substrate_name: beta-Alanine

substrate: beta-Alanine


enzyme_display_name: UDP-N-acetylmuramate--L-alanine ligase

organism: Escherichia coli

substrate_name: L-Ile

source_db: brenda

verification_status: unverified

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

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

enzyme: UDP-N-acetylmuramate--L-alanine ligase

substrate: L-Ile

status: unverified

source: brenda


substrate_name: L-Vinylglycine

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

substrate: L-Vinylglycine


substrate_name: L-Cys

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

substrate: L-Cys


substrate_name: DL-propargylglycine

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

substrate: DL-propargylglycine


substrate_name: L-Val

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

substrate: L-Val


substrate_name: L-Thr

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

substrate: L-Thr


substrate_name: 2-amino-n-butyric acid

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

substrate: 2-amino-n-butyric acid


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

kcat_display: Not reported

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


substrate_name: benzyl L-alaninate

substrate: benzyl L-alaninate


substrate_name: methyl L-alaninate

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

substrate: methyl L-alaninate


substrate_name: ethyl L-alaninate

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

substrate: ethyl L-alaninate


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


enzyme_display_name: D-alanine--D-alanine ligase

substrate_name: ATP

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

mutation_type: substitution

assay_conditions_summary: cofactor ATP

enzyme: D-alanine--D-alanine ligase

substrate: ATP


substrate_name: D-Ala

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

proof_lines: N-terminal Ala, mutant enzyme E15Q, mutant enzyme Y216K

substrate: D-Ala


proof_lines:
N-terminal Ala, mutant enzyme L282R
C-terminal Ala, mutant enzyme L282R


proof_lines:
N-terminal Ala, mutant enzyme H63Q
C-terminal Ala, mutant enzyme H63Q


substrate_name: D-Phe

substrate: D-Phe


substrate_name: D-Met

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

substrate: D-Met


substrate_name: D-norleucine

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

substrate: D-norleucine


proof_lines: C-terminal Ala, mutant enzyme K144A, reaction with 5 mM ATP

proof_lines: C-terminal Ala, mutant enzyme K144A, reaction with 15 mM ATP


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


proof_lines: C-terminal Ala, mutant enzyme K144T, reaction with 5 mM ATP

proof_lines: C-terminal Ala, mutant enzyme K144T, reaction with 15 mM ATP


enzyme_display_name: glutamate--cysteine ligase

organism: Mus musculus

enzyme: glutamate--cysteine ligase


substrate_name: L-threonine

substrate: L-threonine


substrate_name: L-alanine

substrate: L-alanine


substrate_name: L-serine

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

substrate: L-serine


substrate_name: L-methionine

substrate: L-methionine


substrate_name: glycine

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

substrate: glycine


substrate_name: L-valine

substrate: L-valine


substrate_name: L-taurine

substrate: L-taurine


enzyme_display_name: glutathione synthase

organism: Homo sapiens

substrate_name: gamma-L-Glu-L-Cys

km_display: Not reported

proof_lines: mutant E144K and mutant N146D, pH 8.2, 37°C

enzyme: glutathione synthase

substrate: gamma-L-Glu-L-Cys


proof_lines: wild-type, 37°C, pH not specified in the publication


assay_conditions_summary: pH 8.2; 310.15 K; cofactor ATP


enzyme_display_name: ribose-5-phosphate isomerase

substrate_name: D-ribose 5-phosphate

enzyme: ribose-5-phosphate isomerase

substrate: D-ribose 5-phosphate


substrate_name: L-cysteine

proof_lines: recombinant mutant C553G holoenzyme, pH 8.0, 37°C

substrate: L-cysteine


substrate_name: L-Glu

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

substrate: L-Glu


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


substrate_name: gamma-Glu-Cys

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

substrate: gamma-Glu-Cys


substrate_name: L-Cys

proof_lines: mutant R127C, catalytic subunit, pH 8.0, 37°C

proof_lines: mutant R127C, CGL holoenzyme, pH 8.0, 37°C

substrate: L-Cys


proof_lines: wild-type, catalytic subunit, pH 8.0, 37°C


proof_lines: mutant H370L, CGL holoenzyme, pH 8.0, 37°C


proof_lines: mutant P414L, catalytic subunit, pH 8.0, 37°C


substrate_name: ATP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: Gly

proof_lines: mutant G370V, 37°C, pH not specified in the publication

substrate: Gly


proof_lines: mutant G369V, 37°C, pH not specified in the publication


proof_lines: mutant G371V, 37°C, pH not specified in the publication


substrate_name: gamma-L-Glu-aminobutanoate

substrate: gamma-L-Glu-aminobutanoate


assay_conditions_summary: 310.15 K; cofactor ATP


organism: Actinobacillus pleuropneumoniae

assay_conditions_summary: pH 8.5; 313.15 K; cofactor ATP

proof_lines: pH 8.5, 40°C, recombinant His-tagged enzyme


substrate_name: L-glutamate

substrate: L-glutamate


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


substrate_name: gamma-L-glutamyl-L-cysteine

substrate: gamma-L-glutamyl-L-cysteine


substrate_name: UDP-N-acetylmuramate

substrate: UDP-N-acetylmuramate


substrate_name: L-alanine

substrate: L-alanine


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 8; cofactor ATP


assay_conditions_summary: pH 8


organism: Pasteurella multocida

assay_conditions_summary: pH 8.2; 298.15 K; cofactor ATP


assay_conditions_summary: pH 8.2; 298.15 K; buffer 200 mM; cofactor ATP

proof_lines:
pH 8.2, 25°C
inTris-HCl buffer (200 mM, pH 8.2)


substrate_name: gamma-Glu-L-Cys

substrate: gamma-Glu-L-Cys


substrate_name: glycine

substrate: glycine


organism: Streptococcus thermophilus


substrate_name: L-alpha-aminobutyrate

substrate: L-alpha-aminobutyrate


proof_lines:
mutant with a nicked loop
loopless mutant


proof_lines:
loopless mutant
mutant with a nicked loop


organism: Enterococcus faecalis

substrate_name: D-Ala

proof_lines: C-terminal Ala, reaction with D-Ala + ATP, VanB

substrate: D-Ala


smiles: CCCC(C(=O)[O-])O


substrate_name: D-lactate

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

substrate: D-lactate


organism: Staphylococcus aureus

substrate_name: L-lysine

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

substrate: L-lysine


proof_lines: pH 8.6, 37°C, recombinant wild-type enzyme


proof_lines: above, pH 8.6, 37°C, recombinant mutant A409R


proof_lines: above, pH.6, 37°C, recombinant mutant E460A


organism: Arabidopsis thaliana

substrate_name: (R)-pantoate

substrate: (R)-pantoate


substrate_name: beta-Alanine

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

substrate: beta-Alanine


enzyme_display_name: alanine racemase

organism: Streptomyces lavendulae

enzyme: alanine racemase


substrate_name: D-alanine

substrate: D-alanine


substrate_name: ATP

substrate: ATP


substrate_name: D-cycloserine

substrate: D-cycloserine


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

proof_lines:
pH 8.5, 37°C, recombinant enzyme
pH 8.6


substrate_name: L-serine

substrate: L-serine


proof_lines:
at pH 7.6 and 25°C
pH 7.6


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


substrate_name: cysteine

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

proof_lines:
pH 7.6
at pH 7.6 and 25°C

substrate: cysteine


substrate_name: CTP

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

substrate: CTP


substrate_name: L-Cys

proof_lines:
strain B
strain W
strain KM

substrate: L-Cys


substrate_name: L-Glu

substrate: L-Glu


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


substrate_name: L-Ala

substrate: L-Ala


substrate_name: beta-chloro-L-Ala

assay_conditions_summary: 298.15 K; cofactor ATP

proof_lines: pH not specified in the publication, 25°C

substrate: beta-chloro-L-Ala


substrate_name: L-Ser

substrate: L-Ser


substrate_name: Gly

substrate: Gly


proof_lines:
37°C, mutant enzyme S150A, pH 6.0
37°C, mutant enzyme S150A, pH 7.5
37°C, mutant enzyme S150A, pH 9.2


proof_lines:
37°C, mutant enzyme E15Q, pH 6.0
37°C, mutant enzyme E15Q, pH 7.5
37°C, mutant enzyme E15Q, pH 9.2


proof_lines:
37°C, mutant enzyme Y216F, pH 6.0
37°C, mutant enzyme Y216F, pH 7.5
37°C, mutant enzyme Y216F, pH 9.2


proof_lines:
37°C, wild-type enzyme, pH 6.0
37°C, wild-type enzyme, pH 7.5
37°C, wild-type enzyme, pH 9.2


substrate_name: L-cysteine

proof_lines:
37°C, pH 7.2, catalytic subunit GCLC
37°C, pH 7.2, holoenzyme
at pH 8.2 and 37°C

substrate: L-cysteine


substrate_name: L-glutamate

substrate: L-glutamate


assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines:
37°C, pH 7.2,catalytic subunit GCLC
37°C, pH 7.2, holoenzyme
37°C, pH 7.2, catalytic subunit GCLC


substrate_name: Unknown

proof_lines: Kis, 37°C, pH 7.2, catalytic subunit GCLC, versus L-glutamate

proof_lines: Kii, 37°C, pH 7.2, catalytic subunit GCLC, versus ATP

proof_lines: Kii, 37°C, pH 7.2, catalytic subunit GCLC, versus L-glutamate

substrate: Unknown


organism: Nostoc sp.

assay_conditions_summary: pH 8.4; 298.15 K; cofactor ATP


organism: Plasmodium berghei


assay_conditions_summary: pH 8.2; cofactor ATP


organism: [Candida] boidinii


substrate_name: UDP-N-acetylmuramoyl-L-Ala-D-Glu

substrate: UDP-N-acetylmuramoyl-L-Ala-D-Glu


assay_conditions_summary: pH 8.6; 310.15 K; cofactor ATP


substrate_name: L-Lys

substrate: L-Lys


organism: Streptococcus agalactiae


substrate_name: gamma-L-Glu-L-Cys

substrate: gamma-L-Glu-L-Cys


organism: Agrobacterium tumefaciens


substrate_name: ATP

substrate: ATP


organism: Thermus thermophilus

substrate_name: D-alanine

substrate: D-alanine


smiles: N


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


substrate_name: gamma-Glu-L-Cys

proof_lines: 25°C, pH 7.5, with glycine as varied substrate

proof_lines: 25°C, pH 7.5, with ATP as varied substrate

substrate: gamma-Glu-L-Cys


organism: Chlamydia trachomatis

substrate_name: L-alanine

substrate: L-alanine


substrate_name: L-serine

substrate: L-serine


substrate_name: glycine

substrate: glycine


organism: Brassica juncea


assay_conditions_summary: cofactor ATP


substrate_name: cysteine

mutation_type: deletion

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

substrate: cysteine


substrate_name: glutamate

substrate: glutamate


proof_lines: pH 7.0, 25°C, versus glutamate, mutant DELTA85

proof_lines: pH 7.0, 25°C, versus cysteine, mutant DELTA85


organism: Escherichia coli


substrate_name: beta-Alanine

substrate: beta-Alanine


substrate_name: (R)-pantoate

substrate: (R)-pantoate


substrate_name: D-cycloserine

substrate: D-cycloserine


organism: Glycine max

proof_lines: pH 8.0, 30°C, with beta-Ala as cosubstrate


substrate_name: beta-Ala

substrate: beta-Ala


organism: Homo sapiens

substrate_name: gamma-glutamyl-alpha-aminobutyrate

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

substrate: gamma-glutamyl-alpha-aminobutyrate


assay_conditions_summary: pH 8.2; 310.15 K; cofactor ATP


substrate_name: Gly

substrate: Gly


substrate_name: D-pantoate

assay_conditions_summary: pH 7.8; 298.15 K; cofactor ATP

proof_lines: pH and temperature not specified in the publication

substrate: D-pantoate


substrate_name: L-cysteine

proof_lines:
pH 8.2, 37°C
holoenzyme
heavy subunit

substrate: L-cysteine


proof_lines:
pH 8.2, 37°C
holoenzyme


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


organism: Rattus norvegicus

substrate_name: gamma-L-Glu-L-alpha-aminobutyrate

substrate: gamma-L-Glu-L-alpha-aminobutyrate


substrate_name: ATP

substrate: ATP


organism: Enterococcus faecalis

substrate_name: CTP

substrate: CTP


substrate_name: L-Cys

proof_lines:
pH 7.6, 37°C
substrate CTP, pH 7.6, 37°C

substrate: L-Cys


organism: Proteus mirabilis


substrate_name: L-Glu

substrate: L-Glu


organism: Streptococcus pyogenes

assay_conditions_summary: 296.15 K; cofactor ATP


substrate_name: UDP-N-acetylmuramoyl-L-Ala-D-Glu

substrate: UDP-N-acetylmuramoyl-L-Ala-D-Glu


substrate_name: L-Lys

substrate: L-Lys


organism: Saccharomyces cerevisiae

proof_lines: reaction with Glu-alpha-aminobutyrate + hydroxylamine


organism: Staphylococcus aureus

substrate_name: UDP-N-acetylmuramate

substrate: UDP-N-acetylmuramate


substrate_name: L-Ala

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

substrate: L-Ala


organism: Xanthomonas campestris


substrate_name: L-glutamate

substrate: L-glutamate


organism: Zea mays

substrate_name: gamma-Glu-L-Cys

substrate: gamma-Glu-L-Cys


organism: Triticum aestivum

substrate_name: glycine

substrate: glycine


proof_lines:
pH 8.0, 30°C, with Gly as cosubstrate
pH 8.0, 30°C


substrate_name: beta-Ala

substrate: beta-Ala


organism: Bacillus thuringiensis

substrate_name: (R)-pantoate

substrate: (R)-pantoate


substrate_name: beta-Alanine

substrate: beta-Alanine


organism: Acinetobacter baumannii

substrate_name: D-alanine

proof_lines:
pH 7.8, 45°C
pH 7.8, 45°C, first D-Ala
pH 7.8, 45°C, second D-Ala

substrate: D-alanine


assay_conditions_summary: pH 7.8; 318.15 K; cofactor ATP


substrate_name: Gly

substrate: Gly


substrate_name: gamma-Glu-Cys

substrate: gamma-Glu-Cys


organism: Bacillus subtilis


organism: Corynebacterium glutamicum


organism: Helicobacter pylori


substrate_name: ATP

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

substrate: ATP


enzyme_display_name: sulfoquinovose mutarotase

organism: Herbaspirillum seropedicae

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

enzyme: sulfoquinovose mutarotase


organism: Lotus japonicus


proof_lines:
25°C, pH 8.0, at 20 mM pantoate
25°C, pH 8.0, at 0.5 mM pantoate


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

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


enzyme_display_name: mannose 2-epimerase

organism: Runella slithyformis

substrate_name: beta-D-mannopyranose

enzyme: mannose 2-epimerase

substrate: beta-D-mannopyranose


enzyme_display_name: D-tagatose 6-phosphate 4-epimerase

organism: Agrobacterium fabrum

substrate_name: D-tagatose 6-phosphate

protein_accession_database: UniProt

kcat_over_km_origin: calculated

sequence_source: multiple

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

data_origin: experimental

source_databases_merged: brenda uniprot

enzyme: D-tagatose 6-phosphate 4-epimerase

substrate: D-tagatose 6-phosphate


enzyme_display_name: mannuronan 5-epimerase

organism: Azotobacter vinelandii

substrate_name: Unknown

source_db: uniprot

enzyme: mannuronan 5-epimerase

substrate: Unknown

source: uniprot


enzyme_display_name: tRNA pseudouridine(55) synthase

organism: Thermotoga maritima

substrate_name: tRNA uridine55

enzyme: tRNA pseudouridine(55) synthase

substrate: tRNA uridine55


enzyme_display_name: fructoselysine 3-epimerase

organism: Escherichia coli (strain K12)

substrate_name: D-fructosyl-L-lysine

enzyme: fructoselysine 3-epimerase

substrate: D-fructosyl-L-lysine


organism: Escherichia coli

proof_lines: pH 7.5, 37°C, Escherichia coli tRNAPhe, wild-type enzyme

proof_lines: pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe. wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K19M to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, Escherichia coli tRNAPhe, mutant enzyme K19M


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature P20L to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, Escherichia coli tRNAPhe, mutant enzyme P20L


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature P20G to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, Escherichia coli tRNAPhe, mutant enzyme P20G


mutation_signature: pseudouridine synthase TruB with an 10-amino acid N-terminal truncation

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

mutation_type: truncation


organism: Nicotiana tabacum

substrate_name: L-Cys

substrate: L-Cys


organism: Lathyrus oleraceus


organism: Rattus norvegicus


substrate_name: L-alpha-aminobutyrate

substrate: L-alpha-aminobutyrate


organism: Staphylococcus aureus


organism: Thermus thermophilus

proof_lines: in the presence of 100 mM K+, at pH 7.3 and 30°C

proof_lines: in the presence of 50 mM K+, at pH 7.3 and 30°C

proof_lines: in the presence of less than 1 mM Na+, at pH 7.3 and 30°C


assay_conditions_summary: pH 7.3; 303.15 K; cofactor ATP


organism: Dyadobacter fermentans

verification_status: corrected

protein_accession_database: NCBI Protein

sequence_source: GenBank: ACT96842.1

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

assay_conditions_summary: pH 8

column_label: Hokkaido repository PDF Table 2 row Dfer_5652 has the exact Km cell and the paper kcat/kcat/Km cells needed to explain the rounded/computed export values.

table_label: Hokkaido repository PDF Table 2: Kinetic parameters of Runsl_4512 and Dfer_5652 for D-mannose

status: corrected


proof_lines: co-substrate: beta-alanine, pH 8.0, 30°C


proof_lines: co-substrate: (R)-pantoate, pH 8.0, 30°C


organism: Bos taurus

substrate_name: (R)-beta-amino-iso-butyrate

substrate: (R)-beta-amino-iso-butyrate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C58A/C174A/C193A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe, mutant enzyme C58A/C174A/C193A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C58A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe, mutant enzyme C58A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C174A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe, mutant enzyme C174A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C193V to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe, mutant enzyme C193V


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K19R to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, Escherichia coli tRNAPhe, mutant enzyme K19R


organism: Bacillus subtilis

substrate_name: L-Ala

substrate: L-Ala


organism: Onchocerca volvulus

substrate_name: L-glutamate

substrate: L-glutamate


substrate_name: [alginate]-beta-D-mannuronate

proof_lines:
pH 6.8, 37°C
pH 6.8, 30°C, presence of 8.6 mM Ca2+
pH 6.8, 30°C, presence of 0.68 mM Ca2+

substrate: [alginate]-beta-D-mannuronate


organism: Enterococcus faecium

substrate_name: D-Ala

proof_lines:
N-terminal Ala
C-terminal Ala

substrate: D-Ala


assay_conditions_summary: pH 7.4; 298.15 K; cofactor ATP

proof_lines:
pH 7.4, 25°C, versus ATP
pH 7.4, 25°C, versus D-Ala


proof_lines:
strain W
strain KM
pH 7.5, 37°C


source_db: oed

source: oed


enzyme_display_name: Muconate cycloisomerase

organism: Rhodococcus opacus

substrate_name: cis,cis-muconate

enzyme: Muconate cycloisomerase

substrate: cis,cis-muconate


enzyme_display_name: inositol-3-phosphate synthase

organism: Cyberlindnera jadinii

substrate_name: glucose 6-phosphate

enzyme: inositol-3-phosphate synthase

substrate: glucose 6-phosphate


enzyme_display_name: Inositol-3-phosphate synthase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: NAD (at 37 degrees Celsius and pH 7.2)

enzyme: Inositol-3-phosphate synthase

substrate: NAD (at 37 degrees Celsius and pH 7.2)


enzyme_display_name: chalcone isomerase

organism: Citrus sinensis

enzyme: chalcone isomerase


organism: Phaseolus vulgaris


enzyme_display_name: UniProt G4U3G8

organism: Deschampsia antarctica

substrate_name: isoliquiritigenin

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt G4U3G8

substrate: isoliquiritigenin

source: skid


substrate_name: naringenin chalcone

substrate: naringenin chalcone


enzyme_display_name: Chloromuconate cycloisomerase

organism: Delftia acidovorans

enzyme: Chloromuconate cycloisomerase


enzyme_display_name: 23S rRNA pseudouridine(2457) synthase

organism: Escherichia coli

substrate_name: 23S rRNA uridine2457

enzyme: 23S rRNA pseudouridine(2457) synthase

substrate: 23S rRNA uridine2457


enzyme_display_name: phosphoribosylanthranilate isomerase

proof_lines:
25°C, monomeric domain PRAI[ML256-452]
pH 7.5
pH 7.5, 20°C

enzyme: phosphoribosylanthranilate isomerase


enzyme_display_name: D-alanine--D-alanine ligase

proof_lines:
ligase A
ligase B
N-terminal Ala, ligase B

enzyme: D-alanine--D-alanine ligase


enzyme_display_name: glutathione synthase

substrate_name: ATP

proof_lines:
glutathione synthetase
ATP

enzyme: glutathione synthase

substrate: ATP


substrate_name: D-pantoate

substrate: D-pantoate


organism: Cephalocereus senilis

substrate_name: liquiritigenin

substrate: liquiritigenin


proof_lines:
isoenzyme II
isoenzyme I


enzyme_display_name: muconate cycloisomerase

enzyme: muconate cycloisomerase


enzyme_display_name: D-lyxose ketol-isomerase

substrate_name: D-Lyxose

enzyme: D-lyxose ketol-isomerase

substrate: D-Lyxose


organism: Limnospira platensis

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


organism: Synechocystis sp.

substrate_name: D-glucose 6-phosphate

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

proof_lines:
pH 7.5, recombinant refolded enzyme
pH 7.5, native enzyme

substrate: D-glucose 6-phosphate


assay_conditions_summary: pH 7.5; cofactor NAD+


organism: Gleichenia glauca


organism: Pinus ponderosa

substrate_name: D-Glucose 6-phosphate

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

substrate: D-Glucose 6-phosphate


organism: Physcomitrella appendiculatum


organism: Euglena gracilis


substrate_name: 1D-myo-Inositol 3-phosphate

substrate: 1D-myo-Inositol 3-phosphate


proof_lines:
chloroplastic enzyme
cytosolic enzyme from green cells
cytosolic enzyme from dark-grown cells


proof_lines: cytosolic enzyme from streptomycin-bleached cells, and chloroplastidic enzyme


organism: Cicer arietinum

proof_lines:
isozyme MIPS1
isozyme MIPS2


organism: Bacillus sp. (in: firmicutes)


organism: Arthrospira platensis


organism: Taxus baccata


organism: Rhodococcus rhodochrous


organism: Lemna gibba


organism: Eubacterium ramulus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H33Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H33Q, at pH 6.4, temperature not specified in the publication


sequence_variant_note: Mutation signature H33E could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme H33E, at pH 6.4, temperature not specified in the publication


sequence_variant_note: Mutation signature H33A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme H33A, at pH 6.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y48F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y48F, at pH 6.4, temperature not specified in the publication


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

proof_lines: wild type enzyme, at pH 6.4, temperature not specified in the publication


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

proof_lines: mutant enzyme H73A, at pH 6.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R125A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R125A, at pH 6.4, temperature not specified in the publication


organism: Deschampsia antarctica

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature R34A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 298.15 K; buffer DMSO in 50 mM potassium phosphate

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row R34A, isoliquiritigenin column group; column kcat (min^-1) = 0.1 ± 0.03; column Km (uM) = 5.3 ± 7.8; column kcat/Km (M^-1 s^-1) = 314.

raw_value_unit_evidence: Table 4, enzyme row R34A, isoliquiritigenin column group: kcat = 0.1 ± 0.03 min^-1; Km = 5.3 ± 7.8 uM; printed kcat/Km = 314 M^-1 s^-1.

row_label: Table 4, row R34A, isoliquiritigenin column group

table_label: Table 4: Steady-state kinetic parameters of wild-type and mutant DaCHI1 (PLoS ONE 2018, 13(2): e0192415)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature R34M to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row R34M, isoliquiritigenin column group; column kcat (min^-1) = 0.1 ± 0.08; column Km (uM) = 24.3 ± 28.2; column kcat/Km (M^-1 s^-1) = 69.

raw_value_unit_evidence: Table 4, enzyme row R34M, isoliquiritigenin column group: kcat = 0.1 ± 0.08 min^-1; Km = 24.3 ± 28.2 uM; printed kcat/Km = 69 M^-1 s^-1.

row_label: Table 4, row R34M, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature K108A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row K108A, isoliquiritigenin column group; column kcat (min^-1) = 0.2 ± 0.11; column Km (uM) = 11.2 ± 15.9; column kcat/Km (M^-1 s^-1) = 298.

raw_value_unit_evidence: Table 4, enzyme row K108A, isoliquiritigenin column group: kcat = 0.2 ± 0.11 min^-1; Km = 11.2 ± 15.9 uM; printed kcat/Km = 298 M^-1 s^-1.

row_label: Table 4, row K108A, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature S189A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row S189A, isoliquiritigenin column group; column kcat (min^-1) = 0.2 ± 0.03; column Km (uM) = 18.5 ± 6.9; column kcat/Km (M^-1 s^-1) = 180.

raw_value_unit_evidence: Table 4, enzyme row S189A, isoliquiritigenin column group: kcat = 0.2 ± 0.03 min^-1; Km = 18.5 ± 6.9 uM; printed kcat/Km = 180 M^-1 s^-1.

row_label: Table 4, row S189A, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I190M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature Y116A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row Y116A, isoliquiritigenin column group; column kcat (min^-1) = 0.4 ± 0.04; column Km (uM) = 27.6 ± 5.4; column kcat/Km (M^-1 s^-1) = 242.

raw_value_unit_evidence: Table 4, enzyme row Y116A, isoliquiritigenin column group: kcat = 0.4 ± 0.04 min^-1; Km = 27.6 ± 5.4 uM; printed kcat/Km = 242 M^-1 s^-1.

row_label: Table 4, row Y116A, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature M36A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row M36A, isoliquiritigenin column group; column kcat (min^-1) = 0.5 ± 0.15; column Km (uM) = 16.4 ± 10.1; column kcat/Km (M^-1 s^-1) = 508.

raw_value_unit_evidence: Table 4, enzyme row M36A, isoliquiritigenin column group: kcat = 0.5 ± 0.15 min^-1; Km = 16.4 ± 10.1 uM; printed kcat/Km = 508 M^-1 s^-1.

row_label: Table 4, row M36A, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature S189T to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row S189T, isoliquiritigenin column group; column kcat (min^-1) = 1.0 ± 0.04; column Km (uM) = 10.8 ± 1.2; column kcat/Km (M^-1 s^-1) = 1543.

raw_value_unit_evidence: Table 4, enzyme row S189T, isoliquiritigenin column group: kcat = 1.0 ± 0.04 min^-1; Km = 10.8 ± 1.2 uM; printed kcat/Km = 1543 M^-1 s^-1.

row_label: Table 4, row S189T, isoliquiritigenin column group


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

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row DaCHI1, isoliquiritigenin column group; column kcat (min^-1) = 1.3 ± 0.1; column Km (uM) = 15.3 ± 1.5; column kcat/Km (M^-1 s^-1) = 1416.

raw_value_unit_evidence: Table 4, enzyme row DaCHI1, isoliquiritigenin column group: kcat = 1.3 ± 0.1 min^-1; Km = 15.3 ± 1.5 uM; printed kcat/Km = 1416 M^-1 s^-1.

row_label: Table 4, row DaCHI1, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature Q104E to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row Q104E, isoliquiritigenin column group; column kcat (min^-1) = 1.4 ± 0.06; column Km (uM) = 22.5 ± 2.3; column kcat/Km (M^-1 s^-1) = 1011.

raw_value_unit_evidence: Table 4, enzyme row Q104E, isoliquiritigenin column group: kcat = 1.4 ± 0.06 min^-1; Km = 22.5 ± 2.3 uM; printed kcat/Km = 1011 M^-1 s^-1.

row_label: Table 4, row Q104E, isoliquiritigenin column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row S189A, naringenin chalcone column group; column kcat (min^-1) = 299 ± 15; column Km (uM) = 2.4 ± 0.6; column kcat/Km (M^-1 s^-1) = 2.08 x 10^6.

raw_value_unit_evidence: Table 4, enzyme row S189A, naringenin chalcone column group: kcat = 299 ± 15 min^-1; Km = 2.4 ± 0.6 uM; printed kcat/Km = 2.08 x 10^6 M^-1 s^-1.

row_label: Table 4, row S189A, naringenin chalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature M96K to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row M96K, naringenin chalcone column group; column kcat (min^-1) = 468 ± 51; column Km (uM) = 10.5 ± 3.4; column kcat/Km (M^-1 s^-1) = 7.43 x 10^5.

raw_value_unit_evidence: Table 4, enzyme row M96K, naringenin chalcone column group: kcat = 468 ± 51 min^-1; Km = 10.5 ± 3.4 uM; printed kcat/Km = 7.43 x 10^5 M^-1 s^-1.

row_label: Table 4, row M96K, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row Y116A, naringenin chalcone column group; column kcat (min^-1) = 578 ± 68; column Km (uM) = 7.0 ± 2.8; column kcat/Km (M^-1 s^-1) = 1.38 x 10^6.

raw_value_unit_evidence: Table 4, enzyme row Y116A, naringenin chalcone column group: kcat = 578 ± 68 min^-1; Km = 7.0 ± 2.8 uM; printed kcat/Km = 1.38 x 10^6 M^-1 s^-1.

row_label: Table 4, row Y116A, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row M36A, naringenin chalcone column group; column kcat (min^-1) = 2112 ± 239; column Km (uM) = 4.8 ± 2.0; column kcat/Km (M^-1 s^-1) = 7.33 x 10^6.

raw_value_unit_evidence: Table 4, enzyme row M36A, naringenin chalcone column group: kcat = 2112 ± 239 min^-1; Km = 4.8 ± 2.0 uM; printed kcat/Km = 7.33 x 10^6 M^-1 s^-1.

row_label: Table 4, row M36A, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row K108A, naringenin chalcone column group; column kcat (min^-1) = 3416 ± 234; column Km (uM) = 4.8 ± 1.2; column kcat/Km (M^-1 s^-1) = 1.19 x 10^7.

raw_value_unit_evidence: Table 4, enzyme row K108A, naringenin chalcone column group: kcat = 3416 ± 234 min^-1; Km = 4.8 ± 1.2 uM; printed kcat/Km = 1.19 x 10^7 M^-1 s^-1.

row_label: Table 4, row K108A, naringenin chalcone column group


verification_status: verified

assay_conditions_summary: pH 7.6; buffer potassium phosphate

column_label: table label: Table 4. Steady-state kinetic parameters of wild-type and mutant DaCHI1.; row label: DaCHI1; column label: the Naringenin chalcone kcat (min-1) cell and the Naringenin chalcone Km (uM) cell of this one wild-type row; no cell is taken from the Isoliquiritigenin column group of this row, from any mutant row, or from any other table; raw value: kcat 7819 plus-minus 825 min-1, Km 8.5 plus-minus 3.1 uM; raw unit: min-1 for kcat, uM for Km; normalized value: kcat 130.3 s^-1, Km 0.0085 mM, kcat/Km 15329.411764705883 s^-1 mM^-1; normalized unit: s^-1, mM, s^-1 mM^-1; condition label: Table 4 footnote: Km and kcat were calculated using the Michaelis-Menten equation; reactions were performed in potassium phosphate buffer (pH 7.6) as described in Material and Methods; all Km and kcat values are expressed as the mean plus-minus standard deviation of three parallel experiments. Enzymatic activity assay (Materials and Methods, Block RVM0009-METHODS-VERBATIM): the standard reaction was carried out at 25 C using 50 uM substrate in DMSO, 50 mM potassium phosphate buffer (pH 7.6) containing 1 mg bovine serum albumin. The export row carries pH 7.6 and no stored temperature.

normalized_value_unit_evidence: metric: kcat; raw value: 7819 ± 825; raw unit: min–1; normalized value: 130.3 s^-1; normalized unit: s^-1; metric: Km; raw value: 8.5 ± 3.1; raw unit: μM; normalized value: 0.0085 mM; normalized unit: mM; metric: kcat/Km; normalized value: 15329.411764705883 s^-1 mM^-1; normalized unit: s^-1 mM^-1; assay condition: Table 4 footnote: Km and kcat were calculated using the Michaelis-Menten equation; reactions were performed in potassium phosphate buffer (pH 7.6) as described in Material and Methods; all Km and kcat values are expressed as the mean plus-minus standard deviation of three parallel experiments. Enzymatic activity assay (Materials and Methods, Block RVM0009-METHODS-VERBATIM): the standard reaction was carried out at 25 C using 50 uM substrate in DMSO, 50 mM potassium phosphate buffer (pH 7.6) containing 1 mg bovine serum albumin. The export row carries pH 7.6 and no stored temperature. Conversion note: 7819 min-1 divided by 60 is 130.31666666666666 s^-1, stored at the export's one-decimal precision as 130.3 s^-1; 8.5 uM divided by 1000 is 0.0085 mM exactly; kcat/Km is the quotient of this row's own two cells as stored, 130.3 s^-1 divided by 0.0085 mM giving 15329.411764705883 s^-1 mM^-1, which reproduces the printed ratio cell 1.53 x 10^7 M-1 s-1 exactly at that cell's three-significant-figure precision.

raw_value_unit_evidence: Table 4, row DaCHI1, Naringenin chalcone column group: kcat cell 7819 ± 825 min–1; Km cell 8.5 ± 3.1 μM; printed kcat/Km cell 1.53 × 10^7 M–1 s–1 (superscript 7 rendered on the preceding text-layer line).

status: verified


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row Q104E, naringenin chalcone column group; column kcat (min^-1) = 8082 ± 267; column Km (uM) = 6.1 ± 0.7; column kcat/Km (M^-1 s^-1) = 2.208 x 10^7.

raw_value_unit_evidence: Table 4, enzyme row Q104E, naringenin chalcone column group: kcat = 8082 ± 267 min^-1; Km = 6.1 ± 0.7 uM; printed kcat/Km = 2.208 x 10^7 M^-1 s^-1.

row_label: Table 4, row Q104E, naringenin chalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature I190M to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row I190M, naringenin chalcone column group; column kcat (min^-1) = 11860 ± 539; column Km (uM) = 8.6 ± 1.2; column kcat/Km (M^-1 s^-1) = 2.292 x 10^7.

raw_value_unit_evidence: Table 4, enzyme row I190M, naringenin chalcone column group: kcat = 11860 ± 539 min^-1; Km = 8.6 ± 1.2 uM; printed kcat/Km = 2.292 x 10^7 M^-1 s^-1.

row_label: Table 4, row I190M, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row S189T, naringenin chalcone column group; column kcat (min^-1) = 13690 ± 556; column Km (uM) = 9.9 ± 1.2; column kcat/Km (M^-1 s^-1) = 2.306 x 10^7.

raw_value_unit_evidence: Table 4, enzyme row S189T, naringenin chalcone column group: kcat = 13690 ± 556 min^-1; Km = 9.9 ± 1.2 uM; printed kcat/Km = 2.306 x 10^7 M^-1 s^-1.

row_label: Table 4, row S189T, naringenin chalcone column group


organism: Vigna radiata

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


enzyme_display_name: chloromuconate cycloisomerase

organism: Rhodococcus opacus

proof_lines: pH and temperature not specified in the publication

enzyme: chloromuconate cycloisomerase


organism: Pseudomonas reinekei


assay_conditions_summary: buffer air-saturated

column_label: TABLE 2. Substrate specificities of muconate cycloisomerases MCIcatB and MCIsalC from Pseudomonas sp. strain MT1. TABLE 2, MCIsalC row 3-Methylmuconate; column 'Km (uM)' = 26.3; column 'kcat (s^-1)' = 214; column 'kcat/Km (s^-1 uM^-1)' = 8.13.

normalized_value_unit_evidence: Km: printed cell 26.3 uM converts to 0.0263 mM; the exported value is 0.026 mM. kcat: printed cell 214 s^-1 converts to 214.0 s^(-1); the exported value is 214.0 s^(-1). kcat/Km: printed cell 8.13 s^-1 uM^-1 converts to 8130.000000000001 s^(-1)*mM^(-1); the exported value is 8230.76923076923 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 2. Substrate specificities of muconate cycloisomerases MCIcatB and MCIsalC from Pseudomonas sp. strain MT1. TABLE 2, MCIsalC row 3-Methylmuconate: Km = 26.3 uM; kcat = 214 s^-1; printed kcat/Km = 8.13 s^-1 uM^-1.

row_label: TABLE 2, MCIsalC row 3-Methylmuconate


organism: Medicago sativa

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

source_databases_merged: sabio_rk skid uniprot


organism: Delftia acidovorans

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


organism: Arthrobacter sp.

column_label: Table 2. Substrate specificity of the MC from Arthrobacter sp. BA-5-17; row/segment 3-Ethyl-cis,cis-muconate; column/metric Km (uM)

raw_value_unit_evidence: Table 2 reports Km 670 +/- 32 uM for 3-ethyl-cis,cis-muconate.


organism: Homo sapiens


organism: Pseudomonas putida

substrate_name: cis,cis-Muconate

substrate: cis,cis-Muconate


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


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


column_label: PMID 9726873 TABLE 3. Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates; row 2,4-Dichloro-cis,cis-muconate / wild-type enzyme column group (TABLE 3); wild-type enzyme column group, sub-columns Km (uM), kcat (min^-1) and kcat/Km (min^-1 uM^-1); printed cells Km 26 ± 3 uM, kcat 3.3 ± 0.1 min^-1, kcat/Km 0.13 min^-1 uM^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.055 s^-1 / 0.026 mM = 2.1153846153846154 s^-1 mM^-1), not as the paper's rounded printed kcat/Km cell (0.13 min^-1 uM^-1), which agrees with that quotient at the printed cell's precision.

normalized_value_unit_evidence: metric: Km; normalized value: 0.026 mM; metric: kcat; normalized value: 0.055 s^-1; metric: kcat/Km; normalized value: 2.1153846153846154 s^-1 mM^-1; assay condition: Kinetic assay at pH 7.5 in 30 mM Tris-HCl with 1 mM MnSO4 at 25 degrees C, followed spectrophotometrically at 260 nm; purified wild-type P. putida PRS2000 muconate cycloisomerase, the TABLE 3 wild-type enzyme column group; kcat computed for a subunit molecular mass of 40 kDa

raw_value_unit_evidence: Table row as printed: Km 26 ± 3 uM; kcat 3.3 ± 0.1 min^-1; kcat/Km 0.13 min^-1 uM^-1 (wild-type enzyme column group).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature A271S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '2,4-Dichloro-cis,cis-muconate', enzyme column group 'A271S'; column 'Km (uM)' = 44; column 'kcat (min^-1)' = 2.9; column 'kcat/Km (min^-1 uM^-1)' = 0.067.

raw_value_unit_evidence: Table 3, substrate row 2,4-Dichloro-cis,cis-muconate, enzyme column A271S: Km = 44 uM; kcat = 2.9 min^-1; printed kcat/Km = 0.067 min^-1 uM^-1.

table_label: Table 3: Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates (Appl. Environ. Microbiol. 1998, 64(9):3290-3299)


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.


organism: Drosophila melanogaster

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+


organism: Arabidopsis thaliana

proof_lines: kcat is 6.4 min(-1) for D-glucose 6-phosphate. kcat is 5.0 min(-1) for NAD(+).


proof_lines: kcat is 4.0 min(-1) for D-glucose 6-phosphate. kcat is 3.6 min(-1) for NAD(+).


proof_lines: kcat is 5.2 min(-1) for D-glucose 6-phosphate. kcat is 4.8 min(-1) for NAD(+).


substrate_name: NAD(+)

substrate: NAD(+)


organism: Cupriavidus necator

proof_lines:
measurement of substrate consumption
measurement of product formation


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature I54V with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '2,4-Dichloro-cis,cis-muconate', enzyme column group 'I54V'; column 'Km (uM)' = 93; column 'kcat (min^-1)' = 7.2; column 'kcat/Km (min^-1 uM^-1)' = 0.078.

raw_value_unit_evidence: Table 3, substrate row 2,4-Dichloro-cis,cis-muconate, enzyme column I54V: Km = 93 uM; kcat = 7.2 min^-1; printed kcat/Km = 0.078 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I54V/F329I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +3, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature L333V with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '2,4-Dichloro-cis,cis-muconate', enzyme column group 'L333V'; column 'Km (uM)' = 39; column 'kcat (min^-1)' = 0.88; column 'kcat/Km (min^-1 uM^-1)' = 0.022.

raw_value_unit_evidence: Table 3, substrate row 2,4-Dichloro-cis,cis-muconate, enzyme column L333V: Km = 39 uM; kcat = 0.88 min^-1; printed kcat/Km = 0.022 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A271S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature I54V/F329I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '2-Chloro-cis,cis-muconate', enzyme column group 'I54V-F329I'; column 'Km (uM)' = 33; column 'kcat (min^-1)' = 10; column 'kcat/Km (min^-1 uM^-1)' = 0.32.

raw_value_unit_evidence: Table 3, substrate row 2-Chloro-cis,cis-muconate, enzyme column I54V-F329I: Km = 33 uM; kcat = 10 min^-1; printed kcat/Km = 0.32 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature K276N with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '2-Chloro-cis,cis-muconate', enzyme column group 'K276N'; column 'Km (uM)' = 34; column 'kcat (min^-1)' = 3.2; column 'kcat/Km (min^-1 uM^-1)' = 0.095.

raw_value_unit_evidence: Table 3, substrate row 2-Chloro-cis,cis-muconate, enzyme column K276N: Km = 34 uM; kcat = 3.2 min^-1; printed kcat/Km = 0.095 min^-1 uM^-1.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +8, so it is treated as a source-provided variant sequence.


column_label: PMID 9726873 TABLE 3. Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates; row 2-Chloro-cis,cis-muconate / wild-type enzyme column group (TABLE 3); wild-type enzyme column group, sub-columns Km (uM), kcat (min^-1) and kcat/Km (min^-1 uM^-1); printed cells Km 59 ± 5 uM, kcat 49 ± 2 min^-1, kcat/Km 0.83 min^-1 uM^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.817 s^-1 / 0.059 mM = 13.847457627118644 s^-1 mM^-1), not as the paper's rounded printed kcat/Km cell (0.83 min^-1 uM^-1), which agrees with that quotient at the printed cell's precision.

normalized_value_unit_evidence: metric: Km; normalized value: 0.059 mM; metric: kcat; normalized value: 0.817 s^-1; metric: kcat/Km; normalized value: 13.847457627118644 s^-1 mM^-1; assay condition: Kinetic assay at pH 7.5 in 30 mM Tris-HCl with 1 mM MnSO4 at 25 degrees C, followed spectrophotometrically at 260 nm; purified wild-type P. putida PRS2000 muconate cycloisomerase, the TABLE 3 wild-type enzyme column group; kcat computed for a subunit molecular mass of 40 kDa

raw_value_unit_evidence: Table row as printed: Km 59 ± 5 uM; kcat 49 ± 2 min^-1; kcat/Km 0.83 min^-1 uM^-1 (wild-type enzyme column group).


enzyme_display_name: carboxy-cis,cis-muconate cyclase

organism: Neurospora crassa

enzyme: carboxy-cis,cis-muconate cyclase


sequence_variant_note: Mutation signature I59W could not be applied safely because the resolved sequence does not match the expected reference residue(s).


column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '3-Fluoro-cis,cis-muconate', enzyme column group 'K276N'; column 'Km (uM)' = 230; column 'kcat (min^-1)' = 5,200; column 'kcat/Km (min^-1 uM^-1)' = 22.

raw_value_unit_evidence: Table 3, substrate row 3-Fluoro-cis,cis-muconate, enzyme column K276N: Km = 230 uM; kcat = 5,200 min^-1; printed kcat/Km = 22 min^-1 uM^-1.


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

column_label: PMID 9726873 TABLE 3. Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates; row 3-Fluoro-cis,cis-muconate / wild-type enzyme column group (TABLE 3); wild-type enzyme column group, sub-columns Km (uM), kcat (min^-1) and kcat/Km (min^-1 uM^-1); printed cells Km 97 ± 21 uM, kcat 8,900 ± 1,000 min^-1, kcat/Km 92 min^-1 uM^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (148.333 s^-1 / 0.097 mM = 1529.2061855670102 s^-1 mM^-1), not as the paper's rounded printed kcat/Km cell (92 min^-1 uM^-1), which agrees with that quotient at the printed cell's precision.

normalized_value_unit_evidence: metric: Km; normalized value: 0.097 mM; metric: kcat; normalized value: 148.333 s^-1; metric: kcat/Km; normalized value: 1529.2061855670102 s^-1 mM^-1; assay condition: Kinetic assay at pH 7.5 in 30 mM Tris-HCl with 1 mM MnSO4 at 25 degrees C, followed spectrophotometrically at 260 nm; purified wild-type P. putida PRS2000 muconate cycloisomerase, the TABLE 3 wild-type enzyme column group; kcat computed for a subunit molecular mass of 40 kDa

raw_value_unit_evidence: Table row as printed: Km 97 ± 21 uM; kcat 8,900 ± 1,000 min^-1; kcat/Km 92 min^-1 uM^-1 (wild-type enzyme column group).


column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '3-Methyl-cis,cis-muconate', enzyme column group 'A271S'; column 'Km (uM)' = 9.7; column 'kcat (min^-1)' = 680; column 'kcat/Km (min^-1 uM^-1)' = 71.

normalized_value_unit_evidence: Km: printed 9.7 uM; 9.7 / 1000 = 0.0097 mM, carried here at the exported precision as 0.01 mM. kcat: printed 680 min^-1; 680 / 60 = 11.333333 s^-1, carried here at the exported precision as 11.333 s^-1. kcat/Km: printed 71 min^-1 uM^-1; one min^-1 uM^-1 is 1000 / 60 = 16.666667 s^-1 mM^-1, so 71 x 1000 / 60 = 1183.333333 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate row 3-Methyl-cis,cis-muconate, enzyme column A271S: Km = 9.7 uM; kcat = 680 min^-1; printed kcat/Km = 71 min^-1 uM^-1.


column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '3-Methyl-cis,cis-muconate', enzyme column group 'I54V'; column 'Km (uM)' = 7.2; column 'kcat (min^-1)' = 740; column 'kcat/Km (min^-1 uM^-1)' = 100.

raw_value_unit_evidence: Table 3, substrate row 3-Methyl-cis,cis-muconate, enzyme column I54V: Km = 7.2 uM; kcat = 740 min^-1; printed kcat/Km = 100 min^-1 uM^-1.


column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '3-Methyl-cis,cis-muconate', enzyme column group 'I54V-F329I'; column 'Km (uM)' = 6.4; column 'kcat (min^-1)' = 310; column 'kcat/Km (min^-1 uM^-1)' = 49.

normalized_value_unit_evidence: Km: printed 6.4 uM; 6.4 / 1000 = 0.0064 mM, carried here at the exported precision as 0.006 mM. kcat: printed 310 min^-1; 310 / 60 = 5.166667 s^-1, carried here at the exported precision as 5.167 s^-1. kcat/Km: printed 49 min^-1 uM^-1; one min^-1 uM^-1 is 1000 / 60 = 16.666667 s^-1 mM^-1, so 49 x 1000 / 60 = 816.666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate row 3-Methyl-cis,cis-muconate, enzyme column I54V-F329I: Km = 6.4 uM; kcat = 310 min^-1; printed kcat/Km = 49 min^-1 uM^-1.


column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '3-Methyl-cis,cis-muconate', enzyme column group 'K276N'; column 'Km (uM)' = 12; column 'kcat (min^-1)' = 95; column 'kcat/Km (min^-1 uM^-1)' = 8.2.

raw_value_unit_evidence: Table 3, substrate row 3-Methyl-cis,cis-muconate, enzyme column K276N: Km = 12 uM; kcat = 95 min^-1; printed kcat/Km = 8.2 min^-1 uM^-1.


organism: Corynebacterium glutamicum

proof_lines: recombinant enzyme expressed in Escherichia coli BL21(DE3) cells, at pH 7.5 and 37°C

proof_lines: kcat is 2.24 for D-glucose 6-phosphate (at 37 degrees Celsius and pH 7.5).


organism: Citrus sinensis


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


column_label: Table 4. Kinetic constant of the following enzyme; row A271S / 2-Methyl-cis,cis-muconate; columns A271S Km (uM), A271S kcat (min^-1), and A271S kcat/Km (min^-1 uM^-1); cells Km=59 +/- 5, kcat=6400 +/- 200, printed kcat/Km=110.

normalized_value_unit_evidence: kcat normalized_value=106.667 normalized_unit=s^-1; Km normalized_value=0.059 normalized_unit=mM; kcat/Km normalized_value=1807.91525423729 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row A271S / 2-Methyl-cis,cis-muconate: Km 59 +/- 5 uM; kcat 6400 +/- 200 min^-1; printed kcat/Km 110 min^-1 uM^-1.

row_label: A271S / 2-Methyl-cis,cis-muconate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature F329I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '2-Methyl-cis,cis-muconate', enzyme column group 'F329I'; column 'Km (uM)' = 68; column 'kcat (min^-1)' = 10,000; column 'kcat/Km (min^-1 uM^-1)' = 150.

raw_value_unit_evidence: Table 3, substrate row 2-Methyl-cis,cis-muconate, enzyme column F329I: Km = 68 uM; kcat = 10,000 min^-1; printed kcat/Km = 150 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I54V with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic constant of the following enzyme; row I54V / 2-Methyl-cis,cis-muconate; columns I54V Km (uM), I54V kcat (min^-1), and I54V kcat/Km (min^-1 uM^-1); cells Km=58 +/- 5, kcat=650 +/- 30, printed kcat/Km=11.

normalized_value_unit_evidence: kcat normalized_value=10.833 normalized_unit=s^-1; Km normalized_value=0.058 normalized_unit=mM; kcat/Km normalized_value=186.775862068966 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row I54V / 2-Methyl-cis,cis-muconate: Km 58 +/- 5 uM; kcat 650 +/- 30 min^-1; printed kcat/Km 11 min^-1 uM^-1.

row_label: I54V / 2-Methyl-cis,cis-muconate


column_label: Table 4. Kinetic constant of the following enzyme; row I54V-F329I / 2-Methyl-cis,cis-muconate; columns I54V-F329I Km (uM), I54V-F329I kcat (min^-1), and I54V-F329I kcat/Km (min^-1 uM^-1); cells Km=57 +/- 4, kcat=1400 +/- 100, printed kcat/Km=24.

normalized_value_unit_evidence: kcat normalized_value=23.333 normalized_unit=s^-1; Km normalized_value=0.057 normalized_unit=mM; kcat/Km normalized_value=409.350877192982 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row I54V-F329I / 2-Methyl-cis,cis-muconate: Km 57 +/- 4 uM; kcat 1400 +/- 100 min^-1; printed kcat/Km 24 min^-1 uM^-1.

row_label: I54V-F329I / 2-Methyl-cis,cis-muconate


column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '2-Methyl-cis,cis-muconate', enzyme column group 'K276N'; column 'Km (uM)' = 180; column 'kcat (min^-1)' = 1,000; column 'kcat/Km (min^-1 uM^-1)' = 5.8.

raw_value_unit_evidence: Table 3, substrate row 2-Methyl-cis,cis-muconate, enzyme column K276N: Km = 180 uM; kcat = 1,000 min^-1; printed kcat/Km = 5.8 min^-1 uM^-1.


column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '2-Methyl-cis,cis-muconate', enzyme column group 'L333V'; column 'Km (uM)' = 110; column 'kcat (min^-1)' = 320; column 'kcat/Km (min^-1 uM^-1)' = 2.8.

raw_value_unit_evidence: Table 3, substrate row 2-Methyl-cis,cis-muconate, enzyme column L333V: Km = 110 uM; kcat = 320 min^-1; printed kcat/Km = 2.8 min^-1 uM^-1.


column_label: Table 4. Kinetic constant of the following enzyme; row Wild type / 2-Methyl-cis,cis-muconate; columns Wild type Km (uM), Wild type kcat (min^-1), and Wild type kcat/Km (min^-1 uM^-1); cells Km=40 +/- 2, kcat=3900 +/- 100, printed kcat/Km=97.

normalized_value_unit_evidence: kcat normalized_value=65 normalized_unit=s^-1; Km normalized_value=0.04 normalized_unit=mM; kcat/Km normalized_value=1625 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row Wild type / 2-Methyl-cis,cis-muconate: Km 40 +/- 2 uM; kcat 3900 +/- 100 min^-1; printed kcat/Km 97 min^-1 uM^-1.

row_label: Wild type / 2-Methyl-cis,cis-muconate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y59W with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic constant of the following enzyme; row Y59W / 2-Methyl-cis,cis-muconate; columns Y59W Km (uM), Y59W kcat (min^-1), and Y59W kcat/Km (min^-1 uM^-1); cells Km=69 +/- 6, kcat=3700 +/- 200, printed kcat/Km=53.

normalized_value_unit_evidence: kcat normalized_value=61.667 normalized_unit=s^-1; Km normalized_value=0.069 normalized_unit=mM; kcat/Km normalized_value=893.724637681159 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row Y59W / 2-Methyl-cis,cis-muconate: Km 69 +/- 6 uM; kcat 3700 +/- 200 min^-1; printed kcat/Km 53 min^-1 uM^-1.

row_label: Y59W / 2-Methyl-cis,cis-muconate


column_label: Table 4. Kinetic constant of the following enzyme; row A271S / 3-Chloro-cis,cis-muconate; columns A271S Km (uM), A271S kcat (min^-1), and A271S kcat/Km (min^-1 uM^-1); cells Km=180 +/- 20, kcat=960 +/- 60, printed kcat/Km=5.400.

normalized_value_unit_evidence: kcat normalized_value=16 normalized_unit=s^-1; Km normalized_value=0.18 normalized_unit=mM; kcat/Km normalized_value=88.8888888888889 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row A271S / 3-Chloro-cis,cis-muconate: Km 180 +/- 20 uM; kcat 960 +/- 60 min^-1; printed kcat/Km 5.400 min^-1 uM^-1.

row_label: A271S / 3-Chloro-cis,cis-muconate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P28012 and applied mutation signature N113A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer HEPES

column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row N113A, 2′,4′-dihydroxychalcone column group; column kcat (min^-1) = 284 ± 42; column Km (uM) = 17.4 ± 3.6; column kcat/Km (M^-1 s^-1) = 272000.

raw_value_unit_evidence: Table 2, enzyme row N113A, 2′,4′-dihydroxychalcone column group: kcat = 284 ± 42 min^-1; Km = 17.4 ± 3.6 uM; printed kcat/Km = 272000 M^-1 s^-1.

row_label: Table 2, row N113A, 2′,4′-dihydroxychalcone column group

table_label: Table 2: Steady-State Kinetic Parameters of Wild-Type and Mutant CHI (Biochemistry 2002, volume 41, issue 16, pages 5168-5176)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P28012 and applied mutation signature T190A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row T190A, 2′,4′-dihydroxychalcone column group; column kcat (min^-1) = 176 ± 20; column Km (uM) = 19.2 ± 2.5; column kcat/Km (M^-1 s^-1) = 153000.

raw_value_unit_evidence: Table 2, enzyme row T190A, 2′,4′-dihydroxychalcone column group: kcat = 176 ± 20 min^-1; Km = 19.2 ± 2.5 uM; printed kcat/Km = 153000 M^-1 s^-1.

row_label: Table 2, row T190A, 2′,4′-dihydroxychalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T48A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P28012 and applied mutation signature T48S to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row T48S, 2′,4′-dihydroxychalcone column group; column kcat (min^-1) = 519 ± 63; column Km (uM) = 41.0 ± 4.2; column kcat/Km (M^-1 s^-1) = 197000.

raw_value_unit_evidence: Table 2, enzyme row T48S, 2′,4′-dihydroxychalcone column group: kcat = 519 ± 63 min^-1; Km = 41.0 ± 4.2 uM; printed kcat/Km = 197000 M^-1 s^-1.

row_label: Table 2, row T48S, 2′,4′-dihydroxychalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P28012 and applied mutation signature Y106F to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row Y106F, 2′,4′-dihydroxychalcone column group; column kcat (min^-1) = 34.1 ± 3.1; column Km (uM) = 34.6 ± 5.9; column kcat/Km (M^-1 s^-1) = 16400.

raw_value_unit_evidence: Table 2, enzyme row Y106F, 2′,4′-dihydroxychalcone column group: kcat = 34.1 ± 3.1 min^-1; Km = 34.6 ± 5.9 uM; printed kcat/Km = 16400 M^-1 s^-1.

row_label: Table 2, row Y106F, 2′,4′-dihydroxychalcone column group


column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row N113A, 4,2′-dihydroxychalcone column group; column kcat (min^-1) = 343 ± 58; column Km (uM) = 52.5 ± 10.6; column kcat/Km (M^-1 s^-1) = 109000.

raw_value_unit_evidence: Table 2, enzyme row N113A, 4,2′-dihydroxychalcone column group: kcat = 343 ± 58 min^-1; Km = 52.5 ± 10.6 uM; printed kcat/Km = 109000 M^-1 s^-1.

row_label: Table 2, row N113A, 4,2′-dihydroxychalcone column group


column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row T190A, 4,2′-dihydroxychalcone column group; column kcat (min^-1) = 225 ± 47; column Km (uM) = 55.9 ± 8.4; column kcat/Km (M^-1 s^-1) = 67100.

raw_value_unit_evidence: Table 2, enzyme row T190A, 4,2′-dihydroxychalcone column group: kcat = 225 ± 47 min^-1; Km = 55.9 ± 8.4 uM; printed kcat/Km = 67100 M^-1 s^-1.

row_label: Table 2, row T190A, 4,2′-dihydroxychalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P28012 and applied mutation signature T48A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row T48A, 4,2′-dihydroxychalcone column group; column kcat (min^-1) = 0.28 ± 0.05; column Km (uM) = 46.4 ± 7.6; column kcat/Km (M^-1 s^-1) = 101.

raw_value_unit_evidence: Table 2, enzyme row T48A, 4,2′-dihydroxychalcone column group: kcat = 0.28 ± 0.05 min^-1; Km = 46.4 ± 7.6 uM; printed kcat/Km = 101 M^-1 s^-1.

row_label: Table 2, row T48A, 4,2′-dihydroxychalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T48S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y106F to reconstruct the assayed variant sequence.


organism: Rhodococcus erythropolis

sequence: PDLTVSGVRTTIVDLPILRP

wild_type_sequence: PDLTVSGVRTTIVDLPILRP


column_label: Table 1 (Substrate specificity of chloromuconate cycloisomerase from R. erythropolis 1CP) carries one substrate label column and four numeric columns, headed 'K_m,app (uM)', 'V_max (U/mg)', 'k_cat (1/min)' and 'k_cat/K_m,app (uM^-1 . min^-1)'. The cited cell set is the substrate row '3-Methyl-cis,cis-muconate': column 'K_m,app (uM)' = 66; column 'V_max (U/mg)' = 1.2; column 'k_cat (1/min)' = 48; column 'k_cat/K_m,app (uM^-1 . min^-1)' = 0.73. The Km,app and Vmax cells are printed with their standard deviations; the kcat and kcat/Km,app cells are printed on their own.

normalized_value_unit_evidence: Km: printed Table 1 cell 66 under the column head 'K_m,app (uM)'; 66 / 1000 = 0.066 mM. kcat: printed Table 1 cell 48 under the column head 'k_cat (1/min)'; 48 / 60 = 0.8 s^-1. kcat/Km: printed Table 1 cell 0.73 under the column head 'k_cat/K_m,app (uM^-1 . min^-1)'; one uM^-1 min^-1 is 1000 / 60 = 16.666667 s^-1 mM^-1, so 0.73 x 1000 / 60 = 12.166666666666668 s^-1 mM^-1, and the same-row quotient of the two printed component cells is 0.8 / 0.066 = 12.121212121212121 s^-1 mM^-1, which the printed efficiency cell reproduces at the two-figure precision Table 1 prints.

raw_value_unit_evidence: Table 1, substrate row '3-Methyl-cis,cis-muconate': Km,app = 66 uM; Vmax = 1.2 U/mg; kcat = 48 min^-1; printed kcat/Km,app = 0.73 uM^-1 min^-1.

table_label: Table 1: Substrate specificity of chloromuconate cycloisomerase from R. erythropolis 1CP (J. Bacteriol. 1995, 177(10):2821-2826)


column_label: Table 1 (Substrate specificity of chloromuconate cycloisomerase from R. erythropolis 1CP) carries one substrate label column and four numeric columns, headed 'K_m,app (uM)', 'V_max (U/mg)', 'k_cat (1/min)' and 'k_cat/K_m,app (uM^-1 . min^-1)'. The cited cell set is the substrate row '2-Chloro-cis,cis-muconate': column 'K_m,app (uM)' = 312; column 'V_max (U/mg)' = 3.3; column 'k_cat (1/min)' = 132; column 'k_cat/K_m,app (uM^-1 . min^-1)' = 0.42. The Km,app and Vmax cells are printed with their standard deviations; the kcat and kcat/Km,app cells are printed on their own.

normalized_value_unit_evidence: Km: printed Table 1 cell 312 under the column head 'K_m,app (uM)'; 312 / 1000 = 0.312 mM. kcat: printed Table 1 cell 132 under the column head 'k_cat (1/min)'; 132 / 60 = 2.2 s^-1. kcat/Km: printed Table 1 cell 0.42 under the column head 'k_cat/K_m,app (uM^-1 . min^-1)'; one uM^-1 min^-1 is 1000 / 60 = 16.666667 s^-1 mM^-1, so 0.42 x 1000 / 60 = 7.0 s^-1 mM^-1, and the same-row quotient of the two printed component cells is 2.2 / 0.312 = 7.051282051282052 s^-1 mM^-1, which the printed efficiency cell reproduces at the two-figure precision Table 1 prints.

raw_value_unit_evidence: Table 1, substrate row '2-Chloro-cis,cis-muconate': Km,app = 312 uM; Vmax = 3.3 U/mg; kcat = 132 min^-1; printed kcat/Km,app = 0.42 uM^-1 min^-1.


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_rest_accession:P08310 and applied mutation signature I54V/F329I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '3-Chloro-cis,cis-muconate', enzyme column group 'I54V-F329I'; column 'Km (uM)' = 210; column 'kcat (min^-1)' = 110; column 'kcat/Km (min^-1 uM^-1)' = 0.54.

raw_value_unit_evidence: Table 3, substrate row 3-Chloro-cis,cis-muconate, enzyme column I54V-F329I: Km = 210 uM; kcat = 110 min^-1; printed kcat/Km = 0.54 min^-1 uM^-1.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +3, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +8, so it is treated as a source-provided variant sequence.


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

column_label: PMID 9726873 TABLE 3. Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates; row 3-Chloro-cis,cis-muconate^b / wild-type enzyme column group (TABLE 3) (the printed row label carries footnote marker b); wild-type enzyme column group, sub-columns Km (uM), kcat (min^-1) and kcat/Km (min^-1 uM^-1); printed cells Km 320 ± 200 uM, kcat 64 ± 30 min^-1, kcat/Km 0.20 min^-1 uM^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (1.067 s^-1 / 0.32 mM = 3.3343749999999996 s^-1 mM^-1), not as the paper's rounded printed kcat/Km cell (0.20 min^-1 uM^-1), which agrees with that quotient at the printed cell's precision.

normalized_value_unit_evidence: metric: Km; normalized value: 0.32 mM; metric: kcat; normalized value: 1.067 s^-1; metric: kcat/Km; normalized value: 3.3343749999999996 s^-1 mM^-1; assay condition: Kinetic assay at pH 7.5 in 30 mM Tris-HCl with 1 mM MnSO4 at 25 degrees C, followed spectrophotometrically at 260 nm; purified wild-type P. putida PRS2000 muconate cycloisomerase, the TABLE 3 wild-type enzyme column group; kcat computed for a subunit molecular mass of 40 kDa

raw_value_unit_evidence: Table row as printed: Km 320 ± 200 uM; kcat 64 ± 30 min^-1; kcat/Km 0.20 min^-1 uM^-1 (wild-type enzyme column group).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A271S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '3-Fluoro-cis,cis-muconate', enzyme column group 'I54V-F329I'; column 'Km (uM)' = 100; column 'kcat (min^-1)' = 4,900; column 'kcat/Km (min^-1 uM^-1)' = 47.

raw_value_unit_evidence: Table 3, substrate row 3-Fluoro-cis,cis-muconate, enzyme column I54V-F329I: Km = 100 uM; kcat = 4,900 min^-1; printed kcat/Km = 47 min^-1 uM^-1.


substrate_name: Isoliquiritigenin

column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row N113A, 4,2′,4′-trihydroxychalcone column group; column kcat (min^-1) = 304 ± 33; column Km (uM) = 24.3 ± 3.8; column kcat/Km (M^-1 s^-1) = 209000.

raw_value_unit_evidence: Table 2, enzyme row N113A, 4,2′,4′-trihydroxychalcone column group: kcat = 304 ± 33 min^-1; Km = 24.3 ± 3.8 uM; printed kcat/Km = 209000 M^-1 s^-1.

row_label: Table 2, row N113A, 4,2′,4′-trihydroxychalcone column group

substrate: Isoliquiritigenin


column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row T190A, 4,2′,4′-trihydroxychalcone column group; column kcat (min^-1) = 379 ± 54; column Km (uM) = 19.8 ± 2.7; column kcat/Km (M^-1 s^-1) = 319000.

raw_value_unit_evidence: Table 2, enzyme row T190A, 4,2′,4′-trihydroxychalcone column group: kcat = 379 ± 54 min^-1; Km = 19.8 ± 2.7 uM; printed kcat/Km = 319000 M^-1 s^-1.

row_label: Table 2, row T190A, 4,2′,4′-trihydroxychalcone column group


column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row T48A, 4,2′,4′-trihydroxychalcone column group; column kcat (min^-1) = 1.45 ± 0.11; column Km (uM) = 18.9 ± 3.2; column kcat/Km (M^-1 s^-1) = 1280.

raw_value_unit_evidence: Table 2, enzyme row T48A, 4,2′,4′-trihydroxychalcone column group: kcat = 1.45 ± 0.11 min^-1; Km = 18.9 ± 3.2 uM; printed kcat/Km = 1280 M^-1 s^-1.

row_label: Table 2, row T48A, 4,2′,4′-trihydroxychalcone column group


column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row T48S, 4,2′,4′-trihydroxychalcone column group; column kcat (min^-1) = 830 ± 86; column Km (uM) = 21.3 ± 4.1; column kcat/Km (M^-1 s^-1) = 650000.

raw_value_unit_evidence: Table 2, enzyme row T48S, 4,2′,4′-trihydroxychalcone column group: kcat = 830 ± 86 min^-1; Km = 21.3 ± 4.1 uM; printed kcat/Km = 650000 M^-1 s^-1.

row_label: Table 2, row T48S, 4,2′,4′-trihydroxychalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N113A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T190A to reconstruct the assayed variant sequence.


column_label: Table 2 (Steady-State Kinetic Parameters of Wild-Type and Mutant CHI), enzyme row T48A, 4,2′,4′,6′-tetrahydroxychalcone column group; column kcat (min^-1) = 88.6 ± 13; column Km (uM) = 182 ± 91; column kcat/Km (M^-1 s^-1) = 8110.

raw_value_unit_evidence: Table 2, enzyme row T48A, 4,2′,4′,6′-tetrahydroxychalcone column group: kcat = 88.6 ± 13 min^-1; Km = 182 ± 91 uM; printed kcat/Km = 8110 M^-1 s^-1.

row_label: Table 2, row T48A, 4,2′,4′,6′-tetrahydroxychalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T48S with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I190M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature K108A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row K108A, isoliquiritigenin column group; column kcat (min^-1) = 0.2 ± 0.11; column Km (uM) = 11.2 ± 15.9; column kcat/Km (M^-1 s^-1) = 298.

raw_value_unit_evidence: Table 4, enzyme row K108A, isoliquiritigenin column group: kcat = 0.2 ± 0.11 min^-1; Km = 11.2 ± 15.9 uM; printed kcat/Km = 298 M^-1 s^-1.

row_label: Table 4, row K108A, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature M36A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row M36A, isoliquiritigenin column group; column kcat (min^-1) = 0.5 ± 0.15; column Km (uM) = 16.4 ± 10.1; column kcat/Km (M^-1 s^-1) = 508.

raw_value_unit_evidence: Table 4, enzyme row M36A, isoliquiritigenin column group: kcat = 0.5 ± 0.15 min^-1; Km = 16.4 ± 10.1 uM; printed kcat/Km = 508 M^-1 s^-1.

row_label: Table 4, row M36A, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature Q104E to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row Q104E, isoliquiritigenin column group; column kcat (min^-1) = 1.4 ± 0.06; column Km (uM) = 22.5 ± 2.3; column kcat/Km (M^-1 s^-1) = 1011.

raw_value_unit_evidence: Table 4, enzyme row Q104E, isoliquiritigenin column group: kcat = 1.4 ± 0.06 min^-1; Km = 22.5 ± 2.3 uM; printed kcat/Km = 1011 M^-1 s^-1.

row_label: Table 4, row Q104E, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature R34A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row R34A, isoliquiritigenin column group; column kcat (min^-1) = 0.1 ± 0.03; column Km (uM) = 5.3 ± 7.8; column kcat/Km (M^-1 s^-1) = 314.

raw_value_unit_evidence: Table 4, enzyme row R34A, isoliquiritigenin column group: kcat = 0.1 ± 0.03 min^-1; Km = 5.3 ± 7.8 uM; printed kcat/Km = 314 M^-1 s^-1.

row_label: Table 4, row R34A, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature R34M to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row R34M, isoliquiritigenin column group; column kcat (min^-1) = 0.1 ± 0.08; column Km (uM) = 24.3 ± 28.2; column kcat/Km (M^-1 s^-1) = 69.

raw_value_unit_evidence: Table 4, enzyme row R34M, isoliquiritigenin column group: kcat = 0.1 ± 0.08 min^-1; Km = 24.3 ± 28.2 uM; printed kcat/Km = 69 M^-1 s^-1.

row_label: Table 4, row R34M, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature S189A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row S189A, isoliquiritigenin column group; column kcat (min^-1) = 0.2 ± 0.03; column Km (uM) = 18.5 ± 6.9; column kcat/Km (M^-1 s^-1) = 180.

raw_value_unit_evidence: Table 4, enzyme row S189A, isoliquiritigenin column group: kcat = 0.2 ± 0.03 min^-1; Km = 18.5 ± 6.9 uM; printed kcat/Km = 180 M^-1 s^-1.

row_label: Table 4, row S189A, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature S189T to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row S189T, isoliquiritigenin column group; column kcat (min^-1) = 1.0 ± 0.04; column Km (uM) = 10.8 ± 1.2; column kcat/Km (M^-1 s^-1) = 1543.

raw_value_unit_evidence: Table 4, enzyme row S189T, isoliquiritigenin column group: kcat = 1.0 ± 0.04 min^-1; Km = 10.8 ± 1.2 uM; printed kcat/Km = 1543 M^-1 s^-1.

row_label: Table 4, row S189T, isoliquiritigenin column group


column_label: Table 4 | Steady-state kinetic parameters of wild-type and mutant DaCHI1; row DaCHI1; Isoliquiritigenin columns kcat (min^-1), Km (uM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 4 | Steady-state kinetic parameters of wild-type and mutant DaCHI1, isoliquiritigenin row DaCHI1: kcat 1.3 ± 0.1 min^-1; Km 15.3 ± 1.5 uM; kcat/Km 1416 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature Y116A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row Y116A, isoliquiritigenin column group; column kcat (min^-1) = 0.4 ± 0.04; column Km (uM) = 27.6 ± 5.4; column kcat/Km (M^-1 s^-1) = 242.

raw_value_unit_evidence: Table 4, enzyme row Y116A, isoliquiritigenin column group: kcat = 0.4 ± 0.04 min^-1; Km = 27.6 ± 5.4 uM; printed kcat/Km = 242 M^-1 s^-1.

row_label: Table 4, row Y116A, isoliquiritigenin column group


column_label: Table 2 row '2-Methyl-cis,cis-muconate', column 'Km (uM)': 29 +/- 5.2

raw_value_unit_evidence: Km column reports 29 +/- 5.2 uM

table_label: Table 2: Substrate specificity of the MC from Arthrobacter sp. BA-5-17


column_label: Table 2 row '3-Chloro-cis,cis-muconate', column 'Km (uM)': 46 +/- 5.5

raw_value_unit_evidence: Km column reports 46 +/- 5.5 uM


column_label: Table 2 row '3-Methyl-cis,cis-muconate', column 'Km (uM)': 75 +/- 8.9

raw_value_unit_evidence: Km column reports 75 +/- 8.9 uM


substrate_name: cis,cis-muconate

column_label: Table 2 row 'cis,cis-Muconate', column 'Km (uM)': 150 +/- 19

raw_value_unit_evidence: Km column reports 150 +/- 19 uM

row_label: cis,cis-Muconate

substrate: cis,cis-muconate


column_label: PMID 14617643 Table 2, Pseudomonas sp. strain MT1 MCI row for 3-Chloromuconate: Km 410 +/- 75 uM, kcat 7,200 +/- 520 min^-1, kcat/Km 17.6 min^-1 uM^-1.

raw_value_unit_evidence: Table 2 reports 3-Chloromuconate Km = 410 uM, kcat = 7,200 min^-1, and kcat/Km = 17.6 min^-1 uM^-1 for Pseudomonas sp. strain MT1 MCI.

row_label: Pseudomonas sp. strain MT1 / MCI / 3-Chloromuconate

table_label: Table 2. Substrate specificities of chloromuconate cycloisomerase and MCI from different strains and of trans-DLH from Pseudomonas sp. strain MT1


column_label: Retained ASM PDF Table 2, Pseudomonas sp. strain MT1 / MCI / Muconate row: Km 1,730 +/- 350; kcat 7,500 +/- 350; kcat/Km 4.3.

normalized_value_unit_evidence: Km 1.73 mM; kcat 125 s^-1; independently printed kcat/Km 71.66666666666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 Pseudomonas sp. strain MT1 / MCI / Muconate row: Km 1,730 +/- 350 uM; kcat 7,500 +/- 350 min^-1; independently printed kcat/Km 4.3 min^-1 uM^-1.


organism: Pseudomonas sp.


organism: Deschampsia antarctica

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature I190M to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row I190M, naringenin chalcone column group; column kcat (min^-1) = 11860 ± 539; column Km (uM) = 8.6 ± 1.2; column kcat/Km (M^-1 s^-1) = 2.292 x 10^7.

raw_value_unit_evidence: Table 4, enzyme row I190M, naringenin chalcone column group: kcat = 11860 ± 539 min^-1; Km = 8.6 ± 1.2 uM; printed kcat/Km = 2.292 x 10^7 M^-1 s^-1.

row_label: Table 4, row I190M, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row K108A, naringenin chalcone column group; column kcat (min^-1) = 3416 ± 234; column Km (uM) = 4.8 ± 1.2; column kcat/Km (M^-1 s^-1) = 1.19 x 10^7.

raw_value_unit_evidence: Table 4, enzyme row K108A, naringenin chalcone column group: kcat = 3416 ± 234 min^-1; Km = 4.8 ± 1.2 uM; printed kcat/Km = 1.19 x 10^7 M^-1 s^-1.

row_label: Table 4, row K108A, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row M36A, naringenin chalcone column group; column kcat (min^-1) = 2112 ± 239; column Km (uM) = 4.8 ± 2.0; column kcat/Km (M^-1 s^-1) = 7.33 x 10^6.

raw_value_unit_evidence: Table 4, enzyme row M36A, naringenin chalcone column group: kcat = 2112 ± 239 min^-1; Km = 4.8 ± 2.0 uM; printed kcat/Km = 7.33 x 10^6 M^-1 s^-1.

row_label: Table 4, row M36A, naringenin chalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature M96K to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row M96K, naringenin chalcone column group; column kcat (min^-1) = 468 ± 51; column Km (uM) = 10.5 ± 3.4; column kcat/Km (M^-1 s^-1) = 7.43 x 10^5.

raw_value_unit_evidence: Table 4, enzyme row M96K, naringenin chalcone column group: kcat = 468 ± 51 min^-1; Km = 10.5 ± 3.4 uM; printed kcat/Km = 7.43 x 10^5 M^-1 s^-1.

row_label: Table 4, row M96K, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row Q104E, naringenin chalcone column group; column kcat (min^-1) = 8082 ± 267; column Km (uM) = 6.1 ± 0.7; column kcat/Km (M^-1 s^-1) = 2.208 x 10^7.

raw_value_unit_evidence: Table 4, enzyme row Q104E, naringenin chalcone column group: kcat = 8082 ± 267 min^-1; Km = 6.1 ± 0.7 uM; printed kcat/Km = 2.208 x 10^7 M^-1 s^-1.

row_label: Table 4, row Q104E, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row S189A, naringenin chalcone column group; column kcat (min^-1) = 299 ± 15; column Km (uM) = 2.4 ± 0.6; column kcat/Km (M^-1 s^-1) = 2.08 x 10^6.

raw_value_unit_evidence: Table 4, enzyme row S189A, naringenin chalcone column group: kcat = 299 ± 15 min^-1; Km = 2.4 ± 0.6 uM; printed kcat/Km = 2.08 x 10^6 M^-1 s^-1.

row_label: Table 4, row S189A, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row S189T, naringenin chalcone column group; column kcat (min^-1) = 13690 ± 556; column Km (uM) = 9.9 ± 1.2; column kcat/Km (M^-1 s^-1) = 2.306 x 10^7.

raw_value_unit_evidence: Table 4, enzyme row S189T, naringenin chalcone column group: kcat = 13690 ± 556 min^-1; Km = 9.9 ± 1.2 uM; printed kcat/Km = 2.306 x 10^7 M^-1 s^-1.

row_label: Table 4, row S189T, naringenin chalcone column group


assay_conditions_summary: pH 7.6; 298.15 K; buffer potassium phosphate

column_label: table label: Table 4. Steady-state kinetic parameters of wild-type and mutant DaCHI1.; row label: DaCHI1; column label: the Naringenin chalcone kcat (min-1) cell and the Naringenin chalcone Km (uM) cell of this one wild-type row; no cell is taken from the Isoliquiritigenin column group of this row, from any mutant row, or from any other table; raw value: kcat 7819 plus-minus 825 min-1, Km 8.5 plus-minus 3.1 uM; raw unit: min-1 for kcat, uM for Km; normalized value: kcat 130.3 s^-1, Km 0.0085 mM, kcat/Km 15329.411764705883 s^-1 mM^-1; normalized unit: s^-1, mM, s^-1 mM^-1; condition label: Table 4 footnote: Km and kcat were calculated using the Michaelis-Menten equation; reactions were performed in potassium phosphate buffer (pH 7.6) as described in Material and Methods; all Km and kcat values are expressed as the mean plus-minus standard deviation of three parallel experiments. Enzymatic activity assay (Materials and Methods, Block RVM0009-METHODS-VERBATIM): the standard reaction was carried out at 25 C using 50 uM substrate in DMSO, 50 mM potassium phosphate buffer (pH 7.6) containing 1 mg bovine serum albumin. The export row carries pH 7.6 and no stored temperature.

normalized_value_unit_evidence: metric: kcat; raw value: 7819 ± 825; raw unit: min–1; normalized value: 130.3 s^-1; normalized unit: s^-1; metric: Km; raw value: 8.5 ± 3.1; raw unit: μM; normalized value: 0.0085 mM; normalized unit: mM; metric: kcat/Km; normalized value: 15329.411764705883 s^-1 mM^-1; normalized unit: s^-1 mM^-1; assay condition: Table 4 footnote: Km and kcat were calculated using the Michaelis-Menten equation; reactions were performed in potassium phosphate buffer (pH 7.6) as described in Material and Methods; all Km and kcat values are expressed as the mean plus-minus standard deviation of three parallel experiments. Enzymatic activity assay (Materials and Methods, Block RVM0009-METHODS-VERBATIM): the standard reaction was carried out at 25 C using 50 uM substrate in DMSO, 50 mM potassium phosphate buffer (pH 7.6) containing 1 mg bovine serum albumin. The export row carries pH 7.6 and no stored temperature. Conversion note: 7819 min-1 divided by 60 is 130.31666666666666 s^-1, stored at the export's one-decimal precision as 130.3 s^-1; 8.5 uM divided by 1000 is 0.0085 mM exactly; kcat/Km is the quotient of this row's own two cells as stored, 130.3 s^-1 divided by 0.0085 mM giving 15329.411764705883 s^-1 mM^-1, which reproduces the printed ratio cell 1.53 x 10^7 M-1 s-1 exactly at that cell's three-significant-figure precision.

raw_value_unit_evidence: Table 4, row DaCHI1, Naringenin chalcone column group: kcat cell 7819 ± 825 min–1; Km cell 8.5 ± 3.1 μM; printed kcat/Km cell 1.53 × 10^7 M–1 s–1 (superscript 7 rendered on the preceding text-layer line).


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row Y116A, naringenin chalcone column group; column kcat (min^-1) = 578 ± 68; column Km (uM) = 7.0 ± 2.8; column kcat/Km (M^-1 s^-1) = 1.38 x 10^6.

raw_value_unit_evidence: Table 4, enzyme row Y116A, naringenin chalcone column group: kcat = 578 ± 68 min^-1; Km = 7.0 ± 2.8 uM; printed kcat/Km = 1.38 x 10^6 M^-1 s^-1.

row_label: Table 4, row Y116A, naringenin chalcone column group


organism: Eubacterium ramulus

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

source_databases_merged: brenda skid


substrate_name: butein

substrate: butein


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=6.4


organism: Hydrogenophaga intermedia


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


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y106F to reconstruct the assayed variant sequence.


column_label: Table 4. Kinetic constant of the following enzyme; row Wild type / 3-Methyl-cis,cis-muconate; columns Wild type Km (uM), Wild type kcat (min^-1), and Wild type kcat/Km (min^-1 uM^-1); cells Km=6.0 +/- 0.5, kcat=590 +/- 10, printed kcat/Km=99.

normalized_value_unit_evidence: kcat normalized_value=9.833 normalized_unit=s^-1; Km normalized_value=0.006 normalized_unit=mM; kcat/Km normalized_value=1638.83333333333 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row Wild type / 3-Methyl-cis,cis-muconate: Km 6.0 +/- 0.5 uM; kcat 590 +/- 10 min^-1; printed kcat/Km 99 min^-1 uM^-1.

row_label: Wild type / 3-Methyl-cis,cis-muconate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y59W with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic constant of the following enzyme; row Y59W / 3-Methyl-cis,cis-muconate; columns Y59W Km (uM), Y59W kcat (min^-1), and Y59W kcat/Km (min^-1 uM^-1); cells Km=15 +/- 1, kcat=140 +/- 10, printed kcat/Km=9.7.

normalized_value_unit_evidence: kcat normalized_value=2.333 normalized_unit=s^-1; Km normalized_value=0.015 normalized_unit=mM; kcat/Km normalized_value=155.533333333333 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row Y59W / 3-Methyl-cis,cis-muconate: Km 15 +/- 1 uM; kcat 140 +/- 10 min^-1; printed kcat/Km 9.7 min^-1 uM^-1.

row_label: Y59W / 3-Methyl-cis,cis-muconate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A271S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic constant of the following enzyme; row A271S / cis,cis-Muconate; columns A271S Km (uM), A271S kcat (min^-1), and A271S kcat/Km (min^-1 uM^-1); cells Km=35 +/- 3, kcat=7100 +/- 200, printed kcat/Km=200.

normalized_value_unit_evidence: kcat normalized_value=118.333 normalized_unit=s^-1; Km normalized_value=0.035 normalized_unit=mM; kcat/Km normalized_value=3380.94285714286 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row A271S / cis,cis-Muconate: Km 35 +/- 3 uM; kcat 7100 +/- 200 min^-1; printed kcat/Km 200 min^-1 uM^-1.

row_label: A271S / cis,cis-Muconate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature F329I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row 'cis,cis-Muconate', enzyme column group 'F329I'; column 'Km (uM)' = 47; column 'kcat (min^-1)' = 2,600; column 'kcat/Km (min^-1 uM^-1)' = 54.

raw_value_unit_evidence: Table 3, substrate row cis,cis-Muconate, enzyme column F329I: Km = 47 uM; kcat = 2,600 min^-1; printed kcat/Km = 54 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I54V with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic constant of the following enzyme; row I54V / cis,cis-Muconate; columns I54V Km (uM), I54V kcat (min^-1), and I54V kcat/Km (min^-1 uM^-1); cells Km=96 +/- 8, kcat=2500 +/- 100, printed kcat/Km=26.

normalized_value_unit_evidence: kcat normalized_value=41.667 normalized_unit=s^-1; Km normalized_value=0.096 normalized_unit=mM; kcat/Km normalized_value=434.03125 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row I54V / cis,cis-Muconate: Km 96 +/- 8 uM; kcat 2500 +/- 100 min^-1; printed kcat/Km 26 min^-1 uM^-1.

row_label: I54V / cis,cis-Muconate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I54V/F329I with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic constant of the following enzyme; row I54V-F329I / cis,cis-Muconate; columns I54V-F329I Km (uM), I54V-F329I kcat (min^-1), and I54V-F329I kcat/Km (min^-1 uM^-1); cells Km=140 +/- 10, kcat=540 +/- 30, printed kcat/Km=3.80.

normalized_value_unit_evidence: kcat normalized_value=9 normalized_unit=s^-1; Km normalized_value=0.14 normalized_unit=mM; kcat/Km normalized_value=64.2857142857143 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row I54V-F329I / cis,cis-Muconate: Km 140 +/- 10 uM; kcat 540 +/- 30 min^-1; printed kcat/Km 3.80 min^-1 uM^-1.

row_label: I54V-F329I / cis,cis-Muconate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature K276N with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row 'cis,cis-Muconate', enzyme column group 'K276N'; column 'Km (uM)' = 74; column 'kcat (min^-1)' = 2,100; column 'kcat/Km (min^-1 uM^-1)' = 29.

raw_value_unit_evidence: Table 3, substrate row cis,cis-Muconate, enzyme column K276N: Km = 74 uM; kcat = 2,100 min^-1; printed kcat/Km = 29 min^-1 uM^-1.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +8, so it is treated as a source-provided variant sequence.


column_label: Table 4. Kinetic constant of the following enzyme; row Wild type / cis,cis-Muconate; columns Wild type Km (uM), Wild type kcat (min^-1), and Wild type kcat/Km (min^-1 uM^-1); cells Km=40 +/- 4, kcat=12600 +/- 400, printed kcat/Km=310.

normalized_value_unit_evidence: kcat normalized_value=210 normalized_unit=s^-1; Km normalized_value=0.04 normalized_unit=mM; kcat/Km normalized_value=5250 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row Wild type / cis,cis-Muconate: Km 40 +/- 4 uM; kcat 12600 +/- 400 min^-1; printed kcat/Km 310 min^-1 uM^-1.

row_label: Wild type / cis,cis-Muconate


column_label: Table 4. Kinetic constant of the following enzyme; row Y59W / cis,cis-Muconate; columns Y59W Km (uM), Y59W kcat (min^-1), and Y59W kcat/Km (min^-1 uM^-1); cells Km=47 +/- 3, kcat=1100 +/- 100, printed kcat/Km=24.

normalized_value_unit_evidence: kcat normalized_value=18.333 normalized_unit=s^-1; Km normalized_value=0.047 normalized_unit=mM; kcat/Km normalized_value=390.063829787234 normalized_unit=s^-1*mM^-1 from same-row kcat and Km.

raw_value_unit_evidence: Table 4 row Y59W / cis,cis-Muconate: Km 47 +/- 3 uM; kcat 1100 +/- 100 min^-1; printed kcat/Km 24 min^-1 uM^-1.

row_label: Y59W / cis,cis-Muconate


organism: Antrophyum callifolium


organism: Marchantia paleacea


organism: Selaginella moellendorffii


organism: Aspergillus niger


organism: Cutaneotrichosporon cutaneum

column_label: Abstract states the two purified enzyme forms have the same Km value of 25 microM for cis,cis-muconate.

raw_value_unit_evidence: Km raw_value=25 raw_unit=microM

row_label: Trichosporon cutaneum cis,cis-muconate cyclase with cis,cis-muconate

table_label: PubMed/PMC abstract PMID 7193457


organism: Homo sapiens

substrate_name: NAD

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

column_label: Abstract reports K(m) values of 0.57 mm for glucose 6-phosphate and 8 microm for NAD(+).

raw_value_unit_evidence: Km raw_value=8 microm raw_unit=microM

row_label: Recombinant human MIP synthase / NAD+

table_label: PubMed XML abstract PMID 15024000

substrate: NAD


organism: Saccharomyces cerevisiae


organism: Oryza sativa


organism: Medicago sativa

substrate_name: Naringenin chalcone

substrate: Naringenin chalcone


substrate_name: naringenin chalcone

substrate: naringenin chalcone


column_label: Abstract reports the apparent Km was found to be 57 microM at pH 6.0 and 30 degrees C.

raw_value_unit_evidence: Km raw_value=57 microM raw_unit=microM

row_label: Aspergillus niger 3-carboxy-cis,cis-muconate cyclase / 3-carboxy-cis,cis-muconate

table_label: PubMed XML abstract PMID 240704


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

column_label: Table 1 row MIPS1, column kcat/Km (mM^-1 min^-1) for Glc-6-P.

normalized_value_unit_evidence: kcat 0.10666666666666667 s^-1; Km 0.68 mM; explicit kcat/Km 0.15666666666666668 s^-1*mM^-1. Current exported rounded/derived values differ for at least one populated metric.

table_label: Table 1. Steady State Kinetic Parameters for Arabidopsis MIPS


column_label: Table 1 row MIPS2, column kcat/Km (mM^-1 min^-1) for Glc-6-P.

normalized_value_unit_evidence: kcat 0.06666666666666667 s^-1; Km 0.45 mM; explicit kcat/Km 0.14666666666666667 s^-1*mM^-1. Current exported rounded/derived values differ for at least one populated metric.


column_label: Table 1 Steady State Kinetic Parameters for Arabidopsis MIPS: MIPS3 row; columns kcat (min^-1), KmGlc-6-P (mM), kcat/Km (mM^-1 min^-1).

normalized_value_unit_evidence: kcat normalized_value=0.08666666666666667 normalized_unit=s^-1; Km normalized_value=0.31 normalized_unit=mM; explicit kcat/Km normalized_value=0.2833333333333333 normalized_unit=s^-1 mM^-1. CatLog stores derived kcat/Km=0.2806451612903226 from rounded export kcat/Km inputs.

raw_value_unit_evidence: Table 1 row MIPS3 reports kcat=5.2 min^-1, KmGlc-6-P=0.31 mM, kcat/Km=17 mM^-1 min^-1.

row_label: MIPS3 / Glc-6-P

table_label: PMC2861443 Table 1


organism: Rattus norvegicus

column_label: Abstract kinetic summary: glucose 6-phosphate Km 3.8 mM; NAD+ Km 17.9 uM.

normalized_value_unit_evidence: glucose 6-phosphate 3.8 mM; NAD+ 0.0179 mM

raw_value_unit_evidence: Abstract states basal Km values for glucose 6-phosphate and NAD+ were 3.8 mM and 17.9 uM, respectively.

row_label: Glucose-6-phosphate cycloisomerase substrate/cofactor Kms

table_label: Abstract / kinetic summary


organism: Trypanosoma brucei brucei

substrate_name: D-glucose 6-phosphate (at 37 degrees Celsius and pH 8.0)

column_label: PMID 16824097 Results prose/Fig. 2B, recombinant TbINO1 with glucose 6-phosphate: apparent Km = 0.58 mM.

raw_value_unit_evidence: Results prose reports an apparent Km of 0.58 mM and Vmax of 0.25 umol h^-1 for recombinant TbINO1 with glucose 6-phosphate.

row_label: recombinant TbINO1 / glucose 6-phosphate

table_label: Results prose and Fig. 2B


organism: Vigna radiata


substrate_name: (+)-taxifolin

column_label: Results prose reports: The Km for (+)-taxifolin was 4.1 +/- 0.6 uM for recombinant CHI characterization.

raw_value_unit_evidence: Km raw_value=4.1 +/- 0.6 raw_unit=uM

row_label: Recombinant E. ramulus CHI in E. coli pTI2 cell extract / (+)-taxifolin

table_label: Results prose: recombinant chi expression and flavanonol-isomerizing characterization

substrate: (+)-taxifolin


organism: Pseudomonas putida

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


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


proof_lines: pH 7.5, 25°C, mutant enzyme Y59W and A271S


organism: Odontosoria chusana


organism: Lindsaea orbiculata


organism: Acinetobacter calcoaceticus


substrate_name: Unknown

proof_lines: inhibitor of cis,cis-muconate conversion

substrate: Unknown


organism: Rhodococcus erythropolis


proof_lines: pH 7.5, 25°C, mutant enzyme K276N or F329I


proof_lines: pH 7.5, 25°C, mutant enzyme Y59W and F329I


proof_lines: pH 7.5, 25°C, mutant enzyme A271S or I54V/F329


organism: Pseudomonas sp.