sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W374F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; buffer reaction; cofactor NADH

column_label: Table 2 row W374F; columns KM = 11 mM, kcat observed = 0.063 s^-1, glycyl radical normalized kcat = 0.133 s^-1, catalytic efficiency using normalized kcat = 12 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=0.133 normalized_unit=s^-1; km normalized_value=11.0 normalized_unit=mM; kcat_over_km normalized_value=0.012 normalized_unit=s^-1*mM^-1; conversions=12/1000 for catalytic efficiency from M^-1 to mM^-1

raw_value_unit_evidence: KM raw_value=11 raw_unit=mM; observed kcat raw_value=0.063 raw_unit=s^-1; normalized kcat raw_value=0.133 raw_unit=s^-1; kcat/Km raw_value=12 raw_unit=s^-1 M^-1

table_label: Table 2. Activation and kinetics of IslA variants from reactions repeated in triplicate


enzyme_display_name: isethionate sulfite-lyase

organism: Bilophila wadsworthia

substrate_name: isethionate

source_db: brenda

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F682A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: mutant F682A, pH 7.5, 30°C, glycyl radical normalized value

data_origin: experimental

enzyme: isethionate sulfite-lyase

substrate: isethionate

status: unverified

source: brenda


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W374Y to reconstruct the assayed variant sequence.

proof_lines: mutant W374Y, pH 7.5, 30°C, glycyl radical normalized value


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I192A to reconstruct the assayed variant sequence.

column_label: Table 2 row I192A; columns KM = 12 mM, kcat observed = 0.40 s^-1, glycyl radical normalized kcat = 1.9 s^-1, catalytic efficiency using normalized kcat = 160 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=1.9 normalized_unit=s^-1; km normalized_value=12.0 normalized_unit=mM; kcat_over_km normalized_value=0.16 normalized_unit=s^-1*mM^-1; conversions=160/1000 for catalytic efficiency from M^-1 to mM^-1

raw_value_unit_evidence: KM raw_value=12 raw_unit=mM; observed kcat raw_value=0.40 raw_unit=s^-1; normalized kcat raw_value=1.9 raw_unit=s^-1; kcat/Km raw_value=160 raw_unit=s^-1 M^-1

status: corrected


mutation_signature: Unknown

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

column_label: Table 2 row Wild-type; columns KM = 8 mM, kcat observed = 2.0 s^-1, glycyl radical normalized kcat = 9.5 s^-1, catalytic efficiency using normalized kcat = 1200 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=9.5 normalized_unit=s^-1; km normalized_value=8.0 normalized_unit=mM; kcat_over_km normalized_value=1.2 normalized_unit=s^-1*mM^-1; conversions=1200/1000 for catalytic efficiency from M^-1 to mM^-1

raw_value_unit_evidence: KM raw_value=8 raw_unit=mM; observed kcat raw_value=2.0 raw_unit=s^-1; normalized kcat raw_value=9.5 raw_unit=s^-1; kcat/Km raw_value=1200 raw_unit=s^-1 M^-1

row_label: Wild-type


enzyme_display_name: ribonuclease T1

organism: Kitasatospora aureofaciens

substrate_name: poly(I)

verification_status: verified

kcat_over_km_display: Not reported

sequence_variant_note: Resolved canonical sequence from uniprot:P05798 and applied mutation signature E54Q to reconstruct the assayed variant sequence.

column_label: Chrome PDF page 3/5, printed page 154, Table 1, E54Q row: kcat column 0.7 s^-1 and KM column 0.32 mM; assay header states pH 6.2 and 25 C; footnote says parameters were obtained from Figs. 3 and 4.

normalized_value_unit_evidence: kcat normalized_value=0.7 normalized_unit=s^-1; KM normalized_value=0.32 normalized_unit=mM.

raw_value_unit_evidence: Table 1 E54Q row: kcat raw_value=0.7 raw_unit=s^-1; KM raw_value=0.32 raw_unit=mM. The table also prints kcat/KM=0.002 in units of 10^6 M^-1 s^-1 and KiI=1.15 mM.

table_label: PMID 15158454 Table 1: parameters for catalysis of poly(I) cleavage by RNase Sa and E54Q at pH 6.2 and 25 C

enzyme: ribonuclease T1

substrate: poly(I)

status: verified


proof_lines:
25°C, pH 6.2, wild-type enzyme
25°C, pH 6.5, wild-type enzyme


enzyme_display_name: UniProt Q76K71

organism: Rhodococcus sp. N-771

source_db: skid

kcat_display: Not reported

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt Q76K71

source: skid


enzyme_display_name: UniProt P22830

organism: Homo sapiens

enzyme: UniProt P22830


substrate_name: porphyrin

substrate: porphyrin


enzyme_display_name: UniProt P32396

organism: Bacillus subtilis

enzyme: UniProt P32396


proof_lines:
Raw SKiD Env: Temp=-----, pH=7.4
Raw SKiD Env: Temp=21°C, pH=7.4


substrate_name: mesoporphyrin IX

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

substrate: mesoporphyrin IX


substrate_name: protoporphyrin IX

substrate: protoporphyrin IX


substrate_name: deuteroporphyrin IX

substrate: deuteroporphyrin IX


enzyme_display_name: aliphatic aldoxime dehydratase

organism: Rhodococcus erythropolis

substrate_name: (Z)-phenylacetaldoxime

km_display: Not reported

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H320A to reconstruct the assayed variant sequence.

enzyme: aliphatic aldoxime dehydratase

substrate: (Z)-phenylacetaldoxime


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E143Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S219A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F306A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R178Q with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


enzyme_display_name: indoleacetaldoxime dehydratase

organism: Sclerotinia sclerotiorum

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

proof_lines: in 25 mM Tris-HCl buffer pH 7.5, at 23°C

enzyme: indoleacetaldoxime dehydratase


organism: Bacillus sp. OxB-1

proof_lines:
ferric oxidation state, pH 7.0, 23°C
ferrous oxidation state, pH 7.0, 23°C


organism: Fusarium fujikuroi


enzyme_display_name: protoporphyrin ferrochelatase

organism: Mus musculus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K250M/V251L/W256Y with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines: mutant K250M/V251L/W256Y, under strictly anaerobic conditions

enzyme: protoporphyrin ferrochelatase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V251L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q248P/S249G/K250P/G252W with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S249A/K250Q/V251C with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines: mutant S249A/K250Q/V251C, under strictly anaerobic conditions


source_db: oed

source: oed


enzyme_display_name: phenylacetaldoxime dehydratase

organism: Pseudomonas putida

substrate_name: 3-pyridine aldoxime

enzyme: phenylacetaldoxime dehydratase

substrate: 3-pyridine aldoxime


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M267I to reconstruct the assayed variant sequence.

proof_lines: mutant M267I, heterodimer, room temperature

proof_lines: mutant M267I, homodimer, room temperature


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C236Y to reconstruct the assayed variant sequence.

proof_lines: mutant C236Y, heterodimer, room temperature

proof_lines: mutant C236Y, homodimer, room temperature


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature P334L to reconstruct the assayed variant sequence.

proof_lines: mutant P334L, homodimer, room temperature


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K379N to reconstruct the assayed variant sequence.

proof_lines: mutant K379N, homodimer, room temperature

proof_lines: mutant K379N, heterodimer, room temperature


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F682A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

smiles: O=S(=O)(O)CCO

assay_conditions_summary: pH 7.5; 303.15 K; buffer reaction; cofactor NADH

column_label: Table 2 row F682A; columns KM = 6.8 mM, kcat observed = 0.0171 s^-1, glycyl radical normalized kcat = 0.154 s^-1, catalytic efficiency using normalized kcat = 23 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=0.154 normalized_unit=s^-1; km normalized_value=6.8 normalized_unit=mM; kcat_over_km normalized_value=0.023 normalized_unit=s^-1*mM^-1; conversions=23/1000 for catalytic efficiency from M^-1 to mM^-1

raw_value_unit_evidence: KM raw_value=6.8 raw_unit=mM; observed kcat raw_value=0.0171 raw_unit=s^-1; normalized kcat raw_value=0.154 raw_unit=s^-1; kcat/Km raw_value=23 raw_unit=s^-1 M^-1


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

column_label: Table 2 row F682Y; columns KM = 8 mM, kcat observed = 0.0074 s^-1, glycyl radical normalized kcat = 0.023 s^-1, catalytic efficiency using normalized kcat = 2.9 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=0.023 normalized_unit=s^-1; km normalized_value=8.0 normalized_unit=mM; kcat_over_km normalized_value=0.0029 normalized_unit=s^-1*mM^-1; conversions=2.9/1000 for catalytic efficiency from M^-1 to mM^-1

raw_value_unit_evidence: KM raw_value=8 raw_unit=mM; observed kcat raw_value=0.0074 raw_unit=s^-1; normalized kcat raw_value=0.023 raw_unit=s^-1; kcat/Km raw_value=2.9 raw_unit=s^-1 M^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I192A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W374F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W374Y to reconstruct the assayed variant sequence.


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


enzyme_display_name: geranyllinalool synthase

organism: Solanum lycopersicum

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

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

proof_lines: pH and temperature not specified in the publication

enzyme: geranyllinalool synthase

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


substrate_name: geranylgeranyl diphosphate

substrate: geranylgeranyl diphosphate


organism: Nicotiana attenuata


enzyme_display_name: lactoylglutathione lyase

organism: Chlamydomonas reinhardtii

substrate_name: methylglyoxal

smiles: CC(=O)C=O

enzyme: lactoylglutathione lyase

substrate: methylglyoxal


enzyme_display_name: UniProt Q84AR1

organism: Citrobacter freundii

substrate_name: L-methionine

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=7.2
Raw SKiD Env: Temp=30°C, pH=8

enzyme: UniProt Q84AR1

substrate: L-methionine


substrate_name: DL-homocysteine

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

substrate: DL-homocysteine


substrate_name: S-ethyl-L-cysteine

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

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

substrate: S-ethyl-L-cysteine


substrate_name: S-Benzyl-L-cysteine

substrate: S-Benzyl-L-cysteine


substrate_name: L-cysteine

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

substrate: L-cysteine


substrate_name: S-methyl-L-cysteine

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

substrate: S-methyl-L-cysteine


enzyme_display_name: UniProt Q86D28

organism: Entamoeba histolytica

substrate_name: O-acetyl-L-serine

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

enzyme: UniProt Q86D28

substrate: O-acetyl-L-serine


substrate_name: alliin

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

substrate: alliin


substrate_name: methiin

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

substrate: methiin


substrate_name: ethiin

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

substrate: ethiin


organism: Pseudomonas chlororaphis

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

sequence_source: multiple

proof_lines:
ferric oxidation state, pH 7.0, 23°C
ferrous oxidation state, pH 7.0, 23°C
Raw SKiD Env: Temp=23°C, pH=7

source_databases_merged: brenda skid


enzyme_display_name: kunzeaol synthase

organism: Elaeoselinum garganicum

proof_lines: pH 7.5, temperature not specified in the publication

proof_lines: kcat is 0.03 sec(-1) with farnesyl diphosphate as substrate (at pH 7.5 and 28 degrees Celsius).

source_databases_merged: brenda uniprot

enzyme: kunzeaol synthase


enzyme_display_name: methionine gamma-lyase

enzyme: methionine gamma-lyase


organism: Fusobacterium nucleatum subsp. nucleatum

substrate_name: L-Cysteine

substrate: L-Cysteine


enzyme_display_name: L-3-cyanoalanine synthase

organism: Oryza sativa

substrate_name: HCN

smiles: C#N

enzyme: L-3-cyanoalanine synthase

substrate: HCN


proof_lines: recombinant enzyme from Saccharomyces cerevisiae

proof_lines: recombinant enzyme from Arabidopsis thaliana


organism: Colias croceus

substrate_name: hydrogen sulfide

smiles: S

substrate: hydrogen sulfide


organism: Bacillus subtilis (strain 168)

substrate_name: Fe(2+) (at 30 degrees Celsius, pH 7.0 and in microaerobic conditions (1 ppm dissolved oxygen))

source_db: uniprot

assay_conditions_summary: pH 7

proof_lines: kcat is 0.25 sec(-1) with Fe(2+) as substrate (at 30 degrees Celsius, pH 7.0 and in microaerobic conditions (1 ppm dissolved oxygen)) (PubMed:23764491). kcat is 0.65 sec(-1) with Fe(2+) as substrate (at 30 degrees Celsius, pH 7.0, in microa

source: uniprot


substrate_name: H(2)O(2) (at 30 degrees Celsius, pH 7.0 and in microaerobic conditions (1 ppm dissolved oxygen))

smiles: [Ho]


organism: Lathyrus latifolius

substrate_name: cyanide

substrate: cyanide


organism: Lupinus sp.

substrate_name: cysteine

substrate: cysteine


substrate_name: KCN

substrate: KCN


smiles: C(CS)O


organism: Anthocharis cardamines


organism: Micromonospora echinospora

substrate_name: L-Methionine

substrate: L-Methionine


substrate_name: L-methionine

substrate: L-methionine


organism: Homo sapiens


substrate_name: methylglyoxal

substrate: methylglyoxal


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M157Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 1 columns: Glyoxalase I, kcat [s^-1], Km [uM], and kcat/Km [s^-1 uM^-1]; uM-based values converted to mM-based units where needed.

raw_value_unit_evidence: Table 1 row M157Q reports kcat 1650 +/- 67 s^-1, Km 162 +/- 17 uM, and kcat/Km 10 s^-1 uM^-1.

table_label: Table 1: Kinetic constants of human glyoxalase I mutant forms determined with the hemithioacetal of GSH and methylglyoxal


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M157H with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

raw_value_unit_evidence: Table 1 row M157H reports kcat 300 +/- 8 s^-1, Km 89 +/- 8 uM, and kcat/Km 3 s^-1 uM^-1.


organism: Aporia crataegi

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


substrate_name: L-cysteine


organism: Gonepteryx rhamni


organism: Zonocerus variegatus


substrate_name: NaCN

substrate: NaCN


organism: Zygaena filipendulae


substrate: L-cysteine


organism: Vicia sativa subsp. nigra


organism: Plutella xylostella


organism: Citrobacter intermedius


organism: Cladosporium cladosporioides


organism: Aspergillus sp.


organism: Zea mays


organism: Aloe vera


organism: Mytilus galloprovincialis


enzyme_display_name: 7-epizingiberene synthase [(2Z,6Z)-farnesyl diphosphate cyclizing]

organism: Solanum habrochaites

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

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

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


organism: Fusarium graminearum

substrate_name: (E/Z)-n-capronaldoxime

substrate: (E/Z)-n-capronaldoxime


substrate_name: (E/Z)-indoleacetaldoxime

substrate: (E/Z)-indoleacetaldoxime


substrate_name: (E/Z)-n-butyraldoxime

smiles: CCCC=NO

substrate: (E/Z)-n-butyraldoxime


substrate_name: (Z)-phenylacetaldehyde oxime

substrate: (Z)-phenylacetaldehyde oxime


organism: Entamoeba histolytica

substrate_name: DL-homocysteine

proof_lines:
wild-type ehMGL2, pH 7.0, 37°C
wild-type ehMGL1, pH 7.0, 37°C

substrate: DL-homocysteine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C110G with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C113S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y108F with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C110S with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


substrate_name: O-acetyl-L-serine

proof_lines:
wild-type ehMGL1, pH 7.0, 37°C
wild-type ehMGL2, pH 7.0, 37°C

substrate: O-acetyl-L-serine


organism: Cyberlindnera mrakii


organism: Laurus nobilis

substrate_name: geranylgeranyl diphosphate

column_label: PMC Results prose states that the Km and Vmax values of partially purified LnTPS3 with GGPP as the substrate were 30.5 +/- 4.7 uM and 7.3 +/- 0.3 pmol/ng protein*min.

raw_value_unit_evidence: Km raw_value=30.5 +/- 4.7 uM raw_unit=uM

row_label: Partially purified LnTPS3 / GGPP

table_label: PMC Results prose / Biochemical characterization of LnTPS3

substrate: geranylgeranyl diphosphate


organism: Trichomonas vaginalis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature C116G with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature C113G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Rattus norvegicus

substrate_name: p-methoxyphenylglyoxal

substrate: p-methoxyphenylglyoxal


substrate_name: p-phenylphenylglyoxal

substrate: p-phenylphenylglyoxal


substrate_name: p-chlorophenylglyoxal

substrate: p-chlorophenylglyoxal


substrate_name: p-hydroxyphenylglyoxal

substrate: p-hydroxyphenylglyoxal


organism: Spodoptera littoralis

substrate_name: hydrogen sulfide

substrate: hydrogen sulfide


organism: Synechocystis sp.

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


proof_lines: mutant enzyme FeChDELTA347, at pH 8.0 and 30°C


substrate_name: protoporphyrin IX

proof_lines: wild type enzyme, with Zn2+ as cosubstrate, at pH 8.0 and 30°C

substrate: protoporphyrin IX


proof_lines: mutant enzyme FeChDELTA347, with Zn2+ as cosubstrate, at pH 8.0 and 30°C


organism: Pseudomonas chlororaphis

proof_lines: kcat is 5.4 min(-1) with butyraldoxime as substrate. kcat is 5.6 min(-1) with acetaldoxime as substrate. kcat is 0.090 min(-1) with pyridine-2-aldoxime as substrate.

source_databases_merged: brenda skid uniprot


substrate_name: (E/Z)-acetaldoxime

smiles: CC=NO

substrate: (E/Z)-acetaldoxime


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

substrate_name: L-methionine

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.

substrate: L-methionine


substrate_name: L-homocysteine

substrate: L-homocysteine


substrate_name: L-cysteine

substrate: L-cysteine


proof_lines:
36°C, pH 6.8, recombinant EhMGL1
36°C, pH 6.8, recombinant EhMGL2
Raw SKiD Env: Temp=37°C, pH=7


proof_lines:
36°C, pH 6.8, recombinant EhMGL2
36°C, pH 6.8, recombinant EhMGL1
Raw SKiD Env: Temp=37°C, pH=7


enzyme_display_name: nephthenol synthase

organism: Streptomyces sp

enzyme: nephthenol synthase


organism: Bacillus sp. (in: firmicutes)

substrate_name: (Z)-phenylacetaldoxime

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H282G to reconstruct the assayed variant sequence.

proof_lines: H282G mutant in the presence of pyridine

proof_lines: H282G mutant in the presence of 4-chloropyridine

proof_lines: H282G mutant in the presence of 4-methylimidazole

substrate: (Z)-phenylacetaldoxime


organism: Tetranychus urticae

proof_lines: pH 8.5, 37°C, recombinant His-tagged enzyme


organism: Homo sapiens

substrate_name: porphyrin

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F337A to reconstruct the assayed variant sequence.

substrate: porphyrin


substrate_name: mesoporphyrin

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H388A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

substrate: mesoporphyrin


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: Pseudomonas putida

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


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

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


substrate_name: (Z)-phenylacetaldehyde oxime

assay_conditions_summary: pH 7; cofactor FMN

proof_lines: pH.0, 30°C, aerobic conditions, Na2SO3 substitutes for FMN

substrate: (Z)-phenylacetaldehyde oxime


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M157A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 1 columns Glyoxalase I, kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1); Km converted from uM to mM and kcat/Km multiplied by 1000 for mM^-1.

raw_value_unit_evidence: Table 1 row M157A reports kcat 260 +/- 13 s^-1, Km 74 +/- 10 uM, and kcat/Km 4 s^-1 uM^-1.


substrate_name: glutathione

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

substrate: glutathione


substrate_name: trypanothione

substrate: trypanothione


organism: Glycine max

substrate_name: hydrogen cyanide

column_label: Table 1 columns kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1) for row Gm-CAS under KCN give 39.2, 0.26, and 150,769.

row_label: Gm-CAS / CAS reaction substrate KCN

table_label: Table 1. Kinetic Comparison of Gm-CAS and Gm-OASS Substrate Specificities.

substrate: hydrogen cyanide


substrate_name: L-Cysteine

column_label: Table 1 columns kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1) for row Gm-CAS under Cys give 38.9, 0.81, and 48,024.

row_label: Gm-CAS / CAS reaction substrate Cys

substrate: L-Cysteine


organism: Arabidopsis thaliana

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

proof_lines: kcat is 9.5 sec(-1) with L-methionine as substrate, 8.9 sec(-1) with L-ethionine as substrate, 36.2 sec(-1) with L-homocysteine as substrate and 11.6 sec(-1) with seleno-L-methionine as substrate at pH 8 and 30 degrees Celsius.


organism: Novispirillum itersonii

column_label: The abstract reports apparent Km for Fe2+ is 9.5 micrometer in the presence of 20 micrometer CuCl2.

raw_value_unit_evidence: Km raw_value=9.5 micrometer raw_unit=micrometer

row_label: Prose segment: Fe2+ Km with copper

table_label: PubMed PMID 21163 abstract


organism: Rhodococcus erythropolis

substrate_name: Z-phenylacetaldoxime (with Na(2)S)

substrate: Z-phenylacetaldoxime (with Na(2)S)


organism: Rhodococcus globerulus

substrate_name: (E/Z)-n-valeraldoxime

substrate: (E/Z)-n-valeraldoxime


substrate_name: (Z)-naphthoacetaldoxime

substrate: (Z)-naphthoacetaldoxime


enzyme_display_name: cysteine-S-conjugate beta-lyase

organism: Spinacia oleracea

substrate_name: L-selenocystathionine

smiles: C(C[Se]CC(C(=O)O)N)C(C(=O)O)N

enzyme: cysteine-S-conjugate beta-lyase

substrate: L-selenocystathionine


substrate_name: L-cystine

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

substrate: L-cystine


substrate_name: AdoMet

substrate: AdoMet


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


enzyme_display_name: UniProt Q8ZNT7

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: D-cysteine

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

enzyme: UniProt Q8ZNT7

substrate: D-cysteine


enzyme_display_name: UniProt Q99735

enzyme: UniProt Q99735


substrate_name: methylglyoxal

smiles: CC(=O)C=O

proof_lines:
presence of Zn2+, 37°C, pH 6.6
presence of Ni2+, 37°C, pH 6.6
presence of Co2+, 37°C, pH 6.6

substrate: methylglyoxal


substrate_name: Unknown

assay_conditions_summary: pH 8

substrate: Unknown


organism: Entamoeba histolytica

substrate_name: trifluoromethionine

substrate: trifluoromethionine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y111F to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -11, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R58A with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


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


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


organism: Trichomonas vaginalis

substrate_name: L-ethionine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature C113G with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

substrate: L-ethionine


organism: Rattus norvegicus

substrate_name: m-methoxyphenylglyoxal

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

substrate: m-methoxyphenylglyoxal


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)


proof_lines: kcat is 120 min(-1) for O(3)-acetyl-L-serine for the cysteine synthase activity, kcat is 90 min(-1) for Na(2)S for the cysteine synthase activity, kcat is 160 min(-1) for cysteine for the L-3-cyanoalanine synthase activity, kcat is 130 min(


organism: Bacillus subtilis (strain 168)

substrate_name: Fe(2+) (at 30 degrees Celsius, pH 7.0, in microaerobic conditions (1 ppm dissolved oxygen) and in presence of 50uM EfeM)

proof_lines: kcat is 0.25 sec(-1) with Fe(2+) as substrate (at 30 degrees Celsius, pH 7.0 and in microaerobic conditions (1 ppm dissolved oxygen)) (PubMed:23764491). kcat is 0.65 sec(-1) with Fe(2+) as substrate (at 30 degrees Celsius, pH 7.0, in microa


organism: Synechocystis sp. PCC 6714

substrate_name: cystine

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

proof_lines: estimated from steady-state measurements

substrate: cystine


organism: Vachellia farnesiana

substrate_name: O-methyl-DL-serine

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

substrate: O-methyl-DL-serine


organism: Wolbachia pipientis

substrate_name: cystathionine

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

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

substrate: cystathionine


enzyme_display_name: D-cysteine desulfhydrase

organism: Scenedesmus fuscus

enzyme: D-cysteine desulfhydrase


organism: Candidatus Pelagibacter communis

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


organism: Pseudomonas putida

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

proof_lines: double mutant Pseudomonas putida E295S+L322T

proof_lines: double mutant Pseudomonas putida E295S/L322T


organism: Thermotoga maritima

assay_conditions_summary: pH 8; 310.15 K; buffer recombinant His-tagged enzyme

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

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

proof_lines: recombinant His-tagged enzyme, pH 8.0, 70°C, bicine buffer


enzyme_display_name: leukotriene-C4 synthase

organism: Homo sapiens

substrate_name: leukotriene A4

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W116A to reconstruct the assayed variant sequence.

proof_lines: pH 7.8, temperature not specified in the publication, recombinant mutant W116A

enzyme: leukotriene-C4 synthase

substrate: leukotriene A4


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W116F to reconstruct the assayed variant sequence.

proof_lines: pH 7.8, temperature not specified in the publication, recombinant mutant W116F


substrate_name: glutathione

substrate: glutathione


enzyme_display_name: selenocysteine lyase

organism: Leuconostoc mesenteroides

substrate_name: L-selenocysteine

smiles: C(C(C(=O)O)N)[SeH]

enzyme: selenocysteine lyase

substrate: L-selenocysteine


organism: Synechococcus elongatus


substrate_name: L-djenkolate

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

substrate: L-djenkolate


substrate_name: S-methyl-L-cysteine

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

substrate: S-methyl-L-cysteine


organism: Penicillium citrinum


organism: Arabidopsis thaliana

proof_lines: kcat is 1700 min(-1) with methylglyoxal as substrate. kcat is 2200 min(-1) with glutathione as substrate.


substrate_name: L-methionine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C166H with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.

substrate: L-methionine


substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: DL-homocysteine

substrate: DL-homocysteine


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


substrate_name: methylglyoxal

substrate: methylglyoxal


organism: Malus sylvestris

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Spinacia oleracea

substrate_name: L-cystathionine

substrate: L-cystathionine


organism: Solanum lycopersicum

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y152F with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y151G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y151F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


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.


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

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


substrate_name: Na(2)S for the cysteine synthase activity


substrate_name: L-cysteine for the L-3-cyanoalanine synthase activity


substrate_name: KCN for the L-3-cyanoalanine synthase activity


organism: Malus domestica

substrate_name: S-methylmethionine

proof_lines: kcat is 9 sec(-1) per monomer with S-adenosyl-L-methionine as substrate (PubMed:7809054). kcat is 1.8 sec(-1) with L-vinylglycine as substrate (PubMed:10704193). kcat is 2.7 min(-1) with S-methylmethionine as substrate (PubMed:14678788).

substrate: S-methylmethionine


organism: Brevibacterium aurantiacum

substrate_name: L-homocysteine

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

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

substrate: L-homocysteine


organism: Mimosa pudica

substrate_name: L,L-cystathionine

proof_lines: kcat is 12180 sec(-1) with L-mimosine as substrate (PubMed:31368041). kcat is 310 sec(-1) with L,L-cystathionine as substrate (PubMed:31368041).

substrate: L,L-cystathionine


substrate_name: L-ethionine (at pH 8 and 30 degrees Celsius)

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

proof_lines: kcat is 9.5 sec(-1) with L-methionine as substrate, 8.9 sec(-1) with L-ethionine as substrate, 36.2 sec(-1) with L-homocysteine as substrate and 11.6 sec(-1) with seleno-L-methionine as substrate at pH 8 and 30 degrees Celsius.


substrate_name: L-homocysteine (at pH 8 and 30 degrees Celsius)


substrate_name: seleno-L-methionine (at pH 8 and 30 degrees Celsius)

smiles: C[Se]CCC(C(=O)O)N


substrate_name: L-methionine

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


enzyme_display_name: protoporphyrin ferrochelatase

organism: Mus musculus

substrate_name: protoporphyrin IX

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q248P/S249G/K250P/G252W with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines: mutant Q248P/S249G/K250P/G252W, under strictly anaerobic conditions

substrate: protoporphyrin IX


substrate_name: glutathione

proof_lines: kcat is 19 sec(-1) with glutathione as substrate (PubMed:27365393). kcat is 105 sec(-1) with leukotriene A4 as substrate (PubMed:27365393).


organism: Solanum tuberosum

substrate_name: CN for the L-3-cyanoalanine synthase activity (in the presence of 5 mM L-cysteine)


enzyme_display_name: aliphatic aldoxime dehydratase

organism: Pseudomonas sp.

enzyme: aliphatic aldoxime dehydratase


substrate_name: D-cysteine

proof_lines: kcat is 6 sec(-1) for D-cysteine as substrate.

substrate: D-cysteine


substrate_name: leukotriene A4

substrate: leukotriene A4


organism: Trichomonas vaginalis

substrate_name: L-ethionine

substrate: L-ethionine


organism: Escherichia coli (strain K12)

substrate_name: Unknown

substrate: Unknown


substrate_name: L-mimosine

substrate: L-mimosine


proof_lines: kcat is 21000 sec(-1) with L,L-cystathionine as substrate.


substrate_name: cystathionine

substrate: cystathionine


organism: Rattus norvegicus


organism: Staphylococcus haemolyticus (strain JCSC1435)


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


organism: Homo sapiens

proof_lines: kcat is 0.6 sec(-1) for leukotriene A4 as substrate (PubMed:23409838). kcat is 14.3 sec(-1) for 1-chloro-2,4-dinitrobenzene as substrate (PubMed:23409838). kcat is 0.1 sec(-1) for 5-HPETE as substrate (PubMed:23409838).


organism: Brassica sp.

substrate_name: (R)-S-lactoylglutathione

substrate: (R)-S-lactoylglutathione


organism: Arabidopsis thaliana


organism: Oryza sativa subsp. japonica


enzyme_display_name: cembrene C synthase

organism: Streptomyces sp.

substrate_name: geranylgeranyl diphosphate

enzyme: cembrene C synthase

substrate: geranylgeranyl diphosphate


enzyme_display_name: lactoylglutathione lyase

substrate_name: methylglyoxal/glutathione (native form)

proof_lines: Reduction of GLO1 was carried out by incubation with 20 mM betamercaptoethanol prior to kinetic analysis.

substrate: methylglyoxal/glutathione (native form)


organism: Leishmania braziliensis

ki_unit: mM

proof_lines: pH and temperature not specified in the publication


organism: Leishmania major

substrate_name: trypanothione

proof_lines:
purified enzyme, pH 7.0, 27°C
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=27°C, pH=7

substrate: trypanothione


organism: Citrobacter freundii

substrate_name: O-acetyl-L-serine

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.

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

column_label: Table 1 row O-Ac-L-Ser; C115H MGL column group; columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat 2.93 s^-1; Km 3.68 mM; kcat/Km 0.800 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 O-Ac-L-Ser, C115H MGL columns: kcat 2.93 s^-1; Km 3.68 mM; kcat/Km 8.00 x 10^2 M^-1 s^-1.

row_label: O-Ac-L-Ser; C115H MGL

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

substrate: O-acetyl-L-serine


substrate_name: S-ethyl-L-cysteine

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.

column_label: Table 1 row S-Et-L-Cys; C115A MGL column group; columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat 0.57 s^-1; Km 0.255 mM; kcat/Km 2.24 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 S-Et-L-Cys, C115A MGL columns: kcat 0.57 s^-1; Km 0.255 mM; kcat/Km 2.24 x 10^3 M^-1 s^-1.

row_label: S-Et-L-Cys; C115A MGL

substrate: S-ethyl-L-cysteine


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 S-Et-L-Cys; C115H MGL column group; columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat 6.50 s^-1; Km 0.93 mM; kcat/Km 6.99 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 S-Et-L-Cys, C115H MGL columns: kcat 6.50 s^-1; Km 0.93 mM; kcat/Km 6.99 x 10^3 M^-1 s^-1.

row_label: S-Et-L-Cys; C115H MGL


substrate_name: S-methyl-L-cysteine

column_label: Table 1 row S-Met-L-Cys; C115A MGL column group; columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat 1.38 s^-1; Km 0.80 mM; kcat/Km 1.70 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 S-Met-L-Cys, C115A MGL columns: kcat 1.38 s^-1; Km 0.80 mM; kcat/Km 1.70 x 10^3 M^-1 s^-1.

row_label: S-Met-L-Cys; C115A MGL

substrate: S-methyl-L-cysteine


column_label: Table 1 row S-Met-L-Cys; C115H MGL column group; columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat 23.08 s^-1; Km 2.62 mM; kcat/Km 8.81 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 S-Met-L-Cys, C115H MGL columns: kcat 23.08 s^-1; Km 2.62 mM; kcat/Km 8.81 x 10^3 M^-1 s^-1.

row_label: S-Met-L-Cys; C115H MGL


organism: Escherichia coli

substrate_name: L-Cystathionine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W131F/W188F/W230F/W276F to reconstruct the assayed variant sequence.

substrate: L-Cystathionine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W131F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W131F/W188F/W230F/W276F/W300F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W131F/W188F/W230F/W276F/W300F/W340F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W131F/W188F/W230F/W276F/W340F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W131F/W188F/W230F/W300F/W340F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W131F/W188F/W276F/W300F/W340F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W131F/W230F/W276F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W131F/W230F/W276F/W300F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W131F/W230F/W276F/W300F/W340F to reconstruct the assayed variant sequence.


organism: Pseudomonas putida

substrate_name: L-Cysteine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C116H to reconstruct the assayed variant sequence.

substrate: L-Cysteine


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

column_label: Table 1, wild-type kinetic constants rows; row Wild type / L-cysteine; columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

normalized_value_unit_evidence: Km normalized_value=0.2 normalized_unit=mM; kcat normalized_value=2.13 normalized_unit=s^-1; kcat/Km normalized_value=10.7 normalized_unit=s^-1*mM^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y114F/C116H to reconstruct the assayed variant sequence.


substrate_name: L-Methionine

substrate: L-Methionine


column_label: Table 1, wild-type kinetic constants rows; row Wild type / L-methionine; columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

normalized_value_unit_evidence: Km normalized_value=0.5 normalized_unit=mM; kcat normalized_value=33.4 normalized_unit=s^-1; kcat/Km normalized_value=66.8 normalized_unit=s^-1*mM^-1

row_label: Wild type / L-methionine


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


organism: Entamoeba histolytica

substrate_name: trifluoromethionine

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

substrate: trifluoromethionine


organism: Bordetella avium

assay_conditions_summary: pH 8.5; cofactor NADH

column_label: Table III row S-Aminoethyl-L-cysteine, column Km, reports 470 uM.

row_label: S-Aminoethyl-L-cysteine

table_label: Table III: Kinetic parameters (Vmax and Km) of beta-cystathionase for various substrates


organism: Corynebacterium striatum

substrate_name: (S)-S-benzyl-cysteine

assay_conditions_summary: buffer A

column_label: PMID 17191898 Section 2.5 and Fig. 3 kinetics prose, S-benzyl-(S)-cysteine row/prose, Km = 1.8 mM.

raw_value_unit_evidence: Section 2.5/Fig. 3 kinetics prose reports Km = 1.8 mM for S-benzyl-(S)-cysteine.

row_label: (S)-S-benzyl-cysteine / recombinant metC C-S lyase

table_label: Section 2.5 and Fig. 3 kinetics prose

substrate: (S)-S-benzyl-cysteine


organism: Glycine max

substrate_name: methylglyoxal-glutathione adduct

substrate: methylglyoxal-glutathione adduct


organism: Plasmodium falciparum


substrate_name: alliin

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

substrate: alliin


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.

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

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.

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


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

normalized_value_unit_evidence: kcat 0.22 s^-1; Km 0.301 mM; kcat/Km 0.690 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 L-Met, C115A MGL columns: kcat 0.22 s^-1; Km 0.301 mM; kcat/Km 6.90 x 10^2 M^-1 s^-1.

row_label: L-Met; C115A 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


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

normalized_value_unit_evidence: kcat 5.14 s^-1; Km 0.57 mM; kcat/Km 9.02 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, C115H MGL columns: kcat 5.14 s^-1; Km 0.57 mM; kcat/Km 9.02 x 10^3 M^-1 s^-1.

row_label: Methiin; C115H MGL


substrate_name: O-acetyl-L-homoserine

column_label: Table 1 row O-Ac-L-Hse; C115A MGL column group; columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat 6.23 s^-1; Km 6.00 mM; kcat/Km 1.04 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 O-Ac-L-Hse, C115A MGL columns: kcat 6.23 s^-1; Km 6.00 mM; kcat/Km 1.04 x 10^3 M^-1 s^-1.

row_label: O-Ac-L-Hse; C115A MGL

substrate: O-acetyl-L-homoserine


column_label: Table 1 row O-Ac-L-Hse; C115H MGL column group; columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat 18.29 s^-1; Km 2.46 mM; kcat/Km 7.43 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 O-Ac-L-Hse, C115H MGL columns: kcat 18.29 s^-1; Km 2.46 mM; kcat/Km 7.43 x 10^3 M^-1 s^-1.

row_label: O-Ac-L-Hse; C115H MGL


column_label: Table 1 row O-Ac-L-Ser; C115A MGL column group; columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat 1.35 s^-1; Km 2.88 mM; kcat/Km 0.460 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 O-Ac-L-Ser, C115A MGL columns: kcat 1.35 s^-1; Km 2.88 mM; kcat/Km 4.60 x 10^2 M^-1 s^-1.

row_label: O-Ac-L-Ser; C115A MGL


organism: Malus domestica

substrate_name: L-vinylglycine

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

substrate: L-vinylglycine


organism: Pseudomonas sp.

substrate_name: (E/Z)-isobutyraldoxime

smiles: CC(C)C=NO

substrate: (E/Z)-isobutyraldoxime


substrate_name: (E/Z)-propionaldoxime

smiles: CCC=NO

substrate: (E/Z)-propionaldoxime


substrate_name: (Z)-phenylacetaldoxime

substrate: (Z)-phenylacetaldoxime


substrate_name: (E/Z)-n-butyraldoxime

smiles: CCCC=NO

substrate: (E/Z)-n-butyraldoxime


substrate_name: S-Adenosyl-L-methionine

sequence: MGLPGKNKGAVLSKIATNNQHGENSEYFDG

wild_type_sequence: MGLPGKNKGAVLSKIATNNQHGENSEYFDG

substrate: S-Adenosyl-L-methionine


sequence: MKQLSTKVTSNGHGQDSSYFLGWEEYEKNP

wild_type_sequence: MKQLSTKVTSNGHGQDSSYFLGWEEYEKNP


sequence: MVQLSRKATCNSHGQVSSYFLGWEEYEKNP

wild_type_sequence: MVQLSRKATCNSHGQVSSYFLGWEEYEKNP


sequence: MKQLSRKVTSNAHGQDSSYFLGWEEYEKNP

wild_type_sequence: MKQLSRKVTSNAHGQDSSYFLGWEEYEKNP


sequence: MLSSKVVGDSHGQDSSYFLGWQEYEKNPFH

wild_type_sequence: MLSSKVVGDSHGQDSSYFLGWQEYEKNPFH


sequence: MVAFATEKKQDLNLLSKIASGDGHGENSSY

wild_type_sequence: MVAFATEKKQDLNLLSKIASGDGHGENSSY


sequence: MGLPLMMERSSNNNNVELSRVAVSDTHGED

wild_type_sequence: MGLPLMMERSSNNNNVELSRVAVSDTHGED


sequence: MGLLSKKASCNTHGQDSSYFWGWEEYEKNP

wild_type_sequence: MGLLSKKASCNTHGQDSSYFWGWEEYEKNP


organism: Rhodococcus globerulus

substrate_name: (E/Z)-cyclohexanecarboxaldehyde oxime

substrate: (E/Z)-cyclohexanecarboxaldehyde oxime


assay_conditions_summary: pH 7; buffer pH 7

column_label: ACS Table 2, row Z-PAOx, column Km (mM) = 1.40; abbreviation text maps Z-PAOx to Z-phenylacetaldoxime.

raw_value_unit_evidence: Km=1.40 mM in ACS Table 2 row Z-PAOx, column Km (mM)

row_label: Z-PAOx

table_label: Table 2: Kinetic Parameters of the Enzyme for Various Aldoximes


column_label: ACS Table 2, row Z-3-PPOx, column Km (mM) = 2.31; methods/abbreviation text maps Z-3-PPOx to Z-3-phenylpropionaldoxime.

raw_value_unit_evidence: Km=2.31 mM in ACS Table 2 row Z-3-PPOx, column Km (mM)


substrate_name: (E/Z)-indoleacetaldoxime

column_label: ACS Table 2, row E/Z-indoleacetaldoxime, column Km (mM) = 3.91.

raw_value_unit_evidence: Km=3.91 mM in ACS Table 2 row E/Z-indoleacetaldoxime, column Km (mM)

row_label: E/Z-indoleacetaldoxime

substrate: (E/Z)-indoleacetaldoxime


column_label: ACS Table 2, row E/Z-isobutyraldoxime, column Km (mM) = 5.54.

raw_value_unit_evidence: Km=5.54 mM in ACS Table 2 row E/Z-isobutyraldoxime, column Km (mM)

row_label: E/Z-isobutyraldoxime


substrate_name: L-djenkolate

column_label: Table III row L-Djenkolic acid, column Km, reports 33 uM.

raw_value_unit_evidence: 33 uM

row_label: L-Djenkolic acid

substrate: L-djenkolate


substrate_name: L-cystathionine

column_label: Table III row L-Cystathionine, column Km, reports 70 uM.

raw_value_unit_evidence: 70 uM

row_label: L-Cystathionine

substrate: L-cystathionine


substrate_name: Lanthionine

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

column_label: Table III row Lanthionine*, column Km, reports 104 uM; footnote marks a mixture of DL and meso-lanthionine.

row_label: Lanthionine*

substrate: Lanthionine


substrate_name: S-methyl-L-Cys

column_label: Table III row S-Methyl-L-cysteine, column Km, reports 670 uM.

row_label: S-Methyl-L-cysteine

substrate: S-methyl-L-Cys


substrate_name: D-Cys

substrate: D-Cys


substrate_name: L-Cystathionine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W188F to reconstruct the assayed variant sequence.

substrate: L-Cystathionine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W188F/W230F/W276F/W300F/W340F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W230F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W276F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W300F to reconstruct the assayed variant sequence.


organism: Caenorhabditis elegans

substrate_name: O-acetylserine (at 25 degrees Celsius and pH 7.5)


substrate_name: S-sulfocysteine (at 25 degrees Celsius, pH 8.5 and in absence of dithiothreitol)


substrate_name: cysteine (at 25 degrees Celsius and pH 8.5)


substrate_name: sulfide (at 25 degrees Celsius and pH 7.5)


substrate_name: cyanide (at 25 degrees Celsius and pH 7.5)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K42A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S32A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S33A to reconstruct the assayed variant sequence.


organism: Homo sapiens

substrate_name: glutathione

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R104A to reconstruct the assayed variant sequence.

substrate: glutathione


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31A to reconstruct the assayed variant sequence.


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


substrate_name: leukotriene A4 methyl ester

substrate: leukotriene A4 methyl ester


substrate_name: DL-homocysteine

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

substrate: DL-homocysteine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K240I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K240M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K240N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K240R to reconstruct the assayed variant sequence.


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

column_label: Table 1, wild-type kinetic constants rows; row Wild type / DL-homocysteine; columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

normalized_value_unit_evidence: Km normalized_value=1.1 normalized_unit=mM; kcat normalized_value=71.0 normalized_unit=s^-1; kcat/Km normalized_value=64.5 normalized_unit=s^-1*mM^-1

row_label: Wild type / DL-homocysteine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y114F/C116H to reconstruct the assayed variant sequence.


substrate_name: S-methyl-L-cysteine

substrate: S-methyl-L-cysteine


column_label: Table 1, wild-type kinetic constants rows; row Wild type / S-methyl-L-cysteine; columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

normalized_value_unit_evidence: Km normalized_value=0.7 normalized_unit=mM; kcat normalized_value=1.58 normalized_unit=s^-1; kcat/Km normalized_value=2.26 normalized_unit=s^-1*mM^-1

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y58F with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


substrate_name: S-Benzyl-L-cysteine

substrate: S-Benzyl-L-cysteine


substrate_name: S-ethyl-L-cysteine

substrate: S-ethyl-L-cysteine


substrate_name: S-ethyl-L-homocysteine

substrate: S-ethyl-L-homocysteine


substrate_name: L-Methionine

substrate: L-Methionine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S36E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T40E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: leukotriene A4

substrate: leukotriene A4


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature A366Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; 303.15 K; cofactor NADH

table_label: Table 3


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature P357I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature P360Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature V358Y to reconstruct the assayed variant sequence.


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E163Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E163Q/E318Q with inferred residue-numbering offset -33 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E318Q to reconstruct the assayed variant sequence.


organism: Escherichia coli (strain K12)

substrate_name: L-cysteine sulfinate

assay_conditions_summary: pH 8.5; cofactor NAD+

column_label: Primary-paper JBC Table II reports L-cysteine sulfinic acid Km 0.24 mM; source L-cysteine sulfinate maps to this substrate.

raw_value_unit_evidence: L-cysteine sulfinic acid Km 0.24 mM

row_label: L-cysteine sulfinic acid row

table_label: Table II: Substrate specificity of cysteine sulfinate desulfinase and kinetic constants

substrate: L-cysteine sulfinate


substrate_name: L-selenocysteine

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

column_label: Primary-paper JBC Table II reports L-selenocysteine Km 1.0 mM.

raw_value_unit_evidence: L-selenocysteine Km 1.0 mM

row_label: L-selenocysteine row

substrate: L-selenocysteine


substrate_name: L-cysteine

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

column_label: Primary-paper JBC Table II reports L-cysteine Km 35 mM.

raw_value_unit_evidence: L-cysteine Km 35 mM

row_label: L-cysteine row

substrate: L-cysteine


substrate_name: L-cystine

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

column_label: Primary-paper JBC Table II reports L-cystine Km 3.3 mM.

raw_value_unit_evidence: L-cystine Km 3.3 mM

row_label: L-cystine row

substrate: L-cystine


organism: Solanum tuberosum

substrate_name: L-cysteine for the L-3-cyanoalanine synthase activity (in the presence of 5 mM KCN)


substrate_name: O(3)-acetyl-L-serine for the cysteine synthase activity (in the presence of 2.5 mM Na(2)S)


substrate_name: Na(2)S for the cysteine synthase activity (in the presence of 10 mM O(3)-acetyl-L-serine)


organism: Streptomyces avermitilis

substrate_name: L-homocysteine

substrate: L-homocysteine


substrate_name: L-Cysteine

substrate: L-Cysteine


organism: Mus musculus

column_label: Primary-paper PDF Table II lists L-Selenocysteine with Km (mM) = 9.9.

raw_value_unit_evidence: L-Selenocysteine Km 9.9 mM

row_label: L-Selenocysteine row

table_label: Table II: Substrate specificity and kinetic parameters of mSCL


column_label: Primary-paper PDF Table II lists L-Cysteine sulfinate with Km (mM) = 8.6.

raw_value_unit_evidence: L-Cysteine sulfinate Km 8.6 mM

row_label: L-Cysteine sulfinate row


column_label: Primary-paper PDF Table II lists L-Cysteine with Km (mM) = 5.2.

raw_value_unit_evidence: L-Cysteine Km 5.2 mM

row_label: L-Cysteine row


organism: Rattus norvegicus

substrate_name: L-kynurenine (with 2-oxoglutarate as cosubstrate)


substrate_name: pyruvate

substrate: pyruvate


organism: Spinacia oleracea

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


substrate_name: Na(2)S for the cysteine synthase activity with the recombinant enzyme


substrate_name: L-cysteine for the L-3-cyanoalanine synthase activity with the recombinant enzyme


substrate_name: KCN for the L-3-cyanoalanine synthase activity with the recombinant enzyme


substrate_name: chloroalanine for the cysteine synthase activity with the native enzyme (at pH 8.0)

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


organism: Bacillus subtilis (strain 168)

substrate_name: cystathionine

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

substrate: cystathionine


organism: Porphyromonas gingivalis

substrate_name: L-methionine sulfone

substrate: L-methionine sulfone


substrate_name: L-Methionine


enzyme_display_name: phenylacetaldoxime dehydratase

organism: Bacillus sp. (in: firmicutes)

column_label: PMID 10651646 / DOI 10.1021/bi991598u, Table 3, row Z-3-phenylpropionaldoxime, Km (mM) = 1.36.

raw_value_unit_evidence: Table 3 row Z-3-phenylpropionaldoxime, Km (mM) column = 1.36.

table_label: Table 3: Kinetic Parameters for Various Aldoximes of Phenylacetaldoxime Dehydratase

enzyme: phenylacetaldoxime dehydratase


substrate_name: (E/Z)-indoleacetaldoxime

column_label: PMID 10651646 / DOI 10.1021/bi991598u, Table 3, row E/Z-indoleacetaldoxime, Km (mM) = 2.40.

raw_value_unit_evidence: Table 3 row E/Z-indoleacetaldoxime, Km (mM) column = 2.40.

substrate: (E/Z)-indoleacetaldoxime


substrate_name: (E/Z)-propionaldoxime

column_label: PMID 10651646 / DOI 10.1021/bi991598u, Table 3, row E/Z-propionaldoxime, Km (mM) = 4.32.

raw_value_unit_evidence: Table 3 row E/Z-propionaldoxime, Km (mM) column = 4.32.

row_label: E/Z-propionaldoxime

substrate: (E/Z)-propionaldoxime


substrate_name: (E/Z)-n-butyraldoxime

column_label: PMID 10651646 / DOI 10.1021/bi991598u, Table 3, row E/Z-n-butyraldoxime, Km (mM) = 11.1.

raw_value_unit_evidence: Table 3 row E/Z-n-butyraldoxime, Km (mM) column = 11.1.

row_label: E/Z-n-butyraldoxime

substrate: (E/Z)-n-butyraldoxime


substrate_name: glutathione

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

substrate: glutathione


organism: Schizosaccharomyces pombe

substrate_name: Phenylglyoxal

column_label: Primary paper kinetic-parameters prose states phenylglyoxal Km = 0.24 mM.

normalized_value_unit_evidence: Phenylglyoxal Km normalized 0.24 mM; CatLog Km = 0.24 mM.

raw_value_unit_evidence: The kinetic-parameters prose reports the enzyme was active toward phenylglyoxal and Km for phenylglyoxal was 0.24 mM.

row_label: phenylglyoxal Km in kinetic-parameters prose

table_label: Kinetic parameters of glyoxalase I prose section

substrate: Phenylglyoxal


column_label: Primary paper kinetic-parameters prose states glutathione Km = 0.8 mM.

normalized_value_unit_evidence: Glutathione Km normalized 0.8 mM; CatLog Km = 0.8 mM.

raw_value_unit_evidence: The kinetic-parameters prose reports Km values for methylglyoxal and glutathione were 1.6 and 0.8 mM, respectively.

row_label: glutathione Km in kinetic-parameters prose


substrate_name: methylglyoxal

smiles: CC(=O)C=O

column_label: Primary paper kinetic-parameters prose states methylglyoxal Km = 1.6 mM.

normalized_value_unit_evidence: Methylglyoxal Km normalized 1.6 mM; CatLog Km = 1.6 mM.

row_label: methylglyoxal Km in kinetic-parameters prose

substrate: methylglyoxal


enzyme_display_name: phosphosulfolactate synthase

organism: Methanocaldococcus jannaschii

substrate_name: phosphoenolpyruvate

column_label: Full text reports P-enolpyruvate pseudo first-order apparent kinetic parameters: Vmax = 39 units/mg, Km = 9.8 mm, Ki = 1.9 mm.

raw_value_unit_evidence: Km raw_value=9.8 mm raw_unit=mM

row_label: ComA phosphosulfolactate synthase, P-enolpyruvate varied over full tested range

table_label: JBC full text Figure 2 / kinetic-analysis prose

enzyme: phosphosulfolactate synthase

substrate: phosphoenolpyruvate


substrate_name: sulfite

substrate: sulfite


organism: Malus domestica

substrate_name: S-Adenosyl-L-methionine

substrate: S-Adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y233F to reconstruct the assayed variant sequence.


column_label: Table 4. Catalytic properties of glyoxalase I from yeast and from mammals. 'Source of enzyme' row 'Yeast'; 'Oxoaldehyde substrate' sub-row 'Phenylglyoxal'; column 'Molecular activity, kcat. (min-1)' = 402000; column 'Km (mM)' = 0.21. Table 4 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 4 cell 402000 min-1; the printed column header is 'Molecular activity, kcat. (min-1)', so 402000 / 60 = 6700.0 s^(-1); the exported value is 6700.0 s^(-1). Km: printed Table 4 cell 0.21 mM; the printed column header is 'Km (mM)', already the export's unit, so no conversion is applied; the exported value is 0.21 mM. kcat/Km: the paper prints no kcat/Km cell for this or any other row, so nothing is converted; the exported 31904.761904761905 s^(-1)*mM^(-1) is carried unchanged and typed as the quotient of this row's own two confirmed printed components.

raw_value_unit_evidence: Table 4 (journal page 28), 'Source of enzyme' row 'Yeast', 'Oxoaldehyde substrate' sub-row 'Phenylglyoxal': Molecular activity, kcat. = 402000 min-1; Km = 0.21 mM. Table 4 prints no kcat/Km column and the article prints no per-enzyme kcat/Km value.

row_label: Table 4, 'Source of enzyme' row 'Yeast', 'Oxoaldehyde substrate' sub-row 'Phenylglyoxal'

enzyme: lactoylglutathione lyase


organism: Plasmodium falciparum

substrate_name: (R)-S-lactoylglutathione

substrate: (R)-S-lactoylglutathione


substrate_name: leukotriene A4

column_label: Results prose and Fig. 4B report that incubation of LTA4 with GSTM4 gave Km 98.0 +/- 6.6 uM.

raw_value_unit_evidence: Km raw_value=98.0 +/- 6.6 raw_unit=uM

row_label: Human recombinant GSTM4 with LTA4 substrate, right panel

table_label: Fig. 4B, human recombinant GSTM4 conversion of LTA4 to LTC4

substrate: leukotriene A4


organism: Onchocerca volvulus


organism: Arabidopsis thaliana

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


substrate_name: Na(2)S for the cysteine synthase activity


substrate_name: O(3)-acetyl-L-serine for the cysteine synthase activity (in the presence of 2.5 mM Na(2)S)


substrate_name: Na(2)S for the cysteine synthase activity (in the presence of 10 mM O(3)-acetyl-L-serine)


organism: Ovis aries

assay_conditions_summary: pH 6.8; buffer 80 mM imidazole-HCl

column_label: Table 2 reports Methylglyoxal Km = 0.078 mM.

raw_value_unit_evidence: Km raw_value=0.078 mM raw_unit=mM

row_label: Methylglyoxal row / Km column

table_label: Wiley PDF PMID 19241 Table 2


column_label: Table 2 reports Phenylglyoxal Km = 0.113 mM.

raw_value_unit_evidence: Km raw_value=0.113 mM raw_unit=mM

row_label: Phenylglyoxal row / Km column


column_label: Table 4. Catalytic properties of glyoxalase I from yeast and from mammals. 'Source of enzyme' row 'Rat liver'; 'Oxoaldehyde substrate' sub-row 'Phenylglyoxal'; column 'Molecular activity, kcat. (min-1)' = 66000; column 'Km (mM)' = 0.06. Table 4 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 4 cell 66000 min-1; the printed column header is 'Molecular activity, kcat. (min-1)', so 66000 / 60 = 1100.0 s^(-1); the exported value is 1100.0 s^(-1). Km: printed Table 4 cell 0.06 mM; the printed column header is 'Km (mM)', already the export's unit, so no conversion is applied; the exported value is 0.06 mM. kcat/Km: the paper prints no kcat/Km cell for this or any other row, so nothing is converted; the exported 18333.333333333336 s^(-1)*mM^(-1) is carried unchanged and typed as the quotient of this row's own two confirmed printed components.

raw_value_unit_evidence: Table 4 (journal page 28), 'Source of enzyme' row 'Rat liver', 'Oxoaldehyde substrate' sub-row 'Phenylglyoxal': Molecular activity, kcat. = 66000 min-1; Km = 0.06 mM. Table 4 prints no kcat/Km column and the article prints no per-enzyme kcat/Km value.

row_label: Table 4, 'Source of enzyme' row 'Rat liver', 'Oxoaldehyde substrate' sub-row 'Phenylglyoxal'


organism: Entamoeba histolytica

substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: L-Cysteine


organism: Xenopus laevis

enzyme: protoporphyrin ferrochelatase


substrate_name: protoporphyrin

substrate: protoporphyrin


organism: Candidatus Pelagibacter ubique

substrate_name: cystathionine

assay_conditions_summary: pH 8; 310.15 K; buffer as 50 mM Tris·HCl pH 8

column_label: Table 2 (Steady state kinetic parameters for MBP-PuCBL, wMelCBL and TmCBL), Enzyme block 'MBP-PuCBL', Function row 'CBL', Conditions column '37 C, Tris'; column 'kcat (s^-1)' = 1.0; column 'KM (mM)' = 2.1; column 'kcat/KM (s^-1 M^-1)' = 470. The CBL line is the only line this Enzyme block prints for that activity, and the block prints no second buffer or temperature for it.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.0 s^-1; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 1.0 s^(-1). Km: printed Table 2 cell 2.1 mM; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 2.1 mM. kcat/Km: printed Table 2 cell 470 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 470 / 1000 = 0.47 s^-1 mM^-1. Closure disclosure: the quotient of this row's own two printed component cells is 1.0 / 2.1 = 0.47619047619047616 s^-1 mM^-1, against the printed efficiency cell 0.47 s^-1 mM^-1 carried at the two-significant-figure precision of the printed efficiency column.

raw_value_unit_evidence: Table 2, Enzyme block 'MBP-PuCBL', Function row 'CBL', Conditions '37 C, Tris': kcat = 1.0 s^-1; KM = 2.1 mM; printed kcat/KM = 470 s^-1 M^-1.

table_label: Table 2: Steady state kinetic parameters for MBP-PuCBL, wMelCBL and TmCBL (Mol. Microbiol. 2017, 105(4):508-524)


organism: Treponema denticola

substrate: L-Cysteine


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


substrate_name: gamma-glutamylcysteine

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

substrate: gamma-glutamylcysteine


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

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


substrate: Na(2)S for the cysteine synthase activity


organism: Escherichia coli (strain K12)

substrate_name: L-cystine

substrate: L-cystine


organism: Staphylococcus haemolyticus (strain JCSC1435)

substrate_name: L-cystathionine

substrate: L-cystathionine


organism: Corynebacterium striatum

substrate: cystathionine


organism: Thermotoga maritima


enzyme_display_name: ophiobolin F synthase

organism: Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)

substrate_name: geranylgeranyl diphosphate (GGDP)

enzyme: ophiobolin F synthase

substrate: geranylgeranyl diphosphate (GGDP)


organism: Escherichia coli

source_databases_merged: skid uniprot


organism: Latilactobacillus sakei

column_label: Table 4 beta-Lyase / L-Cys row reports kcat 9.30 +/- 2.05 x 10^2 s^-1, Km 11.5 +/- 1.1 mM, and kcat/Km 80.9 s^-1 mM^-1.

normalized_value_unit_evidence: kcat=930 s^-1; Km=11.5 mM; independently printed kcat/Km=80.9 s^-1 mM^-1; current quotient-derived kcat/Km=80.8695652173913 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 beta-Lyase / L-Cys row: kcat 9.30 +/- 2.05 x 10^2 s^-1; Km 11.5 +/- 1.1 mM; independently printed kcat/Km 80.9 s^-1 mM^-1.

row_label: beta-Lyase / L-Cys

table_label: Table 4. Kinetic parameters of racemase and beta-lyase reactions


organism: Gallus gallus


organism: Oryza sativa subsp. japonica

substrate_name: D-cysteine

column_label: PubMed abstract states kinetics analysis indicated Km and Vmax values for D-cys of 136 microM and 45.5 micromol/min/mg protein, respectively.

raw_value_unit_evidence: Km raw_value=136 raw_unit=microM

row_label: recombinant OsDCD1 from Oryza sativa with D-cysteine

table_label: PubMed abstract PMID 37499960

substrate: D-cysteine


organism: Spinacia oleracea

assay_conditions_summary: pH 9


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


organism: Wolbachia pipientis

column_label: Table 2 (Steady state kinetic parameters for MBP-PuCBL, wMelCBL and TmCBL), Enzyme block 'wMelCBL', Function row 'CBL', Conditions column '37 C, Tris'; column 'kcat (s^-1)' = 1.1 x 10^-3; column 'KM (mM)' = 0.02; column 'kcat/KM (s^-1 M^-1)' = 60. The CBL line is the only line this Enzyme block prints for that activity, and the block prints no second buffer or temperature for it.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.1 x 10^-3 s^-1; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 0.0011 s^(-1). Km: printed Table 2 cell 0.02 mM; the printed unit is already the canonical one, so no unit conversion applies; the exported value is 0.02 mM. kcat/Km: printed Table 2 cell 60 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 60 / 1000 = 0.06 s^-1 mM^-1. Closure disclosure: the quotient of this row's own two printed component cells is 1.1 x 10^-3 / 0.02 = 0.055 s^-1 mM^-1, against the printed efficiency cell 0.06 s^-1 mM^-1 carried at the two-significant-figure precision of the printed efficiency column.

raw_value_unit_evidence: Table 2, Enzyme block 'wMelCBL', Function row 'CBL', Conditions '37 C, Tris': kcat = 1.1 x 10^-3 s^-1; KM = 0.02 mM; printed kcat/KM = 60 s^-1 M^-1.


organism: Arabidopsis thaliana

substrate_name: L-selenocysteine

smiles: C(C(C(=O)O)N)[SeH]

column_label: Official JBC full-text Table III lists substrates and Km values for ABA3-NifS; the L-selenocysteine row reports Km 200 uM. The results prose also states that the Km for L-selenocysteine is 200 uM.

raw_value_unit_evidence: Km raw_value=200 raw_unit=uM

row_label: L-selenocysteine

table_label: JBC Table III PMID 15561708 substrate specificity and kinetic properties of ABA3-NifS

substrate: L-selenocysteine


organism: Homo sapiens

substrate_name: 15-deoxy-Delta12,14-prostaglandin J2

column_label: Results state: The apparent Michaelis constant (Km) for MGST3 was determined to 9.2 microM (Fig. 3B).

raw_value_unit_evidence: Km raw_value=9.2 raw_unit=microM

row_label: human MGST3 conjugation of 15dPGJ2 with GSH

table_label: PMC full-text PMID 36370807 / Results paragraph and Fig. 3B caption

substrate: 15-deoxy-Delta12,14-prostaglandin J2


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


organism: Rattus norvegicus

column_label: Rendered PMC Results section, Purification and Properties of Rat SCL: L-selenocysteine Km = 5.5 mM.

raw_value_unit_evidence: Results prose reports Vmax and Km values for L-selenocysteine were 26 μmol min^-1 mg^-1 and 5.5 mM, respectively.

row_label: Rat SCL / L-selenocysteine

table_label: PMC2852952 rendered Results prose


organism: Mus musculus

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


substrate_name: glutathione

substrate: glutathione


organism: Leishmania major


substrate_name: kethoxal

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

substrate: kethoxal


substrate_name: glutatione

substrate: glutatione


enzyme_display_name: UniProt O34667

organism: Bacillus subtilis

substrate_name: S-ribosylhomocysteine

enzyme: UniProt O34667

substrate: S-ribosylhomocysteine


enzyme_display_name: UniProt B2CMA5

organism: Streptococcus suis

enzyme: UniProt B2CMA5


organism: Rhodococcus sp. N-771


substrate_name: glutamine

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

substrate: glutamine


substrate_name: histidine

substrate: histidine


substrate_name: cysteine

substrate: cysteine


substrate_name: methionine

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

substrate: methionine


substrate_name: phenylalanine

substrate: phenylalanine


substrate_name: asparagine

substrate: asparagine


substrate_name: kynurenine

substrate: kynurenine


substrate_name: tryptophan

substrate: tryptophan


substrate_name: serine

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

substrate: serine


substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: phenylpyruvate

column_label: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids; row Keto acid substrates / Phenylpyruvate; column Km (mM).

normalized_value_unit_evidence: km paper=0.6 mM

raw_value_unit_evidence: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids, row Keto acid substrates / Phenylpyruvate: Km 0.6 ± 0.3 mM; kcat 152.0 ± 27.3 min^-1; kcat/Km 253.3 min^-1 mM^-1.

row_label: Keto acid substrates / Phenylpyruvate

substrate: phenylpyruvate


organism: Mycobacterium tuberculosis

substrate_name: protoporphyrin IX

substrate: protoporphyrin IX


organism: Haloferax volcanii

substrate_name: L-selenocysteine

substrate: L-selenocysteine


enzyme_display_name: L-cysteine desulfidase

organism: Treponema denticola

substrate_name: L-cysteine

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

assay_conditions_summary: pH 7.4; 295.15 K; buffer pH and temperature not specified in the publication

proof_lines: pH and temperature not specified in the publication, addition of Brij 35 to the assay buffer

proof_lines: pH and temperature not specified in the publication, in absence of Brij 35

enzyme: L-cysteine desulfidase

substrate: L-cysteine


substrate_name: S-methyl-L-cysteine

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

assay_conditions_summary: buffer pH and temperature not specified in the publication

substrate: S-methyl-L-cysteine


substrate_name: S-ethyl-L-cysteine

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

substrate: S-ethyl-L-cysteine


substrate_name: beta-chloro-L-alanine

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

substrate: beta-chloro-L-alanine


substrate_name: L-cysteine methyl ester

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

substrate: L-cysteine methyl ester


substrate_name: Unknown

substrate: Unknown


organism: Lactobacillus delbrueckii subsp. bulgaricus

substrate_name: L-Cystathionine

substrate: L-Cystathionine


substrate_name: S-aminoethyl-L-cysteine

substrate: S-aminoethyl-L-cysteine


substrate_name: L-cystine

substrate: L-cystine


substrate_name: L-Cysteine

substrate: L-Cysteine


substrate_name: L-Djenkolic acid

substrate: L-Djenkolic acid


organism: Methanocaldococcus jannaschii

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


organism: Brassica napus

column_label: Downloaded Springer PDF Table 2 lists the DES reaction Kmcys (mM) cell as 0.1 +/- 0.0 for recombinant His-tagged BnDES1; the footnote maps DES substrate to L-cysteine.

raw_value_unit_evidence: Table 2 reports Kmcys raw_value=0.1 +/- 0.0 raw_unit=mM for the DES reaction.

row_label: recombinant His-tagged BnDES1 / DES reaction

table_label: PDF Table 2


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

substrate_name: L-cysteine (at 65 degrees Celsius)

proof_lines: kcat is 39.6 sec(-1) (at 65 degrees Celsius).

substrate: L-cysteine (at 65 degrees Celsius)


enzyme_display_name: 2-hydroxypropyl-CoM lyase

organism: Xanthobacter autotrophicus

substrate_name: CoM

proof_lines: kcat is 6.5 sec(-1) with R-epoxypropane as substrate.

enzyme: 2-hydroxypropyl-CoM lyase

substrate: CoM


organism: Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)

substrate_name: R-epoxypropane

substrate: R-epoxypropane


organism: Escherichia coli (strain K12)


enzyme_display_name: S-ribosylhomocysteine lyase

substrate_name: S-Ribosyl-L-homocysteine

enzyme: S-ribosylhomocysteine lyase

substrate: S-Ribosyl-L-homocysteine


organism: Arabidopsis thaliana


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


substrate_name: L-cystathionine

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

substrate: L-cystathionine


substrate_name: L-djenkolic acid

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

substrate: L-djenkolic acid


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


substrate_name: epoxypropane

column_label: PMID 11939797 page 5009, prose under Determination of Kinetic Constants for EaCoMT gives Km,epoxypropane and kcat; page 5011 Discussion states catalytic efficiency for the epoxide substrate is 3.6 x 10^6 M^-1 s^-1.

raw_value_unit_evidence: Km,epoxypropane = 1.8 plus/minus 0.17 uM; Km,CoM = 33.6 plus/minus 1.6 uM; kcat = 6.5 s^-1; catalytic efficiency for the epoxide substrate = 3.6 x 10^6 M^-1 s^-1.

row_label: EaCoMT / R-epoxypropane with CoM

table_label: Determination of Kinetic Constants for EaCoMT; Figure 3 kinetic analysis; Discussion catalytic-efficiency prose

substrate: epoxypropane


organism: Oryza sativa subsp. japonica

substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


enzyme_display_name: L-cysteate sulfo-lyase

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

substrate_name: L-cysteate

column_label: PMID 16302849 DOI 10.1042/BJ20051311, Results prose under Purification and some properties of CuyA from S. pomeroyi DSS-3; CuyA; substrate L-cysteate; metric Km; 11.7 +/- 2.1 mM.

raw_value_unit_evidence: Results prose reports Km 11.7 +/- 2.1 mM for L-cysteate.

row_label: CuyA / L-cysteate

table_label: Results prose, Purification and some properties of CuyA from S. pomeroyi DSS-3

enzyme: L-cysteate sulfo-lyase

substrate: L-cysteate


substrate_name: S-ribosylhomocysteine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C82S with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

substrate: S-ribosylhomocysteine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F80M with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:B2CMA5 and applied mutation signature F80M/H87Y to reconstruct the assayed variant sequence.

column_label: PLOS PDF page 8 / full-text XML Table 4 row F80M/H87Y, columns KM (uM), Kcat (s^-1), and Kcat/KM (M^-1 s^-1), reports 60.4+/-4, 0.009+/-0.002, and 1.49x10^2.

table_label: Table 4. Kinetic parameters for SAH, wild-type and mutant enzymes, measured at pH7.2


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H87Y to reconstruct the assayed variant sequence.


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

column_label: PLOS PDF page 8 / full-text XML Table 4 row Wild-type, columns KM (uM), Kcat (s^-1), and Kcat/KM (M^-1 s^-1), reports 16.4+/-0.5, 0.102+/-0.01, and 6.21x10^3.

row_label: Wild-type


organism: Prevotella intermedia

substrate_name: L-cysteine

substrate: L-cysteine


organism: Pseudomonas chlororaphis


column_label: Results text reports the measured Km of the purified recombinant enzyme for cysteine was 1.78 +/- 0.14 mM, the turnover number was 39.6 s^-1, and kcat/Km was 22.2 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=1.78 normalized_unit=mM; kcat normalized_value=39.6 normalized_unit=s^-1; kcat/Km normalized_value=22.2 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=1.78 +/- 0.14 mM; kcat raw_value=39.6 s^-1; kcat/Km raw_value=22.2 mM^-1 s^-1

row_label: Purified recombinant MJ1025-derived L-cysteine desulfidase / cysteine

table_label: Results prose, PMID 15683250 PDF page 1664


organism: Fusobacterium nucleatum

proof_lines: pH 7.5, 37°C, recombinant enzyme purified from Escherichia coli

proof_lines: pH 7.5, 37°C, enzyme purified from Fusobacterium nucleatum

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


enzyme_display_name: methionine gamma-lyase

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

substrate_name: L-methionine

column_label: Abstract reports the identified gene produced a METase with K(m) value for L-methionine of 0.55mM.

raw_value_unit_evidence: Km raw_value=0.55 mM raw_unit=mM

row_label: Treponema denticola METase / L-methionine

table_label: PubMed XML abstract PMID 15845368

enzyme: methionine gamma-lyase

substrate: L-methionine


enzyme_display_name: geranyllinalool synthase

organism: Zea mays

substrate_name: farnesyl diphosphate (at pH 7.5)

enzyme: geranyllinalool synthase

substrate: farnesyl diphosphate (at pH 7.5)


substrate_name: geranylgeranyl diphosphate (at pH 7.5)

substrate: geranylgeranyl diphosphate (at pH 7.5)


substrate_name: geranyl diphosphate (at pH 7.5)

substrate: geranyl diphosphate (at pH 7.5)


organism: Novispirillum itersonii

substrate_name: protoporphyrin

column_label: The abstract reports apparent Km for protoporphyrin is 50 micrometer.

raw_value_unit_evidence: Km raw_value=50 micrometer raw_unit=micrometer

row_label: Prose segment: protoporphyrin Km

table_label: PubMed PMID 21163 abstract

substrate: protoporphyrin


organism: Pseudomonas putida

substrate_name: S-methyl-L-cysteine

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

proof_lines: pH 8.0, 37°C, recombinant mutant Y114F/C116H

substrate: S-methyl-L-cysteine


substrate_name: DL-homocysteine

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

substrate: DL-homocysteine


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


proof_lines: pH 8.0, 37°C, recombinant mutants K240R and K240M


proof_lines: pH 8.0, 37°C, recombinant mutants K240I and K240N


organism: Citrobacter freundii


substrate_name: alliin

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

substrate: alliin


substrate_name: S-ethyl-L-cysteine

substrate: S-ethyl-L-cysteine


substrate_name: ethiin

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

substrate: ethiin


substrate_name: O-acetyl-L-serine

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

substrate: O-acetyl-L-serine


substrate_name: methiin

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

substrate: methiin


substrate_name: O-acetyl-L-homoserine

substrate: O-acetyl-L-homoserine


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

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

column_label: Results paragraph states the Km and Vmax of W83 recombinant enzyme were 23.1 mM and 21.9 umol/min/mg of protein, respectively.

raw_value_unit_evidence: Km raw_value=23.1 raw_unit=mM

row_label: recombinant METase of P. gingivalis W83 / L-methionine breakdown assay

table_label: Results prose: Characterization of recombinant METase of P. gingivalis W83


organism: Bacillus subtilis

proof_lines: R31G, pH 7.6, 30°C, unaerobic conditions


proof_lines: wild-type, pH 7.6, 30°C, unaerobic conditions


proof_lines: mutant T302A, pH 7.6, 30°C, unaerobic conditions


proof_lines: mutant D76G/K102T, pH 7.6, 30°C, unaerobic conditions


proof_lines: M11V/G104A, pH 7.6, 30°C, unaerobic conditions


proof_lines: mutant E61K, pH 7.6, 30°C, unaerobic conditions


proof_lines: E61K/L185Q/G212D, pH 7.6, 30°C, unaerobic conditions


substrate_name: protoporphyrin IX

substrate: protoporphyrin IX


enzyme_display_name: cysteine-S-conjugate beta-lyase

organism: Escherichia coli

substrate_name: L-cystathionine

proof_lines: pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W276F

enzyme: cysteine-S-conjugate beta-lyase

substrate: L-cystathionine


proof_lines: pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W276F/W300F


proof_lines: pH 8.5, 25°C, recombinant mutant W131F/W188F/W276F/W300F/W340F


proof_lines: pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W300F/W340F


proof_lines: pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W276F/W340F


proof_lines: pH 8.5, 25°C, recombinant mutant W188F/W230F/W276F/W300F/W340F


proof_lines: pH 8.5, 25°C, recombinant mutant W131F/W188F/W230F/W276F/W300F/W340F


proof_lines: pH 8.5, 25°C, recombinant mutant W131F/W230F/W276F/W300F/W340F


proof_lines: pH 8.5, 25°C, recombinant mutant W131FF/W230FF/W276F


proof_lines:
pH 8.5, 25°C, recombinant mutant W340F
mutant enzyme W340F, at 25°C


proof_lines: pH 8.5, 25°C, recombinant mutant W131F/W230F/W276F/W340F


proof_lines: pH 8.5, 25°C, recombinant mutant W131F/W230F/W276F/W300F


proof_lines: pH 8.5, 25°C, recombinant mutants W340F and W131F/W230F/W276F/W340F


proof_lines:
recombinant enzyme
30°C, pH 8.0


substrate_name: L-ethionine

substrate: L-ethionine


proof_lines:
recombinant enzyme
30°C, pH 8.0
pH 8.0, 30°C


proof_lines:
wild-type
wild-type, pH 7.2, 30°C


substrate_name: S-Benzyl-L-cysteine

proof_lines: pH and temperature not specified in the publication

substrate: S-Benzyl-L-cysteine


substrate_name: S-Ribosyl-L-homocysteine

substrate: S-Ribosyl-L-homocysteine


enzyme_display_name: selenocysteine lyase

organism: Enterococcus faecalis

substrate_name: L-selenocysteine

smiles: C(C(C(=O)O)N)[SeH]

enzyme: selenocysteine lyase

substrate: L-selenocysteine


substrate_name: L-cysteine

substrate: L-cysteine


enzyme_display_name: phycoerythrocyanin alpha-cysteine-84 phycoviolobilin lyase/isomerase

organism: Mastigocladus laminosus

substrate_name: apo-[phycoerythrocyanin alpha-subunit]

proof_lines: depending on apo phycoerythrocyanin alpha-subunit (0.0048-0.019 mM), pH and temperature not specified in the publication

proof_lines: at 0.014 mM (2R,3E)-phycocyanobilin, pH and temperature not specified in the publication

substrate: apo-[phycoerythrocyanin alpha-subunit]


proof_lines: at 0.014 mM apo phycoerythrocyanin alpha-subunit, pH and temperature not specified in the publication

proof_lines: depending on apo-[phycoerythrocyanin alpha-subunit] (0.0048-0.019 mM), pH and temperature not specified in the publication

enzyme: phycoerythrocyanin alpha-cysteine-84 phycoviolobilin lyase/isomerase


substrate_name: phycocyanobilin

substrate: phycocyanobilin


enzyme_display_name: phycobiliprotein cysteine-84 phycobilin lyase

organism: Anabaena sp.


enzyme: phycobiliprotein cysteine-84 phycobilin lyase


enzyme_display_name: L-cystine beta-lyase

organism: Brassica oleracea var. italica

substrate_name: L-cystine

enzyme: L-cystine beta-lyase

substrate: L-cystine


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: hercynylcysteine S-oxide lyase

organism: Neurospora crassa

substrate_name: S-(hercyn-2-yl)-L-cysteine S-oxide

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

enzyme: hercynylcysteine S-oxide lyase

substrate: S-(hercyn-2-yl)-L-cysteine S-oxide


substrate_name: apo-[allophycocyanin beta-subunit]

proof_lines: pH and temperature not specified in the publication, apo-[allophycocyanin beta-subunit] encoded by apcF

proof_lines: pH and temperature not specified in the publication, apo-[allophycocyanin alpha-subunit] encoded by apcA1

proof_lines: pH and temperature not specified in the publication, apo allophycocyanin alpha-subunit encoded by apcA1

substrate: apo-[allophycocyanin beta-subunit]


organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)


enzyme_display_name: C-phycocyanin alpha-cysteine-84 phycocyanobilin lyase

organism: Synechococcus elongatus


substrate_name: apo-[C-phycocyanin alpha-subunit]

enzyme: C-phycocyanin alpha-cysteine-84 phycocyanobilin lyase

substrate: apo-[C-phycocyanin alpha-subunit]


proof_lines: pH 7.5, 37°C, cosubstrate: apo phycoerythrocyanin beta-subunit mutant C155I

proof_lines: pH 7.5, 37°C, cosubstrate: apo C-phycocyanin beta-subunit mutant C155I

proof_lines: pH 7.5, 37°C, cosubstrate: apo-[phycoerythrocyanin beta-subunit] mutant C155I


enzyme_display_name: D-cysteine desulfhydrase

organism: Methylorubrum extorquens

substrate_name: D-cysteine

enzyme: D-cysteine desulfhydrase

substrate: D-cysteine


organism: Arabidopsis thaliana


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8YZ70 and applied mutation signature R147Q to reconstruct the assayed variant sequence.

column_label: Table 1: Relative activities and enzyme kinetic constants of wild-type and mutant lyase, CpcS1, and the amount of chromophore bound to lyase (J. Biol. Chem. 2009, 284(52):36405-36414), enzyme-form row 'R147Q'; column 'Km (uM)' = 2.29; column 'kcat x 10^5 (s-1)' = 1.69; column 'kcat/Km x 10^5 (s-1 uM-1)' = 0.74.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.69 in the column headed kcat x 10^5 (s-1), so the constant is 1.69 x 10^-5 s^-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.0000169 s^(-1); the exported value is 0.0000169 s^(-1). Km: printed Table 1 cell 2.29 uM; 2.29 / 1000 = 0.00229 mM; the paper value is 0.00229 mM; the exported value is 0.00229 mM. kcat/Km: printed Table 1 cell 0.74 in the column headed kcat/Km x 10^5 (s-1 uM-1), so the constant is 0.74 x 10^-5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.74 x 10^-5 x 1000 = 0.0074 s^-1 mM^-1; the paper value is 0.0074 s^(-1)*mM^(-1); the exported value is 0.007379912663755459 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme-form row 'R147Q': Km = 2.29 uM; kcat = 1.69 x 10^-5 s^-1; printed kcat/Km = 0.74 x 10^-5 s^-1 uM^-1.

row_label: Table 1, mutant row 'R147Q'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8YZ70 and applied mutation signature H80L to reconstruct the assayed variant sequence.

column_label: Table 1: Relative activities and enzyme kinetic constants of wild-type and mutant lyase, CpcS1, and the amount of chromophore bound to lyase (J. Biol. Chem. 2009, 284(52):36405-36414), enzyme-form row 'H80L'; column 'Km (uM)' = 1.70; column 'kcat x 10^5 (s-1)' = 2.46; column 'kcat/Km x 10^5 (s-1 uM-1)' = 1.47.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.46 in the column headed kcat x 10^5 (s-1), so the constant is 2.46 x 10^-5 s^-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.0000246 s^(-1); the exported value is 0.0000246 s^(-1). Km: printed Table 1 cell 1.70 uM; 1.70 / 1000 = 0.0017 mM; the paper value is 0.0017 mM; the exported value is 0.0017 mM. kcat/Km: printed Table 1 cell 1.47 in the column headed kcat/Km x 10^5 (s-1 uM-1), so the constant is 1.47 x 10^-5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.47 x 10^-5 x 1000 = 0.0147 s^-1 mM^-1; the paper value is 0.0147 s^(-1)*mM^(-1); the exported value is 0.014470588235294119 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme-form row 'H80L': Km = 1.70 uM; kcat = 2.46 x 10^-5 s^-1; printed kcat/Km = 1.47 x 10^-5 s^-1 uM^-1.

row_label: Table 1, mutant row 'H80L'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8YZ70 and applied mutation signature H21T/H22V to reconstruct the assayed variant sequence.

column_label: Table 1: Relative activities and enzyme kinetic constants of wild-type and mutant lyase, CpcS1, and the amount of chromophore bound to lyase (J. Biol. Chem. 2009, 284(52):36405-36414), enzyme-form row 'H21T/H22V'; column 'Km (uM)' = 1.34; column 'kcat x 10^5 (s-1)' = 0.95; column 'kcat/Km x 10^5 (s-1 uM-1)' = 0.71.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.95 in the column headed kcat x 10^5 (s-1), so the constant is 0.95 x 10^-5 s^-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.0000095 s^(-1); the exported value is 0.0000095 s^(-1). Km: printed Table 1 cell 1.34 uM; 1.34 / 1000 = 0.00134 mM; the paper value is 0.00134 mM; the exported value is 0.00134 mM. kcat/Km: printed Table 1 cell 0.71 in the column headed kcat/Km x 10^5 (s-1 uM-1), so the constant is 0.71 x 10^-5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.71 x 10^-5 x 1000 = 0.0071 s^-1 mM^-1; the paper value is 0.0071 s^(-1)*mM^(-1); the exported value is 0.0070895522388059705 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme-form row 'H21T/H22V': Km = 1.34 uM; kcat = 0.95 x 10^-5 s^-1; printed kcat/Km = 0.71 x 10^-5 s^-1 uM^-1.

row_label: Table 1, mutant row 'H21T/H22V'


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W69M with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.