-dimethyl-beta-propiothetin

assay_conditions_summary: pH 6

proof_lines: pH and temperature not specified in the publication

substrate: S,S-dimethyl-beta-propiothetin


organism: Toxoplasma gondii

substrate_name: djenkolic acid

source_db: oed

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from ncbi_refseq_transcript:XM_002364464.2;protein:XP_002364505.1 and applied mutation signature N360S to reconstruct the assayed variant sequence.

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

assay_conditions_summary: pH 9; 313.15 K; buffer 50 mM MOPS/bicine/proline (MBP

column_label: Table 1. Steady-state kinetic parameters of TgCGL variants at pH 9 and 37 C; row Hydrolysis of djenkolic acid / N360S / LDH assay; columns kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1); kcat 0.19 +/- 0.01 s^-1; Km 0.86 +/- 0.03 mM; kcat/Km (2.2 +/- 0.2) x 10^2 M^-1 s^-1. The paper-printed efficiency converts from M^-1 s^-1 to 0.22 s^-1*mM^-1 and is preserved instead of the quotient-derived export value.

substrate: djenkolic acid

status: corrected

source: oed


sequence_variant_note: Resolved canonical sequence from ncbi_refseq_transcript:XM_002364464.2;protein:XP_002364505.1 and applied mutation signature S77A to reconstruct the assayed variant sequence.

column_label: Table 1. Steady-state kinetic parameters of TgCGL variants at pH 9 and 37 C; row Hydrolysis of djenkolic acid / S77A / LDH assay; columns kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1); kcat 0.22 +/- 0.02 s^-1; Km 1.5 +/- 0.2 mM; kcat/Km (1.5 +/- 0.3) x 10^2 M^-1 s^-1. The paper-printed efficiency converts from M^-1 s^-1 to 0.15 s^-1*mM^-1 and is preserved instead of the quotient-derived export value.


column_label: Table 1. Steady-state kinetic parameters of TgCGL variants at pH 9 and 37 C; row Hydrolysis of djenkolic acid / WT / LDH assay; columns kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1); kcat 0.24 +/- 0.01 s^-1; Km 0.51 +/- 0.01 mM; kcat/Km (4.7 +/- 0.3) x 10^2 M^-1 s^-1. The paper-printed efficiency converts from M^-1 s^-1 to 0.47 s^-1*mM^-1 and is preserved instead of the quotient-derived export value.


substrate_name: L-Cystathionine

column_label: Table 1. Steady-state kinetic parameters of TgCGL variants at pH 9 and 37 C; row Hydrolysis of L-Cystathionine / N360S / DTNB assay; columns kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1); kcat 0.24 +/- 0.02 s^-1; Km 6.1 +/- 1.2 mM; kcat/Km (3.9 +/- 1.1) x 10 M^-1 s^-1. The paper-printed efficiency converts from M^-1 s^-1 to 0.039 s^-1*mM^-1 and is preserved instead of the quotient-derived export value.

substrate: L-Cystathionine


column_label: Table 1. Steady-state kinetic parameters of TgCGL variants at pH 9 and 37 C; row Hydrolysis of L-Cystathionine / S77A / DTNB assay; columns kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1); kcat 0.7 +/- 0.1 s^-1; Km 2.4 +/- 0.3 mM; kcat/Km (2.9 +/- 0.8) x 10^2 M^-1 s^-1. The paper-printed efficiency converts from M^-1 s^-1 to 0.29 s^-1*mM^-1 and is preserved instead of the quotient-derived export value.


substrate_name: L-Cysteine

column_label: Table 1. Steady-state kinetic parameters of TgCGL variants at pH 9 and 37 C; row Hydrolysis of L-Cysteine / N360S / LDH assay; columns kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1); kcat 0.007 +/- 0.001 s^-1; Km 0.4 +/- 0.1 mM; kcat/Km (1.8 +/- 0.7) x 10 M^-1 s^-1. The paper-printed efficiency converts from M^-1 s^-1 to 0.018 s^-1*mM^-1 and is preserved instead of the quotient-derived export value.

substrate: L-Cysteine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N349S/N360S to reconstruct the assayed variant sequence.

column_label: Table 1. Steady-state kinetic parameters of TgCGL variants at pH 9 and 37 C; row Hydrolysis of L-Cysteine / WT / LDH assay; columns kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1); kcat 0.009 +/- 0.001 s^-1; Km 0.21 +/- 0.1 mM; kcat/Km (4.3 +/- 2.1) x 10 M^-1 s^-1. The paper-printed efficiency converts from M^-1 s^-1 to 0.043 s^-1*mM^-1 and is preserved instead of the quotient-derived export value.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N349S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9; 313.15 K; buffer MBP

column_label: Table 1 lists wild type TgCGL hydrolysis of L-cystathionine by DTNB with kcat 2.0+/-0.1 s^-1, Km 0.9+/-0.1 mM, and kcat/Km (2.2+/-0.4)x10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=2.0 normalized_unit=s^-1; Km normalized_value=0.9 normalized_unit=mM; kcat/Km normalized_value=2.2 normalized_unit=s^-1 mM^-1; computed from table kcat/Km inputs=2.2222222222222223 s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=2.0+/-0.1 raw_unit=s^-1; Km raw_value=0.9+/-0.1 raw_unit=mM; kcat/Km raw_value=(2.2+/-0.4)x10^3 raw_unit=M^-1 s^-1

row_label: Hydrolysis of L-cystathionine / wild type / DTNB assay

table_label: Table 1, steady-state kinetic parameters of TgCGL variants at pH 9 and 37 C


organism: Arabidopsis thaliana

substrate_name: L-cysteine for the cystathionine gamma-lyase activity


substrate_name: O(3)-acetyl-L-serine for the cysteine synthase activity


enzyme_display_name: alliin lyase

organism: Allium hymenorrhizum

substrate_name: (+)-S-(2-propenyl)-L-cysteine sulfoxide

enzyme: alliin lyase

substrate: (+)-S-(2-propenyl)-L-cysteine sulfoxide


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P32929 and applied mutation signature Q240E to reconstruct the assayed variant sequence.

column_label: Table 1: Comparison of the kinetic parameters for the polymorphic variants and pathogenic mutants of CGL (Biochemistry 2008, 47(23):6226-6232); the printed table is transposed: each printed column is one enzyme form and each printed line inside a substrate block is one parameter. Table 1, substrate block 'Csta', printed variant column 'Q240E'; row 'KM, mM' = 0.72; row 'kcat, s-1' = 0.02; row 'kcat/KM' = 0.028. captured primary segment: Table 1 | substrate Csta | human CGL Q240E | KM 0.72 mM | kcat 0.02 s-1 | kcat/KM 0.028 mM-1 s-1 | assay DTNB cysteine release from cystathionine, at 37 °C

normalized_value_unit_evidence: KM: printed Table 1 cell 0.72 mM; the printed row head is 'KM, mM', so no unit conversion applies and the paper value is 0.72 mM. kcat: printed Table 1 cell 0.02 s-1; the printed row head is 'kcat, s-1', already per second, so no unit conversion applies and the paper value is 0.02 s^(-1). kcat/KM: printed Table 1 cell 0.028 mM-1 s-1; footnote c states that kcat/KM is expressed in units of mM-1 s-1, which is the canonical unit, so no unit conversion applies and the printed cell is 0.028 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.02 / 0.72 = 0.02777777777777778 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.028 mM-1 s-1, which is that quotient written to the place the printed literal carries.

raw_value_unit_evidence: Table 1, substrate block 'Csta', printed variant column 'Q240E': kcat = 0.02 s-1; KM = 0.72 mM; printed kcat/KM = 0.028 mM-1 s-1.

row_label: Table 1, substrate block 'Csta' (cystathionine), printed variant column 'Q240E'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P32929 and applied mutation signature T67I to reconstruct the assayed variant sequence.

column_label: Table 1: Comparison of the kinetic parameters for the polymorphic variants and pathogenic mutants of CGL (Biochemistry 2008, 47(23):6226-6232); the printed table is transposed: each printed column is one enzyme form and each printed line inside a substrate block is one parameter. Table 1, substrate block 'Csta', printed variant column 'T67I'; row 'KM, mM' = 0.6; row 'kcat, s-1' = 0.45; row 'kcat/KM' = 0.86. captured primary segment: Table 1 | substrate Csta | human CGL T67I | KM 0.6 mM | kcat 0.45 s-1 | kcat/KM 0.86 mM-1 s-1 | assay DTNB cysteine release from cystathionine, at 37 °C

normalized_value_unit_evidence: KM: printed Table 1 cell 0.6 mM; the printed row head is 'KM, mM', so no unit conversion applies and the paper value is 0.6 mM. kcat: printed Table 1 cell 0.45 s-1; the printed row head is 'kcat, s-1', already per second, so no unit conversion applies and the paper value is 0.45 s^(-1). kcat/KM: the paper's own printed efficiency cell 0.86 mM-1 s-1 is already in the canonical unit, so the paper value for this metric is 0.86 s^(-1)*mM^(-1). The quotient of the two printed component cells is 0.45 / 0.6 = 0.75 s^-1 mM^-1, which falls outside the rounding interval of the printed cell 0.86 at every place value that literal could carry, so the printed efficiency is the paper's own independently fitted primary value and is carried as the paper value for this metric.

raw_value_unit_evidence: Table 1, substrate block 'Csta', printed variant column 'T67I': kcat = 0.45 s-1; KM = 0.6 mM; printed kcat/KM = 0.86 mM-1 s-1.

row_label: Table 1, substrate block 'Csta' (cystathionine), printed variant column 'T67I'


column_label: Table 1: Comparison of the kinetic parameters for the polymorphic variants and pathogenic mutants of CGL (Biochemistry 2008, 47(23):6226-6232); the printed table is transposed: each printed column is one enzyme form and each printed line inside a substrate block is one parameter. Table 1, substrate block 'Cys', printed variant column 'T67I'; row 'KM, mM' = 4.1; row 'kcat, s-1' = 0.30; row 'kcat/KM' = 0.07. captured primary segment: Table 1 | substrate Cys | human CGL T67I | KM 4.1 mM | kcat 0.30 s-1 | kcat/KM 0.07 mM-1 s-1 | assay 40 mM borate pH 7.0 lead acetate H2S release, at 37 °C

normalized_value_unit_evidence: KM: printed Table 1 cell 4.1 mM; the printed row head is 'KM, mM', so no unit conversion applies and the paper value is 4.1 mM. kcat: printed Table 1 cell 0.30 s-1; the printed row head is 'kcat, s-1', already per second, so no unit conversion applies and the paper value is 0.3 s^(-1). kcat/KM: printed Table 1 cell 0.07 mM-1 s-1; footnote c states that kcat/KM is expressed in units of mM-1 s-1, which is the canonical unit, so no unit conversion applies and the printed cell is 0.07 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.30 / 4.1 = 0.07317073170731708 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.07 mM-1 s-1, which is that quotient written to the place the printed literal carries.

raw_value_unit_evidence: Table 1, substrate block 'Cys', printed variant column 'T67I': kcat = 0.30 s-1; KM = 4.1 mM; printed kcat/KM = 0.07 mM-1 s-1.

row_label: Table 1, substrate block 'Cys' (cysteine), printed variant column 'T67I'


substrate_name: L-Homocysteine

table_label: Table 1: Comparison of the kinetic parameters for the polymorphic variants and pathogenic mutants of CGL (Biochemistry 2008, 47(23):6226-6232)

substrate: L-Homocysteine


organism: Citrobacter freundii

substrate_name: alliin

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C115A with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; buffer pH 8; cofactor NADH

column_label: Table 1 row Alliin; C115A MGL column group; columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat 0.41 s^-1; Km 1.75 mM; kcat/Km 0.230 s^-1*mM^-1 (table kcat/Km converted from M^-1 s^-1 to s^-1*mM^-1).

raw_value_unit_evidence: Table 1 row Alliin, C115A MGL columns: kcat 0.41 s^-1; Km 1.75 mM; kcat/Km 2.30 x 10^2 M^-1 s^-1.

row_label: Alliin; C115A MGL

table_label: Table 1, Kinetic parameters for the gamma- and beta-elimination reactions

substrate: alliin


sequence_variant_note: Resolved canonical sequence from package_local_exact_accession:Q84AR1 and applied mutation signature C115H to reconstruct the assayed variant sequence.

column_label: Table 1 row Alliin; C115H MGL column group; columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat 11.31 s^-1; Km 0.44 mM; kcat/Km 25.7 s^-1*mM^-1 (table kcat/Km converted from M^-1 s^-1 to s^-1*mM^-1).

raw_value_unit_evidence: Table 1 row Alliin, C115H MGL columns: kcat 11.31 s^-1; Km 0.44 mM; kcat/Km 2.57 x 10^4 M^-1 s^-1.

row_label: Alliin; C115H MGL


substrate_name: ethiin

column_label: Table 1 row Ethiin; C115A MGL column group; columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat 1.25 s^-1; Km 5.48 mM; kcat/Km 0.230 s^-1*mM^-1 (table kcat/Km converted from M^-1 s^-1 to s^-1*mM^-1).

raw_value_unit_evidence: Table 1 row Ethiin, C115A MGL columns: kcat 1.25 s^-1; Km 5.48 mM; kcat/Km 2.30 x 10^2 M^-1 s^-1.

row_label: Ethiin; C115A MGL

substrate: ethiin


column_label: Table 1 row Ethiin; C115H MGL column group; columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat 5.59 s^-1; Km 0.47 mM; kcat/Km 12.0 s^-1*mM^-1 (table kcat/Km converted from M^-1 s^-1 to s^-1*mM^-1).

raw_value_unit_evidence: Table 1 row Ethiin, C115H MGL columns: kcat 5.59 s^-1; Km 0.47 mM; kcat/Km 1.20 x 10^4 M^-1 s^-1.

row_label: Ethiin; C115H MGL


substrate_name: methiin

column_label: Table 1 row Methiin; C115A MGL column group; columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat 1.63 s^-1; Km 0.63 mM; kcat/Km 2.60 s^-1*mM^-1 (table kcat/Km converted from M^-1 s^-1 to s^-1*mM^-1).

raw_value_unit_evidence: Table 1 row Methiin, C115A MGL columns: kcat 1.63 s^-1; Km 0.63 mM; kcat/Km 2.60 x 10^3 M^-1 s^-1.

row_label: Methiin; C115A MGL

substrate: methiin


substrate_name: (+-)-ethiin

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C115H with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

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

substrate: (+-)-ethiin


substrate_name: (+)-methiin

substrate: (+)-methiin


substrate_name: (+-)-methiin

substrate: (+-)-methiin


substrate_name: (+)-propiin

substrate: (+)-propiin


substrate_name: (+-)-propiin

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

substrate: (+-)-propiin


substrate_name: cystathionine

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

source_databases_merged: brenda skid

substrate: cystathionine


substrate_name: L,L-cystathionine

substrate: L,L-cystathionine


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -1, so it is treated as a source-provided variant sequence.

proof_lines:
Treponema denticola cystalysin K238R
beta-chloro-L-alanine activity
3-Chloro-L-alanine


proof_lines: K238R retains 0.3% of wild-type activity


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

source_databases_merged: sabio_rk skid uniprot


substrate_name: L-cystathionine

column_label: Abstract reports the Km value for catalysis of L-cystathionine was 0.81 mM and Vmax was 0.0013 unit/mg protein.

raw_value_unit_evidence: Km raw_value=0.81 mM raw_unit=mM

row_label: Murine cystathionine gamma-lyase / L-cystathionine

table_label: PubMed XML abstract PMID 16327076

substrate: L-cystathionine


substrate_name: L-cysteine

source_databases_merged: brenda skid uniprot

substrate: L-cysteine


organism: Bacillus subtilis (strain 168)


substrate_name: L-homocysteine

substrate: L-homocysteine


organism: Saccharomyces cerevisiae


proof_lines:
Saccharomyces cerevisiae
CYS3
cystathionine gamma-lyase

source_databases_merged: skid uniprot


substrate_name: L-methionine

proof_lines:
Porphyromonas gingivalis W83
mgl
METase

substrate: L-methionine


organism: Homo sapiens

column_label: No checked primary/sibling paper evidence supports 0.3 mM for L,L-cystathionine; the closest official sources report higher Cst Km values.

normalized_value_unit_evidence: Observed paper Km values are 0.5 mM and 0.4-0.72 mM; exported value is 0.3 mM.

row_label: Human cystathionine gamma-lyase / L-cystathionine (Cst)

table_label: PubMed abstract PMID 10212249 plus PMC Table 1 PMID 18476726


organism: Alcaligenes sp.

substrate_name: dimethylsulfoniopropionate

column_label: Abstract reports DMSP lyase is a 48-kDa monomer with a Michaelis-Menten constant for DMSP of 1.4 mM.

raw_value_unit_evidence: Km raw_value=1.4 mM raw_unit=mM

row_label: Alcaligenes-like marine isolate DMSP lyase / DMSP

table_label: PubMed XML abstract PMID 16534905

substrate: dimethylsulfoniopropionate


organism: Alcaligenes faecalis

substrate_name: beta-dimethylsulfoniopropanoate

smiles: C[S+](C)CCC(=O)O

proof_lines:
DddY
Alcaligenes faecalis M3A
bona fide DMSP lyases

substrate: beta-dimethylsulfoniopropanoate


organism: Halodesulfovibrio aestuarii


organism: Roseovarius nubinhibens

substrate_name: S,S-dimethyl-beta-propiothetin

substrate: S,S-dimethyl-beta-propiothetin


organism: Allium sativum

substrate_name: S-allylcysteine sulfoxide

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

column_label: Abstract states alliinase Km using synthetic S-allylcysteine sulfoxide (+ isomer) as substrate was 1.1 mM, with pH optimum 6.5.

raw_value_unit_evidence: Km raw_value=1.1 raw_unit=mM

row_label: Allium sativum alliinase with synthetic S-allylcysteine sulfoxide

table_label: PubMed abstract PMID 7979352

substrate: S-allylcysteine sulfoxide


organism: Rattus norvegicus

substrate_name: L-cystine

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

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

substrate: L-cystine


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


proof_lines: mutant enzyme C136V/C171V, at pH 7.5 and 37°C


substrate_name: beta-chloro-L-alanine

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

substrate: beta-chloro-L-alanine


proof_lines: mutant enzyme C136V/C171V, at pH 8.0 and 37°C


organism: Ruegeria pomeroyi

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

proof_lines: pH 6.0, temperature not specified in the publication


substrate_name: ethylmethylsulfoniopropionate

proof_lines: presence of Mn2+, pH 8.0, temperature not specified in the publication

proof_lines: presence of Fe2+, pH 8.0, temperature not specified in the publication

substrate: ethylmethylsulfoniopropionate


substrate_name: diethylsulfoniopropionate

substrate: diethylsulfoniopropionate


organism: Streptomyces phaeochromogenes


substrate_name: DL-lanthionine

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

substrate: DL-lanthionine


substrate_name: beta-chloro-L-Ala

substrate: beta-chloro-L-Ala


substrate_name: DL-vinylglycine

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

substrate: DL-vinylglycine


substrate_name: L-homoserine

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

substrate: L-homoserine


organism: Oleidesulfovibrio alaskensis

substrate_name: choline

substrate: choline


proof_lines: catalytic alliinase-specific variable domain of the heavy chain of a heavy-chain antibody VHH C-10, pH 7.0, 35°C


substrate_name: alliin

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

substrate: alliin


enzyme_display_name: L-serine ammonia-lyase

organism: Aspergillus terreus

substrate_name: L-serine

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

enzyme: L-serine ammonia-lyase

substrate: L-serine


substrate_name: L-threonine

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

substrate: L-threonine


organism: Oenococcus oeni

substrate_name: L-Cys

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

substrate: L-Cys


substrate_name: L-cystathionine

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

substrate: L-cystathionine


substrate_name: (DL)-homocysteine

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

substrate: (DL)-homocysteine


organism: Lactiplantibacillus plantarum


substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: L-homocysteine

substrate: L-homocysteine


substrate_name: L-cystine

substrate: L-cystine


organism: Bacillus anthracis

substrate_name: pyruvate

substrate: pyruvate


substrate_name: L-aspartate 4-semialdehyde

substrate: L-aspartate 4-semialdehyde


proof_lines:
at pH 8.0 and 37°C
at pH 8.0 and 25°C


enzyme_display_name: pyridoxal 5'-phosphate synthase (glutamine hydrolyzing)

organism: Bacillus subtilis

substrate_name: D-ribose 5-phosphate

substrate: D-ribose 5-phosphate


substrate_name: D-ribulose 5-phosphate

smiles: C(C(C(C(=O)CO)O)O)OP(=O)(O)O

proof_lines: pH 8.0, 37°C, free pyridoxal 5'-phosphate synthase subunit (Pdx1)

enzyme: pyridoxal 5'-phosphate synthase (glutamine hydrolyzing)

substrate: D-ribulose 5-phosphate


enzyme_display_name: adenylosuccinate lyase

enzyme: adenylosuccinate lyase


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


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


enzyme_display_name: 3-dehydroquinate synthase

enzyme: 3-dehydroquinate synthase


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


enzyme_display_name: heparin lyase

organism: Bacteroides thetaiotaomicron

substrate_name: heparin, 20-mer / heparin, 6-mer

mutation_signature: deletion mutant 191-213 protein

mutation_type: deletion

enzyme: heparin lyase

substrate: heparin, 20-mer / heparin, 6-mer


substrate_name: heparin, 20-mer / heparin, 8-mer / heparin, 6-mer


enzyme_display_name: ureidoglycolate lyase

organism: Burkholderia cepacia

substrate_name: phenylacetyl-alpha-hydroxyglycine

enzyme: ureidoglycolate lyase

substrate: phenylacetyl-alpha-hydroxyglycine


substrate_name: (S)-ureidoglycolate / ureidoglycolate

substrate: (S)-ureidoglycolate / ureidoglycolate


enzyme_display_name: methylaspartate ammonia-lyase

organism: Carboxydothermus hydrogenoformans

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

enzyme: methylaspartate ammonia-lyase


substrate_name: L-aspartate

substrate: L-aspartate


enzyme_display_name: threonine ammonia-lyase

organism: Chloroflexus aurantiacus

substrate_name: L-Thr

proof_lines:
Ile-sensitive enzyme
Ile-insensitive enzyme

enzyme: threonine ammonia-lyase

substrate: L-Thr


substrate_name: L-Ser

substrate: L-Ser


enzyme_display_name: short-chain-enoyl-CoA hydratase

organism: Clostridium acetobutylicum

substrate_name: crotonyl-CoA

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines:
25°C, pH 7.5
at pH 8.0 and 25°C

enzyme: short-chain-enoyl-CoA hydratase

substrate: crotonyl-CoA


substrate_name: hexenoyl-CoA

substrate: hexenoyl-CoA


organism: Citrobacter amalonaticus

substrate_name: mesaconic acid

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

substrate: mesaconic acid


substrate_name: (2R,3S)-3-chloroaspartic acid

substrate: (2R,3S)-3-chloroaspartic acid


enzyme_display_name: pectate lyase

substrate_name: trigalacturonate

enzyme: pectate lyase

substrate: trigalacturonate


substrate_name: tetragalacturonate / polygalacturonate

proof_lines:
at pH8.5 and in the presence of 5mMCa2+
pH 9.4, 50°C

substrate: tetragalacturonate / polygalacturonate


enzyme_display_name: bile-acid 7alpha-dehydratase

organism: Clostridium scindens

assay_conditions_summary: pH 7.3; 298.15 K; cofactor CoA

proof_lines:
25°C in 20 mM Tris-HCl, pH 7.3
25°C in 20 mM Tris-HCl pH 7.3

enzyme: bile-acid 7alpha-dehydratase


enzyme_display_name: oligogalacturonide lyase

organism: Dickeya chrysanthemi

substrate_name: trigalacturonic acid

enzyme: oligogalacturonide lyase

substrate: trigalacturonic acid


substrate_name: digalacturonic acid

substrate: digalacturonic acid


enzyme_display_name: crotonobetainyl-CoA hydratase

organism: Escherichia coli

substrate_name: crotonobetainyl-CoA

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

enzyme: crotonobetainyl-CoA hydratase

substrate: crotonobetainyl-CoA


enzyme_display_name: diaminopropionate ammonia-lyase

enzyme: diaminopropionate ammonia-lyase


substrate_name: D-serine

substrate: D-serine


enzyme_display_name: aspartate ammonia-lyase

substrate_name: L-aspartic acid

enzyme: aspartate ammonia-lyase

substrate: L-aspartic acid


substrate_name: L-aspartic acid alpha-amide

substrate: L-aspartic acid alpha-amide


organism: Corynebacterium glutamicum

substrate_name: L-aspartate 4-semialdehyde

assay_conditions_summary: cofactor NADPH

proof_lines: reaction mixture includes 100 mM Tris-HCl, 2.5 mM pyruvate, 0.05-0.1 microg dihydrodipicolinate synthase and 0.2 mM NADPH, from 5.6 to 22.4 mM plots deviate from typical Michaelis-Menten kinetics, increased concentration fits an uncompetiti

substrate: L-aspartate 4-semialdehyde


substrate_name: pyruvate

proof_lines: 2.5 mM pyruvate replaced by 0.1-2 mM, no substrate inhibition observed at high concentrations of pyruvate

substrate: pyruvate


substrate_name: (S)-aspartate 4-semialdehyde

proof_lines: at pH 7.0, temperature not specified in the publication

substrate: (S)-aspartate 4-semialdehyde


assay_conditions_summary: pH 8; 303.15 K; buffer 100 mM HEPES


enzyme_display_name: DNA-(apurinic or apyrimidinic site) lyase

substrate_name: 35 base pair oligonucleotide containing 5,6-dihydrouracil opposite A

proof_lines: wild-type in rAP-containing oligonucleotide cleavage assay


substrate_name: 35 base pair oligonucleotide containing 5,6-dihydroxy-5,6-dihydrothymine opposite A

enzyme: DNA-(apurinic or apyrimidinic site) lyase


substrate_name: AP-DNA

proof_lines: mutant Y72A in rAP-containing oligonucleotide cleavage assay

substrate: AP-DNA


proof_lines: mutant Y72F in rAP-containing oligonucleotide cleavage assay


mutation_type: truncation

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

proof_lines: C-terminal truncated DHDPS (H225*), at 30°C, in 150 mM HEPES, pH 8.0, 0.16 mM NADPH, 50 microg/ml DHDPR


substrate_name: L-Ser

proof_lines:
in presence of AMP
in absence of AMP

substrate: L-Ser


substrate_name: L-Thr

proof_lines:
in presence of AMP
without AMP
in absence of AMP

substrate: L-Thr


assay_conditions_summary: pH 8; 303.15 K; buffer 100 mM HEPES; cofactor NADPH

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

proof_lines: wild-type, in 100 mM HEPES buffer, pH 8.0, 0.2 mM NADPH, 50 microg/ml DHDPR


enzyme_display_name: D-lactate dehydratase

smiles: CC(=O)C=O

enzyme: D-lactate dehydratase


enzyme_display_name: ethanolamine ammonia-lyase

substrate_name: ethanolamine

smiles: C(CO)N

assay_conditions_summary: pH 7

proof_lines:
pH 7
pH 5.8

enzyme: ethanolamine ammonia-lyase

substrate: ethanolamine


substrate_name: Unknown

substrate: Unknown


proof_lines:
pH 6.8, 25°C
at 20°C and pH 7.8
at 20°C and pH 8.5


enzyme_display_name: D-serine ammonia-lyase

substrate_name: D-allothreonine

enzyme: D-serine ammonia-lyase

substrate: D-allothreonine


organism: Gallus gallus

substrate_name: D-threonine

substrate: D-threonine


substrate_name: L-serine

substrate: L-serine


enzyme_display_name: peptidylamidoglycolate lyase

organism: Homo sapiens

enzyme: peptidylamidoglycolate lyase


enzyme_display_name: enoyl-CoA hydratase 2

assay_conditions_summary: pH 5; cofactor CoA

proof_lines:
mutant enzyme E366A, pH 5
mutant enzyme E366A, pH 8

enzyme: enoyl-CoA hydratase 2


proof_lines:
wild type enzyme, pH 5
wild type enzyme, pH 8
wild type, pH 8


enzyme_display_name: adenylosuccinate lyase

enzyme: adenylosuccinate lyase


proof_lines: recombinant His-tagged wild-type enzyme, pH 7.4, 25°C


proof_lines: recombinant His-tagged mutant R426H, pH 7.4, 25°C


substrate_name: succinyladenosine monophosphate

proof_lines: recombinant His-tagged mutant R303C, pH 7.4, 25°C

substrate: succinyladenosine monophosphate


enzyme_display_name: argininosuccinate lyase

substrate_name: (Nomega-L-arginino)succinate

proof_lines:
mutant c.532 G>A, pH 7.5, 37°C
mutant c.1135 C>T, pH 7.5, 37°C

enzyme: argininosuccinate lyase

substrate: (Nomega-L-arginino)succinate


substrate_name: DNA containing an abasic site

proof_lines: pH 7.5, mutant enzyme Y128A, high salt concentration (150 mM NaCl)

proof_lines: pH 7.5, mutant enzyme Y128A, low salt concentration (82 mM NaCl)

substrate: DNA containing an abasic site


proof_lines: pH 7.5, mutant enzyme Y269A, high salt concentration (150 mM NaCl)

proof_lines: pH 7.5, mutant enzyme Y269A, low salt concentration (82 mM NaCl)


proof_lines:
enzyme from cell line 1751
enzyme from cell line 1753


enzyme_display_name: phenylalanine ammonia-lyase

organism: Jatropha curcas

substrate_name: L-Tyr

enzyme: phenylalanine ammonia-lyase

substrate: L-Tyr


substrate_name: L-Phe

substrate: L-Phe


organism: Klebsiella pneumoniae

substrate_name: D-Ser

substrate: D-Ser


substrate_name: D-Thr

substrate: D-Thr


enzyme_display_name: threonine synthase

organism: Lathyrus oleraceus

substrate_name: O-phosphohomoserine

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

enzyme: threonine synthase

substrate: O-phosphohomoserine


proof_lines:
at low substrate concentrations
at high substrate concentrationas


enzyme_display_name: cystathionine gamma-lyase

organism: Neurospora sp.

substrate_name: L-cystine

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

enzyme: cystathionine gamma-lyase

substrate: L-cystine


substrate_name: Lanthionine

substrate: Lanthionine


organism: Nicotiana tabacum

substrate_name: L-phenylalanine

proof_lines: isoform PAL3, at 30°C in 50 mM Tris/HCl, pH 8.5

proof_lines: isoform PAL1, at 30°C in 50 mM Tris/HCl, pH 8.5

proof_lines: isoform PAL2, at 30°C in 50 mM Tris/HCl, pH 8.5

substrate: L-phenylalanine


enzyme_display_name: 5-epiaristolochene synthase

substrate_name: (2E,6E)-farnesyl diphosphate

proof_lines: fusion construct epiaristolochene synthase/farnesyl diphosphate synthase, pH 8.0, 30°C

enzyme: 5-epiaristolochene synthase

substrate: (2E,6E)-farnesyl diphosphate


substrate_name: (2E,6Z)-6-fluorofarnesyl diphosphate

substrate: (2E,6Z)-6-fluorofarnesyl diphosphate


organism: Petroselinum crispum


organism: Leishmania major

substrate_name: DNA

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +15, so it is treated as a source-provided variant sequence.

proof_lines: LMAP mutant A138D, 3'-phosphodiesterase activity

proof_lines: LMAP mutant A138D, AP endonuclease activity

substrate: DNA


substrate_name: THF-containing oligonucleotide

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

proof_lines:
LMAP, 3'-phosphodiesterase activity
LMAP, AP endonuclease activity

substrate: THF-containing oligonucleotide


substrate_name: N-methyl-L-phenylalanine

substrate: N-methyl-L-phenylalanine


smiles: N

assay_conditions_summary: pH 10


enzyme_display_name: (+)-car-3-ene synthase

organism: Picea sitchensis

substrate_name: geranyl diphosphate

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

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

enzyme: (+)-car-3-ene synthase

substrate: geranyl diphosphate


proof_lines: mutant L596F, 30°C, pH not specified in the publication


organism: Priestia megaterium


substrate_name: pyruvate

substrate: pyruvate


organism: Propionibacterium freudenreichii subsp. shermanii

substrate_name: L-aspartate

proof_lines: 100 mM Bis-Tris-propane hydrochloride buffer, pH 6.2

substrate: L-aspartate


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: 3-dehydroquinate synthase

organism: Providencia alcalifaciens

enzyme: 3-dehydroquinate synthase


enzyme_display_name: (-)-beta-pinene synthase

organism: Pinus contorta

substrate_name: (3S)-linalyl diphosphate

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

enzyme: (-)-beta-pinene synthase

substrate: (3S)-linalyl diphosphate


organism: Pseudomonas aeruginosa

proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme


proof_lines:
isoform DHDPS2, at pH 6.8 and 37°C
isoform DHDPS1, at pH 6.8 and 37°C


enzyme_display_name: threonine ammonia-lyase

organism: Pseudomonas putida

substrate_name: L-Thr

enzyme: threonine ammonia-lyase

substrate: L-Thr


substrate_name: L-Ser

substrate: L-Ser


assay_conditions_summary: cofactor CoA


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


enzyme_display_name: 6-pyruvoyltetrahydropterin synthase

organism: Rattus norvegicus

enzyme: 6-pyruvoyltetrahydropterin synthase


organism: Pseudomonas sp. T62

proof_lines: exhibits dehydratase activity specific only to L-threo-3-hydroxyaspartate


proof_lines:
strong competitive inhibition
non-competitive inhibition


organism: Homo sapiens

substrate_name: Arg

substrate: Arg


substrate_name: fumarate

substrate: fumarate


enzyme_display_name: histidine ammonia-lyase

organism: Klebsiella pneumoniae subsp. pneumoniae

substrate_name: Urocanate

enzyme: histidine ammonia-lyase

substrate: Urocanate


enzyme_display_name: ethanolamine-phosphate phospho-lyase

substrate_name: Ethanolamine phosphate

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

proof_lines:
at pH 6.0 and 30°C
at pH 7.4 and 30°C
at pH 8.0 and 30°C

enzyme: ethanolamine-phosphate phospho-lyase

substrate: Ethanolamine phosphate


proof_lines:
at pH 6.0 and 30°C
at pH 8.0 and 30°C


organism: Mus musculus


enzyme_display_name: carotenoid 1,2-hydratase

organism: Rhodobacter capsulatus

substrate_name: lycopene

enzyme: carotenoid 1,2-hydratase

substrate: lycopene


substrate_name: Neurosporene

substrate: Neurosporene


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


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


enzyme_display_name: D-lactate dehydratase

organism: Schizosaccharomyces pombe

substrate_name: methylglyoxal

proof_lines: recombinant mutant SpDJ-1 H130A, pH and temperature not specified in the publication

enzyme: D-lactate dehydratase

substrate: methylglyoxal


proof_lines: recombinant wild-type SpDJ-1, pH and temperature not specified in the publication


enzyme_display_name: D-serine ammonia-lyase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: D-Ser

assay_conditions_summary: pH 7.5; 310.15 K; buffer K+-phosphate

proof_lines:
pH 7.5, 37°C, buffer K+-phosphate
pH 7.5, 37°C, buffer Na+-phosphate

enzyme: D-serine ammonia-lyase

substrate: D-Ser


substrate_name: D-Thr

assay_conditions_summary: pH 7.5; 310.15 K; buffer Na+-phosphate

proof_lines:
pH 7.5, 37°C, buffer Na+-phosphate
pH 7.5, 37°C, buffer K+-phosphate

substrate: D-Thr


enzyme_display_name: etheroleic acid synthase

organism: Selaginella moellendorffii

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

enzyme: etheroleic acid synthase


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


enzyme_display_name: ethanolamine ammonia-lyase

substrate_name: ethanolamine

enzyme: ethanolamine ammonia-lyase

substrate: ethanolamine


proof_lines: R160K EAL shows a 30fold increase relative to wild-type enzyme


organism: Solanum lycopersicum

proof_lines: Ile-sensitive enzyme form and Ile-insensitive form


proof_lines:
Ile-insensitive enzyme form
Ile-sensitive form


organism: Sorghum bicolor

substrate_name: L-phenylalanine

substrate: L-phenylalanine


organism: Staphylococcus aureus

substrate_name: pyruvate

proof_lines: similar to those of DHDPS enzyme of Escherichia coli

substrate: pyruvate


substrate_name: (S)-aspartate 4-semialdehyde

substrate: (S)-aspartate 4-semialdehyde


enzyme_display_name: short-chain-enoyl-CoA hydratase

organism: Syntrophothermus lipocalidus

assay_conditions_summary: pH 7.8; 315.15 K; cofactor CoA

proof_lines: pH 7.8, 42°C, kcat is calculated for the activities at 55°C

enzyme: short-chain-enoyl-CoA hydratase


organism: Trichormus variabilis

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


substrate_name: Unknown

substrate: Unknown


organism: Streptomyces venezuelae

substrate_name: S-adenosyl-L-methionine

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication

substrate: S-adenosyl-L-methionine


substrate_name: TDP-D-quinovose

substrate: TDP-D-quinovose


organism: Vibrio cholerae

proof_lines:
pH 8.0, 30°C, untagged enzyme
pH 8.0, 30°C, His-tagged enzyme


organism: Triticum aestivum


enzyme_display_name: tuliposide A-converting enzyme

organism: Tulipa gesneriana

substrate_name: 6-tuliposide B

proof_lines: pH and temperature not specified in the publication

enzyme: tuliposide A-converting enzyme

substrate: 6-tuliposide B


substrate_name: 6-tuliposide A

substrate: 6-tuliposide A


enzyme_display_name: guluronate-specific alginate lyase

organism: Vibrio sp. NJ-04

enzyme: guluronate-specific alginate lyase


substrate_name: alginate

substrate: alginate


enzyme_display_name: peptidylamidoglycolate lyase

organism: Xenopus laevis

proof_lines: 37°C, pH 6.6, PGL domain of transmembrane truncated enzyme: dAE

enzyme: peptidylamidoglycolate lyase


proof_lines: 37°C, pH 6.6, PGL domain of full expressed enzyme: AE


enzyme_display_name: phosphomevalonate dehydratase

organism: Aeropyrum pernix

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

enzyme: phosphomevalonate dehydratase


enzyme_display_name: alliin lyase

organism: Allium cepa

substrate_name: cystine

proof_lines:
alliinase I
alliinase II

enzyme: alliin lyase

substrate: cystine


proof_lines:
alliin lyase II
alliin lyase I
alliinase I


organism: Allium cepa * Allium chevsuricum

substrate_name: L-(+)-alliin

substrate: L-(+)-alliin


enzyme_display_name: ornithine cyclodeaminase

organism: Agrobacterium tumefaciens

substrate_name: L-ornithine

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

proof_lines: 0.5 mM NAD+, in the presence of L-arginine

enzyme: ornithine cyclodeaminase

substrate: L-ornithine


enzyme_display_name: (-)-alpha-pinene synthase

organism: Abies grandis

substrate_name: geranyl diphosphate

proof_lines: pH 7.8, temperature not specified in the publication

enzyme: (-)-alpha-pinene synthase

substrate: geranyl diphosphate


organism: Allium cepa * Allium oliquum


organism: Allium cepa * Allium altyncolicum


organism: Allium cepa * Allium globosum


organism: Allium cepa * Allium senescens


organism: Allium cepa * Allium saxatile


organism: Allium sativum

substrate_name: L-cystine

proof_lines: homogenous alliinase prepared from fresh garlic cloves

proof_lines: preparation obtained from garlic powder, activity calculated from the amount of enzymatically formed pyruvate

substrate: L-cystine


substrate_name: S-allyl-L-Cys sulfoxide

proof_lines:
pH 7.0, 25°C
enzyme from garlic powder

substrate: S-allyl-L-Cys sulfoxide


organism: Allium fistulosum

substrate_name: S-ethyl-L-cysteine sulfoxide

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

substrate: S-ethyl-L-cysteine sulfoxide


enzyme_display_name: L-serine ammonia-lyase

organism: Anaerotignum propionicum

substrate_name: L-Ser

enzyme: L-serine ammonia-lyase

substrate: L-Ser


enzyme_display_name: threonine ammonia-lyase

organism: Morganella morganii

substrate_name: L-Thr

proof_lines:
in presence of 1 mM AMP
in absence of AMP

enzyme: threonine ammonia-lyase

substrate: L-Thr


proof_lines:
in presence of AMP
in absence of AMP


enzyme_display_name: argininosuccinate lyase

organism: Anser sp.

substrate_name: argininosuccinate

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

enzyme: argininosuccinate lyase

substrate: argininosuccinate


organism: Arabidopsis thaliana

substrate_name: fumarate

substrate: fumarate


enzyme_display_name: threonine synthase

substrate_name: O-phosphohomoserine

proof_lines:
without S-adenosylmethionine
in presence of S-adenosylmethionine
at 0.06 mM S-adenosylmethionine

enzyme: threonine synthase

substrate: O-phosphohomoserine


enzyme_display_name: gamma-glutamylcyclotransferase

substrate_name: glutathione

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

enzyme: gamma-glutamylcyclotransferase

substrate: glutathione


enzyme_display_name: ent-kaurene synthase

substrate_name: [15-3H]ent-copalyl diphosphate

proof_lines: pseudo-binding constant for [15-3H]ent-copalyl diphosphate with GST-recombinant kaurene synthase

enzyme: ent-kaurene synthase

substrate: [15-3H]ent-copalyl diphosphate


organism: Anas platyrhynchos

substrate_name: N(omega)-(L-Arginino)succinate

proof_lines: delta-crystallin Ia and delta-crystallin IIa

substrate: N(omega)-(L-Arginino)succinate


enzyme_display_name: dolabella-3,7-dien-18-ol synthase

substrate_name: geranylgeranyl diphosphate

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

enzyme: dolabella-3,7-dien-18-ol synthase

substrate: geranylgeranyl diphosphate


organism: Allium tuberosum

substrate_name: S-ethyl-L-Cys sulfoxide

column_label: Official Wiley/FEBS ePDF Results section reports Km 2.7 mM for S-ethyl-L-cysteine sulfoxide as substrate for purified Allium tuberosum alliinase.

raw_value_unit_evidence: Km raw_value=2.7 raw_unit=mM

row_label: purified alliinase from A. tuberosum with S-ethyl-L-cysteine sulfoxide substrate

table_label: Wiley ePDF Results - purification and properties of alliinase from A. tuberosum

substrate: S-ethyl-L-Cys sulfoxide


organism: Arthrobacter globiformis


enzyme_display_name: amorpha-4,11-diene synthase

organism: Artemisia annua

sequence_source: UniProtKB/Swiss-Prot Q9AR04 FASTA

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

enzyme: amorpha-4,11-diene synthase


substrate_name: (2E,6E)-farnesyl diphosphate

substrate: (2E,6E)-farnesyl diphosphate


organism: Arthrobacter sp.

substrate_name: inulin

proof_lines:
with MW of inulin taken as 5000 Da
pH 5.5, 55°C

substrate: inulin


enzyme_display_name: pectin lyase

organism: Aspergillus flavus

substrate_name: Pectin

enzyme: pectin lyase

substrate: Pectin


substrate_name: citrus pectin

substrate: citrus pectin


enzyme_display_name: pectate lyase

organism: Aspergillus nidulans

substrate_name: rhamnogalacturonan-I

enzyme: pectate lyase

substrate: rhamnogalacturonan-I


organism: Aspergillus japonicus

substrate_name: pectin 26% methylated

substrate: pectin 26% methylated


enzyme_display_name: mannuronate-specific alginate lyase

organism: Azotobacter vinelandii phage

substrate_name: alginate

proof_lines: bacterial alginate containing 25.5% mannuronic acid, determined on the basis of polymeric mannuronic acid available in the substrate

proof_lines: algal alginate containing 31.5% mannuronic acid, determined on the basis of polymeric mannuronic acid available in the substrate

proof_lines: bacterial alginate containing 55% mannuronic acid, determined on the basis of polymeric mannuronic acid available in the substrate

enzyme: mannuronate-specific alginate lyase

substrate: alginate


enzyme_display_name: cystathionine gamma-lyase

organism: Bacillus cereus

substrate_name: L-cystathionine

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

enzyme: cystathionine gamma-lyase

substrate: L-cystathionine


organism: Bacillus licheniformis

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


organism: Azotobacter vinelandii


substrate_name: pyruvate

substrate: pyruvate


proof_lines:
wild type enzyme, at pH 7.2 and 30°C
wild type enzyme, at pH 7.0 and 30°C


enzyme_display_name: aspartate ammonia-lyase

organism: Bacillus sp. (in: firmicutes)

substrate_name: L-aspartate

enzyme: aspartate ammonia-lyase

substrate: L-aspartate


organism: Bacillus sp. RN1

substrate_name: Polygalacturonate

proof_lines: pH 10.0, temperature not specified in the publication

substrate: Polygalacturonate


organism: Bacillus subtilis

substrate_name: L-serine

proof_lines: pH 7, temperature not specified in the publication, 100 mM KCl

proof_lines: pH 7, temperature not specified in the publication, 300 mM KCl

substrate: L-serine


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

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

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


enzyme_display_name: 7-carboxy-7-deazaguanine synthase

proof_lines: pH 7,4, temperature not specified in the publication, recombinant enzyme

enzyme: 7-carboxy-7-deazaguanine synthase


substrate_name: fumarate

proof_lines: co-substrate: NH3, pH 7.5, 37?, free-enzyme

proof_lines: co-substrate: NH3, pH 7.5, 37?, LentiKats-immobilized enzyme

proof_lines: co-substrate: NH3, pH 7.5, 37?, EupergitC-immobilized enzyme

substrate: fumarate


enzyme_display_name: 3-dehydroshikimate dehydratase

organism: Bacillus thuringiensis

enzyme: 3-dehydroshikimate dehydratase


enzyme_display_name: heparin lyase

organism: Bacteroides thetaiotaomicron

substrate_name: heparin

enzyme: heparin lyase

substrate: heparin


enzyme_display_name: adenylosuccinate lyase

substrate_name: adenylsuccinate

enzyme: adenylosuccinate lyase

substrate: adenylsuccinate


enzyme_display_name: dimethylpropiothetin dethiomethylase

organism: Streptococcus oralis

substrate_name: L-Cysteine; H2O

enzyme: dimethylpropiothetin dethiomethylase

substrate: L-Cysteine; H2O


organism: Streptococcus salivarius

substrate_name: H2O; L-Cysteine

substrate: H2O; L-Cysteine


organism: Streptococcus sobrinus


enzyme_display_name: alliin lyase

organism: Allium ampeloprasum

substrate_name: S-allyl-L-Cys sulfoxide

enzyme: alliin lyase

substrate: S-allyl-L-Cys sulfoxide


enzyme_display_name: phenylalanine ammonia-lyase

organism: Bambusa oldhamii

substrate_name: L-phenylalanine

proof_lines: recombinant enzyme, in 50 mM Tris-HCl, pH 8.5, at 37°C

proof_lines: recombinant enzyme expressed in Escherichia coli, at 37°C and pH 8.5

enzyme: phenylalanine ammonia-lyase

substrate: L-phenylalanine


enzyme_display_name: 6-pyruvoyltetrahydropterin synthase

organism: Bombyx mori

substrate_name: 7,8-dihydroneopterin triphosphate

enzyme: 6-pyruvoyltetrahydropterin synthase

substrate: 7,8-dihydroneopterin triphosphate


enzyme_display_name: chondroitin AC lyase

organism: Bacteroides stercoris

substrate_name: chondroitin sulfate C

proof_lines:
native protein
recombinant protein

enzyme: chondroitin AC lyase

substrate: chondroitin sulfate C


organism: Brassica juncea

substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


enzyme_display_name: germacrene-A synthase

organism: Barnadesia spinosa

substrate_name: (2E,6E)-farnesyl diphosphate

proof_lines:
isoform GAS1, at pH 7.0 and 23°C
isoform GAS2, at pH 7.0 and 23°C

enzyme: germacrene-A synthase

substrate: (2E,6E)-farnesyl diphosphate


enzyme_display_name: L-serine ammonia-lyase

organism: Campylobacter jejuni

enzyme: L-serine ammonia-lyase


enzyme_display_name: argininosuccinate lyase

organism: Bos taurus

substrate_name: argininosuccinate

proof_lines: Km-value at low concentrations of argininosuccinate

enzyme: argininosuccinate lyase

substrate: argininosuccinate


substrate_name: UDP-N-acetyl-alpha-D-glucosamine

substrate: UDP-N-acetyl-alpha-D-glucosamine


substrate_name: L-aspartate

proof_lines: pH 6.5, recombinant produced and purified AspA enzyme

proof_lines: pH 7.0, recombinant produced and purified AspA enzyme

proof_lines: pH 8.0, recombinant produced and purified AspA enzyme

substrate: L-aspartate


substrate_name: pyruvate

proof_lines: pH and temperature not specified in the publication

substrate: pyruvate


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: (4S)-limonene synthase

organism: Cannabis sativa

substrate_name: geranyl diphosphate

enzyme: (4S)-limonene synthase

substrate: geranyl diphosphate


enzyme_display_name: enoyl-CoA hydratase 2

organism: Candida tropicalis

enzyme: enoyl-CoA hydratase 2


enzyme_display_name: methylglyoxal synthase

organism: Capra hircus

substrate_name: dihydroxyacetone phosphate

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

enzyme: methylglyoxal synthase

substrate: dihydroxyacetone phosphate


substrate_name: heparin

sequence: MADEALQHTFFA

wild_type_sequence: MADEALQHTFFA

proof_lines: Heparin lyase I was purified to homogeneity from Bacteroides stercoris HJ-15.

proof_lines: pH 7.0, 45°C, heparin from porcine mucosa

substrate: heparin


enzyme_display_name: threonine ammonia-lyase

substrate_name: L-Thr

enzyme: threonine ammonia-lyase

substrate: L-Thr


enzyme_display_name: pectate lyase

organism: Cellvibrio japonicus

substrate_name: 89% esterified citrus pectin

enzyme: pectate lyase

substrate: 89% esterified citrus pectin


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

organism: Clostridioides difficile

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: pH 8.0, temperature not specified in the publication

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


organism: Chlamydomonas reinhardtii


organism: Cichorium intybus

substrate_name: 2-trans,6-trans-farnesyl diphosphate

substrate: 2-trans,6-trans-farnesyl diphosphate


enzyme_display_name: ethanolamine ammonia-lyase

organism: Clostridium sp.

substrate_name: ethanolamine

smiles: C(CO)N

enzyme: ethanolamine ammonia-lyase

substrate: ethanolamine


organism: Brassica rapa subsp. oleifera

substrate_name: L-Phe

substrate: L-Phe


organism: Corynebacterium sp.


enzyme_display_name: 3-dehydroshikimate dehydratase

organism: Corynebacterium glutamicum

proof_lines: pH 7.5, 20°C, N-terminal domain (N-QsuB)

enzyme: 3-dehydroshikimate dehydratase


organism: Cucumis sativus

proof_lines:
at low substrate concentrations
at high substrate concentrations


enzyme_display_name: methylaspartate ammonia-lyase

organism: Carboxydothermus hydrogenoformans

substrate_name: (2S,3S)-3-ethylaspartic acid

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

proof_lines:
pH 9, 30°C
pH 9, 70°C

enzyme: methylaspartate ammonia-lyase

substrate: (2S,3S)-3-ethylaspartic acid


enzyme_display_name: DNA-(apurinic or apyrimidinic site) lyase

organism: Daucus carota

substrate_name: alkylated-depurinated DNA

proof_lines: ratio dT:dU is 15, partially depyrimidinated by uracil-DNA glycosylase, pH 8

substrate: alkylated-depurinated DNA


enzyme_display_name: ent-kaurene synthase

organism: Cucurbita maxima

substrate_name: copalyl diphosphate

enzyme: ent-kaurene synthase

substrate: copalyl diphosphate


enzyme_display_name: peptidylamidoglycolate lyase

enzyme: peptidylamidoglycolate lyase


organism: Deinococcus radiodurans

substrate_name: THF.T DNA duplex

enzyme: DNA-(apurinic or apyrimidinic site) lyase

substrate: THF.T DNA duplex


organism: Clostridium acetobutylicum


enzyme_display_name: D-serine ammonia-lyase

organism: Dictyostelium discoideum

substrate_name: D-serine

enzyme: D-serine ammonia-lyase

substrate: D-serine


enzyme_display_name: cyanase

organism: Ectopseudomonas oleovorans

substrate_name: CNO-

enzyme: cyanase

substrate: CNO-


enzyme_display_name: mannuronate-specific alginate lyase

organism: Ectopseudomonas mendocina

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

enzyme: mannuronate-specific alginate lyase

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


organism: Cricetulus griseus

substrate_name: 18-mer containing P33-labeled tetrahydrofuran

proof_lines: enzyme phosphorylated by casein kinase II, pH 7.5, 22°C

proof_lines: enzyme dephosphorylated by lambda phosphatase, pH 7.5, 22°C


organism: Drosophila melanogaster


enzyme_display_name: aspartate ammonia-lyase

organism: Escherichia coli

substrate_name: L-aspartate

enzyme: aspartate ammonia-lyase

substrate: L-aspartate


organism: Dickeya chrysanthemi

substrate_name: galacturonan

substrate: galacturonan


enzyme_display_name: o-succinylbenzoate synthase

enzyme: o-succinylbenzoate synthase


substrate_name: L-aspartate 4-semialdehyde

proof_lines:
at 30°C, in 100 mM HEPES buffer, pH 8.0
pH 8.0

substrate: L-aspartate 4-semialdehyde


enzyme_display_name: L-serine ammonia-lyase

substrate_name: Unknown

enzyme: L-serine ammonia-lyase

substrate: Unknown


substrate_name: Cyanate

substrate: Cyanate


enzyme_display_name: threonine synthase

enzyme: threonine synthase


enzyme_display_name: methylglyoxal synthase

substrate_name: dihydroxyacetone phosphate

enzyme: methylglyoxal synthase

substrate: dihydroxyacetone phosphate


enzyme_display_name: guluronate-specific alginate lyase

organism: Flammeovirga sp. NJ-04

proof_lines:
at pH 8.0 and 40°C
pH 7.0, 50°C

enzyme: guluronate-specific alginate lyase


substrate_name: L-serine

proof_lines:
pH 8.0, 37°C
anaerobically isolated enzyme, pH 8.0

substrate: L-serine


substrate_name: adenosylcobalamin

substrate: adenosylcobalamin


enzyme_display_name: phenylalanine ammonia-lyase

organism: Fagopyrum esculentum

enzyme: phenylalanine ammonia-lyase


enzyme_display_name: trichodiene synthase

organism: Fusarium graminearum

substrate_name: (2E,6E)-farnesyl diphosphate

enzyme: trichodiene synthase

substrate: (2E,6E)-farnesyl diphosphate


enzyme_display_name: D-lactate dehydratase

substrate_name: methylglyoxal

smiles: CC(=O)C=O

proof_lines: pH 7.5, temperature not specified in the publication, wild-type enzyme

enzyme: D-lactate dehydratase

substrate: methylglyoxal


enzyme_display_name: chorismate synthase

enzyme: chorismate synthase


enzyme_display_name: threonine ammonia-lyase

organism: Geobacillus stearothermophilus

substrate_name: L-Thr

proof_lines:
at 40°C
at 65°C

enzyme: threonine ammonia-lyase

substrate: L-Thr


organism: Glycine max

substrate_name: L-Phe

substrate: L-Phe


enzyme_display_name: (+)-delta-cadinene synthase

organism: Gossypium arboreum

proof_lines: in presence of 0.25 mM inorganic disphosphate, pH and temperature not specified in the publication

enzyme: (+)-delta-cadinene synthase


substrate_name: alginate

substrate: alginate


enzyme_display_name: N-acetylmuramic acid 6-phosphate etherase

organism: Haemophilus influenzae


enzyme_display_name: germacrene-A synthase

organism: Helianthus annuus

enzyme: germacrene-A synthase


organism: Gossypium hirsutum

substrate_name: 2-trans,6-trans-farnesyl diphosphate

substrate: 2-trans,6-trans-farnesyl diphosphate


enzyme_display_name: 3-dehydroquinate synthase

organism: Helicobacter pylori

proof_lines: contains 5 functional groups (OH, COOH and phosphate)

enzyme: 3-dehydroquinate synthase


substrate_name: nerolidyl diphosphate

proof_lines: pH 7.5, 30°C, recombinant CDN1-C1 enzyme

substrate: nerolidyl diphosphate


enzyme_display_name: argininosuccinate lyase

organism: Homo sapiens

substrate_name: argininosuccinate

enzyme: argininosuccinate lyase

substrate: argininosuccinate


substrate_name: arginine

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

substrate: arginine


enzyme_display_name: DNA-(apurinic or apyrimidinic site) lyase

substrate_name: 43-mer oligonucleotide containing apurinic/apyrimidinic sites


substrate_name: oligomer with G/U pair

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -15, so it is treated as a source-provided variant sequence.

enzyme: DNA-(apurinic or apyrimidinic site) lyase

substrate: oligomer with G/U pair


enzyme_display_name: 6-pyruvoyltetrahydropterin synthase

enzyme: 6-pyruvoyltetrahydropterin synthase


enzyme_display_name: adenylosuccinate lyase

substrate_name: adenylosuccinate

proof_lines:
histidine-tagged enzyme
none-tagged enzyme

enzyme: adenylosuccinate lyase

substrate: adenylosuccinate


substrate_name: 43-mer oligonucleotide containing the AP-site analog THF at nt 31


organism: Fusarium sporotrichioides

substrate_name: farnesyl diphosphate

substrate: farnesyl diphosphate


assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: isoform HCAD4, in 50 mM HEPES-NaOH (pH 7.4), 150 mM NaCl, 10% (v/v) glycerol, 1 mM dithiothreitol, 1 mM phenylmethylsulfonyl fluoride, at 37°C

proof_lines: isoform HCAD1, in 50 mM HEPES-NaOH (pH 7.4), 150 mM NaCl, 10% (v/v) glycerol, 1 mM dithiothreitol, 1 mM phenylmethylsulfonyl fluoride, at 37°C

proof_lines: isoform HCAD3, in 50 mM HEPES-NaOH (pH 7.4), 150 mM NaCl, 10% (v/v) glycerol, 1 mM dithiothreitol, 1 mM phenylmethylsulfonyl fluoride, at 37°C


substrate_name: 12-mer oligodeoxyribonucleotide containing a natural AP site


substrate_name: 30mer THF-T duplex

proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme

substrate: 30mer THF-T duplex


enzyme_display_name: gamma-glutamylcyclotransferase

proof_lines: pH 6.5, temperature not specified in the publication

proof_lines: pH 8.0, temperature not specified in the publication

enzyme: gamma-glutamylcyclotransferase


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


proof_lines: pH 6.8, 37°C, nucleotide incison repair activity

proof_lines: pH 6.8, 37°C,nucleotide incison repair activity


substrate_name: 7,8-dihydroneopterin triphosphate

proof_lines: pH 7.4, 37°C, shows positive cooperativity

substrate: 7,8-dihydroneopterin triphosphate


enzyme_display_name: vetispiradiene synthase

organism: Hyoscyamus muticus

substrate_name: trans,trans-farnesyl diphosphate

proof_lines:
recombinant enzyme
native enzyme

enzyme: vetispiradiene synthase

substrate: trans,trans-farnesyl diphosphate


organism: Hordeum vulgare


organism: Lactuca sativa

substrate_name: Unknown

substrate: Unknown


substrate_name: glutathione

substrate: glutathione


enzyme_display_name: ethanolamine ammonia-lyase

organism: Klebsiella aerogenes

substrate_name: ethanolamine

enzyme: ethanolamine ammonia-lyase

substrate: ethanolamine


enzyme_display_name: L-serine ammonia-lyase

organism: Legionella pneumophila

substrate_name: L-serine

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

proof_lines: pH 7, temperature not specified in the publication

proof_lines: pH 7.0, temperature not specified in the publication, native enzyme

enzyme: L-serine ammonia-lyase

substrate: L-serine


organism: Limosilactobacillus fermentum

substrate_name: L-Ser

substrate: L-Ser


enzyme_display_name: phenylalanine ammonia-lyase

organism: Ipomoea batatas

substrate_name: L-Phenylalanine

proof_lines:
at low substrate concentrations
at high substrate concentrations

substrate: L-Phenylalanine


organism: Listeria monocytogenes

proof_lines: pH and temperature not specified in the publication


organism: Micrococcus luteus

substrate_name: thymidine-labeled DNA

substrate: thymidine-labeled DNA


organism: Ligilactobacillus murinus


organism: Mus musculus


organism: Medicago sativa

substrate_name: L-Phe

proof_lines:
enzyme form 1
enzyme form 2
enzyme form 3

substrate: L-Phe


organism: Musca domestica


organism: Mycobacterium tuberculosis

substrate_name: NADH

assay_conditions_summary: cofactor NADH

proof_lines: kinetics of reduction of the MtCS-bound FMNox is determined using fixed amount of holoenzyme and varying levels of NADH

substrate: NADH


enzyme_display_name: threonine synthase

substrate_name: O-phospho-L-homoserine

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

enzyme: threonine synthase

substrate: O-phospho-L-homoserine


enzyme_display_name: isochorismate lyase

enzyme: isochorismate lyase


substrate_name: succinyladenosine monophosphate

substrate: succinyladenosine monophosphate


proof_lines:
wild type enzyme, at pH 7.5 and 25°C
pH 7.4, 25°C, wild-type enzyme


enzyme_display_name: dihydroxy-acid dehydratase

enzyme: dihydroxy-acid dehydratase


organism: Mycolicibacterium smegmatis

proof_lines: pH 7, temperature not specified in the publication, Vmax: 11.7/min/mg


enzyme_display_name: 5-epiaristolochene synthase

organism: Nicotiana tabacum

substrate_name: (2E,6E)-farnesyl diphosphate

proof_lines:
wild-type, pH 7.5, 30°C
wild-type, pH 8.0, 30°C

enzyme: 5-epiaristolochene synthase

substrate: (2E,6E)-farnesyl diphosphate


enzyme_display_name: demethyl-4-deoxygadusol synthase

organism: Nostoc punctiforme

substrate_name: D-sedoheptulose 7-phosphate

smiles: C(C(C(C(C(C(=O)CO)O)O)O)O)OP(=O)(O)O

enzyme: demethyl-4-deoxygadusol synthase

substrate: D-sedoheptulose 7-phosphate


organism: Mortierella alpina


enzyme_display_name: choline trimethylamine-lyase

organism: Oleidesulfovibrio alaskensis

substrate_name: choline

smiles: C[N+](C)(C)CCO

proof_lines: calculated from the EPR activation measurement, recombinant enzyme, pH 8.0, temperature not specified in the publication

enzyme: choline trimethylamine-lyase

substrate: choline


organism: Escherichia coli


organism: Oryza sativa

enzyme: phenylalanine ammonia-lyase


enzyme_display_name: ectoine synthase

organism: Paenibacillus lautus

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

enzyme: ectoine synthase


enzyme_display_name: thebaine synthase

organism: Papaver somniferum

substrate_name: salutaridinol 7-O-acetate

proof_lines: allosteric enzyme, Ka value, pH not specified in the publication, temperature not specified in the publication

enzyme: thebaine synthase

substrate: salutaridinol 7-O-acetate


organism: Olea europaea

substrate_name: L-phenylalanine

proof_lines: enzyme from cultivar Verdial, in 37.5 mM borate buffer pH 8.8, at 40°C

proof_lines: enzyme from cultivar Arbequina, in 37.5 mM borate buffer pH 8.8, at 40°C

proof_lines: enzyme from cultivar Frantonio, in 37.5 mM borate buffer pH 8.8, at 40°C

substrate: L-phenylalanine


organism: Paracoccus seriniphilus


enzyme_display_name: heparin lyase

organism: Pedobacter heparinus

substrate_name: heparin pentasaccharide

column_label: Printed page 553/PDF page 5, Table 3, sole heparinase-I/pentasaccharide row, Km (uM) column, cell 18.

raw_value_unit_evidence: Table 3 reports Km raw_value=18 raw_unit=uM; the footnote states hyperbolic-fit optimization and standard errors below 10%.

row_label: Heparinase I / synthetic heparin pentasaccharide

table_label: Table 3. Kinetic constants for heparinase I acting on pentasaccharide at 30 C

enzyme: heparin lyase

substrate: heparin pentasaccharide


enzyme_display_name: ethanolamine-phosphate phospho-lyase

organism: Oryctolagus cuniculus

substrate_name: Ethanolamine phosphate

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

enzyme: ethanolamine-phosphate phospho-lyase

substrate: Ethanolamine phosphate


enzyme_display_name: pectin lyase

organism: Penicillium citrinum

substrate_name: Pectin

enzyme: pectin lyase

substrate: Pectin


substrate_name: heparin

substrate: heparin


enzyme_display_name: heparin-sulfate lyase

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

proof_lines: recombinant wild-type enzyme, pH 7.6, 35°C

enzyme: heparin-sulfate lyase


enzyme_display_name: pectate lyase

organism: Paenibacillus polymyxa

substrate_name: Polygalacturonate

enzyme: pectate lyase

substrate: Polygalacturonate


enzyme_display_name: histidine ammonia-lyase

organism: Oncorhynchus mykiss

substrate_name: L-histidine

assay_conditions_summary: pH 9

enzyme: histidine ammonia-lyase

substrate: L-histidine


organism: Pinus taeda


organism: Petroselinum crispum

substrate_name: L-propargylglycine

smiles: C#CCC(C(=O)O)N

substrate: L-propargylglycine


enzyme_display_name: (+)-car-3-ene synthase

organism: Picea sitchensis

substrate_name: geranyl diphosphate

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

proof_lines: pH 7.4, 30°C, proteins from both susceptible and resistant plants have similar kinetic parameters

enzyme: (+)-car-3-ene synthase

substrate: geranyl diphosphate


enzyme_display_name: dihydroneopterin aldolase

organism: Pneumocystis carinii

enzyme: dihydroneopterin aldolase


enzyme_display_name: L-serine ammonia-lyase

organism: Peptoniphilus asaccharolyticus

substrate_name: L-Ser

enzyme: L-serine ammonia-lyase

substrate: L-Ser


organism: Pinus contorta


enzyme_display_name: chorismate synthase

organism: Plasmodium falciparum

substrate_name: Unknown

proof_lines: theoretical Ki value obtained using AUTODOCK software version 4, pH not specified in the publication, temperature not specified in the publication

enzyme: chorismate synthase

substrate: Unknown


enzyme_display_name: methylglyoxal synthase

organism: Proteus vulgaris

substrate_name: dihydroxyacetone phosphate

proof_lines:
enzyme form II
enzyme form I

enzyme: methylglyoxal synthase

substrate: dihydroxyacetone phosphate


enzyme_display_name: patchoulol synthase

organism: Pogostemon cablin

assay_conditions_summary: pH 7; 303.15 K; buffer MES reaction

proof_lines: pH 6.4, 34°C, recombinant enzyme, in MES reaction buffer

enzyme: patchoulol synthase


enzyme_display_name: guluronate-specific alginate lyase

organism: Pseudoalteromonas carrageenovora

substrate_name: sodium alginate

proof_lines: without salt additive, at pH 8.0 and 50°C

proof_lines: in the presence of 1 M KCl, at pH 8.0 and 50°C

proof_lines: in the presence of 300 mM KCl, at pH 8.0 and 50°C

enzyme: guluronate-specific alginate lyase

substrate: sodium alginate


organism: Pseudomonas aeruginosa

substrate_name: L-aspartate 4-semialdehyde

proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme

substrate: L-aspartate 4-semialdehyde


enzyme_display_name: D-serine ammonia-lyase

substrate_name: D-serine

proof_lines: pH and temperature not specified in the publication

enzyme: D-serine ammonia-lyase

substrate: D-serine


organism: Pseudomonas fluorescens


organism: Pseudomonas putida


enzyme_display_name: isoprene synthase

organism: Populus trichocarpa

substrate_name: dimethylallyl diphosphate

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

enzyme: isoprene synthase

substrate: dimethylallyl diphosphate


enzyme_display_name: isochorismate lyase

organism: Mycobacterium tuberculosis

substrate_name: isochorismate

enzyme: isochorismate lyase

substrate: isochorismate


organism: Pseudomonas marginalis


proof_lines:
competitive inhibition
mixed inhibition


enzyme_display_name: aspartate ammonia-lyase

substrate_name: L-aspartate

proof_lines: pH 8.8, 30°C, enzyme covalently immobilized on epoxy-functionalized magnetic nanoparticles

enzyme: aspartate ammonia-lyase

substrate: L-aspartate


enzyme_display_name: threonine synthase

organism: Raphanus sativus

substrate_name: O-phosphohomoserine

enzyme: threonine synthase

substrate: O-phosphohomoserine


organism: Pseudomonas sp.


organism: Rattus norvegicus

substrate_name: L-threonine

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

proof_lines: in presence and in absence of 20 mM NH4Cl

substrate: L-threonine


enzyme_display_name: enoyl-CoA hydratase 2

enzyme: enoyl-CoA hydratase 2


enzyme_display_name: mannuronate-specific alginate lyase

substrate_name: alginate

proof_lines:
protein PA1167, pH 7.5, 37°C
AlgL

enzyme: mannuronate-specific alginate lyase

substrate: alginate


organism: Populus alba


substrate_name: L-serine

proof_lines:
pH 8.3, 37°C
37°C, pH 8.3, recombinant SDH
in presence of 20 mM NH4Cl

substrate: L-serine


enzyme_display_name: DNA-(apurinic or apyrimidinic site) lyase


enzyme_display_name: peptidylamidoglycolate lyase

proof_lines: 37°C, pH 7.4, with endoprotease Arg-C digested PAM-3 protein

enzyme: peptidylamidoglycolate lyase


enzyme_display_name: dimethylpropiothetin dethiomethylase

organism: Ruegeria pomeroyi

substrate_name: dimethylsulfoxonium propionate

enzyme: dimethylpropiothetin dethiomethylase

substrate: dimethylsulfoxonium propionate


organism: Roseateles saccharophilus


enzyme_display_name: ethanolamine-phosphate phospho-lyase

substrate_name: Ethanolamine phosphate

enzyme: ethanolamine-phosphate phospho-lyase

substrate: Ethanolamine phosphate


enzyme_display_name: casbene synthase

organism: Ricinus communis

substrate_name: geranylgeranyl diphosphate

enzyme: casbene synthase

substrate: geranylgeranyl diphosphate


substrate_name: dansyl-Tyr-Val-Gly

substrate: dansyl-Tyr-Val-Gly


enzyme_display_name: D-lactate dehydratase

organism: Saccharomyces cerevisiae

substrate_name: methylglyoxal

proof_lines: recombinant ScHsp31, pH and temperature not specified in the publication

enzyme: D-lactate dehydratase

substrate: methylglyoxal


enzyme_display_name: adenylosuccinate lyase

enzyme: adenylosuccinate lyase


enzyme_display_name: chorismate synthase

enzyme: chorismate synthase


enzyme_display_name: 6-pyruvoyltetrahydropterin synthase

organism: Salmo salar

substrate_name: 7,8-Dihydroneopterin 3'-triphosphate

enzyme: 6-pyruvoyltetrahydropterin synthase

substrate: 7,8-Dihydroneopterin 3'-triphosphate


substrate_name: glutathione

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

substrate: glutathione


substrate_name: 37mer with AP/A

enzyme: DNA-(apurinic or apyrimidinic site) lyase

substrate: 37mer with AP/A


enzyme_display_name: ethanolamine ammonia-lyase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: ethanolamine

proof_lines: reconstituted EAL (from EutB and EutC subunits), pH 7.5, 25°C

enzyme: ethanolamine ammonia-lyase

substrate: ethanolamine


smiles: CC(CN)O

proof_lines: dissociation constant for interaction with holo-EAL


enzyme_display_name: threonine ammonia-lyase

substrate_name: L-Thr

proof_lines:
with AMP
in the presence of 5 mM AMP
in the presence of 5 mM CMP

enzyme: threonine ammonia-lyase

substrate: L-Thr


enzyme_display_name: diaminopropionate ammonia-lyase

enzyme: diaminopropionate ammonia-lyase


enzyme_display_name: ornithine cyclodeaminase

organism: Sinorhizobium meliloti

substrate_name: L-ornithine

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

assay_conditions_summary: cofactor NAD+

proof_lines: 0.5 mM NAD+ and 0.1 mM L-arginine, strain GR4

enzyme: ornithine cyclodeaminase

substrate: L-ornithine


smiles: CC(CO)N


enzyme_display_name: dihydroxy-acid dehydratase

organism: Spinacia oleracea

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

enzyme: dihydroxy-acid dehydratase


enzyme_display_name: dihydroneopterin aldolase

organism: Staphylococcus aureus

substrate_name: glycoaldehyde

smiles: C(C=O)O

enzyme: dihydroneopterin aldolase

substrate: glycoaldehyde


enzyme_display_name: (-)-5-epieremophilene synthase

organism: Salvia miltiorrhiza

proof_lines:
30°C, pH 7.0, enzyme form SmSTPS3
30°C, pH 7.0, enzyme form SmSTPS2
30°C, pH 7.0, enzyme form SmSTPS1

enzyme: (-)-5-epieremophilene synthase


enzyme_display_name: phenylalanine ammonia-lyase

organism: Solanum tuberosum

substrate_name: L-Phenylalanine

proof_lines:
at low substrate concentrations
at high substrate concentrations

enzyme: phenylalanine ammonia-lyase

substrate: L-Phenylalanine


enzyme_display_name: mannuronate-specific alginate lyase

organism: Sphingomonas sp.

substrate_name: Unknown

enzyme: mannuronate-specific alginate lyase

substrate: Unknown


substrate_name: 5-enolpyruvylshikimate 3-phosphate

substrate: 5-enolpyruvylshikimate 3-phosphate


enzyme_display_name: hyaluronate lyase

organism: Streptococcus pyogenes phage H4489A

substrate_name: hyaluronan

proof_lines:
recombinant enzyme, pH 6.0, 30°C
pH 5.5, 37°C, recombinant enzyme

enzyme: hyaluronate lyase

substrate: hyaluronan


organism: Streptococcus equi subsp. equi 4047

substrate_name: hyaluronic acid

proof_lines: concentration expressed as the concentration of its disaccharide unit (equivalent to 0.29 mg/ml)

substrate: hyaluronic acid


organism: Streptococcus sp.

substrate_name: hyaluronate

substrate: hyaluronate


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

proof_lines: wild type enzyme, 0.680 using Lathyrus sativus seed extracts as substrate


enzyme_display_name: histidine ammonia-lyase

organism: Streptomyces griseus

substrate_name: L-histidine

proof_lines: histidine ammonia-lyase (histidase; HutH) has been purified to homogeneity from Streptomyces griseus

proof_lines: the N-terminal amino acid sequence used to clone the histidase-encoding structural gene, hutH

enzyme: histidine ammonia-lyase

substrate: L-histidine


enzyme_display_name: pentalenene synthase

organism: Streptomyces sp.

substrate_name: (E,E)-farnesyl diphosphate

enzyme: pentalenene synthase

substrate: (E,E)-farnesyl diphosphate


organism: Streptococcus equi subsp. zooepidemicus


enzyme_display_name: cis-L-3-hydroxyproline dehydratase

organism: Roseibium aggregatum

proof_lines: pH 8.0, temperature not specified in the publication

enzyme: cis-L-3-hydroxyproline dehydratase


enzyme_display_name: imidazole glycerol-phosphate synthase

organism: Thermotoga maritima

substrate_name: L-glutamine

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

proof_lines: pH 8.0, 25°C, wild-type HisH-HisF complex

proof_lines: pH 8.0, 37°C, wild-type enzyme, activated by 1 mM 5-[(5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide

enzyme: imidazole glycerol-phosphate synthase

substrate: L-glutamine


organism: Sus scrofa


proof_lines: pH 6.0, 25°C, recombinant wild-type enzyme


organism: Streptomyces venezuelae

proof_lines: pH 8, 25°C, in presence of 0.1 mM S-adenosyl-L-methionine


organism: Triticum aestivum

substrate_name: L-Phe

substrate: L-Phe


enzyme_display_name: guluronate-specific alginate lyase

organism: Vibrio sp. NJU-03

enzyme: guluronate-specific alginate lyase


enzyme_display_name: DNA-(apurinic or apyrimidinic site) lyase

organism: Toxoplasma gondii


enzyme_display_name: cyanase

organism: Thiohalophilus thiocyanatoxydans

substrate_name: Cyanate

proof_lines: cyanate concentrations between 0.2 mM and 1 mM, in presence of 3 mM NaHCO3, at 37°C and pH 7.5

enzyme: cyanase

substrate: Cyanate


organism: Vitis vinifera

proof_lines: versus L-aspartate-4-semialdehyde, pH 8.0, 30°C, recombinant enzyme


enzyme_display_name: chorismate dehydratase

organism: Thermus thermophilus

substrate_name: chorismate

proof_lines: pH and temperature not specified in the publication

enzyme: chorismate dehydratase

substrate: chorismate


enzyme_display_name: threonine ammonia-lyase

organism: Thermus sp.


organism: Arabidopsis thaliana


organism: Zea mays

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


organism: Petroselinum crispum

substrate_name: trans-cinnamate

substrate: trans-cinnamate


enzyme_display_name: adenylosuccinate lyase

organism: Homo sapiens

substrate_name: adenylsuccinate

proof_lines:
50 mM HEPES, pH 7.0, 25°C
inhibition kinetics, overview

enzyme: adenylosuccinate lyase

substrate: adenylsuccinate


enzyme_display_name: galactonate dehydratase

organism: Haloferax volcanii

substrate_name: D-galactonate

enzyme: galactonate dehydratase

substrate: D-galactonate


enzyme_display_name: Delta(6)-protoilludene synthase

organism: Stereum hirsutum

substrate_name: (2E,6E)-farnesyl diphosphate

enzyme: Delta(6)-protoilludene synthase

substrate: (2E,6E)-farnesyl diphosphate


proof_lines: in the absence of N'-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide, pH and temperature not specified in the publication


enzyme_display_name: tuliposide A-converting enzyme

organism: Tulipa gesneriana

substrate_name: tuliposide F

enzyme: tuliposide A-converting enzyme

substrate: tuliposide F


proof_lines: at low substrate substrate concentrations


enzyme_display_name: (S)-beta-bisabolene synthase

enzyme: (S)-beta-bisabolene synthase


enzyme_display_name: diaminopropionate ammonia-lyase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

proof_lines:
pH 7.5, 37°C
pH 7.4, 30°C, sDAPL

enzyme: diaminopropionate ammonia-lyase


organism: Thermotoga maritima


enzyme_display_name: ethanolamine-phosphate phospho-lyase

organism: Oryctolagus cuniculus

substrate_name: H2O; Ethanolamine phosphate

enzyme: ethanolamine-phosphate phospho-lyase

substrate: H2O; Ethanolamine phosphate


organism: Rattus norvegicus


enzyme_display_name: hyaluronate lyase

organism: Streptococcus pyogenes

substrate_name: Hyaluronate

substrate: Hyaluronate


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

organism: Gracilariopsis sp.

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


enzyme_display_name: histidine ammonia-lyase

organism: Delftia acidovorans

substrate_name: Histidine

substrate: Histidine


substrate_name: NH3; Urocanate

substrate: NH3; Urocanate


enzyme_display_name: argininosuccinate lyase

organism: Sus scrofa

substrate_name: N(omega)-(L-Arginino)succinate

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

enzyme: argininosuccinate lyase

substrate: N(omega)-(L-Arginino)succinate


enzyme_display_name: phenylalanine ammonia-lyase

organism: Fagopyrum esculentum

substrate_name: L-Phenylalanine

enzyme: phenylalanine ammonia-lyase

substrate: L-Phenylalanine


organism: Triticum aestivum

substrate_name: L-Aspartate 4-semialdehyde; Pyruvate

substrate: L-Aspartate 4-semialdehyde; Pyruvate


enzyme_display_name: mannonate dehydratase

organism: Chromohalobacter israelensis

substrate_name: D-mannonate

enzyme: mannonate dehydratase

substrate: D-mannonate


organism: Pisum sativum


organism: Solanum lycopersicum


organism: Homo sapiens

substrate_name: L-Threonine

enzyme: threonine ammonia-lyase

substrate: L-Threonine


organism: Arabidopsis thaliana

substrate_name: L-Tyrosine

substrate: L-Tyrosine


enzyme_display_name: UniProt E5Y378

organism: Bilophila wadsworthia

substrate_name: isethionate

enzyme: UniProt E5Y378

substrate: isethionate


enzyme_display_name: S-adenosyl-L-methionine lyase

organism: Escherichia coli

substrate_name: S-adenosyl-L-methionine

enzyme: S-adenosyl-L-methionine lyase

substrate: S-adenosyl-L-methionine


enzyme_display_name: isethionate sulfite-lyase

organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough)

enzyme: isethionate sulfite-lyase


enzyme_display_name: DDT-dehydrochlorinase

organism: Anopheles dirus

enzyme: DDT-dehydrochlorinase


enzyme_display_name: canavanine-gamma-lyase

organism: Pseudomonas alvandae

substrate_name: L-canavanine

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

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

enzyme: canavanine-gamma-lyase

substrate: L-canavanine


organism: Pseudomonas putida


organism: Corynebacterium sp.

substrate_name: S-adenosyl-L-methionine chloride

substrate: S-adenosyl-L-methionine chloride


substrate_name: S-adenosyl-L-methionine iodide

substrate: S-adenosyl-L-methionine iodide


substrate_name: Unknown

proof_lines: competitive inhibitor to S-adenosylmethionine

substrate: Unknown


organism: Pseudomonas canavaninivorans

substrate_name: canavanine

substrate: canavanine


organism: Drosophila melanogaster


organism: Musca domestica


organism: Nitratidesulfovibrio vulgaris


substrate_name: glutathione

substrate: glutathione


organism: Enterobacteria phage T3


enzyme_display_name: (2S)-3-sulfopropanediol sulfolyase

proof_lines:
pH 7.5, 23°C
Raw SKiD Env: Temp=23°C, pH=7.5

enzyme: (2S)-3-sulfopropanediol sulfolyase


enzyme_display_name: ribonuclease T1

organism: Bacillus amyloliquefaciens

proof_lines: poly(I) substrate, measurement is performed in 10 mM Tris, pH 7.0, containing 0.14 M NaCl and 0.1 mM EDTA

enzyme: ribonuclease T1


organism: Bos taurus

proof_lines: poly(I) * poly(C) substrate, measurement is performed in 10 mM Tris, pH 7.0, containing 0.14 M NaCl and 0.1 mM EDTA


enzyme_display_name: ribotoxin

organism: Aspergillus restrictus

substrate_name: SRL

proof_lines: sarcin/ricin loop in ribosomal RNA, 10 mM Tris-HCl, 0-5 mM KCl, pH 7-7.4, 37°C

enzyme: ribotoxin

substrate: SRL


organism: Bacillus intermedius


enzyme_display_name: Bacillus subtilis ribonuclease

organism: Bacillus subtilis

substrate_name: pre-tRNAAsp

proof_lines: R60C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue

enzyme: Bacillus subtilis ribonuclease

substrate: pre-tRNAAsp


proof_lines: R65C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue


proof_lines: R7C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue


proof_lines: D15C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue


proof_lines: N61C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue


proof_lines: R68C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue


proof_lines: wild-type, single turnover cleavage rate constant kobs


proof_lines: K64C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue


proof_lines: H3C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue


proof_lines: D42C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue


proof_lines: R62C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue


proof_lines: E40C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue


organism: Aspergillus giganteus

substrate_name: ApA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H50Q with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

proof_lines:
pH 7.0, 37°C, mutant H50Q
pH 5.0, 37°C, mutant H50Q

substrate: ApA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R121Q with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R121K with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L145F with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y48F with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


proof_lines:
wild-type
pH 5.0, 37°C, wild-type


organism: Desulfovibrio desulfuricans

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


organism: Kitasatospora aureofaciens

substrate_name: poly(I)

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D79E to reconstruct the assayed variant sequence.

substrate: poly(I)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D79N to reconstruct the assayed variant sequence.


organism: Ustilago sphaerogena

substrate_name: GpC

proof_lines:
RNase N1
RNase U1
RNase T1

substrate: GpC


proof_lines: R45C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue


proof_lines: V46C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue


proof_lines: Q38C mutant, single turnover cleavage rate constant kobs, protein contains an AOP modification at the cysteine residue


organism: Bilophila wadsworthia (strain 3_1_6)

proof_lines: kcat is 26 sec(-1) with (2S)-3-sulfopropanediol as substrate. kcat is 0.57 sec(-1) with isethionate as substrate.


organism: Aspergillus oryzae

proof_lines:
pH 6.0, 25°C, N43H mutant
pH 7.5, 25°C, N43H


proof_lines:
pH 6.0, 25°C, Q46_P47insQ mutant
pH 6.0, 25°C, Q46_Q47insP mutant
pH 6.0, 25°C, Q46_P47insP mutant


proof_lines:
pH 6.0, 25°C, N43T mutant
pH 7.5, 25°C, N43T


proof_lines:
pH 6.0, 25°C, Y45S mutant
pH 7.5, 25°C, Y45S


proof_lines:
pH 6.0, 25°C, N44H mutant
pH 7.5, 25°C, N44H


proof_lines:
pH 6.0, 25°C, N43I mutant
pH 7.5, 25°C, N43I


substrate_name: RNA

proof_lines:
pH 7.5, 25°C, N43G
pH 6.0, 25°C, N43G mutant

substrate: RNA


substrate_name: polyinosinic acid

substrate: polyinosinic acid


substrate_name: guanosine-2',3'-cyclic monophosphate

substrate: guanosine-2',3'-cyclic monophosphate


substrate_name: 30 nt RNA

proof_lines:
RNase J2
RNase J1/J2 complex
RNase J1

substrate: 30 nt RNA


substrate_name: GpA

substrate: GpA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q38A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D79K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D79R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D79W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D79I to reconstruct the assayed variant sequence.


substrate_name: GpU

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

proof_lines: poly(I) substrate, measurement is performed in 10 mM Tris, pH 7.0, containing 0.14 M NaCl and 0.1 mM EDTA

substrate: GpU


enzyme_display_name: Enterobacter ribonuclease

organism: Enterobacter sp.

proof_lines: pH and temperature not specified in the publication

enzyme: Enterobacter ribonuclease


enzyme_display_name: L-piperazate synthase

organism: Kutzneria sp. 744

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

proof_lines: as-purified enzyme (oxidized), at pH 8.0 and 26°C

proof_lines: dithionite-reduced enzyme, at pH 8.0 and 26°C

enzyme: L-piperazate synthase


organism: Penicillium brevicompactum

proof_lines: poly(A) * poly(U) substrate, measurement is performed in 10 mM Tris, pH 7.0, containing 0.14 M NaCl and 0.1 mM EDTA


substrate_name: GpG

substrate: GpG


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

proof_lines:
pH 7.06, 25°C, 5K mutant
pH 7.50, 25°C, 5K mutant
pH 8.10, 25°C, 5K mutant


proof_lines:
pH 6.50, 25°C, wild-type enzyme
pH 6.05, 25°C, wild-type enzyme
pH 5.60, 25°C, wild-type enzyme


organism: Rhizobium leguminosarum bv. trifolii (strain WSM2304)

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

column_label: Results state: With a KM of 390 +/- 13 microM and a kcat of 1.23 +/- 0.011 s^-1 RCanγL displayed kinetic parameters similar to CanγL.

raw_value_unit_evidence: Km raw_value=390 +/- 13 raw_unit=microM

row_label: rhizobial canavanine-gamma-lyase (RCanγL, WP_012555980.1) with canavanine

table_label: PMC full-text PMID 36320885 / Results paragraph and Fig. 6C caption


organism: Bilophila wadsworthia

substrate_name: isethionate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F682Y with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

proof_lines: mutant F682Y, pH 7.5, 30°C, glycyl radical normalized value

substrate: isethionate